(data stored in ACNUC7421 zone)

SWISSPROT: SYP_EDWI9

ID   SYP_EDWI9               Reviewed;         572 AA.
AC   C5B780;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 53.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569};
DE            Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569};
GN   Name=proS {ECO:0000255|HAMAP-Rule:MF_01569};
GN   OrderedLocusNames=NT01EI_0627;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-
CC       Rule:MF_01569}.
CC   -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP +
CC       diphosphate + L-prolyl-tRNA(Pro). {ECO:0000255|HAMAP-
CC       Rule:MF_01569}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic
CC       domain, the editing domain and the C-terminal anticodon-binding
CC       domain. {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}.
DR   EMBL; CP001600; ACR67854.1; -; Genomic_DNA.
DR   RefSeq; WP_015870051.1; NC_012779.2.
DR   SMR; C5B780; -.
DR   STRING; 634503.NT01EI_0627; -.
DR   PRIDE; C5B780; -.
DR   EnsemblBacteria; ACR67854; ACR67854; NT01EI_0627.
DR   GeneID; 7960393; -.
DR   KEGG; eic:NT01EI_0627; -.
DR   PATRIC; fig|634503.3.peg.569; -.
DR   eggNOG; ENOG4105C90; Bacteria.
DR   eggNOG; COG0442; LUCA.
DR   HOGENOM; HOG000076893; -.
DR   KO; K01881; -.
DR   OMA; IQPAELW; -.
DR   OrthoDB; POG091H0290; -.
DR   Proteomes; UP000001485; 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-KW.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.40.50.800; -; 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; 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; 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; SSF52954; SSF52954; 1.
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; C5B780.
DR   SWISS-2DPAGE; C5B780.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN         1    572       Proline--tRNA ligase.
FT                                /FTId=PRO_1000215528.
SQ   SEQUENCE   572 AA;  63414 MW;  3C2DEEFC7518EAC4 CRC64;
     MRTSQYLLST LKETPADAEV ISHQLMLRAG MIRKLASGLY TWLPTGLRVL NKVENIVREE
     MNYAGAIEVS MPVVQPADLW QESGRWEQYG PELLRFVDRG DRPFVLGPTH EEVITDLVRN
     EISSYKQLPL NFYQIQTKFR DEVRPRFGVM RSREFLMKDA YSFHTTQESL QETYEAMYAA
     YSRIFSRMGL DFRAVQADTG SIGGNASHEF QVLAQSGEDD IVFSTASDYA ANIELAEALA
     PATGRAAANQ PMQLVNTPDA RTIAELVEQH GLPIEKTVKT LLVHASEESG HALVALLVRG
     DHELNEVKAE KLALVASPLT FANEAEIRAL VNAGPGSLGP VNLPLPIVAD RAVAAMSDFG
     AGANIDGKHY FGINWERDAA LPQIADIRNV IEGDPSPDGK GTLLIKRGIE VGHIFQLGTK
     YTEALNATVQ GEDGRNQLMT MGCYGIGVTR VVAAAIEQNH DERGIIWPDA IAPFQVAILP
     MNMHKSFRVK EVAERLYDGL RAKGIEVLLD DRKERPGVMF ADMELIGIPH TIVIGDRNLD
     NNEIEYKYRR SGDKLMISVD EIEAFLQAQI AR
//

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