ID A0A0N1NXW7_9EURO Unreviewed; 533 AA.
AC A0A0N1NXW7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Carboxypeptidase M14B {ECO:0000256|ARBA:ARBA00042017};
DE AltName: Full=Carboxypeptidase MCPB {ECO:0000256|ARBA:ARBA00041263};
GN ORFNames=AB675_7216 {ECO:0000313|EMBL:KPI35073.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI35073.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI35073.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI35073.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Extracellular metalloprotease that contributes to
CC pathogenicity. {ECO:0000256|ARBA:ARBA00003091}.
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:KPI35073.1}.
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DR EMBL; LFJN01000045; KPI35073.1; -; Genomic_DNA.
DR RefSeq; XP_017995036.1; XM_018147567.1.
DR AlphaFoldDB; A0A0N1NXW7; -.
DR GeneID; 28739447; -.
DR OrthoDB; 2665904at2759; -.
DR Proteomes; UP000038010; 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; cd06242; M14-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF83; INACTIVE METALLOCARBOXYPEPTIDASE ECM14; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:KPI35073.1};
KW Hydrolase {ECO:0000313|EMBL:KPI35073.1};
KW Protease {ECO:0000313|EMBL:KPI35073.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..533
FT /note="Carboxypeptidase M14B"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005879428"
FT DOMAIN 98..188
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|Pfam:PF00246"
SQ SEQUENCE 533 AA; 59844 MW; D91367DC6AB941C7 CRC64;
MYFRVLALAA AITGVSAQGL QYGENQRGTI KDSDIVAQAF PDVDGIELLS PAFLRPNSTP
PGWSNGTDGP TDDAEMDYWY RTIARRNDWL HYLGAEFSSE EGRPIPYLFL TSPDSNNATK
LKVYIQAAIH GDEPAGDQSV MALLGKMDAN QTWTASLLER MDIKILPRYN PDGVAYFQRQ
LASNLDGNRE HLKLDRQQSR VIKKVFMDYS PHISIDMHEF TAPTVYGGDY QHGADALISG
GINPNIHPAI REQLLEVFIP AMGERLETNG LRWEPYVTGS SNRTQGSRIE FEEAVTEART
GRNAYGLTQT ISFLCELRGI RLADQHFQRR VTTGLLKLEA ILETARDNFD SALSIVEDAR
EEFINGNDDI VITDSYTPSV RNFTMVNRET GEIEQVEVDF WETTPSVANL TRPRPEAYLI
PRTWSDVAAR LENYGLEVET LDYEYRGTVE VLNITSTELD DAIYEGHVLN TVTAEPLYKE
VRLPVGSFLV STRQKNAALA FIALEPENID SYVTFNLIPV DVGDEYPIFR VMG
//
