(data stored in ACNUC7421 zone)

SWISSPROT: C4KK90_SULIK

ID   C4KK90_SULIK            Unreviewed;       212 AA.
AC   C4KK90;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   16-JAN-2019, entry version 56.
DE   RecName: Full=Ribonuclease HII {ECO:0000256|HAMAP-Rule:MF_00052};
DE            Short=RNase HII {ECO:0000256|HAMAP-Rule:MF_00052};
DE            EC=3.1.26.4 {ECO:0000256|HAMAP-Rule:MF_00052};
GN   Name=rnhB {ECO:0000256|HAMAP-Rule:MF_00052};
GN   OrderedLocusNames=M164_0197 {ECO:0000313|EMBL:ACR40831.1};
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118 {ECO:0000313|EMBL:ACR40831.1, ECO:0000313|Proteomes:UP000001479};
RN   [1] {ECO:0000313|EMBL:ACR40831.1, ECO:0000313|Proteomes:UP000001479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3 {ECO:0000313|Proteomes:UP000001479};
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
CC       DNA hybrids. {ECO:0000256|HAMAP-Rule:MF_00052,
CC       ECO:0000256|RuleBase:RU003515}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.;
CC         EC=3.1.26.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00052,
CC         ECO:0000256|RuleBase:RU003515};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00052};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00052};
CC       Note=Manganese or magnesium. Binds 1 divalent metal ion per
CC       monomer in the absence of substrate. May bind a second metal ion
CC       after substrate binding. {ECO:0000256|HAMAP-Rule:MF_00052};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00052}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000256|HAMAP-
CC       Rule:MF_00052, ECO:0000256|RuleBase:RU003515}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001402; ACR40831.1; -; Genomic_DNA.
DR   EnsemblBacteria; ACR40831; ACR40831; M164_0197.
DR   KEGG; sid:M164_0197; -.
DR   HOGENOM; HOG000100289; -.
DR   KO; K03470; -.
DR   OMA; REECRFF; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
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   Gene3D; 1.10.10.460; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00052_A; RNase_HII_A; 1.
DR   InterPro; IPR004649; RNase_H2_suA.
DR   InterPro; IPR001352; RNase_HII/HIII.
DR   InterPro; IPR024567; RNase_HII/HIII_dom.
DR   InterPro; IPR020787; RNase_HII_arc.
DR   InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10954; PTHR10954; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   TIGRFAMs; TIGR00729; TIGR00729; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KK90.
DR   SWISS-2DPAGE; C4KK90.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001479};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00052};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|RuleBase:RU003515};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|RuleBase:RU003515, ECO:0000313|EMBL:ACR40831.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00052};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00052};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|RuleBase:RU003515}.
FT   DOMAIN        3    193       RNase_HII. {ECO:0000259|Pfam:PF01351}.
FT   METAL         6      6       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00052}.
FT   METAL         7      7       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00052}.
FT   METAL       103    103       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00052}.
SQ   SEQUENCE   212 AA;  23924 MW;  9449817A0610860B CRC64;
     MRIGIDEAGR GALIGPMIVA GVAISDSKLK FLKGIGVKDS KQLTRERREK LFDIIASTVD
     AFTVVKVFPY EIDNYNLNDL TYDAVSKIIL SLSVFNPEIV TVDKVGEEKP VIELIRKLGY
     KSNVVHKADV LFVEASAASI IAKVIRDNYI DELKKVYGDF GSGYPADPRT IKWLKSFYEK
     NPNPPPIVRR SWKILRSTAP LYYISKEGRR LW
//

If you have problems or comments...

PBIL Back to PBIL home page