ID Q22620_CAEEL Unreviewed; 581 AA.
AC Q22620;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 180.
DE RecName: Full=proline--tRNA ligase {ECO:0000256|ARBA:ARBA00012831};
DE EC=6.1.1.15 {ECO:0000256|ARBA:ARBA00012831};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00029731};
GN Name=pars-1 {ECO:0000313|EMBL:CCD73349.1,
GN ECO:0000313|WormBase:T20H4.3a};
GN ORFNames=CELE_T20H4.3 {ECO:0000313|EMBL:CCD73349.1}, T20H4.3
GN {ECO:0000313|WormBase:T20H4.3a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD73349.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD73349.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD73349.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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};
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DR EMBL; BX284603; CCD73349.1; -; Genomic_DNA.
DR PIR; T16915; T16915.
DR RefSeq; NP_001022777.1; NM_001027606.3.
DR AlphaFoldDB; Q22620; -.
DR SMR; Q22620; -.
DR DIP; DIP-27500N; -.
DR STRING; 6239.T20H4.3a.2; -.
DR EPD; Q22620; -.
DR PaxDb; 6239-T20H4-3a; -.
DR PeptideAtlas; Q22620; -.
DR EnsemblMetazoa; T20H4.3a.1; T20H4.3a.1; WBGene00004189.
DR UCSC; T20H4.3b; c. elegans.
DR AGR; WB:WBGene00004189; -.
DR WormBase; T20H4.3a; CE00748; WBGene00004189; pars-1.
DR eggNOG; KOG4163; Eukaryota.
DR InParanoid; Q22620; -.
DR OMA; EVYWVTH; -.
DR OrthoDB; 2733051at2759; -.
DR PhylomeDB; Q22620; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00004189; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; Q22620; baseline and differential.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; cd00862; ProRS_anticodon_zinc; 1.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 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 InterPro; IPR009068; uS15_NS1_RNA-bd_sf.
DR InterPro; IPR000738; WHEP-TRS_dom.
DR NCBIfam; TIGR00408; proS_fam_I; 1.
DR PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF09180; ProRS-C_1; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF00458; WHEP-TRS; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SMART; SM00946; ProRS-C_1; 1.
DR SMART; SM00991; WHEP-TRS; 1.
DR SUPFAM; SSF64586; C-terminal domain of ProRS; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF47060; S15/NS1 RNA-binding domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51185; WHEP_TRS_2; 1.
PE 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCD73349.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Proteomics identification {ECO:0007829|EPD:Q22620,
KW ECO:0007829|PeptideAtlas:Q22620};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 3..60
FT /note="WHEP-TRS"
FT /evidence="ECO:0000259|PROSITE:PS51185"
FT DOMAIN 120..371
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 53..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 581 AA; 65819 MW; 7B30D42FF83C05EF CRC64;
MSTKEEITKE IEEQGAEVRR VKGDKNSTEE AKKEAIDKLL ALKLTYKEVT GQEYAAPNAR
QSKPKKEEKP KQQPKQQEKK QDGKKQTLLG VGTKKDDNYS EWYSEVITKA EMIEYYDVSG
CYVLRPWSFA VWESIQEWFD SGIKKLGVKN CYFPMFVSNA ALEREKTHIA DFAPEVAWVT
RAGNSEMAEP IAIRPTSETV MYPSYKKWVQ SHRDLPIKLN QWCNVVRWEF KHPTPFLRTR
EFLWQEGHTA FANPADAEKE VFQILDLYAG VYTDLLAIPV VKGRKSEKEK FAGGDFTTTV
EAYVACNGRG IQGATSHHLG QNFSKMFDIS YEDPAKEGER AFAWQNSWGL STRTIGAMVM
IHGDDKGLVL PPRVAAVQVI VVPVGFKTEN KQSLFDAVDK VTKDLVADGV KAEHDLRENY
NAGWKFNHWE LKGVPIRFEV GPNDLAKNQV TAVIRHNGEK KQLSLEGLSK TVKSLLDEIH
TAMYNKVLAQ RDSHLKSTTC IEEFKKLLDE KCIILSPFCG RPDCEEEIKK ASTREDGEGA
QMGAKTLCIP LDQPKQELPS KCLFPSCTYN AKAFALFGRS Y
//
