ID A0A0M9A3I0_9HYME Unreviewed; 306 AA.
AC A0A0M9A3I0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 13-SEP-2023, entry version 23.
DE RecName: Full=Ribonuclease H2 subunit B {ECO:0000256|ARBA:ARBA00019062};
DE AltName: Full=Ribonuclease HI subunit B {ECO:0000256|ARBA:ARBA00033464};
GN ORFNames=WN51_12475 {ECO:0000313|EMBL:KOX76495.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX76495.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX76495.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX76495.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX76495.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; KQ435747; KOX76495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9A3I0; -.
DR STRING; 166423.A0A0M9A3I0; -.
DR OrthoDB; 38794at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032299; C:ribonuclease H2 complex; IEA:InterPro.
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:UP000053105}.
FT DOMAIN 38..98
FT /note="Rnh202 triple barrel"
FT /evidence="ECO:0000259|Pfam:PF17745"
FT DOMAIN 101..226
FT /note="Ribonuclease H2 subunit B wHTH"
FT /evidence="ECO:0000259|Pfam:PF09468"
FT REGION 236..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 306 AA; 34923 MW; A0EFA090A1DEF6B7 CRC64;
MPRTKSLPKK CIKTANSHPG TNTWVFLMKG DNLNSTDDDV PDVIKLRHPA TNQPAMFVFS
PGNVTVQEVL TFDENKRSWF IDDNVKSDGK LHLSTPIDPI FLILPYLRKS QQAQPLEQCL
WDEDFPEMTR LTQCQNLKLT LVAERKGDES LQAYKFNEEK ALIWLHKKVE RVVEVLKQKG
IHVSQGAISA TYVKSTMLET VSEIEYLKYA HGIVSEYLQE DISKKLAQHL NLPDETENKK
RKLSNSPEDT VVEKKSKKET PEKESVLKPK TPESIKEKKA TVSKKELARQ KAATGSKNIT
SFFKKK
//