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Database: UniProt
Entry: R6YN34_9FIRM
LinkDB: R6YN34_9FIRM
Original site: R6YN34_9FIRM 
ID   R6YN34_9FIRM            Unreviewed;       582 AA.
AC   R6YN34;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01569};
DE            EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01569};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01569};
DE            Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01569};
GN   Name=proS {ECO:0000256|HAMAP-Rule:MF_01569};
GN   ORFNames=BN600_01546 {ECO:0000313|EMBL:CDD35260.1};
OS   Roseburia sp. CAG:309.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX   NCBI_TaxID=1262945 {ECO:0000313|EMBL:CDD35260.1, ECO:0000313|Proteomes:UP000018292};
RN   [1] {ECO:0000313|EMBL:CDD35260.1, ECO:0000313|Proteomes:UP000018292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:309 {ECO:0000313|Proteomes:UP000018292};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|ARBA:ARBA00000857,
CC         ECO:0000256|HAMAP-Rule:MF_01569};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01569}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CDD35260.1}.
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DR   EMBL; CBGX010000178; CDD35260.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6YN34; -.
DR   STRING; 1262945.BN600_01546; -.
DR   Proteomes; UP000018292; Unassembled WGS sequence.
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:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd04334; ProRS-INS; 1.
DR   CDD; cd00861; ProRS_anticodon_short; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 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; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR   NCBIfam; TIGR00409; proS_fam_II; 1.
DR   PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42753:SF2; PROLYL-TRNA SYNTHETASE; 1.
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; 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.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_01569};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01569};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01569};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01569};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01569};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_01569}; Reference proteome {ECO:0000313|Proteomes:UP000018292}.
FT   DOMAIN          48..465
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   582 AA;  65566 MW;  ACE2A685DF1D6E70 CRC64;
     MKLDKMIGDR FKERPSDCAI ESHALMVRGG YMKSVANGIY SQFPPLKRIT AKIEKIIREE
     MDALDGQEVL FPVALPGSLW EESGRFESVG SELLRFKDRN NAQMVLGMTH EEAAVHLVRE
     YANSYTKYPF MIYQVQTKFR DEARPRAGMI RVREFTMKDA YSFHTSQEDL EKYYDRMYKA
     YQRIFARAGI PEVAVVASDS GMMGGSLSHE YMLLTPVGED TIVLCDECDY RANMEAAESI
     IENKDQKLEK AELKLVDTPN QHTIEEVCDY LHLPVENSMK AVVYQKNEDD SYVVLFIRGD
     LEANETKITN YLGAAIHPAV ITEDCGLHAG FIGAYQLPEG ITVLYDNSLK GIENLCCGGN
     EVDKHYVGLN MERDVPDAEY GDFAKAIDGG ICPCCGKPKL KIARGIEVGN IFQLGTKYTK
     TMGMEYLDQD GKKHNPIMGC YGIGVGRLAA SVCEVRRDDY GPIWPITIAP WEVQLCCMRA
     DDAECKEFAD KLYDGLQKDR LEVLYDDRNV RAGAMFSDAD LLGVPVRVVV SPRNMKNGVV
     EISTRDKSVQ VQVPVEEAVT KVKELVQKLY DEIEEGVKQF QE
//
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