ID A0A1B9FTR2_9TREE Unreviewed; 1143 AA.
AC A0A1B9FTR2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=DNA repair protein RAD16 {ECO:0000313|EMBL:OCF22159.1};
GN ORFNames=I302_07803 {ECO:0000313|EMBL:OCF22159.1};
OS Kwoniella bestiolae CBS 10118.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Kwoniella.
OX NCBI_TaxID=1296100 {ECO:0000313|EMBL:OCF22159.1, ECO:0000313|Proteomes:UP000092730};
RN [1] {ECO:0000313|EMBL:OCF22159.1, ECO:0000313|Proteomes:UP000092730}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 10118 {ECO:0000313|EMBL:OCF22159.1,
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; KI894025; OCF22159.1; -; Genomic_DNA.
DR RefSeq; XP_019043229.1; XM_019194393.1.
DR AlphaFoldDB; A0A1B9FTR2; -.
DR STRING; 1296100.A0A1B9FTR2; -.
DR GeneID; 30212202; -.
DR VEuPathDB; FungiDB:I302_07803; -.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal 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; 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; 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:SF12; DNA REPAIR PROTEIN RAD16; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000092730};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 532..704
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 873..917
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 956..1109
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..254
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..384
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1143 AA; 127262 MW; F9ADBD5DD36698D3 CRC64;
MPPRRSARQS LPTPAHSTTS STPGKKEVVA NGVSSTSQAK TSKSNVQPET PTSLEDEDAL
ALTLGDEASD DGIVDYGVKE ESPESPFTST TTSATSSSSK RYRLDSVTLP SRRSKLGLDK
TDSADNMTLD SPSNGRGQAN GNGSVKMELE DVEMKDEQEQ QEDIKPPTTT TTTSRSRKGK
SKVDPTEQAP FNIGKFSSVS KAQVSDLALS PLETKSARGR LPRASKGKAK KEMTPPLTDE
ETEYDAEAGY AMDSEEEENQ LKRAIKASTQ KSKTSTRSRS NPSSGTATPT KGARKSTGNQ
TALRAAVAKA AEKRLTKNGK STPSTRGNTS AGDITPRSVG SNAATDITPL SDDDSGLSTV
LSDISADEAQ ITDSEDDMSE SEYDSDDSLA LQSKKKKGRF AGKGRSLADG KTYEELADEL
GSEGEGLDPD EMRKMSIKKM RDKARSERRK ADADAAPRKK KERELSKKLG RKLTNGEKNL
VALSMNHPEL EDVWGDLQAN VEPVKPVTME AHKSLKLTLL PFQKESLYWM KKQEEGPWKG
GMLADEMGMG KTIQTIALLL SEPRRKPSLV VAPVVALMQW KHEIETHAEG FTVCLWHGQQ
RMKAAELKKY DVVLSSYGTL EAAFRRQQRG FKRGNNFIKE KSPMHEFEWY RVILDEAHNI
KERSTNAAKA AFALHATYKW CLSGTPLQNR VGELYSLVRF LGADPFSHYF CKKCDCKSLH
WQFKDKRTCD QCGHTPMAHV CFWNTEILTP IARYGIEEGG PGHTAFKKLK ILLDRMMLRR
TKLERADDLG LPPRTIVVRR DFFSPAEKEL YMSLFTTAKR QFSTYVGQGT VLNNYSNIFS
LITRMRQMAC HPDLVLRGKT SALVTDAPEG TVCRLCNDTA EDAIMSQCHH VFDRECIRQY
LEVKQARGHK PECPVCHIEI SIDLEAEALD LEDNNKKARQ GILSRLDLQN WRSSSKLEAL
VEELEKLRNK DCTIKSLVFS QFVSFLDLIA FRLQRAGFNI CRLEGGMTPQ QRDATIQHFM
NNTHVTVFLI SLKAGGVALN LTEASMVFMM DSWWNPSVEY QAMDRIHRLG QKRPVKVVKL
VIEDSIEDQI VQLQHKKLAM TEAALNKDPD AALGKLTVED VSFLLGFALS TFSFLFFRCR
DVS
//
