ID A0A1J7HBU3_LUPAN Unreviewed; 920 AA.
AC A0A1J7HBU3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA repair protein RAD16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=TanjilG_19700 {ECO:0000313|EMBL:OIV99204.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV99204.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV99204.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV99204.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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DR EMBL; CM007373; OIV99204.1; -; Genomic_DNA.
DR RefSeq; XP_019413600.1; XM_019558055.1.
DR AlphaFoldDB; A0A1J7HBU3; -.
DR STRING; 3871.A0A1J7HBU3; -.
DR EnsemblPlants; OIV99204; OIV99204; TanjilG_19700.
DR GeneID; 109325605; -.
DR Gramene; OIV99204; OIV99204; TanjilG_19700.
DR KEGG; lang:109325605; -.
DR OMA; YFCKQCD; -.
DR OrthoDB; 11932at2759; -.
DR Proteomes; UP000188354; Chromosome LG13.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProt.
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; IPR027370; Znf-RING_euk.
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; PF13445; zf-RING_UBOX; 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:UP000188354};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 221..495
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 666..706
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 746..910
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..52
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 104596 MW; F59FF41D00D004F5 CRC64;
MELRSHRRRL SESSLSGTGK EKQPRDGIGE DETNSKCSND TNEHVHDISS DSDFNCEDEE
FGVNFIPDLN EEPISSISVS DGEDILSDSY DAIEPLLNSG KSQSRRKRKK SGFGEPSDGD
RVVENGDDEE HLMVFQQSAP INLTKTKKKK KGKRTRKEDS KPVLLWHAWE EQQEKWVDEN
LLEDFDIDHQ SEVMNETVEP SSDLIMPLLR YQKEWLAWAL KQESSVTKGG ILADEMGMGK
TIQAIALVLA KREFHQMSCE ADEPSSSPGS STVLPAIKGT LVICPVVAVT QWVSEIDRFT
LKGSTKVLVY HGAKREKSGE QFSEYDFVIT TYSIVESEYR KHMMPPKEEC QYCGKLFNPR
SLTSHQRYFC GPGATRTDKQ AKQIKKKKRD LTKKKLKELK SWDEELEKGF MKKKNLELRS
RTKDSDTKDR DKSFLHAVKW QRIILDEAHY IKSRHSNTAK AVLALESSYR WALSGTPLQN
RVGELYSLVR FLQIIPYSYY LCKDCDCKIL DHSSSRQCSN CNHSTVRHFC WWNKYVATPI
QSYGYGDCGR RAMILLKHKV LKNIVLRRTK IGRAADLALP PRIVSLRKDS LDIKEQDYYE
SLYNESQSQF NTYVEANTLM NNYAHIFDLL TRLRQAVDHP YLVVYSPTAA LRGGNLAGNG
TVEQECGLCH DQVEDPVVTS CEHVFCKSCL IDFSTSLGRV SCPSCSKLLT VDLTSNMVAG
VHANKTTIKG FRSSSILNRI QLENFQTSTK IEALREEIRF MVERDGSAKG IVFSQYTSFL
DLINYALNKS GVSCVQLNGQ MSLPARDAAI KRFIDNPECR IFLMSLKAGG VALNLTVASH
VFLMDPWWNP AVERQAQDRI HRIGQYKPIR IVRFVIENTI EERILKLQEK KELVFEGTIG
GSSEALGKLT EADLKFLFVT
//
