ECM14_PARBD
ID ECM14_PARBD Reviewed; 591 AA.
AC C1GDH9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ECM14; ORFNames=PADG_05315;
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18;
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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 489 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; KN275962; EEH49236.1; -; Genomic_DNA.
DR RefSeq; XP_010760957.1; XM_010762655.1.
DR AlphaFoldDB; C1GDH9; -.
DR SMR; C1GDH9; -.
DR STRING; 121759.XP_010760957.1; -.
DR PRIDE; C1GDH9; -.
DR EnsemblFungi; EEH49236; EEH49236; PADG_05315.
DR GeneID; 22584264; -.
DR KEGG; pbn:PADG_05315; -.
DR VEuPathDB; FungiDB:PADG_05315; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR OMA; SACEGNV; -.
DR Proteomes; UP000001628; 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.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 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..175
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453247"
FT CHAIN 176..591
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /id="PRO_0000411187"
FT REGION 533..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..547
FT /note="Basic and acidic residues"
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 265..268
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 265
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 323
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 340..341
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 398..399
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 334..357
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 591 AA; 67374 MW; E0584C49D55FEF47 CRC64;
MRLFSHLAVL AILACAVPIT AIPSFLSNSY PAHPAEGISL FPQTQPQAPL GLWTRLRNTV
IERLWRVPPQ LCKNRPGHKG KFPLFSAPAS LRARYGDDVV LRFTIRNAEE VKALAEASNI
LFLDVWASTD EWVDIRLSKD VVPSLLGLLP KSLQTSHIPL IHDLPQTIYE SYPSSSQRSS
YDVQGFSPST KHSSDKTNIF FQDYQPFSVI VPWMRLLTSM FSSHVQMINI GSTFEGRDIP
ALQIGVWPAN NPKPRKTVVV SGGSHAREWI SVSTVNYVAY SLITNYAKSK HVAELLQQFD
FIFIPTLNPD GYIYTWEVDR IWRKNRQDTS LPFCPGVDLD RTWGFKWDGN ITADNPCSES
YPGEDPFAGI EAKQFSQWAK NQTAQNNTEF VAFIDLHSYS QQIRYPYSYS CQPDPPNLEN
LEELAIGIAK AIRLTNRETY EVSSACEGLM ASQAKVKSDD PFPRIERTGG SALDWFYHDL
NVKYSYQIKL RDRGSYGFLL PRENIVPTGQ EMFNAVMVLG RFLSGHDGFG PLDWEDESQR
PKADEDDIPS ENELDENDDS WIPYDYRNHD DQNEGEGYDN DEWGFRRRRK R
