ECM14_ASPCL
ID ECM14_ASPCL Reviewed; 590 AA.
AC A1CSU3;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ecm14; ORFNames=ACLA_080640;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027060; EAW06380.1; -; Genomic_DNA.
DR RefSeq; XP_001267806.1; XM_001267805.1.
DR AlphaFoldDB; A1CSU3; -.
DR SMR; A1CSU3; -.
DR STRING; 5057.CADACLAP00007898; -.
DR EnsemblFungi; EAW06380; EAW06380; ACLA_080640.
DR GeneID; 4700124; -.
DR KEGG; act:ACLA_080640; -.
DR VEuPathDB; FungiDB:ACLA_080640; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR OMA; SACEGNV; -.
DR OrthoDB; 524270at2759; -.
DR Proteomes; UP000006701; 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..22
FT /evidence="ECO:0000255"
FT PROPEP 23..175
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453234"
FT CHAIN 176..590
FT /note="Inactive metallocarboxypeptidase ecm14"
FT /id="PRO_0000411175"
FT REGION 549..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..582
FT /note="Acidic residues"
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 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 336..359
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 590 AA; 65533 MW; 90BD0AC3442BB512 CRC64;
MRLLLSVLLV LVASVGVGLV SAVPAGSSIT PPPPIEPIHL LSAPSPSQDS RRPWTRLRDW
VIESIWGISK SCSHPHSSSH SSSRDRPPSQ ALARYGSDVV LRFYPGSAQD AEALAEASEI
LFLDVWASTP EFVDIRLAEE VISSLLGLLP DSLRTAYTPL IDDLAEMIHA SYPTRRSAGV
GDQSGFMPTV RQSAQLGDLF FRDYQPLSVI VPWMRLMASM FSSHVEKISV GVSYEGREIP
ALRLGVREAD PEPARPRKTI LIVGGSHARE WISTSTVTYV AYQLIARYGK SPEVTRLLED
YDWVLVPTLN PDGYAYTWES DRLWRKNRQP TSLRFCPGID LDRAWAFEWD GERTRTNPCS
ETYAGDAPFD GTEAQQLAQW ALAQTQSANA TIVGFLDLHA YSQQILYPYS YSCSAVPPTL
ESLEELAMGL AKVIRLTTHE VYDVTSACEG ITVSKSTPHV QTNPGSSGGS ALDWFYHQLH
TNYAYQIKLR DRGSYGFLLP AEYIVPTGRE IYNVVLTFGK FLLGDAAAHL DHLDWEAAMA
TEPEGVVEAQ QTLHQPEGGE VAAAADQTED ENENEDEDEE WDEHGWEFRR
