(data stored in ACNUC7421 zone)

SWISSPROT: C1ASX2_RHOOB

ID   C1ASX2_RHOOB            Unreviewed;       475 AA.
AC   C1ASX2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   07-JUN-2017, entry version 68.
DE   RecName: Full=GTPase Der {ECO:0000256|HAMAP-Rule:MF_00195, ECO:0000256|RuleBase:RU004481, ECO:0000256|SAAS:SAAS00336749};
DE   AltName: Full=GTP-binding protein EngA {ECO:0000256|HAMAP-Rule:MF_00195};
GN   Name=engA {ECO:0000313|EMBL:BAH48904.1};
GN   Synonyms=der {ECO:0000256|HAMAP-Rule:MF_00195};
GN   OrderedLocusNames=ROP_06570 {ECO:0000313|EMBL:BAH48904.1};
OS   Rhodococcus opacus (strain B4).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH48904.1, ECO:0000313|Proteomes:UP000002212};
RN   [1] {ECO:0000313|EMBL:BAH48904.1, ECO:0000313|Proteomes:UP000002212}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:BAH48904.1,
RC   ECO:0000313|Proteomes:UP000002212};
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus
RT   erythropolis PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: GTPase that plays an essential role in the late steps of
CC       ribosome biogenesis. {ECO:0000256|HAMAP-Rule:MF_00195,
CC       ECO:0000256|RuleBase:RU004481, ECO:0000256|SAAS:SAAS00534042}.
CC   -!- SUBUNIT: Associates with the 50S ribosomal subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_00195, ECO:0000256|SAAS:SAAS00336741}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
CC       like GTPase superfamily. EngA (Der) GTPase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00195, ECO:0000256|PROSITE-
CC       ProRule:PRU01049, ECO:0000256|RuleBase:RU004481,
CC       ECO:0000256|SAAS:SAAS00534053}.
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DR   EMBL; AP011115; BAH48904.1; -; Genomic_DNA.
DR   RefSeq; WP_012687907.1; NC_012522.1.
DR   ProteinModelPortal; C1ASX2; -.
DR   STRING; 632772.ROP_06570; -.
DR   EnsemblBacteria; BAH48904; BAH48904; ROP_06570.
DR   KEGG; rop:ROP_06570; -.
DR   PATRIC; fig|632772.20.peg.717; -.
DR   eggNOG; ENOG4105DKZ; Bacteria.
DR   eggNOG; COG1160; LUCA.
DR   HOGENOM; HOG000242861; -.
DR   KO; K03977; -.
DR   OMA; FCNLPQY; -.
DR   OrthoDB; POG091H00QI; -.
DR   Proteomes; UP000002212; Chromosome.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_00195; GTPase_Der; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR031166; G_ENGA.
DR   InterPro; IPR016484; GTP-bd_EngA.
DR   InterPro; IPR006073; GTP_binding_domain.
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   SMART; SM00382; AAA; 2.
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;
DR   PRODOM; C1ASX2.
DR   SWISS-2DPAGE; C1ASX2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002212};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00195,
KW   ECO:0000256|RuleBase:RU004481, ECO:0000256|SAAS:SAAS00038177};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00195,
KW   ECO:0000256|RuleBase:RU004481, ECO:0000256|SAAS:SAAS00038187};
KW   Repeat {ECO:0000256|RuleBase:RU004481, ECO:0000256|SAAS:SAAS00038179};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00195,
KW   ECO:0000256|SAAS:SAAS00038183}.
FT   DOMAIN       39    202       EngA-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51712}.
FT   DOMAIN      212    385       EngA-type G (guanine nucleotide-binding).
FT                                {ECO:0000259|PROSITE:PS51712}.
FT   NP_BIND      45     52       GTP 1. {ECO:0000256|HAMAP-Rule:MF_00195}.
FT   NP_BIND      92     96       GTP 1. {ECO:0000256|HAMAP-Rule:MF_00195}.
FT   NP_BIND     154    157       GTP 1. {ECO:0000256|HAMAP-Rule:MF_00195}.
FT   NP_BIND     218    225       GTP 2. {ECO:0000256|HAMAP-Rule:MF_00195}.
FT   NP_BIND     265    269       GTP 2. {ECO:0000256|HAMAP-Rule:MF_00195}.
FT   NP_BIND     330    333       GTP 2. {ECO:0000256|HAMAP-Rule:MF_00195}.
SQ   SEQUENCE   475 AA;  51950 MW;  10817AD8E07BE805 CRC64;
     MTEQFTTEFA GDGTWSEESD WEVLDLEDGG DGEAHVPVPT LAVVGRPNVG KSTLVNRIIG
     RREAVVEDIP GVTRDRVSYE ANWSGRRFMV QDTGGWEPDA KGLQQSVARQ AELAMQTADA
     ILLVVDAVVG ATATDEAVAK VLRRSKTPVL LVANKVDDGR TESEVAALWS LGLGQPHSVS
     ATHGRGTGDL LDEVLAALPE TPREGIPGGG PRRVALVGKP NVGKSSLLNK LSGDERSVVH
     NVAGTTVDPV DSIVELGGRP WRFVDTAGLR KRVSHASGAE FYASLRTKSA IEAAEVAILL
     IDASEPISEQ DLRVLSMVAD AGRALVIAFN KWDLVDEDRR LQLDREVDRD LVRVPWAQRV
     NISAQTGRAV QKLVPALDTA LESWDKRIPT GRLNTWLKEV VAATPPPMRG GRLPRVMFAT
     QAGTRPPTFV LFTTGFLEAG YRRFLERRLR EEFNFDGSPV RISVRVREKR ERRSR
//

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