ID W6Z863_COCMI Unreviewed; 587 AA.
AC W6Z863;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Peptidase M20 dimerisation domain-containing protein {ECO:0000259|Pfam:PF07687};
GN ORFNames=COCMIDRAFT_6849 {ECO:0000313|EMBL:EUC43754.1};
OS Bipolaris oryzae ATCC 44560.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=930090 {ECO:0000313|EMBL:EUC43754.1};
RN [1] {ECO:0000313|EMBL:EUC43754.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC43754.1};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family.
CC {ECO:0000256|ARBA:ARBA00006247}.
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DR EMBL; KI964020; EUC43754.1; -; Genomic_DNA.
DR RefSeq; XP_007689719.1; XM_007691529.1.
DR AlphaFoldDB; W6Z863; -.
DR STRING; 930090.W6Z863; -.
DR GeneID; 19125102; -.
DR KEGG; bor:COCMIDRAFT_6849; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_11_0_1; -.
DR OrthoDB; 3672990at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05674; M20_yscS; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017141; Pept_M20_carboxypep.
DR InterPro; IPR047177; Pept_M20A.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR45962; N-FATTY-ACYL-AMINO ACID SYNTHASE/HYDROLASE PM20D1; 1.
DR PANTHER; PTHR45962:SF1; N-FATTY-ACYL-AMINO ACID SYNTHASE_HYDROLASE PM20D1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037217; Carboxypeptidase_S; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037217-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037217-2}.
FT DOMAIN 288..448
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT ACT_SITE 241
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-1"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
FT BINDING 557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037217-2"
SQ SEQUENCE 587 AA; 63797 MW; DE690420252A8D22 CRC64;
MAGKDLGEQA VPHSSPNTTS HKRKFAAGAV LCLAALAILR NCATTPTTWS FLSNSSKSRL
DLQCQQADPL FPSRKTKELD DMESYLTSDD FRNVAIERLS GAVKIPTQSY DDMGDIGADP
RWDIFYSFAD YLSKTYPLAH ATLQLEKVNT HGLLYTWTGT NPGLKPNLLM AHQDVVPVPD
STLKQWTHPP FSGHYDGKFV WGRGASDCKN QLMAILNAIE ALIAADFTPQ RTLILSFGFD
EEISGGEGAK HLSAYLLKKL GHNSIAAIVD EGAVNIESWG ANFAIPGVAE KGYVDVDIVV
RMPGGHSSIP PPHNGIGVAS ELITLIEANR YEPHLADENP YLGLLQCGEK YAPEFPHQLG
KLLDKRSRRH GTCNKKDDLA LEAAKAGPGI KYLFTTSVAV DIIHGGVKTN ALPERTQFTV
NHRINVGSTS SQVKSHISSL AAQVAEKYNL TLHAFTGEET PSSISLSHGP TILEPAPITP
TSLVQSSSSS NASVSTTTTP FALLAGTTRA LYGRDLIVSP GLMTGNTDTR FYWDLSEHIF
RYGPGWDREQ VGLGNIHTVD EKVGVTAHLD TVKWMVGWIR NVDEAVI
//
