ECM14_LEPMJ
ID ECM14_LEPMJ Reviewed; 573 AA.
AC E5A0U8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Inactive metallocarboxypeptidase ECM14 {ECO:0000305};
DE Flags: Precursor;
GN Name=ECM14; ORFNames=Lema_P103750;
OS Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
OS (Blackleg fungus) (Phoma lingam).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Leptosphaeriaceae;
OC Leptosphaeria; Leptosphaeria maculans species complex.
OX NCBI_TaxID=985895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8;
RX PubMed=21326234; DOI=10.1038/ncomms1189;
RA Rouxel T., Grandaubert J., Hane J.K., Hoede C., van de Wouw A.P.,
RA Couloux A., Dominguez V., Anthouard V., Bally P., Bourras S.,
RA Cozijnsen A.J., Ciuffetti L.M., Degrave A., Dilmaghani A., Duret L.,
RA Fudal I., Goodwin S.B., Gout L., Glaser N., Linglin J., Kema G.H.J.,
RA Lapalu N., Lawrence C.B., May K., Meyer M., Ollivier B., Poulain J.,
RA Schoch C.L., Simon A., Spatafora J.W., Stachowiak A., Turgeon B.G.,
RA Tyler B.M., Vincent D., Weissenbach J., Amselem J., Quesneville H.,
RA Oliver R.P., Wincker P., Balesdent M.-H., Howlett B.J.;
RT "Effector diversification within compartments of the Leptosphaeria maculans
RT genome affected by Repeat-Induced Point mutations.";
RL Nat. Commun. 2:202-202(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 504 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; FP929131; CBX97244.1; -; Genomic_DNA.
DR RefSeq; XP_003840723.1; XM_003840675.1.
DR AlphaFoldDB; E5A0U8; -.
DR SMR; E5A0U8; -.
DR STRING; 985895.E5A0U8; -.
DR EnsemblFungi; CBX97244; CBX97244; LEMA_P103750.1.
DR GeneID; 13283799; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_0_1; -.
DR InParanoid; E5A0U8; -.
DR OMA; SACEGNV; -.
DR OrthoDB; 524270at2759; -.
DR Proteomes; UP000002668; Genome.
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..21
FT /evidence="ECO:0000255"
FT PROPEP 22..186
FT /evidence="ECO:0000250|UniProtKB:P38836"
FT /id="PRO_0000453244"
FT CHAIN 187..573
FT /note="Inactive metallocarboxypeptidase ECM14"
FT /id="PRO_0000411184"
FT REGION 23..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 281..284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 339
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 356..357
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT BINDING 414..415
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00730"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 350..373
FT /evidence="ECO:0000250|UniProtKB:P15085"
SQ SEQUENCE 573 AA; 64366 MW; 62C73C8A2E63B792 CRC64;
MRQPTFAALS LLLVAPSLVA AVPHDSTSTS TSTSTRSPSY DPDSTAAHDT TTPHTPPSPW
RRLSEAIIRR IGSLPHENHL QKSMLALATG PSSRAPGKQW VAHYGGDVVL RFKMQTADEA
RALSQAAATL FLDVWEFNED WADIRLAKDV LPSLLGLLPR SLHASYEPLM QDAALVQAIF
DTYPSSSASP SHNTNRFSPN LRPSPHHANG HPFFQDYQPL SVIDPWMSLM SSMFTTHVRK
INIGISYEGR DIPALRVGVH PTNKDEPTKP RKTVLITAGL HAREWISTST VNYLAWSVIN
AYGKDREITH LLEKFDFVFV PTLNPDGYVY TWETDRLWRK NRQPTSLRFC HGIDLDRSFP
YQWNGDQMGS NPCSESFAGD APFEGVESQR FADWARNETE SNNVEFVGLL DLHSYSQQIL
YPYSYSCHDE PPSLEDLEEL GLGLAKAIRI SRKGHTYKVT SACEGNVAFA NKEKTVLPRI
ESSGGSALDF FYHELRVKYS YQIKLRDTGN YGFLLPKEEI IPTGEEMLDA VLYLGRFMLG
EVGWARRRSR SRWSAPDRGT GDFDEAEQVA IEL
