GenomeNet

Database: UniProt
Entry: B3S7Q1_TRIAD
LinkDB: B3S7Q1_TRIAD
Original site: B3S7Q1_TRIAD 
ID   B3S7Q1_TRIAD            Unreviewed;       303 AA.
AC   B3S7Q1;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Ribonuclease H2 subunit B {ECO:0000256|ARBA:ARBA00019062};
DE   AltName: Full=Ribonuclease HI subunit B {ECO:0000256|ARBA:ARBA00033464};
GN   ORFNames=TRIADDRAFT_60250 {ECO:0000313|EMBL:EDV21233.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV21233.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV21233.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV21233.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
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.
CC       {ECO:0000256|ARBA:ARBA00024778}.
CC   -!- SUBUNIT: The RNase H2 complex is a heterotrimer composed of the
CC       catalytic subunit RNASEH2A and the non-catalytic subunits RNASEH2B and
CC       RNASEH2C. {ECO:0000256|ARBA:ARBA00011277}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RNase H2 subunit B family.
CC       {ECO:0000256|ARBA:ARBA00009823}.
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; DS985254; EDV21233.1; -; Genomic_DNA.
DR   RefSeq; XP_002116200.1; XM_002116164.1.
DR   AlphaFoldDB; B3S7Q1; -.
DR   STRING; 10228.B3S7Q1; -.
DR   EnsemblMetazoa; TriadT60250; TriadP60250; TriadG60250.
DR   GeneID; 6757513; -.
DR   KEGG; tad:TRIADDRAFT_60250; -.
DR   CTD; 6757513; -.
DR   eggNOG; KOG4705; Eukaryota.
DR   HOGENOM; CLU_059802_0_0_1; -.
DR   InParanoid; B3S7Q1; -.
DR   OMA; AQWVLIA; -.
DR   OrthoDB; 38794at2759; -.
DR   PhylomeDB; B3S7Q1; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR   GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central.
DR   GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR   CDD; cd09270; RNase_H2-B; 1.
DR   Gene3D; 1.10.20.120; -; 1.
DR   Gene3D; 2.20.25.530; -; 1.
DR   InterPro; IPR040456; RNase_H2_suB.
DR   InterPro; IPR019024; RNase_H2_suB_wHTH.
DR   InterPro; IPR041195; Rnh202_N.
DR   PANTHER; PTHR13383; RIBONUCLEASE H2 SUBUNIT B; 1.
DR   PANTHER; PTHR13383:SF11; RIBONUCLEASE H2 SUBUNIT B; 1.
DR   Pfam; PF09468; RNase_H2-Ydr279; 1.
DR   Pfam; PF17745; Ydr279_N; 1.
PE   3: Inferred from homology;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009022}.
FT   DOMAIN          18..88
FT                   /note="Rnh202 triple barrel"
FT                   /evidence="ECO:0000259|Pfam:PF17745"
FT   DOMAIN          91..217
FT                   /note="Ribonuclease H2 subunit B wHTH"
FT                   /evidence="ECO:0000259|Pfam:PF09468"
FT   REGION          229..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   303 AA;  34328 MW;  895C3795F480C92C CRC64;
     MASAANQNKC PQNQWVAILP AAIANTNGSK NRIITLRHPR FDIGCQFLLC QESHSLFEIM
     EFKEEPRSWF VNNTVQQNGA LLISTPVDPI FMILPYLAKV KDKFIPMDQI LMDDKFPSCS
     RLYDCVSAND LAKVCECKGS EDLFAYRLST DKLIGWIQRK IERVADDLRH LGVYAGTGSQ
     SETFTRSSKD SSTSKDDYIK YTFGLISDYL SKDICALVEK KMNITSQKIE MPPSKKLKQE
     TKSQGPTDDY TKFNPPSTLA AQVQSSHDDK ARKLTSSERK LKKVDKTNIK SISSYFFRDK
     KAS
//
DBGET integrated database retrieval system