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Database: UniProt
Entry: A0A0L0C4C2_LUCCU
LinkDB: A0A0L0C4C2_LUCCU
Original site: A0A0L0C4C2_LUCCU 
ID   A0A0L0C4C2_LUCCU        Unreviewed;       364 AA.
AC   A0A0L0C4C2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Ribonuclease H2 subunit B {ECO:0000256|ARBA:ARBA00019062};
DE   AltName: Full=Ribonuclease HI subunit B {ECO:0000256|ARBA:ARBA00033464};
GN   ORFNames=FF38_02658 {ECO:0000313|EMBL:KNC27213.1};
OS   Lucilia cuprina (Green bottle fly) (Australian sheep blowfly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Oestroidea;
OC   Calliphoridae; Luciliinae; Lucilia.
OX   NCBI_TaxID=7375 {ECO:0000313|EMBL:KNC27213.1, ECO:0000313|Proteomes:UP000037069};
RN   [1] {ECO:0000313|EMBL:KNC27213.1, ECO:0000313|Proteomes:UP000037069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LS {ECO:0000313|EMBL:KNC27213.1,
RC   ECO:0000313|Proteomes:UP000037069};
RC   TISSUE=Full body {ECO:0000313|EMBL:KNC27213.1};
RX   PubMed=26108605; DOI=10.1038/ncomms8344;
RA   Anstead C.A., Korhonen P.K., Young N.D., Hall R.S., Jex A.R., Murali S.C.,
RA   Hughes D.S., Lee S.F., Perry T., Stroehlein A.J., Ansell B.R.,
RA   Breugelmans B., Hofmann A., Qu J., Dugan S., Lee S.L., Chao H., Dinh H.,
RA   Han Y., Doddapaneni H.V., Worley K.C., Muzny D.M., Ioannidis P.,
RA   Waterhouse R.M., Zdobnov E.M., James P.J., Bagnall N.H., Kotze A.C.,
RA   Gibbs R.A., Richards S., Batterham P., Gasser R.B.;
RT   "Lucilia cuprina genome unlocks parasitic fly biology to underpin future
RT   interventions.";
RL   Nat. Commun. 6:7344-7344(2015).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KNC27213.1}.
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DR   EMBL; JRES01000930; KNC27213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L0C4C2; -.
DR   STRING; 7375.A0A0L0C4C2; -.
DR   EnsemblMetazoa; KNC27213; KNC27213; FF38_02658.
DR   OMA; MACDIVG; -.
DR   Proteomes; UP000037069; 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:UP000037069}.
FT   DOMAIN          47..106
FT                   /note="Rnh202 triple barrel"
FT                   /evidence="ECO:0000259|Pfam:PF17745"
FT   DOMAIN          109..240
FT                   /note="Ribonuclease H2 subunit B wHTH"
FT                   /evidence="ECO:0000259|Pfam:PF09468"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..293
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..329
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   364 AA;  40693 MW;  75F6579A309ED0DB CRC64;
     MSKSKSTRST KIKEDPDAST KSTKNSTVPS ALRKIFYISQ HMLQDETEKL CLERFYHPGK
     GKAALFITKD DKHIMEILEF AEPRRSWLID SEVCSNGHIY FTTPIDVTFL ALHHLRKHCV
     KRALALDSIH DDEDPSAAKI LNNFVDPKNL ACIADVKTAG GDMTFYKYNH DKTMAWLSLK
     TKRLAKLLQS SGIYCGNSAV SQNFARSEKA LDETAKDSDY LRMACDYVGG YIAVELHEEL
     TKLLDIPSEI QAITEDKKVS TNKRKSGDKL TSAGTKKQKL ENGAASKLKN SNLLDESFDN
     EEEDIKDEEE ENKVNTSIKE EHKSPKAATA TPLKERSLSA KEKSLAKSAK GTKSIASFFM
     KKAA
//
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