ELG1_SCHPO
ID ELG1_SCHPO Reviewed; 920 AA.
AC O43086;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Telomere length regulation protein elg1;
DE AltName: Full=Telomere elongation suppressor elg1;
GN Name=elg1; ORFNames=SPBC947.11c;
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 1-18; 67-72; 105-126; 170-182; 235-251; 281-299;
RP 331-372; 419-460; 471-482; 485-518; 572-580; 587-665; 667-677; 684-776;
RP 797-810 AND 885-909, FUNCTION, AND SUBUNIT.
RX PubMed=16040599; DOI=10.1093/nar/gki728;
RA Kim J., Robertson K., Mylonas K.J.L., Gray F.C., Charapitsa I.,
RA MacNeill S.A.;
RT "Contrasting effects of Elg1-RFC and Ctf18-RFC inactivation in the absence
RT of fully functional RFC in fission yeast.";
RL Nucleic Acids Res. 33:4078-4089(2005).
CC -!- FUNCTION: Involved in the negative control of telomere length and in
CC telomeric silencing through a replication-mediated pathway. May have a
CC role in Okazaki fragment maturation. Required for S-phase progression.
CC An RFC-like complex (elg1-RFC) is formed where elg1 replaces rfc1 in
CC the RFC complex. This complex appears to have a role in DNA
CC replication, replication fork re-start, recombination and repair.
CC {ECO:0000269|PubMed:16040599}.
CC -!- SUBUNIT: Heteropentamer of elg1, rfc2, rfc3, rfc4 and rfc5 forming the
CC elg1-RFC complex. {ECO:0000269|PubMed:16040599}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ELG1 family. {ECO:0000305}.
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DR EMBL; CU329671; CAA17039.1; -; Genomic_DNA.
DR PIR; T40771; T40771.
DR RefSeq; NP_595265.1; NM_001021172.2.
DR AlphaFoldDB; O43086; -.
DR BioGRID; 277790; 9.
DR STRING; 4896.SPBC947.11c.1; -.
DR iPTMnet; O43086; -.
DR MaxQB; O43086; -.
DR PaxDb; O43086; -.
DR PRIDE; O43086; -.
DR EnsemblFungi; SPBC947.11c.1; SPBC947.11c.1:pep; SPBC947.11c.
DR GeneID; 2541276; -.
DR KEGG; spo:SPBC947.11c; -.
DR PomBase; SPBC947.11c; elg1.
DR VEuPathDB; FungiDB:SPBC947.11c; -.
DR eggNOG; KOG1968; Eukaryota.
DR HOGENOM; CLU_316904_0_0_1; -.
DR InParanoid; O43086; -.
DR OMA; LMQLNFW; -.
DR PRO; PR:O43086; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0031391; C:Elg1 RFC-like complex; IDA:PomBase.
DR GO; GO:0043599; C:nuclear DNA replication factor C complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISM:PomBase.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0061860; F:DNA clamp unloader activity; IC:PomBase.
DR GO; GO:0090618; P:DNA clamp unloading; IMP:PomBase.
DR GO; GO:0006310; P:DNA recombination; ISO:PomBase.
DR GO; GO:1902969; P:mitotic DNA replication; ISO:PomBase.
DR GO; GO:0000723; P:telomere maintenance; ISO:PomBase.
DR GO; GO:0070914; P:UV-damage excision repair; IDA:PomBase.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Chromosome; Direct protein sequencing; DNA damage;
KW DNA recombination; DNA repair; DNA replication; Nucleus;
KW Reference proteome; Telomere.
FT CHAIN 1..920
FT /note="Telomere length regulation protein elg1"
FT /id="PRO_0000239057"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 112..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..407
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 920 AA; 103843 MW; AB5BD076ECC88DD6 CRC64;
MQIVGYLSAD SQSNPDLKSE NEAKEEKPIG RRHTMSPVPA TSENKYFGKS PLSGSRKPRR
SRSLHKERSY MRKFFDMDME ESKDFENDQS LLVTLKVSTS LGQKIENILH PKLSNDTNST
AFPPAKSSGE ASDTNILVEN INSQETVNSS PLVSELHYSN LADSPSNLRN TVTSMHPFFM
SKSVKKNSEI KFVSEERGGT KPERLLDPLW PTPDSQSMLE YAGSIEPSVF WFPKKHLEEA
ILEETSHLSF KEVLSSTTAN MITPLAEKNK TEVLQVTPSK LHTFALESLC FSPAPFIQKV
LSRLLPSDPN VEMPMIPQIL EKGLWVSKYA PSKTQDCCAF SQCLSKIADW LRSCRLTKPE
SSSVPPSSSI SRSSTIHSCT SSKRNEDSLS ESDFEPDIIE EEDDSDEFNP SVSRKKAKLT
SSQFSNWMLV TGVTGIGKTS CLYAICRELN FEVVEIHPGM RRSGKELLER IGELTQSHIV
DKSRLNNTPD ILILLEEVDI LFQDDRGFWQ AVSTLIEKSK RPVVMTCNET DFLPSAFLQE
DHIVQFQSIS SALLTDYISS VLYADRCIIS RNVVESISYR YGSDLRGILM QLNFWSLVNF
PSLPSKDKQD DSHEPFIEAT ISAFDEGVGV YNPRIQTSED LLQTYSEEQM GDIGLLFMPN
LVNWRKVCVP KSEMEEKEAI MEKLIYSHQY ADSLSYVDYR FSSQPTIYET YELMNDSASF
EDMSLECRDN CANAFQDNLV GFPTISNPFH ANAPPEPHEL KLQYHSFCFI NNLFSKSSLK
AISSNDSIVP KALNNRELQL SALASTIGYK LDPDDVYNIL SFLSFANSQV TSYTPPNSID
RPNDILILEV APFVRCMRRY DRIRLNSYKL LLSSKGRSAS HISRRGAASI LRSAGYNYGR
LQYLEGSDRI LSTWFSTTLD
