ID A0A3Q7HED3_SOLLC Unreviewed; 930 AA.
AC A0A3Q7HED3;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA repair protein RAD16 {ECO:0008006|Google:ProtNLM};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081 {ECO:0000313|EnsemblPlants:Solyc07g052100.3.1};
RN [1] {ECO:0000313|EnsemblPlants:Solyc07g052100.3.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc07g052100.3.1};
RX PubMed=22660326; DOI=10.1038/nature11119;
RG Tomato Genome Consortium;
RT "The tomato genome sequence provides insights into fleshy fruit
RT evolution.";
RL Nature 485:635-641(2012).
RN [2] {ECO:0000313|EnsemblPlants:Solyc07g052100.3.1}
RP IDENTIFICATION.
RC STRAIN=cv. Heinz 1706 {ECO:0000313|EnsemblPlants:Solyc07g052100.3.1};
RG EnsemblPlants;
RL Submitted (JAN-2019) 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 AlphaFoldDB; A0A3Q7HED3; -.
DR STRING; 4081.A0A3Q7HED3; -.
DR PaxDb; 4081-Solyc07g052100-2-1; -.
DR EnsemblPlants; Solyc07g052100.3.1; Solyc07g052100.3.1; Solyc07g052100.3.
DR Gramene; Solyc07g052100.3.1; Solyc07g052100.3.1; Solyc07g052100.3.
DR InParanoid; A0A3Q7HED3; -.
DR OMA; LANNKYS; -.
DR Proteomes; UP000004994; Chromosome 7.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
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:SF33; 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; 2.
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:UP000004994};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 119..431
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 599..661
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 732..896
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 314..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 930 AA; 105875 MW; 3E2DCE57DF768DDD CRC64;
MSADSMHNPS LNEEVVHTAE VFNAVKQEQM DVVTEKEWEY RALKARIEER KKDRKKKQED
RPTLMWETWE ETYDKWLVKH FADDLDNQNE LLCETVEPSS DMIVPLFRYQ KEWLFWALKQ
EESSSKGGIL ADEMGMGKTI QAIALVLAKR ELGKTISKPS LLSSSSSTNK QEPSAVKGTL
ILCPMVAVLQ WVTEINRCTI EGSNKILVYH GSNRRKLSRD IEEYDFVITT YSTVEAEYRK
FVMQPKQKCE WCGKAYYEEK LPIHQKSFCG PDGVKTAKQS KKQRKKLKLD EELLMQKTDS
TESETYLQIT DFMESETNVQ EEGSTAETDM KKTGRRKYMK RSSMAEEGKN DGSMDTSSSV
NQDLPQRKSI LHSVKWDRII LDEAHYVKDR RCNTTKATLS LKSSYKWALS GTPIQNLVGE
LYSLVRFLQI VPYSFYFCKD CDCRTLDYSS TSECPQCPHK SVRHFCFWNR YIATPIKREG
SYGSGRDAMF LLKHKILKSI LLRRSKKGRA ADLALPLKIV TLRKDSLDVI EEDYYTSLYN
KSQAQFNTYV KGGTVMNNYA HIFELLTRLR QAVDHPYLVV YSSTALAKMA NSGNVEQPCG
LCHDAVEDPA KPLEVHEYLG EHFPGAPKTF FPVTSCMHVF CKTCLIDFAA SARQVPCPLC
SELLTIDFTV NTDKVDQNSK QTLKGFRSSS ILNRIQLDDF QSSTKIDALH AGTSSCKGSE
PLLIIVGLTV ILITESAYDA REEIRFMIER DGSAKGIVFS QFTSFLDLIH YSLQKSGINC
VQLVGSMSID ARAAAVTKFT EDSDCRIFLM SLKAGSVALN LTVASQVFMM DPWWNPAVER
QAQDRIHRIG QYKPVRIVRF VIENTVEEKI LKLQEKKELV FEGTIGGSSE AFAKLTEADL
KFLKCRFCIT IIAYDLCITI IAYDLGRVSV
//
