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Database: UniProt
Entry: A0A066XKV4_COLSU
LinkDB: A0A066XKV4_COLSU
Original site: A0A066XKV4_COLSU 
ID   A0A066XKV4_COLSU        Unreviewed;       533 AA.
AC   A0A066XKV4;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   28-MAR-2018, entry version 15.
DE   SubName: Full=Putative aminopeptidase I zinc metalloprotease {ECO:0000313|EMBL:KDN66381.1};
GN   ORFNames=CSUB01_06840 {ECO:0000313|EMBL:KDN66381.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Glomerellales; Glomerellaceae;
OC   Colletotrichum.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN66381.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive
RT   pathogen of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN66381.1}.
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DR   EMBL; JMSE01000938; KDN66381.1; -; Genomic_DNA.
DR   EnsemblFungi; KDN66381; KDN66381; CSUB01_06840.
DR   OMA; FQCIVER; -.
DR   Proteomes; UP000027238; Unassembled WGS sequence.
DR   GO; GO:0000324; C:fungal-type vacuole; IEA:EnsemblFungi.
DR   GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:EnsemblFungi.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 2.30.250.10; -; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; PTHR28570; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KDN66381.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000027238};
KW   Hydrolase {ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|RuleBase:RU004386,
KW   ECO:0000313|EMBL:KDN66381.1};
KW   Protease {ECO:0000256|RuleBase:RU004386, ECO:0000313|EMBL:KDN66381.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW   Zinc {ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   533 AA;  56596 MW;  DB9B2C8C3C1389A7 CRC64;
     MTKHTPESLR TRVSSLSLRL QAMEAAEALS RSQSPAPSSM SASTTLPSAA LNAAPASAPA
     SKHFLLADMD GRSPSENPVC ESCWNSLRYS EVKQTTRAAH PSACRLCAVA AGKPEAYTKP
     FVDFLAENPT IFHTVDHFKD KLAAAGFTEL PARDSWADKL QPGGKYWTTR NGSALIAFTV
     GKAYKPGNGV AMIAGHIDAL TARLKPVSSK PTRAGYLQLG VAPYAGALNQ TWWDRDLSIG
     GRVVVRDESS HKTTTRLVRL DWPIARIPTL APHFGVGMMG QNNPETQAVP IIGLDSSSSD
     DSSSAAAAAP VEPLGPKGAF VNSQPPKLVK LISSQLGLAS PSQILNWELE LYDAQPAQTG
     GLDREFIFGG RIDDKLCSWA ALTALLAAES DPDDGVIKLV ALFDDEEIGS LLRQGARGNF
     LPLTIERAVE SLSTAAAANV PFGTDVLCRT FAASFLLSAD VTHAGNPNFL GYYLDEHVPR
     LNVGVTICGD SNGHMTTDAV STAILQRVGE LSGAPTQTFQ IRNDTRSGGX XXX
//
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