ID A0A1J7HYC3_LUPAN Unreviewed; 945 AA.
AC A0A1J7HYC3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OIW06805.1};
GN ORFNames=TanjilG_11530 {ECO:0000313|EMBL:OIW06805.1};
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:OIW06805.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIW06805.1, 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:OIW06805.1};
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; CM007368; OIW06805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7HYC3; -.
DR STRING; 3871.A0A1J7HYC3; -.
DR EnsemblPlants; OIW06805; OIW06805; TanjilG_11530.
DR Gramene; OIW06805; OIW06805; TanjilG_11530.
DR OMA; CHPHLIN; -.
DR Proteomes; UP000188354; Chromosome LG08.
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; 3.
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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 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; PF13923; zf-C3HC4_2; 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 207..483
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 637..673
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 772..940
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 945 AA; 105470 MW; 1DA6BBAF052E18BB CRC64;
MDNYICLSSS DDDLEEIEDP RRSLPQWAAP ERNSDNGGWS KKGNSSGGAN TSNTTSNVNS
HSQIRPHTQP SSSNNSLNHR VSQRDEPSYR TQNGNSGQHH TVNSRISNAS GSDYDKMSSQ
EAFKRTLPLS LQSSITKALS SSSFAPDIRA SSSKDHMSSS HFHDTYNSRR HGDLYRSKTE
TDLPDGLMSV PLLRHQKIGL AWMLQKENRS LHCLGGILAD DQGLGKTISM IALILMQRSL
QSKSRTDDAF NHKTEALNLD DDDDDNGIVD VDKIKKNEEA DDINPITEPS SSIRAPSRKR
PAAGTLVVCP ASVVRQWARE LDEKVGNEKL SALIYHGGSR TKNPDELATY DVVITTYAIV
TNEVPKQPLV DEDESDEKNG ERFGLSSEFS ASKKRKKTYN GNKKSRKGRK GIDSSLDCGS
GPLAKVGWFR VILDEAQTIK NHRTQVARAC CSLRAKRRWC LSGTPIQNTI DDLYSYFRFL
RYDPYAVYKS FYNTIKVPIS RNAVQGYKKL QAVLRAIMLR RTKGTLIDGQ PIINLPPKTI
ELSKVDFSSE ERAFYTKLEA DSRSQFKAYA AAGTVNQNYA NILLMLLRLR QACDHPLLVK
DYNSNPVGQD SIEMAKRLPR DLLINLFKEL DTTSAICHVC NDPPEDPVIT MCSHVFCYQC
VSDFLTADDN TCPATYCKET VGEDVVFSKA TLRSCISDDL GGSSSSNSHH VDYSLFQDSE
YNSSKIKAVL EILMSNRKMK APTYGSPNSC GGRGDLLSSD ISFIEDCDSD VQVTKHTKKY
SEPTTEGPIK AIIFSQWTSM LDLVEDALKQ SRIRIRYRRL DGRMTLLARD KAVKDFNTDP
EVTVMLMSLK AGNLGLNMVA ACQVILLDLW WNPTTEDQAV DRAHRIGQTR PVTVTRLTIK
DTVEDRILAL QEEKRKMVAS AFGEDHAGGT ATRLTVDDLK YLFMV
//
