(data stored in ACNUC7421 zone)

SWISSPROT: A1AZ38_PARDP

ID   A1AZ38_PARDP            Unreviewed;       303 AA.
AC   A1AZ38;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   08-MAY-2019, entry version 104.
DE   RecName: Full=GTPase Era {ECO:0000256|HAMAP-Rule:MF_00367, ECO:0000256|SAAS:SAAS00085723};
GN   Name=era {ECO:0000256|HAMAP-Rule:MF_00367};
GN   OrderedLocusNames=Pden_0418 {ECO:0000313|EMBL:ABL68532.1};
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL68532.1, ECO:0000313|Proteomes:UP000000361};
RN   [1] {ECO:0000313|Proteomes:UP000000361}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Munk A.C., Brettin T., Bruce D., Han C., Tapia R.,
RA   Gilna P., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Spiro S., Richardson D.J., Moir J.W.B., Ferguson S.J.,
RA   van Spanning R.J.M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans
RT   PD1222.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: An essential GTPase that binds both GDP and GTP, with
CC       rapid nucleotide exchange. Plays a role in 16S rRNA processing and
CC       30S ribosomal subunit biogenesis and possibly also in cell cycle
CC       regulation and energy metabolism. {ECO:0000256|HAMAP-
CC       Rule:MF_00367}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00367,
CC       ECO:0000256|SAAS:SAAS00085777}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367}.
CC       Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00367}; Peripheral
CC       membrane protein {ECO:0000256|HAMAP-Rule:MF_00367}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-
CC       like GTPase superfamily. Era GTPase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00367, ECO:0000256|RuleBase:RU003761,
CC       ECO:0000256|SAAS:SAAS00858963}.
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DR   EMBL; CP000489; ABL68532.1; -; Genomic_DNA.
DR   RefSeq; WP_011746765.1; NC_008686.1.
DR   STRING; 318586.Pden_0418; -.
DR   PRIDE; A1AZ38; -.
DR   EnsemblBacteria; ABL68532; ABL68532; Pden_0418.
DR   KEGG; pde:Pden_0418; -.
DR   eggNOG; ENOG4105CWT; Bacteria.
DR   eggNOG; COG1159; LUCA.
DR   HOGENOM; HOG000245597; -.
DR   KO; K03595; -.
DR   OMA; HVKVAKD; -.
DR   BioCyc; PDEN318586:G1GW1-418-MONOMER; -.
DR   Proteomes; UP000000361; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070181; F:small ribosomal subunit rRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0042274; P:ribosomal small subunit biogenesis; IEA:UniProtKB-UniRule.
DR   CDD; cd04163; Era; 1.
DR   Gene3D; 3.30.300.20; -; 1.
DR   HAMAP; MF_00367; GTPase_Era; 1.
DR   InterPro; IPR030388; G_ERA_dom.
DR   InterPro; IPR005662; GTP-bd_Era.
DR   InterPro; IPR006073; GTP_binding_domain.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR004044; KH_dom_type_2.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   Pfam; PF07650; KH_2; 1.
DR   Pfam; PF01926; MMR_HSR1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54814; SSF54814; 1.
DR   TIGRFAMs; TIGR00436; era; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51713; G_ERA; 1.
DR   PROSITE; PS50823; KH_TYPE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A1AZ38.
DR   SWISS-2DPAGE; A1AZ38.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00367};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00367,
KW   ECO:0000256|SAAS:SAAS00165085};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000361};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00367,
KW   ECO:0000256|SAAS:SAAS00165149};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00367,
KW   ECO:0000256|RuleBase:RU003761, ECO:0000256|SAAS:SAAS00165089};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00367,
KW   ECO:0000256|SAAS:SAAS00085743};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00367,
KW   ECO:0000256|RuleBase:RU003761, ECO:0000256|SAAS:SAAS00415662};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000361};
KW   Ribosome biogenesis {ECO:0000256|HAMAP-Rule:MF_00367,
KW   ECO:0000256|SAAS:SAAS00165087};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00367, ECO:0000256|PROSITE-
KW   ProRule:PRU00118, ECO:0000256|RuleBase:RU003761,
KW   ECO:0000256|SAAS:SAAS00510808};
KW   rRNA-binding {ECO:0000256|HAMAP-Rule:MF_00367,
KW   ECO:0000256|SAAS:SAAS00165093}.
FT   DOMAIN        5    174       Era-type G. {ECO:0000259|PROSITE:
FT                                PS51713}.
FT   DOMAIN      205    282       KH type-2. {ECO:0000259|PROSITE:PS50823}.
FT   NP_BIND      13     20       GTP. {ECO:0000256|HAMAP-Rule:MF_00367}.
FT   NP_BIND      60     64       GTP. {ECO:0000256|HAMAP-Rule:MF_00367}.
FT   NP_BIND     124    127       GTP. {ECO:0000256|HAMAP-Rule:MF_00367}.
SQ   SEQUENCE   303 AA;  33630 MW;  4593C07D2CAD29F6 CRC64;
     MTQTRAGFVA LIGEPNAGKS TLLNRMVGAK VSIVTHKVQT TRARIRGIAM RGASQIVFVD
     TPGIFRPRRR LDRSMVKAAW GGAADADVIL LLIEAHRGLT DGTQAIIDNL RDHAGTTPVV
     LVINKIDRVK SETLLALSQQ VNAAFDFTRT FMISAEKGHG CDDLLEWLAG QVPEGPWLYP
     EDQVADLPMR MIAAEITREK LTLRLHEEIP YQLTVETERW EEKKDGSARV DQIVYVARPG
     HKGIVLGKGG ETIKAVGQAA RAELAEFMGR PVHLFLQVKV RENWLDEAER YNEMGLDFRD
     GDA
//

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