ID A0A2T4GX50_FUSCU Unreviewed; 426 AA.
AC A0A2T4GX50;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Metallocarboxypeptidase A-like protein M {ECO:0000313|EMBL:PTD08136.1};
GN ORFNames=FCULG_00006153 {ECO:0000313|EMBL:PTD08136.1}, HYE67_001967
GN {ECO:0000313|EMBL:QPC59736.1};
OS Fusarium culmorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=5516 {ECO:0000313|EMBL:PTD08136.1, ECO:0000313|Proteomes:UP000241587};
RN [1] {ECO:0000313|EMBL:PTD08136.1, ECO:0000313|Proteomes:UP000241587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PV {ECO:0000313|EMBL:PTD08136.1,
RC ECO:0000313|Proteomes:UP000241587};
RA Schmidt R.;
RT "Fusarium culmorum secondary metabolites in fungal-bacterial-plant
RT interactions.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QPC59736.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Class2-1B {ECO:0000313|EMBL:QPC59736.1};
RA Yuan Z.;
RT "The chromosome-scale genome resource for two endophytic Fusarium species:
RT F. culmorum and F. pseudograminearum.";
RL Submitted (NOV-2020) 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; PVEM01000006; PTD08136.1; -; Genomic_DNA.
DR EMBL; CP064747; QPC59736.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4GX50; -.
DR OMA; KYNTWSD; -.
DR Proteomes; UP000241587; Unassembled WGS sequence.
DR Proteomes; UP000663297; Chromosome 1.
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; 3.40.630.10; Zn peptidases; 1.
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; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:PTD08136.1};
KW Hydrolase {ECO:0000313|EMBL:PTD08136.1};
KW Protease {ECO:0000313|EMBL:PTD08136.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000241587};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..426
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033324626"
FT DOMAIN 309..319
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 426 AA; 48187 MW; 2F0BD3B95EAFF011 CRC64;
MRFSIIVAAL LPFAFSKVTY NKWKGYSIDI CDLSQDDVTK ALGGINHVPL GEHRDTIEVA
VHPTSVHNFE GLALKSTLVI EDMAEEFAKE GNFEDLTAAR THDRVKLAQP DKSYFKSYHS
FEQHTQFLKD LQSSFSKNSE VFSTGKSVEG RDVQGIHLWG KSGKGKKPAI IWHGNVHARE
WISSMTVEYL AWKLVQGYHD KNKLSRSIID THDFYILPIV NPDGFVYTTK SDRLWRKNRQ
KTPYKKCVGT DMNRNWPYKW DIPGGSSTDP CEETYRGVKP GDTPEIKALT NHTMAISQKT
GISSYIDWHS YSQLILLPYG YTCDQNATNI DYQMELAGEV ASAIEDYEGT YFDYGPTCQT
IYQTSGGSSD WVYDVAEAEL AWGIELRPAR LRGDGFVLPP KNIVASGEEI WAGMQVLFKS
LVEKDK
//
