ID A0A109FH72_9BASI Unreviewed; 1331 AA.
AC A0A109FH72;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KWU44413.1};
DE Flags: Fragment;
GN ORFNames=RHOSPDRAFT_18100 {ECO:0000313|EMBL:KWU44413.1};
OS Rhodotorula sp. JG-1b.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU44413.1, ECO:0000313|Proteomes:UP000062823};
RN [1] {ECO:0000313|EMBL:KWU44413.1, ECO:0000313|Proteomes:UP000062823}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JG-1b {ECO:0000313|EMBL:KWU44413.1,
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.
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DR EMBL; KQ954479; KWU44413.1; -; Genomic_DNA.
DR STRING; 1305733.A0A109FH72; -.
DR OrthoDB; 5482994at2759; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18665; CD1_tandem_CHD1_yeast_like; 1.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 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; IPR041150; Cdh1_DBD.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_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 PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF18196; Cdh1_DBD_1; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 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 Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 97..153
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 191..258
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 297..465
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 590..746
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 865..913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1122..1205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 959..986
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 884..913
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KWU44413.1"
SQ SEQUENCE 1331 AA; 150766 MW; 47E726EF2569C7E7 CRC64;
DSDDSEDDGD YVQNKKKHGS KRRKTAPKRT QRDFEMPRFS SRNGKALPNY NEADMFSDLS
GSDDGFSYGV DEEDQRAFLR SLALGEQHPE DGVDGVFAHK RMEGHEEDEK DEPKRNMLFL
VKWQNYSHIH DTWEPYERLK RFRGLKRVDN YIKSVLFAQN KRLKDPTLSR EDLEALHLEK
ERQAEQLELY KQVERIIAQR DAPANEEIDH DHVEYLCKWK ALQYSDSTWE AHDTVHQIAA
NEIEEYLQRV ANPRLPAKSA SYSRNRPTFK KLTAEPDYIT PCGTLKDFQM TGLNWLAYLW
SKGDNGILAD EMGLGKTVQS CSFLSYLYHE HQQYGPFLVV VPLSTLPAWQ MQLAQWAPDL
NTIAYNGTAA SRAIIRDYEF GSLKKPAFNV LLTTYEFVLK DKADLGQIKW QYLMVDEAHR
LKNSESALYE ALASFHAAAK LLITGTPLQN NVKELLALMH FLHPERFELA GDFDLNDEEN
EAKIRDLHGK LESIMLRRLK RDVIKELPTK SERILRVEMS NMQTWWYKNI LTRNYAALSG
ADQQVSLLNI AMELKKASNH PYLFEGAEPR TESREETLKG LVMNSGKMVL LDKLLSRLKQ
DGHRVLVFSQ MVRMLDILSD FCTMRNYLHQ RLDGTVPSEL RRKAIGHFNA PDSPDFVFLL
STRAGGLGIN LETADTVIIF DSDWNPQNDL QAMARAHRIG QKSHVNVYRF VTKDTVEEDV
LERARKKMIL EYAIVNQMDT SGKNIGQAQS ATRPENYTKE ELASILKFGA ANIFKSEGGQ
AKLEEMDLDD VINQAEEYET ATAPTGTSLG GEEFLNQFAV QDVKADMSSW EDIIPAEDRE
RVQAEIAEQE KAAAALESSR RAAAQVAPGA YGGQSGGLAS RDSSPASEKE DSKEPKKPAA
PRKTDAQRSM ELKERDLRNL VRGLQRFGDI RHRYDSIVKD ARLESKNRTV VTQAVDDLLK
ICKEELQKKH DTLERMKANN EEITNKFRNQ AVLVTFRGIN NINAETTVQR AEELKILHSH
LHKAPNALKW ELPLDNVKAT SAWNCEWSNE DDAHLLVGVW KYGHGNWEPI REDPSLGLAD
KLFLEDAKVK PGSGEKPRLP NAIHLVRRAD YLLHALRELD HSKRSEQSGV ASTSKTHQPR
AGGHRPKGSS ERASEGASSA APSGSRLKST TSKSAASKPP KRKATPQYSS SEDSGSGYDS
MDEEACKEAL RPVKRELKRL KSGTDGLSRE EKVTHLKETL SAIGARIEVI AAAEKTPALQ
EQRRKHLCEC LRWPTLSARA QHKTDDAFYL VCVQGNGRLI SGRRTGSPPY SCARCLSSSP
RSRTRPCLRL R
//
