ID A0A1M3MBU3_9BACT Unreviewed; 423 AA.
AC A0A1M3MBU3;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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 ORFNames=BGP01_04060 {ECO:0000313|EMBL:OJX90567.1};
OS Paludibacter sp. 47-17.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=1895899 {ECO:0000313|EMBL:OJX90567.1, ECO:0000313|Proteomes:UP000183960};
RN [1] {ECO:0000313|EMBL:OJX90567.1, ECO:0000313|Proteomes:UP000183960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=47-17 {ECO:0000313|EMBL:OJX90567.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OJX90567.1}.
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DR EMBL; MKVT01000013; OJX90567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3MBU3; -.
DR STRING; 1895899.BGP01_04060; -.
DR Proteomes; UP000183960; Unassembled WGS sequence.
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:OJX90567.1};
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 72..106
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 423 AA; 47208 MW; 220B351C17B8F44A CRC64;
MLTLKYITEN PQEVTARLAK KHFPAEAIIA QVIELDTQRK QTQTSADQAL AQSNALSKEI
GILLKQGKTD EATAAKEQTT ELKKRIQELT DLQASLEQQL TDLLVQIPNL PHHSVPEGRH
AEHNVVERTG GELPQLPAGA LPHWELAKKY DLIDFELGVK ITGAGFPVYK GKGARLQRAL
INFFLDNARD AGYLEVQPPY VVNAASGYGT GQLPDKEGQM YHATADDLYL IPTAEVPVTN
IYRDVILNES ELPIKNTAYS ACFRREAGSY GKDVRGLNRL HQFDKVEIVQ IQHPDKSYES
LTDMVNYVQT LVEKLELPWR ILRLCGGDMS FTSALTFDFE VYSAAQQRWL EVSSVSNFEN
YQANRLKCRF KGNDKKTQLC HTLNGSALAL PRIVAALLEN NQTAEGIRIP AALVPYTGFE
MIG
//
