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Entry: SYP_STRSV
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ID   SYP_STRSV               Reviewed;         616 AA.
AC   A3CQI5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   03-SEP-2014, entry version 56.
DE   RecName: Full=Proline--tRNA ligase;
DE            EC=6.1.1.15;
DE   AltName: Full=Prolyl-tRNA synthetase;
DE            Short=ProRS;
GN   Name=proS; OrderedLocusNames=SSA_2069;
OS   Streptococcus sanguinis (strain SK36).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=388919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SK36;
RX   PubMed=17277061; DOI=10.1128/JB.01808-06;
RA   Xu P., Alves J.M., Kitten T., Brown A., Chen Z., Ozaki L.S.,
RA   Manque P., Ge X., Serrano M.G., Puiu D., Hendricks S., Wang Y.,
RA   Chaplin M.D., Akan D., Paik S., Peterson D.L., Macrina F.L.,
RA   Buck G.A.;
RT   "Genome of the opportunistic pathogen Streptococcus sanguinis.";
RL   J. Bacteriol. 189:3166-3175(2007).
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a
CC       two-step reaction: proline is first activated by ATP to form Pro-
CC       AMP and then transferred to the acceptor end of tRNA(Pro). As
CC       ProRS can inadvertently accommodate and process non-cognate amino
CC       acids such as alanine and cysteine, to avoid such errors it has
CC       two additional distinct editing activities against alanine. One
CC       activity is designated as 'pretransfer' editing and involves the
CC       tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other
CC       activity is designated 'posttransfer' editing and involves
CC       deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-
CC       tRNA(Pro) is not edited by ProRS (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
CC       diphosphate + L-prolyl-tRNA(Pro).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic
CC       domain, the editing domain and the C-terminal anticodon-binding
CC       domain (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 1 subfamily.
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DR   EMBL; CP000387; ABN45440.1; -; Genomic_DNA.
DR   RefSeq; WP_011837531.1; NC_009009.1.
DR   RefSeq; YP_001035990.1; NC_009009.1.
DR   ProteinModelPortal; A3CQI5; -.
DR   SMR; A3CQI5; 1-614.
DR   STRING; 388919.SSA_2069; -.
DR   EnsemblBacteria; ABN45440; ABN45440; SSA_2069.
DR   GeneID; 4806247; -.
DR   KEGG; ssa:SSA_2069; -.
DR   PATRIC; 19771055; VBIStrSan33173_1962.
DR   eggNOG; COG0442; -.
DR   HOGENOM; HOG000076893; -.
DR   KO; K01881; -.
DR   OMA; MHQAYCN; -.
DR   OrthoDB; EOG6TTVMR; -.
DR   BioCyc; SSAN388919:GHEN-2041-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 3.40.50.800; -; 1.
DR   Gene3D; 3.90.960.10; -; 1.
DR   HAMAP; MF_01569; Pro_tRNA_synth_type1; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb_cons-dom.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR   InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR   PANTHER; PTHR11451:SF3; PTHR11451:SF3; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF04073; tRNA_edit; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF52954; SSF52954; 1.
DR   SUPFAM; SSF55826; SSF55826; 1.
DR   TIGRFAMs; TIGR00409; proS_fam_II; 2.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    616       Proline--tRNA ligase.
FT                                /FTId=PRO_0000288383.
SQ   SEQUENCE   616 AA;  68571 MW;  211961C324AC567F CRC64;
     MKQSKMLIPT LREMPSDAQV ISHALMLRAG YVRQVSAGVY SYLPLANRVI EKAKRIMREE
     FDKIGAVEML APALLSADLW RESGRYETYG EDLYKLKNRE KSDFILGPTH EETFTAIVRD
     SVKSYKQLPL NLYQIQPKYR DEKRPRNGLL RTREFIMKDA YSFHANYDSL DVAYDEYKSA
     YEKIFTRSEL DFKAIIGDGG AMGGKDSQEF MAITPDRTDL NRWVVLDKSV ASFDEIPEDV
     QEAIRTELTS WMVSGEDTIA YSSESSYAAN LEMATDEYKP AGRVVTEEEV ARVSTPDCKT
     IDEVAAFLGL DESQTIKTLV YMADESPVVA LLVGNDQLNE VKLKNHLAAD FFDVASEDQV
     RQLLGAGFGS LGPVNLPEGV RIIADRKVQD LANAVVGANE DGYHLTGVNP GRDFTAEFVD
     IREVREGEIS PDGQGVLKFA RGIEIGHIFK LGTRYSDSMN ANVLDENGRA VPMIMGCYGI
     GVSRLLSAVM EQHARLFVNK TPKGEFRYAW GINFPKELAP FDVHLIPVNV KDEEALALTD
     QIEANLLSAG YEVLVDDRNE RAGVKFSDSD LIGLPIRVTV GKKAAEGIVE VKIKATGDTI
     EVHADNLLET LSILTK
//
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