(data stored in SCRATCH zone)

SWISSPROT: D5E9R5_METMS

ID   D5E9R5_METMS            Unreviewed;       459 AA.
AC   D5E9R5;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   11-DEC-2019, entry version 47.
DE   RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase {ECO:0000256|HAMAP-Rule:MF_01675};
DE            EC=2.5.1.73 {ECO:0000256|HAMAP-Rule:MF_01675};
DE   AltName: Full=Sep-tRNA:Cys-tRNA synthase {ECO:0000256|HAMAP-Rule:MF_01675};
DE            Short=SepCysS {ECO:0000256|HAMAP-Rule:MF_01675};
GN   OrderedLocusNames=Mmah_0384 {ECO:0000313|EMBL:ADE35916.1};
OS   Methanohalophilus mahii (strain ATCC 35705 / DSM 5219 / SLP).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanohalophilus.
OX   NCBI_TaxID=547558 {ECO:0000313|EMBL:ADE35916.1, ECO:0000313|Proteomes:UP000001059};
RN   [1] {ECO:0000313|EMBL:ADE35916.1, ECO:0000313|Proteomes:UP000001059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35705 / DSM 5219 / SLP
RC   {ECO:0000313|Proteomes:UP000001059};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Lykidis A., Saunders E., Brettin T., Detter J.C., Han C., Land M.,
RA   Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D.,
RA   Spring S., Schneider S., Schroeder M., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Methanohalophilus mahii DSM 5219.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-
CC       cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). {ECO:0000256|HAMAP-Rule:MF_01675}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-
CC         cysteinyl-tRNA(Cys) + phosphate; Xref=Rhea:RHEA:25686, Rhea:RHEA-
CC         COMP:9679, Rhea:RHEA-COMP:9719, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:78517, ChEBI:CHEBI:78551; EC=2.5.1.73;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01675};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01675};
CC   -!- SUBUNIT: Homodimer. Interacts with SepRS. {ECO:0000256|HAMAP-
CC       Rule:MF_01675}.
CC   -!- SIMILARITY: Belongs to the SepCysS family. {ECO:0000256|HAMAP-
CC       Rule:MF_01675}.
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DR   EMBL; CP001994; ADE35916.1; -; Genomic_DNA.
DR   EnsemblBacteria; ADE35916; ADE35916; Mmah_0384.
DR   KEGG; mmh:Mmah_0384; -.
DR   eggNOG; arCOG00091; Archaea.
DR   eggNOG; COG1103; LUCA.
DR   HOGENOM; HOG000015511; -.
DR   KO; K06868; -.
DR   OMA; WKLNTYG; -.
DR   BioCyc; MMAH547558:G1GHT-381-MONOMER; -.
DR   Proteomes; UP000001059; Chromosome.
DR   GO; GO:0043766; F:Sep-tRNA:Cys-tRNA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01675; Sep_Cys_tRNA_synth; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR013375; Sep_Cys-tRNA_synth_arc.
DR   InterPro; IPR008829; SepSecS/SepCysS.
DR   PANTHER; PTHR43586:SF3; PTHR43586:SF3; 1.
DR   Pfam; PF05889; SepSecS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02539; SepCysS; 1.
PE   3: Inferred from homology;
DR   PRODOM; D5E9R5.
DR   SWISS-2DPAGE; D5E9R5.
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_01675};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01675};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001059};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01675, ECO:0000313|EMBL:ADE35916.1}.
FT   REGION          152..153
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   REGION          280..282
FT                   /note="Pyridoxal phosphate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   BINDING         153
FT                   /note="Sulfur donor or Sep-tRNA(Cys)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   BINDING         177
FT                   /note="Sulfur donor or Sep-tRNA(Cys)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   BINDING         178
FT                   /note="Sulfur donor or Sep-tRNA(Cys)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   BINDING         257
FT                   /note="Pyridoxal phosphate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   BINDING         349
FT                   /note="Sulfur donor or Sep-tRNA(Cys)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   BINDING         358
FT                   /note="Sulfur donor or Sep-tRNA(Cys)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
FT   MOD_RES         283
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01675"
SQ   SEQUENCE   459 AA;  51249 MW;  F71B53DBECB31E64 CRC64;
     MKGAKDHLIG KTFEALFELE DMREVIRRSL PTGMSATEET AFMESTANLK SVIEDLEKGT
     SENQTNFPQI VDRIGLRYRE EGSINIQPIQ AAGRLTPEAR KALISYGDGY STCDSCRKPF
     RLDKISRPPI ADFHEELAGF VNMDTARVVP GARRGFQAVT SSLVGKGDSV IVSSLAHYTE
     FLAVEAAGGK VREIPLDHGN KVDIDSMAEK IEDVIREDGK PPSLMMMDHY DYQYANQHDI
     RSIAKVAHDY DIPVLYNGAY TVGVMPVDAK KLGADFVVGS GHKSMASPAP SGILATTDEY
     SDLVFRTTRM KGDVTGRKFG IKEVEMMGCT LMGGTLLAMM ASFPHVKERT QNWDEEVRNS
     NRFIEEFLKI EGNKVLSEYP RRHTLTKVDT THTFDKVAKE HKRRGFFLSD ELSKLGIVGM
     FPGATRAWKL NTYGLSREKI DYLSDAFKEI AVKYNLNVD
//

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