ID A0A367XYY2_9ASCO Unreviewed; 469 AA.
AC A0A367XYY2;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN Name=ECM14_1 {ECO:0000313|EMBL:RCK57981.1};
GN ORFNames=Cantr_06539 {ECO:0000313|EMBL:RCK57981.1};
OS Candida viswanathii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5486 {ECO:0000313|EMBL:RCK57981.1, ECO:0000313|Proteomes:UP000253472};
RN [1] {ECO:0000313|EMBL:RCK57981.1, ECO:0000313|Proteomes:UP000253472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20962 {ECO:0000313|EMBL:RCK57981.1,
RC ECO:0000313|Proteomes:UP000253472};
RA Ahn J.;
RT "Whole genome sequencing of Candida tropicalis (genome annotated by CSBL at
RT Korea University).";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inactive carboxypeptidase that may play a role in cell wall
CC organization and biogenesis. {ECO:0000256|ARBA:ARBA00025210}.
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:RCK57981.1}.
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DR EMBL; QLNQ01000028; RCK57981.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367XYY2; -.
DR STRING; 5486.A0A367XYY2; -.
DR Proteomes; UP000253472; 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; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF147; INACTIVE METALLOCARBOXYPEPTIDASE ECM14; 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:RCK57981.1};
KW Hydrolase {ECO:0000313|EMBL:RCK57981.1};
KW Protease {ECO:0000313|EMBL:RCK57981.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000253472};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..469
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016883611"
FT DOMAIN 349..359
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 469 AA; 54641 MW; E6FEE34382042292 CRC64;
MNYKLVLLLL AHVAFTVQLQ LPFHLDGILP QTSSKAHYSS VDPRDHPINL SQYAHDSVIR
IDYSQSRELE TYLKSKSSNE TSDSIVFKKW GKNISRKTID IQISQPDMFK LIQKFKHALK
FEVLIDDLPQ KIFETYPQAS AQSEEVVTNT ELFFQDYRNL DTINAWLELL AASYPEIISL
EDIGETFEHR KLKVVHFTVP HEHPDDEDHG DRRTVVITGG VHSREWISVS STLYAIYELV
ELYKVDPDSK IFVELDFLFI PVYNPDGYQY TWNTDRLWRK NRQKTIKPNC FGIDIDHAFD
YHWTRSSDWA CGDEYSGEYP FEALEARIWH EYLNETNADH KIWGFIDLHS YAEEILYPYA
FSCEDQPRDE ENLIEVAYGL AKAIRLQTGR LYQVFAACLD RDADLLPDLG AGTILDYMYH
NRADFAYQLK LRDTGNHGFL LPAKQIIPVG KEVVASLKYL FHFLIDNDR
//
