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Database: UniProt
Entry: K9SHF2_9CYAN
LinkDB: K9SHF2_9CYAN
Original site: K9SHF2_9CYAN 
ID   K9SHF2_9CYAN            Unreviewed;      1104 AA.
AC   K9SHF2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   18-JUL-2018, entry version 38.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|HAMAP-Rule:MF_00100, ECO:0000256|RuleBase:RU000644};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=Pse7367_1758 {ECO:0000313|EMBL:AFY70037.1};
OS   Pseudanabaena sp. PCC 7367.
OC   Bacteria; Cyanobacteria; Synechococcales; Pseudanabaenaceae;
OC   Pseudanabaena.
OX   NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY70037.1, ECO:0000313|Proteomes:UP000010386};
RN   [1] {ECO:0000313|EMBL:AFY70037.1, ECO:0000313|Proteomes:UP000010386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY70037.1,
RC   ECO:0000313|Proteomes:UP000010386};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y.,
RA   Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A.,
RA   Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL   Submitted (MAY-2012) 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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100}.
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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR   EMBL; CP003592; AFY70037.1; -; Genomic_DNA.
DR   RefSeq; WP_015165003.1; NC_019701.1.
DR   EnsemblBacteria; AFY70037; AFY70037; Pse7367_1758.
DR   KEGG; pseu:Pse7367_1758; -.
DR   PATRIC; fig|82654.3.peg.2046; -.
DR   KO; K02519; -.
DR   OrthoDB; POG091H00EY; -.
DR   Proteomes; UP000010386; 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; 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; PF04760; IF2_N; 2.
DR   PRINTS; PR00315; ELONGATNFCT.
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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000010386};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW   Initiation factor {ECO:0000256|HAMAP-Rule:MF_00100,
KW   ECO:0000256|RuleBase:RU000644, ECO:0000313|EMBL:AFY70037.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00100,
KW   ECO:0000256|RuleBase:RU000644};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010386}.
FT   DOMAIN      596    768       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND     605    612       GTP. {ECO:0000256|HAMAP-Rule:MF_00100}.
FT   NP_BIND     655    659       GTP. {ECO:0000256|HAMAP-Rule:MF_00100}.
FT   NP_BIND     709    712       GTP. {ECO:0000256|HAMAP-Rule:MF_00100}.
SQ   SEQUENCE   1104 AA;  118976 MW;  D9B9B1B44D6D3D12 CRC64;
     MSISRVRVYE LKRELDLETK EILGICDRLG IPVKSHSSTI TEAEADRIRN FAQNRDQSAK
     LDKSEPEVAE PVSSANKESS TASASKQEIL INTVSRPATI KQLQKPTAAE PPAPSRPVVV
     EPSPQEQAEP AVAATKPSKK NSKATTNTKG TAQNTDNGAI AKAPTSSSSA QLKQPPARPA
     ESAGEVVEIS EIAPANDQPE LAKPPAAKAK SKAAQEAAPA ANTASNAASK AEQNKAEQKP
     EATLAKKPEL IKPVPRSTAI EQPAQTAAIA GNSSSSTSST SSANPVSPTS SGKKASKTSK
     PGKSAEPDKT TISVGSAPKN NREQPARPQL HRPKPVKDAV LIERGITAPT EPKPQQILQP
     PVRPTAKPVA KDDEATETDG AEIAAKPPGL ELAAPPERPI KLSRVAAKVN KRGKTKREEE
     EEEDTEVRAK KPNRLKRYKV IEDDIDDIDD DLENGDLDDA SNLSTARPTA RPPKPKQARS
     TGAENKPIPA KPSRKPARDR RSSQPEKQIE KPELIELSDS VTVQELADQM LVSETEVIRT
     LFMKGVMVNI NQTLDVPTAR MVAEELGYEV EEIETDAPAR KITEMIDLED IESLVRRPPV
     VTIMGHVDHG KTTLLDSIRE SKVAQGEAGG ITQHIGAYHV DVEHEDGVKQ VVFLDTPGHE
     AFTAMRARGA RVTDIAILVV AADDGVQPQT IEAISHAKAA NVPIVVAINK VDKPEAQPDR
     IRQELTEYGL VDEEWGGETI MVPVSAIEGS NLDTLLEMIL LVAEIEDLQA NPDRTARGTI
     IEAHLDKARG PVATFLVQNG TLRVGDVFVA GSVFGKVRAM IDDRGERVDA ADPSFAVEVL
     GLNEVPAAGD EFQVYLEEKK ARSLASDRAE QQRQSRLQQT MSSRRVTLGT VSAQAQEGEL
     KELNLILKAD VQGSVEAILG SLEQLPQEEV QIRVLLSAPG EITENDVELA AASDAVIIGF
     NTSMATGARQ AADNLGVDVR DYDVIYKLLE DIRDAMEGLL EPELVEEHLG QAEVRALFTV
     GKGVVAGCYV QSGKLIRNCK VRVLRKGEVI TTGSLDSLKR MREDAKEVAS GFECGVGIDR
     FASWQEGDIV DAYRMVTKRR TLKS
//
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