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Database: UniProt
Entry: A0A915N266_MELJA
LinkDB: A0A915N266_MELJA
Original site: A0A915N266_MELJA 
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
//
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