ID A0A365MYJ5_GIBIN Unreviewed; 438 AA.
AC A0A365MYJ5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00132};
GN ORFNames=FPRO05_02422 {ECO:0000313|EMBL:RBA13629.1};
OS Gibberella intermedia (Bulb rot disease fungus) (Fusarium proliferatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=948311 {ECO:0000313|EMBL:RBA13629.1, ECO:0000313|Proteomes:UP000251714};
RN [1] {ECO:0000313|EMBL:RBA13629.1, ECO:0000313|Proteomes:UP000251714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ITEM 2341 {ECO:0000313|EMBL:RBA13629.1,
RC ECO:0000313|Proteomes:UP000251714};
RA Almiman B.F., Shittu T.A., Muthumeenakshi S., Baroncelli R.,
RA Sreenivasaprasada S.;
RT "Genome sequence of the mycotoxigenic crop pathogen Fusarium proliferatum,
RT strain ITEM 2341 from Date Palm.";
RL Submitted (DEC-2017) 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}.
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:RBA13629.1}.
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DR EMBL; PKMI01000028; RBA13629.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365MYJ5; -.
DR Proteomes; UP000251714; Unassembled WGS sequence.
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.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..438
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016916460"
FT DOMAIN 163..185
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 438 AA; 49579 MW; EE676BAB80AEFF36 CRC64;
MRYSIVSLLT LALGALAVPK TEIKSYDGYK VFRVNTHGKA AIKEKLTPVT FDEWEHGYQH
VDIVVAPNDI SAFESLKLDY TTLHENLGTS ITGESVSRKK WKRQADDDSW FDEFHNYEDH
IDYFRDLQAQ FPNNSKLVSS GKSYQKRNIY GLHLWGNDGP GKPAVLYHGT VHAREWISGP
TLEYITLQLV KGFKSGDEDV QTYLNKYDFY IFPFVNPDGF VYSTTADRLW RKNRQPPPAT
AANQSCYGRD INRNWEFGWD SNKRGASTDP CSQVYRGEKP ADTPENQGLD KFVRQLRDTV
GIALYIDWHS YGQYILSPFG YKEDLYAPEL GKWTKAAALV SEAIRESTDD HTTYTFGPSG
AVLYVTTGAA PDHVYSVGGA KFSYTIEQRD TGENGFVLPP EQIRPNAEEQ WAGQKVLLSL
LDETFFDGKG PALYQGQT
//
