ID L2GC76_COLFN Unreviewed; 428 AA.
AC L2GC76;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Zinc carboxypeptidase {ECO:0000313|EMBL:ELA36269.1};
GN ORFNames=CGGC5_4172 {ECO:0000313|EMBL:ELA36269.1};
OS Colletotrichum fructicola (strain Nara gc5) (Anthracnose fungus)
OS (Colletotrichum gloeosporioides (strain Nara gc5)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1213859 {ECO:0000313|EMBL:ELA36269.1};
RN [1] {ECO:0000313|EMBL:ELA36269.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Nara gc5 {ECO:0000313|EMBL:ELA36269.1};
RA Gan P.H.P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Genome analysis of Colletotrichum orbiculare and Colletotrichum
RT fructicola.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; KB020526; ELA36269.1; -; Genomic_DNA.
DR RefSeq; XP_007274695.1; XM_007274633.1.
DR AlphaFoldDB; L2GC76; -.
DR STRING; 1213859.L2GC76; -.
DR MEROPS; M14.014; -.
DR EnsemblFungi; ELA36269; ELA36269; CGGC5_4172.
DR HOGENOM; CLU_019326_1_1_1; -.
DR OrthoDB; 3540647at2759; -.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd03860; M14_CP_A-B_like; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:ELA36269.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000313|EMBL:ELA36269.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:ELA36269.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..428
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003959662"
FT DOMAIN 112..403
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
SQ SEQUENCE 428 AA; 48072 MW; 3F9A3F7192FB42D4 CRC64;
MHPLALFALI GGLVSASSPV SYDGYQVLRV TTGANSAAVL EKLSSIEYDE WNTVVNKHID
IAIAPNQIER FQTLALEYHV MHENLAVSIA SESATGTTWK RQIDDLEWYD SYHPYDDHKA
YFEALHNAFP NNSEIVSSGT SFEGRDIFGI HFWGSDGPGK PAVLWHGTVH AREWIVAPVM
EYLTLQLIQG YGVDNTTTAF VDTYDFWVFP FVNPDGFVYT QTTERLWRKN RQPAPTSTNS
TCYGRDINRN WPYKWDANPL GTSTDPCSQT YKGIEAGDTP EMEGLHKLVD TLRDASGLKL
YIDWHSYSQY FLTPVGYNCT YYIDTLGQHI KLAQLASDAI REVEGVTFTY GPSCATLYPT
TGASFDYAYA VGKTQWSYLI ELRDTGDFGF VLPPEQIRGS VKEQWEGMKV MLSVLGEVFF
DGEGPAAF
//
