ECM14_AJECG
ID ECM14_AJECG Reviewed; 597 AA.
AC C0NM08;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ECM14; ORFNames=HCBG_04538;
OS Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=447093;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432;
RA Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Inactive carboxypeptidase that may play a role in cell wall
CC organization and biogenesis. {ECO:0000250|UniProtKB:P38836}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P00730};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P00730};
CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000250|UniProtKB:P38836}. Secreted
CC {ECO:0000250|UniProtKB:P38836}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved Glu residue in position 488 essential for
CC carbopeptidase activity. The mature form lacks catalytic activity
CC towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}.
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DR EMBL; GG663367; EEH07659.1; -; Genomic_DNA.
DR AlphaFoldDB; C0NM08; -.
DR SMR; C0NM08; -.
DR STRING; 447093.C0NM08; -.
DR PRIDE; C0NM08; -.
DR EnsemblFungi; EEH07659; EEH07659; HCBG_04538.
DR VEuPathDB; FungiDB:HCBG_04538; -.
DR HOGENOM; CLU_019326_1_0_1; -.
DR InParanoid; C0NM08; -.
DR OrthoDB; 524270at2759; -.
DR Proteomes; UP000001631; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
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 InterPro; IPR000834; Peptidase_M14.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW Metal-binding; Reference proteome; Secreted; Signal; Vacuole; Zinc.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..174
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453227"
FT CHAIN 175..597
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /id="PRO_0000411168"
FT REGION 170..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 264..267
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 267
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 339..340
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 397..398
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 333..356
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 597 AA; 67624 MW; 535561674D59B952 CRC64;
MRLFTHGQVL ALLAFVNTIS ATPSFSTNSY PAHPAEPVSL FSQHQPQAPL GLWTRLRNSV
IERVWGVPPQ QRHRGGNKHQ YPPFSAPASL RARYGDDVVL RFKLQTADEV KALVEASNIL
FLDVWSSTDE WIDIRLAKDV VPSLLGLLPK SLQTTHVPLI RDLPQTIYES YPSPSQSPSG
RERGFLPSGE PSSDVTNIFF ENYQPLSVIV PWMRLLASMF PSHAQFISIG SSFEGRDIPA
LRVGVRPAND QKPRRTLIIE GGSHAREWIG VSTVNYVAYS LITSYGKSKP ISTLLEQFDF
IFIPTINPDG YVYTWETDRL WRKNRQETSL PFCPGVDLDR TWGFEWNGNA TGDNPCLESY
GGDKPFAGVE AHQLAEWVKE QTEQRNTKFV AYMDLHSYSQ QILYPYSYSC LYQPPNLENL
EELAMGIAKA IRLTNRKTYA VSSACGGLMA SQKKKAKPET FLRMESTGGS ALDWFYHDFG
VKYAYQLKLR DRGSYGFLLP RENIVPTGKE VFNAVMMLGR FLLGESNAFQ ELDWDAGFQR
PKKDDKPILN DDDDDDADTN DDGIGRKDDS WIPDEYKGDN DRDESDGGWA FRRLRKR
