ID A0A1G9HZ95_9RHOB Unreviewed; 847 AA.
AC A0A1G9HZ95;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=SAMN04487971_10775 {ECO:0000313|EMBL:SDL18116.1};
OS Paracoccus chinensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=525640 {ECO:0000313|EMBL:SDL18116.1, ECO:0000313|Proteomes:UP000199555};
RN [1] {ECO:0000313|EMBL:SDL18116.1, ECO:0000313|Proteomes:UP000199555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7655 {ECO:0000313|EMBL:SDL18116.1,
RC ECO:0000313|Proteomes:UP000199555};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; FNGE01000007; SDL18116.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9HZ95; -.
DR STRING; 525640.SAMN04487971_10775; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000199555; 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; IPR013575; IF2_assoc_dom_bac.
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; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 1.
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}.
FT DOMAIN 345..513
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 354..361
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 401..405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 455..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 847 AA; 91125 MW; F6F5F5AAE81BAB43 CRC64;
MNDRDGKKPL GLGGGTGGRS GQVKQSFSHG RTHNVVVETK RKRVVTPKPA TGPNPALRPN
SPASVASDPS KRPAGITEAE MERRLKALAA AKAREAEDNA RRAAEEKARE EERERRRAEI
EAKEREERER EEALRLKAEE DARKLREAEL RAQKKAEVTA KPAERTAAPD RAAAEAAAAR
AEKPGVAAGP RRTDRDRRDT GGDSDAKAKA KAEESRRTGR LSLTQALAGG EGGRQRSLAA
MKRKQEKARA KAMGQMQRAE KQVRDVQLPE TIVVSELANR MAERAADVIK SLMKMGMMVT
ANQTIDADTA ELVIEEFGHR AVRVSDADVE QVIQTVEDKA EDLQARPPIV TIMGHVDHGK
TSLLDLIRQA NVVAGEAGGI TQHIGAYQVT TESGALLSFL DTPGHAAFTS MRARGANVTD
IVVLVVAADD AVMPQTVEAI NHAKAAGVPM IVAINKIDKP TANPQKVRTD LLQHEVVVEA
MSGDVQDVEV SAHTGQGIDQ LLEAIALQAE ILELRANPNR AALGAVIEAK LDVGRGPVAT
VLVQNGTLKQ GDIFVVGEQW GKVRALINDK GERVTEAGPS VPVEVLGING TPEAGDVLNV
VETEAQAREI ADYRIQAAKD KRAAAGAATT LQELMAKAKA DESVAELPVV VKADVQGSAE
AIVQALEKVG NEEVRVRVLH YGVGAITESD VGLAEASKAP VIGFNVRANA PARNAANQKG
VEIRYYSIIY DLIDDIKAAA SGLLSAEVRE NFIGYAEIKE VFRVTGVGNV AGCLVTEGVA
RRSAGVRLLR DNVVIHEGTL KTLKRFKDEV KEVQSGQECG MAFENYDDIR KGDIIEIFER
EEVERRL
//
