ID K0P089_9BACT Unreviewed; 423 AA.
AC K0P089;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Serine--tRNA ligase {ECO:0000256|ARBA:ARBA00039158};
DE EC=6.1.1.11 {ECO:0000256|ARBA:ARBA00012840};
DE AltName: Full=Seryl-tRNA synthetase {ECO:0000256|ARBA:ARBA00031113};
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000256|ARBA:ARBA00033352};
GN Name=serS {ECO:0000313|EMBL:CCM10287.1};
GN ORFNames=CAHE_0510 {ECO:0000313|EMBL:CCM10287.1};
OS Cardinium endosymbiont cEper1 of Encarsia pergandiella.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Amoebophilaceae;
OC Cardinium.
OX NCBI_TaxID=1231626 {ECO:0000313|EMBL:CCM10287.1, ECO:0000313|Proteomes:UP000003996};
RN [1] {ECO:0000313|EMBL:CCM10287.1, ECO:0000313|Proteomes:UP000003996}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zchori-Fein et al. 2004 {ECO:0000313|Proteomes:UP000003996};
RX PubMed=23133394; DOI=10.1371/journal.pgen.1003012;
RA Penz T., Schmitz-Esser S., Kelly S.E., Cass B.N., Muller A., Woyke T.,
RA Malfatti S.A., Hunter M.S., Horn M.;
RT "Comparative Genomics Suggests an Independent Origin of Cytoplasmic
RT Incompatibility in Cardinium hertigii.";
RL PLoS Genet. 8:e1003012-e1003012(2012).
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC {ECO:0000256|ARBA:ARBA00005045}.
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DR EMBL; HE983995; CCM10287.1; -; Genomic_DNA.
DR RefSeq; WP_014934660.1; NC_018605.1.
DR AlphaFoldDB; K0P089; -.
DR STRING; 1231626.CAHE_0510; -.
DR KEGG; che:CAHE_0510; -.
DR PATRIC; fig|1231626.3.peg.505; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_023797_1_1_10; -.
DR OrthoDB; 9804647at2; -.
DR BioCyc; CEND1231626:AL022_RS02365-MONOMER; -.
DR Proteomes; UP000003996; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:InterPro.
DR Gene3D; 1.10.287.40; Serine-tRNA synthetase, tRNA binding domain; 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; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR042103; SerRS_1_N_sf.
DR InterPro; IPR010978; tRNA-bd_arm.
DR NCBIfam; TIGR00414; serS; 1.
DR PANTHER; PTHR43697:SF1; SERINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43697; SERYL-TRNA SYNTHETASE; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF46589; tRNA-binding arm; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:CCM10287.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 175..415
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
FT COILED 40..94
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 423 AA; 47323 MW; 79ADD1C54FFF0953 CRC64;
MIELHRIRTD KEAVINGLHQ RGVSNAEELI QAICNLDIEK RAIQFQLDNL SATLNKLNQE
IADLLRKNDG AAPLEAKKEE SNQLKKSIKQ LVEKFKAHAL DLLVQLYALP NLPHESVPVG
SHADHNLIIY QTSRMVVKGP LAHWDLVKKY DLVDFELGNK ITGAGFPVYK GKGARLQRAL
INFFLDQALK AGYTEIQPPI LVNEASAYAT GQLPDKEGQM YQIGSTPLYL IPTSEVSITN
IYRDAIIAET ALPIKHVGYT PCFRREAGSW GADVRGLNRL HQFDKVELVQ IAHPDASYAN
LEEMLTYVQG LVEHLALPYR VLKLCHGDLG FCAAMTYDIE VHAIGQDKWL EVSSISNFET
FQSNRLSLRY KDKTKKTCLL HTLNGSGLAL PRVLAALLEL NQTPEGIRIP KVLQPYTGFD
IID
//
