SMC6_SCHPO
ID SMC6_SCHPO Reviewed; 1140 AA.
AC P53692;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Structural maintenance of chromosomes protein 6;
DE AltName: Full=DNA repair protein rad18;
GN Name=smc6; Synonyms=rad18; ORFNames=SPCC5E4.06;
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=8524274; DOI=10.1128/mcb.15.12.7067;
RA Lehmann A.R., Walicka M., Griffiths D.J.F., Murray J.M., Watts F.Z.,
RA McCready S., Carr A.M.;
RT "The rad18 gene of Schizosaccharomyces pombe defines a new subgroup of the
RT SMC superfamily involved in DNA repair.";
RL Mol. Cell. Biol. 15:7067-7080(1995).
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 PARTIAL PROTEIN SEQUENCE.
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 [4]
RP PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION BY MASS 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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTANT NA74.
RX PubMed=10473635; DOI=10.1091/mbc.10.9.2905;
RA Verkade H.M., Bugg S.J., Lindsay H.D., Carr A.M., O'Connell M.J.;
RT "Rad18 is required for DNA repair and checkpoint responses in fission
RT yeast.";
RL Mol. Biol. Cell 10:2905-2918(1999).
RN [6]
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 [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, AND SUMOYLATION BY 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 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 {ECO:0000269|PubMed:10473635}.
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.
CC -!- INTERACTION:
CC P53692; Q53EK2: nse1; NbExp=4; IntAct=EBI-603745, EBI-605440;
CC P53692; Q4PIR3: nse2; NbExp=3; IntAct=EBI-603745, EBI-605449;
CC P53692; Q9Y7U4: nse3; NbExp=5; IntAct=EBI-603745, EBI-605466;
CC P53692; Q6BDR8: nse4; NbExp=4; IntAct=EBI-603745, EBI-605484;
CC P53692; O94668: nse5; NbExp=2; IntAct=EBI-603745, EBI-1150352;
CC P53692; O13688: nse6; NbExp=4; IntAct=EBI-603745, EBI-1150368;
CC P53692; O13710: smc5; NbExp=10; IntAct=EBI-603745, EBI-603756;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
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 smc5, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- PTM: Sumoylated by nse2. {ECO:0000269|PubMed:15601841}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC6 subfamily. {ECO:0000305}.
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DR EMBL; X80929; CAA56900.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21961.1; -; Genomic_DNA.
DR PIR; T41457; T41457.
DR RefSeq; NP_587906.1; NM_001022898.2.
DR PDB; 5MG8; X-ray; 2.75 A; B/D=448-720.
DR PDBsum; 5MG8; -.
DR AlphaFoldDB; P53692; -.
DR SMR; P53692; -.
DR BioGRID; 275593; 35.
DR IntAct; P53692; 8.
DR STRING; 4896.SPCC5E4.06.1; -.
DR iPTMnet; P53692; -.
DR MaxQB; P53692; -.
DR PaxDb; P53692; -.
DR PRIDE; P53692; -.
DR EnsemblFungi; SPCC5E4.06.1; SPCC5E4.06.1:pep; SPCC5E4.06.
DR GeneID; 2539020; -.
DR KEGG; spo:SPCC5E4.06; -.
DR PomBase; SPCC5E4.06; smc6.
DR VEuPathDB; FungiDB:SPCC5E4.06; -.
DR eggNOG; KOG0250; Eukaryota.
DR HOGENOM; CLU_009063_0_0_1; -.
DR InParanoid; P53692; -.
DR OMA; CHRSLGP; -.
DR PhylomeDB; P53692; -.
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:P53692; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IGI:PomBase.
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; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR027132; SMC6.
DR PANTHER; PTHR19306:SF6; PTHR19306:SF6; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromosome; Coiled coil;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW Meiosis; Nucleotide-binding; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..1140
FT /note="Structural maintenance of chromosomes protein 6"
FT /id="PRO_0000119021"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..710
FT /note="Flexible hinge"
FT COILED 262..290
FT /evidence="ECO:0000255"
FT COILED 329..369
FT /evidence="ECO:0000255"
FT COILED 448..493
FT /evidence="ECO:0000255"
FT COILED 711..978
FT /evidence="ECO:0000255"
FT COILED 1113..1140
FT /evidence="ECO:0000255"
FT MOTIF 22..25
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 41..44
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 15..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 124..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MUTAGEN 151
FT /note="A->T: In NA74; induces defects in DNA repair."
FT HELIX 450..491
FT /evidence="ECO:0007829|PDB:5MG8"
FT TURN 492..498
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 502..511
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:5MG8"
FT TURN 515..522
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 524..528
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 532..539
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 553..556
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 557..560
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 562..564
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 565..571
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 575..577
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 578..583
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 584..597
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 603..605
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 614..616
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 626..628
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 629..632
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 634..644
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:5MG8"
FT HELIX 655..663
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 671..675
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 677..679
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 683..686
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 693..698
FT /evidence="ECO:0007829|PDB:5MG8"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:5MG8"
SQ SEQUENCE 1140 AA; 130929 MW; 2D9680F4771016ED CRC64;
MTTELTNVSL EEAITEKTSE NRRKRDSDVL QTEEVDLSNV KRIRASRNQD NRPERQSRLQ
RSSSLIEQVR GNEDGENDVL NQTRETNSNF DNRVGVIECI HLVNFMCHDS LKINFGPRIN
FVIGHNGSGK SAILTGLTIC LGAKASNTNR APNMKSLVKQ GKNYARISVT ISNRGFEAYQ
PEIYGKSITI ERTIRREGSS EYRLRSFNGT VISTKRDELD NICDHMGLQI DNPMNILTQD
TARQFLGNSS PKEKYQLFMK GIQLKQLEEN YSLIEQSLIN TKNVLGNKKT GVSYLAKKEE
EYKLLWEQSR ETENLHNLLE QKKGEMVWAQ VVEVEKELLL AEKEFQHAEV KLSEAKENLE
SIVTNQSDID GKISSKEEVI GRAKGETDTT KSKFEDIVKT FDGYRSEMND VDIQKRDIQN
SINAAKSCLD VYREQLNTER ARENNLGGSQ IEKRANESNN LQREIADLSE QIVELESKRN
DLHSALLEMG GNLTSLLTKK DSIANKISDQ SEHLKVLEDV QRDKVSAFGK NMPQLLKLIT
RETRFQHPPK GPMGKYMTVK EQKWHLIIER ILGNVINGFI VRSHHDQLIL KELMRQSNCH
ATVVVGKYDP FDYSSGEPDS QYPTVLKIIK FDDDEVLHTL INHLGIEKML LIEDRREAEA
YMKRGIANVT QCYALDPRNR GYGFRIVSTQ RSSGISKVTP WNRPPRIGFS SSTSIEAEKK
ILDDLKKQYN FASNQLNEAK IEQAKFKRDE QLLVEKIEGI KKRILLKRRE VNSLESQELS
VLDTEKIQTL ERRISETEKE LESYAGQLQD AKNEEHRIRD NQRPVIEEIR IYREKIQTET
QRLSSLQTEL SRLRDEKRNS EVDIERHRQT VESCTNILRE KEAKKVQCAQ VVADYTAKAN
TRCERVPVQL SPAELDNEIE RLQMQIAEWR NRTGVSVEQA AEDYLNAKEK HDQAKVLVAR
LTQLLQALEE TLRRRNEMWT KFRKLITLRT KELFELYLSQ RNFTGKLVIK HQEEFLEPRV
YPANRNLATA HNRHEKSKVS VQGLSGGEKS FATICMLLSI WEAMSCPLRC LDEFDVFMDA
VNRLVSIKMM VDSAKDSSDK QFIFITPQDM GQIGLDKDVV VFRLSDPVVS SSALPPSTAP
