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DER_COREF
ID   DER_COREF               Reviewed;         528 AA.
AC   Q8FTK5;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 2.
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=CE1561;
OS   Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS   / NBRC 100395).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX   PubMed=12840036; DOI=10.1101/gr.1285603;
RA   Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA   Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT   "Comparative complete genome sequence analysis of the amino acid
RT   replacements responsible for the thermostability of Corynebacterium
RT   efficiens.";
RL   Genome Res. 13:1572-1579(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC18371.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000035; BAC18371.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q8FTK5; -.
DR   SMR; Q8FTK5; -.
DR   STRING; 196164.23493401; -.
DR   PRIDE; Q8FTK5; -.
DR   EnsemblBacteria; BAC18371; BAC18371; BAC18371.
DR   KEGG; cef:CE1561; -.
DR   eggNOG; COG1160; Bacteria.
DR   HOGENOM; CLU_016077_6_2_11; -.
DR   Proteomes; UP000001409; 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..528
FT                   /note="GTPase Der"
FT                   /id="PRO_0000178987"
FT   DOMAIN          90..253
FT                   /note="EngA-type G 1"
FT   DOMAIN          263..436
FT                   /note="EngA-type G 2"
FT   DOMAIN          437..519
FT                   /note="KH-like"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..62
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         96..103
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         143..147
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         205..208
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         269..276
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         316..320
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
FT   BINDING         381..384
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00195"
SQ   SEQUENCE   528 AA;  59233 MW;  1B81E91361798BE6 CRC64;
     MDVEGAFADE EELAPHGGWA SKDFDPSEFG YDDDFAPDDS DEDEDDDDYE FDEDDFAAPD
     FGEDYTEEEW EELERSLGIE RREHLEESLC TVAIVGRPNV GKSTLVNRFI GRREAVVEDF
     PGVTRDRISY LSDWGGQRFW VQDTGGWDPN VKGIHASIAH QAELAMASAD VIVFVVDTKV
     GITETDAVMA RKLKRADVPV ILVANKFDSD SQWADMAEFY ALGLGDPFPV SAQHGRGGAD
     VLDKILESFP EEPRAKSIVE GPRRVALVGK PNVGKSSLLN KFAGEERSVV DNVAGTTVDP
     VDSIIQLDQK MWKFIDTAGL RKKVKTATGH EFYASLRTRS VIDSAEVCVL LIDSSEPITE
     QDQRVLAMIT DAGKALVVAF NKWDLMDEDR RWELDRELDL QLAHIPWAKR INISAKTGRA
     LQRLEPAMIE ALENWDRRVS TGQLNNWLRE AIAANPPPMR GGRLPRVLFA TQASTRPPVI
     VLFTTGFLEA GYRRYLERKF RERFGFNGTP IRIAVRVRER RGKGGKKQ
 
 
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