ID SMC1_YEAST Reviewed; 1225 AA. AC P32908; D6VTM2; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 02-SEP-2026, entry version 218. DE RecName: Full=Structural maintenance of chromosomes protein 1; DE AltName: Full=DA-box protein SMC1; GN Name=SMC1; Synonyms=CHL10; OrderedLocusNames=YFL008W; 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, AND MUTANTS SMC1-1 AND SMC1-2. RX PubMed=8276886; DOI=10.1083/jcb.123.6.1635; RA Strunnikov A.V., Larionov V.L., Koshland D.; RT "SMC1: an essential yeast gene encoding a putative head-rod-tail protein is RT required for nuclear division and defines a new ubiquitous protein RT family."; RL J. Cell Biol. 123:1635-1648(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). 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 IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; IRR1 AND MCD1, AND RP INTERACTION OF THE COHESIN COMPLEX WITH SCC2. RX PubMed=9990856; DOI=10.1101/gad.13.3.320; RA Toth A., Ciosk R., Uhlmann F., Galova M., Schleiffer A., Nasmyth K.; RT "Yeast cohesin complex requires a conserved protein, Eco1p(Ctf7), to RT establish cohesion between sister chromatids during DNA replication."; RL Genes Dev. 13:320-333(1999). RN [5] RP IDENTIFICATION IN A COHESIN COMPLEX WITH SMC3; MCD1 AND IRR1, AND RP STRUCTURE. RX PubMed=11983169; DOI=10.1016/s1097-2765(02)00515-4; RA Haering C.H., Loewe J., Hochwagen A., Nasmyth K.; RT "Molecular architecture of SMC proteins and the yeast cohesin complex."; RL Mol. Cell 9:773-788(2002). 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). CC -!- FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA CC repair. Central component of cohesin complex. The cohesin complex is CC required for the cohesion of sister chromatids after DNA replication. CC The cohesin complex apparently forms a large proteinaceous ring within CC which sister chromatids can be trapped. At anaphase, the complex is CC cleaved and dissociates from chromatin, allowing sister chromatids to CC segregate. CC -!- SUBUNIT: Cohesin complexes are composed of the SMC1 and SMC3 CC heterodimer attached via their SMC hinge domain, MCD1/SCC1 which link CC them, and IRR1/SCC3, which interacts with MCD1. The cohesin complex CC also interacts with SCC2, which is required for its association with CC chromosomes. {ECO:0000269|PubMed:11983169, ECO:0000269|PubMed:9990856}. CC -!- INTERACTION: CC P32908; P36022: DYN1; NbExp=3; IntAct=EBI-17402, EBI-6230; CC P32908; P17119: KAR3; NbExp=4; IntAct=EBI-17402, EBI-9499; CC P32908; Q12158: MCD1; NbExp=10; IntAct=EBI-17402, EBI-16655; CC P32908; P47149: NNF1; NbExp=6; IntAct=EBI-17402, EBI-12098; CC P32908; P53253: NNF2; NbExp=4; IntAct=EBI-17402, EBI-23229; CC P32908; P32908: SMC1; NbExp=7; IntAct=EBI-17402, EBI-17402; CC P32908; P38989: SMC2; NbExp=3; IntAct=EBI-17402, EBI-17412; CC P32908; P47037: SMC3; NbExp=20; IntAct=EBI-17402, EBI-17423; CC P32908; Q12306: SMT3; NbExp=2; IntAct=EBI-17402, EBI-17490; CC P32908; P36094: SPC42; NbExp=3; IntAct=EBI-17402, EBI-17777; CC P32908; P32558: SPT16; NbExp=2; IntAct=EBI-17402, EBI-4334; CC P32908; Q9UQE7: SMC3; Xeno; NbExp=4; IntAct=EBI-17402, EBI-80718; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Associates with CC chromatin. Before prophase it is scattered along chromosome arms. At CC anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading CC to the dissociation of the complex from chromosomes, allowing CC chromosome separation. CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large CC intramolecular coiled coil regions, allows the heterotypic interaction CC with the corresponding domain of SMC3, forming a V-shaped heterodimer. CC The two heads of the heterodimer are then connected by different ends CC of the cleavable MCD1 protein, forming a ring structure. CC -!- MISCELLANEOUS: Present with 5710 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the SMC family. SMC1 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; L00602; AAA16595.1; -; Unassigned_DNA. DR EMBL; D50617; BAA09230.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12432.1; -; Genomic_DNA. DR PIR; A49464; A49464. DR RefSeq; NP_116647.1; NM_001179958.1. DR PDB; 1W1W; X-ray; 2.90 A; A/B/C/D=1-214, A/B/C/D=1024-1225. DR PDB; 6ZZ6; EM; 3.40 A; A=1003-1224. DR PDB; 7OGT; EM; 5.50 A; A=1-1225. DR AlphaFoldDB; P32908; -. DR EMDB; EMD-11585; -. DR EMDB; EMD-12887; -. DR MDposit; P32908; -. DR SMR; P32908; -. DR BioGRID; 31139; 472. DR ComplexPortal; CPX-1408; Nuclear meiotic cohesin complex. DR ComplexPortal; CPX-1867; Nuclear mitotic cohesin complex. DR DIP; DIP-2982N; -. DR FunCoup; P32908; 955. DR IntAct; P32908; 29. DR MINT; P32908; -. DR STRING; 4932.YFL008W; -. DR iPTMnet; P32908; -. DR PaxDb; 4932-YFL008W; -. DR PeptideAtlas; P32908; -. DR EnsemblFungi; YFL008W_mRNA; YFL008W; YFL008W. DR GeneID; 850540; -. DR KEGG; sce:YFL008W; -. DR AGR; SGD:S000001886; -. DR SGD; S000001886; SMC1. DR VEuPathDB; FungiDB:YFL008W; -. DR eggNOG; KOG0018; Eukaryota. DR HOGENOM; CLU_001042_0_1_1; -. DR InParanoid; P32908; -. DR OMA; KHMDFQR; -. DR OrthoDB; 5575062at2759; -. DR BioCyc; YEAST:G3O-30448-MONOMER; -. DR Reactome; R-SCE-2468052; Establishment of Sister Chromatid Cohesion. DR Reactome; R-SCE-2500257; Resolution of Sister Chromatid Cohesion. DR Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins. DR BioGRID-ORCS; 850540; 0 hits in 10 CRISPR screens. DR CD-CODE; 5F622AE2; Synthetic Condensate 000372. DR EvolutionaryTrace; P32908; -. DR PRO; PR:P32908; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P32908; protein. DR GO; GO:0008278; C:cohesin complex; IBA:GO_Central. DR GO; GO:0030893; C:meiotic cohesin complex; NAS:ComplexPortal. DR GO; GO:0030892; C:mitotic cohesin complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0000217; F:DNA secondary structure binding; IDA:SGD. DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:SGD. DR GO; GO:0006302; P:double-strand break repair; IMP:SGD. DR GO; GO:0034089; P:establishment of meiotic sister chromatid cohesion; NAS:ComplexPortal. DR GO; GO:0034087; P:establishment of mitotic sister chromatid cohesion; NAS:ComplexPortal. DR GO; GO:0007064; P:mitotic sister chromatid cohesion; IGI:SGD. DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD. DR CDD; cd03275; ABC_SMC1_euk; 2. DR FunFam; 3.40.50.300:FF:003350; Structural maintenance of chromosomes protein 1; 1. DR Gene3D; 1.10.287.1490; -; 2. DR Gene3D; 1.20.1060.20; -; 1. DR Gene3D; 3.30.70.1620; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR InterPro; IPR024704; SMC. DR InterPro; IPR028468; Smc1_ABC. DR InterPro; IPR010935; SMC_hinge. DR InterPro; IPR036277; SMC_hinge_sf. DR PANTHER; PTHR18937:SF12; STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN; 1. DR PANTHER; PTHR18937; STRUCTURAL MAINTENANCE OF CHROMOSOMES SMC FAMILY MEMBER; 1. DR Pfam; PF06470; SMC_hinge; 1. DR Pfam; PF02463; SMC_N; 1. DR PIRSF; PIRSF005719; SMC; 1. DR SMART; SM00968; SMC_hinge; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF75553; Smc hinge domain; 1. DR SUPFAM; SSF57997; Tropomyosin; 1. DR PDBsum; 1W1W; -. DR PDBsum; 6ZZ6; -. DR PDBsum; 7OGT; -. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell cycle; Cell division; Chromosome; KW Coiled coil; Mitosis; Nucleotide-binding; Nucleus; Reference proteome. FT CHAIN 1..1225 FT /note="Structural maintenance of chromosomes protein 1" FT /id="PRO_0000119011" FT DOMAIN 527..641 FT /note="SMC hinge" FT COILED 173..489 FT /evidence="ECO:0000255" FT COILED 679..1063 FT /evidence="ECO:0000255" FT MOTIF 1057..1061 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT BINDING 33..40 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255" FT MUTAGEN 173 FT /note="S->L: In temperature-sensitive mutant SMC1-2." FT MUTAGEN 458 FT /note="N->D: In temperature-sensitive mutant SMC1-1." FT STRAND 4..11 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 17..22 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 27..32 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 39..49 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 91..100 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 103..112 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 117..121 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 124..126 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 128..137 FT /evidence="ECO:0007829|PDB:1W1W" FT TURN 142..144 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 156..159 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 162..167 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 170..173 FT /evidence="ECO:0007829|PDB:1W1W" FT TURN 175..178 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 179..188 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 240..259 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 274..279 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 287..290 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 298..300 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 304..319 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 325..331 FT /evidence="ECO:0007829|PDB:1W1W" FT TURN 332..335 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 338..350 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 352..357 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 361..364 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 1005..1016 FT /evidence="ECO:0007829|PDB:6ZZ6" FT HELIX 1022..1037 FT /evidence="ECO:0007829|PDB:6ZZ6" FT HELIX 1068..1071 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 1079..1081 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 1086..1088 FT /evidence="ECO:0007829|PDB:6ZZ6" FT STRAND 1096..1102 FT /evidence="ECO:0007829|PDB:6ZZ6" FT TURN 1107..1109 FT /evidence="ECO:0007829|PDB:6ZZ6" FT STRAND 1112..1117 FT /evidence="ECO:0007829|PDB:6ZZ6" FT HELIX 1131..1148 FT /evidence="ECO:0007829|PDB:6ZZ6" FT STRAND 1152..1158 FT /evidence="ECO:0007829|PDB:6ZZ6" FT HELIX 1165..1178 FT /evidence="ECO:0007829|PDB:6ZZ6" FT STRAND 1181..1188 FT /evidence="ECO:0007829|PDB:6ZZ6" FT TURN 1192..1194 FT /evidence="ECO:0007829|PDB:6ZZ6" FT HELIX 1195..1197 FT /evidence="ECO:0007829|PDB:6ZZ6" FT STRAND 1199..1207 FT /evidence="ECO:0007829|PDB:1W1W" FT TURN 1208..1211 FT /evidence="ECO:0007829|PDB:1W1W" FT STRAND 1212..1219 FT /evidence="ECO:0007829|PDB:1W1W" FT HELIX 1220..1222 FT /evidence="ECO:0007829|PDB:1W1W" SQ SEQUENCE 1225 AA; 141280 MW; B504017AA0ECCA8C CRC64; MGRLVGLELS NFKSYRGVTK VGFGESNFTS IIGPNGSGKS NMMDAISFVL GVRSNHLRSN ILKDLIYRGV LNDENSDDYD NEGAASSNPQ SAYVKAFYQK GNKLVELMRI ISRNGDTSYK IDGKTVSYKD YSIFLENENI LIKAKNFLVF QGDVEQIAAQ SPVELSRMFE EVSGSIQYKK EYEELKEKIE KLSKSATESI KNRRRIHGEL KTYKEGINKN EEYRKQLDKK NELQKFQALW QLYHLEQQKE ELTDKLSALN SEISSLKGKI NNEMKSLQRS KSSFVKESAV ISKQKSKLDY IFKDKEKLVS DLRLIKVPQQ AAGKRISHIE KRIESLQKDL QRQKTYVERF ETQLKVVTRS KEAFEEEIKQ SARNYDKFKL NENDLKTYNC LHEKYLTEGG SILEEKIAVL NNDKREIQEE LERFNKRADI SKRRITEELS ITGEKLDTQL NDLRVSLNEK NALHTERLHE LKKLQSDIES ANNQEYDLNF KLRETLVKID DLSANQRETM KERKLRENIA MLKRFFPGVK GLVHDLCHPK KEKYGLAVST ILGKNFDSVI VENLTVAQEC IAFLKKQRAG TASFIPLDTI ETELPTLSLP DSQDYILSIN AIDYEPEYEK AMQYVCGDSI ICNTLNIAKD LKWKKGIRGK LVTIEGALIH KAGLMTGGIS GDANNRWDKE EYQSLMSLKD KLLIQIDELS NGQRSNSIRA REVENSVSLL NSDIANLRTQ VTQQKRSLDE NRLEIKYHND LIEKEIQPKI TELKKKLDDL ENTKDNLVKE KEALQNNIFK EFTSKIGFTI KEYENHSGEL MRQQSKELQQ LQKQILTVEN KLQFETDRLS TTQRRYEKAQ KDLENAQVEM KSLEEQEYAI EMKIGSIESK LEEHKNHLDE LQKKFVTKQS ELNSSEDILE DMNSNLQVLK RERDGIKEDI EKFDLERVTA LKNCKISNIN IPISSETTID DLPISSTDNE AITISNSIDI NYKGLPKKYK ENNTDSARKE LEQKIHEVEE ILNELQPNAR ALERYDEAEG RFEVINNETE QLKAEEKKIL NQFLKIKKKR KELFEKTFDY VSDHLDAIYR ELTKNPNSNV ELAGGNASLT IEDEDEPFNA GIKYHATPPL KRFKDMEYLS GGEKTVAALA LLFAINSYQP SPFFVLDEVD AALDITNVQR IAAYIRRHRN PDLQFIVISL KNTMFEKSDA LVGVYRQQQE NSSKIITLDL SNYAE //