ID A0A915N266_MELJA Unreviewed; 651 AA.
AC A0A915N266;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 14.
DE RecName: Full=ribonuclease H {ECO:0000256|ARBA:ARBA00012180};
DE EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180};
OS Meloidogyne javanica (Root-knot nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Meloidogynidae; Meloidogyninae;
OC Meloidogyne; Meloidogyne incognita group.
OX NCBI_TaxID=6303 {ECO:0000313|Proteomes:UP000887561, ECO:0000313|WBParaSite:scaffold617_cov188.g1431};
RN [1] {ECO:0000313|WBParaSite:scaffold617_cov188.g1431}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2022) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000077};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the RNase H family.
CC {ECO:0000256|ARBA:ARBA00005300}.
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DR AlphaFoldDB; A0A915N266; -.
DR WBParaSite; scaffold617_cov188.g1431; scaffold617_cov188.g1431; scaffold617_cov188.g1431.
DR Proteomes; UP000887561; Unplaced.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:TreeGrafter.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro.
DR CDD; cd09280; RNase_HI_eukaryote_like; 1.
DR FunFam; 3.40.970.10:FF:000001; Ribonuclease H1; 1.
DR Gene3D; 3.90.1170.40; Molybdopterin biosynthesis MoaE subunit; 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; IPR036563; MoaE_sf.
DR InterPro; IPR003448; Mopterin_biosynth_MoaE.
DR InterPro; IPR041084; Ncstrn_small.
DR InterPro; IPR009027; Ribosomal_bL9/RNase_H1_N.
DR InterPro; IPR026140; Ribosomal_mS26.
DR InterPro; IPR050092; RNase_H.
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; PF02391; MoaE; 1.
DR Pfam; PF14943; MRP-S26; 1.
DR Pfam; PF18266; Ncstrn_small; 1.
DR Pfam; PF00075; RNase_H; 1.
DR SUPFAM; SSF55658; L9 N-domain-like; 1.
DR SUPFAM; SSF54690; Molybdopterin synthase subunit MoaE; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Reference proteome {ECO:0000313|Proteomes:UP000887561}.
FT DOMAIN 349..495
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT COILED 114..178
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 446..473
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 651 AA; 75285 MW; F5DBFE92564F8F26 CRC64;
MGTTRDTFED KIVKQLEYEA YNDMAFSEMS KLCKEVRNKI PTIERICICH RLGDDQMQIP
TKMELYEVKQ AEWTAPEDVA DLFWRRIVYN SAILSMRRIF REEYEASPTG FNAIQIKKEA
NEELDRLIEE NEKRNKDLAD ARVKREKEVI ERLEEETLLE IERRLDRETE KAAIKTEQIL
SLIEQSKNFI TKENLDEKVR EALENPINLD YAIDLNGAKI ENVQPQKCFE GIKATQRGRA
FDHQPGYTLR KLDTIVRLVL MPKFYAVARG WQTGIYKTWS ECQKHVLKFP RASYKKFESE
EEAKEFIEKN GVTSIPQLRQ VKRVAKTKTK LNLPVCEPDK INEFGLIMKD GVPVVYTDGA
CSNNGSFGSK AGIGVYWGDD HKWNISAPIT GRATNNVAEY TAIIFAMEKA ISEGLSSLLI
RTDSRLIISS MNLWIRKWKQ NDWKTYEGND VKNRDLLERI DELKKQIHVL FEKVHGHSGD
YCNDQADKLA KEANGGYLRE EIVFELTPLE FYCTRILNGT DSVGCQSNKN GNTGVIIEIS
NPKVIDEIVK ELPLRIQNLI VLIDINNLDS KLIEAVQTNE NVQGIILFYR GEKLPKTFYK
SEQQHCQRWN SLGAISTNGL RFKNFDIPIF FIENQTQIDI LTEKNQAWLS Y
//