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DER_CAMJE
ID   DER_CAMJE               Reviewed;         460 AA.
AC   Q9PIB6; Q0PBC4;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=GTPase Der {ECO:0000255|HAMAP-Rule:MF_00195};
DE   AltName: Full=GTP-binding protein EngA {ECO:0000255|HAMAP-Rule:MF_00195};
GN   Name=der {ECO:0000255|HAMAP-Rule:MF_00195}; Synonyms=engA;
GN   OrderedLocusNames=Cj0386;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
CC   -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC       ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_00195}.
CC   -!- SUBUNIT: Associates with the 50S ribosomal subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00195}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. EngA (Der) GTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00195}.
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DR   EMBL; AL111168; CAL34536.1; -; Genomic_DNA.
DR   PIR; H81381; H81381.
DR   RefSeq; WP_002858744.1; NC_002163.1.
DR   RefSeq; YP_002343823.1; NC_002163.1.
DR   AlphaFoldDB; Q9PIB6; -.
DR   SMR; Q9PIB6; -.
DR   IntAct; Q9PIB6; 7.
DR   STRING; 192222.Cj0386; -.
DR   PaxDb; Q9PIB6; -.
DR   PRIDE; Q9PIB6; -.
DR   EnsemblBacteria; CAL34536; CAL34536; Cj0386.
DR   GeneID; 904709; -.
DR   KEGG; cje:Cj0386; -.
DR   PATRIC; fig|192222.6.peg.377; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_7; -.
DR   OMA; KFRFLEY; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_00195; GTPase_Der; 1.
DR   InterPro; IPR031166; G_ENGA.
DR   InterPro; IPR006073; GTP-bd.
DR   InterPro; IPR016484; GTP-bd_EngA.
DR   InterPro; IPR032859; KH_dom-like.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   Pfam; PF14714; KH_dom-like; 1.
DR   Pfam; PF01926; MMR_HSR1; 2.
DR   PIRSF; PIRSF006485; GTP-binding_EngA; 1.
DR   PRINTS; PR00326; GTP1OBG.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   TIGRFAMs; TIGR03594; GTPase_EngA; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 2.
DR   PROSITE; PS51712; G_ENGA; 2.
PE   3: Inferred from homology;
KW   GTP-binding; Nucleotide-binding; Reference proteome; Repeat;
KW   Ribosome biogenesis.
FT   CHAIN           1..460
FT                   /note="GTPase Der"
FT                   /id="PRO_0000178977"
FT   DOMAIN          2..164
FT                   /note="EngA-type G 1"
FT   DOMAIN          196..368
FT                   /note="EngA-type G 2"
FT   DOMAIN          369..453
FT                   /note="KH-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         8..15
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         55..59
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         116..119
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         202..209
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         249..253
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         313..316
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   460 AA;  52641 MW;  0BCE9E2509F560C2 CRC64;
     MQSIILIGKP NVGKSSLFNR MARQRIAITS DISGTTRDTN KTQIHIHSKK AMLIDSGGLD
     ESDELFKNVK KNTLKVAKES DIILYLVDGK LAPDDEDRQF FYSLKKLGKP IALVINKVDN
     KKDEERAWEF ANFGVKEIFN LSVTHNVGLD ELYEWLEKFL HEEFLIPDEE ENLEDFLEYY
     EEGKEFQFKE VDQNHIRVGI VGRVNVGKSS LLNALVKQER SVVSSIAGTT IDPVNESVVH
     KDKVIEFVDT AGIRKRGKIQ GLERFALNRT EKILSHSQIA LLVLDAHEGF NELDERIAGL
     VAKHYLGVII VLNKWDKSEM DFDKTVKELR LDRFKFLAYA PVISVSALSG KRVHVLLDKI
     LQIFENFTQK IQTSKLNTLI ENATRAHPLP HDYGKLVKIY YAVQYDLAPP KIALIMNRPK
     ALHFSYKRYL QNQIRKEFNF EGVPLVIASR KKGSKENDES
 
 
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