ECM14_ASPNC
ID ECM14_ASPNC Reviewed; 621 AA.
AC A2QZA2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ecm14; ORFNames=An12g04170;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
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 487 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; AM270267; CAK46187.1; -; Genomic_DNA.
DR RefSeq; XP_001395491.1; XM_001395454.2.
DR AlphaFoldDB; A2QZA2; -.
DR SMR; A2QZA2; -.
DR PaxDb; A2QZA2; -.
DR EnsemblFungi; CAK46187; CAK46187; An12g04170.
DR GeneID; 4985765; -.
DR KEGG; ang:ANI_1_520104; -.
DR VEuPathDB; FungiDB:An12g04170; -.
DR HOGENOM; CLU_019326_1_0_1; -.
DR Proteomes; UP000006706; Chromosome 3L.
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..171
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453238"
FT CHAIN 172..621
FT /note="Inactive metallocarboxypeptidase ecm14"
FT /id="PRO_5000220731"
FT REGION 544..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..609
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 262..265
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 262
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 320
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 337..338
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 394
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 395..396
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 331..354
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 621 AA; 70041 MW; 32E264C96A4B3A94 CRC64;
MRHLLSLLVL LIASAALVSA VPAGSIITPQ PPVEPVHLLS SQPSDPRRPW IRLRDWIIES
IWGIEKPASR RFPLNDSPRN RSPPSRILAR YGSDVVLRFS LRNHDEAEAL AQAADILFLD
VWASTPAFVD IRLAEEVIPS LLGLLPNSLQ TAYTPLIDNL AERIYTTYPS KKPIGLEGQS
GFASSSRPAP KFGDLFFHEY QPLSVIIPWM RLLASMFPSH VRMISVGVSY EGREIPALRL
SAGSSTAASG PRKTIIVTGG SHAREWIGTS TVNHVMYTLI TKYGKSKAVT RLLQDFDWIM
IPTINPDGYV YTWETDRLWR KNRQRTSLRF CPGIDLDRAW GFEWDGGRTR ANPCSENYAG
DEPFEGMEAQ QLAQWALNET QNNNADIVSF LDLHSYSQTI LYPFSYSCSS IPPTLESLEE
LGLGLAKAIR YATHEIYDVT SACEGIVTAS AADNNPGRFF PIGGNSGGSA LDWFYHQVHA
TYSYQIKLRD RGSYGFLLPS EHIIPTGKEI YNVVLKLGSF LIGGDSFDVD WESELFDLSK
DESDLDSRYS KSNDRSPAYL HNANGPLPNI DEDEDKEWVM VEEEDYTDDD DDDDDDDEEE
EEEEEDTYWA TEHTYEFRRR R
