ID A5I7N0_CLOBH Unreviewed; 545 AA.
AC A5I7N0; A7G8W2;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Prolyl-tRNA synthetase {ECO:0000313|EMBL:CAL85065.1};
DE EC=6.1.1.15 {ECO:0000313|EMBL:CAL85065.1};
GN Name=proS2 {ECO:0000313|EMBL:CAL85065.1};
GN OrderedLocusNames=CBO3503 {ECO:0000313|EMBL:CAL85065.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL85065.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL85065.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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DR EMBL; AM412317; CAL85065.1; -; Genomic_DNA.
DR RefSeq; WP_012048362.1; NC_009698.1.
DR RefSeq; YP_001255986.1; NC_009495.1.
DR RefSeq; YP_001389227.1; NC_009698.1.
DR AlphaFoldDB; A5I7N0; -.
DR GeneID; 5187728; -.
DR KEGG; cbh:CLC_3452; -.
DR KEGG; cbo:CBO3503; -.
DR PATRIC; fig|413999.7.peg.3481; -.
DR HOGENOM; CLU_016739_0_0_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd04334; ProRS-INS; 1.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.90.960.10; YbaK/aminoacyl-tRNA synthetase-associated domain; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42753:SF2; PROLINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF04073; tRNA_edit; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55826; YbaK/ProRS associated domain; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000313|EMBL:CAL85065.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT DOMAIN 234..350
FT /note="YbaK/aminoacyl-tRNA synthetase-associated"
FT /evidence="ECO:0000259|Pfam:PF04073"
FT DOMAIN 450..540
FT /note="Anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF03129"
SQ SEQUENCE 545 AA; 62422 MW; 2B74095B68357516 CRC64;
MKLSKTLVHS LREDPADVEM DSQKLLLKGG LIAKVDSGLY AFTPLGYRFL EDIQKVVENN
SKKIGGSQIS IPYVNNLEEV SEKNNGFILN FNEETLSFIN FLKSSVTSYK QLPLFFYENN
TEFSYKGKNN LGIMGGRQIL REYFYMVLDG ENDKFNKKEL IKLYKNIFEI MNLQYNMVED
ELDGTIKFII YNNIGDLHIV ACKSCNYGNE VNRASSIPDY QIEKDLKELN KIETPDIKTI
EELGEFFKVP YRKFTKTIIY KCNNDSIVAV MVRGDRDIDE FKVIKNLGNI KSLELAGEDI
VRQATNAEVG FAGPINLKVD KILIDEEITK MNNFMIGANE TGYHYENVNY ERDFKGIVGE
FRKIHKYSKC ILCGDKLEVN EGFVIGEIKK IEENLIKNEC ATFIDNKGKS KPFTIYKGFM
DIYKIISWTI EQNKDELGIV WPMETSAFKV IVTIANVKDE QQFKVGEKIY SSLVNIGIGT
ILDDRKERAG VKFKDADLWG IPIRITVGKN IKENNVEIKL RNSKEKKEIP IDQLQESIKS
LLGIG
//
