Protein ID | Hirsu2|5923 |
Gene name | |
Location | Contig_3:42689..44277 |
Strand | - |
Gene length (bp) | 1588 |
Transcript length (bp) | 1266 |
Coding sequence length (bp) | 1266 |
Protein length (aa) | 422 |
PFAM Domain ID | Short name | Long name | E-value | Start | End |
---|---|---|---|---|---|
PF00246 | Peptidase_M14 | Zinc carboxypeptidase | 1.1E-84 | 128 | 411 |
PF02244 | Propep_M14 | Carboxypeptidase activation peptide | 1.4E-09 | 40 | 102 |
Swissprot ID | Swissprot Description | Start | End | E-value |
---|---|---|---|---|
sp|C5FH26|MCPAL_ARTOC | Metallocarboxypeptidase A-like protein MCYG_01475 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) GN=MCYG_01475 PE=3 SV=1 | 2 | 421 | 9.0E-162 |
sp|D4B5N0|MCPAL_ARTBC | Metallocarboxypeptidase A-like protein ARB_03789 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) GN=ARB_03789 PE=3 SV=1 | 23 | 421 | 1.0E-156 |
sp|D4D675|MCPAL_TRIVH | Metallocarboxypeptidase A-like protein TRV_02598 OS=Trichophyton verrucosum (strain HKI 0517) GN=TRV_02598 PE=3 SV=1 | 23 | 421 | 1.0E-154 |
sp|C5FVN6|MCPA_ARTOC | Metallocarboxypeptidase A OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) GN=MCPA PE=3 SV=1 | 2 | 418 | 1.0E-149 |
sp|B6V865|MCPA_TRITO | Metallocarboxypeptidase A OS=Trichophyton tonsurans GN=MCPA PE=3 SV=1 | 2 | 418 | 5.0E-149 |
Swissprot ID | Swissprot Description | Start | End | E-value |
---|---|---|---|---|
sp|C5FH26|MCPAL_ARTOC | Metallocarboxypeptidase A-like protein MCYG_01475 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) GN=MCYG_01475 PE=3 SV=1 | 2 | 421 | 9.0E-162 |
sp|D4B5N0|MCPAL_ARTBC | Metallocarboxypeptidase A-like protein ARB_03789 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) GN=ARB_03789 PE=3 SV=1 | 23 | 421 | 1.0E-156 |
sp|D4D675|MCPAL_TRIVH | Metallocarboxypeptidase A-like protein TRV_02598 OS=Trichophyton verrucosum (strain HKI 0517) GN=TRV_02598 PE=3 SV=1 | 23 | 421 | 1.0E-154 |
sp|C5FVN6|MCPA_ARTOC | Metallocarboxypeptidase A OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) GN=MCPA PE=3 SV=1 | 2 | 418 | 1.0E-149 |
sp|B6V865|MCPA_TRITO | Metallocarboxypeptidase A OS=Trichophyton tonsurans GN=MCPA PE=3 SV=1 | 2 | 418 | 5.0E-149 |
sp|B8XGR3|MCPA_TRIEQ | Metallocarboxypeptidase A OS=Trichophyton equinum GN=MCPA PE=3 SV=1 | 2 | 418 | 7.0E-149 |
sp|A6XGK3|MCPA_TRIRU | Metallocarboxypeptidase A OS=Trichophyton rubrum GN=MCPA PE=1 SV=1 | 2 | 418 | 1.0E-147 |
sp|D4DL57|MCPA_TRIVH | Probable metallocarboxypeptidase A OS=Trichophyton verrucosum (strain HKI 0517) GN=MCPA PE=3 SV=1 | 2 | 418 | 4.0E-147 |
sp|D4AS12|MCPA_ARTBC | Probable metallocarboxypeptidase A OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) GN=MCPA PE=1 SV=2 | 2 | 418 | 4.0E-147 |
sp|P48052|CBPA2_HUMAN | Carboxypeptidase A2 OS=Homo sapiens GN=CPA2 PE=1 SV=3 | 27 | 421 | 2.0E-86 |
sp|Q504N0|CBPA2_MOUSE | Carboxypeptidase A2 OS=Mus musculus GN=Cpa2 PE=1 SV=1 | 25 | 421 | 2.0E-82 |
sp|P19222|CBPA2_RAT | Carboxypeptidase A2 OS=Rattus norvegicus GN=Cpa2 PE=1 SV=1 | 25 | 421 | 4.0E-82 |
sp|Q9UI42|CBPA4_HUMAN | Carboxypeptidase A4 OS=Homo sapiens GN=CPA4 PE=1 SV=2 | 25 | 421 | 1.0E-80 |
sp|P09954|CBPA1_PIG | Carboxypeptidase A1 OS=Sus scrofa GN=CPA1 PE=1 SV=2 | 2 | 419 | 3.0E-79 |
sp|P00730|CBPA1_BOVIN | Carboxypeptidase A1 OS=Bos taurus GN=CPA1 PE=1 SV=3 | 2 | 419 | 4.0E-78 |
sp|Q6P8K8|CBPA4_MOUSE | Carboxypeptidase A4 OS=Mus musculus GN=Cpa4 PE=2 SV=2 | 2 | 421 | 8.0E-78 |
sp|P15085|CBPA1_HUMAN | Carboxypeptidase A1 OS=Homo sapiens GN=CPA1 PE=1 SV=2 | 28 | 419 | 8.0E-78 |
sp|P00731|CBPA1_RAT | Carboxypeptidase A1 OS=Rattus norvegicus GN=Cpa1 PE=2 SV=2 | 27 | 419 | 1.0E-74 |
sp|P00732|CBPB1_BOVIN | Carboxypeptidase B OS=Bos taurus GN=CPB1 PE=1 SV=2 | 28 | 416 | 1.0E-72 |
sp|Q8R4H4|CBPA5_MOUSE | Carboxypeptidase A5 OS=Mus musculus GN=Cpa5 PE=2 SV=1 | 25 | 419 | 6.0E-72 |
sp|Q7TPZ8|CBPA1_MOUSE | Carboxypeptidase A1 OS=Mus musculus GN=Cpa1 PE=1 SV=1 | 27 | 419 | 4.0E-70 |
sp|P15089|CBPA3_MOUSE | Mast cell carboxypeptidase A OS=Mus musculus GN=Cpa3 PE=2 SV=1 | 11 | 419 | 4.0E-70 |
sp|O02350|CBPA1_ANOGA | Zinc carboxypeptidase A 1 OS=Anopheles gambiae GN=AGAP009593 PE=2 SV=3 | 12 | 418 | 1.0E-69 |
sp|P15086|CBPB1_HUMAN | Carboxypeptidase B OS=Homo sapiens GN=CPB1 PE=1 SV=4 | 28 | 416 | 5.0E-69 |
sp|P15088|CBPA3_HUMAN | Mast cell carboxypeptidase A OS=Homo sapiens GN=CPA3 PE=1 SV=2 | 6 | 416 | 1.0E-68 |
sp|P21961|CBPA3_RAT | Mast cell carboxypeptidase A (Fragment) OS=Rattus norvegicus GN=Cpa3 PE=1 SV=2 | 11 | 416 | 2.0E-68 |
sp|Q8WXQ8|CBPA5_HUMAN | Carboxypeptidase A5 OS=Homo sapiens GN=CPA5 PE=2 SV=1 | 3 | 419 | 8.0E-68 |
sp|P04069|CBPB_ASTAS | Carboxypeptidase B OS=Astacus astacus PE=1 SV=1 | 118 | 421 | 3.0E-67 |
sp|P09955|CBPB1_PIG | Carboxypeptidase B OS=Sus scrofa GN=CPB1 PE=1 SV=5 | 28 | 416 | 3.0E-66 |
sp|Q5U901|CBPA6_MOUSE | Carboxypeptidase A6 OS=Mus musculus GN=Cpa6 PE=2 SV=1 | 28 | 420 | 3.0E-65 |
sp|P55261|CBPB1_CANLF | Carboxypeptidase B OS=Canis lupus familiaris GN=CPB1 PE=2 SV=1 | 28 | 416 | 1.0E-64 |
sp|P38836|ECM14_YEAST | Putative metallocarboxypeptidase ECM14 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=ECM14 PE=1 SV=1 | 11 | 416 | 1.0E-64 |
sp|P42788|CBPZ_SIMVI | Zinc carboxypeptidase (Fragment) OS=Simulium vittatum PE=2 SV=1 | 121 | 421 | 2.0E-64 |
sp|Q4R7R2|CBPA5_MACFA | Carboxypeptidase A5 OS=Macaca fascicularis GN=CPA5 PE=2 SV=1 | 3 | 419 | 4.0E-64 |
sp|P19223|CBPB1_RAT | Carboxypeptidase B OS=Rattus norvegicus GN=Cpb1 PE=1 SV=1 | 28 | 416 | 1.0E-63 |
sp|B6Q972|ECM14_TALMQ | Putative metallocarboxypeptidase ecm14 OS=Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) GN=ecm14 PE=3 SV=1 | 115 | 416 | 5.0E-61 |
sp|Q8N4T0|CBPA6_HUMAN | Carboxypeptidase A6 OS=Homo sapiens GN=CPA6 PE=1 SV=2 | 28 | 420 | 2.0E-60 |
sp|B8M2K0|ECM14_TALSN | Putative metallocarboxypeptidase ecm14 OS=Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006) GN=ecm14 PE=3 SV=1 | 115 | 416 | 3.0E-60 |
sp|E4UPZ6|ECM14_ARTGP | Putative metallocarboxypeptidase ECM14 OS=Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) GN=ECM14 PE=3 SV=1 | 114 | 413 | 2.0E-59 |
sp|D4DIW7|ECM14_TRIVH | Putative metallocarboxypeptidase ECM14 OS=Trichophyton verrucosum (strain HKI 0517) GN=ECM14 PE=3 SV=1 | 113 | 413 | 8.0E-59 |
sp|D4AKU7|ECM14_ARTBC | Putative metallocarboxypeptidase ECM14 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) GN=ECM14 PE=3 SV=1 | 114 | 413 | 4.0E-58 |
sp|C5G6U8|ECM14_AJEDR | Putative metallocarboxypeptidase ECM14 OS=Ajellomyces dermatitidis (strain ER-3 / ATCC MYA-2586) GN=ECM14 PE=3 SV=1 | 21 | 416 | 5.0E-58 |
sp|Q5B011|ECM14_EMENI | Putative metallocarboxypeptidase ecm14 OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) GN=ecm14 PE=3 SV=2 | 113 | 418 | 2.0E-57 |
sp|C5JZS0|ECM14_AJEDS | Putative metallocarboxypeptidase ECM14 OS=Ajellomyces dermatitidis (strain SLH14081) GN=ECM14 PE=3 SV=1 | 21 | 416 | 2.0E-57 |
sp|C5FPR9|ECM14_ARTOC | Putative metallocarboxypeptidase ECM14 OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) GN=ECM14 PE=3 SV=1 | 114 | 413 | 2.0E-57 |
sp|A6RCF5|ECM14_AJECN | Putative metallocarboxypeptidase ECM14 OS=Ajellomyces capsulatus (strain NAm1 / WU24) GN=ECM14 PE=3 SV=1 | 113 | 416 | 4.0E-57 |
sp|C6H4F1|ECM14_AJECH | Putative metallocarboxypeptidase ECM14 OS=Ajellomyces capsulatus (strain H143) GN=ECM14 PE=3 SV=1 | 113 | 416 | 1.0E-56 |
sp|Q9VL86|CBPA1_DROME | Zinc carboxypeptidase A 1 OS=Drosophila melanogaster GN=CG17633 PE=2 SV=1 | 7 | 421 | 1.0E-56 |
sp|C0NM08|ECM14_AJECG | Putative metallocarboxypeptidase ECM14 OS=Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) GN=ECM14 PE=3 SV=1 | 113 | 416 | 2.0E-56 |
sp|B6H233|ECM14_PENRW | Putative metallocarboxypeptidase ecm14 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) GN=ecm14 PE=3 SV=1 | 112 | 413 | 5.0E-56 |
sp|Q9JHH6|CBPB2_MOUSE | Carboxypeptidase B2 OS=Mus musculus GN=Cpb2 PE=1 SV=1 | 27 | 413 | 5.0E-56 |
sp|C1HE31|ECM14_PARBA | Putative metallocarboxypeptidase ECM14 OS=Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) GN=ECM14 PE=3 SV=1 | 115 | 416 | 6.0E-56 |
sp|C4JEE1|ECM14_UNCRE | Putative metallocarboxypeptidase ECM14 OS=Uncinocarpus reesii (strain UAMH 1704) GN=ECM14 PE=3 SV=1 | 109 | 417 | 9.0E-56 |
sp|A1CSU3|ECM14_ASPCL | Putative metallocarboxypeptidase ecm14 OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) GN=ecm14 PE=3 SV=1 | 99 | 417 | 1.0E-55 |
sp|C1GDH9|ECM14_PARBD | Putative metallocarboxypeptidase ECM14 OS=Paracoccidioides brasiliensis (strain Pb18) GN=ECM14 PE=3 SV=1 | 115 | 416 | 2.0E-55 |
sp|C0SAI5|ECM14_PARBP | Putative metallocarboxypeptidase ECM14 OS=Paracoccidioides brasiliensis (strain Pb03) GN=ECM14 PE=3 SV=1 | 115 | 416 | 2.0E-55 |
sp|Q29NC4|CBPA1_DROPS | Zinc carboxypeptidase A 1 OS=Drosophila pseudoobscura pseudoobscura GN=GA14587 PE=3 SV=1 | 25 | 413 | 3.0E-55 |
sp|Q96IY4|CBPB2_HUMAN | Carboxypeptidase B2 OS=Homo sapiens GN=CPB2 PE=1 SV=2 | 8 | 413 | 4.0E-55 |
sp|E5A0U8|ECM14_LEPMJ | Putative metallocarboxypeptidase ECM14 OS=Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8) GN=ECM14 PE=3 SV=1 | 117 | 420 | 5.0E-55 |
sp|E9DD69|ECM14_COCPS | Putative metallocarboxypeptidase ECM14 OS=Coccidioides posadasii (strain RMSCC 757 / Silveira) GN=ECM14 PE=3 SV=1 | 13 | 413 | 6.0E-55 |
sp|C5PHW9|ECM14_COCP7 | Putative metallocarboxypeptidase ECM14 OS=Coccidioides posadasii (strain C735) GN=ECM14 PE=3 SV=1 | 13 | 413 | 2.0E-54 |
sp|Q9EQV9|CBPB2_RAT | Carboxypeptidase B2 OS=Rattus norvegicus GN=Cpb2 PE=2 SV=1 | 12 | 413 | 5.0E-54 |
sp|Q4X1U0|ECM14_ASPFU | Putative metallocarboxypeptidase ecm14 OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) GN=ecm14 PE=3 SV=1 | 115 | 420 | 7.0E-54 |
sp|B0XRS8|ECM14_ASPFC | Putative metallocarboxypeptidase ecm14 OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) GN=ecm14 PE=3 SV=1 | 115 | 420 | 7.0E-54 |
sp|A2QZA2|ECM14_ASPNC | Putative metallocarboxypeptidase ecm14 OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) GN=ecm14 PE=3 SV=1 | 115 | 416 | 1.0E-53 |
sp|A1DGH9|ECM14_NEOFI | Putative metallocarboxypeptidase ecm14 OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) GN=ecm14 PE=3 SV=1 | 115 | 420 | 1.0E-53 |
sp|O74818|YBJ7_SCHPO | Uncharacterized carboxypeptidase C337.07c OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) GN=SPBC337.07c PE=3 SV=1 | 112 | 415 | 6.0E-53 |
sp|Q0C9B4|ECM14_ASPTN | Putative metallocarboxypeptidase ecm14 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) GN=ecm14 PE=3 SV=1 | 115 | 410 | 1.0E-52 |
sp|B8NBP9|ECM14_ASPFN | Putative metallocarboxypeptidase ecm14 OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) GN=ecm14 PE=3 SV=1 | 21 | 410 | 3.0E-51 |
sp|Q2TZK2|ECM14_ASPOR | Putative metallocarboxypeptidase ecm14 OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) GN=ecm14 PE=3 SV=1 | 21 | 410 | 3.0E-51 |
sp|A7EUC0|ECM14_SCLS1 | Putative metallocarboxypeptidase ecm14 OS=Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) GN=ecm14 PE=3 SV=1 | 103 | 416 | 4.0E-51 |
sp|Q0II73|CBPO_BOVIN | Carboxypeptidase O OS=Bos taurus GN=CPO PE=2 SV=1 | 92 | 420 | 9.0E-51 |
sp|Q2KIG3|CBPB2_BOVIN | Carboxypeptidase B2 OS=Bos taurus GN=CPB2 PE=1 SV=1 | 41 | 413 | 1.0E-50 |
sp|Q8IVL8|CBPO_HUMAN | Carboxypeptidase O OS=Homo sapiens GN=CPO PE=2 SV=1 | 118 | 420 | 4.0E-47 |
sp|P29068|CBPT_THEVU | Carboxypeptidase T OS=Thermoactinomyces vulgaris GN=cpt PE=1 SV=1 | 105 | 402 | 7.0E-28 |
sp|P18143|CBPS_STRGR | Zinc carboxypeptidase OS=Streptomyces griseus GN=scpD PE=1 SV=2 | 121 | 402 | 2.0E-25 |
sp|P39041|CBPS_STRMP | Zinc carboxypeptidase OS=Saccharothrix mutabilis subsp. capreolus PE=3 SV=1 | 118 | 378 | 1.0E-24 |
sp|O75976|CBPD_HUMAN | Carboxypeptidase D OS=Homo sapiens GN=CPD PE=1 SV=2 | 170 | 306 | 4.0E-09 |
sp|O89001|CBPD_MOUSE | Carboxypeptidase D OS=Mus musculus GN=Cpd PE=1 SV=2 | 170 | 306 | 8.0E-09 |
sp|Q9JHW1|CBPD_RAT | Carboxypeptidase D OS=Rattus norvegicus GN=Cpd PE=1 SV=2 | 170 | 306 | 8.0E-09 |
sp|Q9JHW1|CBPD_RAT | Carboxypeptidase D OS=Rattus norvegicus GN=Cpd PE=1 SV=2 | 93 | 349 | 4.0E-07 |
sp|Q03415|ENP1_LYSSH | Gamma-D-glutamyl-L-diamino acid endopeptidase 1 OS=Lysinibacillus sphaericus PE=1 SV=1 | 166 | 290 | 6.0E-07 |
sp|O89001|CBPD_MOUSE | Carboxypeptidase D OS=Mus musculus GN=Cpd PE=1 SV=2 | 93 | 349 | 8.0E-07 |
sp|P42787|CBPD_DROME | Carboxypeptidase D OS=Drosophila melanogaster GN=svr PE=1 SV=2 | 134 | 263 | 8.0E-07 |
sp|Q8R4V4|CBPZ_MOUSE | Carboxypeptidase Z OS=Mus musculus GN=Cpz PE=2 SV=2 | 120 | 259 | 1.0E-06 |
sp|Q4R4M3|CBPE_MACFA | Carboxypeptidase E OS=Macaca fascicularis GN=CPE PE=2 SV=1 | 121 | 259 | 1.0E-06 |
sp|O54858|CBPZ_RAT | Carboxypeptidase Z OS=Rattus norvegicus GN=Cpz PE=2 SV=1 | 120 | 259 | 1.0E-06 |
sp|P42787|CBPD_DROME | Carboxypeptidase D OS=Drosophila melanogaster GN=svr PE=1 SV=2 | 121 | 262 | 2.0E-06 |
sp|Q90240|CBPD_ANAPL | Carboxypeptidase D OS=Anas platyrhynchos GN=CPD PE=1 SV=1 | 121 | 259 | 2.0E-06 |
sp|P83852|CBPD_LOPSP | Carboxypeptidase D (Fragment) OS=Lophonetta specularioides GN=CPD PE=1 SV=1 | 121 | 259 | 3.0E-06 |
sp|Q9JHW1|CBPD_RAT | Carboxypeptidase D OS=Rattus norvegicus GN=Cpd PE=1 SV=2 | 121 | 259 | 4.0E-06 |
sp|O75976|CBPD_HUMAN | Carboxypeptidase D OS=Homo sapiens GN=CPD PE=1 SV=2 | 121 | 259 | 4.0E-06 |
sp|O89001|CBPD_MOUSE | Carboxypeptidase D OS=Mus musculus GN=Cpd PE=1 SV=2 | 121 | 259 | 5.0E-06 |
sp|Q9EQV8|CBPN_RAT | Carboxypeptidase N catalytic chain OS=Rattus norvegicus GN=Cpn1 PE=2 SV=1 | 121 | 306 | 9.0E-06 |
GO Term | Description | Terminal node |
---|---|---|
GO:0006508 | proteolysis | Yes |
GO:0004181 | metallocarboxypeptidase activity | Yes |
GO:0008270 | zinc ion binding | Yes |
GO:0044238 | primary metabolic process | No |
GO:0016787 | hydrolase activity | No |
GO:0008150 | biological_process | No |
GO:0019538 | protein metabolic process | No |
GO:0005488 | binding | No |
GO:0003824 | catalytic activity | No |
GO:0071704 | organic substance metabolic process | No |
GO:0008238 | exopeptidase activity | No |
GO:0008152 | metabolic process | No |
GO:0008235 | metalloexopeptidase activity | No |
GO:0006807 | nitrogen compound metabolic process | No |
GO:0043169 | cation binding | No |
GO:0008237 | metallopeptidase activity | No |
GO:0043167 | ion binding | No |
GO:0046872 | metal ion binding | No |
GO:0008233 | peptidase activity | No |
GO:1901564 | organonitrogen compound metabolic process | No |
GO:0140096 | catalytic activity, acting on a protein | No |
GO:0003674 | molecular_function | No |
GO:0046914 | transition metal ion binding | No |
GO:0043170 | macromolecule metabolic process | No |
GO:0004180 | carboxypeptidase activity | No |
Localizations | Signals | Cytoplasm | Nucleus | Extracellular | Cell membrane | Mitochondrion | Plastid | Endoplasmic reticulum | Lysosome vacuole | Golgi apparatus | Peroxisome |
---|---|---|---|---|---|---|---|---|---|---|---|
Extracellular | Signal peptide | 0.084 | 0.0185 | 0.94 | 0.0893 | 0.0827 | 0.07 | 0.2652 | 0.4861 | 0.1793 | 0.0085 |
SignalP signal predicted | Location | Score |
---|---|---|
Yes | 1 - 17 | 0.999686 |
Orthofinder run ID | 4 |
Orthogroup | 3260 |
Change Orthofinder run |
Type of sequence | Sequence |
---|---|
Locus | Download genbank file of locus
Download genbank file of locus (reverse complement)
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|5923 MMKSLLVLPSLLAAVSAAVTPTPTQVSFDGYKVFRVPVRTQVQRVNEVVEKLDLSFWQPASRKGAFADIQVPPNK VDDFRHAMEGLELITMHEDLGKSIAEEAVFEAYVEGSANDTWFKSYHAYDDHLQWLQDLQGQHPKNSEIVTSGQS GEGNAITGIHFYGNEGKGTKPAVVFHGTVHAREWISSKVVEYLAYSLLSGYQNDDEIKSLVDKYDFYLFPVVNPD GFKFTQSGNRMWRKNRQRDSGSRCFGRDINRNWPYKWDGPGSSTNPCAEDYRGEEAGDTPEAKALTAFLNQVKEA QSVKLYIDWHSYSQLFMTPYGYTCDSVPQNNDELQSLASGAVDAIRSVHGTTFNSGPICSTIYQTAGNSVDYVAD IIKSDYNFAVELRDTGRYGFVLPPNQIAPTGEEAFAGVKYLLQNMK* |
Coding | >Hirsu2|5923 ATGATGAAGTCGCTTCTCGTCCTGCCGTCGCTCCTGGCTGCCGTCTCGGCAGCCGTGACCCCGACGCCCACCCAG GTGTCCTTCGACGGATACAAAGTCTTTCGAGTGCCTGTGCGAACGCAGGTCCAGCGGGTCAATGAAGTCGTGGAG AAGCTCGACCTCAGCTTCTGGCAGCCGGCCTCGCGCAAGGGCGCCTTCGCCGACATTCAGGTGCCGCCCAACAAG GTCGACGACTTTCGCCATGCGATGGAAGGCCTCGAGTTGATCACGATGCACGAGGATCTGGGCAAGTCGATCGCC GAGGAGGCCGTCTTTGAAGCCTATGTCGAGGGGTCGGCCAACGACACGTGGTTCAAGTCGTATCACGCTTATGAT GACCATCTTCAGTGGCTTCAAGACCTGCAGGGTCAGCACCCCAAAAACTCGGAGATTGTGACCTCGGGCCAGTCG GGCGAGGGCAACGCCATCACGGGCATCCACTTCTACGGAAACGAGGGCAAAGGCACCAAGCCCGCCGTCGTCTTC CACGGCACGGTTCATGCTCGCGAGTGGATTTCTTCCAAGGTTGTCGAGTACTTGGCCTACTCCCTCCTAAGCGGC TATCAGAACGACGACGAGATCAAGTCATTGGTCGACAAGTACGACTTCTACCTCTTCCCTGTCGTCAATCCCGAC GGATTCAAGTTCACTCAGTCAGGCAACCGCATGTGGCGCAAGAACCGACAGAGGGACTCCGGAAGCAGATGCTTT GGGCGCGACATCAACCGCAACTGGCCATATAAATGGGACGGGCCTGGCTCCTCGACCAACCCCTGCGCGGAAGAC TACCGGGGCGAAGAGGCCGGCGACACGCCAGAGGCCAAGGCCCTGACCGCATTCCTCAACCAGGTCAAGGAAGCC CAGAGTGTGAAGCTTTACATCGACTGGCACTCGTACTCCCAACTCTTCATGACTCCCTACGGTTATACGTGCGAC AGCGTGCCGCAGAACAACGACGAGCTGCAATCTCTAGCTAGCGGCGCCGTCGACGCAATCCGCTCTGTCCACGGC ACCACCTTCAACTCCGGCCCCATCTGCTCCACCATCTACCAGACGGCCGGCAATAGCGTCGACTACGTGGCCGAC ATCATCAAGTCCGACTACAACTTTGCCGTGGAGCTGCGCGACACGGGCCGCTACGGCTTCGTCCTGCCCCCGAAC CAGATCGCCCCTACCGGCGAGGAAGCCTTCGCCGGCGTCAAGTATCTGCTGCAGAACATGAAGTAA |
Transcript | >Hirsu2|5923 ATGATGAAGTCGCTTCTCGTCCTGCCGTCGCTCCTGGCTGCCGTCTCGGCAGCCGTGACCCCGACGCCCACCCAG GTGTCCTTCGACGGATACAAAGTCTTTCGAGTGCCTGTGCGAACGCAGGTCCAGCGGGTCAATGAAGTCGTGGAG AAGCTCGACCTCAGCTTCTGGCAGCCGGCCTCGCGCAAGGGCGCCTTCGCCGACATTCAGGTGCCGCCCAACAAG GTCGACGACTTTCGCCATGCGATGGAAGGCCTCGAGTTGATCACGATGCACGAGGATCTGGGCAAGTCGATCGCC GAGGAGGCCGTCTTTGAAGCCTATGTCGAGGGGTCGGCCAACGACACGTGGTTCAAGTCGTATCACGCTTATGAT GACCATCTTCAGTGGCTTCAAGACCTGCAGGGTCAGCACCCCAAAAACTCGGAGATTGTGACCTCGGGCCAGTCG GGCGAGGGCAACGCCATCACGGGCATCCACTTCTACGGAAACGAGGGCAAAGGCACCAAGCCCGCCGTCGTCTTC CACGGCACGGTTCATGCTCGCGAGTGGATTTCTTCCAAGGTTGTCGAGTACTTGGCCTACTCCCTCCTAAGCGGC TATCAGAACGACGACGAGATCAAGTCATTGGTCGACAAGTACGACTTCTACCTCTTCCCTGTCGTCAATCCCGAC GGATTCAAGTTCACTCAGTCAGGCAACCGCATGTGGCGCAAGAACCGACAGAGGGACTCCGGAAGCAGATGCTTT GGGCGCGACATCAACCGCAACTGGCCATATAAATGGGACGGGCCTGGCTCCTCGACCAACCCCTGCGCGGAAGAC TACCGGGGCGAAGAGGCCGGCGACACGCCAGAGGCCAAGGCCCTGACCGCATTCCTCAACCAGGTCAAGGAAGCC CAGAGTGTGAAGCTTTACATCGACTGGCACTCGTACTCCCAACTCTTCATGACTCCCTACGGTTATACGTGCGAC AGCGTGCCGCAGAACAACGACGAGCTGCAATCTCTAGCTAGCGGCGCCGTCGACGCAATCCGCTCTGTCCACGGC ACCACCTTCAACTCCGGCCCCATCTGCTCCACCATCTACCAGACGGCCGGCAATAGCGTCGACTACGTGGCCGAC ATCATCAAGTCCGACTACAACTTTGCCGTGGAGCTGCGCGACACGGGCCGCTACGGCTTCGTCCTGCCCCCGAAC CAGATCGCCCCTACCGGCGAGGAAGCCTTCGCCGGCGTCAAGTATCTGCTGCAGAACATGAAGTAA |
Gene | >Hirsu2|5923 ATGATGAAGTCGCTTCTCGTCCTGCCGTCGCTCCTGGCTGCCGTCTCGGCAGCCGTGACCCCGACGCCCACCCAG GTGTCCTTCGACGGATACAAAGTCTTTCGAGTGCCTGTGCGAACGCAGGTCCAGCGGGTCAATGAAGTCGTGGAG AAGCTCGACCTCAGCTTCTGGCAGCCGGCCTCGCGCAAGGGCGCCTTCGCCGACATTCAGGTGCCGCCCAACAAG GTCGACGACTTTCGCCATGCGATGGAAGGCCTCGAGTTGATCACGATGCACGAGGATCTGGGCAAGTCGATCGCC GAGGAGGCCGTCTTTGAAGCCTATGTCGGTTAGTGCTTCCGTCCACCCTTCCGCTGCGTCGGCCCGTCCGAACTG GCTGATCGTCAGACCAACTAACCTGGCTTGAACAGAGGGGTCGGCCAACGACACGTGGTTCAAGTCGTATCACGC TTATGATGACCATCTTCAGTGGCTTCAAGACCTGCAGGGTCAGCACCCCAAAAACTCGGAGATTGTGACCTCGGG CCAGTCGGGCGAGGGCAACGCCATCACGGGCATCCACTTCTACGGAAACGAGGGCAAAGGCACCAAGCCCGCCGT CGTCTTCCACGGCACGGTTCATGCTCGCGAGTGGATTTCTTCCAAGGTCCGTGTGACGCAGGCCCATCCCGTAGA TGACACCAGCTAACAGCCGGCACGTAGGTTGTCGAGTACTTGGCCTACTCCCTCCTAAGCGGCTATCAGAACGAC GACGAGATCAAGTCATTGGTCGACAAGTACGACTTCTACCTCTTCCCTGTCGTCAATCCCGACGGTAAGTAAAGG AAGTCTCATAGGAAGCATAGATTTCTCTCCGTCTCTGCTCTATCAGAGATTATGTCAATTGCTAACCGCCTGCCA ACAATCTCTCTCCATACGCTGTCCTCAGGATTCAAGTTCACTCAGTCAGGCAACCGCATGTGGCGCAAGAACCGA CAGAGGGACTCCGGAAGCAGATGCTTTGGGCGCGACATCAACCGCAACTGGCCATATAAATGGGACGGGCCTGGC TCCTCGACCAACCCCTGCGCGGAAGACTACCGGGGCGAAGAGGCCGGCGACACGCCAGAGGCCAAGGCCCTGACC GCATTCCTCAACCAGGTCAAGGAAGCCCAGAGTGTGAAGCTTTACATCGACTGGCACTCGTACTCCCAACTCTTC ATGACTCGTAAGTCCGCCCGCCTCGTCAGGTGAACTGTTCCCAAGTCGAGAGCTCGGTGGCTCACGAGCAACAAC AGCCTACGGTTATACGTGCGACAGCGTGCCGCAGAACAACGACGAGCTGCAATCTCTAGCTAGCGGCGCCGTCGA CGCAATCCGCTCTGTCCACGGCACCACCTTCAACTCCGGCCCCATCTGCTCCACCATCTACCAGACGGCCGGCAA TAGCGTCGACTACGTGGCCGACATCATCAAGTCCGACTACAACTTTGCCGTGGAGCTGCGCGACACGGGCCGCTA CGGCTTCGTCCTGCCCCCGAACCAGATCGCCCCTACCGGCGAGGAAGCCTTCGCCGGCGTCAAGTATCTGCTGCA GAACATGAAGTAA |