NSE1_SCHPO
ID NSE1_SCHPO Reviewed; 232 AA.
AC Q53EK2;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Non-structural maintenance of chromosomes element 1;
DE Short=Non-SMC element 1;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q8WV22};
GN Name=nse1; ORFNames=SPCC550.05;
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 [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 [2]
RP PROTEIN SEQUENCE OF 17-21; 34-104; 112-148; 156-188 AND 210-232, FUNCTION,
RP INTERACTION WITH SMC5 AND SMC6, AND SUBCELLULAR LOCATION.
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 [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 INTERACTION WITH NSE3.
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 [6]
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:12966087}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q8WV22};
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 Q53EK2; Q9Y7U4: nse3; NbExp=9; IntAct=EBI-605440, EBI-605466;
CC Q53EK2; Q6BDR8: nse4; NbExp=5; IntAct=EBI-605440, EBI-605484;
CC Q53EK2; O13688: nse6; NbExp=2; IntAct=EBI-605440, EBI-1150368;
CC Q53EK2; O13710: smc5; NbExp=6; IntAct=EBI-605440, EBI-603756;
CC Q53EK2; P53692: smc6; NbExp=4; IntAct=EBI-605440, EBI-603745;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12966087,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the NSE1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329672; CAI84978.1; -; Genomic_DNA.
DR RefSeq; XP_001713165.1; XM_001713113.2.
DR AlphaFoldDB; Q53EK2; -.
DR SMR; Q53EK2; -.
DR BioGRID; 276111; 15.
DR IntAct; Q53EK2; 6.
DR STRING; 4896.SPCC550.05.1; -.
DR MaxQB; Q53EK2; -.
DR PaxDb; Q53EK2; -.
DR EnsemblFungi; SPCC550.05.1; SPCC550.05.1:pep; SPCC550.05.
DR PomBase; SPCC550.05; nse1.
DR VEuPathDB; FungiDB:SPCC550.05; -.
DR eggNOG; KOG4718; Eukaryota.
DR HOGENOM; CLU_1185613_0_0_1; -.
DR InParanoid; Q53EK2; -.
DR OMA; CGYCLHV; -.
DR PhylomeDB; Q53EK2; -.
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR PRO; PR:Q53EK2; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; TAS:PomBase.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:PomBase.
DR GO; GO:0007127; P:meiosis I; IMP:PomBase.
DR GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR CDD; cd16493; RING-CH-C4HC3_NSE1; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR011513; Nse1.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR014857; Znf_RING-like.
DR PANTHER; PTHR20973; PTHR20973; 1.
DR Pfam; PF07574; SMC_Nse1; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW Meiosis; Metal-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..232
FT /note="Non-structural maintenance of chromosomes element 1"
FT /id="PRO_0000114115"
FT ZN_FING 181..222
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
SQ SEQUENCE 232 AA; 27052 MW; 9255E146B354CEA8 CRC64;
MEKERQDGLS DKHKFILQYI MCRTAGVDNE QVRELVQEQY GETATVEDVI NELNNSLHNF
DFKIKRVQDQ LDGRLTLHFQ NLSGDPVSQM ATPYPPVQIE LMRKIIEWIM KCDDYQYSLT
TLQIQKLSRK EMGLAPSVIE SHLHTFERDG WLRQREGIWT FTNHALAELD AYLHNEYESN
LYECNACREI VIAGYVCDCG YCLHVYCCKH LAHVNCINCN TPWANATVIG RW
