SMC6B_ARATH
ID SMC6B_ARATH Reviewed; 1057 AA.
AC Q9FII7; Q9S722;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Structural maintenance of chromosomes protein 6B;
DE AltName: Full=DNA repair protein RAD18;
DE Short=AtRAD18;
GN Name=SMC6B; Synonyms=MIM; OrderedLocusNames=At5g61460; ORFNames=MCI2.2;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY,
RP INDUCTION BY MMS, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=10449416; DOI=10.1093/emboj/18.16.4505;
RA Mengiste T., Revenkova E., Bechtold N., Paszkowski J.;
RT "An SMC-like protein is required for efficient homologous recombination in
RT Arabidopsis.";
RL EMBO J. 18:4505-4512(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10048488; DOI=10.1093/dnares/5.6.379;
RA Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT features of the regions of 1,081,958 bp covered by seventeen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:379-391(1998).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION.
RX PubMed=11069693; DOI=10.1046/j.1365-313x.2000.00867.x;
RA Hanin M., Mengiste T., Bogucki A., Paszkowski J.;
RT "Elevated levels of intrachromosomal homologous recombination in
RT Arabidopsis overexpressing the MIM gene.";
RL Plant J. 24:183-189(2000).
RN [5]
RP FUNCTION.
RX PubMed=19070688; DOI=10.1016/j.dnarep.2008.11.012;
RA Kozak J., West C.E., White C., da Costa-Nunes J.A., Angelis K.J.;
RT "Rapid repair of DNA double strand breaks in Arabidopsis thaliana is
RT dependent on proteins involved in chromosome structure maintenance.";
RL DNA Repair 8:413-419(2009).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=19737979; DOI=10.1105/tpc.108.060525;
RA Watanabe K., Pacher M., Dukowic S., Schubert V., Puchta H., Schubert I.;
RT "The STRUCTURAL MAINTENANCE OF CHROMOSOMES 5/6 complex promotes sister
RT chromatid alignment and homologous recombination after DNA damage in
RT Arabidopsis thaliana.";
RL Plant Cell 21:2688-2699(2009).
CC -!- FUNCTION: Core component of the SMC5-SMC6 complex that promotes sister
CC chromatid alignment after DNA damage and facilitates double-stranded
CC DNA breaks (DSBs) repair via homologous recombination between sister
CC chromatids. {ECO:0000269|PubMed:10449416, ECO:0000269|PubMed:11069693,
CC ECO:0000269|PubMed:19070688, ECO:0000269|PubMed:19737979}.
CC -!- SUBUNIT: Forms a heterodimer with SMC5. The SMC5-SMC6 complex is
CC composed of the SMC5 and SMC6 heterodimer attached via their hinge
CC domain and from the non-SMC subunit NSE4A or NSE4B (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC Note=Associates with chromatin. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, rosette leaves and floral
CC buds. {ECO:0000269|PubMed:10449416, ECO:0000269|PubMed:19737979}.
CC -!- INDUCTION: By methyl methanesulfonate (MMS) treatment.
CC {ECO:0000269|PubMed:10449416}.
CC -!- DOMAIN: The flexible hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC6, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Delayed root growth in seedlings.
CC Hypersensitivity to genotoxic stress such as UV-C, X-rays, methyl
CC methanesulfonate (MMS) and mitomycin C (MMC).
CC {ECO:0000269|PubMed:10449416, ECO:0000269|PubMed:19737979}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD54769.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=AAD54770.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF120932; AAD54769.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF120933; AAD54770.1; ALT_SEQ; mRNA.
DR EMBL; AB016887; BAB10445.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97471.1; -; Genomic_DNA.
DR RefSeq; NP_200954.1; NM_125539.2.
DR AlphaFoldDB; Q9FII7; -.
DR SMR; Q9FII7; -.
DR STRING; 3702.AT5G61460.1; -.
DR iPTMnet; Q9FII7; -.
DR PaxDb; Q9FII7; -.
DR PRIDE; Q9FII7; -.
DR ProteomicsDB; 232564; -.
DR EnsemblPlants; AT5G61460.1; AT5G61460.1; AT5G61460.
DR GeneID; 836267; -.
DR Gramene; AT5G61460.1; AT5G61460.1; AT5G61460.
DR KEGG; ath:AT5G61460; -.
DR Araport; AT5G61460; -.
DR TAIR; locus:2161163; AT5G61460.
DR eggNOG; KOG0250; Eukaryota.
DR HOGENOM; CLU_009063_1_0_1; -.
DR InParanoid; Q9FII7; -.
DR OMA; MCHDHFY; -.
DR OrthoDB; 263113at2759; -.
DR PhylomeDB; Q9FII7; -.
DR PRO; PR:Q9FII7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FII7; baseline and differential.
DR Genevisible; Q9FII7; AT.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:TAIR.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:TAIR.
DR GO; GO:0010165; P:response to X-ray; IMP:TAIR.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:TAIR.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR027132; SMC6.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR19306:SF9; PTHR19306:SF9; 1.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chromosome; Coiled coil; DNA damage; DNA recombination;
KW DNA repair; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1057
FT /note="Structural maintenance of chromosomes protein 6B"
FT /id="PRO_0000424413"
FT DOMAIN 22..1047
FT /note="Zinc-hook"
FT REGION 449..632
FT /note="Flexible hinge"
FT REGION 818..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..448
FT /evidence="ECO:0000255"
FT COILED 633..904
FT /evidence="ECO:0000255"
FT COMPBIAS 818..832
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49..56
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1057 AA; 121779 MW; 0A7C5732B7B98F68 CRC64;
MVKSGARASD SFIKQRSGSG SILRIKVENF MCHSNLQIEF GEWVNFITGQ NGSGKSAILT
ALCVAFGCRA RGTQRAATLK DFIKTGCSYA VVQVEMKNSG EDAFKPEIYG GVIIIERRIT
ESATATVLKD YLGKKVSNKR DELRELVEHF NIDVENPCVV MSQDKSREFL HSGNDKDKFK
FFFKATLLQQ VNDLLQSIYE HLTKATAIVD ELENTIKPIE KEISELRGKI KNMEQVEEIA
QRLQQLKKKL AWSWVYDVDR QLQEQTEKIV KLKERIPTCQ AKIDWELGKV ESLRDTLTKK
KAQVACLMDE STAMKREIES FHQSAKTAVR EKIALQEEFN HKCNYVQKIK DRVRRLERQV
GDINEQTMKN TQAEQSEIEE KLKYLEQEVE KVETLRSRLK EEENCFLEKA FEGRKKMEHI
EDMIKNHQKR QRFITSNIND LKKHQTNKVT AFGGDRVINL LQAIERNHRR FRKPPIGPIG
SHVTLVNGNK WASSVEQALG TLLNAFIVTD HKDSLTLRGC ANEANYRNLK IIIYDFSRPR
LNIPRHMVPQ TEHPTIFSVI DSDNPTVLNV LVDQSGVERQ VLAENYEEGK AVAFGKRLSN
LKEVYTLDGY KMFFRGPVQT TLPPLSRRPS RLCASFDDQI KDLEIEASKE QNEINQCMRR
KREAEENLEE LELKVRQLKK HRSQAEKVLT TKELEMHDLK NTVAAEIEAL PSSSVNELQR
EIMKDLEEID EKEAFLEKLQ NCLKEAELKA NKLTALFENM RESAKGEIDA FEEAENELKK
IEKDLQSAEA EKIHYENIMK NKVLPDIKNA EANYEELKNK RKESDQKASE ICPESEIESL
GPWDGSTPEQ LSAQITRMNQ RLHRENQQFS ESIDDLRMMY ESLERKIAKK RKSYQDHREK
LMACKNALDS RWAKFQRNAS LLRRQLTWQF NAHLGKKGIS GHIKVSYENK TLSIEVKMPQ
DATSNVVRDT KGLSGGERSF STLCFALALH EMTEAPFRAM DEFDVFMDAV SRKISLDALV
DFAIGEGSQW MFITPHDISM VKSHERIKKQ QMAAPRS
