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Database: UniProt
Entry: L5KRB2_PTEAL
LinkDB: L5KRB2_PTEAL
Original site: L5KRB2_PTEAL 
ID   L5KRB2_PTEAL            Unreviewed;       285 AA.
AC   L5KRB2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Ribonuclease H1 {ECO:0000256|PIRNR:PIRNR036852};
DE            Short=RNase H1 {ECO:0000256|PIRNR:PIRNR036852};
DE            EC=3.1.26.4 {ECO:0000256|PIRNR:PIRNR036852};
GN   ORFNames=PAL_GLEAN10020070 {ECO:0000313|EMBL:ELK13954.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK13954.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC       hybrids. {ECO:0000256|PIRNR:PIRNR036852}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|PIRNR:PIRNR036852};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR036852};
CC   -!- SIMILARITY: Belongs to the RNase H family.
CC       {ECO:0000256|ARBA:ARBA00005300, ECO:0000256|PIRNR:PIRNR036852}.
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DR   EMBL; KB030580; ELK13954.1; -; Genomic_DNA.
DR   RefSeq; XP_006910275.1; XM_006910213.1.
DR   AlphaFoldDB; L5KRB2; -.
DR   STRING; 9402.L5KRB2; -.
DR   GeneID; 102891766; -.
DR   KEGG; pale:102891766; -.
DR   CTD; 246243; -.
DR   eggNOG; KOG3752; Eukaryota.
DR   InParanoid; L5KRB2; -.
DR   OrthoDB; 3280806at2759; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR   CDD; cd09280; RNase_HI_eukaryote_like; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 3.40.970.10; Ribonuclease H1, N-terminal domain; 1.
DR   InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR   InterPro; IPR017067; RNase_H1_euk.
DR   InterPro; IPR011320; RNase_H1_N.
DR   InterPro; IPR037056; RNase_H1_N_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10642; RIBONUCLEASE H1; 1.
DR   PANTHER; PTHR10642:SF26; RIBONUCLEASE H1; 1.
DR   Pfam; PF01693; Cauli_VI; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   PIRSF; PIRSF036852; Ribonuclease_H1_euk; 1.
DR   SUPFAM; SSF55658; L9 N-domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|PIRNR:PIRNR036852};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR036852};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR036852};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR036852};
KW   Nuclease {ECO:0000256|PIRNR:PIRNR036852};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552}.
FT   DOMAIN          135..281
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   REGION          72..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   285 AA;  31369 MW;  2B0E285D1C8DDA7B CRC64;
     MTRLLGVARR VALAAVRRGC GCGALGMFYA VRRGRRAGVF LTWSECRAQV DRFPAARFKK
     FATEEEAWAF VRNSGSPGGA EGQKDEPVQE SEAKASKRLR EPPADGDEDS EPCAKLAKPR
     AGPAPAVGKD TFSYMGEHAI VYTDGCCSRN GRHRARAGIG VYWGPGHPLN ISVRLPGRQT
     NQRAEIHAAC KAIEQARAQR ISKLALYTDS MFTINGITNW VEGWKKNGWR TSTGKEVINK
     EDFAELERLT QGMDIQWMHI PGHSGFVGNE EADRLARLGA RQPEA
//
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