IF2_PSYCK
ID IF2_PSYCK Reviewed; 908 AA.
AC Q1QEP5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Pcryo_0074;
OS Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS / K5).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=335284;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Richardson P.;
RT "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL Submitted (MAR-2006) 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; CP000323; ABE73858.1; -; Genomic_DNA.
DR RefSeq; WP_011512449.1; NC_007969.1.
DR AlphaFoldDB; Q1QEP5; -.
DR SMR; Q1QEP5; -.
DR STRING; 335284.Pcryo_0074; -.
DR KEGG; pcr:Pcryo_0074; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002425; 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.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..908
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008308"
FT DOMAIN 409..578
FT /note="tr-type G"
FT REGION 52..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..425
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 443..447
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 464..467
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 518..521
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 554..556
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 67..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 418..425
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 464..468
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 518..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 908 AA; 99947 MW; 7460D657C6362DB2 CRC64;
MADKTVKELA DMVSKTASAV QQQLVDAGLP ARAEGDLVTE LEQEKLVTYL KQSHGQEEKR
RISLKSKTTS TARVTGSSGK SKSVNVEVRK KKVFEKPDPE KMAEELAARE QAMIESQARA
AKDAEDRAAT KKKSEERQAA TLAAMRASLG SSKKSDDKND DISTSVVVKK GGKTTIEVKP
KDQPKKKVTA TKPKVETAVE RKAREVREKE EARLREIETE TRRTQAEEAQ KRTLEQMRKM
AGQYTDQPAT EVRKDEPLAE GLVGDALEES FEKERREIKR GTSTTSARGR GRRKNQDERE
IKNRKNGLRS SQSSQHKFEK PVEKIVYDVE ISEQITVSDL AQRMAVKARE VTKLLMKMGE
IARESDMIDQ ATASLIVEEM GHNPVPVSDT KVEDDLQDAV DERSSNVQTR PPVVTIMGHV
DHGKTSLLDK IRETKVATGE AGGITQHIGA YHVKTARGVI TFLDTPGHAA FSAMRSRGAQ
ATDIVVLVVA ADDGMMPQTE EAIDHARAAG TPLIVAINKM DKPSADPDRV LNELTAKEVV
SEDWGGDTPM ARISAKTGDG IDELLELISL QAELMELEAP LDGPAQGVVI ESRLEKGRGP
VVSVLVKKGT LKQGDLVLAG EYYGKVRAMT DEHGKRIQSA GPSIPVEILG LPETPAAGSE
FLVLTDEKKA REVADFRTNR ERERQLERQN AMRLESMFDQ MEQGNVSYLN IVLKTDVRGS
LEALLAALNE LSTDEVKVRV ISSGVGPISE SDVTLAESSE AVLLGFNVRA DATARRKSDS
ANMDIRYYSV IYGLIDDVKA AMSGMLAPEH REKILGVADV REVFRSSKFG AAAGCMVVEG
TIYRNKPIRV LRNDQVIFTG QLQSLRRYKE DVNEVRTGME CGLAVRGYDV EAGDKIEVFE
IQEFARTI
