SMC5_YEAST
ID SMC5_YEAST Reviewed; 1093 AA.
AC Q08204; D6W231;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Structural maintenance of chromosomes protein 5;
GN Name=SMC5; OrderedLocusNames=YOL034W;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [2]
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 [3]
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 [4]
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 [5]
RP SUBUNIT, AND SUMOYLATION BY MMS21.
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.
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 Q08204; P38632: MMS21; NbExp=5; IntAct=EBI-34125, EBI-11017;
CC Q08204; P40562: MPH1; NbExp=5; IntAct=EBI-34125, EBI-25369;
CC Q08204; Q07913: NSE1; NbExp=5; IntAct=EBI-34125, EBI-30144;
CC Q08204; Q05541: NSE3; NbExp=3; IntAct=EBI-34125, EBI-36625;
CC Q08204; P43124: NSE4; NbExp=3; IntAct=EBI-34125, EBI-14410;
CC Q08204; Q03718: NSE5; NbExp=3; IntAct=EBI-34125, EBI-27756;
CC Q08204; Q12306: SMT3; NbExp=5; IntAct=EBI-34125, EBI-17490;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome {ECO:0000305}.
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 smc6, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- PTM: Sumoylated by MMS21. {ECO:0000269|PubMed:15738391}.
CC -!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily. {ECO:0000305}.
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DR EMBL; Z74776; CAA99034.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10747.1; -; Genomic_DNA.
DR PIR; S66717; S66717.
DR RefSeq; NP_014608.1; NM_001183288.1.
DR PDB; 3HTK; X-ray; 2.31 A; A=304-363, B=739-811.
DR PDB; 7P47; X-ray; 3.31 A; B=737-777.
DR PDBsum; 3HTK; -.
DR PDBsum; 7P47; -.
DR AlphaFoldDB; Q08204; -.
DR SMR; Q08204; -.
DR BioGRID; 34366; 224.
DR ComplexPortal; CPX-1364; SMC5-SMC6 SUMO ligase complex.
DR DIP; DIP-1979N; -.
DR IntAct; Q08204; 18.
DR MINT; Q08204; -.
DR STRING; 4932.YOL034W; -.
DR MaxQB; Q08204; -.
DR PaxDb; Q08204; -.
DR PRIDE; Q08204; -.
DR EnsemblFungi; YOL034W_mRNA; YOL034W; YOL034W.
DR GeneID; 854123; -.
DR KEGG; sce:YOL034W; -.
DR SGD; S000005394; SMC5.
DR VEuPathDB; FungiDB:YOL034W; -.
DR eggNOG; KOG0979; Eukaryota.
DR GeneTree; ENSGT00550000074816; -.
DR HOGENOM; CLU_004969_2_0_1; -.
DR InParanoid; Q08204; -.
DR OMA; SAEFFPG; -.
DR BioCyc; YEAST:G3O-33450-MON; -.
DR Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR EvolutionaryTrace; Q08204; -.
DR PRO; PR:Q08204; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08204; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; 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; IDA:SGD.
DR GO; GO:0003684; F:damaged DNA binding; IDA:SGD.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR GO; GO:0051304; P:chromosome separation; IMP:SGD.
DR GO; GO:0006281; P:DNA repair; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0000725; P:recombinational repair; IPI:SGD.
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; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; PTHR45916; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
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; Ubl conjugation.
FT CHAIN 1..1093
FT /note="Structural maintenance of chromosomes protein 5"
FT /id="PRO_0000119020"
FT REGION 442..650
FT /note="Flexible hinge"
FT COILED 208..354
FT /evidence="ECO:0000255"
FT COILED 404..441
FT /evidence="ECO:0000255"
FT COILED 651..757
FT /evidence="ECO:0000255"
FT COILED 884..926
FT /evidence="ECO:0000255"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 307..360
FT /evidence="ECO:0007829|PDB:3HTK"
FT TURN 740..742
FT /evidence="ECO:0007829|PDB:3HTK"
FT HELIX 743..808
FT /evidence="ECO:0007829|PDB:3HTK"
SQ SEQUENCE 1093 AA; 126037 MW; 6752B96438CFB549 CRC64;
MTSLIDLGRY VERTHHGEDT EPRSKRVKIA KPDLSSFQPG SIIKIRLQDF VTYTLTEFNL
SPSLNMIIGP NGSGKSTFVC AVCLGLAGKP EYIGRSKKVE DFIKNGQDVS KIEITLKNSP
NVTDIEYIDA RDETIKITRI ITRSKRRSDY LINDYQVSES VVKTLVAQLN IQLDNLCQFL
SQERVEEFAR LKSVKLLVET IRSIDASLLD VLDELRELQG NEQSLQKDLD FKKAKIVHLR
QESDKLRKSV ESLRDFQNKK GEIELHSQLL PYVKVKDHKE KLNIYKEEYE RAKANLRAIL
KDKKPFANTK KTLENQVEEL TEKCSLKTDE FLKAKEKINE IFEKLNTIRD EVIKKKNQNE
YYRGRTKKLQ ATIISTKEDF LRSQEILAQT HLPEKSVFED IDIKRKEIIN KEGEIRDLIS
EIDAKANAIN HEMRSIQRQA ESKTKSLTTT DKIGILNQDQ DLKEVRDAVL MVREHPEMKD
KILEPPIMTV SAINAQFAAY LAQCVDYNTS KALTVVDSDS YKLFANPILD KFKVNLRELS
SADTTPPVPA ETVRDLGFEG YLSDFITGDK RVMKMLCQTS KIHTIPVSRR ELTPAQIKKL
ITPRPNGKIL FKRIIHGNRL VDIKQSAYGS KQVFPTDVSI KQTNFYQGSI MSNEQKIRIE
NEIINLKNEY NDRKSTLDAL SNQKSGYRHE LSELASKNDD INREAHQLNE IRKKYTMRKS
TIETLREKLD QLKREARKDV SQKIKDIDDQ IQQLLLKQRH LLSKMASSMK SLKNCQKELI
STQILQFEAQ NMDVSMNDVI GFFNEREADL KSQYEDKKKF VKEMRDTPEF QSWMREIRSY
DQDTKEKLNK VAEKYEEEGN FNLSFVQDVL DKLESEIAMV NHDESAVTIL DQVTAELREL
EHTVPQQSKD LETIKAKLKE DHAVLEPKLD DIVSKISARF ARLFNNVGSA GAVRLEKPKD
YAEWKIEIMV KFRDNAPLKK LDSHTQSGGE RAVSTVLYMI ALQEFTSAPF RVVDEINQGM
DSRNERIVHK AMVENACAEN TSQYFLITPK LLTGLHYHEK MRIHCVMAGS WIPNPSEDPK
MIHFGETSNY SFD
