CND3_YEAST
ID CND3_YEAST Reviewed; 1035 AA.
AC Q06680; D6VSV8;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Condensin complex subunit 3;
DE AltName: Full=CAPG homolog;
GN Name=YCG1; Synonyms=YCS5; OrderedLocusNames=YDR325W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP SEQUENCE REVISION.
RA Sethuraman A., Dolinski K.J.;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
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 CONDENSIN COMPLEX WITH SMC2; SMC4; BRN1 AND YCS4.
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 [5]
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-981, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-933 AND SER-1008, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-198, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Regulatory subunit 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. The condensin complex probably
CC also plays a role during interphase.
CC -!- SUBUNIT: Component of the condensin complex, which contains the SMC2
CC and SMC4 heterodimer, and three non SMC subunits that probably regulate
CC the complex: BRN1, YCS4 and YCG1/YCS5. {ECO:0000269|PubMed:10811823}.
CC -!- INTERACTION:
CC Q06680; P38989: SMC2; NbExp=3; IntAct=EBI-4799, EBI-17412;
CC Q06680; Q12267: SMC4; NbExp=2; IntAct=EBI-4799, EBI-17430;
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 -!- MISCELLANEOUS: Present with 1920 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CND3 (condensin subunit 3) family.
CC {ECO:0000305}.
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DR EMBL; U32517; AAB64761.2; -; Genomic_DNA.
DR EMBL; BK006938; DAA12168.1; -; Genomic_DNA.
DR RefSeq; NP_010612.2; NM_001180633.1.
DR PDB; 5OQN; X-ray; 3.15 A; A=6-932.
DR PDB; 5OQO; X-ray; 3.25 A; A=6-932.
DR PDB; 5OQP; X-ray; 2.98 A; A=6-932.
DR PDB; 5OQQ; X-ray; 2.79 A; A/B=6-932.
DR PDB; 6YVD; EM; 7.60 A; A=1-1035.
DR PDB; 7Q2Z; EM; 3.20 A; E=1-1035.
DR PDBsum; 5OQN; -.
DR PDBsum; 5OQO; -.
DR PDBsum; 5OQP; -.
DR PDBsum; 5OQQ; -.
DR PDBsum; 6YVD; -.
DR PDBsum; 7Q2Z; -.
DR AlphaFoldDB; Q06680; -.
DR SMR; Q06680; -.
DR BioGRID; 32383; 221.
DR ComplexPortal; CPX-1869; Nuclear condensin complex.
DR IntAct; Q06680; 6.
DR MINT; Q06680; -.
DR STRING; 4932.YDR325W; -.
DR iPTMnet; Q06680; -.
DR MaxQB; Q06680; -.
DR PaxDb; Q06680; -.
DR PRIDE; Q06680; -.
DR EnsemblFungi; YDR325W_mRNA; YDR325W; YDR325W.
DR GeneID; 851925; -.
DR KEGG; sce:YDR325W; -.
DR SGD; S000002733; YCG1.
DR VEuPathDB; FungiDB:YDR325W; -.
DR eggNOG; KOG2025; Eukaryota.
DR GeneTree; ENSGT00390000001577; -.
DR HOGENOM; CLU_004446_1_1_1; -.
DR InParanoid; Q06680; -.
DR OMA; MRGFWEG; -.
DR BioCyc; YEAST:G3O-29882-MON; -.
DR Reactome; R-SCE-2514853; Condensation of Prometaphase Chromosomes.
DR PRO; PR:Q06680; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q06680; protein.
DR GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR GO; GO:0000796; C:condensin complex; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IGI: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; IMP:SGD.
DR GO; GO:0051307; P:meiotic chromosome separation; IMP: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; IMP:SGD.
DR GO; GO:0070058; P:tRNA gene clustering; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027165; CND3.
DR InterPro; IPR025977; Cnd3_C.
DR PANTHER; PTHR14418; PTHR14418; 1.
DR Pfam; PF12719; Cnd3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW DNA condensation; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..1035
FT /note="Condensin complex subunit 3"
FT /id="PRO_0000095048"
FT REPEAT 113..150
FT /note="HEAT 1"
FT REPEAT 153..191
FT /note="HEAT 2"
FT REPEAT 201..239
FT /note="HEAT 3"
FT REPEAT 597..635
FT /note="HEAT 4"
FT REPEAT 827..864
FT /note="HEAT 5"
FT REGION 500..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 909..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 959..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1012..1035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..535
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 198
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 933
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 1008
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 31..47
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 51..63
FT /evidence="ECO:0007829|PDB:5OQQ"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 73..98
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:5OQQ"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 131..144
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:5OQQ"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:5OQQ"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 237..241
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:5OQQ"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 273..285
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 289..300
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:5OQQ"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 326..336
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 348..353
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 356..371
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 375..378
FT /evidence="ECO:0007829|PDB:5OQQ"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 385..400
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 415..430
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 437..451
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 458..471
FT /evidence="ECO:0007829|PDB:5OQQ"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 475..497
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 572..586
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 593..595
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 597..605
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 607..612
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 616..630
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 634..639
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 641..649
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 653..670
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 671..674
FT /evidence="ECO:0007829|PDB:5OQQ"
FT STRAND 675..677
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 683..694
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 700..715
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 722..733
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 736..739
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 741..757
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 759..782
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 793..795
FT /evidence="ECO:0007829|PDB:5OQN"
FT HELIX 799..809
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 812..814
FT /evidence="ECO:0007829|PDB:5OQQ"
FT STRAND 819..821
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 827..838
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 839..841
FT /evidence="ECO:0007829|PDB:5OQP"
FT HELIX 845..853
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 855..857
FT /evidence="ECO:0007829|PDB:5OQP"
FT HELIX 866..878
FT /evidence="ECO:0007829|PDB:5OQQ"
FT HELIX 889..910
FT /evidence="ECO:0007829|PDB:5OQQ"
SQ SEQUENCE 1035 AA; 117851 MW; D3EF17EDFA769FF3 CRC64;
MQDPDGIDIN TKIFNSVAEV FQKAQGSYAG HRKHIAVLKK IQSKAVEQGY EDAFNFWFDK
LVTKILPLKK NEIIGDRIVK LVAAFIASLE RELILAKKQN YKLTNDEEGI FSRFVDQFIR
HVLRGVESPD KNVRFRVLQL LAVIMDNIGE IDESLFNLLI LSLNKRIYDR EPTVRIQAVF
CLTKFQDEEQ TEHLTELSDN EENFEATRTL VASIQNDPSA EVRRAAMLNL INDNNTRPYI
LERARDVNIV NRRLVYSRIL KSMGRKCFDD IEPHIFDQLI EWGLEDRELS VRNACKRLIA
HDWLNALDGD LIELLEKLDV SRSSVCVKAI EALFQSRPDI LSKIKFPESI WKDFTVEIAF
LFRAIYLYCL DNNITEMLEE NFPEASKLSE HLNHYILLRY HHNDISNDSQ SHFDYNTLEF
IIEQLSIAAE RYDYSDEVGR RSMLTVVRNM LALTTLSEPL IKIGIRVMKS LSINEKDFVT
MAIEIINDIR DDDIEKQEQE EKIKSKKINR RNETSVDEED ENGTHNDEVN EDEEDDNISS
FHSAVENLVQ GNGNVSESDI INNLPPEKEA SSATIVLCLT RSSYMLELVN TPLTENILIA
SLMDTLITPA VRNTAPNIRE LGVKNLGLCC LLDVKLAIDN MYILGMCVSK GNASLKYIAL
QVIVDIFSVH GNTVVDGEGK VDSISLHKIF YKVLKNNGLP ECQVIAAEGL CKLFLADVFT
DDDLFETLVL SYFSPINSSN EALVQAFAFC IPVYCFSHPA HQQRMSRTAA DILLRLCVLW
DDLQSSVIPE VDREAMLKPN IIFQQLLFWT DPRNLVNQTG STKKDTVQLT FLIDVLKIYA
QIEKKEIKKM IITNINAIFL SSEQDYSTLK ELLEYSDDIA ENDNLDNVSK NALDKLRNNL
NSLIEEINER SETQTKDENN TANDQYSSIL GNSFNKSSND TIEHAADITD GNNTELTKTT
VNISAVDNTT EQSNSRKRTR SEAEQIDTSK NLENMSIQDT STVAKNVSFV LPDEKSDAMS
IDEEDKDSES FSEVC
