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Database: UniProt
Entry: T0LI85_COLGC
LinkDB: T0LI85_COLGC
Original site: T0LI85_COLGC 
ID   T0LI85_COLGC            Unreviewed;       566 AA.
AC   T0LI85;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   22-NOV-2017, entry version 13.
DE   SubName: Full=Aminopeptidase I zinc metalloprotease {ECO:0000313|EMBL:EQB47865.1};
GN   ORFNames=CGLO_12967 {ECO:0000313|EMBL:EQB47865.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB47865.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in
RT   Colletotrichum gloeosporioides as revealed by transcriptome
RT   analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|RuleBase:RU004386}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EQB47865.1}.
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DR   EMBL; AMYD01002802; EQB47865.1; -; Genomic_DNA.
DR   MEROPS; M18.001; -.
DR   EnsemblFungi; EQB47865; EQB47865; CGLO_12967.
DR   OrthoDB; EOG092C3JCE; -.
DR   Proteomes; UP000015530; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; SSF101821; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EQB47865.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000015530};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:EQB47865.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:EQB47865.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   566 AA;  60175 MW;  372095E3616D4BF5 CRC64;
     MTKHTPDSLR TRVSSLSLRL QAMEGAEALS RSQSPAPSMA ASTTIPVTAS KPFLLADMEG
     RPAASNPVCE SCWNALRYSE VKQTSRAASP AACKLCAVAA GKPEAYTQPF VDFLTENPTI
     FHAVSYFKTK LAAAGFTELP ARDSWKLQPG GKYWTTKNGS GLIAFTVGEA YKPGNGVAMI
     AGHIDALTAK LKPVSTKPTR AGYLQLGVAP YAGALNQTWW DRDLSIGGRV IVRDESNKTT
     TKLVRLDWPI ARIPTLAPHF GVGMMGQNNP ETQAVPIIGL ESSSDAASNT PVEPLGPKGS
     FVNTQPPKLV KLISSELGLA SPTQIVNWEL ELYDSQPAQT GGLDREFIFG GRIDDKLCSW
     AAFTGLLAAE SSPSDGIIKL VALFDDEEIG SLLRQGARSN FLPLTIERAV ESLSAAADVP
     FGSNTIGQTY ASSFLVSADV THAGNPNFLG YYLDDHVPRL NVGIAICGDS NGHMTTDAIS
     TAILQRVGEL ADAPTQTFQI RNDTRSGGTV GPALSSAMGV KAADAGLPQL SMHSIRATTG
     ALDPGLGVKF FKGFLDHWEK IDGEWH
//
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