ID A0A1Q5L0H5_9ACTN Unreviewed; 567 AA.
AC A0A1Q5L0H5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01569};
DE EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01569};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01569};
DE Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01569};
GN Name=proS {ECO:0000256|HAMAP-Rule:MF_01569};
GN ORFNames=AMK32_08910 {ECO:0000313|EMBL:OKJ87339.1};
OS Streptomyces sp. CB01883.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ87339.1, ECO:0000313|Proteomes:UP000186398};
RN [1] {ECO:0000313|EMBL:OKJ87339.1, ECO:0000313|Proteomes:UP000186398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01883 {ECO:0000313|EMBL:OKJ87339.1,
RC ECO:0000313|Proteomes:UP000186398};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:0000256|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:0000256|ARBA:ARBA00000857,
CC ECO:0000256|HAMAP-Rule:MF_01569};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|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:0000256|HAMAP-Rule:MF_01569}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01569}.
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:OKJ87339.1}.
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DR EMBL; LIWA01000001; OKJ87339.1; -; Genomic_DNA.
DR RefSeq; WP_073890117.1; NZ_LIWA01000001.1.
DR AlphaFoldDB; A0A1Q5L0H5; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000186398; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.90.960.10; YbaK/aminoacyl-tRNA synthetase-associated domain; 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 NCBIfam; TIGR00409; proS_fam_II; 1.
DR PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42753:SF2; PROLINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
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; 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 ECO:0000256|HAMAP-Rule:MF_01569};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01569};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01569};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01569};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01569};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01569}; Reference proteome {ECO:0000313|Proteomes:UP000186398}.
FT DOMAIN 54..470
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 567 AA; 61253 MW; DF1D3B862CBF6BF9 CRC64;
MANAPVQRMS QLMAKTLRDD PADAEVLSHK LLVRAGYVRR TAAGIWSWLP LGKKVLANVE
RIVREEMDAI GAQEVSLPAL LPREPYEATG RWDEYGQELF RLQDRKGGDY LLGPTHEEIF
TLLVKDQCTS YKDLPVILYQ IQSKFRDEAR PRAGILRGRE FLMKDSYSFD LDDEGLGRSY
ALHREAYRRT FERLGLDYRI VAATAGAMGG SKSEEFLAPA EAGEDTFADC PNCDFAANTE
AVSYELRTVD GSAVPALEEI PTPDTPTIET LAASLGVPAS ATLKNLLVKV DGEIVAVGVP
GDREVDLGKV EAHFAPAAVE MVTEADFAGR PDLVRGYVGP QGLGEKVTYI ADPRVAPGTS
WITGANKDQT HAKNVVAGRD FEVDAYVDVV VVQEGDPCPK CGTGLKLDRA IEIGHIFQLG
RKYADALKLD VLGQNGKPVR VTMGSYGIGV SRAVAALAEQ TADEQGLCWP KEVAPADVHV
VAAGKALQTE LALDVAEKLA AAGVRVLVDD RAGVSPGVKF TDAELMGVPQ ILVAGRRSGE
GVLELKDRRT GEREELSVED AIARLTA
//
