ID PRS1_SCHPO Reviewed; 716 AA.
AC O60155;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=Putative proline--tRNA ligase C19C7.06;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
GN Name=prs1; ORFNames=SPBC19C7.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA19574.1; -; Genomic_DNA.
DR PIR; T39812; T39812.
DR RefSeq; NP_596162.1; NM_001022082.2.
DR AlphaFoldDB; O60155; -.
DR SMR; O60155; -.
DR BioGRID; 276959; 7.
DR STRING; 284812.O60155; -.
DR iPTMnet; O60155; -.
DR MaxQB; O60155; -.
DR PaxDb; 4896-SPBC19C7-06-1; -.
DR EnsemblFungi; SPBC19C7.06.1; SPBC19C7.06.1:pep; SPBC19C7.06.
DR GeneID; 2540431; -.
DR KEGG; spo:SPBC19C7.06; -.
DR PomBase; SPBC19C7.06; prs1.
DR VEuPathDB; FungiDB:SPBC19C7.06; -.
DR eggNOG; KOG4163; Eukaryota.
DR HOGENOM; CLU_001882_4_1_1; -.
DR InParanoid; O60155; -.
DR OMA; EVYWVTH; -.
DR PhylomeDB; O60155; -.
DR PRO; PR:O60155; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043907; F:Cys-tRNA(Pro) hydrolase activity; ISM:PomBase.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IMP:PomBase.
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; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..716
FT /note="Putative proline--tRNA ligase C19C7.06"
FT /id="PRO_0000317133"
FT REGION 655..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 716 AA; 78875 MW; 8C7BDEA8FFE782A5 CRC64;
MSVDSLVSCL EQLITDDLKL VEHQEVSNGA TWASALQSTK DVPSHALTKT IVLKPKTAKS
QTVVPIILAA LETTSTPSGI AAKAVGSKEA RMAAADLVEE VFGIPPTDVG IFSVNKENAS
KVHVVLDAAL IQHNGLLAFH PSSSAKTVFV SPAAVQTYLK SVGVNPIIVD FSAPGSATAP
SKPAAQKKKA EPSKNDAAIE NAALIGITVR KDADFPNWYQ QVLTKSDMIE YYDISGCYIL
KPWSYSIWEA IQGWFDKEIK KLGVRNGYFP LFVSSKVLEK EKDHVEGFAP EVAWVTRAGT
SELDEPIAIR PTSETVMYPY YAKWIRSHRD LPLKLNQWNS VVRWEFKNPQ PFLRTREFLW
QEGHTAHMTL EGATEEVHQI LDLYARIYTD LLAVPVIKGV KSENEKFAGG MFTTTVEGYI
PTTGRGIQGA TSHCLGQNFS KMFNIVVEDP NAEIGPTGER PKLFVWQNSW GLSTRTIGVA
VMVHGDDKGL KLPPAIALVQ SVVVPCGITN KTTDQERNEI EGFCSKLADR LNAADIRTEA
DLRAYTPGYK FSHWEMKGVP LRLEYGPNDA KKNQVTAVRR DTFEKIPVPL NNLEKGVSDL
LAKIQTNMYE TAKAERDAHV VKVKEWADFV PALNKKNIVM IPWCNTTECE KEIKKNSARQ
VNGDEPEDEK APSMGAKSLC IPLEQPSGED AIIEGTTKCA GCGNLAKVWG LFGRSY
//
