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Database: UniProt
Entry: N4V2J3_COLOR
LinkDB: N4V2J3_COLOR
Original site: N4V2J3_COLOR 
ID   N4V2J3_COLOR            Unreviewed;       498 AA.
AC   N4V2J3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Peptide hydrolase {ECO:0000256|RuleBase:RU361240};
DE            EC=3.4.-.- {ECO:0000256|RuleBase:RU361240};
GN   Name=LAP2 {ECO:0000313|EMBL:TDZ22281.1};
GN   ORFNames=Cob_v004881 {ECO:0000313|EMBL:TDZ22281.1};
OS   Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS   414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS   lagenarium).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum orbiculare species complex.
OX   NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ22281.1, ECO:0000313|Proteomes:UP000014480};
RN   [1] {ECO:0000313|Proteomes:UP000014480}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=23252678; DOI=10.1111/nph.12085;
RA   Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA   Takano Y., Kubo Y., Shirasu K.;
RT   "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT   stage shift of Colletotrichum fungi.";
RL   New Phytol. 197:1236-1249(2013).
RN   [2] {ECO:0000313|Proteomes:UP000014480}
RP   GENOME REANNOTATION.
RC   STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC   {ECO:0000313|Proteomes:UP000014480};
RX   PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA   Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA   Shirasu K.;
RT   "Genome sequence resources for four phytopathogenic fungi from the
RT   Colletotrichum orbiculare species complex.";
RL   Mol. Plant Microbe Interact. 32:1088-1090(2019).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M28 family.
CC       {ECO:0000256|RuleBase:RU361240}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:TDZ22281.1}.
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DR   EMBL; AMCV02000011; TDZ22281.1; -; Genomic_DNA.
DR   AlphaFoldDB; N4V2J3; -.
DR   STRING; 1213857.N4V2J3; -.
DR   EnsemblFungi; ENH81624; ENH81624; Cob_09838.
DR   eggNOG; KOG2195; Eukaryota.
DR   HOGENOM; CLU_024336_1_1_1; -.
DR   OrthoDB; 51543at2759; -.
DR   Proteomes; UP000014480; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd04816; PA_SaNapH_like; 1.
DR   Gene3D; 3.50.30.30; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR045175; M28_fam.
DR   InterPro; IPR046450; PA_dom_sf.
DR   InterPro; IPR003137; PA_domain.
DR   InterPro; IPR007484; Peptidase_M28.
DR   PANTHER; PTHR12147; METALLOPEPTIDASE M28 FAMILY MEMBER; 1.
DR   PANTHER; PTHR12147:SF55; PEPTIDE HYDROLASE; 1.
DR   Pfam; PF02225; PA; 1.
DR   Pfam; PF04389; Peptidase_M28; 1.
DR   SUPFAM; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:TDZ22281.1}; Hydrolase {ECO:0000256|RuleBase:RU361240};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU361240};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014480};
KW   Signal {ECO:0000256|RuleBase:RU361240};
KW   Zinc {ECO:0000256|RuleBase:RU361240}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT   CHAIN           20..498
FT                   /note="Peptide hydrolase"
FT                   /evidence="ECO:0000256|RuleBase:RU361240"
FT                   /id="PRO_5035543820"
FT   DOMAIN          126..220
FT                   /note="PA"
FT                   /evidence="ECO:0000259|Pfam:PF02225"
FT   DOMAIN          247..443
FT                   /note="Peptidase M28"
FT                   /evidence="ECO:0000259|Pfam:PF04389"
SQ   SEQUENCE   498 AA;  52947 MW;  7BB07001D68FA881 CRC64;
     MKFTKTTAVL LSLASGSMAQ NTTCRPKIDS ESLQADLTTE NLMANLEALN EIAFANGGNR
     AFGLPGYAAS VDYVWNRVSN ITGTKAWKQD FSAIFGQVTS ISLSVDGESI YVFGLTYSPS
     TSPEGITADL VLGPAGEAGC DAANYAGLDV TDKIVLVQRF RCPTGGTLAG RVRPAAAAGA
     AAVLVYHDIT TNATAGSLSA PDPEGFVPAG FINLADGEKL KARLDTGEAV QAHFQQTQIV
     EDRVTQNVFV ETEEGDPHNV IMLGAHLDSV QAGPGINDDG SGTSLLLELF HALTKYRTKN
     KVRFAWWGAE ENGLLGSKHY CSNLAPADVD DLLVYLNFDM VSKGYFGVAD TDGSSHGSVA
     PPGSDVVEHI YEAYFESKGH EVTPAILTNG SDYASFWQVL NKPFGFLNTG TAVAQDPCYH
     QACDTIENPD PETITVNARA AAHMLTVLSL NGTSLIPKTS VNATMLNHLQ ARDVGTDVLF
     IEELEALGER HFGCGHDI
//
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