SMC5_SCHPO
ID SMC5_SCHPO Reviewed; 1076 AA.
AC O13710;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 3.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Structural maintenance of chromosomes protein 5;
DE AltName: Full=DNA repair protein spr18;
DE AltName: Full=SMC partner of rad18;
GN Name=smc5; Synonyms=spr18; ORFNames=SPAC14C4.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10747036; DOI=10.1093/emboj/19.7.1691;
RA Fousteri M.I., Lehmann A.R.;
RT "A novel SMC protein complex in Schizosaccharomyces pombe contains the
RT Rad18 DNA repair protein.";
RL EMBO J. 19:1691-1702(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [4]
RP PROTEIN SEQUENCE OF 241-254; 738-747; 952-971 AND 982-994, AND INTERACTION
RP WITH RAD60.
RX PubMed=12897162; DOI=10.1128/mcb.23.16.5939-5946.2003;
RA Boddy M.N., Shanahan P., McDonald W.H., Lopez-Girona A., Noguchi E.,
RA Yates J.R. III, Russell P.;
RT "Replication checkpoint kinase Cds1 regulates recombinational repair
RT protein Rad60.";
RL Mol. Cell. Biol. 23:5939-5946(2003).
RN [5]
RP INTERACTION WITH NSE1 AND NSE2.
RX PubMed=12966087; DOI=10.1074/jbc.m308828200;
RA McDonald W.H., Pavlova Y., Yates J.R. III, Boddy M.N.;
RT "Novel essential DNA repair proteins Nse1 and Nse2 are subunits of the
RT fission yeast Smc5-Smc6 complex.";
RL J. Biol. Chem. 278:45460-45467(2003).
RN [6]
RP IDENTIFICATION IN THE SMC5-SMC6 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=15331764; DOI=10.1091/mbc.e04-05-0436;
RA Pebernard S., McDonald W.H., Pavlova Y., Yates J.R. III, Boddy M.N.;
RT "Nse1, Nse2, and a novel subunit of the Smc5-Smc6 complex, Nse3, play a
RT crucial role in meiosis.";
RL Mol. Biol. Cell 15:4866-4876(2004).
RN [7]
RP INTERACTION WITH NSE4.
RX PubMed=15485909; DOI=10.1128/mcb.24.21.9401-9413.2004;
RA Morikawa H., Morishita T., Kawane S., Iwasaki H., Carr A.M., Shinagawa H.;
RT "Rad62 protein functionally and physically associates with the smc5/smc6
RT protein complex and is required for chromosome integrity and recombination
RT repair in fission yeast.";
RL Mol. Cell. Biol. 24:9401-9413(2004).
RN [8]
RP INTERACTION WITH NSE2.
RX PubMed=15601841; DOI=10.1128/mcb.25.1.185-196.2005;
RA Andrews E.A., Palecek J., Sergeant J., Taylor E., Lehmann A.R., Watts F.Z.;
RT "Nse2, a component of the Smc5-6 complex, is a SUMO ligase required for the
RT response to DNA damage.";
RL Mol. Cell. Biol. 25:185-196(2005).
RN [9]
RP INTERACTION WITH NSE2.
RX PubMed=15601840; DOI=10.1128/mcb.25.1.172-184.2005;
RA Sergeant J., Taylor E., Palecek J., Fousteri M., Andrews E.A., Sweeney S.,
RA Shinagawa H., Watts F.Z., Lehmann A.R.;
RT "Composition and architecture of the Schizosaccharomyces pombe Rad18 (Smc5-
RT 6) complex.";
RL Mol. Cell. Biol. 25:172-184(2005).
RN [10]
RP IDENTIFICATION IN THE SMC5-SMC6 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16478984; DOI=10.1128/mcb.26.5.1617-1630.2006;
RA Pebernard S., Wohlschlegel J., McDonald W.H., Yates J.R. III, Boddy M.N.;
RT "The Nse5-Nse6 dimer mediates DNA repair roles of the Smc5-Smc6 complex.";
RL Mol. Cell. Biol. 26:1617-1630(2006).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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. Plays a critical role in meiosis.
CC -!- SUBUNIT: Two subcomplexes smc5-smc6-nse2 and nse1-nse3-nse4 exist.
CC These subcomplexes are then brought together via a number of
CC interactions, forming the Smc5-Smc6 complex. Interacts also with rad60.
CC {ECO:0000269|PubMed:12897162, ECO:0000269|PubMed:12966087,
CC ECO:0000269|PubMed:15331764, ECO:0000269|PubMed:15485909,
CC ECO:0000269|PubMed:15601840, ECO:0000269|PubMed:15601841,
CC ECO:0000269|PubMed:16478984}.
CC -!- INTERACTION:
CC O13710; Q53EK2: nse1; NbExp=6; IntAct=EBI-603756, EBI-605440;
CC O13710; Q4PIR3: nse2; NbExp=9; IntAct=EBI-603756, EBI-605449;
CC O13710; Q9Y7U4: nse3; NbExp=5; IntAct=EBI-603756, EBI-605466;
CC O13710; Q6BDR8: nse4; NbExp=5; IntAct=EBI-603756, EBI-605484;
CC O13710; O94668: nse5; NbExp=4; IntAct=EBI-603756, EBI-1150352;
CC O13710; O13688: nse6; NbExp=5; IntAct=EBI-603756, EBI-1150368;
CC O13710; Q9USX3: rad60; NbExp=2; IntAct=EBI-603756, EBI-3650521;
CC O13710; P53692: smc6; NbExp=10; IntAct=EBI-603756, EBI-603745;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, spindle pole body
CC {ECO:0000269|PubMed:16823372}. Barrier septum
CC {ECO:0000269|PubMed:16823372}. Chromosome
CC {ECO:0000269|PubMed:16823372}.
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 -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily. {ECO:0000305}.
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DR EMBL; AJ277543; CAB89122.1; -; Genomic_DNA.
DR EMBL; CU329670; CAB11195.2; -; Genomic_DNA.
DR PIR; T37687; T37687.
DR RefSeq; NP_594907.2; NM_001020338.2.
DR PDB; 5MG8; X-ray; 2.75 A; A/C=366-692.
DR PDBsum; 5MG8; -.
DR AlphaFoldDB; O13710; -.
DR SMR; O13710; -.
DR BioGRID; 278084; 8.
DR IntAct; O13710; 8.
DR STRING; 4896.SPAC14C4.02c.1; -.
DR iPTMnet; O13710; -.
DR MaxQB; O13710; -.
DR PaxDb; O13710; -.
DR PRIDE; O13710; -.
DR EnsemblFungi; SPAC14C4.02c.1; SPAC14C4.02c.1:pep; SPAC14C4.02c.
DR GeneID; 2541587; -.
DR KEGG; spo:SPAC14C4.02c; -.
DR PomBase; SPAC14C4.02c; smc5.
DR VEuPathDB; FungiDB:SPAC14C4.02c; -.
DR eggNOG; KOG0979; Eukaryota.
DR HOGENOM; CLU_004969_2_0_1; -.
DR InParanoid; O13710; -.
DR OMA; SAEFFPG; -.
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:O13710; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000935; C:division septum; IEA:UniProtKB-SubCell.
DR GO; GO:0072686; C:mitotic spindle; HDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR GO; GO:0006281; P:DNA repair; IC:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038729; Rad50/SbcC_AAA.
DR InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; PTHR45916; 1.
DR Pfam; PF13476; AAA_23; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; DNA damage; DNA recombination;
KW DNA repair; Meiosis; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1076
FT /note="Structural maintenance of chromosomes protein 5"
FT /id="PRO_0000119019"
FT REGION 399..629
FT /note="Flexible hinge"
FT COILED 184..275
FT /evidence="ECO:0000255"
FT COILED 328..398
FT /evidence="ECO:0000255"
FT COILED 630..693
FT /evidence="ECO:0000255"
FT COILED 767..816
FT /evidence="ECO:0000255"
FT COILED 866..907
FT /evidence="ECO:0000255"
FT BINDING 51..58
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT HELIX 411..432
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 437..448
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 461..464
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 466..469
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 470..472
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 473..485
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 487..492
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 493..506
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 533..538
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 545..548
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 553..562
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 565..567
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 577..584
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 593..595
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 603..609
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 617..623
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 637..688
FT /evidence="ECO:0007829|PDB:5MG8"
SQ SEQUENCE 1076 AA; 124261 MW; 40D07ABB385D73DA CRC64;
MDGLRPSKRR KSNPLYSDYA LGSIVRIKLV NFVTYDYCEL FPGPYLNLII GPNGTGKSTI
VSAICIGLGW PPKLLGRAKE AREFIKYGKN TATIEIEMKY RDDETVTITR QISQDKSSSF
SINREACATS SITSLMDTFN VQLNNLCHFL PQDRVAEFAQ LDPYSRLMET ERAIDHEGLL
PAHEKLIDLR KREREILQNK NQGQSTLNSL KDRQQALEKE VNIFKEREKI KSYIEMLGLA
KMLVIYREKT NVFNQLRADK KKLKKDLKDL VEEFQPILDK GEELRSDLKL KDDTFNDYSS
ASMELNTSNL RARASFSNFM ENEKKLYEKV NTNRTLLRNA NLTLNEAQQS VKSLTERQGP
RPSDNGVQDL QEKMQEVNAE KLQHENEKLE SSHELGSIRT LKAQKLIDLD NIKRELSYYN
DATKRKLDFM SSAPGWEDAY QTYQLLKEYE SAFEAPAYGP IYMNLKCKEK GFAALIEGFF
RTDTFRTFIM SNYNDYLKLM DLITSKTKYT PTIREFSSER KKKIEDFEPP CSREKLQSFG
FDGYVIDFLE GPEVVLVALC HMLKIHQIPI AKRELPPASV NALNNFRLAN GDPVLKTYLA
GSSIHLVFRS AYGDREITRR TDPLPSRSIY FSENVEMDLV KRKEEQLNAQ LSQLENLQNE
ERKLQEKVNE HESLLSRTND ILSTLRKERD EKLIPIHEWQ QLQERIEHQT LLLRQREKVP
EQFAAEIEKN EDIRKENFEA LMNSVLKVKE NSIKATNNFE KMLGSRLNVI EAKYKLEKHE
MDANQVNARL TEVQDRLKDI TDKLASARED AMSLYGSVVD SLQTQSSDRQ TAITELNEEF
ATSSEVDNKI SIEETKLKFM NVNSYVMEQY DARKKEIEEL ESKMSDFDQS VEELQDEMNS
IKEDWVSKLE ENVQCISDRF SKGMSGMGYA GEVRLGKSDD YDKWYIDILV QFREEEGLQK
LTGQRQSGGE RSVSTIMYLL SLQGLAIAPF RIVDEINQGM DPRNERVVHR HIVNSVCDNA
VSQYFLVTPK LLPDLTYHRN LKVLCICNGA WLPATFRTSL STYFEKLKKS ALISSS
