ID F8AGQ9_PYRYC Unreviewed; 1053 AA.
AC F8AGQ9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=PYCH_03400 {ECO:0000313|EMBL:AEH24035.1};
OS Pyrococcus yayanosii (strain CH1 / JCM 16557).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=529709 {ECO:0000313|EMBL:AEH24035.1, ECO:0000313|Proteomes:UP000008386};
RN [1] {ECO:0000313|EMBL:AEH24035.1, ECO:0000313|Proteomes:UP000008386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CH1 / JCM 16557 {ECO:0000313|Proteomes:UP000008386};
RX PubMed=21705594; DOI=10.1128/JB.05345-11;
RA Jun X., Lupeng L., Minjuan X., Oger P., Fengping W., Jebbar M., Xiang X.;
RT "Complete genome sequence of the obligate piezophilic hyperthermophilic
RT archaeon Pyrococcus yayanosii CH1.";
RL J. Bacteriol. 193:4297-4298(2011).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; CP002779; AEH24035.1; -; Genomic_DNA.
DR AlphaFoldDB; F8AGQ9; -.
DR STRING; 529709.PYCH_03400; -.
DR KEGG; pya:PYCH_03400; -.
DR eggNOG; arCOG01560; Archaea.
DR eggNOG; arCOG03151; Archaea.
DR HOGENOM; CLU_002656_3_4_2; -.
DR OrthoDB; 30957at2157; -.
DR Proteomes; UP000008386; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
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 GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR CDD; cd03703; aeIF5B_II; 1.
DR CDD; cd00081; Hint; 2.
DR CDD; cd16266; IF2_aeIF5B_IV; 1.
DR CDD; cd01887; IF2_eIF5B; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 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; IPR004161; EFTu-like_2.
DR InterPro; IPR029459; EFTU-type.
DR InterPro; IPR003586; Hint_dom_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
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; TIGR01443; intein_Cterm; 1.
DR NCBIfam; TIGR01445; intein_Nterm; 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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF14890; Intein_splicing; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
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.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022759};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Intron homing {ECO:0000256|ARBA:ARBA00022886};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Protein splicing {ECO:0000256|ARBA:ARBA00023000}.
FT DOMAIN 172..271
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 455..476
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT DOMAIN 460..677
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 533..537
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 587..590
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1053 AA; 119053 MW; 5BC176CCB8DB0DF4 CRC64;
MKRIRQPIIA VLGHVDHGKC LLPEERVVVP GLGSLTLEEL FEIADEIVER DDEKEIRKLR
IPLTAVDGNG AIAMVEGSYV WRLRHRGKIV RVKLKNWHSV SVTPEHPFLT TRGWKRADQL
KPGDYVAVPR YIHGNESRER FMAFVYSKLS KRDGRYARLP RSDDEWRAFF YFAGVMFGDG
SQKVTNDYAE VFERLESIEK LGVELKLLRV LFDYSDGIPD VLFLAPKDYV AEFLRGYFDV
HGSLEDDRVE VTGASREFIE GLSLVLLRFG IVSKIYRSGY TTLVISGRRN LDAFRRHIGF
TVREKAEMLK RAIDKSRGSE AYPIFEELKR LRLLFGFTRA ELDSEVPFYS KYEESEAPSY
ETLMQILDAI ERGSPTLAKK IAVLEGRAKD VNYLKALERD GLIKDGHLTE LGRELLEVWR
NREFDSRDVE YVRNIAESLV FIPVEAVEEL DYDGYVYDLT TETHNFIANG VLVHNTTLLD
RIRKTNVAAK EAGGITQHIG ATEVPIEVVK KIAGPLIKLW KAEIKLPGLL FIDTPGHEAF
TSLRARGGSL ADLAVLVVDI NEGFQPQTIE SIEILRRYKT PFVVAANKID RIRGWVIEED
EPFLVNIKKQ DQRVVQELET KLWELIGKFY EMGFQANRFD RVQNFTRELA IVPISAKYGI
GIPELLVLIA GLSQKYLEEK LRIEVEGPGR GTILEVREEP GLGTTIDVII YDGTLRKDDI
IVVGGKDKAI VTKIRALLKP KPLDEIRDPR FRFDQVEEVT AAAGVKIAAP DLEEALAGSP
VIAARTEEEI ERAKQEILSQ IQSVVISTGK VGVIVKADTL GSLEALSKEL QEKNIPIRKA
DVGNISKTDV MEALSVKEEE EKYGVVLGFN VKVNEDAEEV AKAKGVPIFV GNVIYKLIED
YEAWMKAEEE KKKRELLSRV TFPGVIRLYP DERYVFRRSN PAIVGIEVLE GRIKPGVTLI
KQNGQKVGVI KSIKSRDEFL QEARKGQAVA IAIEGAIVGR HIHPGEILYV DIGRDDAIIL
LKQLRSELED TDIKALKMTA EVKAKEDPFW RAI
//
