GenomeNet

Database: UniProt
Entry: H0QHP9_ARTGO
LinkDB: H0QHP9_ARTGO
Original site: H0QHP9_ARTGO 
ID   H0QHP9_ARTGO            Unreviewed;       958 AA.
AC   H0QHP9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 60.
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   ECO:0000313|EMBL:GAB12350.1};
GN   ORFNames=ARGLB_013_00030 {ECO:0000313|EMBL:GAB12350.1};
OS   Arthrobacter globiformis NBRC 12137.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1077972 {ECO:0000313|EMBL:GAB12350.1, ECO:0000313|Proteomes:UP000003828};
RN   [1] {ECO:0000313|EMBL:GAB12350.1, ECO:0000313|Proteomes:UP000003828}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 12137 {ECO:0000313|EMBL:GAB12350.1,
RC   ECO:0000313|Proteomes:UP000003828};
RA   Miyazawa S., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Arthrobacter globiformis NBRC 12137.";
RL   Submitted (DEC-2011) 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}.
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:GAB12350.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BAEG01000013; GAB12350.1; -; Genomic_DNA.
DR   RefSeq; WP_003798362.1; NZ_BAEG01000013.1.
DR   AlphaFoldDB; H0QHP9; -.
DR   STRING; 1077972.ARGLB_013_00030; -.
DR   eggNOG; COG0532; Bacteria.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000003828; 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; 1.10.10.2480; -; 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; 2.
DR   PRINTS; PR00315; ELONGATNFCT.
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|ARBA:ARBA00022490, 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:UP000003828}.
FT   DOMAIN          451..622
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          51..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..114
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..158
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..241
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         460..467
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         510..514
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         564..567
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   958 AA;  98859 MW;  AEEB426F246AC6C7 CRC64;
     MAKVRVHELA KELGITSKDA VTKLQELGEF VRSASSTIEA PVVRKLRNAF PAAAASKSEA
     PAAAPKSPAK PAETRPAPAP GPAAPKAAAP APAPAPAPAP APKAEAPAAP AAPAAPAAPA
     AATPAAPSTG AKPGARPAPK AETPSRPGGA PRPGGPRPGN NPFATSQGMP RGRGGDGDRP
     PRPGNNPFAT SQGMPRPGGG RTDGDRPGGP RPAAGAGGPR PGAPRPGATP GPRPAAGAGG
     PRPGGPRPGA GGNRPTPGMM PNRTERPAPA GAGRPGGGGR GPGRPGAPGT GGPGGGGGAP
     AGGGFGKGGR GRGGTQGAFG KGGAGRGKQR KSKRAKRQEL EQMSAPSLGG VSVPRGDGNT
     VIRLRRGSSI TDFADKIEAN PAALVTVLFH LGEMATATQS LDEDTFALLG EELGYKLQVV
     SPEDEERELL SAFDIDVEAE LEAEGDEELE ARPPVVTVMG HVDHGKTRLL DAIRNSDVVA
     GEHGGITQHI GAYQISHEHE GALRDITFID TPGHEAFTAM RARGAKVTDI AILVVAADDG
     VMPQTVEALN HAQAANVPIV VAVNKIDKEG ANPDKVKGQL TEYGLVPEEY GGDTMFVEVS
     ARQNVNIDEL IDAVLLTADA ALDLRANPDK AARGIAIEAN LDKGRGSVAT VLVQSGTLAV
     GDTIVAGTAH GRVRAMFDED GEALDVALPS RPVQVLGLSN VPRAGDTFLV TADERTARQI
     AEKREAADRN AQLAKRRKRI SLEDFDQAVA EGKIDTLNLI LKGDVSGAVE ALEDALLKID
     VGEGVQLRVI HRGVGAITQN DVNLATVDSA VIIGFNVKPA ERVAELADRE GVDMRFYSVI
     YSAIDDIELA LKGMLKPEYE EVQLGTAEVR EVFRSSKFGN IAGSIVRTGT IRRNTKARIT
     RAGKLIGDNL TVETLKRFKD DVTEVRTDFE CGIGLGSYND ITEGDIIETF EMREKPRV
//
DBGET integrated database retrieval system