SMC2_YEAST
ID SMC2_YEAST Reviewed; 1170 AA.
AC P38989; D6VTR1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Structural maintenance of chromosomes protein 2;
DE AltName: Full=DA-box protein SMC2;
GN Name=SMC2; OrderedLocusNames=YFR031C;
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=7698648; DOI=10.1101/gad.9.5.587;
RA Strunnikov A.V., Hogan E., Koshland D.;
RT "SMC2, a Saccharomyces cerevisiae gene essential for chromosome segregation
RT and condensation, defines a subgroup within the SMC family.";
RL Genes Dev. 9:587-599(1995).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=8686381;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<177::aid-yea896>3.0.co;2-a;
RA Eki T., Naitou M., Hagiwara H., Abe M., Ozawa M., Sasanuma S., Sasanuma M.,
RA Tsuchiya Y., Shibata T., Watanabe K., Ono A., Yamazaki M., Tashiro H.,
RA Hanaoka F., Murakami Y.;
RT "Fifteen open reading frames in a 30.8 kb region of the right arm of
RT chromosome VI from Saccharomyces cerevisiae.";
RL Yeast 12:177-190(1996).
RN [5]
RP IDENTIFICATION IN A CONDENSIN COMPLEX WITH SMC4; BRN1; YCS4 AND YCG1.
RX PubMed=10811823; DOI=10.1083/jcb.149.4.811;
RA Freeman L., Aragon-Alcaide L., Strunnikov A.V.;
RT "The condensin complex governs chromosome condensation and mitotic
RT transmission of rDNA.";
RL J. Cell Biol. 149:811-824(2000).
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: Central component of the condensin complex, a complex
CC required for conversion of interphase chromatin into mitotic-like
CC condense chromosomes. The condensin complex probably introduces
CC positive supercoils into relaxed DNA in the presence of type I
CC topoisomerases and converts nicked DNA into positive knotted forms in
CC the presence of type II topoisomerases.
CC -!- SUBUNIT: Forms a heterodimer with SMC4. Component of the condensin
CC complex, which contains the SMC2 and SMC4 heterodimer, and three non
CC SMC subunits that probably regulate the complex: BRN1, YCS4 and
CC YCG1/YCS5. {ECO:0000269|PubMed:10811823}.
CC -!- INTERACTION:
CC P38989; P38170: BRN1; NbExp=2; IntAct=EBI-17412, EBI-4792;
CC P38989; P32908: SMC1; NbExp=3; IntAct=EBI-17412, EBI-17402;
CC P38989; Q06680: YCG1; NbExp=3; IntAct=EBI-17412, EBI-4799;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC interphase cells, the majority of the condensin complex is found in the
CC cytoplasm, while a minority of the complex is associated with
CC chromatin. A subpopulation of the complex however remains associated
CC with chromosome foci in interphase cells. During mitosis, most of the
CC condensin complex is associated with the chromatin. At the onset of
CC prophase, condensin associates with chromosome arms and to chromosome
CC condensation. Dissociation from chromosomes is observed in late
CC telophase.
CC -!- DOMAIN: The flexible SMC hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterodimerization with
CC SMC4, forming a V-shaped heterodimer. {ECO:0000250}.
CC -!- MISCELLANEOUS: Present with 3290 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC2 subfamily. {ECO:0000305}.
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DR EMBL; U05820; AAA17416.1; -; Genomic_DNA.
DR EMBL; D50617; BAA09270.1; -; Genomic_DNA.
DR EMBL; BK006940; DAA12471.1; -; Genomic_DNA.
DR PIR; A56157; A56157.
DR RefSeq; NP_116687.1; NM_001179996.2.
DR PDB; 4RSI; X-ray; 2.90 A; A=396-792.
DR PDB; 6YVD; EM; 7.60 A; C=1-1170.
DR PDB; 6YVU; EM; 7.50 A; A=1-1170.
DR PDB; 6YVV; EM; 7.50 A; A=1-1170.
DR PDB; 7Q2X; EM; 3.00 A; A=1-1170.
DR PDB; 7Q2Y; EM; -; A=1-1170.
DR PDBsum; 4RSI; -.
DR PDBsum; 6YVD; -.
DR PDBsum; 6YVU; -.
DR PDBsum; 6YVV; -.
DR PDBsum; 7Q2X; -.
DR PDBsum; 7Q2Y; -.
DR AlphaFoldDB; P38989; -.
DR SMR; P38989; -.
DR BioGRID; 31186; 108.
DR ComplexPortal; CPX-1869; Nuclear condensin complex.
DR DIP; DIP-2983N; -.
DR IntAct; P38989; 15.
DR MINT; P38989; -.
DR STRING; 4932.YFR031C; -.
DR iPTMnet; P38989; -.
DR MaxQB; P38989; -.
DR PaxDb; P38989; -.
DR PRIDE; P38989; -.
DR EnsemblFungi; YFR031C_mRNA; YFR031C; YFR031C.
DR GeneID; 850589; -.
DR KEGG; sce:YFR031C; -.
DR SGD; S000001927; SMC2.
DR VEuPathDB; FungiDB:YFR031C; -.
DR eggNOG; KOG0933; Eukaryota.
DR GeneTree; ENSGT00550000074857; -.
DR HOGENOM; CLU_001042_9_0_1; -.
DR InParanoid; P38989; -.
DR OMA; HNKIAME; -.
DR BioCyc; YEAST:G3O-30479-MON; -.
DR Reactome; R-SCE-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:P38989; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P38989; protein.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:SGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
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:0003680; F:minor groove of adenine-thymine-rich DNA binding; IDA:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030261; P:chromosome condensation; IC:ComplexPortal.
DR GO; GO:0010032; P:meiotic chromosome condensation; IC:SGD.
DR GO; GO:0051307; P:meiotic chromosome separation; IC:SGD.
DR GO; GO:0007076; P:mitotic chromosome condensation; IMP:SGD.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
DR GO; GO:1903342; P:negative regulation of meiotic DNA double-strand break formation; IMP:SGD.
DR GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD.
DR GO; GO:0007130; P:synaptonemal complex assembly; IC:SGD.
DR GO; GO:0070058; P:tRNA gene clustering; IMP:SGD.
DR CDD; cd03273; ABC_SMC2_euk; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR024704; SMC.
DR InterPro; IPR027120; Smc2_ABC.
DR InterPro; IPR010935; SMC_hinge.
DR InterPro; IPR036277; SMC_hinge_sf.
DR Pfam; PF06470; SMC_hinge; 1.
DR Pfam; PF02463; SMC_N; 2.
DR PIRSF; PIRSF005719; SMC; 1.
DR SMART; SM00968; SMC_hinge; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF75553; SSF75553; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Chromosome;
KW Coiled coil; Cytoplasm; DNA condensation; Mitosis; Nucleotide-binding;
KW Nucleus; Reference proteome.
FT CHAIN 1..1170
FT /note="Structural maintenance of chromosomes protein 2"
FT /id="PRO_0000119013"
FT DOMAIN 523..641
FT /note="SMC hinge"
FT COILED 172..469
FT /evidence="ECO:0000255"
FT COILED 678..1027
FT /evidence="ECO:0000255"
FT BINDING 32..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 455..469
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 473..495
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 536..540
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 541..548
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 555..559
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 560..568
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 576..580
FT /evidence="ECO:0007829|PDB:4RSI"
FT TURN 581..583
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 591..600
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 604..607
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 608..611
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 616..618
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 619..626
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 629..634
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 635..642
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 650..653
FT /evidence="ECO:0007829|PDB:4RSI"
FT TURN 654..656
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 657..660
FT /evidence="ECO:0007829|PDB:4RSI"
FT TURN 661..663
FT /evidence="ECO:0007829|PDB:4RSI"
FT STRAND 664..668
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 676..705
FT /evidence="ECO:0007829|PDB:4RSI"
FT TURN 706..711
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 714..721
FT /evidence="ECO:0007829|PDB:4RSI"
FT TURN 722..726
FT /evidence="ECO:0007829|PDB:4RSI"
FT HELIX 727..734
FT /evidence="ECO:0007829|PDB:4RSI"
SQ SEQUENCE 1170 AA; 133928 MW; 142B41AAE109621F CRC64;
MKVEELIIDG FKSYATRTVI TDWDPQFNAI TGLNGSGKSN ILDAICFVLG IASMSTVRAS
SLQDLIYKRG QAGVTKASVT IVFDNTDKSN SPIGFTNSPQ ISVTRQVVLG GTSKYLINGH
RAPQQSVLQL FQSVQLNINN PNFLIMQGKI TKVLNMKPSE ILSLIEEAAG TKMFEDRREK
AERTMSKKET KLQENRTLLT EEIEPKLEKL RNEKRMFLEF QSTQTDLEKT ERIVVSYEYY
NIKHKHTSIR ETLENGETRM KMLNEFVKKT SEEIDSLNED VEEIKLQKEK ELHKEGTISK
LENKENGLLN EISRLKTSLS IKVENLNDTT EKSKALESEI ASSSAKLIEK KSAYANTEKD
YKMVQEQLSK QRDLYKRKEE LVSTLTTGIS STGAADGGYN AQLAKAKTEL NEVSLAIKKS
SMKMELLKKE LLTIEPKLKE ATKDNELNVK HVKQCQETCD KLRARLVEYG FDPSRIKDLK
QREDKLKSHY YQTCKNSEYL KRRVTNLEFN YTKPYPNFEA SFVHGVVGQL FQIDNDNIRY
ATALQTCAGG RLFNVVVQDS QTATQLLERG RLRKRVTIIP LDKIYTRPIS SQVLDLAKKI
APGKVELAIN LIRFDESITK AMEFIFGNSL ICEDPETAKK ITFHPKIRAR SITLQGDVYD
PEGTLSGGSR NTSESLLVDI QKYNQIQKQI ETIQADLNHV TEELQTQYAT SQKTKTIQSD
LNLSLHKLDL AKRNLDANPS SQIIARNEEI LRDIGECENE IKTKQMSLKK CQEEVSTIEK
DMKEYDSDKG SKLNELKKEL KLLAKELEEQ ESESERKYDL FQNLELETEQ LSSELDSNKT
LLHNHLKSIE SLKLENSDLE GKIRGVEDDL VTVQTELNEE KKRLMDIDDE LNELETLIKK
KQDEKKSSEL ELQKLVHDLN KYKSNTNNME KIIEDLRQKH EFLEDFDLVR NIVKQNEGID
LDTYRERSKQ LNEKFQELRK KVNPNIMNMI ENVEKKEAAL KTMIKTIEKD KMKIQETISK
LNEYKRETLV KTWEKVTLDF GNIFADLLPN SFAKLVPCEG KDVTQGLEVK VKLGNIWKES
LIELSGGQRS LIALSLIMAL LQFRPAPMYI LDEVDAALDL SHTQNIGHLI KTRFKGSQFI
VVSLKEGMFA NANRVFRTRF QDGTSVVSIM
