RNH2B_SCHPO
ID RNH2B_SCHPO Reviewed; 293 AA.
AC O94627;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Ribonuclease H2 subunit B;
DE Short=RNase H2 subunit B;
DE Short=Rnh2B;
DE AltName: Full=RNase H(202);
DE AltName: Full=Ribonuclease HI subunit B;
GN Name=rnh202; ORFNames=SPBC1347.08c;
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 [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 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: Non catalytic subunit of RNase H2, an endonuclease that
CC specifically degrades the RNA of RNA:DNA hybrids. Participates in DNA
CC replication, possibly by mediating the removal of lagging-strand
CC Okazaki fragment RNA primers during DNA replication. Mediates the
CC excision of single ribonucleotides from DNA:RNA duplexes (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the RNase H2 complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the RNase H2 subunit B family. {ECO:0000305}.
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DR EMBL; CU329671; CAB37439.1; -; Genomic_DNA.
DR PIR; T39396; T39396.
DR RefSeq; NP_596700.1; NM_001022624.2.
DR AlphaFoldDB; O94627; -.
DR SMR; O94627; -.
DR BioGRID; 276437; 26.
DR STRING; 4896.SPBC1347.08c.1; -.
DR MaxQB; O94627; -.
DR PaxDb; O94627; -.
DR EnsemblFungi; SPBC1347.08c.1; SPBC1347.08c.1:pep; SPBC1347.08c.
DR PomBase; SPBC1347.08c; -.
DR VEuPathDB; FungiDB:SPBC1347.08c; -.
DR eggNOG; KOG4705; Eukaryota.
DR HOGENOM; CLU_950457_0_0_1; -.
DR InParanoid; O94627; -.
DR OMA; CKEHAAY; -.
DR PhylomeDB; O94627; -.
DR PRO; PR:O94627; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0032299; C:ribonuclease H2 complex; ISO:PomBase.
DR GO; GO:1903469; P:removal of RNA primer involved in mitotic DNA replication; IC:PomBase.
DR GO; GO:0009259; P:ribonucleotide metabolic process; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IEA:GOC.
DR CDD; cd09270; RNase_H2-B; 1.
DR InterPro; IPR040456; RNase_H2_suB.
DR InterPro; IPR019024; RNase_H2_suB_wHTH.
DR InterPro; IPR041195; Rnh202_N.
DR PANTHER; PTHR13383; PTHR13383; 1.
DR Pfam; PF09468; RNase_H2-Ydr279; 1.
DR Pfam; PF17745; Ydr279_N; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..293
FT /note="Ribonuclease H2 subunit B"
FT /id="PRO_0000343167"
FT REGION 251..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 293 AA; 33719 MW; 0C5F3520F9DA01D0 CRC64;
MQGKIFILPK DSTNQQFVEL SHPLTGRPLR YLLTNDHLLQ ILQVGDSSKQ RSWFVGDHVV
SDGYLYVCTP IDLLALVLPI IQELTWSRRK EPNRYVSFED FIEHFDNMGP HYPRVSEVLS
PNLLNTLHRI CKVNEPVGSL PKTFQLDESS VVKILLRKAK VAQENLPPSI VTELKKQLAP
LDLRTPLPQD LLELSCKWHA ASLVCEDLQP EWYNKLAYWQ EELAPLHAYT KNLEESRKIL
VEKEALLNSK KRPQNSDITS SLLKKPNRKQ ATKKSKYFSG EGMTKISSFF TKK
