位置:首页 > 蛋白库 > SELA_CLOP1
SELA_CLOP1
ID   SELA_CLOP1              Reviewed;         462 AA.
AC   Q0TNJ4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000255|HAMAP-Rule:MF_00423};
DE            EC=2.9.1.1 {ECO:0000255|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteine synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE            Short=Sec synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000255|HAMAP-Rule:MF_00423};
GN   Name=selA {ECO:0000255|HAMAP-Rule:MF_00423}; OrderedLocusNames=CPF_2373;
OS   Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB
OS   6125 / NCTC 8237 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=195103;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S 107 /
RC   Type A;
RX   PubMed=16825665; DOI=10.1101/gr.5238106;
RA   Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T.,
RA   Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H.,
RA   Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A.,
RA   Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D.,
RA   Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J.,
RA   Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B.,
RA   Paulsen I.T.;
RT   "Skewed genomic variability in strains of the toxigenic bacterial pathogen,
RT   Clostridium perfringens.";
RL   Genome Res. 16:1031-1040(2006).
CC   -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC       required for selenoprotein biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_00423}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-
CC         selenocysteinyl-tRNA(Sec) + phosphate; Xref=Rhea:RHEA:22728,
CC         Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9743, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78533,
CC         ChEBI:CHEBI:78573; EC=2.9.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00423};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00423};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC       (bacterial route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00423}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00423}.
CC   -!- SIMILARITY: Belongs to the SelA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00423}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000246; ABG83629.1; -; Genomic_DNA.
DR   RefSeq; WP_003455025.1; NC_008261.1.
DR   AlphaFoldDB; Q0TNJ4; -.
DR   SMR; Q0TNJ4; -.
DR   STRING; 195103.CPF_2373; -.
DR   PRIDE; Q0TNJ4; -.
DR   EnsemblBacteria; ABG83629; ABG83629; CPF_2373.
DR   GeneID; 29570519; -.
DR   KEGG; cpf:CPF_2373; -.
DR   eggNOG; COG1921; Bacteria.
DR   HOGENOM; CLU_038142_1_0_9; -.
DR   OMA; GATNRTH; -.
DR   OrthoDB; 1124266at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000001823; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   HAMAP; MF_00423; SelA; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR018319; SelA-like.
DR   InterPro; IPR004534; SelA_trans.
DR   Pfam; PF03841; SelA; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00474; selA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Protein biosynthesis; Pyridoxal phosphate; Selenium;
KW   Transferase.
FT   CHAIN           1..462
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_1000050360"
FT   MOD_RES         292
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   462 AA;  51913 MW;  3B593E49C954FA2A CRC64;
     MTKELLRALP KIDEILGIFN EDFLNENGRE TVVSALRDII NENRKAILNE EVDYALTKEE
     AKSKCEHRLL KKRERNLKRV INGTGVVIHT NLGRSLLSKE ATEAVALAAS SYSNLEYDLE
     KGERGSRYSL IEGIIKDITG AEAALVVNNN AAAIMLVLNS LCENKEVIVS RGELVEIGGS
     FRIPEVMNFS RAKLVEVGTT NRTHLYDYED AITEETGAFL KVHSSNFKIV GFTKSVSANE
     ICNLAREKDI PVIEDIGSGV LIDLSKYGLE KEPTVIESLE DGVDVVTFSG DKMLGGAQAG
     IIVGKKKFID KIKRNQLTRA LRVDKFTLAA LEITLKHYLN EKEAIEKIPT LHMMTLDLKE
     IKERANRLYK NLERLNKFYK FSIEEGESTV GGGSMPDSKL STYLLRIDSD SINEVNLERE
     LREYKIPIIT RVYKGAVYID LRTILEDDYE VIFNALKEIG EK
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024