ID A0A061JFR0_9PROT Unreviewed; 843 AA.
AC A0A061JFR0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=K737_301073 {ECO:0000313|EMBL:ETZ04521.1};
OS Holospora undulata HU1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales; Holosporaceae;
OC Holospora.
OX NCBI_TaxID=1321371 {ECO:0000313|EMBL:ETZ04521.1, ECO:0000313|Proteomes:UP000026922};
RN [1] {ECO:0000313|EMBL:ETZ04521.1, ECO:0000313|Proteomes:UP000026922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HU1 {ECO:0000313|EMBL:ETZ04521.1,
RC ECO:0000313|Proteomes:UP000026922};
RX PubMed=23969064;
RA Dohra H., Suzuki H., Suzuki T., Tanaka K., Fujishima M.;
RT "Draft Genome Sequence of Holospora undulata Strain HU1, a Micronucleus-
RT Specific Symbiont of the Ciliate Paramecium caudatum.";
RL Genome Announc. 1:E00664-13(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETZ04521.1}.
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DR EMBL; ARPM03000186; ETZ04521.1; -; Genomic_DNA.
DR RefSeq; WP_006294597.1; NZ_ARPM03000186.1.
DR AlphaFoldDB; A0A061JFR0; -.
DR Proteomes; UP000026922; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000026922}.
FT DOMAIN 340..510
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349..356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 396..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 450..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 843 AA; 93986 MW; 4CCF87FFA3E59694 CRC64;
MTEERKDKKR KPLGLNVGQP QPNPAGKESV KQTFVQGKTK RVTVEVRRGS RAASDRRPGG
TFEKFTDEEQ LRRLRAVQQS LQEKEEAELL RIAKEQADKE RKELEAQEEQ ARIKSAQEEQ
ERMSAAQKLS GVSLDQNIEG LLKSEVPSLD SSSESTLEEN SSKSTAEEKK RKAGSDRPLE
RSDASKVKRS KTESEEAVRP FAKRSKQKYE KISTPVTPLT LEDDFISTLE ETESSFKRGN
VHRSKTSRIK REKKVPSVVL RCIELTGPIV LQDLAEKMAI KAHKVVQLLE NFGKSTTVHS
VLDVETAELI ISEMGHKSLR VGLEDLEARW WNVQGKTLEE RPPVVTIMGH VDHGKTSLLD
ALRQTSVASG EKGGITQHIG AYQTRLSSGK QVTFIDTPGH EAFVRMRERG SAVTDIIVLV
VAADDGVKTQ TIEAIHHAKT SGVPVIVAIN KIDKANAKPD IVRSELLNHG VVVEKMGGEV
LDVEVSALTK KNLDVLIETI LLQAEMMELT CSPDTKARGT IIESHMRKGH GHVATVLIQN
GTLRKGDIFV AGMLSGKVRM MFDAQGCVVQ RATPGQPVEV LGFSHSPVSG ERFLSLEQES
QAREFVEWKK SQMLSGTEEP LSKLPETSHD LEQYFKSQNV KTLFLVINAD VQGSIEGLTY
ELQKIHHGEV ALQIISSEVG PVSESDVMLA KTSNAVILMF NTYVLPDVQK IIDREKVTVL
SHQIVYRATE EVKALLVKLL SPEIQEHFLG KAEIIKVFHV KKASSIAGCL VKEGMLRRGE
FVKIFRDKTM LFEGEIKSLR HVKNDMKEVK FGYECGMILE GFDAFEVGDR VECYEKRSIA
REL
//
