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   27-MAR-2024, entry version 185.
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;
GN   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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   PDB; 7QCD; EM; 8.00 A; B=1-1114.
DR   PDB; 7TVE; EM; 3.80 A; D=1-1114.
DR   PDB; 8T8E; EM; 3.30 A; A=1-1114.
DR   PDB; 8T8F; EM; 4.80 A; E=1-1114.
DR   PDBsum; 7QCD; -.
DR   PDBsum; 7TVE; -.
DR   PDBsum; 8T8E; -.
DR   PDBsum; 8T8F; -.
DR   AlphaFoldDB; Q12749; -.
DR   EMDB; EMD-13895; -.
DR   EMDB; EMD-26140; -.
DR   EMDB; EMD-41097; -.
DR   EMDB; EMD-41098; -.
DR   SMR; Q12749; -.
DR   BioGRID; 31642; 401.
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; 4932-YLR383W; -.
DR   PeptideAtlas; Q12749; -.
DR   EnsemblFungi; YLR383W_mRNA; YLR383W; YLR383W.
DR   GeneID; 851099; -.
DR   KEGG; sce:YLR383W; -.
DR   AGR; SGD:S000004375; -.
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   OrthoDB; 78166at2759; -.
DR   BioCyc; YEAST:G3O-32449-MONOMER; -.
DR   Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR   BioGRID-ORCS; 851099; 1 hit in 10 CRISPR screens.
DR   PRO; PR:Q12749; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; Q12749; Protein.
DR   GO; GO:0000781; C:chromosome, telomeric region; NAS: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:0003684; F:damaged DNA binding; IDA:SGD.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR   GO; GO:0140588; P:chromatin looping; NAS:ComplexPortal.
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; NAS:ComplexPortal.
DR   GO; GO:0032204; P:regulation of telomere maintenance; NAS:ComplexPortal.
DR   GO; GO:0071139; P:resolution of DNA recombination intermediates; IMP:SGD.
DR   Gene3D; 1.10.287.1490; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038729; Rad50/SbcC_AAA.
DR   PANTHER; PTHR19306; STRUCTURAL MAINTENANCE OF CHROMOSOMES 5,6 SMC5, SMC6; 1.
DR   PANTHER; PTHR19306:SF6; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 6; 1.
DR   Pfam; PF13476; AAA_23; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Chromosome; Coiled coil; DNA damage;
KW   DNA recombination; DNA repair; Nucleotide-binding; Nucleus;
KW   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
//