ID A0A125PJB2_9BASI Unreviewed; 1085 AA.
AC A0A125PJB2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KWU47044.1};
GN ORFNames=RHOSPDRAFT_24157 {ECO:0000313|EMBL:KWU47044.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU47044.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU47044.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU47044.1,
RC ECO:0000313|Proteomes:UP000062823};
RG DOE Joint Genome Institute;
RA Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT Antarctica.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; KQ954465; KWU47044.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A125PJB2; -.
DR STRING; 1305733.A0A125PJB2; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000062823; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 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; IPR014905; HIRAN.
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; IPR001202; WW_dom.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF17; HELICASE-LIKE TRANSCRIPTION FACTOR; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 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; PS50020; WW_DOMAIN_2; 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 Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 410..437
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 432..646
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 815..852
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 897..1079
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 57..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..134
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 543..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1085 AA; 118958 MW; 6AB33D4D3EE08165 CRC64;
MFVFRPSLSV CLERSRERST CTRKQDESLV DAYAVLSLSS LHGAGLAGME EQYVKPKVER
DQGPVASTSR LATASSLNNS QDDEKPAIKR SPSPDRKGKG KASPDADADG HADESDAVKP
KDEEDSKPST TEDPNEEILF HTLTKANIVG LAYAGGIRTL KEGMELDLRR DPYNVADKNA
IEVRHSRGQR VGYVAKALAE KLTPLLAARK IRLAATAGPV PANTVGLAKT TMRLEIHGKR
KYINDERLDW CFPERRDKKV EAEKKKKEQQ DLERKLMDKE NEATSGSKSR GRPGQNGSSG
DGGGGGGGGG SGGGGSGGQS GGNDDEAPDS LLEMAAEMER TARPDLIGDL FKVGALDPAR
LPGHPCPPGK DDGSMRSNLL PFQRQGLAWM IRMEHPKLPK TVDDAPVQLW AKRQDLQGGT
YWLNTGTEET TRETPRLKRG GILADEMGLG KTMQTIALIC TDDTGEGVLE GGPEEPDERY
DDMTLIVCPL SVAANWTEQF QQHVGKKRLK WHMYHGEGRD LSKRELRKFD VVISTYQTLA
GSLNDGDSQR SSRASSVKNE VKNAEEDDED ALHPAKKQKV KKDSVLHSIK WRRVVLDEGH
IVKNPKAKMS RACAELKAER RWILTGTPIL NSAADLGAML SFLKLCKPFD EPEVWRQYVS
KAGDEKRAKL LRAIVLSTTL RRTKDMVDSN GKPLITLPKI TYYKHEVELE GEPLQLYREI
EAEISSSVKQ AMKSDVAKPS VTRILLLLLR LRQIACDPSL CPPDFIADMR DRKLAARIQH
DHDAAVGVTS GRPGAEQLSF LRSMVQEMTE AGADCLACGQ WAVDPRITIC QHFFCQSCIE
AAVDARSSCP YCGLHLSRDH VIAPVIERSV TPSTTRSSSV SRNGSVALSE NSAKTAALVR
LLKASAPGVK SLVFSQWTGH LDRIEAALHE EGISTCRFDG SMRQEKREEV VKSFKVPNKT
AVAGSKEDRE NPMVMLLSLQ AGALGLNLTV ASQVFMMDPY VTHSVVSWWQ PAIEAQAIDR
VNRIGQTKPV RVFQIVAKGT VEDRVLAIQA KKEALIAQAF SGHKNAAQAK AKIEITDLAS
IFGLT
//
