ID A0A1B9G296_9TREE Unreviewed; 1188 AA.
AC A0A1B9G296;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=DNA repair protein RAD5 {ECO:0000313|EMBL:OCF25140.1};
GN ORFNames=I302_04950 {ECO:0000313|EMBL:OCF25140.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF25140.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF25140.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF25140.1,
RC ECO:0000313|Proteomes:UP000092730};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Cryptococcus bestiolae CBS10118.";
RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|Proteomes:UP000092730};
RA Cuomo C., Litvintseva A., Heitman J., Chen Y., Sun S., Springer D.,
RA Dromer F., Young S., Zeng Q., Chapman S., Gujja S., Saif S., Birren B.;
RT "Evolution of pathogenesis and genome organization in the Tremellales.";
RL Submitted (DEC-2013) 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}.
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DR EMBL; KI894021; OCF25140.1; -; Genomic_DNA.
DR RefSeq; XP_019046210.1; XM_019191580.1.
DR AlphaFoldDB; A0A1B9G296; -.
DR STRING; 1296100.A0A1B9G296; -.
DR GeneID; 30209349; -.
DR VEuPathDB; FungiDB:I302_04950; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000092730; 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: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; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF22; DNA REPAIR PROTEIN RAD5; 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 Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 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 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:UP000092730};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 505..729
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 918..962
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1010..1161
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 341..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1188 AA; 132579 MW; 96E6487B3D4394D3 CRC64;
MDIDEESSIP SKRSSPDLFF PVSDSEEEED VIIASGALAG PSSSAINPPS TATSTRTNGN
SNNRKTQQSQ EVFGSQNSDD IVPLDIKPTS SNIAGPSRIK RNLSSSPPPS AIPNDFDQGY
LGEFVCEGWS LSKGKGYCSP GSKVVFERPK PKSQVEEKST IRDTKGPARL VNGKVVGAKG
KVIGGKQVTL GSMMSKKSSP ATTGKPVVDS IIRFRNDRGF VGRLSVQEAG FLTHLLDTGV
ISLTGHVIDC PLSLSTGSTI LLNVKVFLAR KAFENVEKKD ERKEEGTFWQ EQKETTEEEA
MRRRKDALGA LFSRIGVKPI RSNALLLAQK KNGAAVINET SLQHFSDSPK PKRSPSPSKG
SNGTASEKGK GKASAANSDN EEEEDEDSGD EAEKLDEKQM NEIDAIYAKA QQGDNRLEES
DPPESFLYTL RPYQKQALTW MSAREKGDES IRDNQSLHPL WEEYAFKKEH VEGQPIEIED
EDDFVDPSRK FYWNPYSGEL SLTFPTSNTR AKGGILADAM GMGKTCMMAS LIHVNIDPDI
SSTPPPTTAE DEEPALKRPK FKQVTLSNQW RAIPTIPKPT NANIPRGTLV VCPVSLASQW
HDELGKMSEK GTITSFMWYG NDRIDIDRLL SQEGKKKVDV IITSYGTLAS EYQKWKKNKD
KATYEGGSLY DHEFLRIVLD EAHNIKNRTA QVSKACYEIK GQRRWALTGT PIVNRLDDLY
SLLHFLRLEP WGHYSFFRSF VTVPFLNQDP KALNVVQYIL ESCLLRREKT MRDKDGKLIV
DLPPKTVDIQ VLDFSRPERQ IYKHLEDRAK RRFIQLDAEG RAMSNYTSIL AMLMKLRQCV
DHPLLVLGKS TEDDESTDKL LDAETGDEKE NLKDLIALYA GGAKATHKTN GEDVEEVDHA
FAERVLKELG EQETTPICDI CSNEMFDEVL LPCYHRCCQD CIVNWIGTCE DQNKPALCPS
CSKGPIKLSD LRSIQRKRKR VNPLTGIHEE GEPGVTLGKV DLVQSTKLRA LVRKLDAMRQ
DDPEVKTLVF SQFTSFLDLI ETTLTKEGVK WLRFDGSMSQ AQRAATIEEF GKKTKEPLVL
LISLKAGGVG LNLTMANHVF MMDTWWNEAI EQQAIDRVHR LGQNKHVYVT RYIIKETVEK
RIMKIQRSKT ALVNASLSGG ASKDKGASLA DIKKIFGLDE DDSEDEVY
//
