SEPS_ARCFU
ID SEPS_ARCFU Reviewed; 534 AA.
AC O30126;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=O-phosphoserine--tRNA(Cys) ligase;
DE Short=O-phosphoserine--tRNA ligase;
DE EC=6.1.1.27;
DE AltName: Full=Non-canonical O-phosphoseryl-tRNA(Cys) synthetase;
DE AltName: Full=O-phosphoseryl-tRNA(Cys) synthetase;
DE Short=SepRS;
GN Name=sepS; OrderedLocusNames=AF_0110;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE,
RP MUTAGENESIS OF GLU-418; GLU-420 AND THR-423, AND SUBUNIT.
RX PubMed=17351629; DOI=10.1038/nsmb1219;
RA Fukunaga R., Yokoyama S.;
RT "Structural insights into the first step of RNA-dependent cysteine
RT biosynthesis in archaea.";
RL Nat. Struct. Mol. Biol. 14:272-279(2007).
CC -!- FUNCTION: Catalyzes the attachment of O-phosphoserine (Sep) to
CC tRNA(Cys). {ECO:0000305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-
CC phospho-L-seryl-tRNA(Cys); Xref=Rhea:RHEA:25678, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9719, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57524, ChEBI:CHEBI:78442, ChEBI:CHEBI:78551,
CC ChEBI:CHEBI:456215; EC=6.1.1.27;
CC -!- SUBUNIT: Homotetramer. Interacts with SepCysS (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC O30126; O30126: sepS; NbExp=2; IntAct=EBI-15624845, EBI-15624845;
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC O-phosphoseryl-tRNA(Cys) synthetase subfamily. {ECO:0000305}.
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DR EMBL; AE000782; AAB91121.1; -; Genomic_DNA.
DR PIR; F69263; F69263.
DR RefSeq; WP_010877624.1; NC_000917.1.
DR PDB; 2DU3; X-ray; 2.60 A; A/B=1-534.
DR PDB; 2DU4; X-ray; 2.80 A; A/B=1-534.
DR PDB; 2DU5; X-ray; 3.20 A; A/B=1-534.
DR PDB; 2DU6; X-ray; 3.30 A; A/B=1-534.
DR PDBsum; 2DU3; -.
DR PDBsum; 2DU4; -.
DR PDBsum; 2DU5; -.
DR PDBsum; 2DU6; -.
DR AlphaFoldDB; O30126; -.
DR SMR; O30126; -.
DR STRING; 224325.AF_0110; -.
DR PRIDE; O30126; -.
DR EnsemblBacteria; AAB91121; AAB91121; AF_0110.
DR GeneID; 24793664; -.
DR KEGG; afu:AF_0110; -.
DR eggNOG; arCOG00411; Archaea.
DR HOGENOM; CLU_506822_0_0_2; -.
DR OMA; RSHMTSG; -.
DR OrthoDB; 6499at2157; -.
DR PhylomeDB; O30126; -.
DR BRENDA; 6.1.1.27; 414.
DR EvolutionaryTrace; O30126; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0043816; F:phosphoserine-tRNA(Cys) ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR GO; GO:0043039; P:tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_01674; Sep_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR005246; O-Pseryl-tRNA(Cys)_ligase.
DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR InterPro; IPR041590; SepRS_C.
DR PANTHER; PTHR11538:SF38; PTHR11538:SF38; 1.
DR Pfam; PF18006; SepRS_C; 1.
DR Pfam; PF01409; tRNA-synt_2d; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00470; sepS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..534
FT /note="O-phosphoserine--tRNA(Cys) ligase"
FT /id="PRO_0000363746"
FT BINDING 186..188
FT /ligand="substrate"
FT BINDING 231..233
FT /ligand="substrate"
FT BINDING 273..274
FT /ligand="substrate"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17351629"
FT MUTAGEN 418
FT /note="E->N: Shows reduced phosphoserine ligation activity.
FT Shows appreciable ligation activity with both suppressor
FT tRNA(Opal) and tRNA(Amber), and reduces ligation activity
FT with tRNA(Cys); when associated with N-420. Shows higher
FT activity than the E418N/E420N mutant with both suppressor
FT tRNA(Opal) and tRNA(Amber), and the activity with
FT tRNA(Opal) and tRNA(Amber) is almost 30% of that of the
FT wild-type SepRS with tRNA(Cys); when associated with N-420
FT and V-423."
FT /evidence="ECO:0000269|PubMed:17351629"
FT MUTAGEN 420
FT /note="E->N: Shows reduced phosphoserine ligation activity.
FT Shows appreciable ligation activity with both suppressor
FT tRNA(Opal) and tRNA(Amber), and reduces ligation activity
FT with tRNA(Cys); when associated with N-418. Shows higher
FT activity than the E418N/E420N mutant with both suppressor
FT tRNA(Opal) and tRNA(Amber), and the activity with
FT tRNA(Opal) and tRNA(Amber) is almost 30% of that of the
FT wild-type SepRS with tRNA(Cys); when associated with N-418
FT and V-423."
FT /evidence="ECO:0000269|PubMed:17351629"
FT MUTAGEN 423
FT /note="T->V: Shows higher activity than the E418N/E420N
FT mutant with both suppressor tRNA(Opal) and tRNA(Amber), and
FT the activity with tRNA(Opal) and tRNA(Amber) is almost 30%
FT of that of the wild-type SepRS with tRNA(Cys); when
FT associated with N-418 and N-420."
FT /evidence="ECO:0000269|PubMed:17351629"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 16..22
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 48..62
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 110..115
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 128..133
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 145..150
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 160..165
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 169..173
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 187..196
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 197..201
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 204..215
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 227..237
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 243..254
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 261..266
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 280..290
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 298..309
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 330..337
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 349..353
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 359..365
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 375..390
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 395..418
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 420..426
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 428..431
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 433..437
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 451..456
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 464..479
FT /evidence="ECO:0007829|PDB:2DU3"
FT TURN 480..483
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 485..494
FT /evidence="ECO:0007829|PDB:2DU3"
FT HELIX 497..500
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:2DU4"
FT HELIX 506..514
FT /evidence="ECO:0007829|PDB:2DU3"
FT STRAND 523..533
FT /evidence="ECO:0007829|PDB:2DU3"
SQ SEQUENCE 534 AA; 61181 MW; ED762519450D50E2 CRC64;
MKFDPQKYRE LAEKDFEAAW KAGKEILAER SPNELYPRVG FSFGKEHPLF ATIQRLREAY
LSIGFSEVVN PLIVEDVHVK KQFGREALAV LDRCFYLATL PKPNVGISAE KIRQIEAITK
REVDSKPLQE IFHRYKKGEI DGDDLSYLIA EVLDVDDITA VKILDEVFPE FKELKPISST
LTLRSHMTTG WFITLSHIAD KLPLPIKLFS IDRCFRREQG EDATRLYTYF SASCVLVDEE
LSVDDGKAVA EALLRQFGFE NFRFRKDEKR SKYYIPDTQT EVFAFHPKLV GSSTKYSDGW
IEIATFGIYS PTALAEYDIP YPVMNLGLGV ERLAMILYGY DDVRKMVYPQ IHGEIKLSDL
DIAREIKVKE VPQTAVGLKI AQSIVETAEK HASEPSPCSF LAFEGEMMGR NVRVYVVEEE
ENTKLCGPAY ANEVVVYKGD IYGIPKTKKW RSFFEEGVPT GIRYIDGFAY YAARKVEEAA
MREQEEVKVK ARIVENLSDI NLYIHENVRR YILWKKGKID VRGPLFVTVK AEIE
