ECM14_SCLS1
ID ECM14_SCLS1 Reviewed; 596 AA.
AC A7EUC0;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Inactive metallocarboxypeptidase ecm14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ecm14; ORFNames=SS1G_08927;
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1;
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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 506 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; CH476632; EDN93062.1; -; Genomic_DNA.
DR RefSeq; XP_001590163.1; XM_001590113.1.
DR AlphaFoldDB; A7EUC0; -.
DR SMR; A7EUC0; -.
DR STRING; 665079.A7EUC0; -.
DR GeneID; 5486328; -.
DR KEGG; ssl:SS1G_08927; -.
DR VEuPathDB; FungiDB:sscle_14g100610; -.
DR InParanoid; A7EUC0; -.
DR OMA; SACEGNV; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IBA:GO_Central.
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; IBA:GO_Central.
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..26
FT /evidence="ECO:0000255"
FT PROPEP 27..190
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453251"
FT CHAIN 191..596
FT /note="Inactive metallocarboxypeptidase ecm14"
FT /id="PRO_0000411190"
FT BINDING 285..288
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 285
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 343
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 360..361
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 417..418
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 354..376
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 596 AA; 66780 MW; AB433B57EB60C776 CRC64;
MSQSHSILSS LILLVAIIFC VPHVIAVPWT TDGHAQLSPV TPRYPTQEPS GIRYRNVIPQ
LTWLCDTAIE KIFGLPPKVA KKPDVPGNVA RPTNAQLPAT LLAKYGGDVV LRFNLTTPAE
EQALAEAADT LFLDIWEFTS NWADIRLRED DVPSLLGLLP KSLQNAYSHL MPDLAKSIYQ
SYPSMAYADA AFSSKHVERA FTPALRTSKV EGADNIFFQN YQPLSVIIPW MRLMSSMFST
HVRMINIGIS YEGRDIPALR IGVSPNLPSE ATKPRKTIIL SGGFHAREWI SVSSVTYAAW
SLITSYGKSP AITKLLQEFD FVLVPTINVD GYVYTWENDR LWRKNRQQTN LRFCRGLDLD
RGFGFEWGSS TQTNPCSESY PGDAPFQAVE SHRFAEWAKN ETENNNVHFV GFLDLHSYSQ
QVLYPYSYSC LADPPSLENL EELGIGLAKA IRISSGEQYT VASACEGAIS SKIPGYSSTS
RMEMGGGSAI DWFYHELGVR YSYQIKLRDT GSYGFLLPKE NIVPTGEEVF NVIKYFGDFL
LGDKGIEKAK SSEEEPITKP VKSELPLGVM EEESVISDEI EDEYEDINLE LKRRRR
