(data stored in ACNUC7421 zone)

SWISSPROT: SYP_ANADF

ID   SYP_ANADF               Reviewed;         575 AA.
AC   A7H7J7;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   11-DEC-2019, entry version 76.
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=Anae109_0478;
OS   Anaeromyxobacter sp. (strain Fw109-5).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter;
OC   unclassified Anaeromyxobacter.
OX   NCBI_TaxID=404589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fw109-5;
RX   PubMed=25614562; DOI=10.1128/genomea.01449-14;
RA   Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA   Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA   Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA   Loeffler F.E., Fields M.W.;
RT   "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT   metal-reducing bacterium isolated from a contaminated subsurface
RT   environment.";
RL   Genome Announc. 3:0-0(2015).
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:0000255|HAMAP-Rule:MF_01569}.
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:0000255|HAMAP-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 domain, the
CC       editing domain and the C-terminal anticodon-binding domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}.
DR   EMBL; CP000769; ABS24693.1; -; Genomic_DNA.
DR   RefSeq; WP_011984799.1; NC_009675.1.
DR   SMR; A7H7J7; -.
DR   STRING; 404589.Anae109_0478; -.
DR   EnsemblBacteria; ABS24693; ABS24693; Anae109_0478.
DR   KEGG; afw:Anae109_0478; -.
DR   eggNOG; ENOG4105C90; Bacteria.
DR   eggNOG; COG0442; LUCA.
DR   HOGENOM; HOG000076893; -.
DR   KO; K01881; -.
DR   OMA; QESGRWD; -.
DR   OrthoDB; 665824at2; -.
DR   BioCyc; ASP404589:G1G9J-489-MONOMER; -.
DR   Proteomes; UP000006382; 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; A7H7J7.
DR   SWISS-2DPAGE; A7H7J7.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..575
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000069118"
SQ   SEQUENCE   575 AA;  63091 MW;  8899C540647D9ECD CRC64;
     MPVVRLSQAF VPTLKEAPAD AQVASHKLLV RAGFIRQLGA GIYDYLPLAK RTLAKIEAIV
     REEMDAIGGQ EFYLPALHPA EIWKESGRWE VMGDNMFRLK DRKNGDYCLG MTHEEIFTAI
     ARDELRSYRQ LPQVWYQIQT KFRDEPRPKS GLLRVRQFTM KDAYSFDVDR AGLDKSYEDQ
     RRAYERIFTR CGLDFVAVQA HSGAMGGSES SEFMVRTDAG EDLVAACPRC RYAANTETAT
     SRLASEQDGA GLPKPEKFAT PGVVTIEALE QPPYGVAARR QLKTLVYVAD EKLVVAVVRG
     DQELNEAKLQ TATGAQVIRP AHPEEIPSLM GARAGSLGAV GFSRAKVFVD PSLADRKDMV
     TGANEDGFHL RGVEVRRDVL TGPHATVAEL RTVRAGEGCP RCDGTLDVFK ALEVGHIFKL
     GTKYSESMKA TVLDADGKAV PIVMGSYGIG VERIMAAAIE LHHDELGIRW PPAIAPFQAT
     VLTLGPEPEL KKAADELVKA LSDAGLEVLH DDREERAGVK FKDADLVGIP LRISVGKKGL
     AEGKVEWKLR GDKAVELVPL AEVARRAAEH VRAGR
//

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