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Database: UniProt
Entry: A0A0K1J7H9_9RHOO
LinkDB: A0A0K1J7H9_9RHOO
Original site: A0A0K1J7H9_9RHOO 
ID   A0A0K1J7H9_9RHOO        Unreviewed;       939 AA.
AC   A0A0K1J7H9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   28-MAR-2018, entry version 18.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|HAMAP-Rule:MF_00100, ECO:0000256|RuleBase:RU000644, ECO:0000256|SAAS:SAAS00048520};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=AzCIB_2622 {ECO:0000313|EMBL:AKU12515.1};
OS   Azoarcus sp. CIB.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Zoogloeaceae; Azoarcus.
OX   NCBI_TaxID=198107 {ECO:0000313|EMBL:AKU12515.1, ECO:0000313|Proteomes:UP000066621};
RN   [1] {ECO:0000313|EMBL:AKU12515.1, ECO:0000313|Proteomes:UP000066621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIB {ECO:0000313|EMBL:AKU12515.1,
RC   ECO:0000313|Proteomes:UP000066621};
RA   Martin-Moldes Z., Zamarro M.T., del Cerro C., Valencia A., Gomez M.J.,
RA   Udaondo Z., Garcia J.L., Nogales J., Carmona M., Diaz E.;
RT   "Whole-genome analysis of Azoarcus sp. strain CIB provides genetic
RT   insights to its different lifestyles and predicts novel metabolic
RT   features.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the essential components for the initiation of
CC       protein synthesis. Protects formylmethionyl-tRNA from spontaneous
CC       hydrolysis and promotes its binding to the 30S ribosomal subunits.
CC       Also involved in the hydrolysis of GTP during the formation of the
CC       70S ribosomal complex. {ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644, ECO:0000256|SAAS:SAAS00320074}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|SAAS:SAAS00362982}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644, ECO:0000256|SAAS:SAAS00554628}.
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DR   EMBL; CP011072; AKU12515.1; -; Genomic_DNA.
DR   RefSeq; WP_050416276.1; NZ_CP011072.1.
DR   EnsemblBacteria; AKU12515; AKU12515; AzCIB_2622.
DR   KEGG; azi:AzCIB_2622; -.
DR   PATRIC; fig|198107.6.peg.2728; -.
DR   KO; K02519; -.
DR   Proteomes; UP000066621; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10050; -; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR013575; IF2_assoc_dom_bac.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; TF_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   PANTHER; PTHR43381; PTHR43381; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF46955; SSF46955; 1.
DR   SUPFAM; SSF50447; SSF50447; 2.
DR   SUPFAM; SSF52156; SSF52156; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00487; IF-2; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000066621};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
KW   ECO:0000256|SAAS:SAAS00048564};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00100,
KW   ECO:0000256|SAAS:SAAS00048516};
KW   Initiation factor {ECO:0000256|HAMAP-Rule:MF_00100,
KW   ECO:0000256|RuleBase:RU000644, ECO:0000256|SAAS:SAAS00440472,
KW   ECO:0000313|EMBL:AKU12515.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00100,
KW   ECO:0000256|SAAS:SAAS00048538};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00100,
KW   ECO:0000256|RuleBase:RU000644, ECO:0000256|SAAS:SAAS00048553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000066621}.
FT   DOMAIN      439    608       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND     448    455       GTP. {ECO:0000256|HAMAP-Rule:MF_00100}.
FT   NP_BIND     494    498       GTP. {ECO:0000256|HAMAP-Rule:MF_00100}.
FT   NP_BIND     548    551       GTP. {ECO:0000256|HAMAP-Rule:MF_00100}.
FT   REGION      442    590       G-domain. {ECO:0000256|HAMAP-Rule:
FT                                MF_00100}.
FT   COILED      230    259       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   939 AA;  101192 MW;  37749675607D2C2C CRC64;
     MEQMSVNQFA GELRMPAAVL LEQLQKAGVE KTSPDQLLTE HDKARLLEYL RRSHGDSQPK
     GKITLTRKET SEIRATDSSG RARTVQVEVR KKRVFVKRDE IGGESGAGEM PSVEETLAAA
     IEAVVEPVAE AVPEAPAVEI PAVVEVEPEP VVESIPEPEP QPEPEPEPEP VIEAAAEEPA
     AEAVEDAPSA PASAQRQRVS ILSDEERASR EREARRHEEL RSRQMADLKA KQEREAAARA
     AAESRRAEEE ARVRAEAEKR AEAAKPEIRE AAKAPSGTLH RPAKSEDKSV GKDAKRGARG
     GVAEAGAGDS AKRRGLKTRG EVGATTGSWR GARGGGRGRG QQDDHKAFQM PTEPVVREIH
     VPETITVADL AHKMAVKAAE VIKALMKMGS MVTINQVLDQ ETAMILVEEM GHKAFAAKLD
     DPDAFLEDTA TQADATVESR APVVTVMGHV DHGKTSLLDY IRRAKVASGE AGGITQHIGA
     YHVETPRGML TFLDTPGHEA FTAMRARGAK ATDIVILVVA ADDGVMPQTR EAIHHAKAAG
     VPIVVAVNKI DKHEANPDRV KQELIVEGVV PEEYGGEVMF INVSAKTGVG IDNLLESILL
     QAEVLELTAP VDTPAKGLII EARLDKGRGP VASLLVQSGT LRKGDVMLVG ATFGRIRAML
     DENGKAIDEA GPSIPVEILG LSDVPAAGDE AIVLADEKKA REIALFRQGK FREVKLAKQQ
     AAKLESMFEQ MAEGEVKSLP LIIKADVQGS QEALVQSLNK LSTDEVRVNA IHSAVGAISE
     SDVNLAQASG AVIIGFNTRA DAGARKLAET FGVDIRYYNI IYDAVDDVRA ALSGLLSPER
     RENQLGLVEV RQVFRVPKIG TVAGCYVLEG NVKRGAQIRV LRGNVVVHTG ELESLKRFKD
     DVKEVKFGFE CGLSVKNYND VQEGDQLEVF EIQEIARTL
//
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