ID A0A085LF81_9MICO Unreviewed; 603 AA.
AC A0A085LF81;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=IU11_09375 {ECO:0000313|EMBL:KFD43627.1};
OS Cellulosimicrobium sp. MM.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=1523621 {ECO:0000313|EMBL:KFD43627.1, ECO:0000313|Proteomes:UP000028634};
RN [1] {ECO:0000313|EMBL:KFD43627.1, ECO:0000313|Proteomes:UP000028634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM {ECO:0000313|EMBL:KFD43627.1,
RC ECO:0000313|Proteomes:UP000028634};
RA Lal R., Sharma A., Sangwan N., Hira P.;
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KFD43627.1, ECO:0000313|Proteomes:UP000028634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM {ECO:0000313|EMBL:KFD43627.1,
RC ECO:0000313|Proteomes:UP000028634};
RA Khurana J.P.;
RT "Draft genome sequence of Cellulosimicrobium sp. MM isolated from arsenic
RT rich microbial mats of a himalayan hotspring.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_01569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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:KFD43627.1}.
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DR EMBL; JPQW01000152; KFD43627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085LF81; -.
DR Proteomes; UP000028634; 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; 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; 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:UP000028634}.
FT DOMAIN 33..499
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 603 AA; 65222 MW; 4C21EC7AED56B318 CRC64;
MRLSTLFVRT LREDPADAEV ASHKLLVRAG YIRRAAPGIY TWLPLGLRVL RKVEAVVREE
MAAAGAQEVH FPALLPKEPY EATGRWTEYG PNIFRLKDRK EADYLLAPTH EEMFTLLVKD
LYSSYKDLPL TIYQIQTKYR DEARPRAGLI RGREFVMKDA YSFDTTDEGL ARSYEAQRAA
YRRIFDRLGL EYVIVAATSG AMGGSRSEEF LTPTAIGEDT FVRSPGGYAA NVEAVVTPAP
EDVDYADAPA AHVEDTPDTP TIESLVALAN ARFPRPDRAW TAADTLKNVV LALTHPDGRR
EVVVVGLPGD REVDLKRVGA AFEPAEVEPA TDADFAAHPE LVKGYIGPQV LGPNARREAP
ADATLAEGEV PERHSVRYLL DPRVVAGTRW ITGANEPGKH VFDLVAERDF AADGTVEAAE
VRAGDPAPDG SGPLELARGI EIGHIFALGR KYAQALGLTV LDENGKQVVV TMGSYGIGVT
RVLAALAEAN HDDAGLAWPA HVAPAHVHVL ATGKDASVFE EAERLATELT ARGVEVVYDD
RPKVSPGVKF KDAELLGVPL LLVVGRGLAD GVVEVRPRAG ESVQVPVADA VEHVAARVAE
LLG
//
