ID D5BET2_ZUNPS Unreviewed; 423 AA.
AC D5BET2;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 OrderedLocusNames=ZPR_0453 {ECO:0000313|EMBL:ADF50811.1};
OS Zunongwangia profunda (strain DSM 18752 / CCTCC AB 206139 / SM-A87) (Wangia
OS profunda).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Zunongwangia.
OX NCBI_TaxID=655815 {ECO:0000313|EMBL:ADF50811.1, ECO:0000313|Proteomes:UP000001654};
RN [1] {ECO:0000313|EMBL:ADF50811.1, ECO:0000313|Proteomes:UP000001654}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18752 / CCTCC AB 206139 / SM-A87
RC {ECO:0000313|Proteomes:UP000001654};
RX PubMed=20398413; DOI=10.1186/1471-2164-11-247;
RA Qin Q.L., Zhang X.Y., Wang X.M., Liu G.M., Chen X.L., Xie B.B., Dang H.Y.,
RA Zhou B.C., Yu J., Zhang Y.Z.;
RT "The complete genome of Zunongwangia profunda SM-A87 reveals its adaptation
RT to the deep-sea environment and ecological role in sedimentary organic
RT nitrogen degradation.";
RL BMC Genomics 11:247-247(2010).
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; CP001650; ADF50811.1; -; Genomic_DNA.
DR RefSeq; WP_013069964.1; NC_014041.1.
DR AlphaFoldDB; D5BET2; -.
DR STRING; 655815.ZPR_0453; -.
DR KEGG; zpr:ZPR_0453; -.
DR eggNOG; COG0172; Bacteria.
DR HOGENOM; CLU_023797_1_1_10; -.
DR OrthoDB; 9804647at2; -.
DR Proteomes; UP000001654; 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 CDD; cd00770; SerRS_core; 1.
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; IPR033729; SerRS_core.
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 ECO:0000313|EMBL:ADF50811.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 142..415
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 423 AA; 47788 MW; 195341F359087DA6 CRC64;
MLQVNNIREH KDAYIEALKK RNFDAESIFD EVLSLDETRR STQSRLDDTL AESNKLSKQI
GLMFKNGEHQ KANLLKEKTG KLKEDSRNYS EVLATTIADL EKLLYTIPNV PNEVVPAGTS
EDDNEEIYKE GDVPVLAEGS LPHWELAKKY DIIDFELGNK VTGAGFPIYK GKGARLQRAL
VSYFLDKAVE AGYSEYQLPL MVNEASGYGT GQLPDKEGQM YHITADDLYM IPTAEVPITN
MYRDNLLTDK DFPIACTGYT PCFRREAGSY GAHVRGLNRL HQFDKVELVR IEKPEDSYAA
LEGMVDHVKV LLKELKLPYR ILRLCGGDLG FTSALTYDFE VFSTAQDRWL EISSVSNFET
FQANRLKLRY KNKEGKKELV HTLNGSALAL PRVLAGILEN YQTENGIKIP DVLVPYTGFD
MID
//
