IF2_PSYIN
ID IF2_PSYIN Reviewed; 880 AA.
AC A1ST45;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ping_0817;
OS Psychromonas ingrahamii (strain 37).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Psychromonadaceae; Psychromonas.
OX NCBI_TaxID=357804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=37;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA Richardson P.;
RT "Complete sequence of Psychromonas ingrahamii 37.";
RL Submitted (JAN-2007) 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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; CP000510; ABM02660.1; -; Genomic_DNA.
DR RefSeq; WP_011769223.1; NC_008709.1.
DR AlphaFoldDB; A1ST45; -.
DR SMR; A1ST45; -.
DR STRING; 357804.Ping_0817; -.
DR PRIDE; A1ST45; -.
DR EnsemblBacteria; ABM02660; ABM02660; Ping_0817.
DR KEGG; pin:Ping_0817; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000639; Chromosome.
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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
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 PANTHER; PTHR43381; PTHR43381; 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; SSF46955; SSF46955; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..880
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008309"
FT DOMAIN 380..549
FT /note="tr-type G"
FT REGION 51..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..396
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 414..418
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 435..438
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 489..492
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 525..527
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389..396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 435..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 489..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 880 AA; 95351 MW; E8BD92BB744679D8 CRC64;
MSDMSLKDLA KDLNKSEEIL VKQFADAGIK KSASDKVSLA EKQTLTSFLQ KQHGGESKTK
MTLQRKTKST LNVKGSTGQA KAVQVEVRKK RTYVKRSDSE TQETQAAELA DQQAANDKLQ
AEIEAKKLLV EKALAEKLAA KKEADEKAKK AAAANKEKQT AVKSEKTAEQ IASEKESAAL
LKKADQEASA KAEKETAQQA ADAKKLVEEN SARWAEEETA RKKAAEGGDY HITSSKEAQA
AEDVLDSKAE GPSRRKKKKK APVEEKFQGR RTRRGKKQRP ATPSALQQAF EKPAAPVERN
VRIGETITVA ELANKMAVKA TEVIKAMMKM GAMATINQVI DQETATIVAE EMGHKVILTK
ENELEEAVMA EAQQGGDRTS RAPVVTIMGH VDHGKTSLLD YIRRAKVADG EAGGITQHIG
AYHVETDKGM ISFLDTPGHA AFTSMRSRGA KATDIVILVV AADDGVMPQT IEAIQHAKAA
KVPLIVAVNK IDKEGADFDR VKSELSQHNI ISEEWGGENI FTYVSAKVGT GVDGLLESIL
LQAEMLDLSA VAKGPAAGVV IESRLDKGRG PVASILVQHG ELKLGDILLC GLEYGRVRAM
RDENGKPIEV AGPSIPVEVL GLSGVPMAGD EATVVKDEKK AREVALYRQG KFRDIKLARQ
QKAKLDNMFA NMEAGEVSEL NIVLKADVQG SLEAICESLN KLSTDEVKVN IIGRGVGGIT
ETDASLASAS GAIVIGFNVR ADASARKLIE NEGVDLHYYS IIYGLIDEVR AAMSGLLAPE
YRQEITGIAD VREVFKSPKI GAIAGCMVTE GTIKRNNPIR VLRENIVIYE GVLESLRRFR
DDLSEVRNGM ECGIGVKNYN DVRVGDQIEV FETIEIKRTL
