ID A0A1S3U8F5_VIGRR Unreviewed; 927 AA.
AC A0A1S3U8F5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=DNA repair protein RAD16 isoform X1 {ECO:0000313|RefSeq:XP_014502305.1};
GN Name=LOC106762762 {ECO:0000313|RefSeq:XP_014502305.1};
OS Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3916 {ECO:0000313|Proteomes:UP000087766, ECO:0000313|RefSeq:XP_014502305.1};
RN [1] {ECO:0000313|RefSeq:XP_014502305.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_014502305.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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DR RefSeq; XP_014502305.1; XM_014646819.2.
DR STRING; 3916.A0A1S3U8F5; -.
DR GeneID; 106762762; -.
DR KEGG; vra:106762762; -.
DR OrthoDB; 11932at2759; -.
DR Proteomes; UP000087766; Chromosome 5.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
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 InterPro; IPR017907; Znf_RING_CS.
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; 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:UP000087766};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 232..502
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 673..714
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 753..917
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 927 AA; 104603 MW; 7790358868A3182E CRC64;
MELRSRRRLS NPAVSGTINC SGNEQQPKDD TVVEDETKGR SNNNKDKGVS VMLSDSDVVS
GSDSDSDYED EELAGGSLLD LNKYPFSTIS FSDGEDYGSD SSDGDIPLFK KAKVPGSRER
RKSTNTEKGE PSDVVRVVDH EYSMISPVLV PSGFKGTKKR KYTKKGSKGD SRPVLLWNAW
EEEQEKWIDQ HISEDFDLDN QSEVMNETAE APSDLTMPLL RYQREWLAWA LKQEHSSSRG
GILADEMGMG KTIQAIALVL AKREFQDSCE PDQSIPCSSN LLPPIKGTLV ICPVVAVTQW
VSEIDRFTLK GSTKVLVYHG ANRGRSGDRF ADYDFVITTY SVVENEYRKH MMPPKERCPY
CGKLFLPSKL MYHQSYFCGP DAVRTEKQSK QVKKKREVTK GKTKECESSK ILKGSIKKKG
DKMCIDMEDS DAVPVRSDRS FLHAVKWQRI ILDEAHYIKS RHCNTAKAVL ALDSTYKWAL
SGTPLQNRVG ELYSLIRFLQ ITPYSYYLCK DCDCRILDHS SKECSVCTHS SVRHFCWWNK
YVATPIQSFG NGDSGKRAMI LLKHKVLKNI VLRRTKIGRA ADLALPPRIV SLRXDCLDIK
EQDYYESLYN ESQAQFNTYI EANTLMHNYA HIFDLLTRLR QAVDHPYLVV YSQSSGSRSA
VMANNATTVE QICGICHEPV EDLVVTSCEH SFCRACLIDY YSTSLGQVSC PACSKLLTVD
LTSNKDAGDQ VKTTIKGFRS SSILNRIRLE NFQTSTKIEA LREEIRFMVE RDGSAKGIVF
SQFTSFLDLI NYSLHKSGVS CVQLNGSMSL NARDAAIRRF TEDPDCKIFL MSLKAGGVAL
NLTVASHVFL MDPWWNPAVE RQAQDRIHRI GQYKPIRIVR FVIENTIEER ILKLQEKKEL
VFEGTIGGSS DALGKLTEAD LRFLFVT
//
