ECM14_UNCRE
ID ECM14_UNCRE Reviewed; 584 AA.
AC C4JEE1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ECM14; ORFNames=UREG_00780;
OS Uncinocarpus reesii (strain UAMH 1704).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Uncinocarpus.
OX NCBI_TaxID=336963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 1704;
RX PubMed=19717792; DOI=10.1101/gr.087551.108;
RA Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA Henn M.R., Birren B.W., Taylor J.W.;
RT "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT and their relatives.";
RL Genome Res. 19:1722-1731(2009).
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 490 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; CH476615; EEP75933.1; -; Genomic_DNA.
DR RefSeq; XP_002541266.1; XM_002541220.1.
DR AlphaFoldDB; C4JEE1; -.
DR SMR; C4JEE1; -.
DR STRING; 336963.C4JEE1; -.
DR EnsemblFungi; EEP75933; EEP75933; UREG_00780.
DR GeneID; 8444375; -.
DR KEGG; ure:UREG_00780; -.
DR VEuPathDB; FungiDB:UREG_00780; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR InParanoid; C4JEE1; -.
DR OrthoDB; 524270at2759; -.
DR Proteomes; UP000002058; 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..20
FT /evidence="ECO:0000255"
FT PROPEP 21..174
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453254"
FT CHAIN 175..584
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /id="PRO_0000411193"
FT REGION 564..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267..270
FT /ligand="substrate"
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 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 342..343
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 399
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 400..401
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 336..359
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 584 AA; 65723 MW; 875815B225C1B1FE CRC64;
MHLLPVITAV ALIYTPLASA VPSSSNPQFP AALLTESNSA ALPTQEWHSP RLWTRLRNSI
IETIWRVPSQ QRHPSRIKSP ASSRKAPASI RARYGDDVVL RFTIQSQSDI QALVEASNIL
FLDIWASTDE WVDIRLAKDV VPSLLGLLPS SLKAASVPVI HDLAQAVYES YPQPSSSTPN
PHRAFSPSIR LSSEAQNIFF QDYQPLSVMT PWMRLLASMF STHVSLISLG TSYEGRDITA
FRIGTHPMNP DNPFGQRKTI IITGGSHARE WISVSTVNYV AYSLITGYGK SKAITKLIEE
FDWVLVPTMN PDGYVYTWET DRLWRKNRQE NNLQFCPGVD LDRTWGFEWD GTDSRSNPCS
EDFAGDGPFG GTEAQRISQW ARNQTMNNNV TFIGFLDLHS YSQQILYPYS YSCNNIPPTL
ENLEELAIGI SRAIRRTDNE HYDVSSACQG SVNSGKKKQG PALKRMESAG GSALDWFYHD
LHVRYAYQLK LRDKGSYGFL LPRSNIIPTG KEVYNAVLEF GKFLLGKEAP SVDWDAEFQV
SDPSRPISPD NEYHDRDVEH EALQQLDDED GEADSHWVLR TQRS
