ID A0A1B8AF08_FUSPO Unreviewed; 440 AA.
AC A0A1B8AF08;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN ORFNames=FPOA_10795 {ECO:0000313|EMBL:OBS19071.1};
OS Fusarium poae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=36050 {ECO:0000313|EMBL:OBS19071.1, ECO:0000313|Proteomes:UP000091967};
RN [1] {ECO:0000313|EMBL:OBS19071.1, ECO:0000313|Proteomes:UP000091967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2516 {ECO:0000313|EMBL:OBS19071.1,
RC ECO:0000313|Proteomes:UP000091967};
RA Vanheule A., Audenaert K., Warris S., Van De Geest H., Schijlen E.,
RA Hofte M., De Saeger S., Haesaert G., Waalwijk C., Van Der Lee T.;
RT "Living apart together: crosstalk between the core and supernumerary
RT genomes in a fungal plant pathogen.";
RL Submitted (JUN-2016) 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:OBS19071.1}.
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DR EMBL; LYXU01000004; OBS19071.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8AF08; -.
DR STRING; 36050.A0A1B8AF08; -.
DR OMA; RYYGKAC; -.
DR OrthoDB; 1893867at2759; -.
DR Proteomes; UP000091967; 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 Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF119; OS02G0119300 PROTEIN; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000091967};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..440
FT /note="Peptidase M14 carboxypeptidase A domain-containing
FT protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008602810"
FT DOMAIN 74..395
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|SMART:SM00631"
FT REGION 183..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 440 AA; 48559 MW; 07D6E60C9E9F5C51 CRC64;
MKLALVAYAL SASACLIPSD SVPHSERNYG LSARQARPEP DFPIGTGDRF NKGKIAPKGL
STSDRNLKSI LTPTEVNSAL EGLAKQFKEV ELIHPPHKTY EGFKTVGAKI GKNPKFFIIS
GAHARERGGP DNVVYWLSDL LHARKAGKGL KYGKTTYTAA EVRKALDGGI VILPNINPDG
VKHDQKTNSC WRKNRNPKSS KGNPDAVGID INRNYDFLFN YKKAFSDTID LSSVASEDPR
SEVFHGTGPN SEPETKNVVW TMDKFKSLSW FVDLHSFGGY MLYAWGDDDA QTTNKAESFA
NKKYDGRRGV LGDDETPKTK YKEYITKSDL SGQLKLGNRM KKVMENAGTS KYTVQEAVGL
YPTSGASTDY ALARYYGKAC GKSKLQSYTI EFGEESGSAA CPFYPDQKQY HMWMKQVASG
LTEVALKAAD TTPEVKKCPY
//
