IF2P_HALLT
ID IF2P_HALLT Reviewed; 597 AA.
AC B9LQL7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=Hlac_2060;
OS Halorubrum lacusprofundi (strain ATCC 49239 / DSM 5036 / JCM 8891 / ACAM
OS 34).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Halorubraceae; Halorubrum.
OX NCBI_TaxID=416348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49239 / DSM 5036 / JCM 8891 / ACAM 34;
RX PubMed=27617060; DOI=10.1186/s40793-016-0194-2;
RA Anderson I.J., DasSarma P., Lucas S., Copeland A., Lapidus A.,
RA Del Rio T.G., Tice H., Dalin E., Bruce D.C., Goodwin L., Pitluck S.,
RA Sims D., Brettin T.S., Detter J.C., Han C.S., Larimer F., Hauser L.,
RA Land M., Ivanova N., Richardson P., Cavicchioli R., DasSarma S.,
RA Woese C.R., Kyrpides N.C.;
RT "Complete genome sequence of the Antarctic Halorubrum lacusprofundi type
RT strain ACAM 34.";
RL Stand. Genomic Sci. 11:70-70(2016).
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; CP001365; ACM57638.1; -; Genomic_DNA.
DR RefSeq; WP_015910763.1; NC_012029.1.
DR AlphaFoldDB; B9LQL7; -.
DR SMR; B9LQL7; -.
DR STRING; 416348.Hlac_2060; -.
DR PRIDE; B9LQL7; -.
DR EnsemblBacteria; ACM57638; ACM57638; Hlac_2060.
DR GeneID; 7402079; -.
DR KEGG; hla:Hlac_2060; -.
DR eggNOG; arCOG01560; Archaea.
DR HOGENOM; CLU_002656_3_3_2; -.
DR OMA; FRQSKPA; -.
DR Proteomes; UP000000740; Chromosome 1.
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.
FT CHAIN 1..597
FT /note="Probable translation initiation factor IF-2"
FT /id="PRO_1000202775"
FT DOMAIN 10..226
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 44..48
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 19..26
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 597 AA; 65186 MW; 3DDFADA33558F9F7 CRC64;
MTDHTNADTL RTPIVAVLGH VDHGKTSLLD TIRGSAVSEG EAGAITQHIG ATDIPLDTIS
EMAGELIDPT DFDLPGLLFI DTPGHHSFST LRARGGALAD IAVLVVDVND GFQPQTEEAI
DILRRTGTPF VVAANKVDTT PGWNPQDGQP IQRSLEAQSE RAESMLNENL YEIIGQLSDA
GFSADLYWRV QDFQKNIGVV PLSAITGEGV PDLLTVLMGL SQRFMKEEMA IDVQGPGEGT
VLEVKDERGF GATIDTVVYD GVVRNGDQIV VGGQDEPIVT EIRALLQPRP LEEIRTEKKF
EKVAEVGAAA GVKIAAPDLD RAMAGAPVRV VRDRPVEEVV EEVKAELAEI EVETAENGVV
VKADTLGSLE AMANALREAE VPILRAEVGD IAPRDIAVAE TANQDEHKAI LGFNVDLLAN
AETELENADV KLFTDEVIYQ LIEDYETYVE EKQRAQQETV LDKVVRPSRF RILPDHTFRQ
NDPAVVGVEV ISGTVQNNRN VGYFEGNEFE RVGQLSGIQK QGDDVDEARA GERVSIAIDG
PTVGRDIEEG DTLWTEIPEK HAKILEQELK EEITADEREA LAAYLETKRK RDPFWGK