IF2P_METKA
ID IF2P_METKA Reviewed; 598 AA.
AC Q8TV06;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Probable translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MK1595;
OS Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC Methanopyrus.
OX NCBI_TaxID=190192;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX PubMed=11930014; DOI=10.1073/pnas.032671499;
RA Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA Koonin E.V., Kozyavkin S.A.;
RT "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT monophyly of archaeal methanogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
CC -!- FUNCTION: Function in general translation initiation by promoting the
CC binding of the formylmethionine-tRNA to ribosomes. Seems to function
CC along with eIF-2. {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; AE009439; AAM02808.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8TV06; -.
DR SMR; Q8TV06; -.
DR STRING; 190192.MK1595; -.
DR PRIDE; Q8TV06; -.
DR EnsemblBacteria; AAM02808; AAM02808; MK1595.
DR KEGG; mka:MK1595; -.
DR PATRIC; fig|190192.8.peg.1756; -.
DR HOGENOM; CLU_002656_3_3_2; -.
DR OMA; FRQSKPA; -.
DR Proteomes; UP000001826; Chromosome.
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 Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_A; IF_2_A; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR004544; TF_aIF-2_arc.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00491; aIF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding; Initiation factor; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..598
FT /note="Probable translation initiation factor IF-2"
FT /id="PRO_0000137302"
FT DOMAIN 8..226
FT /note="tr-type G"
FT REGION 17..24
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 42..46
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 81..84
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 135..138
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 203..205
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 17..24
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 135..138
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 598 AA; 66605 MW; 080BB46FB486FB27 CRC64;
MSESNKAIRQ PIISVLGHVD HGKTTLLDKI RGTAVAAKEA GGITQHIGAS EIPLEVVKEI
CGPLLEQLDV EITIPGLLFI DTPGHEAFTN LRRRGGALAD IAILVIDIME GVMPQTEEAL
RILRRYRTPF VVAANKVDRV PGWKSHEDTP FLESFQKQSP EVQQRLEEKV YELIGQLHQH
GFQAERFDRV RDFTRTVAIV PTSGVTGEGI PELLMVVTGL AQRFLEEQLK IEVEGPGKAA
ILEVKEEPGL GHTVDAILYD GIIRTGDTIV IGHPEEPIVT RVRSLLKPKP LDEMRDPSDR
FRKVDEVTAA AGVKISAPEL EEAVAGAPLR VVGEDEDVEE VVREVQEEVE EVTIETDQEG
IIIKADTLGT LEAVVGEFKE KDVPIRKADV GDITKKDVIE AHAVAEKDPL LGVIVGFNVG
VTEEARELAD EYDVDIIIDD VIYELVEKYE EMVEKRIERE RRKRLDELVR PGKIKVLPGY
IFRQSKPAIV GVQVLAGVIK PGYPLMREDG RELGEIKQIQ MHGEPIKEAK KGQEVAISIE
GPIVGRHFEE GDILYTDVPS EHAKLMFEEF KDLLTEDELE ALKEIAEIKR KEDPFYGM