ID W6ZBK6_COCMI Unreviewed; 788 AA.
AC W6ZBK6;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Glycoside hydrolase family 55 protein {ECO:0000313|EMBL:EUC47168.1};
GN ORFNames=COCMIDRAFT_90841 {ECO:0000313|EMBL:EUC47168.1};
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:EUC47168.1};
RN [1] {ECO:0000313|EMBL:EUC47168.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 44560 {ECO:0000313|EMBL:EUC47168.1};
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI963956; EUC47168.1; -; Genomic_DNA.
DR RefSeq; XP_007686365.1; XM_007688175.1.
DR AlphaFoldDB; W6ZBK6; -.
DR STRING; 930090.W6ZBK6; -.
DR GeneID; 19127765; -.
DR KEGG; bor:COCMIDRAFT_90841; -.
DR eggNOG; ENOG502QV54; Eukaryota.
DR HOGENOM; CLU_002540_2_2_1; -.
DR OrthoDB; 3714838at2759; -.
DR Proteomes; UP000054032; Unassembled WGS sequence.
DR GO; GO:0004650; F:polygalacturonase activity; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR InterPro; IPR024535; Pectate_lyase_SF_prot.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR039279; QRT3-like.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR PANTHER; PTHR33928:SF2; PECTATE LYASE SUPERFAMILY PROTEIN DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR33928; POLYGALACTURONASE QRT3; 1.
DR Pfam; PF12708; Pectate_lyase_3; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 2.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:EUC47168.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..788
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004886835"
FT DOMAIN 687..722
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 788 AA; 83977 MW; B0870694A419D9D3 CRC64;
MRFSSLLACL GAVGIHAAAI PFERRLDNTT DSSGSVDAVQ AAAAIDGYWL NDLSGKGRAP
FNSNPNYKVF RNVKDYGAKG DGVTDDSDAF NRAISDGSRC GPWVCDSSTD SPAVVYVPSG
TYLINKPIIF YYMTALIGNP RELPVLKAAS SLQALALIDG SPYSNQNGEP GWISTNLFLR
QIRNLIIDGT AVAPTSGFQA IHWPASQATT IQNVKIRMTQ ASNSVHAGIF VENGSGGHMA
DLDITGGLYG MNIGNQQFTM RNVKISKAVV GISQIWNWGW LYSGLQISDC GTAFSMGNGG
SAGKQEVGSA VIIDSEITNC QKFVDSAWSQ TSNPTGSGQL VIENIKLTNV PAAVVSNGAT
VLAGGSLTIQ TWGQGNKYAP NASGPSKFQG AISGATRPTG LLQNGKFYSK SKPQYETLST
SSFISARGAG ATGDGVTDDT RAVQAAVTQA ASQNKVLFFE HGVYKVTNTI YVPPGSRLVG
EIFSAIMGSG STFGDQANPV PIIQIGKPGE SGSIEWSDMI VQTQGATPGA IVIQYNLNTA
LGSGLWDVHT RIGGAKGTNL QVAQCPAVLG QVKPECFSAH TNVHVTKGAN GAYFENNWFW
TADHDLDDAD STRINIYTGR GFHVEANNVW IWANGAEHHT MYQYQFNTAQ NIFAGYIQTE
TPYFQPTPIA PLPYVSSSKY SDPVYASSQT SAWGLRLLDA KNVLIYGGGL YSFFDNYNVG
CSSPTAPNGF RDCQTRILSI EGSSSVQAFG FSEVGVEWMV TAAGQDKANW KDNLSVYPTT
IGYLSYGF
//
