SYP_SYNY3
ID SYP_SYNY3 Reviewed; 603 AA.
AC P73942;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569};
DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569};
GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01569}; OrderedLocusNames=sll1425;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-
CC step reaction: proline is first activated by ATP to form Pro-AMP and
CC then transferred to the acceptor end of tRNA(Pro). As ProRS can
CC inadvertently accommodate and process non-cognate amino acids such as
CC alanine and cysteine, to avoid such errors it has two additional
CC distinct editing activities against alanine. One activity is designated
CC as 'pretransfer' editing and involves the tRNA(Pro)-independent
CC hydrolysis of activated Ala-AMP. The other activity is designated
CC 'posttransfer' editing and involves deacylation of mischarged Ala-
CC tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
CC {ECO:0000255|HAMAP-Rule:MF_01569}.
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:0000255|HAMAP-Rule:MF_01569};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}.
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC editing domain and the C-terminal anticodon-binding domain.
CC {ECO:0000255|HAMAP-Rule:MF_01569}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA18008.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000022; BAA18008.1; ALT_INIT; Genomic_DNA.
DR PIR; S75447; S75447.
DR AlphaFoldDB; P73942; -.
DR SMR; P73942; -.
DR STRING; 1148.1653092; -.
DR PaxDb; P73942; -.
DR EnsemblBacteria; BAA18008; BAA18008; BAA18008.
DR KEGG; syn:sll1425; -.
DR eggNOG; COG0442; Bacteria.
DR InParanoid; P73942; -.
DR OMA; NCDYAAN; -.
DR PhylomeDB; P73942; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 2.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_01569; Pro_tRNA_synth_type1; 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; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF04073; tRNA_edit; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF55826; SSF55826; 1.
DR TIGRFAMs; TIGR00409; proS_fam_II; 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..603
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000139347"
SQ SEQUENCE 603 AA; 66929 MW; D3D46036FDA0E20D CRC64;
MRLSQMLFVT LRDDPADAEI PSHKLLVRAG FIRRLGSGLY AYLPLIWRVL EKVKRIVQEE
MNRTGAQECL LPQLQPSELW KMSGRWDTYT ESEGIMFALR DRLERELGLG PTHEEVITAI
AKEMIRSYRQ LPVNLYQIQT KFRDEIRPRF GLMRGREFIM KDAYSFHSDE ASLKATYGAM
DQAYRNIFSR CGLDFRPVDA DSGAIGGSGS QEFMVLADAG EDEILYTEDG LYSANVEKAV
SLAPDAKPSP FSGYKKQSAP NTATIAKMCQ CLDCDASNVV KNVLYQAVYN SGKAVLVLVS
IRGDQEVNEV KLTNELTKLA PHYESTNILS LTVPDEKEQQ KWAAKPLPLG YISPGISDDY
IATNKQVADK FLRLVDQTAV DLTNFATGAD AVDYHVTGAN WSTDFTLPKL VVDVRKALAG
DRPVHDPTGE LKTARGIEVG HIFQLGTKYS QAMGATFTNE QGEEKPLVMG CYGIGVSRLA
QAAVEQSYDK DGIIWPTAIA PYEVVIVVPN VGDEEQMQVA EQIYTEFQAA EVDVLLDDRN
ERAGVKFKDS ELIGIPYRVV TGKSLKQGQL EVVKRADKSV QNLAIAAVVP TLTAWIKAEK
KTS
