SYP_DEIRA
ID SYP_DEIRA Reviewed; 499 AA.
AC Q9RUW4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Proline--tRNA ligase;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
GN Name=proS; OrderedLocusNames=DR_1266;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP PROLINE AND CYSTEINE ACTIVATION, AND KINETIC PARAMETERS.
RX PubMed=12130657; DOI=10.1074/jbc.m206928200;
RA Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H.,
RA Hartsch T., Soell D.;
RT "Cysteine activation is an inherent in vitro property of prolyl-tRNA
RT synthetases.";
RL J. Biol. Chem. 277:34743-34748(2002).
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). Can inadvertently
CC accommodate and process cysteine.
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;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.16 mM for proline {ECO:0000269|PubMed:12130657};
CC KM=0.01 mM for cysteine {ECO:0000269|PubMed:12130657};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC anticodon-binding domain and the C-terminal extension. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 3 subfamily. {ECO:0000305}.
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DR EMBL; AE000513; AAF10837.1; -; Genomic_DNA.
DR PIR; D75416; D75416.
DR RefSeq; NP_294990.1; NC_001263.1.
DR RefSeq; WP_010887909.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RUW4; -.
DR SMR; Q9RUW4; -.
DR STRING; 243230.DR_1266; -.
DR PRIDE; Q9RUW4; -.
DR EnsemblBacteria; AAF10837; AAF10837; DR_1266.
DR KEGG; dra:DR_1266; -.
DR PATRIC; fig|243230.17.peg.1460; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_001882_4_2_0; -.
DR InParanoid; Q9RUW4; -.
DR OMA; EVYWVTH; -.
DR OrthoDB; 665824at2; -.
DR SABIO-RK; Q9RUW4; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 3.30.110.30; -; 1.
DR Gene3D; 3.30.930.10; -; 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; 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; 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 PANTHER; PTHR43382; PTHR43382; 1.
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; SSF55681; SSF55681; 1.
DR SUPFAM; SSF64586; SSF64586; 1.
DR TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..499
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000248228"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 499 AA; 56391 MW; 9E0EC581753030A7 CRC64;
MTKDGGKKDN QGQDKKAQQY GVTPQSVDFN DWYNEVVKKA DLADNSPVAG AMVVRPYGSA
LWENIQRWLD DRFKASGHES LIFPTLIPMN FIMKEADHVE GFAPELFTVN KIGTEELAEP
YVMRPTSETI IGHMWSGWLN SYRDLPFLHY QWGSVFRAEL RTKAFLRTSE FFWHEGHTAH
ADEAEARAEV RQQLDLYHEF CRDVLALPVV RGEKTASERF AGAVATYSIE GMMRDGKALQ
SGTSHYLGQN FSRAFDVKYQ TREQKEEFAH TTSWAISSRI IGAIIMTHGD DSGLMMPPRI
APIQVVVIPV GRKDNFDQMV QEGEKLAAEL RAQGLRVKVD GRDGVTNGFK YNDWELKGVP
VRIELGPRDL ESGVLVVKNR HSEDKETLPR AEAVSGMSAR LDTIHDFLMK RATDFLLANT
AEVDSYDAFQ REIEAGHWVR AYHCGEPACE KSIKEDTKAT ARNVPFDDAE FFAERGEGQC
VKCGQPSAYG KRVLFGRQY
