ECM14_NEOFI
ID ECM14_NEOFI Reviewed; 587 AA.
AC A1DGH9;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ecm14; ORFNames=NFIA_084380;
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC / WB 181;
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 491 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; DS027696; EAW18486.1; -; Genomic_DNA.
DR RefSeq; XP_001260383.1; XM_001260382.1.
DR AlphaFoldDB; A1DGH9; -.
DR SMR; A1DGH9; -.
DR STRING; 36630.CADNFIAP00007325; -.
DR EnsemblFungi; EAW18486; EAW18486; NFIA_084380.
DR GeneID; 4586941; -.
DR KEGG; nfi:NFIA_084380; -.
DR VEuPathDB; FungiDB:NFIA_084380; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR OMA; SACEGNV; -.
DR OrthoDB; 524270at2759; -.
DR Proteomes; UP000006702; 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 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.
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..170
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453245"
FT CHAIN 171..587
FT /note="Inactive metallocarboxypeptidase ecm14"
FT /id="PRO_0000411185"
FT REGION 68..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261..264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 319
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 336..337
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 393
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 394..395
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 330..353
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 587 AA; 66338 MW; 58877BA9B04DCCC4 CRC64;
MRLLLSVLLL LVASLGLVSA VPAGSSITPP PPIEPIQLLS SRSTDSRRPW IRLRDRVIES
IWGISKDSSH HRSVKDSPRS RSPSRSLTRY GSDVVLRFHL RNAEEAEALA EATDVLFLDV
WASTSEFVDI RLAQEVIPSL LGLLPDSLRT AYTPLIDNLA EMIYATYPTR RPVGFEDHPG
FIPSVRQSTQ FGDLFFRDYQ PLSVIVPWMR LMASMFSSHV QMINVGVSYE GREIPALRLG
TRGQTAEPYP RKTIVVVGGS HAREWISTST VIYTAYSLIT RYGKSHEVTR LLEDFDWVFV
PTLNPDGYVY TWESDRLWRK NRQPTSLHFC PGIDLDRAWE FQWDGERTRS NPCSENYAGT
EPFEGMEAHQ LAQWALNETQ TNNAKIVGFL DLHSYSQQIL YPFSFSCSSV PPTLESLEEL
GMGLAKVIRL TTHEIYDVTS ACEGTITADD QARNRNSPPK KPIFPTGGSS GGSALDWFYH
QLHTDYAYQI KLRDRGSYGF LLPSEYIVPT GKEIFNVVLT FGKFLVGDLA HNINLDWDAE
LQRTEPEEAP ASQGDEPAPA TQQVLQADVE DEETEWVEKA RSEFRRR
