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DER_CHLTR
ID   DER_CHLTR               Reviewed;         490 AA.
AC   O84709;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=CT_703;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68298.1; -; Genomic_DNA.
DR   PIR; H71480; H71480.
DR   RefSeq; NP_220222.1; NC_000117.1.
DR   RefSeq; WP_009872078.1; NC_000117.1.
DR   AlphaFoldDB; O84709; -.
DR   SMR; O84709; -.
DR   STRING; 813.O172_03885; -.
DR   EnsemblBacteria; AAC68298; AAC68298; CT_703.
DR   GeneID; 884507; -.
DR   KEGG; ctr:CT_703; -.
DR   PATRIC; fig|272561.5.peg.774; -.
DR   HOGENOM; CLU_016077_6_2_0; -.
DR   InParanoid; O84709; -.
DR   OMA; KFRFLEY; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
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; 1.
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..490
FT                   /note="GTPase Der"
FT                   /id="PRO_0000178982"
FT   DOMAIN          1..165
FT                   /note="EngA-type G 1"
FT   DOMAIN          227..400
FT                   /note="EngA-type G 2"
FT   DOMAIN          401..485
FT                   /note="KH-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         7..14
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         54..58
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         117..120
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         233..240
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         280..284
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         345..348
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   490 AA;  55569 MW;  203A51FF454071F4 CRC64;
     MRIAILGRPN VGKSSLFNRL CKRSLAIVNS QEGTTRDRLY GEIRAWDSII HVIDTGGVDQ
     ESTDRFQKQI HQQALAAAEE ASVLLLVVDI RCGITKQDEE LAKRLLPLKK PLILVMNKAD
     SQQDLQRIHE FYGLGISDMI ATSASHDKHI DLLLERIRQI AQIPVPSVEE QDAVQEDELP
     SEEAAISLHA FADETLFENE SLSQEEASFL EELVAQTATP APVDRPLKVA LIGHPNVGKS
     SIINALLKEE RCITDNSPGT TRDNIDVAYT HNNKEYVFID TAGLRKTKSI KNSVEWMSSS
     RTEKAISRTD ICLLVIDATQ QLSYQDKRIL SMIARYKKPH VILVNKWDLM FGVRMEHYVQ
     DLRKMDPYIG QARILCISAK QRRNLLQIFS AIDDIYTIAT TKLSTSLVNK VLASAMQRHH
     PQVINGKRLR IYYAIHKTTT PFTFLLFINS NSLLTKPYEL YLKNTLKAAF NLYRVPFDLE
     YKAKPARKSN
 
 
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