ID B2VRH2_PYRTR Unreviewed; 1794 AA.
AC B2VRH2;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE SubName: Full=Helicase SWR1 {ECO:0000313|EMBL:EDU39644.1};
GN ORFNames=PTRG_00206 {ECO:0000313|EMBL:EDU39644.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU39644.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS231615; EDU39644.1; -; Genomic_DNA.
DR RefSeq; XP_001930539.1; XM_001930504.1.
DR STRING; 426418.B2VRH2; -.
DR EnsemblFungi; EDU39644; EDU39644; PTRG_00206.
DR GeneID; 6340427; -.
DR eggNOG; KOG0392; Eukaryota.
DR HOGENOM; CLU_000315_1_0_1; -.
DR InParanoid; B2VRH2; -.
DR OMA; WYSDIAC; -.
DR OrthoDB; 180798at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0000228; C:nuclear chromosome; IEA:EnsemblFungi.
DR GO; GO:0005667; C:transcription regulator complex; IEA:EnsemblFungi.
DR GO; GO:0005774; C:vacuolar membrane; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:EnsemblFungi.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0015098; F:molybdate ion transmembrane transporter activity; IEA:EnsemblFungi.
DR GO; GO:0017025; F:TBP-class protein binding; IEA:EnsemblFungi.
DR GO; GO:0090414; P:molybdate ion export from vacuole; IEA:EnsemblFungi.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:EnsemblFungi.
DR GO; GO:0042790; P:nucleolar large rRNA transcription by RNA polymerase I; IEA:EnsemblFungi.
DR GO; GO:0045898; P:regulation of RNA polymerase II transcription preinitiation complex assembly; IEA:EnsemblFungi.
DR GO; GO:0006364; P:rRNA processing; IEA:EnsemblFungi.
DR CDD; cd17999; DEXHc_Mot1; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044972; Mot1.
DR InterPro; IPR044078; Mot1_ATP-bd.
DR InterPro; IPR022707; Mot1_central_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR36498; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR PANTHER; PTHR36498:SF1; TATA-BINDING PROTEIN-ASSOCIATED FACTOR 172; 1.
DR Pfam; PF12054; DUF3535; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:EDU39644.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1204..1377
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1559..1707
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 73..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1727..1754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..628
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1794 AA; 197640 MW; 2FB1018484A3CB5F CRC64;
MSATRLDRLV TLLETGSTAL IRNTAADQLA DVQKQHPDEL FNLLTRVIPY LRSKSWETRV
AAAKAIGGIA ANADKFDPNA HDQDESTKDV KSEPESNGHL KSEDSNGGPV KKEENGDAPL
PPLAQGLDLA TLDLPSILKF GKVLASLGTK EHDYKLAAMD PAERLEYQKS TLLKRLGFEG
AWVEDLTPPQ EAMPQTPGPK TPAIHRIDTN LPRSDNTNTA SSPPLGTPNG GPGLSKRQQN
ALKRKAKKNA AGGANKVQVV DFNATSRKDS TSELGDTPAR PHPIALKLEK SENGDEGDGL
NDYFSLERNG GDDDAKFVKE FKGAPVPEKS SFQTEAEEAG LEWPFERVCS YLAVELFDYT
WEVRHGAAMG LREILRIHGG GAGRRKGLSR TENDQLNQRW LNDLACRMIC IFMLDRFADF
TGDSAIAPIR ETAGQALGSL LQFMSRDNVL ATFQVLNRLI MHHDLPLDSS PLSAPWALCQ
GGMIGLRYLV ASETSEGWID SKALQLIFQN ILLERNEGVL RLSIQLWNAV VESLGSRLAA
LLEPVLDSIV PLTLTPIGVS RHPIPLNMSL LIKPSGQAMG PPPSTEPNRK SSPADGNEPA
QKRRKKSRHG KDDMSTPTPS TQSHNVDGHM ISGDLELIGA DVMIRSRTSA AQALGKAMGA
WPEESRAEAF KPRLLKSLSS TNSSTQLTAC IIIEEFGKNL AAKDVLAESF VQALLPMVEG
ERPAAYEDLV PKLQIVRTQC NSLLSIFHEA HVQNLPQIAA LVQGMPNSNH YAFGVPDAEK
LVTVQYEKLK KAMTPSSRMV AATNLETARK EVESSIQEAK DIKEERDVRI KAAAAGALVA
LNSPPKKPSP PIKAMMDSVK KEENAELQKR SAAAVAGYIV YLVNAKRTGV VNKVVGNLVK
FYCMETAETP EFAGQSHIET GILTLKKDED IRDHPDAARF AEESRAARIT KRGAREGLEQ
VVSSFGAEIF DKVPILKDLI ERPIKEAFTE ATLPAHIFNE DGVFGQEVVD ALSTLRALVG
SFHPSVRNFV KELLPLIAKA LQSKLYVLRY AAAKCFATIC SVMSVQGVTM LVESVLPTIS
DGGNVHARQG AIECIYHLIH VMEDAILPYV IFLITPVLGR MSDSDNDVRL LATTSFATLV
KLVPLESGIP DPPDLPESLL KGRDRERKFV AQMLDAKKVE PFEIPVGIKA TLRSYQQDGV
NWLAFLNRYN LHGILCDDMG LGKTLQTLCM VASDHHMRAA EFAKSGDPNF RRLPSLIVCP
PTLSGHWQQE IRQYAPFLSC VAYVGSPPIR GQHRNELDKV DIVITSYDIC RNDADILKPI
NWNYCVLDEG HLIKNSKSKT SQAVKQFQSN HRLILSGTPI QNNVLELWSL FDFLMPGFLG
TEKVFQERFA KPIAASRFAK SSSKEQERGA LAIEALHKQV LPFLLRRLKE EVLDDLPPKI
LQNYYCDLSE LQRNLFDDFT KRQGKEIQSK AGNADRESKQ HIFQALQYMK KLCNSPSLVV
KGPSNKAYEP TQQYLKKNNT TIDDIVHAPK LGALKDLLVD CGIGASDVVS DKSANANGDL
PEAVSQHRAL VFCQMKEMLD MVQHNVLEKL LPSVQFMRLD GGVEATKRQE IVNKFNTDPS
YDVLLLTTSV GGLGLNLTGA DTVIFVEHDW NPQKDIQAMD RAHRIGQKKV VNVYRIVTRG
TLEEKILNLQ RFKIDIASTV VNQQNAGLQS MQTDQILDLF NVSADSNDPA ALPAPPSNAK
DDRTGIDEND AVDATGALRE KGKKGFLDEL GELWDEKQYD EEFDLDGFLG KMKA
//
