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Database: UniProt
Entry: K1WN82_MARBU
LinkDB: K1WN82_MARBU
Original site: K1WN82_MARBU 
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
//
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