(data stored in ACNUC9435 zone)

SWISSPROT: SYP2_CLOD6

ID   SYP2_CLOD6              Reviewed;         481 AA.
AC   Q18CD7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=Proline--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_01571};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571};
DE   AltName: Full=Prolyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01571};
DE            Short=ProRS 2 {ECO:0000255|HAMAP-Rule:MF_01571};
GN   Name=proS2 {ECO:0000255|HAMAP-Rule:MF_01571};
GN   OrderedLocusNames=CD630_00500;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
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). {ECO:0000255|HAMAP-
CC       Rule:MF_01571}.
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_01571};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       anticodon-binding domain and the C-terminal extension.
CC       {ECO:0000255|HAMAP-Rule:MF_01571}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571}.
DR   EMBL; AM180355; CAJ66864.1; -; Genomic_DNA.
DR   RefSeq; WP_009895182.1; NZ_CP010905.2.
DR   RefSeq; YP_001086513.1; NC_009089.1.
DR   SMR; Q18CD7; -.
DR   STRING; 272563.CD630_00500; -.
DR   EnsemblBacteria; CAJ66864; CAJ66864; CD630_00500.
DR   GeneID; 4916662; -.
DR   KEGG; cdf:CD630_00500; -.
DR   KEGG; pdc:CDIF630_00113; -.
DR   PATRIC; fig|272563.120.peg.54; -.
DR   eggNOG; ENOG4105C90; Bacteria.
DR   eggNOG; COG0442; LUCA.
DR   HOGENOM; HOG000167538; -.
DR   KO; K01881; -.
DR   OMA; EVYWVTH; -.
DR   Proteomes; UP000001978; 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; 3.30.110.30; -; 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; IPR017449; Pro-tRNA_synth_II.
DR   InterPro; IPR033721; ProRS_core_arch_euk.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF09180; ProRS-C_1; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   SUPFAM; SSF64586; SSF64586; 1.
DR   TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q18CD7.
DR   SWISS-2DPAGE; Q18CD7.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..481
FT                   /note="Proline--tRNA ligase 2"
FT                   /id="PRO_0000288406"
SQ   SEQUENCE   481 AA;  55146 MW;  DB35FDC8BADC924A CRC64;
     MAKNEKQFVE EITKMEDDFP QWYTDVITKT DLVDYAPVKG FMVVKPYGYA LWEKMQEFMD
     KKFKETGHKN CYFPLLIPES LLNKEAEHVE GFAPEVAWVT HGGNKKLEER LCVRPTSETI
     ICTMYAKWLK SYRELPYLYN QWCSVVRWEK STRPFLRTSE FLWQEGHTLH ETAEEAQEET
     IQQLEVYKAL CEELLAMPVV AGQKSESEKF AGGERTYTIE AMMHDGKALQ SGTSHFLGQH
     FTKAFDITFA DREGNLANPY HTSWGASTRL IGGLIMTHSD NRGLVLPPRV APIQVVIVPI
     AAKKGNVMET VDKIYADLKA KGVAVEVDDR DNYTTGWKFN EWEMKGVPVR VEIGPKDIEN
     NQAMVFRRDT LEKDSMPLEG LADAICDLFD VIHNDMFEKA RKHREDNTSI VENMDEFRKA
     LEEKPGFIKT MWCGDAECEA KIKEETGATI RCLPFEQENL GHKCVYCGKE ADSMVVMAKA
     Y
//

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