SMC6A_ARATH
ID SMC6A_ARATH Reviewed; 1058 AA.
AC Q9FLR5; C4P4D4;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Structural maintenance of chromosomes protein 6A;
GN Name=SMC6A; OrderedLocusNames=At5g07660; ORFNames=MBK20.10;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION
RP 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(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).
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: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:19737979}.
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 {ECO:0000269|PubMed:19737979}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACQ84165.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; FJ869873; ACQ84165.1; ALT_SEQ; mRNA.
DR EMBL; AB010070; BAB11444.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91190.1; -; Genomic_DNA.
DR RefSeq; NP_196383.1; NM_120848.2.
DR AlphaFoldDB; Q9FLR5; -.
DR SMR; Q9FLR5; -.
DR STRING; 3702.AT5G07660.1; -.
DR iPTMnet; Q9FLR5; -.
DR PaxDb; Q9FLR5; -.
DR PRIDE; Q9FLR5; -.
DR ProteomicsDB; 234540; -.
DR EnsemblPlants; AT5G07660.1; AT5G07660.1; AT5G07660.
DR GeneID; 830659; -.
DR Gramene; AT5G07660.1; AT5G07660.1; AT5G07660.
DR KEGG; ath:AT5G07660; -.
DR Araport; AT5G07660; -.
DR TAIR; locus:2160289; AT5G07660.
DR eggNOG; KOG0250; Eukaryota.
DR HOGENOM; CLU_009063_1_0_1; -.
DR InParanoid; Q9FLR5; -.
DR OMA; YSQIMER; -.
DR OrthoDB; 263113at2759; -.
DR PhylomeDB; Q9FLR5; -.
DR PRO; PR:Q9FLR5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLR5; baseline and differential.
DR Genevisible; Q9FLR5; 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:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
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; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR027132; SMC6.
DR InterPro; IPR036277; SMC_hinge_sf.
DR PANTHER; PTHR19306:SF9; PTHR19306:SF9; 1.
DR Pfam; PF02463; SMC_N; 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..1058
FT /note="Structural maintenance of chromosomes protein 6A"
FT /id="PRO_0000424412"
FT DOMAIN 23..1049
FT /note="Zinc-hook"
FT REGION 450..633
FT /note="Flexible hinge"
FT COILED 136..449
FT /evidence="ECO:0000255"
FT COILED 634..927
FT /evidence="ECO:0000255"
FT BINDING 50..57
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1058 AA; 122195 MW; A098205C094A72FC CRC64;
MDEHGDHRQS NPFNDQQTSS GKILRIRLEN FMCHSNLEIE FGDWVNFITG QNGSGKSAIL
TALCVAFGCR ARGTQRAATL KDFIKTGCSY ALVYVELKNQ GEDAFKPEIY GDTLIIERRI
SDSTSLTVLK DHQGRKISSR KEELRELVEH YNIDVENPCV IMSQDKSREF LHSGNDKDKF
KFFYKATLLQ QVDDILQSIG TKLNSANALL DEMEKTIKPI EKEINELLEK IKNMEHVEEI
TQQVLHLKKK LAWSWVYDVD RQLKEQNEKI VKFKERVPTC QNKIDRKLGE VESLRVSLTE
KKAQVACLID ESTAMKRELE CLRQSMKKAA REKIALEEEY HHKCSNIQKI KDRVRRLERQ
IEDINEMTIR STQVEQSEIE GKLNQLTVEV EKAESLVSSL KEEENMVMEK ASAGGKEKEH
IEEMIRDHEK KQRNMNAHIN DLKKHQTNKV TAFGGDKVIN LLRAIERHHR RFKMPPIGPI
GAHVTLINGN RWASAVEQAL GNLLNAFIVT DHKDLVALRD CGKEAKYNNL KIIIYDFSRP
RLDIPRHMIP QTEHPTILSV LHSENTTVLN VLVDVSCVER HVLAENYEVG KIIAFERRLS
HLKDVFTIDG YRMFSRGPVQ TTLPPRPRRP TRLCASFDDQ IKDLEIEASR EQSEIQECRG
QKREAEMNLE GLESTMRRLK KQRTQLEKDL TRKELEMQDL KNSVASETKA SPTSSVNELH
LEIMKFQKEI EEKESLLEKL QDSLKEAELK ANELKASYEN LYESAKGEIE ALEKAEDELK
EKEDELHSAE TEKNHYEDIM KDKVLPEIKQ AETIYKELEM KRQESNKKAS IICPESEIKA
LGPWDGPTPL QLSAQINKIN HRLKRENENY SESIDDLRIM HGEKEQKIGK KRKTYKSCRE
KLKVCKDAVD SRWNKLQRNK DLLKRELTWQ FNHHLGKKGI SGNIRVSYED KTLSIEVKMP
QDATNSAVRD TRGLSGGERS FSTLCFTLAL QNMTEAPIRA MDEFDVFMDA VSRKISLDTL
IDFALKQGSQ WMFITPHDIS MVKSHEKIKK QQMAAPRS
