ID B2W412_PYRTR Unreviewed; 916 AA.
AC B2W412;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0000313|EMBL:EDU48119.1};
GN ORFNames=PTRG_05212 {ECO:0000313|EMBL:EDU48119.1};
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:EDU48119.1, 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}.
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; DS231618; EDU48119.1; -; Genomic_DNA.
DR RefSeq; XP_001935545.1; XM_001935510.1.
DR AlphaFoldDB; B2W412; -.
DR STRING; 426418.B2W412; -.
DR EnsemblFungi; EDU48119; EDU48119; PTRG_05212.
DR GeneID; 6343462; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_17_3_1; -.
DR InParanoid; B2W412; -.
DR OMA; PNIFTDW; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18009; DEXHc_HELLS_SMARCA6; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
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; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR044753; HELLS_N.
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; PTHR10799:SF923; PASG; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00384; AT_hook; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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 Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT DOMAIN 245..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 672..845
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 801..889
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..564
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..598
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 103651 MW; 00F7627461C2F81A CRC64;
MPASSITGAA SETKSTPASS PPPADMDTKN VPESLQAEEE RIRAQREKDD AKRDAQLEKE
RQEDIKSGRE VLDKKFQQLE FLMNKSKLYA TVMLAQMQRQ EEEEQAQDEK TKGQTTKREK
NAEKTAAESQ RRATRGSAAS APKTDEPETT PKRGRGRPKK QDNKGNAKLK KQGSDISSYF
SKADLEKKTD HKNVGDALKE AAEEDKDNVK TSDIGMTDLK SARQPKLVTG GTMRSYQLEG
LEWMVSLYNN GINGILADEM GLGKTIQTIA MLAHLWENKS YGPFLIAAPL STTSNWVAEF
EKWTPTLPVM LYHGDKKERE RLRKTRLRNP GTADFPIMIT SYEICMNDRK YLTSFGWQFI
IIDEGHRIKN LDCRLIRELQ QFQSANRLLI TGTPLQNNLT ELWSLLHFLL PTVFDKLSTF
ESWFDFSGLK DKSSFEQLLS EERQQYLVKS LHAVLKPFLL RRVKTDVESL MPKKREYVLY
APLTAMQREL YQAILDGTSR SYLEEKAVER LSIGLSSRAG TPLSIRSNNG GLKRKALSRL
NTPSKSAKTS RAGTPASVAS TRSRGRPKKN YEEVSDNEFF DNMDKPEEEE EEEELSSDAE
DEKIRAATFE IAKRQLMQKK LGNPIMQLRL CCNSPYNFFN PFIKADTDGT ETFASETEPD
ETIVSTSGKM LLLDSLLPEL IRRGHKVLIF SQFTTTLDLL GHYLDLRSWN YARIDGSVAQ
TDRQEQILAF NKPSTTKEAA DIFILSTRAG GQGINLAAAD TVILFDSDWN PQQDLQAMDR
AHRIGQTRNV IVYRFATRNT VEQKLLESAE AKRRLEKLVI RKGGVRNDRG SGRGNDKEQE
VEELQRLLRR SDGEKFDVEG TEVGKILGEE ELEILLDRSE EAYERAERGL DIGGEGKVFQ
AVGKREEGAL MEGLRA
//
