(data stored in SCRATCH zone)

SWISSPROT: E3J8K6_FRAIE

ID   E3J8K6_FRAIE            Unreviewed;       468 AA.
AC   E3J8K6;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   16-JAN-2019, entry version 48.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01571};
DE            EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01571};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01571};
DE            Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01571};
GN   Name=proS {ECO:0000256|HAMAP-Rule:MF_01571};
GN   OrderedLocusNames=FraEuI1c_0363 {ECO:0000313|EMBL:ADP78449.1};
OS   Frankia inefficax (strain DSM 45817 / CECT 9037 / EuI1c).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298654 {ECO:0000313|EMBL:ADP78449.1, ECO:0000313|Proteomes:UP000002484};
RN   [1] {ECO:0000313|EMBL:ADP78449.1, ECO:0000313|Proteomes:UP000002484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45817 / CECT 9037 / EuI1c
RC   {ECO:0000313|Proteomes:UP000002484};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA   Beauchemin N., Sen A., Sur S.A., Gtari M., Wall L., Tisa L., Woyke T.;
RT   "Complete sequence of Frankia sp. EuI1c.";
RL   Submitted (OCT-2010) 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).
CC       {ECO:0000256|HAMAP-Rule:MF_01571}.
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_01571};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01571}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic
CC       domain, the anticodon-binding domain and the C-terminal extension.
CC       {ECO:0000256|HAMAP-Rule:MF_01571}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family. ProS type 3 subfamily. {ECO:0000256|HAMAP-Rule:MF_01571}.
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DR   EMBL; CP002299; ADP78449.1; -; Genomic_DNA.
DR   RefSeq; WP_013421572.1; NC_014666.1.
DR   STRING; 298654.FraEuI1c_0363; -.
DR   EnsemblBacteria; ADP78449; ADP78449; FraEuI1c_0363.
DR   KEGG; fri:FraEuI1c_0363; -.
DR   eggNOG; ENOG4107R1M; Bacteria.
DR   eggNOG; COG0442; LUCA.
DR   HOGENOM; HOG000167538; -.
DR   KO; K01881; -.
DR   OMA; EVYWVTH; -.
DR   OrthoDB; 665824at2; -.
DR   BioCyc; FSP298654:G1GOT-364-MONOMER; -.
DR   Proteomes; UP000002484; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd00778; ProRS_core_arch_euk; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR   InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR   InterPro; IPR033721; ProRS_core_arch_euk.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; E3J8K6.
DR   SWISS-2DPAGE; E3J8K6.
KW   Aminoacyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01571,
KW   ECO:0000313|EMBL:ADP78449.1};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01571};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002484};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01571};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01571, ECO:0000313|EMBL:ADP78449.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01571};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01571};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002484}.
FT   DOMAIN       31    280       AA_TRNA_LIGASE_II. {ECO:0000259|PROSITE:
FT                                PS50862}.
SQ   SEQUENCE   468 AA;  51114 MW;  CE95AD596C4013D6 CRC64;
     MAVLTLRSDD FPRWYQDVIA KAELADNGPV RGSMVIRPYG YSLWERMQAD VDARIKAAGA
     VNAYFPLFIP ESYLRREAEH VEGFSPELAV VTHGGGKELE EPVVVRPTSE TVIGEYMAKW
     TQSYRDLPLL LNQWANVVRW ELRPRLFLRT SEFLWQEGHT AHADGPDAAA YARRIALEVY
     QDFMVSVLAM PVFVGRKTRK ERFAGAINTL TCEGMMGDGK ALQMATSHEL GQNFARAFDI
     DYLGADGARH LAWTTSWGSS TRMVGGLIMA HGDDAGLRVP PRLAPTQVVV LPVRDDEKVV
     ATATQIADAL KAAGVRATLD ARPGLSFGRR VTDWELKGAP VRVEVGPRDL AVGNVTLARR
     DTGEKITVPL AEAAARVPAL LDDVQAGLYQ QALALRDSRT ADVTSLADAI EAAATGFARL
     PWRLVGDEGE ARLAAESLTV RCIQNADGTL PTGTDDTDDL VCLVARAY
//

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