SYP1_CLOD6
ID SYP1_CLOD6 Reviewed; 571 AA.
AC Q18CD2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Proline--tRNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_01569};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569};
DE AltName: Full=Prolyl-tRNA synthetase 1 {ECO:0000255|HAMAP-Rule:MF_01569};
DE Short=ProRS 1 {ECO:0000255|HAMAP-Rule:MF_01569};
GN Name=proS1 {ECO:0000255|HAMAP-Rule:MF_01569};
GN OrderedLocusNames=CD630_00490;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; 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). 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}.
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DR EMBL; AM180355; CAJ66863.1; -; Genomic_DNA.
DR RefSeq; WP_009895180.1; NZ_CP010905.2.
DR RefSeq; YP_001086512.1; NC_009089.1.
DR AlphaFoldDB; Q18CD2; -.
DR SMR; Q18CD2; -.
DR STRING; 272563.CD630_00490; -.
DR EnsemblBacteria; CAJ66863; CAJ66863; CD630_00490.
DR KEGG; cdf:CD630_00490; -.
DR KEGG; pdc:CDIF630_00112; -.
DR PATRIC; fig|272563.120.peg.53; -.
DR eggNOG; COG0442; Bacteria.
DR OMA; NCDYAAN; -.
DR PhylomeDB; Q18CD2; -.
DR BioCyc; PDIF272563:G12WB-101-MON; -.
DR Proteomes; UP000001978; 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; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 2.
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; IPR045864; aa-tRNA-synth_II/BPL/LPL.
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; IPR044140; ProRS_anticodon_short.
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; SSF55681; SSF55681; 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;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..571
FT /note="Proline--tRNA ligase 1"
FT /id="PRO_0000288320"
SQ SEQUENCE 571 AA; 64400 MW; 2281503B4C0D44B8 CRC64;
MKMSKMFMPT LKEIPADAEI TSHQLMVRSG MIKKMTSGVY NQLPMGLRVF KKIEQIIREE
LNKKDCQEIL CAALLPSELW KESGRWTAMG EEMFRLKDRT EREYCLGPTH EEAFTDIIRQ
EITSYKQLPL NLYQIQVKYR DERRPRFGVM RTKTFTMKDA YSFDVDDKGL DKSYQDMFDA
YVSIFDRCGL ENSPVQADSG AIGGSTSAEF MVKSEVGEDE VVFCSGCDYA ANVERAESCN
LASQKEEMKE LEEVHTPGAA TIKELEEFLK TSPDKFAKTL VYEADGKTVV VVVRGDREVN
EIKVSNAIGS VIEFALATDD VVRKVTNAEV GFAGPIGINA DYVFIDKEIV EQRNIVVGAN
KTEYHIKNAN YGRDFEGIVG DFRNVQEGDK CIVCGKPLEI ARGVEVGHIF KLGTKYSESM
NANFIDKDGK SKPIVMGCYG IGVERTAAAI IEQHNDEKGI IWPLSVAPYH VVIVPANMKN
EEQISIAENI YNDLQAMGVE VLLDDRDERI GVKFNDSELI GIPMRITVGK NINEGKVEFK
LRHKEDKEII DIEEINEKVK AEFIRNNVRL G
