ID A0A061HB47_BLUGR Unreviewed; 1971 AA.
AC A0A061HB47;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Bgt-4186 {ECO:0000313|EMBL:SUZ13696.1};
DE SubName: Full=RNA helicase {ECO:0000313|EMBL:EPQ61733.1};
GN ORFNames=BGT96224_4186 {ECO:0000313|EMBL:EPQ61733.1},
GN BGT96224V2_LOCUS6845 {ECO:0000313|EMBL:SUZ13696.1};
OS Blumeria graminis f. sp. tritici 96224.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Blumeria.
OX NCBI_TaxID=1268274 {ECO:0000313|EMBL:SUZ13696.1};
RN [1] {ECO:0000313|Proteomes:UP000053110}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=96224 {ECO:0000313|Proteomes:UP000053110};
RX PubMed=23852167; DOI=10.1038/ng.2704;
RA Wicker T., Oberhaensli S., Parlange F., Buchmann J.P., Shatalina M.,
RA Roffler S., Ben-David R., Dolezel J., Simkova H., Schulze-Lefert P.,
RA Spanu P.D., Bruggmann R., Amselem J., Quesneville H.,
RA Ver Loren van Themaat E., Paape T., Shimizu K.K., Keller B.;
RT "The wheat powdery mildew genome shows the unique evolution of an obligate
RT biotroph.";
RL Nat. Genet. 45:1092-1096(2013).
RN [2] {ECO:0000313|EMBL:EPQ61733.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:EPQ61733.1};
RA Oberhaensli S., Wicker T., Keller B.;
RT "The wheat powdery mildew genome reveals unique evolution of an obligate
RT biotroph.";
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:SUZ13696.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=96224 {ECO:0000313|EMBL:SUZ13696.1};
RA Quirk P.G., Krulwich T.A.;
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KE375216; EPQ61733.1; -; Genomic_DNA.
DR EMBL; UIGY01000246; SUZ13696.1; -; Genomic_DNA.
DR HOGENOM; CLU_000335_2_0_1; -.
DR OrthoDB; 57056at2759; -.
DR Proteomes; UP000053110; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProt.
DR CDD; cd18020; DEXHc_ASCC3_1; 1.
DR CDD; cd18022; DEXHc_ASCC3_2; 1.
DR CDD; cd18795; SF2_C_Ski2; 2.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041094; Brr2_helicase_PWI.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR47961; DNA POLYMERASE THETA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G05260)-RELATED; 1.
DR PANTHER; PTHR47961:SF13; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 2.
DR Pfam; PF18149; Helicase_PWI; 1.
DR Pfam; PF02889; Sec63; 2.
DR PIRSF; PIRSF039073; BRR2; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 4.
DR SUPFAM; SSF158702; Sec63 N-terminal domain-like; 2.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EPQ61733.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053110}.
FT DOMAIN 288..481
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 512..731
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1149..1324
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1354..1565
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
SQ SEQUENCE 1971 AA; 223684 MW; 9ED143E7F5377098 CRC64;
MGSSITDWRM QATAMKAAVA ELGFSTKLDR SILDIYASNF GYDNSFITYA NRNKNADPHS
EDDEDSWSSE VGEDLNLEYN HCSVTGDYDQ LWLKKKCKDI AEGLKGLSAE ELHNQIMSSI
LSEDPEEELA SALTNIIGYD HLDLIIELIA HRREIKKNHL LKPKENEVRS VKLLTKLQRL
EALEQGDYQH KTQKLLPAHS RDEPQYPHVF KTYSAGNILD SRGHKYGLPA GSETKVTAIY
EEHIIPASRV GTLGLEKKLV AVSTMDGLCK KTFKGYNNLN RMQSLVYPIA YETSENMLIC
APTGAGKTDA AMLTILHTIG QNVFPSPAEF PERTEFDVNL EDFKIVYVAP MKALAAEITQ
KMSTRLSWLG INARELTGDM HLTKKEILTT QIIVTTPEKW DVITRKSTGD TELVRKVRLL
IIDEIHMLHD DRGSVLESLV ARTQRQVEST QSLIRIVGLS ATLPNYIDAA DFLKVNRHAG
LFYFDASFRP VPLEQHFIGV KGKPNSKTSR DNIDKTTFEK VKQMRQQDHQ VMVFVHSRRD
TFNTSKMIFE KALEEMCAEL FDPTTHPEYE AAVRDIKSSR GRELRELLPK GIGIHHAGMA
RSDRNLMERL FGSGVLKVLC CTATLAWGVN LPAAAVVIKG TQVYSAQDGK FIDLGILDVL
QIFGRAGRPQ FQDTGIGMIV TSHEKLSHYL TAVTAQVPIE SRFSKHLVDN LNAEISLGTV
TSIPDAVQWL GYSFLFVRMM RNPTTYGIDW TEQSKDPNLV QRRRQLVIQA ARTLQKNQMI
IFNDVTDELR SKDIGRIASQ YYILHTSIEI FNNLMKPQAT EADIISMIAM SGEFDNIQYR
ETEEKELTNL KEDFTQCNIR DHTDSPQAKT NILLQAFISR ANIEDFALAN DSNYIAQQSA
RICRALFMIA LNRRWGHQCL ILLSLCKSIE KKVWSFQHPL HQFDLPKPIM NQLDARKTST
SIETLRDMEP AEIGSLVHNF SAGKTIRKII DSFPTISLES EIAPLNRDVL RIRLFITPDF
RWDDRYHGTS ESYWVWVENS ETFEIYHHEF FILNRKKLYD DHELEFTIPL SDPLPTQIYV
RAVSDRWLGA ETVHPISFQH LIRPETESLY TDLLNLQPLP VTALKNRDLE AIYRKKFQYF
NPMQTQIFHC LYHTSENVLL GSPTGSGKTI ASELAMWWAF REYPNSKVVY IAPMKALVRE
RVKDWSSRLT KRMNLKLVEL TGDNTPDTRT IKDANIIITT PEKWDGISRS WVTRSYVRQV
SLVIIDEIHL LGGDRGPILE IIVSRMNFIA AQSNNRIRLV GMSTACANAS DLGNWLGVNE
GLFNFRHSVR PVPLEIFIDG FPDTHGFCPL MQSMNRPAFH AIKTHSPEKP VIVFVASRRQ
TRLTAKDLIN LCGMEDNPRR FMKMPEEELQ DTLRRVKNDA LKESINFGIG LHHAGLVESD
RSLSEELFAK NKIQVLVATS TLAWGVNLPA HLVIVKGTQY FDAKIEGYRD MDLTDVLQML
GRAGRPQFDT SGIAKIFTQN AKKAFYKNFL HTGFPVESSL HNALDNHLSA EISAETIRTK
QDALDYLTWT FFFRRLHKNP SYYGLEITAE DQNTAAAQEM ANEYMISMVD KSLEQLSESK
CLELYPNGNI KTTPFGKIMS YYYLSHRTIR HFALNAKPNA SFDEVLSWMC SAAEYDELPV
RHNEDLINAE LARNLPLTTA YFDQLPMWDP HLKAFLLLQA HFSRIELPIS DYIGDQTSVL
DQAIRIVQAG IDILAEMGYF SSVVQMITLL QCIKCARWHD DHPLSILPGV EDVPTNVTGI
SQTLQEFSAA SEKTYQQMIS KLNISSYLKS QFENAASMIP NIKVDVQDVN AMKINVVLHR
LNLRRNVDGR MYAPNFPKSQ SEGYFVLVRG ANKDEIVALK RVGLTSFDSN TSNMRAIFEI
PEGGVHGSNV DILVVSDGYL AMSWSVKSVE IPDIPRPPSE TLKKAIKVLA G
//
