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Database: UniProt
Entry: A0A0Q0ZQY2_9EURY
LinkDB: A0A0Q0ZQY2_9EURY
Original site: A0A0Q0ZQY2_9EURY 
ID   A0A0Q0ZQY2_9EURY        Unreviewed;       591 AA.
AC   A0A0Q0ZQY2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Probable translation initiation factor IF-2 {ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=APR53_10640 {ECO:0000313|EMBL:KQC04493.1};
OS   Methanoculleus sp. SDB.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX   NCBI_TaxID=1735326 {ECO:0000313|EMBL:KQC04493.1, ECO:0000313|Proteomes:UP000051748};
RN   [1] {ECO:0000313|EMBL:KQC04493.1, ECO:0000313|Proteomes:UP000051748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDB {ECO:0000313|EMBL:KQC04493.1};
RA   Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA   Suflita J.M., Callaghan A.V.;
RT   "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00024852, ECO:0000256|HAMAP-
CC       Rule:MF_00100, ECO:0000256|RuleBase:RU000644}.
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: 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:KQC04493.1}.
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DR   EMBL; LKUD01000049; KQC04493.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q0ZQY2; -.
DR   STRING; 1735326.APR53_10640; -.
DR   Proteomes; UP000051748; Unassembled WGS sequence.
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; cd03703; aeIF5B_II; 1.
DR   CDD; cd16266; IF2_aeIF5B_IV; 1.
DR   CDD; cd01887; IF2_eIF5B; 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_A; IF_2_A; 1.
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   NCBIfam; TIGR00491; aIF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF14578; GTP_EFTU_D4; 1.
DR   Pfam; PF11987; IF-2; 1.
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; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}.
FT   DOMAIN          6..220
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         15..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         76..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         130..133
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   591 AA;  65098 MW;  79DA4706288328F6 CRC64;
     MSKAAIRTPI VCVLGHVDHG KTSLLDRIRG SSVVDTEEGA ITQHIGATLV PLDVIEQMSG
     VAGSMQFDIP GLLFIDTPGH HAFTTLRSRG GALADMAILV VDLNEGFQPQ TIEALQILRS
     QKTPFVVAAN KIDRIHGWRV MENMPFKKTF SRQNERVQGV VETKIYELVG KLSEMGFNCE
     RYDRIRDFAR NIAIVPVSAI TGEGIPDLLM VMVGLAQRYL TESLRLTVEG PGSGTVLEVK
     EERGLGITLD VILYDGILKV GDEIVVGGHD GVITTKVRSL LKPRPMKEIL VEDRFERVKS
     VTAATGIKVA APRLDGSVAG TPLRVVRGDR DAVIADVTRE MQDIQVTLKD EGVYIKADTI
     GALEALSKEL EANTIPVMRA EVGPVSRHDI IEVSTIKNPL YSAVLSFNTP ILPDAIDTLA
     EPSMKQVMLF EGGVIYRLID DFLEWQEDTR RAMEKQRFEN LVMPGKISLL PDCVFRQSNP
     AVVGVRILGG KLQSGVNLIH LDGRKVGRVK MMKSGQETVH EADAGDEIAI SIEGPTVGRQ
     INVGDELYVD IPERHVKVIE TEMMSHLNTS MQMILEEFTA MRRKSDPFWG K
//
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