Fungal Genomics

at Utrecht University

General Properties

Protein IDAgabiH97|056320
Gene name
Locationscaffold_3:889628..892369
Strand+
Gene length (bp)2741
Transcript length (bp)1824
Coding sequence length (bp)1824
Protein length (aa) 608

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PFAM Domains

PFAM Domain ID Short name Long name E-value Start End
PF00441 Acyl-CoA_dh_1 Acyl-CoA dehydrogenase, C-terminal domain 2.2E-41 451 598
PF06090 Ins_P5_2-kin Inositol-pentakisphosphate 2-kinase 2.5E-37 1 197
PF02771 Acyl-CoA_dh_N Acyl-CoA dehydrogenase, N-terminal domain 5.3E-32 228 339
PF02770 Acyl-CoA_dh_M Acyl-CoA dehydrogenase, middle domain 1.7E-22 344 439
PF08028 Acyl-CoA_dh_2 Acyl-CoA dehydrogenase, C-terminal domain 1.2E-13 473 579

Swissprot hits

[Show all]
Swissprot ID Swissprot Description Start End E-value
sp|Q75IM9|IVD_ORYSJ Isovaleryl-CoA dehydrogenase, mitochondrial OS=Oryza sativa subsp. japonica GN=Os05g0125500 PE=2 SV=2 205 599 3.0E-176
sp|Q9JHI5|IVD_MOUSE Isovaleryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Ivd PE=1 SV=1 211 600 4.0E-171
sp|Q5RBD5|IVD_PONAB Isovaleryl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=IVD PE=2 SV=1 207 600 7.0E-171
sp|P26440|IVD_HUMAN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=IVD PE=1 SV=1 212 600 5.0E-170
sp|Q9FS88|MBCD_SOLTU 2-methylacyl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=2MBCD PE=1 SV=2 227 602 2.0E-169
[Show all]
[Show less]
Swissprot ID Swissprot Description Start End E-value
sp|Q75IM9|IVD_ORYSJ Isovaleryl-CoA dehydrogenase, mitochondrial OS=Oryza sativa subsp. japonica GN=Os05g0125500 PE=2 SV=2 205 599 3.0E-176
sp|Q9JHI5|IVD_MOUSE Isovaleryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Ivd PE=1 SV=1 211 600 4.0E-171
sp|Q5RBD5|IVD_PONAB Isovaleryl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=IVD PE=2 SV=1 207 600 7.0E-171
sp|P26440|IVD_HUMAN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=IVD PE=1 SV=1 212 600 5.0E-170
sp|Q9FS88|MBCD_SOLTU 2-methylacyl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=2MBCD PE=1 SV=2 227 602 2.0E-169
sp|P12007|IVD_RAT Isovaleryl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Ivd PE=1 SV=2 207 600 1.0E-168
sp|Q9FS87|IVD_SOLTU Isovaleryl-CoA dehydrogenase, mitochondrial OS=Solanum tuberosum GN=IVD PE=1 SV=2 229 599 2.0E-168
sp|Q3SZI8|IVD_BOVIN Isovaleryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=IVD PE=2 SV=1 203 600 2.0E-166
sp|Q9SWG0|IVD_ARATH Isovaleryl-CoA dehydrogenase, mitochondrial OS=Arabidopsis thaliana GN=IVD PE=1 SV=2 229 599 4.0E-166
sp|P45857|ACDB_BACSU Acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=mmgC PE=2 SV=3 227 597 2.0E-85
sp|P45867|ACDA_BACSU Acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=acdA PE=2 SV=1 227 597 9.0E-85
sp|P52042|ACDS_CLOAB Acyl-CoA dehydrogenase, short-chain specific OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) GN=bcd PE=1 SV=1 227 595 5.0E-82
sp|O34421|ACDC_BACSU Probable acyl-CoA dehydrogenase YngJ OS=Bacillus subtilis (strain 168) GN=yngJ PE=3 SV=1 227 599 4.0E-77
sp|Q07417|ACADS_MOUSE Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acads PE=1 SV=2 234 596 2.0E-75
sp|Q06319|ACDS_MEGEL Acyl-CoA dehydrogenase, short-chain specific OS=Megasphaera elsdenii PE=1 SV=1 227 596 1.0E-74
sp|P15651|ACADS_RAT Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acads PE=1 SV=2 234 596 2.0E-74
sp|Q5RAS0|ACADS_PONAB Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=ACADS PE=2 SV=1 240 595 4.0E-74
sp|P16219|ACADS_HUMAN Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADS PE=1 SV=1 240 595 2.0E-73
sp|Q9DBL1|ACDSB_MOUSE Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadsb PE=1 SV=1 217 600 6.0E-73
sp|P70584|ACDSB_RAT Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadsb PE=1 SV=1 227 600 1.0E-72
sp|P45954|ACDSB_HUMAN Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADSB PE=1 SV=1 227 600 4.0E-72
sp|Q5RF40|ACDSB_PONAB Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pongo abelii GN=ACADSB PE=2 SV=1 227 600 6.0E-72
sp|P79273|ACADS_PIG Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADS PE=2 SV=1 234 596 6.0E-71
sp|G3KIM8|ACRC_CLOPR Acryloyl-CoA reductase (NADH) OS=Clostridium propionicum GN=acrC PE=1 SV=1 227 598 4.0E-70
sp|Q5EAD4|ACDSB_BOVIN Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADSB PE=2 SV=1 227 597 1.0E-69
sp|Q3ZBF6|ACADS_BOVIN Short-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADS PE=1 SV=1 234 596 1.0E-69
sp|Q54RR5|ACDSB_DICDI Probable short/branched chain specific acyl-CoA dehydrogenase OS=Dictyostelium discoideum GN=acadsb PE=3 SV=1 224 598 5.0E-68
sp|Q54IM8|ACAD8_DICDI Isobutyryl-CoA dehydrogenase, mitochondrial OS=Dictyostelium discoideum GN=acad8 PE=3 SV=1 212 604 1.0E-65
sp|P9WQG1|ACDP_MYCTU Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE25 PE=1 SV=1 227 597 2.0E-65
sp|P9WQG0|ACDP_MYCTO Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE25 PE=3 SV=1 227 597 2.0E-65
sp|P63428|ACDP_MYCBO Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE25 PE=3 SV=1 227 597 2.0E-65
sp|Q2LQN9|CH1CO_SYNAS Cyclohex-1-ene-1-carbonyl-CoA dehydrogenase OS=Syntrophus aciditrophicus (strain SB) GN=SYN_02587 PE=1 SV=1 227 599 2.0E-64
sp|P46703|ACDP_MYCLE Probable acyl-CoA dehydrogenase fadE25 OS=Mycobacterium leprae (strain TN) GN=fadE25 PE=3 SV=1 227 597 7.0E-63
sp|P51174|ACADL_MOUSE Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadl PE=1 SV=2 234 599 8.0E-62
sp|P15650|ACADL_RAT Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadl PE=1 SV=1 234 599 3.0E-61
sp|P79274|ACADL_PIG Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADL PE=2 SV=1 234 599 7.0E-61
sp|Q0NXR6|ACAD8_BOVIN Isobutyryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACAD8 PE=2 SV=1 226 599 1.0E-60
sp|Q9D7B6|ACAD8_MOUSE Isobutyryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acad8 PE=1 SV=2 205 599 3.0E-60
sp|Q9H845|ACAD9_HUMAN Acyl-CoA dehydrogenase family member 9, mitochondrial OS=Homo sapiens GN=ACAD9 PE=1 SV=1 233 607 2.0E-59
sp|Q8JZN5|ACAD9_MOUSE Acyl-CoA dehydrogenase family member 9, mitochondrial OS=Mus musculus GN=Acad9 PE=1 SV=2 233 607 2.0E-58
sp|P28330|ACADL_HUMAN Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADL PE=1 SV=2 234 599 3.0E-58
sp|Q9UKU7|ACAD8_HUMAN Isobutyryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACAD8 PE=1 SV=1 226 599 4.0E-58
sp|Q9VSA3|ACADM_DROME Probable medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Drosophila melanogaster GN=CG12262 PE=1 SV=1 221 601 5.0E-58
sp|Q60HI0|ACADL_MACFA Long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADL PE=2 SV=1 234 598 6.0E-58
sp|Q2LQP0|CHCOA_SYNAS Cyclohexane-1-carbonyl-CoA dehydrogenase OS=Syntrophus aciditrophicus (strain SB) GN=SYN_02586 PE=1 SV=1 221 602 1.0E-56
sp|C3UVB0|ACD_DESML Glutaryl-CoA dehydrogenase OS=Desulfococcus multivorans GN=Acd PE=1 SV=1 227 595 3.0E-56
sp|P41367|ACADM_PIG Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Sus scrofa GN=ACADM PE=1 SV=3 227 598 3.0E-56
sp|Q22347|ACADM_CAEEL Probable medium-chain specific acyl-CoA dehydrogenase 10, mitochondrial OS=Caenorhabditis elegans GN=acdh-10 PE=2 SV=1 211 602 4.0E-56
sp|A8XNF0|ACAD1_CAEBR Probable medium-chain specific acyl-CoA dehydrogenase 1, mitochondrial OS=Caenorhabditis briggsae GN=CBG15946 PE=3 SV=1 211 602 1.0E-55
sp|P11310|ACADM_HUMAN Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADM PE=1 SV=1 227 598 1.0E-54
sp|A5A6I0|ACADM_PANTR Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Pan troglodytes GN=ACADM PE=2 SV=1 227 598 2.0E-54
sp|O32176|FADE_BACSU Probable acyl-CoA dehydrogenase OS=Bacillus subtilis (strain 168) GN=fadE PE=2 SV=1 227 599 3.0E-54
sp|Q8HXY8|ACADM_MACFA Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADM PE=2 SV=1 227 598 2.0E-53
sp|Q3SZB4|ACADM_BOVIN Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADM PE=2 SV=1 211 598 6.0E-52
sp|P45952|ACADM_MOUSE Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadm PE=1 SV=1 227 601 6.0E-52
sp|Q20772|GCDH_CAEEL Probable glutaryl-CoA dehydrogenase, mitochondrial OS=Caenorhabditis elegans GN=F54D5.7 PE=1 SV=1 227 597 8.0E-52
sp|A8WP91|ACAD2_CAEBR Probable medium-chain specific acyl-CoA dehydrogenase 2, mitochondrial OS=Caenorhabditis briggsae GN=CBG00953 PE=3 SV=2 227 602 1.0E-51
sp|P08503|ACADM_RAT Medium-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadm PE=1 SV=1 205 601 3.0E-51
sp|P49748|ACADV_HUMAN Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=ACADVL PE=1 SV=1 227 595 1.0E-50
sp|Q8HXY7|ACADV_MACFA Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=ACADVL PE=2 SV=1 227 595 1.0E-49
sp|Q54R47|GCDH_DICDI Glutaryl-CoA dehydrogenase, mitochondrial OS=Dictyostelium discoideum GN=gcdh PE=3 SV=1 227 597 4.0E-49
sp|P45953|ACADV_RAT Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Rattus norvegicus GN=Acadvl PE=1 SV=1 262 595 8.0E-47
sp|P48818|ACADV_BOVIN Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=ACADVL PE=2 SV=3 265 595 3.0E-46
sp|P50544|ACADV_MOUSE Very long-chain specific acyl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Acadvl PE=1 SV=3 262 595 8.0E-46
sp|Q96329|ACOX4_ARATH Acyl-coenzyme A oxidase 4, peroxisomal OS=Arabidopsis thaliana GN=ACX4 PE=1 SV=1 227 598 3.0E-45
sp|Q2KHZ9|GCDH_BOVIN Glutaryl-CoA dehydrogenase, mitochondrial OS=Bos taurus GN=GCDH PE=2 SV=1 227 597 2.0E-43
sp|P81140|GCDH_PIG Glutaryl-CoA dehydrogenase, mitochondrial (Fragment) OS=Sus scrofa GN=GCDH PE=1 SV=1 227 597 3.0E-42
sp|Q92947|GCDH_HUMAN Glutaryl-CoA dehydrogenase, mitochondrial OS=Homo sapiens GN=GCDH PE=1 SV=1 227 597 3.0E-41
sp|Q0T8F5|CAIA_SHIF8 Crotonobetainyl-CoA dehydrogenase OS=Shigella flexneri serotype 5b (strain 8401) GN=caiA PE=3 SV=1 251 597 1.0E-40
sp|Q3Z5W9|CAIA_SHISS Crotonobetainyl-CoA dehydrogenase OS=Shigella sonnei (strain Ss046) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|P60587|CAIA_SHIFL Crotonobetainyl-CoA dehydrogenase OS=Shigella flexneri GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|Q32K58|CAIA_SHIDS Crotonobetainyl-CoA dehydrogenase OS=Shigella dysenteriae serotype 1 (strain Sd197) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B7LWN0|CAIA_ESCF3 Crotonobetainyl-CoA dehydrogenase OS=Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|Q1RGF9|CAIA_ECOUT Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain UTI89 / UPEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B1LFX2|CAIA_ECOSM Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain SMS-3-5 / SECEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B6HYZ0|CAIA_ECOSE Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain SE11) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B7N7R4|CAIA_ECOLU Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|P60584|CAIA_ECOLI Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12) GN=caiA PE=1 SV=1 251 597 2.0E-40
sp|B1IRD7|CAIA_ECOLC Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|P60585|CAIA_ECOL6 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|A1A789|CAIA_ECOK1 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O1:K1 / APEC GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|A7ZVY9|CAIA_ECOHS Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O9:H4 (strain HS) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B1XBG4|CAIA_ECODH Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12 / DH10B) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|C4ZPW5|CAIA_ECOBW Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain K12 / MC4100 / BW2952) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B7MNP6|CAIA_ECO81 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O81 (strain ED1a) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B7NHE3|CAIA_ECO7I Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O7:K1 (strain IAI39 / ExPEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B5YYD3|CAIA_ECO5E Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O157:H7 (strain EC4115 / EHEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|P60586|CAIA_ECO57 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O157:H7 GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B7L4G2|CAIA_ECO55 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli (strain 55989 / EAEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B7MAG2|CAIA_ECO45 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O45:K1 (strain S88 / ExPEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|B7UI85|CAIA_ECO27 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O127:H6 (strain E2348/69 / EPEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|A7ZHD0|CAIA_ECO24 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O139:H28 (strain E24377A / ETEC) GN=caiA PE=3 SV=1 251 597 2.0E-40
sp|Q0TLV0|CAIA_ECOL5 Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O6:K15:H31 (strain 536 / UPEC) GN=caiA PE=3 SV=1 251 597 3.0E-40
sp|B7M0D6|CAIA_ECO8A Crotonobetainyl-CoA dehydrogenase OS=Escherichia coli O8 (strain IAI1) GN=caiA PE=3 SV=1 251 597 3.0E-40
sp|Q8HXX8|GCDH_MACFA Glutaryl-CoA dehydrogenase, mitochondrial OS=Macaca fascicularis GN=GCDH PE=2 SV=1 227 597 5.0E-40
sp|Q60759|GCDH_MOUSE Glutaryl-CoA dehydrogenase, mitochondrial OS=Mus musculus GN=Gcdh PE=1 SV=2 227 597 2.0E-39
sp|Q8GB20|CAIA_PROSL Crotonobetainyl-CoA dehydrogenase OS=Proteus sp. (strain LE138) GN=caiA PE=3 SV=1 227 597 3.0E-39
sp|B4EY23|CAIA_PROMH Crotonobetainyl-CoA dehydrogenase OS=Proteus mirabilis (strain HI4320) GN=caiA PE=3 SV=1 227 597 3.0E-39
sp|A9MQH5|CAIA_SALAR Crotonobetainyl-CoA dehydrogenase OS=Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980) GN=caiA PE=3 SV=1 251 597 7.0E-39
sp|Q8ZRX2|CAIA_SALTY Crotonobetainyl-CoA dehydrogenase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|B4TWR6|CAIA_SALSV Crotonobetainyl-CoA dehydrogenase OS=Salmonella schwarzengrund (strain CVM19633) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|B5BL57|CAIA_SALPK Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi A (strain AKU_12601) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|C0Q4L5|CAIA_SALPC Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi C (strain RKS4594) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|A9MYJ9|CAIA_SALPB Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|Q5PIN6|CAIA_SALPA Crotonobetainyl-CoA dehydrogenase OS=Salmonella paratyphi A (strain ATCC 9150 / SARB42) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|B4T6J8|CAIA_SALNS Crotonobetainyl-CoA dehydrogenase OS=Salmonella newport (strain SL254) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|B4TIH2|CAIA_SALHS Crotonobetainyl-CoA dehydrogenase OS=Salmonella heidelberg (strain SL476) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|B5RGA6|CAIA_SALG2 Crotonobetainyl-CoA dehydrogenase OS=Salmonella gallinarum (strain 287/91 / NCTC 13346) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|B5R1R2|CAIA_SALEP Crotonobetainyl-CoA dehydrogenase OS=Salmonella enteritidis PT4 (strain P125109) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|B5FHG7|CAIA_SALDC Crotonobetainyl-CoA dehydrogenase OS=Salmonella dublin (strain CT_02021853) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|Q57TI8|CAIA_SALCH Crotonobetainyl-CoA dehydrogenase OS=Salmonella choleraesuis (strain SC-B67) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|B5F752|CAIA_SALA4 Crotonobetainyl-CoA dehydrogenase OS=Salmonella agona (strain SL483) GN=caiA PE=3 SV=1 251 597 1.0E-38
sp|Q8Z9L2|CAIA_SALTI Crotonobetainyl-CoA dehydrogenase OS=Salmonella typhi GN=caiA PE=3 SV=1 251 597 4.0E-38
sp|P34275|IVD_CAEEL Probable acyl-CoA dehydrogenase 6 OS=Caenorhabditis elegans GN=acdh-6 PE=3 SV=2 221 595 5.0E-38
sp|A8ALR4|CAIA_CITK8 Crotonobetainyl-CoA dehydrogenase OS=Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696) GN=caiA PE=3 SV=1 251 597 6.0E-38
sp|P0A9U8|YDIO_ECOLI Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli (strain K12) GN=ydiO PE=3 SV=1 254 598 9.0E-35
sp|P0A9U9|YDIO_ECOL6 Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) GN=ydiO PE=3 SV=1 254 598 9.0E-35
sp|P0A9V0|YDIO_ECO57 Probable acyl-CoA dehydrogenase YdiO OS=Escherichia coli O157:H7 GN=ydiO PE=3 SV=1 254 598 9.0E-35
sp|P63430|Y897_MYCBO Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE10 PE=3 SV=1 253 598 2.0E-31
sp|P9WQF7|Y873_MYCTU Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE10 PE=1 SV=1 253 598 2.0E-31
sp|P9WQF6|Y873_MYCTO Probable acyl-CoA dehydrogenase FadE10 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE10 PE=3 SV=1 253 598 2.0E-31
sp|Q9KJE8|BBSG_THAAR (R)-benzylsuccinyl-CoA dehydrogenase OS=Thauera aromatica GN=bbsG PE=1 SV=1 270 599 1.0E-22
sp|P9WQG3|ACDC_MYCTU Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=fadE12 PE=1 SV=1 262 590 6.0E-22
sp|P9WQG2|ACDC_MYCTO Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=fadE12 PE=3 SV=1 262 590 6.0E-22
sp|Q7U0Y2|ACDC_MYCBO Acyl-CoA dehydrogenase fadE12 OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=fadE12 PE=3 SV=1 262 590 8.0E-22
sp|P0CO34|IPPK_CRYNJ Inositol-pentakisphosphate 2-kinase OS=Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC MYA-565) GN=IPK1 PE=3 SV=1 1 198 2.0E-19
sp|P0CO35|IPPK_CRYNB Inositol-pentakisphosphate 2-kinase OS=Cryptococcus neoformans var. neoformans serotype D (strain B-3501A) GN=IPK1 PE=3 SV=1 1 198 2.0E-19
sp|P33224|AIDB_ECOLI Putative acyl-CoA dehydrogenase AidB OS=Escherichia coli (strain K12) GN=aidB PE=1 SV=3 336 602 5.0E-18
sp|Q73ZP8|MBTN_MYCPA Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) GN=mbtN PE=3 SV=1 260 590 2.0E-17
sp|Q1BBA3|MBTN_MYCSS Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium sp. (strain MCS) GN=mbtN PE=3 SV=1 329 590 2.0E-16
sp|Q8K370|ACD10_MOUSE Acyl-CoA dehydrogenase family member 10 OS=Mus musculus GN=Acad10 PE=1 SV=1 226 597 8.0E-16
sp|P9WQF9|MBTN_MYCTU Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) GN=mbtN PE=1 SV=1 233 603 2.0E-15
sp|P9WQF8|MBTN_MYCTO Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) GN=mbtN PE=3 SV=1 233 603 2.0E-15
sp|P63432|MBTN_MYCBO Acyl-[acyl-carrier-protein] dehydrogenase MbtN OS=Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97) GN=mbtN PE=3 SV=1 233 603 2.0E-15
sp|Q6JQN1|ACD10_HUMAN Acyl-CoA dehydrogenase family member 10 OS=Homo sapiens GN=ACAD10 PE=1 SV=1 242 597 1.0E-14
sp|Q4P4C1|IPPK_USTMA Inositol-pentakisphosphate 2-kinase OS=Ustilago maydis (strain 521 / FGSC 9021) GN=IPK1 PE=3 SV=2 12 203 2.0E-14
sp|Q5LLW7|DMDC_RUEPO 3-methylmercaptopropionyl-CoA dehydrogenase OS=Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) GN=dmdC PE=1 SV=1 264 598 7.0E-14
sp|Q9XWZ2|ACD11_CAEEL Acyl-CoA dehydrogenase family member 11 OS=Caenorhabditis elegans GN=acdh-11 PE=1 SV=1 289 607 6.0E-12
sp|Q8X7R2|FADE_ECO57 Acyl-coenzyme A dehydrogenase OS=Escherichia coli O157:H7 GN=fadE PE=3 SV=2 219 566 1.0E-11
sp|Q8ZRJ7|FADE_SALTY Acyl-coenzyme A dehydrogenase OS=Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) GN=fadE PE=2 SV=1 219 566 1.0E-11
sp|Q8Z937|FADE_SALTI Acyl-coenzyme A dehydrogenase OS=Salmonella typhi GN=fadE PE=3 SV=1 219 566 2.0E-11
sp|Q47146|FADE_ECOLI Acyl-coenzyme A dehydrogenase OS=Escherichia coli (strain K12) GN=fadE PE=2 SV=2 219 566 2.0E-11
sp|P96608|YDBM_BACSU Putative acyl-CoA dehydrogenase YdbM OS=Bacillus subtilis (strain 168) GN=ydbM PE=2 SV=1 245 579 3.0E-11
sp|Q8ZBY6|FADE_YERPE Acyl-coenzyme A dehydrogenase OS=Yersinia pestis GN=fadE PE=3 SV=1 219 564 6.0E-11
sp|Q5ZHT1|ACD11_CHICK Acyl-CoA dehydrogenase family member 11 OS=Gallus gallus GN=ACAD11 PE=2 SV=1 320 597 6.0E-11
sp|Q8RWZ3|IBR3_ARATH Probable acyl-CoA dehydrogenase IBR3 OS=Arabidopsis thaliana GN=IBR3 PE=1 SV=1 272 597 7.0E-10
sp|B3DMA2|ACD11_RAT Acyl-CoA dehydrogenase family member 11 OS=Rattus norvegicus GN=Acad11 PE=1 SV=1 320 597 7.0E-09
sp|Q80XL6|ACD11_MOUSE Acyl-CoA dehydrogenase family member 11 OS=Mus musculus GN=Acad11 PE=1 SV=2 320 597 3.0E-08
sp|Q5R778|ACD11_PONAB Acyl-CoA dehydrogenase family member 11 OS=Pongo abelii GN=ACAD11 PE=2 SV=2 320 591 1.0E-07
sp|Q709F0|ACD11_HUMAN Acyl-CoA dehydrogenase family member 11 OS=Homo sapiens GN=ACAD11 PE=1 SV=2 320 591 1.0E-07
sp|P54998|SOXC_RHOSG Dibenzothiophene desulfurization enzyme C OS=Rhodococcus sp. (strain IGTS8) GN=soxC PE=1 SV=1 250 583 3.0E-07
sp|Q7XQZ6|IPK1_ORYSJ Inositol-pentakisphosphate 2-kinase IPK1 OS=Oryza sativa subsp. japonica GN=IPK1 PE=2 SV=1 1 203 2.0E-06
sp|B8AVX5|IPK1_ORYSI Inositol-pentakisphosphate 2-kinase IPK1 OS=Oryza sativa subsp. indica GN=IPK1 PE=3 SV=1 1 203 2.0E-06
sp|O64894|ACOX2_CUCMA Acyl-coenzyme A oxidase, peroxisomal OS=Cucurbita maxima GN=Acx PE=1 SV=1 295 590 5.0E-06
sp|P0CZ23|ACOX3_ARATH Acyl-coenzyme A oxidase 3, peroxisomal OS=Arabidopsis thaliana GN=ACX3 PE=1 SV=1 282 493 7.0E-06
[Show less]

GO

GO Term Description Terminal node
GO:0016627 oxidoreductase activity, acting on the CH-CH group of donors Yes
GO:0035299 inositol pentakisphosphate 2-kinase activity Yes
GO:0050660 flavin adenine dinucleotide binding Yes
GO:0005524 ATP binding Yes
GO:0097367 carbohydrate derivative binding No
GO:0036094 small molecule binding No
GO:0030554 adenyl nucleotide binding No
GO:1901363 heterocyclic compound binding No
GO:0005488 binding No
GO:0043167 ion binding No
GO:0016773 phosphotransferase activity, alcohol group as acceptor No
GO:0032559 adenyl ribonucleotide binding No
GO:0043168 anion binding No
GO:0016301 kinase activity No
GO:0016772 transferase activity, transferring phosphorus-containing groups No
GO:0097159 organic cyclic compound binding No
GO:0017076 purine nucleotide binding No
GO:0035639 purine ribonucleoside triphosphate binding No
GO:0016740 transferase activity No
GO:0003674 molecular_function No
GO:1901265 nucleoside phosphate binding No
GO:0032553 ribonucleotide binding No
GO:0003824 catalytic activity No
GO:0016491 oxidoreductase activity No
GO:0032555 purine ribonucleotide binding No
GO:0000166 nucleotide binding No

SignalP

[Help with interpreting these statistics]
SignalP signal predicted Location
(based on Ymax)
D score
(significance: > 0.45)
No 1 - 13 0.45

Transmembrane Domains

(None)

Transcription Factor Class

(None)

Expression data

Analysis 1: Developmental stages of Agaricus bisporus (strain A15). Published in Pelkmans et al, Applied Microbiology and Biotechnology, 2016

Click here for more information

Sequences

Type of sequenceSequence
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 >AgabiH97|056320
MHSHMRSSKDCKYANKYCPLDLFSGNPHRVQQAIDDLWDAWERSDGEVNNLKIFSRGKAVRPGQIVRLLHEDFIT
SVSPDRIQEVFKKALCDTLLQSPILSIISRLQRTLDVLDIEGLSKLWREAQLESLSDEQIQTSSPPLTYLLSATF
KDCSIIARLGLLKPGNHSEIQEEQIRVIDLDPKSLNRLPRWEELDREIVMSYVPAERKMPALQKRAISLYNSEVS
GLTDEELEFRNAVVDFAQKEVAPRAAEIDRTNISPMDLWEKLGSMGLLGITVDQKYNGLNLGYLHHTLAMEALSE
ASGSVALSYGAHSNLCVNQIHRHGTEAQKEKYLKDLVDGTKVGSLAMSETGSGSDVVSMRLKAEKVQGGWKLNGN
KFWITNGPVASTLVVYAKTAPELGSKGITTFVIERGFEGFSTSQKLDKFGMRGSDTCELVFEDCVVPEENVLGQV
NKGAAVLMSGLDLERVVLSGGPLGLMQAAFDYAVEYIHDRKQFGQPVGTFQLMQAKIADMYTKLNASRSYVYSVA
RACDRGKVSRKDCAGAIMYSTEKAVEVALEGMQCLGGNGYINDYPMGRILRDSRLYTVGAGTQEIRRMLIGREFN
EHDYCIL*
Coding >AgabiH97|056320
ATGCATAGTCATATGCGTAGCAGTAAAGATTGCAAGTATGCCAACAAGTACTGCCCCCTCGACTTGTTCTCTGGA
AACCCCCATCGTGTTCAACAAGCCATCGACGACTTATGGGACGCCTGGGAGCGAAGTGACGGCGAGGTCAACAAT
CTAAAAATATTTTCACGCGGGAAGGCAGTTAGGCCAGGCCAGATTGTACGCTTGTTGCACGAAGATTTCATAACG
TCCGTATCTCCTGATAGGATACAAGAGGTTTTCAAAAAGGCGTTGTGTGACACCCTTCTGCAATCGCCCATTCTC
AGCATCATCTCGAGGCTCCAGAGGACTTTGGATGTTTTGGATATCGAGGGTCTATCGAAATTATGGCGTGAAGCT
CAACTTGAGTCTCTCTCTGACGAGCAGATACAGACTTCGTCACCGCCTTTGACGTATCTACTTTCGGCAACATTC
AAGGACTGCTCAATCATTGCCAGGCTGGGGTTGCTGAAACCCGGGAACCATTCTGAAATTCAGGAAGAACAAATA
CGTGTGATTGACTTGGACCCCAAGAGTCTGAACCGGCTGCCGCGCTGGGAAGAGTTGGATAGGGAGATTGTGATG
AGTTATGTACCTGCTGAGAGGAAGATGCCCGCTCTCCAGAAACGCGCCATTTCTCTGTACAATTCCGAAGTCTCT
GGTCTCACGGACGAAGAACTCGAGTTTCGTAATGCCGTCGTCGACTTTGCACAGAAAGAAGTAGCACCGAGGGCA
GCCGAGATAGATAGGACGAATATCTCTCCCATGGACCTCTGGGAGAAGCTCGGTTCTATGGGTCTCCTCGGTATA
ACCGTAGATCAAAAATATAATGGCTTAAATCTTGGATATCTTCACCACACGCTTGCAATGGAAGCTCTATCTGAG
GCCTCGGGATCTGTAGCACTGTCCTACGGAGCCCATTCCAACCTCTGTGTGAACCAGATTCACCGACACGGGACG
GAAGCACAAAAGGAGAAATACCTCAAGGATCTTGTTGACGGAACCAAAGTCGGAAGCTTGGCAATGAGTGAAACT
GGAAGTGGAAGTGACGTGGTCAGTATGCGTTTAAAGGCGGAAAAGGTTCAAGGCGGATGGAAGCTGAATGGTAAC
AAATTTTGGATCACAAATGGGCCCGTCGCCTCCACGCTGGTCGTATATGCCAAAACGGCTCCAGAATTGGGGTCT
AAAGGGATCACAACTTTCGTTATTGAGCGTGGTTTCGAGGGTTTTTCCACCAGCCAGAAGCTTGATAAATTTGGA
ATGAGAGGAAGTGATACCTGTGAACTTGTCTTCGAGGATTGCGTAGTTCCTGAGGAGAATGTCCTCGGCCAGGTC
AACAAGGGTGCTGCCGTTTTGATGTCAGGATTAGATCTTGAACGAGTGGTTCTCAGCGGCGGTCCTTTGGGGTTA
ATGCAGGCGGCGTTTGACTATGCCGTGGAGTATATCCACGATAGGAAGCAGTTTGGTCAACCCGTTGGTACATTC
CAGTTAATGCAAGCCAAAATTGCCGACATGTATACGAAGCTGAATGCTAGTCGGTCGTATGTATATTCAGTAGCC
CGTGCGTGCGATCGAGGTAAAGTTAGTCGCAAAGATTGTGCTGGCGCTATCATGTATTCGACGGAGAAAGCCGTC
GAAGTTGCTCTGGAAGGTATGCAGTGCCTTGGAGGTAATGGCTACATCAACGATTACCCAATGGGTCGTATTCTC
CGGGATTCTCGCTTATATACCGTCGGAGCCGGCACTCAAGAAATTCGGCGAATGCTAATTGGAAGGGAATTCAAC
GAGCACGACTATTGTATTTTATAG
Transcript >AgabiH97|056320
ATGCATAGTCATATGCGTAGCAGTAAAGATTGCAAGTATGCCAACAAGTACTGCCCCCTCGACTTGTTCTCTGGA
AACCCCCATCGTGTTCAACAAGCCATCGACGACTTATGGGACGCCTGGGAGCGAAGTGACGGCGAGGTCAACAAT
CTAAAAATATTTTCACGCGGGAAGGCAGTTAGGCCAGGCCAGATTGTACGCTTGTTGCACGAAGATTTCATAACG
TCCGTATCTCCTGATAGGATACAAGAGGTTTTCAAAAAGGCGTTGTGTGACACCCTTCTGCAATCGCCCATTCTC
AGCATCATCTCGAGGCTCCAGAGGACTTTGGATGTTTTGGATATCGAGGGTCTATCGAAATTATGGCGTGAAGCT
CAACTTGAGTCTCTCTCTGACGAGCAGATACAGACTTCGTCACCGCCTTTGACGTATCTACTTTCGGCAACATTC
AAGGACTGCTCAATCATTGCCAGGCTGGGGTTGCTGAAACCCGGGAACCATTCTGAAATTCAGGAAGAACAAATA
CGTGTGATTGACTTGGACCCCAAGAGTCTGAACCGGCTGCCGCGCTGGGAAGAGTTGGATAGGGAGATTGTGATG
AGTTATGTACCTGCTGAGAGGAAGATGCCCGCTCTCCAGAAACGCGCCATTTCTCTGTACAATTCCGAAGTCTCT
GGTCTCACGGACGAAGAACTCGAGTTTCGTAATGCCGTCGTCGACTTTGCACAGAAAGAAGTAGCACCGAGGGCA
GCCGAGATAGATAGGACGAATATCTCTCCCATGGACCTCTGGGAGAAGCTCGGTTCTATGGGTCTCCTCGGTATA
ACCGTAGATCAAAAATATAATGGCTTAAATCTTGGATATCTTCACCACACGCTTGCAATGGAAGCTCTATCTGAG
GCCTCGGGATCTGTAGCACTGTCCTACGGAGCCCATTCCAACCTCTGTGTGAACCAGATTCACCGACACGGGACG
GAAGCACAAAAGGAGAAATACCTCAAGGATCTTGTTGACGGAACCAAAGTCGGAAGCTTGGCAATGAGTGAAACT
GGAAGTGGAAGTGACGTGGTCAGTATGCGTTTAAAGGCGGAAAAGGTTCAAGGCGGATGGAAGCTGAATGGTAAC
AAATTTTGGATCACAAATGGGCCCGTCGCCTCCACGCTGGTCGTATATGCCAAAACGGCTCCAGAATTGGGGTCT
AAAGGGATCACAACTTTCGTTATTGAGCGTGGTTTCGAGGGTTTTTCCACCAGCCAGAAGCTTGATAAATTTGGA
ATGAGAGGAAGTGATACCTGTGAACTTGTCTTCGAGGATTGCGTAGTTCCTGAGGAGAATGTCCTCGGCCAGGTC
AACAAGGGTGCTGCCGTTTTGATGTCAGGATTAGATCTTGAACGAGTGGTTCTCAGCGGCGGTCCTTTGGGGTTA
ATGCAGGCGGCGTTTGACTATGCCGTGGAGTATATCCACGATAGGAAGCAGTTTGGTCAACCCGTTGGTACATTC
CAGTTAATGCAAGCCAAAATTGCCGACATGTATACGAAGCTGAATGCTAGTCGGTCGTATGTATATTCAGTAGCC
CGTGCGTGCGATCGAGGTAAAGTTAGTCGCAAAGATTGTGCTGGCGCTATCATGTATTCGACGGAGAAAGCCGTC
GAAGTTGCTCTGGAAGGTATGCAGTGCCTTGGAGGTAATGGCTACATCAACGATTACCCAATGGGTCGTATTCTC
CGGGATTCTCGCTTATATACCGTCGGAGCCGGCACTCAAGAAATTCGGCGAATGCTAATTGGAAGGGAATTCAAC
GAGCACGACTATTGTATTTTATAG
Gene >AgabiH97|056320
ATGCATAGTCATATGCGTAGCAGTAAAGATTGCAAGTATGCCAACAAGTACTGCCCCCTCGACTTGTTCTCTGGA
AACCCCCATCGTGTTCAACAAGCCATCGACGACTTATGGGACGCCTGGGAGCGAAGTGACGGCGAGGTCAACAAT
CTAAAAATATTTTCACGCGGGAAGGCAGTTAGGCCAGGCCAGGTACGCTTGTTTCTGCACATGCGATACTGTAGC
TTAAGCTAAAGGCAATCGAGATTGTACGCTTGTTGCACGAAGATTTCATAACGTCCGTATCTCCTGATAGGATAC
AAGAGGTTTTCAAAAAGGCGTTGTGTGACACCCTTCTGCAATCGCCCATTCTCAGCATCATCTCGAGGCTCCAGA
GGACTTTGGATGTTTTGGATATCGAGGGTCTATCGAAATTATGGCGTGAAGCTCAACTTGAGTCTCTCTCTGACG
AGCAGATACAGGTACCTCCGCTCGGCGTTTCGCAATCGGAGCCCGGAATGACGGATTGGGTAGACTTCGTCACCG
CCTTTGAGTCTGTTGAGATGAAGGAACTGGACCATGACCAGCCAAGGACAAGCAATCTTCGATATTACATTTTAG
CGTATCTACTTTCGGCAACATTCAAGGACTGCTCAATCATTGCCAGGCTGGGGTTGCTGAAACCCGGGAACCATT
CTGAAATTCAGGAAGAACAAATACGTGTGATTGACTTGGACCCCAAGAGTCTGAACCGGCTGCCGCGCTGGGAAG
AGTTGGATAGGGAGATTGTGATGAGTTATGTACCTGCTGAGAGGAAGATGTGCGTTGACGAGAACATAGTACCAT
CACGTGTAGCCTCCGGCAATGGTCCGGAGAGTTAAGTAGGACCGTCTTGAGTCGAATTTTGACCTTGCACACACA
TGGCTTCTCTCCGAACCTTGCTTCGTCCTCTGAACCGTCTATCCATCAGGCCCGCTCTCCAGAAACGCGCCATTT
CTCTGTACAATTCCGAAGTCTCTGGTCTCACGGACGAAGAACTCGAGGTTCGTCGTTTCGACGGCAAATTCTGAC
ATCCTCGTTGACGAGAGCTACTTAGTTTCGTAATGCCGTCGTCGACTTTGCACAGAAAGAAGTAGCACCGAGGGC
AGCCGAGATAGATAGGACGAATATCTCTCCCATGGTGTGACCTTCGACATATCAGAGTAATATTGTGCTTACTCG
CGAACTTCCCTAGGACCTCTGGGAGAAGCTCGGTTCTATGGGTCTCCTCGGTATAACCGTAGATCAAAAATATAA
TGGCTTAAATCTTGGATATCTTCACCACACGCTTGCAATGGAAGCTCTATCTGAGGCCTCGGGATCTGTAGCACT
GTCCTACGGAGCCCATTCCAACCTCTGTGTGAACCAGATTCACCGACACGGGACGGAAGCACAAAAGGAGAAATA
CCTCAAGGATCTTGTTGACGGAACCAAAGTCGGAAGCTTGGCAATGAGTGAAACTGGAAGTGGAAGTGACGTGGT
CAGTATGCGTTTAAAGGCGGAAAAGGTTCAAGGCGGATGGAAGCTGAATGGTAACAAATTTTGGTGAGTTGTATA
CTCGATCCATTCTCTCGCACGGGTACCTATGTGCTGATAGGAGGGCTTAAAGGATCACAAATGGGCCCGTCGCCT
CCACGCTGGTCGTATATGCCAAAACGGCTCCAGAATTGGGGTCTAAAGGGATCACAACTTTCGTTATTGAGCGTG
GTTTCGAGGGTTTTTCCACCAGCCAGAAGCTTGATAAATTTGGAATGAGAGGAAGTGATACCTGTGAACTTGTCT
TCGAGGATTGCGTAGTTCCTGAGGGTATGTTTGTTTTTGGTTCCTCGAGTCAAATTTACGATCCAATGCTACTAT
AGAGAATGTCCTCGGCCAGGTCAACAAGGGTGCTGCCGTTTTGATGTCAGGATTAGATCTTGAACGAGTGGTTCT
CAGCGGCGGTCCTTTGGGGTTTGTTGATTACATCGATCTTGCTGGTTGTAACGGCGGTTGATCACTAAGTTAGGT
TAATGCAGGCGGCGTTTGACTATGCCGTGGAGTATATCCACGATAGGAAGCAGTTTGGTCAACCCGTTGGTACAT
TCCAGTTAATGCAAGGCGAGTCATCCTTATTAGATTCATTTTATTCTCTTTTAACGCTCTTGTAGCCAAAATTGC
CGACATGTATACGAAGCTGAATGCTAGTCGGTCGTATGTATATTCAGTAGCCCGTGCGTGCGATCGAGGTAAAGT
TAGTCGCAAAGTAAGTCATGCGTTTCCTACTTCAAGCAATCTCCTGCTTGGTTTGTGTAGCGGCACTGATAATTT
GCGGTTATAGGATTGTGCTGGCGCTATCATGTATTCGACGGAGAAAGCCGTCGAAGTTGCTCTGGAAGGTATGCA
GTGCCTTGGAGGTAATGGCTACATCAACGGTTAGTACATCTATGAGATCTGGCCTAAATCTTGCCTAAGTTGTTG
CATCTGCTCAGATTACCCAATGGGTCGTATTCTCCGGGATTCTCGCTTATATACCGTCGGAGCCGGCACTCAAGA
AATTCGGCGAATGCTAATTGGAAGGGAATTCAACGAGCAGTTTAAGGCATGAAGCGGAATGTTATGTGCTTTTGG
CAAACTATCGAACGAACTGTCAAAAGAGTTTGTTAGCGAGTGAGAACTCGTCTTTCATATACTTTGTGGCTGGCC
TGTCCACACACTAATTTTGCTTTAGCTATTGTATTTTATAG

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