ID Q4DZZ4_TRYCC Unreviewed; 810 AA.
AC Q4DZZ4;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 100.
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 ORFNames=Tc00.1047053509805.130 {ECO:0000313|EMBL:EAN98098.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN98098.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN98098.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN98098.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
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 -!- 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:EAN98098.1}.
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DR EMBL; AAHK01000071; EAN98098.1; -; Genomic_DNA.
DR RefSeq; XP_819949.1; XM_814856.1.
DR AlphaFoldDB; Q4DZZ4; -.
DR SMR; Q4DZZ4; -.
DR STRING; 353153.Q4DZZ4; -.
DR PaxDb; 353153-Q4DZZ4; -.
DR EnsemblProtists; EAN98098; EAN98098; Tc00.1047053509805.130.
DR GeneID; 3552487; -.
DR KEGG; tcr:509805.130; -.
DR eggNOG; KOG4163; Eukaryota.
DR InParanoid; Q4DZZ4; -.
DR OMA; LCMPFDQ; -.
DR OrthoDB; 2733051at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd04335; PrdX_deacylase; 1.
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; 3.90.960.10; YbaK/aminoacyl-tRNA synthetase-associated domain; 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; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-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; PF04073; tRNA_edit; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SMART; SM00946; ProRS-C_1; 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; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:EAN98098.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000002296}.
FT DOMAIN 341..584
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT REGION 259..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 810 AA; 91267 MW; 0AB977F2E78AA3A1 CRC64;
MKMSYGVHSP PALRCWCTLP FSSRRKASSL ENTYFSNRTV FCSSARWIYR RHCEASVSGA
DLSSGFFFYS SLNKEQVTNS TRTMSASDCR GESEMLKILR ALGMDLPTIS HEEKHTVEEA
NKELGRFGVP CTGTKNIFLK SKKEDLVLVT ALHTTRTNMK VIQDALSLKD LRFAPEDVLR
THLGVVQGGV TPLALVNNES KNIKLVLDKA LVESTVPVVL HPCRNDKSCL ITPKQLQDFL
RKLEYPFVVV DFSAEATGGT PSGDNTRAKS STSQKETGKK TSQPAAAAIT GGANVTGETK
LGILVKREEN FSQWYVEVIT KAEMIEYYDV SGCYIIRPWA FFIWSRIQRF FGARIESMGV
EDCYFPMFVS KSCLEREKDH VEGFAPEVAW VTKAGETDLE VPVAIRPTSE TVMYPYYAKW
IRSHRDLPVR LNMWNNVIRW EFSHPTPFIR TREFLWQEGH CAWQTEEECS QEVLEILDHY
AAVYEELLAV PVVKGRKTEK EKFAGGYYTT TVETYIAAVG RGCQGGTSHN LGQNFGKMFN
ISFQDPEKND GSTLIPWQNS WGLSTRVIGV MTMVHGDDSG MVLPPRVASV QVVIIPVGIT
KNTTDEERKS LLEGCKTLER VLVSGGIRAK ADLRDNYSPG WRFNHWEVKG VPVRVELGPR
ELASLKISLV LRHDGSRRSL LWDKELPTAM TLLMDEIHNS MFAKAKRERQ ENTKKLTEWS
DFTPALNRKC LVLAPWCGEM SCEDQVKKDS AEESKAMQSE EVKDDARAPS MGAKTLCIPF
DQPESVEGKT CICKSCSRPA KHWVLFGRSY
//