ID A0A556TKZ9_BAGYA Unreviewed; 494 AA.
AC A0A556TKZ9;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN ORFNames=Baya_1395 {ECO:0000313|EMBL:TSK18015.1};
OS Bagarius yarrelli (Goonch) (Bagrus yarrelli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Sisoridae; Sisorinae; Bagarius.
OX NCBI_TaxID=175774 {ECO:0000313|EMBL:TSK18015.1, ECO:0000313|Proteomes:UP000319801};
RN [1] {ECO:0000313|EMBL:TSK18015.1, ECO:0000313|Proteomes:UP000319801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JWS20170419001 {ECO:0000313|EMBL:TSK18015.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TSK18015.1};
RX PubMed=31274158;
RA Jiang W., Lv Y., Cheng L., Yang K., Chao B., Wang X., Li Y., Pan X.,
RA You X., Zhang Y., Yang J., Li J., Zhang X., Liu S., Sun C., Yang J.,
RA Shi Q.;
RT "Whole-Genome Sequencing of the Giant Devil Catfish, Bagarius yarrelli.";
RL Genome Biol. Evol. 11:2071-2077(2019).
CC -!- FUNCTION: Catalytic subunit of RNase HII, 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:ARBA00024981}.
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|RuleBase:RU003515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077, ECO:0000256|PROSITE-
CC ProRule:PRU01319, ECO:0000256|RuleBase:RU003515};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01319};
CC Note=Manganese or magnesium. Binds 1 divalent metal ion per monomer in
CC the absence of substrate. May bind a second metal ion after substrate
CC binding. {ECO:0000256|PROSITE-ProRule:PRU01319};
CC -!- SIMILARITY: Belongs to the RNase HII family. Eukaryotic subfamily.
CC {ECO:0000256|ARBA:ARBA00007058}.
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:TSK18015.1}.
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DR EMBL; VCAZ01000004; TSK18015.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A556TKZ9; -.
DR Proteomes; UP000319801; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd07181; RNase_HII_eukaryota_like; 1.
DR CDD; cd12481; RRM2_U2B; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR Gene3D; 1.10.10.460; Ribonuclease hii. Domain 2; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR004649; RNase_H2_suA.
DR InterPro; IPR001352; RNase_HII/HIII.
DR InterPro; IPR024567; RNase_HII/HIII_dom.
DR InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034562; U2B''_RRM2.
DR NCBIfam; TIGR00729; ribonuclease HII; 1.
DR PANTHER; PTHR10954; RIBONUCLEASE H2 SUBUNIT A; 1.
DR PANTHER; PTHR10954:SF7; RIBONUCLEASE H2 SUBUNIT A; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
DR PROSITE; PS50102; RRM; 2.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01319};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722, ECO:0000256|PROSITE-
KW ProRule:PRU01319}; Reference proteome {ECO:0000313|Proteomes:UP000319801};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 28..251
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT DOMAIN 299..361
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 420..494
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 371..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 34
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 35
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 142
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 494 AA; 55039 MW; 1108D07619723A56 CRC64;
MDLSDFEADN SVSCRLSSPV PELCRTEDCC LGIDEAGRGP VLGPMVYGIC FCPVSKKEGL
KNLKVADSKT LSEAEREALF LKLDKAKSFV GWALQILSPN TISTSMLQRS KYNLNALSHD
AAIGLVQYAL DCGVQLKEVF VDTVGPAEKY EEKLSQRFPG VNVTVRPKAD SLFPVVSAAS
ICAKVARDHA VKGWKFAEDL GDVDTEYGSG YPNDPKTKSW LLKYLDPVFG YPQFVRFSWS
TAQTLLDSKA VPVHWDDDEE DGEKIAARQK NTSMLSYFNR SKPASNTNTR ETHRFFKLKR
SLYALFSQFG QIIEIVAMKT MNMRGQAFVV FKELAAATNA LRQLQGFPFY NKPMRIQYAK
TDSDIVSKMR GTYGDKEKKK EKKKKAQEQA ANAAKKPANA LNTQPPPPAT VQVPDNPPNY
ILFLTNLPEE TNEMMLSMLF NQFPGFKEVR LVPGKHDIAF VEFESEGQAG VAKDALQGFR
ITATCAMKIT YAKK
//
