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RTI1_SCHPO
ID   RTI1_SCHPO              Reviewed;         371 AA.
AC   O42905;
DT   06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 126.
DE   RecName: Full=DNA repair and recombination protein rti1;
DE   AltName: Full=Rad twenty-two isogene 1;
DE   AltName: Full=Rad22 homolog;
GN   Name=rti1; ORFNames=SPBC119.14;
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=10512870; DOI=10.1091/mbc.10.10.3331;
RA   Suto K., Nagata A., Murakami H., Okayama H.;
RT   "A double-strand break repair component is essential for S phase completion
RT   in fission yeast cell cycling.";
RL   Mol. Biol. Cell 10:3331-3343(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   INTERACTION WITH RPH51 AND RPH54.
RX   PubMed=14551247; DOI=10.1091/mbc.e03-05-0288;
RA   Catlett M.G., Forsburg S.L.;
RT   "Schizosaccharomyces pombe Rdh54 (TID1) acts with Rhp54 (RAD54) to repair
RT   meiotic double-strand breaks.";
RL   Mol. Biol. Cell 14:4707-4720(2003).
CC   -!- FUNCTION: Active in the repair of DNA damage and in mating-type
CC       switching. Probably involved in the repair of DNA double-strands
CC       breaks. Has a role in promoting S phase completion.
CC       {ECO:0000269|PubMed:10512870}.
CC   -!- SUBUNIT: Interacts with rph51 and rph54. {ECO:0000269|PubMed:14551247}.
CC   -!- INTERACTION:
CC       O42905; P36601: rhp51; NbExp=3; IntAct=EBI-1167500, EBI-926960;
CC   -!- SIMILARITY: Belongs to the RAD52 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA17929.1; -; Genomic_DNA.
DR   PIR; T39312; T39312.
DR   RefSeq; NP_595296.1; NM_001021203.2.
DR   AlphaFoldDB; O42905; -.
DR   SMR; O42905; -.
DR   BioGRID; 276658; 14.
DR   IntAct; O42905; 3.
DR   STRING; 4896.SPBC119.14.1; -.
DR   PaxDb; O42905; -.
DR   EnsemblFungi; SPBC119.14.1; SPBC119.14.1:pep; SPBC119.14.
DR   GeneID; 2540121; -.
DR   KEGG; spo:SPBC119.14; -.
DR   PomBase; SPBC119.14; rti1.
DR   VEuPathDB; FungiDB:SPBC119.14; -.
DR   eggNOG; KOG4141; Eukaryota.
DR   HOGENOM; CLU_011431_3_0_1; -.
DR   InParanoid; O42905; -.
DR   OMA; LAFEKCK; -.
DR   PhylomeDB; O42905; -.
DR   PRO; PR:O42905; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000228; C:nuclear chromosome; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0000150; F:DNA strand exchange activity; ISO:PomBase.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:PomBase.
DR   GO; GO:0000730; P:DNA recombinase assembly; ISO:PomBase.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR   GO; GO:0045002; P:double-strand break repair via single-strand annealing; IBA:GO_Central.
DR   GO; GO:0006312; P:mitotic recombination; IBA:GO_Central.
DR   GO; GO:0007131; P:reciprocal meiotic recombination; IMP:PomBase.
DR   Gene3D; 3.30.390.80; -; 1.
DR   InterPro; IPR004585; DNA_recomb/repair_Rad52.
DR   InterPro; IPR041247; Rad52_fam.
DR   InterPro; IPR007232; Rad52_Rad59_Rad22.
DR   InterPro; IPR042525; Rad52_Rad59_Rad22_sf.
DR   PANTHER; PTHR12132; PTHR12132; 1.
DR   Pfam; PF04098; Rad52_Rad22; 1.
DR   TIGRFAMs; TIGR00607; rad52; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA recombination; DNA repair; Reference proteome.
FT   CHAIN           1..371
FT                   /note="DNA repair and recombination protein rti1"
FT                   /id="PRO_0000173893"
FT   REGION          346..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  41835 MW;  62280F122A2991B0 CRC64;
     MGSLPDQSSC EEFTDSQQDK MTKLLAMQLG PEYISRRSGP GGGSVTYLEA WKAIELANEI
     FGFNGWSSSI QDIHVDYVEE TKEKKFNVGI SVIVRVTLKD GSFHEDVGYG SIENCRVKAL
     AYEKCKKEGT TDALKRALRN FGSSMGNCLY DKRYIQKILK MAPAQAEFNY DNLLRANKRP
     YARFAQKVST PIESHANKSV KLEHKNSIEK KISNVDKPIS DLIENDIHES LPALQNPPIQ
     SHSETDLYAD EELDSILMHH ERPPIPESPR VEEFEELLNQ FEGDEKVSVD KIDAHDKMTE
     AQVVKIPPVQ FMNARVAAAE NPHIKHEGMA FQLHKKSNSI LKSSNIDHNR SMPIRRPSLT
     SNNSANTFST K
 
 
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