SMC6_YEAST
ID SMC6_YEAST Reviewed; 1114 AA.
AC Q12749; D6VZ18;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Structural maintenance of chromosomes protein 6;
DE AltName: Full=DNA repair protein RHC18;
DE AltName: Full=Rad18 homolog;
GN Name=SMC6; Synonyms=RHC18; OrderedLocusNames=YLR383W; ORFNames=L3502.2;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8524274; DOI=10.1128/mcb.15.12.7067;
RA Lehmann A.R., Walicka M., Griffiths D.J.F., Murray J.M., Watts F.Z.,
RA McCready S., Carr A.M.;
RT "The rad18 gene of Schizosaccharomyces pombe defines a new subgroup of the
RT SMC superfamily involved in DNA repair.";
RL Mol. Cell. Biol. 15:7067-7080(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-184.
RC STRAIN=AB1-4A/8/55;
RX PubMed=3034607; DOI=10.1002/j.1460-2075.1987.tb04812.x;
RA Labouesse M., Herbert C.J., Dujardin G., Slonimski P.P.;
RT "Three suppressor mutations which cure a mitochondrial RNA maturase
RT deficiency occur at the same codon in the open reading frame of the nuclear
RT NAM2 gene.";
RL EMBO J. 6:713-721(1987).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION.
RX PubMed=15010319; DOI=10.1016/j.dnarep.2003.12.007;
RA Onoda F., Takeda M., Seki M., Maeda D., Tajima J., Ui A., Yagi H.,
RA Enomoto T.;
RT "SMC6 is required for MMS-induced interchromosomal and sister chromatid
RT recombinations in Saccharomyces cerevisiae.";
RL DNA Repair 3:429-439(2004).
RN [8]
RP SUBUNIT.
RX PubMed=15738391; DOI=10.1073/pnas.0500537102;
RA Zhao X., Blobel G.;
RT "A SUMO ligase is part of a nuclear multiprotein complex that affects DNA
RT repair and chromosomal organization.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:4777-4782(2005).
CC -!- FUNCTION: Acts in a DNA repair pathway for removal of UV-induced DNA
CC damage that is distinct from classical nucleotide excision repair and
CC in repair of ionizing radiation damage. Functions in homologous
CC recombination repair of DNA double strand breaks and in recovery of
CC stalled replication forks. Probably plays a role in structure.
CC {ECO:0000269|PubMed:15010319}.
CC -!- SUBUNIT: Component of the Smc5-Smc6 complex which consists of KRE29,
CC MMS21, NSE1, NSE3, NSE4, NSE5, SMC5 and SMC6.
CC {ECO:0000269|PubMed:15738391}.
CC -!- INTERACTION:
CC Q12749; Q07913: NSE1; NbExp=4; IntAct=EBI-15099, EBI-30144;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
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 SMC5, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily. {ECO:0000305}.
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DR EMBL; X80930; CAA56902.1; -; Genomic_DNA.
DR EMBL; U19104; AAB67273.1; -; Genomic_DNA.
DR EMBL; X05143; CAA28789.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09684.1; -; Genomic_DNA.
DR PIR; S51470; S51470.
DR RefSeq; NP_013487.1; NM_001182272.1.
DR AlphaFoldDB; Q12749; -.
DR SMR; Q12749; -.
DR BioGRID; 31642; 399.
DR ComplexPortal; CPX-1364; SMC5-SMC6 SUMO ligase complex.
DR DIP; DIP-6624N; -.
DR IntAct; Q12749; 41.
DR STRING; 4932.YLR383W; -.
DR iPTMnet; Q12749; -.
DR MaxQB; Q12749; -.
DR PaxDb; Q12749; -.
DR PRIDE; Q12749; -.
DR EnsemblFungi; YLR383W_mRNA; YLR383W; YLR383W.
DR GeneID; 851099; -.
DR KEGG; sce:YLR383W; -.
DR SGD; S000004375; SMC6.
DR VEuPathDB; FungiDB:YLR383W; -.
DR eggNOG; KOG0250; Eukaryota.
DR GeneTree; ENSGT00550000074816; -.
DR HOGENOM; CLU_009063_0_0_1; -.
DR InParanoid; Q12749; -.
DR OMA; MCHDHFY; -.
DR BioCyc; YEAST:G3O-32449-MON; -.
DR Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:Q12749; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12749; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0035861; C:site of double-strand break; IDA:SGD.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:SGD.
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; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0051304; P:chromosome separation; IMP:SGD.
DR GO; GO:1990683; P:DNA double-strand break attachment to nuclear envelope; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:SGD.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0071139; P:resolution of recombination intermediates; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR027132; SMC6.
DR PANTHER; PTHR19306:SF6; PTHR19306:SF6; 1.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; SSF52540; 3.
PE 1: Evidence at protein level;
KW ATP-binding; Chromosome; Coiled coil; DNA damage; DNA recombination;
KW DNA repair; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1114
FT /note="Structural maintenance of chromosomes protein 6"
FT /id="PRO_0000119022"
FT REGION 26..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..695
FT /note="Flexible hinge"
FT COILED 259..529
FT /evidence="ECO:0000255"
FT COILED 696..969
FT /evidence="ECO:0000255"
FT MOTIF 35..39
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 43..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1114 AA; 128009 MW; 55C166C5B72CD957 CRC64;
MISTTISGKR PIEQVDDELL SLTAQQENEE QQQQRKRRRH QFAPMTQFNS NTLDEDSGFR
SSSDVATADQ DNFLEESPSG YIKKVILRNF MCHEHFELEL GSRLNFIVGN NGSGKSAILT
AITIGLGAKA SETNRGSSLK DLIREGCYSA KIILHLDNSK YGAYQQGIFG NEIIVERIIK
RDGPASFSLR SENGKEISNK KKDIQTVVDY FSVPVSNPMC FLSQDAARSF LTASTSQDKY
SHFMKGTLLQ EITENLLYAS AIHDSAQENM ALHLENLKSL KAEYEDAKKL LRELNQTSDL
NERKMLLQAK SLWIDVAHNT DACKNLENEI SGIQQKVDEV TEKIRNRQEK IERYTSDGTT
IEAQIDAKVI YVNEKDSEHQ NARELLRDVK SRFEKEKSNQ AEAQSNIDQG RKKVDALNKT
IAHLEEELTK EMGGDKDQMR QELEQLEKAN EKLREVNNSL VVSLQDVKNE ERDIQHERES
ELRTISRSIQ NKKVELQNIA KGNDTFLMNF DRNMDRLLRT IEQRKNEFET PAIGPLGSLV
TIRKGFEKWT RSIQRAISSS LNAFVVSNPK DNRLFRDIMR SCGIRSNIPI VTYCLSQFDY
SKGRAHGNYP TIVDALEFSK PEIECLFVDL SRIERIVLIE DKNEARNFLQ RNPVNVNMAL
SLRDRRSGFQ LSGGYRLDTV TYQDKIRLKV NSSSDNGTQY LKDLIEQETK ELQNIRDRYE
EKLSEVRSRL KEIDGRLKST KNEMRKTNFR MTELKMNVGK VVDTGILNSK INERKNQEQA
IASYEAAKEE LGLKIEQIAQ EAQPIKEQYD STKLALVEAQ DELQQLKEDI NSRQSKIQKY
KDDTIYYEDK KKVYLENIKK IEVNVAALKE GIQRQIQNAC AFCSKERIEN VDLPDTQEEI
KRELDKVSRM IQKAEKSLGL SQEEVIALFE KCRNKYKEGQ KKYMEIDEAL NRLHNSLKAR
DQNYKNAEKG TCFDADMDFR ASLKVRKFSG NLSFIKDTKS LEIYILTTND EKARNVDTLS
GGEKSFSQMA LLLATWKPMR SRIIALDEFD VFMDQVNRKI GTTLIVKKLK DIARTQTIII
TPQDIGKIAD IDSSGVSIHR MRDPERQNNS NFYN
