ID A0A2A2JJ70_9BILA Unreviewed; 790 AA.
AC A0A2A2JJ70;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Ribonuclease {ECO:0000256|RuleBase:RU003515};
DE EC=3.1.26.4 {ECO:0000256|RuleBase:RU003515};
GN ORFNames=WR25_11139 {ECO:0000313|EMBL:PAV61717.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV61717.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV61717.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV61717.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-DNA
CC hybrids. {ECO:0000256|RuleBase:RU003515}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-(alpha-D-glucosaminyl)-(1-octadecanoyl,2-(9Z)-octadecenoyl-
CC sn-glycero-3-phospho)-1D-myo-inositol(in) = 6-(alpha-D-glucosaminyl)-
CC (1-octadecanoyl,2-(9Z)-octadecenoyl-sn-glycero-3-phospho)-1D-myo-
CC inositol(out); Xref=Rhea:RHEA:71495, ChEBI:CHEBI:190691;
CC Evidence={ECO:0000256|ARBA:ARBA00036810};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU01319,
CC ECO:0000256|RuleBase:RU003515};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out);
CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880;
CC Evidence={ECO:0000256|ARBA:ARBA00035895};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000256|ARBA:ARBA00024631};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000256|ARBA:ARBA00024615};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-
CC myo-inositol(in) = an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-
CC phospho)-1D-myo-inositol(out); Xref=Rhea:RHEA:71491,
CC ChEBI:CHEBI:57997; Evidence={ECO:0000256|ARBA:ARBA00036071};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the CLPTM1 family.
CC {ECO:0000256|ARBA:ARBA00009310}.
CC -!- SIMILARITY: Belongs to the RNase HII family.
CC {ECO:0000256|RuleBase:RU003515}.
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:PAV61717.1}.
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DR EMBL; LIAE01010401; PAV61717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2JJ70; -.
DR STRING; 2018661.A0A2A2JJ70; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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 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; IPR008429; CLPTM1.
DR InterPro; IPR004649; RNase_H2_suA.
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 NCBIfam; TIGR00729; ribonuclease HII; 1.
DR PANTHER; PTHR21347; CLEFT LIP AND PALATE ASSOCIATED TRANSMEMBRANE PROTEIN-RELATED; 1.
DR PANTHER; PTHR21347:SF0; CLEFT LIP AND PALATE TRANSMEMBRANE PROTEIN 1-LIKE PROTEIN; 1.
DR Pfam; PF05602; CLPTM1; 1.
DR Pfam; PF01351; RNase_HII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS51975; RNASE_H_2; 1.
PE 3: Inferred from homology;
KW Endonuclease {ECO:0000256|PROSITE-ProRule:PRU01319,
KW ECO:0000256|RuleBase:RU003515};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU01319,
KW ECO:0000256|RuleBase:RU003515};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01319};
KW Nuclease {ECO:0000256|PROSITE-ProRule:PRU01319,
KW ECO:0000256|RuleBase:RU003515};
KW Reference proteome {ECO:0000313|Proteomes:UP000218231};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 531..551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 572..588
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 594..612
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 647..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 679..698
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 23..250
FT /note="RNase H type-2"
FT /evidence="ECO:0000259|PROSITE:PS51975"
FT REGION 768..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 29
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 30
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
FT BINDING 140
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01319"
SQ SEQUENCE 790 AA; 89510 MW; 96AA87E353138C60 CRC64;
MSAETNDSIQ RSPTWNGFAE REPCVLGIDE AGRGPVLGPM VYGCAVSPLS QAEQLKALGV
ADSKQLTEEK RGKIFKRMES DEQTQGVVAY ALRSLSPQYI SCSMLKRAKF SLNEISHSAA
IALIRDALSA GINVVEIKVD TVGPKATYQA KLESIFPGIS ITVTEKADSL FPVVSAASIA
AKVTRDRSLR DWAFAEKNVK VPKEGWGSGY PGDPTTKKFL QESVDPVFGY SGLAKMGIFS
ISNLITVVFI GYMSHSMYDL YTLLTPKECT SSTRHCLKPK FSPDKDGLFP PLQLRVYVSK
SERELGSLLF STKDFQLAWE FEKKVNFEFN FFFKCIFQVN LTLTPTMRRN STKIFAQAIF
LPNDYSHDQP FQGPWYETKI DSMIVYQPPI PETFNLMQKD EQKKIEEKMS KEKPVPHFRS
VLPLVASKDP VSFDLALMSN MIRGLISTDR EDSSKYMPFI MIDTLSMRSK DLVELKSTTE
QVELSIHYRP VSMAKYLLLA HMGVACSQVK QMGFGEKDVD QIKSLFVDTN VYLIGATFVV
SALHLLFDIL SFKNDISFWR AKRTMVGIST KALLWKVFSY TVLFFHLFEE NTSLLVVIPM
GVSALIEYWK AIKAFKISFS ISGGIKFGEH SKDEVETEQL DNQAMKYLSY LMAPLCIGGA
IYSLAYIPHK SWRSWVLESL ANGIYAFGFL FMLPQLFLNY KLKSVAHLPW RAFMYKAFNT
FIDDLFAFVI TMPTAHRIAC FRDDVVFVIY LYQKWLYPVD YRRVNEFGQS GDENGDDKKS
GKSEKLKKEE
//
