ECM14_ASPOR
ID ECM14_ASPOR Reviewed; 604 AA.
AC Q2TZK2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ecm14; ORFNames=AO090011000821;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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 482 essential for
CC carbopeptidase activity. The mature form lacks catalytic activity
CC towards synthetic peptide substrates. {ECO:0000250|UniProtKB:P38836}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP007171; BAE65263.1; -; Genomic_DNA.
DR RefSeq; XP_001826396.1; XM_001826344.2.
DR AlphaFoldDB; Q2TZK2; -.
DR SMR; Q2TZK2; -.
DR STRING; 510516.Q2TZK2; -.
DR EnsemblFungi; BAE65263; BAE65263; AO090011000821.
DR GeneID; 5998499; -.
DR KEGG; aor:AO090011000821; -.
DR VEuPathDB; FungiDB:AO090011000821; -.
DR HOGENOM; CLU_019326_1_0_1; -.
DR OMA; SACEGNV; -.
DR Proteomes; UP000006564; Chromosome 7.
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 Gene3D; 3.30.70.340; -; 1.
DR InterPro; IPR036990; M14A-like_propep.
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..18
FT /evidence="ECO:0000255"
FT PROPEP 19..169
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453239"
FT CHAIN 170..604
FT /note="Inactive metallocarboxypeptidase ecm14"
FT /id="PRO_0000411179"
FT REGION 542..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..569
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 260..263
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 318
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 335..336
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 392
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 393..394
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 329..352
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 604 AA; 68175 MW; F008F81E21D59E71 CRC64;
MRYLFLIILV AFAALTTAVP AGSSITPPPP IEPVQLLSPQ SSDVRRPWTR VRDWIIETVW
GLPKPTSYRL PFNHLSHDQS APSRVQARYG SDVVLRFRLR NDKEAEALEQ ATEILFLDVW
ASTSDFVDVR LAEEVIPSLL GLLPDSLRTA YSPLIDNLPE LIYTTYPTRR PIGLEGQPGF
RPSVRQSAQL GDLFFQDYQP LSVIVPWMRL MASMFPSHVR MINVGISYEG REIPALRLGA
GSNRAQSAPR RTIVMVGGSH AREWISTSTV TYVASNLISN FGKSRAVTRL LEDFDVVLVP
TINPDGYVYT WEVDRLWRKS RQRTSLRFCP GIDLDRSWNF EWDGERTRSN PCSENYAGDE
PFEGVEAAQF AQWALNETQN NNVDIVGFLD LHSYSQQVLY PFSFSCSSVP PTLETLEELA
MGFAKVIRQT THEIYDVTSA CEGTVTATDK ASAKTFFPVS GGGSALDWFY HQLHASFAYQ
IKLRDRGSYG FLIPSEYIVP TGKEIYNVVL KMGEFLVKET ASPANKADIN WDADLLVHDD
STRTSSSESV SDPLSEANID STSTVKATPL PFPEDTLDSE WVPFDQNEEE NEEEQNWELR
RRRR
