(data stored in SCRATCH zone)

SWISSPROT: C6B2J4_RHILS

ID   C6B2J4_RHILS            Unreviewed;       506 AA.
AC   C6B2J4;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 61.
DE   RecName: Full=Histidine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00127};
DE            EC=6.1.1.21 {ECO:0000256|HAMAP-Rule:MF_00127};
DE   AltName: Full=Histidyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00127};
DE            Short=HisRS {ECO:0000256|HAMAP-Rule:MF_00127};
GN   Name=hisS {ECO:0000256|HAMAP-Rule:MF_00127};
GN   OrderedLocusNames=Rleg_0509 {ECO:0000313|EMBL:ACS54814.1};
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:ACS54814.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54814.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54814.1,
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   -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP +
CC       diphosphate + L-histidyl-tRNA(His). {ECO:0000256|HAMAP-
CC       Rule:MF_00127, ECO:0000256|SAAS:SAAS00359674}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00127,
CC       ECO:0000256|SAAS:SAAS00742603}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127,
CC       ECO:0000256|SAAS:SAAS00808017}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. {ECO:0000256|HAMAP-Rule:MF_00127,
CC       ECO:0000256|SAAS:SAAS00676298}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001622; ACS54814.1; -; Genomic_DNA.
DR   RefSeq; WP_012756200.1; NC_012850.1.
DR   EnsemblBacteria; ACS54814; ACS54814; Rleg_0509.
DR   KEGG; rlg:Rleg_0509; -.
DR   HOGENOM; HOG000018071; -.
DR   KO; K01892; -.
DR   OMA; CDFDFIG; -.
DR   OrthoDB; POG091H021E; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   CDD; cd00859; HisRS_anticodon; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_00127; His_tRNA_synth; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR015807; His-tRNA-ligase.
DR   InterPro; IPR004516; HisRS/HisZ.
DR   InterPro; IPR033656; HisRS_anticodon.
DR   PANTHER; PTHR11476; PTHR11476; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF52954; SSF52954; 1.
DR   TIGRFAMs; TIGR00442; hisS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B2J4.
DR   SWISS-2DPAGE; C6B2J4.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS00502864, ECO:0000313|EMBL:ACS54814.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS00502908};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS00808019};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS00502874, ECO:0000313|EMBL:ACS54814.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS00502847};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00127,
KW   ECO:0000256|SAAS:SAAS00502923}.
FT   DOMAIN       31    381       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   506 AA;  55641 MW;  0EF73909CB4C4170 CRC64;
     MNDKQKKPQK LKARLPRGFV DRTAGDIRAV NEMTAKIREV YEHYGFDPLE TPLFEYTDAL
     GKFLPDSDRP NEGVFSLQDD DEQWMSLRYD LTAPLARHVA ENFNEIQLPY RTYRAGYVFR
     NEKPGPGRFR QFMQFDADTV GAPGVQADAE MCMMMADTLE ALGIKRGDYL IRVNNRKVLD
     GVLEAIGLGG DDKAGQRLNV LRAIDKLDKF GPEGVALLLG PGRKDESGDF TKGAGLDKEQ
     IDKVLFFVGI TDYAESVARL AELVAGTARG GEGVDELNFI GALVTSAGYG PDRIKIDPSV
     VRGLEYYTGP VYEAELTFDV TNEKGEKVVF GSVGGGGRYD GLVSRFMGQP VPATGFSIGV
     SRLMTALKNL GKLGASEVIE PVLVTVMDGD VEAMGRYQKM TQELRAAGIR AEMFQGNWKK
     FGNQLKYADR RGCPVAIIQG GDERATSVVQ IKDLIEGKRL SGEIEDNASW REARVAQETV
     PEADLVAKVR EILAAQAEDR KRAANV
//

If you have problems or comments...

PBIL Back to PBIL home page