ECM14_AJECN
ID ECM14_AJECN Reviewed; 607 AA.
AC A6RCF5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ECM14; ORFNames=HCAG_07313;
OS Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma;
OC unclassified Histoplasma.
OX NCBI_TaxID=2059318;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAm1 / WU24;
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 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; CH476662; EDN10852.1; -; Genomic_DNA.
DR RefSeq; XP_001537891.1; XM_001537841.1.
DR AlphaFoldDB; A6RCF5; -.
DR SMR; A6RCF5; -.
DR STRING; 339724.A6RCF5; -.
DR EnsemblFungi; EDN10852; EDN10852; HCAG_07313.
DR GeneID; 5444075; -.
DR KEGG; aje:HCAG_07313; -.
DR VEuPathDB; FungiDB:HCAG_07313; -.
DR HOGENOM; CLU_019326_1_0_1; -.
DR OMA; SACEGNV; -.
DR OrthoDB; 524270at2759; -.
DR Proteomes; UP000009297; 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_0000453229"
FT CHAIN 175..607
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /id="PRO_0000411170"
FT REGION 539..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..569
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..601
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 607 AA; 68688 MW; 4D81EED248E92E2E CRC64;
MRLFTHGQVL ALLAFVNTIS AIPSFSTNSY PAHPAEPVSL VSQHQPQAPL GLWTRLRNSV
IERVWGVPPQ QRHRGGNKHQ YPPFSAPASL RTRYGDDVVL RFKLQTADEV KALVEASNIL
FLDVWSSTDE WIDIRLAKDV VPSLLGLLPK SLQTTHVPLI RDLPQTIYES YPSPFQSSSG
HERGFLPSGE PSSDATNIFF ENYQPLSVIV PWMRLLASMF PSHAQFISIG SSFEGRDIPA
LRVGVRPAND QKPRRTLIIE GGSHAREWIG VSTVNYVAYS LITSYGKSKP ISTLLEQFDF
IFIPTINPDG YVYTWETDRL WRKNRQETSL PFCHGVDLDR TWGFEWNGNV TGDNPCLESY
GGDKPFAGVE AHQLAEWVKE QTEQRNAKFV AFVDLHSYSQ QILYPYSYSC LSQPPNLENL
EELAMGIAKA IRLTNRKTYA VSSACGGLMA SQKKKVKSET FLRMESTGGS ALDWFYHDFG
VKYAYQLKLR DRGSYGFLLP RENIVPTGNE VFNAVMMLGR FLLGKSRAFQ ELDWDAGFQR
PNKDDKPILN DDDDDDNDDD DDDDDDADTN DDGIGRKDDS WVPDEYKGDN DRDESDGGWG
FRRLRKR
