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Database: UniProt
Entry: B6WX87_9DELT
LinkDB: B6WX87_9DELT
Original site: B6WX87_9DELT 
ID   B6WX87_9DELT            Unreviewed;       610 AA.
AC   B6WX87;
DT   20-JAN-2009, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2009, sequence version 1.
DT   28-MAR-2018, entry version 51.
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   ECO:0000313|EMBL:EEB32407.1};
GN   ORFNames=DESPIG_02713 {ECO:0000313|EMBL:EEB32407.1};
OS   Desulfovibrio piger ATCC 29098.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=411464 {ECO:0000313|EMBL:EEB32407.1, ECO:0000313|Proteomes:UP000003676};
RN   [1] {ECO:0000313|EMBL:EEB32407.1, ECO:0000313|Proteomes:UP000003676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29098 {ECO:0000313|EMBL:EEB32407.1,
RC   ECO:0000313|Proteomes:UP000003676};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M.,
RA   Liep D., Gordon J.;
RT   "Draft genome sequence of Desulvovibrio piger (ATCC 29098).";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEB32407.1, ECO:0000313|Proteomes:UP000003676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29098 {ECO:0000313|EMBL:EEB32407.1,
RC   ECO:0000313|Proteomes:UP000003676};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H.,
RA   Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2008) 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: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EEB32407.1}.
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DR   EMBL; ABXU01000078; EEB32407.1; -; Genomic_DNA.
DR   ProteinModelPortal; B6WX87; -.
DR   STRING; 411464.DESPIG_02713; -.
DR   EnsemblBacteria; EEB32407; EEB32407; DESPIG_02713.
DR   eggNOG; ENOG4107QHU; Bacteria.
DR   eggNOG; COG0532; LUCA.
DR   OrthoDB; POG091H00EY; -.
DR   Proteomes; UP000003676; Unassembled WGS sequence.
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; 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   Complete proteome {ECO:0000313|Proteomes:UP000003676};
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:EEB32407.1};
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:UP000003676}.
FT   DOMAIN      109    278       Tr-type G. {ECO:0000259|PROSITE:PS51722}.
FT   NP_BIND     118    125       GTP. {ECO:0000256|HAMAP-Rule:MF_00100}.
FT   NP_BIND     164    168       GTP. {ECO:0000256|HAMAP-Rule:MF_00100}.
FT   NP_BIND     218    221       GTP. {ECO:0000256|HAMAP-Rule:MF_00100}.
FT   REGION      112    260       G-domain. {ECO:0000256|HAMAP-Rule:
FT                                MF_00100}.
SQ   SEQUENCE   610 AA;  66238 MW;  F9F9283BAB80CDED CRC64;
     MNRSTRGRRK PGKPAAVQAT QPLKAAKRKI RVTEAIRVAD MAHQMGLKAN EIIKVLFGLG
     VMATINQSLD IDTATLVAAE FDYEVEKAGF SEEDYLLPQQ EDKPEDLKPR PPVVTIMGHV
     DHGKTSLLDA IRKSNVTSGE AGGITQHIGA YHVKTKRGEI VFLDTPGHEA FTAMRARGAQ
     VTDLVILVVA ADDGVMEQTR EAVNHSRAAG VPIMVAVNKM DKPGADPDRV LRELSEMGLQ
     PEDWGGDTIV AKVSAKTRQG LDDLLELVAL QSEIMDLKAN PNKPAHGRIV EAKLDKGRGP
     VATVLIQEGT LHQGDNFVCG QFSGRVRALM NDQGKKVKEA GPSIPVEVQG FEGVPEAGEE
     FFAVADEKLA RRIAEMRATK QRERDLASES KVTLETFLSR RASDQETLTL NLVLKADVQG
     SLEAITEALN KQSTEKVRIN VVHGGTGAIS ESDIMLASAS QAIIIGFNVR PTSRIKDIAE
     RENVDIRFYD IIYKLVDDIK SAMAGLLAPV QREVYLGQAE VRNTFSVPKV GIIAGSYVAD
     GKIARNAGVR LLRDGVVVYT GKISSLKRFK DDAREVVKGN ECGVGLENFN DVKIGDIIEA
     FETVEEAATL
//
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