SYPM_SCHPO
ID SYPM_SCHPO Reviewed; 425 AA.
AC O74765;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Probable proline--tRNA ligase, mitochondrial;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
DE Flags: Precursor;
GN ORFNames=SPBC24C6.03;
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] {ECO:0000312|EMBL:CAA21147.1}
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] {ECO:0000305}
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; Evidence={ECO:0000250|UniProtKB:P39965};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255}.
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DR EMBL; CU329671; CAA21147.1; -; Genomic_DNA.
DR PIR; T39967; T39967.
DR RefSeq; NP_595957.1; NM_001021866.2.
DR AlphaFoldDB; O74765; -.
DR SMR; O74765; -.
DR STRING; 4896.SPBC24C6.03.1; -.
DR MaxQB; O74765; -.
DR PaxDb; O74765; -.
DR PRIDE; O74765; -.
DR EnsemblFungi; SPBC24C6.03.1; SPBC24C6.03.1:pep; SPBC24C6.03.
DR GeneID; 2540642; -.
DR KEGG; spo:SPBC24C6.03; -.
DR PomBase; SPBC24C6.03; -.
DR VEuPathDB; FungiDB:SPBC24C6.03; -.
DR eggNOG; KOG2324; Eukaryota.
DR HOGENOM; CLU_016739_4_2_1; -.
DR InParanoid; O74765; -.
DR OMA; NCDYAAN; -.
DR PhylomeDB; O74765; -.
DR PRO; PR:O74765; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005759; C:mitochondrial matrix; IC:PomBase.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004827; F:proline-tRNA ligase activity; ISM:PomBase.
DR GO; GO:0032543; P:mitochondrial translation; NAS:PomBase.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF55681; SSF55681; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Mitochondrion;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..425
FT /note="Probable proline--tRNA ligase, mitochondrial"
FT /id="PRO_0000314630"
SQ SEQUENCE 425 AA; 47932 MW; B833CA619C00E4E3 CRC64;
MLQHLRNRAS IEVLGKAIRK YNVPESANQL LIDMGFIQPS MPGIFQYLPL GLRVQNKICD
LLHISMRSLG ASAISLAHLS SKEIWEKSGR WQKTGSELFR LHDRNDREMC LAPTHEEDVT
RTMATIIDSQ KQLPIRVYQI GRKFRDELRP RGGLLRGREF MMKDLYTFDI DKASAMKTYE
DVLQAYHTFF KEVGLPFVMV KAATGNIGGN LSHEFHYRHP VGEDVIYTCP SCHYSTNSEM
LDLSKTSSDI SCPNCNDQLT STTAIEVGHA FYLGKIYSSK FNATVEVKNK QEVLHMGCYG
IGVSRLIAAV AHVTKDAKGL VWPSSIAPWK VLVVPTSDNH IQSAETVYDA TANVVGFDNV
LLEDRQNRAF GYKMRDAELI GYPFVIVVGS RFQEEGICEI IVRSSGERYK LDKDSLHQVL
LGNFL
