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PRS1_SCHPO
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   25-MAY-2022, entry version 137.
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; 4896.SPBC19C7.06.1; -.
DR   iPTMnet; O60155; -.
DR   MaxQB; O60155; -.
DR   PaxDb; O60155; -.
DR   PRIDE; O60155; -.
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:0005737; C:cytoplasm; 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; ISM:PomBase.
DR   GO; GO:0002181; P:cytoplasmic translation; NAS:PomBase.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IMP:PomBase.
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   Gene3D; 3.90.960.10; -; 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   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   Pfam; PF04073; tRNA_edit; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SMART; SM00946; ProRS-C_1; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   SUPFAM; SSF55826; SSF55826; 1.
DR   SUPFAM; SSF64586; SSF64586; 1.
DR   TIGRFAMs; TIGR00408; proS_fam_I; 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
 
 
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