ID A0A1C1CMS0_9EURO Unreviewed; 581 AA.
AC A0A1C1CMS0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN Name=ECM14 {ECO:0000313|EMBL:OCT49818.1};
GN ORFNames=CLCR_06954 {ECO:0000313|EMBL:OCT49818.1};
OS Cladophialophora carrionii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT49818.1, ECO:0000313|Proteomes:UP000094526};
RN [1] {ECO:0000313|Proteomes:UP000094526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL Submitted (JUL-2015) 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 -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000256|ARBA:ARBA00004116}.
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:OCT49818.1}.
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DR EMBL; LGRB01000010; OCT49818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C1CMS0; -.
DR STRING; 86049.A0A1C1CMS0; -.
DR VEuPathDB; FungiDB:CLCR_06954; -.
DR VEuPathDB; FungiDB:G647_08740; -.
DR eggNOG; KOG2650; Eukaryota.
DR Proteomes; UP000094526; Unassembled WGS sequence.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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:OCT49818.1};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000313|EMBL:OCT49818.1};
KW Protease {ECO:0000313|EMBL:OCT49818.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094526};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..581
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008650970"
FT DOMAIN 399..409
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
FT REGION 535..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 65569 MW; 4593034FA860B37C CRC64;
MAPFFRDIFI LATIITSAVA IPTSESLPHT SLEPNVAFTH RDKPAGPFRR LRDAIIERIW
SVPGKSPYKS SPGSRLPKAP EGFRARYGAD VVLRFRVRTQ EEAKAISEAA DILYLDIWEA
TNEWVDIRIA KEVVPSFIGL LPPSLHDSYV PLIQDIARAV FDTYPDSSSP HERALISSLM
DAPDWRLKGN TPHDLFFQDY QPLSVMYPWL RLLASLFPTH ASLTTIGTSA EGRDIPALRI
GSRFNSSTAD SHDSRHTLLI VGGTHAREWI SVSTVAYIAY SLVTRYGHPQ FPEVTKILDH
FDLVFIPVLN PDGYEYTWTT DRLWRKNRQS TFIPFCPGID LDRAFRFGWD GYWNRDNACS
DDYAGPEPLA AVEAQVLTEW ARNETAYNNV SFVSYLDFHS YSQEVLYPYS YTCDTAPPNL
EDLEEVALGI AKSFRLTNGH VYNVESACEG DVAFQSEAKQ TRVQIEAQGG SALDFFYHDL
DVKLAFQIKL RDTGTYGFLL PRSHILPTGQ EAYEGVVGLG RWMLGNHGIE NIDDPRSVWG
NEAPGTSSQN VGSTQGAEEL STEEEYDFDK GDFELRRRRR R
//
