(data stored in ACNUC1104 zone)

SWISSPROT: D3UWI0_XENBS

ID   D3UWI0_XENBS            Unreviewed;       573 AA.
AC   D3UWI0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 69.
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:CBJ79754.1};
GN   OrderedLocusNames=XBJ1_0610 {ECO:0000313|EMBL:CBJ79754.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79754.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79754.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79754.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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. {ECO:0000256|HAMAP-
CC       Rule:MF_01569, ECO:0000256|SAAS:SAAS00761654}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-
CC         prolyl-tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700,
CC         Rhea:RHEA-COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:60039, ChEBI:CHEBI:78442, ChEBI:CHEBI:78532,
CC         ChEBI:CHEBI:456215; EC=6.1.1.15; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01569, 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
CC       domain, the editing domain and the C-terminal anticodon-binding
CC       domain. {ECO:0000256|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01569,
CC       ECO:0000256|SAAS:SAAS00632846}.
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DR   EMBL; FN667741; CBJ79754.1; -; Genomic_DNA.
DR   RefSeq; WP_012987208.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0610; -.
DR   EnsemblBacteria; CBJ79754; CBJ79754; XBJ1_0610.
DR   GeneID; 8830232; -.
DR   KEGG; xbo:XBJ1_0610; -.
DR   PATRIC; fig|406818.4.peg.563; -.
DR   eggNOG; ENOG4105C90; Bacteria.
DR   eggNOG; COG0442; LUCA.
DR   HOGENOM; HOG000076893; -.
DR   KO; K01881; -.
DR   OMA; QESGRWD; -.
DR   BioCyc; XBOV406818:XBJ1_RS02660-MONOMER; -.
DR   Proteomes; UP000002045; 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   PIRSF; PIRSF001535; ProRS_1; 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; D3UWI0.
DR   SWISS-2DPAGE; D3UWI0.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682373, ECO:0000313|EMBL:CBJ79754.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682365};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00632883};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01569,
KW   ECO:0000256|SAAS:SAAS00682366, ECO:0000313|EMBL:CBJ79754.1};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN       32    468       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   573 AA;  64156 MW;  42DEFCAA9C311648 CRC64;
     MRTSQYLLST LKETPADAEV VSHKLMLRAG MTRKLASGLY NWMPTGVRVL KKVENIVREE
     MNNAGAIEVS MPVVQPADLW QESGRWEQYG PELLRFEDRG ARPFVLGPTH EEVITDLVRN
     EVTSYKQLPL NLFQIQTKFR DEVRPRFGVM RSREFIMKDA YSFHTSQESL QETYDKMYDA
     YSKIFTRIGL DFRAVLADTG SIGGSASHEF QVLADSGEDD IAFSTESNYA ANIELAEAVM
     PSHERAVPSE DMHLVETPNA KTIAELVEQF NLPIEKTVKT LIVHAAKESS HQLVALLVRG
     DHELNEIKAE KLPLVASPLS FATEEEIRAV VQAGPGSLGP VNLPMPVIID RSVSVMSDFG
     AGANVDDKHY FGINWERDLP LPEIADIRNV LEGDASPDGQ GTLLIKRGIE VGHIFQLGTK
     YSDALKATVQ NEDGHNQVVS MGCYGIGVTR IVAAAIEQNH DDRGIIWPDA IAPFQVALLP
     MNMHKSYRVK EVAEKLYADL RANGIDVIFD DRKERPGVMF ADMELIGVPH TLVIGDRNLD
     NGEVEYKYRR NGDKQMLKLE GIIEYLKEQI KQH
//

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