ID X0CAV5_FUSOX Unreviewed; 557 AA.
AC X0CAV5;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000256|ARBA:ARBA00026187};
DE AltName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000256|ARBA:ARBA00026213};
GN ORFNames=FOQG_06297 {ECO:0000313|EMBL:EXK91555.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK91555.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK91555.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK91555.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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}.
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DR EMBL; JH658372; EXK91555.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CAV5; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR Proteomes; UP000030663; 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; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..557
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004936269"
FT DOMAIN 245..267
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT REGION 528..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 557 AA; 63144 MW; 58B6E02A6BD71061 CRC64;
MRLPLLAASL LLLQASSAHA AGIDTHRAVP DLQNNENNNN DANKRLFPFL SKLRDKAIET
VFGRHPSKNT PPPVINQLRA QYLNQLVLRF NVTTSHEEGA LADAAARLFL DVWAFTDDYV
DIRLHADEVR PLLSLLPKTL HASHSILIPD LAAAVYKSLP IGGNPAYYDP KPAPPVLKVA
SSPGDNLFFQ DYQSLPVVMR WMRLLEAMFP SYVKYINIGK SYEGRDIPAL RVGIPNTAPD
APRRKTIMIM GGSHAREWIS TSTVNYLAWS FITSYGKERM ITKLLDEFDL VFLPIANPDG
FEYTWHIDRL WRKTRQQTNL QFCRGLDLDR AYGYEWDGSQ VQRDPCSESY GGEKPFQAVE
AVHIADWARN QTWNNNVRFV GLIDLHSYSQ QILYPYSYTC SVDPPNLENL EELAAGIAKS
IRLSNGESYT VASACEGAVS AREFSGGRYW SRIESGGGSA VDWFYHEMRA HYSYQLKLRD
TGSYGFLLPK EHIVPTGEEI FNAMKYYGDY LLGNNGIESI TEAEEDDKVE MHENQPVQDS
EQNPTVGQEL RRRRLRR
//
