RHP26_SCHPO
ID RHP26_SCHPO Reviewed; 973 AA.
AC Q9UR24;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA repair protein rhp26;
DE EC=3.6.4.-;
DE AltName: Full=RAD26 homolog;
GN Name=rhp26; ORFNames=SPCP25A2.02c;
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], AND FUNCTION.
RX PubMed=10480889; DOI=10.1074/jbc.274.38.26822;
RA Yasuhira S., Morimyo M., Yasui A.;
RT "Transcription dependence and the roles of two excision repair pathways for
RT UV damage in fission yeast Schizosaccharomyces pombe.";
RL J. Biol. Chem. 274:26822-26827(1999).
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 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: Involved in transcription-coupled repair (TCR).
CC {ECO:0000269|PubMed:10480889}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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DR EMBL; AB022912; BAA84456.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB62827.1; -; Genomic_DNA.
DR PIR; T50449; T50449.
DR RefSeq; NP_588091.1; NM_001023082.2.
DR AlphaFoldDB; Q9UR24; -.
DR SMR; Q9UR24; -.
DR BioGRID; 276036; 27.
DR STRING; 4896.SPCP25A2.02c.1; -.
DR iPTMnet; Q9UR24; -.
DR MaxQB; Q9UR24; -.
DR PaxDb; Q9UR24; -.
DR PRIDE; Q9UR24; -.
DR EnsemblFungi; SPCP25A2.02c.1; SPCP25A2.02c.1:pep; SPCP25A2.02c.
DR GeneID; 2539473; -.
DR KEGG; spo:SPCP25A2.02c; -.
DR PomBase; SPCP25A2.02c; rhp26.
DR VEuPathDB; FungiDB:SPCP25A2.02c; -.
DR eggNOG; KOG0387; Eukaryota.
DR HOGENOM; CLU_000315_7_0_1; -.
DR InParanoid; Q9UR24; -.
DR OMA; PREWGYC; -.
DR PhylomeDB; Q9UR24; -.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR PRO; PR:Q9UR24; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; NAS:PomBase.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; IMP:PomBase.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding; Coiled coil; Cytoplasm; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..973
FT /note="DNA repair protein rhp26"
FT /id="PRO_0000372387"
FT DOMAIN 289..490
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 629..789
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 230..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 35..107
FT /evidence="ECO:0000255"
FT MOTIF 441..444
FT /note="DEAH box"
FT COMPBIAS 815..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 302..309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 973 AA; 110914 MW; 4A8C61319B7D29EB CRC64;
MSVNEDLSHL GVFSVDQENL ERDVTNTASE YIAHESREIE KKRLQKVRKE ISSVKEKIRR
LDERIDSRLT KISVKENFRK QLSKFRDTLQ SLQSDENDIK RRLNNEDSAN APGIGAFSTE
ELERQELIRT GKVTPFRNLS GLQKEVDFDD ESSIREAVIK SEGTYYETAP HLSSEPSNID
HGIIPRDEKD EYVTVDAVTE KVVTAAIDDG DDLVYRQRLN AWCANRKELR DQASASENNK
DRGEFEGKDE WLLPHPSKKG QTFEGGFTIP GDIRPHLFRY QVTCVQWLWE LYCQEAGGII
GDEMGLGKTI QIVSFLSSLH HSGKFQKPAL IVCPATLMKQ WVNEFHTWWA PLRVVVLHAT
GSGQRASREK RQYESDASES EAEESKTSIK LRGASSSFHR YAKNLVESVF TRGHILITTY
AGLRIYGDLI LPREWGYCVL DEGHKIRNPD SEISISCKQI RTVNRIILSG TPIQNNLTEL
WNLFDFVFPG RLGTLPVFQN QFALPINIGG YANASNVQVQ TAYKCACMLR DLISPYLLRR
MKLDVAADLP KKSEQVLFCK LTPLQRKAYQ DFLQGSDMQK ILNGKRQMLY GIDILRKICN
HPDLVTREYL LHKEDYNYGD PEKSGKLKVI RALLTLWKKQ GHRTLLFSQT RQMLDILEIG
LKDLPDVHYC RMDGSTSIAL RQDLVDNFNK NEYFDVFLLT TRVGGLGVNL TGADRVILFD
PDWNPSTDAQ ARERAWRLGQ KKDVVVYRLM TAGTIEEKIY HRQIFKQFLT NKILKDPKQR
RFFKMTDLHD LFTLGDNKTE GTETGSMFLG SERVLRKDNS SRNGNEAEDI PARDRKKHKI
HDKGKKVNSS KVFEKMGIAS MEKYKPPQES NVTKTNSDST LGDDSVLDDI FASAGIQSTL
KHDDIMEASQ TESILVEKEA TRVANEALRA VSSFRRPPRQ LIPPQQSTNV PGTSKPSGPI
TSSTLLARLK QRR
