(data stored in SCRATCH zone)

SWISSPROT: C6B2P4_RHILS

ID   C6B2P4_RHILS            Unreviewed;       229 AA.
AC   C6B2P4;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 64.
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=Rleg_0560 {ECO:0000313|EMBL:ACS54864.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54864.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54864.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54864.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA-
CC       DNA hybrids. {ECO:0000256|HAMAP-Rule:MF_00052,
CC       ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS00728525}.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
CC       phosphomonoester. {ECO:0000256|HAMAP-Rule:MF_00052,
CC       ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS00728538}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00728495};
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       ECO:0000256|SAAS:SAAS00728638}.
CC   -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000256|HAMAP-
CC       Rule:MF_00052, ECO:0000256|RuleBase:RU003515,
CC       ECO:0000256|SAAS:SAAS00728574}.
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DR   EMBL; CP001622; ACS54864.1; -; Genomic_DNA.
DR   RefSeq; WP_012756244.1; NC_012850.1.
DR   ProteinModelPortal; C6B2P4; -.
DR   EnsemblBacteria; ACS54864; ACS54864; Rleg_0560.
DR   KEGG; rlg:Rleg_0560; -.
DR   HOGENOM; HOG000100288; -.
DR   KO; K03470; -.
DR   OMA; NILHASM; -.
DR   OrthoDB; POG091H011N; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-HAMAP.
DR   CDD; cd07182; RNase_HII_bacteria_HII_like; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_00052_B; RNase_HII_B; 1.
DR   InterPro; IPR022898; RNase_HII.
DR   InterPro; IPR001352; RNase_HII/HIII.
DR   InterPro; IPR024567; RNase_HII/HIII_dom.
DR   InterPro; IPR012337; RNaseH-like_dom.
DR   PANTHER; PTHR10954; PTHR10954; 1.
DR   PANTHER; PTHR10954:SF15; PTHR10954:SF15; 1.
DR   Pfam; PF01351; RNase_HII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B2P4.
DR   SWISS-2DPAGE; C6B2P4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|SAAS:SAAS00728481};
KW   Endonuclease {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS00728608};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS00728599,
KW   ECO:0000313|EMBL:ACS54864.1};
KW   Manganese {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|SAAS:SAAS00728488};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|SAAS:SAAS00728620};
KW   Nuclease {ECO:0000256|HAMAP-Rule:MF_00052,
KW   ECO:0000256|RuleBase:RU003515, ECO:0000256|SAAS:SAAS00728548}.
FT   DOMAIN       37    212       RNase_HII. {ECO:0000259|Pfam:PF01351}.
FT   METAL        40     40       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00052}.
FT   METAL        41     41       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00052}.
FT   METAL       131    131       Divalent metal cation.
FT                                {ECO:0000256|HAMAP-Rule:MF_00052}.
SQ   SEQUENCE   229 AA;  24483 MW;  5D2F6032F395FB33 CRC64;
     MKPRTSPDSP LLFDTAPLVP DFRLELKARK AGHWPVAGAD EAGRGPLAGP VVAAAVILDP
     RRIPEGLNDS KQLSAQRREE LFVQILATAT VSIASSSSTR IDETDIRKAS LDAMRRAICS
     LAIPASYVLT DGLDVPPGLD CPGQAVVKGD ARSVSIAAAS IVAKVTRDRM MARAHSVFPD
     YGFAAHVGYG TAQHRAGIER HGPCSLHRMS FRPLRKTEGA PETDELLSE
//

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