ID C9SL06_VERA1 Unreviewed; 316 AA.
AC C9SL06;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Zinc carboxypeptidase A {ECO:0000313|EMBL:EEY19374.1};
GN ORFNames=VDBG_05483 {ECO:0000313|EMBL:EEY19374.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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DR EMBL; DS985219; EEY19374.1; -; Genomic_DNA.
DR RefSeq; XP_003004370.1; XM_003004324.1.
DR AlphaFoldDB; C9SL06; -.
DR STRING; 526221.C9SL06; -.
DR GeneID; 9531356; -.
DR KEGG; val:VDBG_05483; -.
DR eggNOG; KOG2650; Eukaryota.
DR HOGENOM; CLU_019326_1_1_1; -.
DR OMA; DYQKDPA; -.
DR OrthoDB; 3540647at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 2.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EEY19374.1};
KW Hydrolase {ECO:0000313|EMBL:EEY19374.1};
KW Protease {ECO:0000313|EMBL:EEY19374.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..316
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003002955"
FT DOMAIN 99..121
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
SQ SEQUENCE 316 AA; 35481 MW; 2D43C06FEF3B9F98 CRC64;
MRFIAAFPLV TLWASANNIV SYDGCHALRV RSEGDLPAVQ SKFSKLSYDE WERTADDITI
TLSPEQIPAF NSLGLGYDVM HVRDIFGIHF WGDEGPGKPA VFFHGTVHAR EWISAPFIEY
VTLQLLTGYG NDNQTTVARD SYDLCIFPFA NPDVGCQPER RFGYKGEAPG DTPEMAGLHG
FIDKLRDANG IKLFIDWHSY SQYLLAPLSW NCTQYIPKLG QHVNLARRAT RAIREVEGTQ
FVFGPSCATL YVATGYSIDY AYEVGKADWA YVIELRDTGN HGFVLPPEQI RGSAEEQWGG
IKTILQYLDV EDIFEA
//
