(data stored in ACNUC7421 zone)

SWISSPROT: D2RBU7_GARV4

ID   D2RBU7_GARV4            Unreviewed;       610 AA.
AC   D2RBU7;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   11-DEC-2019, entry version 70.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01569};
DE            EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01569};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01569};
DE            Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01569};
GN   Name=proS {ECO:0000256|HAMAP-Rule:MF_01569,
GN   ECO:0000313|EMBL:ADB13647.1};
GN   OrderedLocusNames=HMPREF0424_1079 {ECO:0000313|EMBL:ADB13647.1};
OS   Gardnerella vaginalis (strain 409-05).
OC   Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC   Gardnerella.
OX   NCBI_TaxID=553190 {ECO:0000313|EMBL:ADB13647.1, ECO:0000313|Proteomes:UP000001888};
RN   [1] {ECO:0000313|Proteomes:UP000001888}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=409-05 {ECO:0000313|Proteomes:UP000001888};
RX   PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA   Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M., Sutton G.,
RA   Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X., Gibbs R.A.,
RA   Leigh S.R., Stumpf R., White B.A., Highlander S.K., Nelson K.E.,
RA   Wilson B.A.;
RT   "Comparative genomics of Gardnerella vaginalis strains reveals substantial
RT   differences in metabolic and virulence potential.";
RL   PLoS ONE 5:E12411-E12411(2010).
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-
CC       step reaction: proline is first activated by ATP to form Pro-AMP and
CC       then transferred to the acceptor end of tRNA(Pro). As ProRS can
CC       inadvertently accommodate and process non-cognate amino acids such as
CC       alanine and cysteine, to avoid such errors it has two additional
CC       distinct editing activities against alanine. One activity is designated
CC       as 'pretransfer' editing and involves the tRNA(Pro)-independent
CC       hydrolysis of activated Ala-AMP. The other activity is designated
CC       'posttransfer' editing and involves deacylation of mischarged Ala-
CC       tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
CC       {ECO:0000256|HAMAP-Rule:MF_01569, ECO:0000256|SAAS:SAAS00761654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC         tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC         COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC         EC=6.1.1.15; Evidence={ECO:0000256|HAMAP-Rule:MF_01569,
CC         ECO:0000256|SAAS:SAAS01124670};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01569,
CC       ECO:0000256|SAAS:SAAS00632876}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01569,
CC       ECO:0000256|SAAS:SAAS00632870}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       editing domain and the C-terminal anticodon-binding domain.
CC       {ECO:0000256|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01569,
CC       ECO:0000256|SAAS:SAAS00632846}.
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DR   EMBL; CP001849; ADB13647.1; -; Genomic_DNA.
DR   RefSeq; WP_012914388.1; NC_013721.1.
DR   EnsemblBacteria; ADB13647; ADB13647; HMPREF0424_1079.
DR   GeneID; 29691725; -.
DR   KEGG; gva:HMPREF0424_1079; -.
DR   eggNOG; ENOG4105C90; Bacteria.
DR   eggNOG; COG0442; LUCA.
DR   HOGENOM; HOG000076893; -.
DR   KO; K01881; -.
DR   OMA; QESGRWD; -.
DR   BioCyc; GCF_000025205-HMP:HMPREF0424_RS05275-MONOMER; -.
DR   Proteomes; UP000001888; Chromosome.
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-UniRule.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00779; ProRS_core_prok; 1.
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.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
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; IPR033730; ProRS_core_prok.
DR   InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
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; SSF55826; SSF55826; 1.
DR   TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; D2RBU7.
DR   SWISS-2DPAGE; D2RBU7.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682373};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682365};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01569, ECO:0000256|SAAS:SAAS00632883};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01569, ECO:0000256|SAAS:SAAS00682366,
KW   ECO:0000313|EMBL:ADB13647.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682360};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682364}.
FT   DOMAIN          51..504
FT                   /note="AA_TRNA_LIGASE_II"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   610 AA;  67137 MW;  7EB72A62CFBCF763 CRC64;
     MNSNVLRMSQ LFLRTLREDP ADADVTSAKL MQRAGYIRKS APGVWTWLPL GLKVLNKVQA
     IIRDEINGIG AQEVHFPALL PREPYEATNR WEEYGDNIFR LKDRHQADYL LAPTHEEVFT
     LLVKDMYSSY KDLPVTLYQI QTKYRDEFRP RAGLIRGREF IMQDGYSFSI DEDGLKSAYV
     EERAAYARIF DRLGIKYVIV HAVSGPMGGS DSEEFLAPMP IGEDTFALAP SGKAWNVEAL
     TTPEMQDVDY SATPAAQSLE TPDAKTIEAL VKVSNDLHPR KDGREWQADD TLKNLIIAVK
     HPADAEGGEH EEPWREIVAI GIPGDRQVDM KRLEAQFAPA EIEEATEDDL KSHPEFVKGY
     IGFSVLGPQA RKEGRGIANP VRYLMDAHVA KGSAWITGAD EDGKHVYNAV YGRDFEADGV
     VEAAQVRDGD MSPDGSGPLS FERGVEIGQV FQLGLKYSKA LGLSVLNENG KAVPVWMGCY
     GIGVSRVIAC LAETHHDDAG LAWPMAIAPA QVHVVATGKD QVAFDAAEKV VEELSKQGIE
     VIFDDRPKVS PGVKFKDAEL VGVPLIAVAG RDTVNNGTIE IRDRNGSNVE AVPVDEAAAR
     IVERVSELLA
//

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