ID A0A0D2FVT0_9EURO Unreviewed; 1133 AA.
AC A0A0D2FVT0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=SWI/SNF family DNA-dependent ATPase Ris1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV04_02851 {ECO:0000313|EMBL:KIW70595.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW70595.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW70595.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW70595.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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; KN846957; KIW70595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D2FVT0; -.
DR STRING; 5601.A0A0D2FVT0; -.
DR HOGENOM; CLU_000315_2_0_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000054266; 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: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; cd16449; RING-HC; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF24; 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; PF13920; zf-C3HC4_3; 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; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 411..599
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 761..805
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 938..1112
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 58..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1085
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..855
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1133 AA; 127487 MW; A9B29796C485379B CRC64;
MDGPSDPALL AEIEDLRDEI ALKEAILESL DDNGNGSEDE ELRKTAKKEL KRLRKHLRVL
QPASEDEEDN LDPSQALGQT PELTPDYRSV SRPPQPAYRS DHLSPSTRYD PVSRKRQRAL
SDDERQESFK SRRTTPNSAL TAPSPPATSA SLDSLDDPFL DSLFGGLSKE ELEHNQEFWR
QKQQEENDEK IALSLSQEWG GGMTTEPTQP TLPYRSDYTQ SFLRANGSFV KSEPSSSTSR
STGIKADPAN AYVSPSRLLE NPTTLGVPVK HEQPGRVPFN VKHEPGMGPS LSVPGAFPGA
LPQNQSYDSL GGLSVYNSQG GAGPGPDSLD RYARPHGQLD PDSESGALPM AFERSLDGSR
EHAQTQAELR QLLQHIRPDE ELTADQMPEQ PQGLKVSLMP HQLSGLAWMK RMEEGTNKGG
ILADDMGLGK TLQSIALMLE RPPPENKHRP TLVVAPVALM HQWRREFEKM VRPRYRMNIF
VLHGETRKAT WSSLRAYDVI LTTYGLLASE LKRKAVLDEK AKRLQNYVPT PAEDCPVLGD
RSHFHRVILD EAHNIKNRGT KAAHAAYRIQ AEYRWCLTGT PMMNETEELF SLVKFCRIRP
YCEWERFRRD IAAPLKRRHE VQQERGMATL QALLRAILLR RTKQSNIHGR PILQLPPRET
TEDRVAFGED QREFYFALES NAQIQMNRYL QRGTVGRHYA NILVLLLRLR QAACHPFLVT
ASKDFVQLPG GELSTDVLMR NAAQLDIKVV ERLKQLDAYE CPICFDVTEN PSLFFCGHAI
CGDCLSRLTE DGNNNGGRPK CPQCRADIDV NNVTDYTSFL RIHCPEHDSL QGLDLERESD
SDSDSDSDSE SDGGDEGADL GGFIVYDTDP DDDSGSRKPA RRRKKSKKRS EPKSQARQKP
PPKSLGQLRK EGIRNKSARR RYLRRLKKTF QPSAKTIRTL ELLEEIKDRG EGEKTIVFSN
FTSFLDIVET TLYDHKTLGN YVRYDGSMSS NERNDAVLEF TENPNCGVIL VSLRSGNAGL
NLTAANHVIM LDPFWNPFVE YQAADRCYRI GQQRPVTVHR ILIGQGEPED ENPLTGNGAP
RDPSVGYTVE DRILNLQEKK RRLVETALDE TAGRQVSRLG VRELGYLFGL NSL
//
