NSE6_SCHPO
ID NSE6_SCHPO Reviewed; 522 AA.
AC O13688;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Non-structural maintenance of chromosome element 6;
DE Short=Non-SMC element 6;
DE AltName: Full=Core protein 1;
GN Name=nse6; Synonyms=cor1; ORFNames=SPAC11E3.08c;
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 [MRNA].
RA Sawin K.E., Hajibagheri M., Nurse P.;
RT "A marker for cell middles in fission yeast: evidence for a loss of apical
RT identity in a polarity mutant.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
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, FUNCTION, IDENTIFICATION IN THE SMC5/SMC6
RP COMPLEX, INTERACTION WITH NSE5, SUBCELLULAR LOCATION, AND IDENTIFICATION BY
RP 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 [4]
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. May prevent formation of excessive Holliday
CC junctions or assist in their resolution. {ECO:0000269|PubMed:16478984}.
CC -!- SUBUNIT: Component of the smc5/smc6 complex which consists of two
CC subcomplexes, smc5-smc6-nse2 and nse1-nse2-nse4. Interacts with nse5.
CC {ECO:0000269|PubMed:16478984}.
CC -!- INTERACTION:
CC O13688; Q53EK2: nse1; NbExp=2; IntAct=EBI-1150368, EBI-605440;
CC O13688; Q4PIR3: nse2; NbExp=2; IntAct=EBI-1150368, EBI-605449;
CC O13688; O94668: nse5; NbExp=7; IntAct=EBI-1150368, EBI-1150352;
CC O13688; O13710: smc5; NbExp=5; IntAct=EBI-1150368, EBI-603756;
CC O13688; P53692: smc6; NbExp=4; IntAct=EBI-1150368, EBI-603745;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16478984,
CC ECO:0000269|PubMed:16823372}. Chromosome {ECO:0000269|PubMed:16478984}.
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DR EMBL; AJ002494; CAA05501.1; -; mRNA.
DR EMBL; CU329670; CAB11187.1; -; Genomic_DNA.
DR PIR; T37536; T37536.
DR RefSeq; NP_594933.1; NM_001020364.2.
DR AlphaFoldDB; O13688; -.
DR BioGRID; 278013; 121.
DR IntAct; O13688; 7.
DR MINT; O13688; -.
DR STRING; 4896.SPAC11E3.08c.1; -.
DR iPTMnet; O13688; -.
DR MaxQB; O13688; -.
DR PaxDb; O13688; -.
DR EnsemblFungi; SPAC11E3.08c.1; SPAC11E3.08c.1:pep; SPAC11E3.08c.
DR GeneID; 2541512; -.
DR KEGG; spo:SPAC11E3.08c; -.
DR PomBase; SPAC11E3.08c; nse6.
DR VEuPathDB; FungiDB:SPAC11E3.08c; -.
DR HOGENOM; CLU_521904_0_0_1; -.
DR OMA; RCEVKDY; -.
DR PRO; PR:O13688; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:PomBase.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IC:PomBase.
DR GO; GO:0048478; P:replication fork protection; IGI:PomBase.
DR InterPro; IPR014803; DNA_repair_Nse5/Nse6.
DR Pfam; PF08691; Nse5; 1.
PE 1: Evidence at protein level;
KW Chromosome; Direct protein sequencing; DNA damage; DNA recombination;
KW DNA repair; Nucleus; Reference proteome.
FT CHAIN 1..522
FT /note="Non-structural maintenance of chromosome element 6"
FT /id="PRO_0000079254"
FT REGION 482..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..496
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..522
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 59899 MW; 36CF241DD74AF0F5 CRC64;
MNASNNISKF PDLDNSSKLI DHILDSDDSE ELDELPDISS LVPSARAQSR KQYLKNDSSN
SSTYRWNIDL LSSTATIDDS VAKRRKLAVQ NLLQYDSTQT FQTGDEIDEL IGKSVGSNVL
NVLRSNPIYD DDLRYEYCSN SKARVPDWNT LKAECLKDND LEFNEGIIPT TFGDLLSAKL
VPLDIALSIC SLQFFRSLGD TTCSEWIANL EKIFYSYKSS SNNLNQIVRF IFETTADMIG
IDLAKRQVPI QLERTSASEN LKSNLKIKVI NFLKCCGTLY RFSDDTVRFE MIQDACRILI
DNQVGSFCKW QFSQFMELPI SLNPDFLISN IHKVSESPRV WVTILSSLSR SCQKFRKKIA
FTLFVGKQSK NDDSDFSSLC QRLDEISASC NNDYTTLLYQ IRTFGYAVDE KHFKTNERLE
CLLEKLRKID LTISGSTDHL LLSRCEVKDC IHRLFMVLYY LNTNSAPELE RIIESDLPNN
NKQKDRYFKD KTSNLSMKEN KSFSAKKVKK GKKKNKRQAY KR