ID G3AQH9_SPAPN Unreviewed; 492 AA.
AC G3AQH9;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN ORFNames=SPAPADRAFT_62113 {ECO:0000313|EMBL:EGW31526.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW31526.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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}.
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DR EMBL; GL996503; EGW31526.1; -; Genomic_DNA.
DR RefSeq; XP_007376304.1; XM_007376242.1.
DR AlphaFoldDB; G3AQH9; -.
DR STRING; 619300.G3AQH9; -.
DR GeneID; 18874188; -.
DR KEGG; spaa:SPAPADRAFT_62113; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR InParanoid; G3AQH9; -.
DR OMA; YRIYNVQ; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000000709; 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 Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..492
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003442561"
FT DOMAIN 370..380
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 492 AA; 57734 MW; E52B0A968E08680A CRC64;
MQHFQKIGLI LTLLGLSTAL QWQFPFDISK FRLNGGDSTH LHFSTVDPSD FPIDLLKYHD
DYVIRVNYGD NAELKRFLLS KSGDSSNDTQ IKFSRWTRNT STRQIDLQID ENNLIKLIEK
FPLISYDIII EDLSQKVYET YPKDFHNSIT TKDSKYQYQS THDVINATTA NVFSEVFFKE
YRPLETIDSW LELLQETYPD ILSIEEIGHT YENRPYKVVH FAVPNDDVKH GDRRTIVITG
GTHAREWISV SSVLYAIYDL LQFYAEEPES KIFKELDFLF IPVANPDGYE YTWKADRLWR
KNRQQTVQPN CFGIDLDHSY DYHWTKSTDW ECGEEYSGEY PFEAIESKIW EEYLNNTNHD
HKIWGYIDLH SYSQEVLYPY AYSCDQQPRD EENLIEAAYG IAKSIRLQSG VNYHVLPACI
DRDADLLPDL GSGSALDFMY HNRAYWAFQL KLRDSGSHGF LLPPKYIEPV GREVFAGFKY
FCYFILSDER QH
//
