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Database: UniProt
Entry: A0A286EBP6_9NEIS
LinkDB: A0A286EBP6_9NEIS
Original site: A0A286EBP6_9NEIS 
ID   A0A286EBP6_9NEIS        Unreviewed;       946 AA.
AC   A0A286EBP6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=SAMN02746062_01194 {ECO:0000313|EMBL:SOD68300.1};
OS   Alysiella filiformis DSM 16848.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Alysiella.
OX   NCBI_TaxID=1120981 {ECO:0000313|EMBL:SOD68300.1, ECO:0000313|Proteomes:UP000219669};
RN   [1] {ECO:0000313|EMBL:SOD68300.1, ECO:0000313|Proteomes:UP000219669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16848 {ECO:0000313|EMBL:SOD68300.1,
RC   ECO:0000313|Proteomes:UP000219669};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       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 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
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DR   EMBL; OCNF01000008; SOD68300.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A286EBP6; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000219669; 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   CDD; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_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   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
DR   PROSITE; PS01176; IF2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000219669}.
FT   DOMAIN          446..615
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..597
FT                   /note="G-domain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   COMPBIAS        7..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..59
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..257
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..340
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         455..462
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         501..505
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         555..558
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   946 AA;  101517 MW;  61BF1BE021E682AC CRC64;
     MSNNRNNKPE VEHKGGKKVK MSREEMLAQL KAEQSAQTAK TETPATPAPA NTAPQPENAS
     APLSAEDAER AAKKAAAEAE AAKLKAAKAA KSAKSETAKT VKETVADSPE TPSVSTENSS
     EKQPEKAPAA PSDNAPAGEN GETKEKRKRS RGGRNRNKNK DKDGAPEAVP TLVEVVNAEE
     AARREAEAEQ ERKRREAQEA LLREKQERAE RQARREAAKA QAAEEARLAA AAKKEGKDGK
     GVRTAKPSEE KLAQKAAETK SPKPIAKTND KASKPAEKVA KPVSGSLNDE NPSSGSRKKD
     DRRHSRDDDA PKGKGGKNVK GGRNDSRNAG GDDERVRGGN KKAKKLKLAP NQHAFQAPTE
     PVVHEVLVPE TITVADLAHK MAVKGVEVVK TLMKMGMMVT INQSLDQDTA LLVVEEMGHI
     GKPAAIDDPD AFLNDDSTHV DAEMLPRPPV VTVMGHVDHG KTSLLDHIRK TRVVSGEAGG
     ITQHIGAYHV ETPRGVVTFL DTPGHEAFTA MRARGAKATD IVILVVAADD GVMPQTVEAI
     AHAKAAGVPI VVAVNKIDKD SANPERIRQE LTQHEVVCDE WGGDVQFVDV SAKHGINIDK
     LLEAVLLEAE VLELKAPVAA PAKGLIVEAK LDKGRGAVAT LLVQSGTLRK GDMLLAGTTF
     GKIRAMLDEN GKPIDEAGPS IPVEILGLSD VPNAGEDALV LADEKKAREV ALFRQGKFRD
     VRLAKQQAAK LENMFNNMGE NQAQNLSIII KADVQGSYEA LAGSLQKLST DEVRVQVLHS
     GVGGISESDV NLAIASGALI IAFNVRADNA ARKLAETEDV EIRYYNIIYD AIDDVKAAMS
     GMLSPEEKEQ ITGTVEIRQV ITVSKVGNIA GCMVTDGLVK RDSKVRLIRN NVVIHTGELS
     SLKRFKDDVK EVKMGFECGL MIKNFNEIME GDQLECFDVV EVARTL
//
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