Protein ID | Hirsu2|2957 |
Gene name | |
Location | Contig_1741:1778..3505 |
Strand | - |
Gene length (bp) | 1727 |
Transcript length (bp) | 1653 |
Coding sequence length (bp) | 1653 |
Protein length (aa) | 551 |
PFAM Domain ID | Short name | Long name | E-value | Start | End |
---|---|---|---|---|---|
PF16113 | ECH_2 | Enoyl-CoA hydratase/isomerase | 1.1E-128 | 86 | 419 |
PF00378 | ECH_1 | Enoyl-CoA hydratase/isomerase | 1.1E-26 | 84 | 258 |
Swissprot ID | Swissprot Description | Start | End | E-value |
---|---|---|---|---|
sp|Q5ZJ60|HIBCH_CHICK | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Gallus gallus GN=HIBCH PE=2 SV=1 | 72 | 417 | 1.0E-88 |
sp|Q58EB4|HIBCH_DANRE | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Danio rerio GN=hibch PE=2 SV=1 | 76 | 417 | 1.0E-87 |
sp|O74802|HIBCH_SCHPO | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN=ehd3 PE=3 SV=1 | 77 | 409 | 9.0E-85 |
sp|A2VDC2|HIBCH_XENLA | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Xenopus laevis GN=hibch PE=2 SV=1 | 88 | 417 | 2.0E-84 |
sp|Q5XIE6|HIBCH_RAT | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Rattus norvegicus GN=Hibch PE=1 SV=2 | 64 | 417 | 2.0E-83 |
Swissprot ID | Swissprot Description | Start | End | E-value |
---|---|---|---|---|
sp|Q5ZJ60|HIBCH_CHICK | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Gallus gallus GN=HIBCH PE=2 SV=1 | 72 | 417 | 1.0E-88 |
sp|Q58EB4|HIBCH_DANRE | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Danio rerio GN=hibch PE=2 SV=1 | 76 | 417 | 1.0E-87 |
sp|O74802|HIBCH_SCHPO | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN=ehd3 PE=3 SV=1 | 77 | 409 | 9.0E-85 |
sp|A2VDC2|HIBCH_XENLA | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Xenopus laevis GN=hibch PE=2 SV=1 | 88 | 417 | 2.0E-84 |
sp|Q5XIE6|HIBCH_RAT | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Rattus norvegicus GN=Hibch PE=1 SV=2 | 64 | 417 | 2.0E-83 |
sp|Q6NVY1|HIBCH_HUMAN | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Homo sapiens GN=HIBCH PE=1 SV=2 | 72 | 417 | 1.0E-81 |
sp|Q28FR6|HIBCH_XENTR | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Xenopus tropicalis GN=hibch PE=2 SV=1 | 88 | 438 | 5.0E-81 |
sp|Q8QZS1|HIBCH_MOUSE | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Mus musculus GN=Hibch PE=1 SV=1 | 64 | 417 | 8.0E-80 |
sp|Q9LKJ1|HIBC1_ARATH | 3-hydroxyisobutyryl-CoA hydrolase 1 OS=Arabidopsis thaliana GN=CHY1 PE=1 SV=1 | 77 | 415 | 1.0E-78 |
sp|Q55GS6|HIBCH_DICDI | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Dictyostelium discoideum GN=hibch PE=3 SV=1 | 63 | 417 | 1.0E-76 |
sp|Q6NMB0|HIBC3_ARATH | Probable 3-hydroxyisobutyryl-CoA hydrolase 3 OS=Arabidopsis thaliana GN=At2g30660 PE=2 SV=1 | 77 | 415 | 6.0E-76 |
sp|P28817|HIBCH_YEAST | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=EHD3 PE=1 SV=2 | 77 | 501 | 3.0E-71 |
sp|Q1PEY5|HIBC2_ARATH | Probable 3-hydroxyisobutyryl-CoA hydrolase 2 OS=Arabidopsis thaliana GN=At2g30650 PE=2 SV=1 | 77 | 417 | 3.0E-70 |
sp|Q2HJ73|HIBCH_BOVIN | 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial OS=Bos taurus GN=HIBCH PE=2 SV=1 | 72 | 417 | 2.0E-67 |
sp|Q9SHJ8|HIBC8_ARATH | 3-hydroxyisobutyryl-CoA hydrolase-like protein 5 OS=Arabidopsis thaliana GN=At1g06550 PE=1 SV=2 | 69 | 417 | 1.0E-59 |
sp|Q8RXN4|HIBC5_ARATH | 3-hydroxyisobutyryl-CoA hydrolase-like protein 2, mitochondrial OS=Arabidopsis thaliana GN=At4g31810 PE=2 SV=1 | 71 | 437 | 4.0E-58 |
sp|Q5XF59|HIBC4_ARATH | 3-hydroxyisobutyryl-CoA hydrolase-like protein 1, mitochondrial OS=Arabidopsis thaliana GN=At3g60510 PE=2 SV=1 | 72 | 428 | 4.0E-56 |
sp|Q9LK08|HIBC7_ARATH | 3-hydroxyisobutyryl-CoA hydrolase-like protein 4, mitochondrial OS=Arabidopsis thaliana GN=At3g24360 PE=2 SV=1 | 84 | 417 | 8.0E-47 |
sp|Q9T0K7|HIBC6_ARATH | 3-hydroxyisobutyryl-CoA hydrolase-like protein 3, mitochondrial OS=Arabidopsis thaliana GN=At4g13360 PE=1 SV=2 | 84 | 417 | 1.0E-46 |
sp|Q3TLP5|ECHD2_MOUSE | Enoyl-CoA hydratase domain-containing protein 2, mitochondrial OS=Mus musculus GN=Echdc2 PE=1 SV=2 | 84 | 257 | 2.0E-18 |
sp|O34893|YNGF_BACSU | Putative enoyl-CoA hydratase/isomerase YngF OS=Bacillus subtilis (strain 168) GN=yngF PE=3 SV=1 | 88 | 231 | 5.0E-18 |
sp|Q2TBT3|ECHD2_BOVIN | Enoyl-CoA hydratase domain-containing protein 2, mitochondrial OS=Bos taurus GN=ECHDC2 PE=2 SV=1 | 84 | 257 | 2.0E-17 |
sp|P52046|CRT_CLOAB | Short-chain-enoyl-CoA hydratase OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) GN=crt PE=1 SV=1 | 73 | 321 | 6.0E-17 |
sp|Q86YB7|ECHD2_HUMAN | Enoyl-CoA hydratase domain-containing protein 2, mitochondrial OS=Homo sapiens GN=ECHDC2 PE=1 SV=2 | 84 | 257 | 6.0E-17 |
sp|A4YI89|HPCD_METS5 | 3-hydroxypropionyl-coenzyme A dehydratase OS=Metallosphaera sedula (strain ATCC 51363 / DSM 5348) GN=Msed_2001 PE=1 SV=1 | 88 | 275 | 1.0E-16 |
sp|Q8GB17|CAID_PROSL | Carnitinyl-CoA dehydratase OS=Proteus sp. (strain LE138) GN=caiD PE=1 SV=3 | 81 | 275 | 3.0E-15 |
sp|B4EY26|CAID_PROMH | Carnitinyl-CoA dehydratase OS=Proteus mirabilis (strain HI4320) GN=caiD PE=3 SV=1 | 81 | 275 | 3.0E-15 |
sp|Q52995|ECHH_RHIME | Probable enoyl-CoA hydratase OS=Rhizobium meliloti (strain 1021) GN=fadB1 PE=3 SV=2 | 80 | 259 | 8.0E-15 |
sp|Q8BH95|ECHM_MOUSE | Enoyl-CoA hydratase, mitochondrial OS=Mus musculus GN=Echs1 PE=1 SV=1 | 60 | 275 | 1.0E-14 |
sp|P14604|ECHM_RAT | Enoyl-CoA hydratase, mitochondrial OS=Rattus norvegicus GN=Echs1 PE=1 SV=1 | 88 | 278 | 2.0E-14 |
sp|P30084|ECHM_HUMAN | Enoyl-CoA hydratase, mitochondrial OS=Homo sapiens GN=ECHS1 PE=1 SV=4 | 88 | 275 | 4.0E-14 |
sp|Q9TM10|MENB_CYACA | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Cyanidium caldarium GN=menB PE=3 SV=1 | 76 | 310 | 9.0E-14 |
sp|Q869N6|CRTL_DICDI | 3-hydroxybutyryl-CoA dehydratase-like protein, mitochondrial OS=Dictyostelium discoideum GN=DDB_G0271866 PE=3 SV=1 | 84 | 275 | 1.0E-13 |
sp|P23966|MENB_BACSU | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Bacillus subtilis (strain 168) GN=menB PE=1 SV=2 | 76 | 231 | 1.0E-13 |
sp|Q5R646|ECHM_PONAB | Enoyl-CoA hydratase, mitochondrial OS=Pongo abelii GN=ECHS1 PE=2 SV=1 | 88 | 275 | 1.0E-13 |
sp|O85078|CBAD1_ARTSP | 4-chlorobenzoyl coenzyme A dehalogenase-1 OS=Arthrobacter sp. GN=fcbB1 PE=1 SV=2 | 72 | 251 | 1.0E-13 |
sp|Q7CQ56|MENB_SALTY | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=menB PE=1 SV=1 | 76 | 231 | 6.0E-13 |
sp|Q5HQC3|MENB_STAEQ | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) GN=menB PE=3 SV=1 | 73 | 231 | 8.0E-13 |
sp|Q8CPQ4|MENB_STAES | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus epidermidis (strain ATCC 12228) GN=menB PE=3 SV=1 | 73 | 231 | 8.0E-13 |
sp|Q9LCU3|CBAD2_ARTSP | 4-chlorobenzoyl coenzyme A dehalogenase-2 OS=Arthrobacter sp. GN=fcbB2 PE=1 SV=1 | 72 | 251 | 8.0E-13 |
sp|Q4L549|MENB_STAHJ | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus haemolyticus (strain JCSC1435) GN=menB PE=3 SV=1 | 73 | 231 | 9.0E-13 |
sp|P0ABU0|MENB_ECOLI | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Escherichia coli (strain K12) GN=menB PE=1 SV=1 | 76 | 231 | 1.0E-12 |
sp|P0ABU1|MENB_ECOL6 | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=menB PE=3 SV=1 | 76 | 231 | 1.0E-12 |
sp|Q49WG8|MENB_STAS1 | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) GN=menB PE=3 SV=1 | 73 | 231 | 2.0E-12 |
sp|B5RGA4|CAID_SALG2 | Carnitinyl-CoA dehydratase OS=Salmonella gallinarum (strain 287/91 / NCTC 13346) GN=caiD PE=3 SV=1 | 88 | 277 | 2.0E-12 |
sp|B5R1Q9|CAID_SALEP | Carnitinyl-CoA dehydratase OS=Salmonella enteritidis PT4 (strain P125109) GN=caiD PE=3 SV=1 | 88 | 277 | 2.0E-12 |
sp|A9MYJ5|CAID_SALPB | Carnitinyl-CoA dehydratase OS=Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) GN=caiD PE=3 SV=1 | 88 | 277 | 2.0E-12 |
sp|B5FHG4|CAID_SALDC | Carnitinyl-CoA dehydratase OS=Salmonella dublin (strain CT_02021853) GN=caiD PE=3 SV=1 | 88 | 277 | 2.0E-12 |
sp|Q8ZRX5|CAID_SALTY | Carnitinyl-CoA dehydratase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=caiD PE=3 SV=3 | 88 | 264 | 2.0E-12 |
sp|B4TWR3|CAID_SALSV | Carnitinyl-CoA dehydratase OS=Salmonella schwarzengrund (strain CVM19633) GN=caiD PE=3 SV=1 | 88 | 264 | 2.0E-12 |
sp|B4TIG9|CAID_SALHS | Carnitinyl-CoA dehydratase OS=Salmonella heidelberg (strain SL476) GN=caiD PE=3 SV=1 | 88 | 264 | 2.0E-12 |
sp|B1LFW9|CAID_ECOSM | Carnitinyl-CoA dehydratase OS=Escherichia coli (strain SMS-3-5 / SECEC) GN=caiD PE=3 SV=1 | 88 | 296 | 3.0E-12 |
sp|Q8FLA6|CAID_ECOL6 | Carnitinyl-CoA dehydratase OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=caiD PE=3 SV=3 | 88 | 296 | 3.0E-12 |
sp|Q0TLV3|CAID_ECOL5 | Carnitinyl-CoA dehydratase OS=Escherichia coli O6:K15:H31 (strain 536 / UPEC) GN=caiD PE=3 SV=1 | 88 | 296 | 3.0E-12 |
sp|B4T6J5|CAID_SALNS | Carnitinyl-CoA dehydratase OS=Salmonella newport (strain SL254) GN=caiD PE=3 SV=1 | 88 | 264 | 3.0E-12 |
sp|Q8NXA0|MENB_STAAW | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus aureus (strain MW2) GN=menB PE=3 SV=1 | 73 | 231 | 3.0E-12 |
sp|Q6GAG7|MENB_STAAS | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus aureus (strain MSSA476) GN=menB PE=3 SV=1 | 73 | 231 | 3.0E-12 |
sp|B5BL54|CAID_SALPK | Carnitinyl-CoA dehydratase OS=Salmonella paratyphi A (strain AKU_12601) GN=caiD PE=3 SV=1 | 88 | 277 | 4.0E-12 |
sp|C0Q4L2|CAID_SALPC | Carnitinyl-CoA dehydratase OS=Salmonella paratyphi C (strain RKS4594) GN=caiD PE=3 SV=1 | 88 | 277 | 4.0E-12 |
sp|Q5PIL1|CAID_SALPA | Carnitinyl-CoA dehydratase OS=Salmonella paratyphi A (strain ATCC 9150 / SARB42) GN=caiD PE=3 SV=1 | 88 | 277 | 4.0E-12 |
sp|Q57TJ1|CAID_SALCH | Carnitinyl-CoA dehydratase OS=Salmonella choleraesuis (strain SC-B67) GN=caiD PE=3 SV=1 | 88 | 277 | 4.0E-12 |
sp|B5F749|CAID_SALA4 | Carnitinyl-CoA dehydratase OS=Salmonella agona (strain SL483) GN=caiD PE=3 SV=1 | 88 | 277 | 4.0E-12 |
sp|Q6GI37|MENB_STAAR | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus aureus (strain MRSA252) GN=menB PE=3 SV=1 | 73 | 231 | 4.0E-12 |
sp|Q5HH38|MENB_STAAC | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus aureus (strain COL) GN=menB PE=1 SV=1 | 73 | 231 | 4.0E-12 |
sp|Q8Z9L5|CAID_SALTI | Carnitinyl-CoA dehydratase OS=Salmonella typhi GN=caiD PE=3 SV=3 | 88 | 264 | 4.0E-12 |
sp|Q7A6A9|MENB_STAAN | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus aureus (strain N315) GN=menB PE=1 SV=1 | 73 | 231 | 4.0E-12 |
sp|Q99V48|MENB_STAAM | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) GN=menB PE=3 SV=1 | 73 | 231 | 4.0E-12 |
sp|P31551|CAID_ECOLI | Carnitinyl-CoA dehydratase OS=Escherichia coli (strain K12) GN=caiD PE=1 SV=4 | 88 | 296 | 4.0E-12 |
sp|B1IRE0|CAID_ECOLC | Carnitinyl-CoA dehydratase OS=Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) GN=caiD PE=3 SV=1 | 88 | 296 | 4.0E-12 |
sp|Q1ZXF1|ECHM_DICDI | Probable enoyl-CoA hydratase, mitochondrial OS=Dictyostelium discoideum GN=echs1 PE=3 SV=1 | 82 | 275 | 4.0E-12 |
sp|Q8XA35|CAID_ECO57 | Carnitinyl-CoA dehydratase OS=Escherichia coli O157:H7 GN=caiD PE=3 SV=3 | 88 | 296 | 5.0E-12 |
sp|A8ALR7|CAID_CITK8 | Carnitinyl-CoA dehydratase OS=Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) GN=caiD PE=3 SV=1 | 81 | 277 | 7.0E-12 |
sp|A9MR28|CAID_SALAR | Carnitinyl-CoA dehydratase OS=Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) GN=caiD PE=3 SV=1 | 88 | 264 | 8.0E-12 |
sp|P59395|CAID_SHIFL | Carnitinyl-CoA dehydratase OS=Shigella flexneri GN=caiD PE=3 SV=2 | 88 | 296 | 2.0E-11 |
sp|Q58DM8|ECHM_BOVIN | Enoyl-CoA hydratase, mitochondrial OS=Bos taurus GN=ECHS1 PE=2 SV=1 | 81 | 259 | 2.0E-11 |
sp|Q96DC8|ECHD3_HUMAN | Enoyl-CoA hydratase domain-containing protein 3, mitochondrial OS=Homo sapiens GN=ECHDC3 PE=1 SV=2 | 84 | 228 | 5.0E-11 |
sp|Q9CLV5|MENB_PASMU | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Pasteurella multocida (strain Pm70) GN=menB PE=3 SV=1 | 76 | 231 | 7.0E-11 |
sp|P9WNN9|ECHA8_MYCTU | Probable enoyl-CoA hydratase echA8 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=echA8 PE=1 SV=1 | 80 | 270 | 1.0E-10 |
sp|P9WNN8|ECHA8_MYCTO | Probable enoyl-CoA hydratase echA8 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=echA8 PE=3 SV=1 | 80 | 270 | 1.0E-10 |
sp|P64017|ECHA8_MYCBO | Probable enoyl-CoA hydratase echA8 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=echA8 PE=3 SV=1 | 80 | 270 | 1.0E-10 |
sp|P77467|PAAG_ECOLI | 1,2-epoxyphenylacetyl-CoA isomerase OS=Escherichia coli (strain K12) GN=paaG PE=1 SV=1 | 84 | 272 | 2.0E-10 |
sp|Q9D9V3|ECHD1_MOUSE | Ethylmalonyl-CoA decarboxylase OS=Mus musculus GN=Echdc1 PE=1 SV=2 | 62 | 232 | 3.0E-10 |
sp|Q8GYN9|MENB_ARATH | 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal OS=Arabidopsis thaliana GN=MENB PE=1 SV=2 | 51 | 231 | 3.0E-10 |
sp|P44960|MENB_HAEIN | 1,4-dihydroxy-2-naphthoyl-CoA synthase OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) GN=menB PE=3 SV=1 | 84 | 231 | 3.0E-10 |
sp|Q62651|ECH1_RAT | Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial OS=Rattus norvegicus GN=Ech1 PE=1 SV=2 | 63 | 256 | 8.0E-10 |
sp|O07137|ECHA8_MYCLE | Probable enoyl-CoA hydratase echA8 OS=Mycobacterium leprae (strain TN) GN=echA8 PE=3 SV=1 | 82 | 264 | 1.0E-09 |
sp|O35459|ECH1_MOUSE | Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial OS=Mus musculus GN=Ech1 PE=1 SV=1 | 88 | 231 | 1.0E-09 |
sp|Q5LLW6|DMDD_RUEPO | Methylthioacryloyl-CoA hydratase OS=Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) GN=dmdD PE=1 SV=1 | 84 | 264 | 2.0E-09 |
sp|Q9WUR2|ECI2_MOUSE | Enoyl-CoA delta isomerase 2, mitochondrial OS=Mus musculus GN=Eci2 PE=1 SV=2 | 62 | 257 | 2.0E-09 |
sp|Q3MIE0|ECHD3_RAT | Enoyl-CoA hydratase domain-containing protein 3, mitochondrial OS=Rattus norvegicus GN=Echdc3 PE=2 SV=1 | 70 | 228 | 2.0E-09 |
sp|Q5RFG0|ECH1_PONAB | Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial OS=Pongo abelii GN=ECH1 PE=2 SV=1 | 88 | 256 | 5.0E-09 |
sp|A0PJR5|ECHD3_DANRE | Enoyl-CoA hydratase domain-containing protein 3, mitochondrial OS=Danio rerio GN=echdc3 PE=2 SV=2 | 71 | 228 | 5.0E-09 |
sp|Q13011|ECH1_HUMAN | Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial OS=Homo sapiens GN=ECH1 PE=1 SV=2 | 88 | 256 | 6.0E-09 |
sp|Q6AYG5|ECHD1_RAT | Ethylmalonyl-CoA decarboxylase OS=Rattus norvegicus GN=Echdc1 PE=1 SV=1 | 62 | 232 | 6.0E-09 |
sp|Q9D7J9|ECHD3_MOUSE | Enoyl-CoA hydratase domain-containing protein 3, mitochondrial OS=Mus musculus GN=Echdc3 PE=1 SV=1 | 73 | 228 | 6.0E-09 |
sp|Q7N288|FADJ_PHOLL | Fatty acid oxidation complex subunit alpha OS=Photorhabdus luminescens subsp. laumondii (strain TT01) GN=fadJ PE=3 SV=2 | 88 | 255 | 8.0E-09 |
sp|P41942|YKB4_CAEEL | Uncharacterized protein B0272.4 OS=Caenorhabditis elegans GN=B0272.4 PE=3 SV=1 | 77 | 259 | 9.0E-09 |
sp|B4SZR0|FADJ_SALNS | Fatty acid oxidation complex subunit alpha OS=Salmonella newport (strain SL254) GN=fadJ PE=3 SV=1 | 94 | 289 | 9.0E-09 |
sp|Q8Z4Z0|FADJ_SALTI | Fatty acid oxidation complex subunit alpha OS=Salmonella typhi GN=fadJ PE=3 SV=1 | 94 | 289 | 9.0E-09 |
sp|B4TCA8|FADJ_SALHS | Fatty acid oxidation complex subunit alpha OS=Salmonella heidelberg (strain SL476) GN=fadJ PE=3 SV=1 | 94 | 289 | 9.0E-09 |
sp|B5EZR9|FADJ_SALA4 | Fatty acid oxidation complex subunit alpha OS=Salmonella agona (strain SL483) GN=fadJ PE=3 SV=1 | 94 | 289 | 9.0E-09 |
sp|Q8ZNA7|FADJ_SALTY | Fatty acid oxidation complex subunit alpha OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=fadJ PE=3 SV=1 | 94 | 289 | 9.0E-09 |
sp|B5R3R9|FADJ_SALEP | Fatty acid oxidation complex subunit alpha OS=Salmonella enteritidis PT4 (strain P125109) GN=fadJ PE=3 SV=1 | 94 | 289 | 1.0E-08 |
sp|A9JS71|ECHD3_XENLA | Enoyl-CoA hydratase domain-containing protein 3, mitochondrial OS=Xenopus laevis GN=echdc3 PE=2 SV=1 | 78 | 282 | 1.0E-08 |
sp|B5RCL3|FADJ_SALG2 | Fatty acid oxidation complex subunit alpha OS=Salmonella gallinarum (strain 287/91 / NCTC 13346) GN=fadJ PE=3 SV=1 | 94 | 289 | 1.0E-08 |
sp|Q57LW6|FADJ_SALCH | Fatty acid oxidation complex subunit alpha OS=Salmonella choleraesuis (strain SC-B67) GN=fadJ PE=3 SV=1 | 94 | 289 | 1.0E-08 |
sp|A9N453|FADJ_SALPB | Fatty acid oxidation complex subunit alpha OS=Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) GN=fadJ PE=3 SV=1 | 94 | 289 | 1.0E-08 |
sp|Q39TV7|BAMA_GEOMG | 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase OS=Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) GN=bamA PE=1 SV=1 | 88 | 244 | 1.0E-08 |
sp|Q8FFG4|FADJ_ECOL6 | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 1.0E-08 |
sp|B4TQC2|FADJ_SALSV | Fatty acid oxidation complex subunit alpha OS=Salmonella schwarzengrund (strain CVM19633) GN=fadJ PE=3 SV=1 | 94 | 289 | 1.0E-08 |
sp|B5FPN1|FADJ_SALDC | Fatty acid oxidation complex subunit alpha OS=Salmonella dublin (strain CT_02021853) GN=fadJ PE=3 SV=1 | 94 | 289 | 1.0E-08 |
sp|Q31YB7|FADJ_SHIBS | Fatty acid oxidation complex subunit alpha OS=Shigella boydii serotype 4 (strain Sb227) GN=fadJ PE=3 SV=1 | 88 | 289 | 1.0E-08 |
sp|A5JTM5|CBADH_PSEUC | 4-chlorobenzoyl coenzyme A dehalogenase OS=Pseudomonas sp. (strain CBS-3) PE=1 SV=1 | 84 | 243 | 2.0E-08 |
sp|B2TWV4|FADJ_SHIB3 | Fatty acid oxidation complex subunit alpha OS=Shigella boydii serotype 18 (strain CDC 3083-94 / BS512) GN=fadJ PE=3 SV=1 | 88 | 289 | 2.0E-08 |
sp|B5BBA1|FADJ_SALPK | Fatty acid oxidation complex subunit alpha OS=Salmonella paratyphi A (strain AKU_12601) GN=fadJ PE=3 SV=1 | 94 | 289 | 2.0E-08 |
sp|Q5PCX6|FADJ_SALPA | Fatty acid oxidation complex subunit alpha OS=Salmonella paratyphi A (strain ATCC 9150 / SARB42) GN=fadJ PE=3 SV=1 | 94 | 289 | 2.0E-08 |
sp|Q64428|ECHA_RAT | Trifunctional enzyme subunit alpha, mitochondrial OS=Rattus norvegicus GN=Hadha PE=1 SV=2 | 83 | 243 | 2.0E-08 |
sp|B7NP24|FADJ_ECO7I | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O7:K1 (strain IAI39 / ExPEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 3.0E-08 |
sp|Q54HG7|AUHM_DICDI | Methylglutaconyl-CoA hydratase, mitochondrial OS=Dictyostelium discoideum GN=auh PE=3 SV=1 | 84 | 231 | 3.0E-08 |
sp|A7ZPF8|FADJ_ECO24 | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O139:H28 (strain E24377A / ETEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 4.0E-08 |
sp|B1LME7|FADJ_ECOSM | Fatty acid oxidation complex subunit alpha OS=Escherichia coli (strain SMS-3-5 / SECEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 4.0E-08 |
sp|B7M6M2|FADJ_ECO8A | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O8 (strain IAI1) GN=fadJ PE=3 SV=1 | 88 | 289 | 4.0E-08 |
sp|B6I6Q4|FADJ_ECOSE | Fatty acid oxidation complex subunit alpha OS=Escherichia coli (strain SE11) GN=fadJ PE=3 SV=1 | 88 | 289 | 4.0E-08 |
sp|B1IXA5|FADJ_ECOLC | Fatty acid oxidation complex subunit alpha OS=Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) GN=fadJ PE=3 SV=1 | 88 | 289 | 4.0E-08 |
sp|P34559|ECHM_CAEEL | Probable enoyl-CoA hydratase, mitochondrial OS=Caenorhabditis elegans GN=ech-6 PE=3 SV=1 | 88 | 275 | 5.0E-08 |
sp|B7LBJ5|FADJ_ECO55 | Fatty acid oxidation complex subunit alpha OS=Escherichia coli (strain 55989 / EAEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 5.0E-08 |
sp|Q0T2E6|FADJ_SHIF8 | Fatty acid oxidation complex subunit alpha OS=Shigella flexneri serotype 5b (strain 8401) GN=fadJ PE=3 SV=1 | 88 | 289 | 5.0E-08 |
sp|Q3YZM2|FADJ_SHISS | Fatty acid oxidation complex subunit alpha OS=Shigella sonnei (strain Ss046) GN=fadJ PE=3 SV=1 | 88 | 289 | 6.0E-08 |
sp|Q83QQ0|FADJ_SHIFL | Fatty acid oxidation complex subunit alpha OS=Shigella flexneri GN=fadJ PE=3 SV=1 | 88 | 289 | 6.0E-08 |
sp|Q8DSN0|FABM_STRMU | Trans-2-decenoyl-[acyl-carrier-protein] isomerase OS=Streptococcus mutans serotype c (strain ATCC 700610 / UA159) GN=fabM PE=3 SV=1 | 75 | 271 | 7.0E-08 |
sp|A7MH81|FADJ_CROS8 | Fatty acid oxidation complex subunit alpha OS=Cronobacter sakazakii (strain ATCC BAA-894) GN=fadJ PE=3 SV=1 | 94 | 273 | 7.0E-08 |
sp|A8A2L0|FADJ_ECOHS | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O9:H4 (strain HS) GN=fadJ PE=3 SV=1 | 88 | 289 | 7.0E-08 |
sp|B7MY16|FADJ_ECO81 | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O81 (strain ED1a) GN=fadJ PE=3 SV=1 | 88 | 289 | 7.0E-08 |
sp|B7N5V2|FADJ_ECOLU | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 8.0E-08 |
sp|Q8BMS1|ECHA_MOUSE | Trifunctional enzyme subunit alpha, mitochondrial OS=Mus musculus GN=Hadha PE=1 SV=1 | 83 | 243 | 8.0E-08 |
sp|P76082|PAAF_ECOLI | 2,3-dehydroadipyl-CoA hydratase OS=Escherichia coli (strain K12) GN=paaF PE=1 SV=1 | 88 | 238 | 8.0E-08 |
sp|Q8XCP2|FADJ_ECO57 | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O157:H7 GN=fadJ PE=3 SV=1 | 88 | 289 | 1.0E-07 |
sp|Q0TFA6|FADJ_ECOL5 | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O6:K15:H31 (strain 536 / UPEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 1.0E-07 |
sp|B5YXY4|FADJ_ECO5E | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O157:H7 (strain EC4115 / EHEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 1.0E-07 |
sp|B7UFZ8|FADJ_ECO27 | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O127:H6 (strain E2348/69 / EPEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 1.0E-07 |
sp|Q1R972|FADJ_ECOUT | Fatty acid oxidation complex subunit alpha OS=Escherichia coli (strain UTI89 / UPEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 2.0E-07 |
sp|A1ADI8|FADJ_ECOK1 | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O1:K1 / APEC GN=fadJ PE=3 SV=1 | 88 | 289 | 2.0E-07 |
sp|B7MGV7|FADJ_ECO45 | Fatty acid oxidation complex subunit alpha OS=Escherichia coli O45:K1 (strain S88 / ExPEC) GN=fadJ PE=3 SV=1 | 88 | 289 | 2.0E-07 |
sp|P53526|ECH12_MYCLE | Probable enoyl-CoA hydratase echA12 OS=Mycobacterium leprae (strain TN) GN=echA12 PE=3 SV=1 | 88 | 247 | 2.0E-07 |
sp|P94549|FADB_BACSU | Probable enoyl-CoA hydratase OS=Bacillus subtilis (strain 168) GN=fadB PE=2 SV=1 | 97 | 239 | 3.0E-07 |
sp|Q32DJ4|FADJ_SHIDS | Fatty acid oxidation complex subunit alpha OS=Shigella dysenteriae serotype 1 (strain Sd197) GN=fadJ PE=3 SV=1 | 88 | 289 | 4.0E-07 |
sp|A1JIG4|FADB_YERE8 | Fatty acid oxidation complex subunit alpha OS=Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) GN=fadB PE=3 SV=1 | 84 | 232 | 6.0E-07 |
sp|B7LLD0|FADJ_ESCF3 | Fatty acid oxidation complex subunit alpha OS=Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) GN=fadJ PE=3 SV=1 | 94 | 255 | 7.0E-07 |
sp|Q29554|ECHA_PIG | Trifunctional enzyme subunit alpha, mitochondrial OS=Sus scrofa GN=HADHA PE=1 SV=1 | 83 | 243 | 7.0E-07 |
sp|O75521|ECI2_HUMAN | Enoyl-CoA delta isomerase 2, mitochondrial OS=Homo sapiens GN=ECI2 PE=1 SV=4 | 77 | 264 | 7.0E-07 |
sp|O87872|BAMA_THAAR | 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase OS=Thauera aromatica GN=oah PE=1 SV=1 | 88 | 296 | 9.0E-07 |
sp|O69762|HCHL_PSEFL | Hydroxycinnamoyl-CoA hydratase-lyase OS=Pseudomonas fluorescens PE=1 SV=1 | 77 | 218 | 1.0E-06 |
sp|P77399|FADJ_ECOLI | Fatty acid oxidation complex subunit alpha OS=Escherichia coli (strain K12) GN=fadJ PE=1 SV=1 | 88 | 289 | 1.0E-06 |
sp|B1X9L4|FADJ_ECODH | Fatty acid oxidation complex subunit alpha OS=Escherichia coli (strain K12 / DH10B) GN=fadJ PE=3 SV=1 | 88 | 289 | 1.0E-06 |
sp|C4ZVN2|FADJ_ECOBW | Fatty acid oxidation complex subunit alpha OS=Escherichia coli (strain K12 / MC4100 / BW2952) GN=fadJ PE=3 SV=1 | 88 | 289 | 1.0E-06 |
sp|Q50130|ECHA6_MYCLE | Probable enoyl-CoA hydratase echA6 OS=Mycobacterium leprae (strain TN) GN=echA6 PE=3 SV=1 | 84 | 256 | 1.0E-06 |
sp|Q5R5M8|ECHP_PONAB | Peroxisomal bifunctional enzyme OS=Pongo abelii GN=EHHADH PE=2 SV=1 | 96 | 243 | 1.0E-06 |
sp|Q7MZ92|FADB_PHOLL | Fatty acid oxidation complex subunit alpha OS=Photorhabdus luminescens subsp. laumondii (strain TT01) GN=fadB PE=3 SV=1 | 84 | 231 | 2.0E-06 |
sp|Q5E3U1|FADJ_VIBF1 | Fatty acid oxidation complex subunit alpha OS=Vibrio fischeri (strain ATCC 700601 / ES114) GN=fadJ PE=3 SV=2 | 94 | 269 | 2.0E-06 |
sp|Q5HZQ8|ECHD1_XENLA | Ethylmalonyl-CoA decarboxylase OS=Xenopus laevis GN=echdc1 PE=2 SV=1 | 80 | 262 | 2.0E-06 |
sp|Q5XIC0|ECI2_RAT | Enoyl-CoA delta isomerase 2, mitochondrial OS=Rattus norvegicus GN=Eci2 PE=1 SV=1 | 71 | 300 | 4.0E-06 |
sp|Q6NYL3|ECHP_DANRE | Peroxisomal bifunctional enzyme OS=Danio rerio GN=ehhadh PE=2 SV=1 | 88 | 243 | 4.0E-06 |
sp|Q08426|ECHP_HUMAN | Peroxisomal bifunctional enzyme OS=Homo sapiens GN=EHHADH PE=1 SV=3 | 96 | 243 | 4.0E-06 |
sp|Q28C91|ECHD1_XENTR | Ethylmalonyl-CoA decarboxylase OS=Xenopus tropicalis GN=echdc1 PE=2 SV=1 | 84 | 232 | 5.0E-06 |
sp|Q39659|MFPA_CUCSA | Glyoxysomal fatty acid beta-oxidation multifunctional protein MFP-a OS=Cucumis sativus PE=1 SV=1 | 89 | 255 | 5.0E-06 |
sp|Q3K9D8|FADB_PSEPF | Fatty acid oxidation complex subunit alpha OS=Pseudomonas fluorescens (strain Pf0-1) GN=fadB PE=3 SV=1 | 78 | 232 | 6.0E-06 |
sp|C3K613|FADB_PSEFS | Fatty acid oxidation complex subunit alpha OS=Pseudomonas fluorescens (strain SBW25) GN=fadB PE=3 SV=1 | 78 | 232 | 7.0E-06 |
sp|P24162|ECHH_RHOCB | Probable enoyl-CoA hydratase OS=Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) GN=fadB1 PE=3 SV=1 | 75 | 231 | 8.0E-06 |
GO Term | Description | Terminal node |
---|---|---|
GO:0003860 | 3-hydroxyisobutyryl-CoA hydrolase activity | Yes |
GO:0003824 | catalytic activity | Yes |
GO:0016289 | CoA hydrolase activity | No |
GO:0016788 | hydrolase activity, acting on ester bonds | No |
GO:0016790 | thiolester hydrolase activity | No |
GO:0003674 | molecular_function | No |
GO:0016787 | hydrolase activity | No |
SignalP signal predicted | Location (based on Ymax) |
D score (significance: > 0.45) |
---|---|---|
No | 1 - 18 | 0.45 |
Type of sequence | Sequence |
---|---|
Locus | Download genbank file of locus
The gene with 5 kb flanks (if sufficient flanking sequence is available). For use in cloning design programs. NOTE: features (genes or exons) that are only partially contained within the sequence are completely excluded. |
Protein | >Hirsu2|2957 MSFRALLLRAGPAAGAARRSSSVIRSAGIRSSSTRSMAPDAEAPGRPSGRGPPPPAEALTPEARRIREQPGDEPH DVVFESRYGLRSIMLNRPKKLNSLDGSMIRKIVPRLVEWEKSDMANVVVIKGAGDKAFCAGGDVAVLAQQNKQGT DGWKGSAEYFALEYKLDHYIATYPKPFIAFMDGITMGGGVGLSVHAPFRIATERTVFAMPETTIGFFPDVGASFF LPRMNGAVGTYLALTSNRLKGANVFYAGVATHYLHSTSLPSLEARLAELIFHDGHNLPKRLQIINQTLEEFCTGL PPSPPMELAGELRRAIDRCFSKNTVAQIMAALEAETGETKEWAQQQLETLHKRSPTAVHVTLRQMREGGKWNIAE AFSKEHQMASKFMRHPDFTEGVTALLLRKETPRWKPESLEAIPAGNDVARPFFRFDPKSRLDLLTIRNSYRAYPF RKLGVPSEVEIRDLLSSKPLTPEELADEVIASRGGRQGIAEIVQEIIARKVTVNAEGKATWTNDEGDAKSDEGEA ASDEGDATSSEGEAAGDEGAAPSKL* |
Coding | >Hirsu2|2957 ATGTCCTTCCGTGCCCTCCTCCTCCGCGCCGGGCCAGCCGCCGGTGCTGCGCGCCGCAGCTCCTCCGTCATCCGC AGCGCAGGCATCCGCAGCAGCAGCACGCGTAGCATGGCTCCCGACGCAGAGGCACCCGGTCGCCCGTCCGGCCGC GGTCCACCGCCCCCCGCCGAGGCCCTCACGCCCGAGGCCCGCAGGATCCGAGAACAGCCGGGCGACGAGCCGCAC GACGTCGTGTTCGAGAGCCGGTACGGCCTCCGGTCCATCATGCTGAACCGGCCCAAGAAGCTCAACTCGCTCGAC GGGTCCATGATCCGCAAGATCGTGCCGCGCCTGGTCGAGTGGGAGAAGTCGGACATGGCCAACGTGGTCGTCATC AAGGGCGCGGGCGACAAGGCCTTCTGCGCCGGCGGCGACGTCGCCGTGCTCGCCCAGCAAAACAAGCAGGGCACC GATGGCTGGAAGGGGTCGGCCGAGTACTTCGCCCTCGAGTACAAGCTCGACCACTACATCGCCACCTACCCGAAG CCCTTCATCGCCTTCATGGACGGCATCACCATGGGCGGCGGCGTCGGCCTCAGCGTCCACGCCCCCTTCCGCATC GCGACCGAGAGGACCGTCTTCGCCATGCCGGAGACGACCATCGGCTTCTTCCCGGACGTCGGCGCCTCCTTCTTC CTGCCCCGCATGAACGGCGCCGTCGGCACCTACCTGGCCCTGACCAGCAACCGGCTGAAGGGCGCCAACGTCTTC TACGCCGGCGTCGCCACCCACTACCTGCACTCCACCAGCCTGCCGAGCCTCGAGGCCCGCCTGGCCGAGCTGATC TTCCACGACGGCCACAACCTGCCCAAGAGGCTGCAGATCATCAACCAGACGCTCGAGGAGTTCTGCACCGGCCTG CCGCCCAGCCCGCCCATGGAGCTGGCCGGAGAGCTGCGCCGCGCCATCGACCGCTGCTTCAGCAAAAACACCGTC GCCCAAATCATGGCCGCCCTCGAGGCCGAGACGGGCGAGACCAAGGAATGGGCCCAGCAGCAGCTGGAGACGCTG CACAAGCGGTCTCCGACGGCCGTGCACGTCACGCTCAGGCAAATGCGCGAGGGCGGCAAGTGGAACATAGCCGAG GCCTTTAGCAAAGAGCACCAGATGGCGTCCAAGTTCATGCGGCACCCGGACTTCACCGAGGGCGTCACGGCCCTG CTTCTCCGCAAGGAGACGCCGCGATGGAAGCCCGAGTCGCTCGAGGCCATCCCCGCCGGCAACGACGTGGCCAGG CCCTTCTTCCGATTCGACCCGAAAAGCCGGCTCGACCTCCTCACCATCCGCAATTCGTACCGGGCGTATCCTTTC CGCAAGCTCGGCGTTCCCTCGGAGGTGGAGATCAGGGACCTCCTCTCCTCGAAGCCCTTGACCCCGGAGGAGCTT GCCGACGAGGTCATCGCCTCGCGCGGCGGCCGCCAGGGCATCGCGGAGATCGTCCAGGAAATCATCGCCCGAAAG GTCACGGTCAATGCCGAGGGCAAGGCGACATGGACGAATGACGAGGGCGACGCCAAGAGCGACGAAGGCGAAGCC GCGAGCGACGAGGGCGACGCCACCAGCTCCGAGGGTGAAGCCGCGGGTGATGAAGGCGCCGCGCCCAGCAAGCTG TAG |
Transcript | >Hirsu2|2957 ATGTCCTTCCGTGCCCTCCTCCTCCGCGCCGGGCCAGCCGCCGGTGCTGCGCGCCGCAGCTCCTCCGTCATCCGC AGCGCAGGCATCCGCAGCAGCAGCACGCGTAGCATGGCTCCCGACGCAGAGGCACCCGGTCGCCCGTCCGGCCGC GGTCCACCGCCCCCCGCCGAGGCCCTCACGCCCGAGGCCCGCAGGATCCGAGAACAGCCGGGCGACGAGCCGCAC GACGTCGTGTTCGAGAGCCGGTACGGCCTCCGGTCCATCATGCTGAACCGGCCCAAGAAGCTCAACTCGCTCGAC GGGTCCATGATCCGCAAGATCGTGCCGCGCCTGGTCGAGTGGGAGAAGTCGGACATGGCCAACGTGGTCGTCATC AAGGGCGCGGGCGACAAGGCCTTCTGCGCCGGCGGCGACGTCGCCGTGCTCGCCCAGCAAAACAAGCAGGGCACC GATGGCTGGAAGGGGTCGGCCGAGTACTTCGCCCTCGAGTACAAGCTCGACCACTACATCGCCACCTACCCGAAG CCCTTCATCGCCTTCATGGACGGCATCACCATGGGCGGCGGCGTCGGCCTCAGCGTCCACGCCCCCTTCCGCATC GCGACCGAGAGGACCGTCTTCGCCATGCCGGAGACGACCATCGGCTTCTTCCCGGACGTCGGCGCCTCCTTCTTC CTGCCCCGCATGAACGGCGCCGTCGGCACCTACCTGGCCCTGACCAGCAACCGGCTGAAGGGCGCCAACGTCTTC TACGCCGGCGTCGCCACCCACTACCTGCACTCCACCAGCCTGCCGAGCCTCGAGGCCCGCCTGGCCGAGCTGATC TTCCACGACGGCCACAACCTGCCCAAGAGGCTGCAGATCATCAACCAGACGCTCGAGGAGTTCTGCACCGGCCTG CCGCCCAGCCCGCCCATGGAGCTGGCCGGAGAGCTGCGCCGCGCCATCGACCGCTGCTTCAGCAAAAACACCGTC GCCCAAATCATGGCCGCCCTCGAGGCCGAGACGGGCGAGACCAAGGAATGGGCCCAGCAGCAGCTGGAGACGCTG CACAAGCGGTCTCCGACGGCCGTGCACGTCACGCTCAGGCAAATGCGCGAGGGCGGCAAGTGGAACATAGCCGAG GCCTTTAGCAAAGAGCACCAGATGGCGTCCAAGTTCATGCGGCACCCGGACTTCACCGAGGGCGTCACGGCCCTG CTTCTCCGCAAGGAGACGCCGCGATGGAAGCCCGAGTCGCTCGAGGCCATCCCCGCCGGCAACGACGTGGCCAGG CCCTTCTTCCGATTCGACCCGAAAAGCCGGCTCGACCTCCTCACCATCCGCAATTCGTACCGGGCGTATCCTTTC CGCAAGCTCGGCGTTCCCTCGGAGGTGGAGATCAGGGACCTCCTCTCCTCGAAGCCCTTGACCCCGGAGGAGCTT GCCGACGAGGTCATCGCCTCGCGCGGCGGCCGCCAGGGCATCGCGGAGATCGTCCAGGAAATCATCGCCCGAAAG GTCACGGTCAATGCCGAGGGCAAGGCGACATGGACGAATGACGAGGGCGACGCCAAGAGCGACGAAGGCGAAGCC GCGAGCGACGAGGGCGACGCCACCAGCTCCGAGGGTGAAGCCGCGGGTGATGAAGGCGCCGCGCCCAGCAAGCTG TAG |
Gene | >Hirsu2|2957 ATGTCCTTCCGTGCCCTCCTCCTCCGCGCCGGGCCAGCCGCCGGTGCTGCGCGCCGCAGCTCCTCCGTCATCCGC AGCGCAGGCATCCGCAGCAGCAGCACGCGTAGCATGGCTCCCGACGCAGAGGCACCCGGTCGCCCGTCCGGCCGC GGTCCACCGGTGAGACGGAAAACGACTTCCCGTGTGTGCCCGTCGGCCGCGTGCTGACGAGAAGCCCCCCCCCCC GCCGGCAGCCCCCCGCCGAGGCCCTCACGCCCGAGGCCCGCAGGATCCGAGAACAGCCGGGCGACGAGCCGCACG ACGTCGTGTTCGAGAGCCGGTACGGCCTCCGGTCCATCATGCTGAACCGGCCCAAGAAGCTCAACTCGCTCGACG GGTCCATGATCCGCAAGATCGTGCCGCGCCTGGTCGAGTGGGAGAAGTCGGACATGGCCAACGTGGTCGTCATCA AGGGCGCGGGCGACAAGGCCTTCTGCGCCGGCGGCGACGTCGCCGTGCTCGCCCAGCAAAACAAGCAGGGCACCG ATGGCTGGAAGGGGTCGGCCGAGTACTTCGCCCTCGAGTACAAGCTCGACCACTACATCGCCACCTACCCGAAGC CCTTCATCGCCTTCATGGACGGCATCACCATGGGCGGCGGCGTCGGCCTCAGCGTCCACGCCCCCTTCCGCATCG CGACCGAGAGGACCGTCTTCGCCATGCCGGAGACGACCATCGGCTTCTTCCCGGACGTCGGCGCCTCCTTCTTCC TGCCCCGCATGAACGGCGCCGTCGGCACCTACCTGGCCCTGACCAGCAACCGGCTGAAGGGCGCCAACGTCTTCT ACGCCGGCGTCGCCACCCACTACCTGCACTCCACCAGCCTGCCGAGCCTCGAGGCCCGCCTGGCCGAGCTGATCT TCCACGACGGCCACAACCTGCCCAAGAGGCTGCAGATCATCAACCAGACGCTCGAGGAGTTCTGCACCGGCCTGC CGCCCAGCCCGCCCATGGAGCTGGCCGGAGAGCTGCGCCGCGCCATCGACCGCTGCTTCAGCAAAAACACCGTCG CCCAAATCATGGCCGCCCTCGAGGCCGAGACGGGCGAGACCAAGGAATGGGCCCAGCAGCAGCTGGAGACGCTGC ACAAGCGGTCTCCGACGGCCGTGCACGTCACGCTCAGGCAAATGCGCGAGGGCGGCAAGTGGAACATAGCCGAGG CCTTTAGCAAAGAGCACCAGATGGCGTCCAAGTTCATGCGGCACCCGGACTTCACCGAGGGCGTCACGGCCCTGC TTCTCCGCAAGGAGACGCCGCGATGGAAGCCCGAGTCGCTCGAGGCCATCCCCGCCGGCAACGACGTGGCCAGGC CCTTCTTCCGATTCGACCCGAAAAGCCGGCTCGACCTCCTCACCATCCGCAATTCGTACCGGGCGTATCCTTTCC GCAAGCTCGGCGTTCCCTCGGAGGTGGAGATCAGGGACCTCCTCTCCTCGAAGCCCTTGACCCCGGAGGAGCTTG CCGACGAGGTCATCGCCTCGCGCGGCGGCCGCCAGGGCATCGCGGAGATCGTCCAGGAAATCATCGCCCGAAAGG TCACGGTCAATGCCGAGGGCAAGGCGACATGGACGAATGACGAGGGCGACGCCAAGAGCGACGAAGGCGAAGCCG CGAGCGACGAGGGCGACGCCACCAGCTCCGAGGGTGAAGCCGCGGGTGATGAAGGCGCCGCGCCCAGCAAGCTGT AG |