ID K1WN82_MARBU Unreviewed; 1308 AA.
AC K1WN82;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=SWI/SNF family DNA-dependent ATPase Ris1 {ECO:0000313|EMBL:EKD14371.1};
GN ORFNames=MBM_07601 {ECO:0000313|EMBL:EKD14371.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD14371.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD14371.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD14371.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; JH921446; EKD14371.1; -; Genomic_DNA.
DR RefSeq; XP_007295490.1; XM_007295428.1.
DR STRING; 1072389.K1WN82; -.
DR GeneID; 18763536; -.
DR KEGG; mbe:MBM_07601; -.
DR eggNOG; KOG1001; Eukaryota.
DR HOGENOM; CLU_000315_2_0_1; -.
DR InParanoid; K1WN82; -.
DR OMA; RNCENAF; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 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 Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF47; ATP-DEPENDENT HELICASE ULS1; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 563..753
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 922..975
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1142..1298
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 72..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 999..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1002..1020
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1044..1060
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1100
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1308 AA; 144504 MW; 8F3B00689C673A05 CRC64;
MSHPNLHSPE ITRQIEVLED EIAFQNVLFA SIDDNVQDRE QAEQDIRDEI CSLERQLKDL
KRCTSAATIT TASNYPSSQN SSQSFQAAFS SSSRKNNAIS NLDGGVDGEP AGEMNGYLGQ
GQDQWRPLAS HSLTPSTPGS DPLGNPLLTP SHTKLSARKR SHSKYLDDQL APVEGNKSRR
TSQSPFGTGP PTPSTISSGE DSFSAWQRKQ NDEATRIKRE REDAELARII QESLDNLSTS
SMQPPARSDR SAFDRLSGAH QLSSSSGSPY SSSLSQQGST YSGPSRSMTP GTKREVPRSS
MSGLSSYASS NPPSGFTRKT PADPSYTSSA FKSERPSRPI PGSYQDDSSN ASDSDIEIIP
ASAFRANGRS SRPTGNMANS YTLPSPLPKS KPLGFGNSAA DVQFLRQQAA STSNDTLQRA
MFGTHPKPQW MNAVQPSMGG GNMLSKNEIS SAYSMNDIPV YQSHGSMAMA GSPPHSNFFE
DIITRGGDSI NAVSAYLGLN DHMLDQLGYI MNDPRKNAEE IKNLLENIRP DEEVAPEDRE
GTPEGLVYPL YEHQKIALGW LKNMEVGNNK GGILADDMGL GKTISALALI LSRPSSDPAR
KTTLIVGPVA LVRQWGREFR SKILPGYRLS VFMAHGTTKS LNWDEIRTYD VVLTTYGKLG
HEYKRLQKFR DNHKLNGGMA DHNAMKKDFP FLGPKSKFYR VILDEAQCIK NKSTHAARGC
CSIAARYRFC LTGTPMMNNV QELYSLINFL RIGPYDEWTR FNSTFGILTK ADKKSKQSVL
ERDLKNAMTK LQALLKAILL RRTKKTEIDG KPIITLPPKT EEIQHVVFDE DEQAFYTALE
CKTQTQFNKF VKAGTVTKNY ANVLVLLLRL RQASCHPHLI QDFEQAPVSA SDVTLETMRE
LARGLKPDVI ARLLDSNDIF ECPVCYDPAS NPKIITPCGH DTCSECLAKI TDQAVQQNVA
AGNDAGGNAK CPTCRGDLFK EKVIDYSAFK EVHKPAIEST DDFETASDDS DDDSEYDNES
DSDTASEKDA DARGNLKGFV VSDDQDEEVD DDETASEDDD GPEVMVEKSQ SKSNDTGKGK
EKEQKHKQLK KSKGKDKGKQ PGKKQHISIA MLKKEASKSA AGRRRYMKYL RKHWVPSAKT
TKCVELLDQF QADGQKTIIF SQFVSLLDLL QVPIDEKGWK CLRYDGSMSA DARNNAVNQF
CDSRDYNIML ISLKAGNAGL NLVAASRVII LDPFWNPYIE MQAVDRAYRI GQQHSVEVHR
ILVEGTVEDR IIDLQNRKKE LVESALDENA AKSVSRLGVA ELAFLFNG
//