IF2P_PYRFU
ID IF2P_PYRFU Reviewed; 984 AA.
AC Q8U1R8;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable translation initiation factor IF-2;
DE Contains:
DE RecName: Full=Pfu infB intein;
DE AltName: Full=Pfu IF2 intein;
GN Name=infB; OrderedLocusNames=PF1137;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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 (By similarity). {ECO:0000250}.
CC -!- PTM: This protein undergoes a protein self splicing that involves a
CC post-translational excision of the intervening region (intein) followed
CC by peptide ligation. {ECO:0000305}.
CC -!- MISCELLANEOUS: The intein interrupts the GTP-binding site.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE009950; AAL81261.1; -; Genomic_DNA.
DR RefSeq; WP_011012277.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U1R8; -.
DR SMR; Q8U1R8; -.
DR STRING; 186497.PF1137; -.
DR MEROPS; N10.004; -.
DR PRIDE; Q8U1R8; -.
DR EnsemblBacteria; AAL81261; AAL81261; PF1137.
DR GeneID; 41712946; -.
DR KEGG; pfu:PF1137; -.
DR PATRIC; fig|186497.12.peg.1198; -.
DR eggNOG; arCOG01560; Archaea.
DR eggNOG; arCOG03151; Archaea.
DR HOGENOM; CLU_002656_3_4_2; -.
DR OMA; DHGKCLL; -.
DR OrthoDB; 604at2157; -.
DR PhylomeDB; Q8U1R8; -.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 Gene3D; 3.10.28.10; -; 1.
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; 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 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 Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00305; HintC; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF51294; SSF51294; 1.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55608; SSF55608; 1.
DR TIGRFAMs; TIGR00491; aIF-2; 1.
DR TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 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; Endonuclease; GTP-binding; Hydrolase;
KW Initiation factor; Intron homing; Nuclease; Nucleotide-binding;
KW Protein biosynthesis; Protein splicing; Reference proteome.
FT CHAIN 1..19
FT /note="Probable translation initiation factor IF-2, 1st
FT part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014490"
FT CHAIN 20..406
FT /note="Pfu infB intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014491"
FT CHAIN 407..984
FT /note="Probable translation initiation factor IF-2, 2nd
FT part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014492"
FT DOMAIN 94..215
FT /note="DOD-type homing endonuclease"
FT DOMAIN 391..608
FT /note="tr-type G"
FT BINDING 464..468
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 518..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 984 AA; 110945 MW; DA1277D8F666BF02 CRC64;
MKKIRQPIIA VLGHVDHGKC LLPEEKVVLP EIGLVTLREL FELANEVVVK DEEKEVRKLG
KMLTGVDERG NVKLLNALYV WRVAHKGEMI RVKVNGWYSV TVTPEHPFLT NRGWVKAGEL
KEGDYIAIPR RVYGNEDLMK FSKIAKELGI KGDEKEFYLA GASLDIPIKV LFLAPSKLVS
AFLRGYFDAK GVVRENYIEV PLFEDLPLLL LRFGIVSRIE KSTLKISGKR NLELFRKHVG
FTDSEKAKAL DELISKAKES ERYPILEELR RLGLLFGFTR NELRIEENPT YEVLMEILER
IERGSPNLAE KIAVLEGRIK EENYLRILEE EGLIENGKLT ELGKELLEVW RNREFDSKDV
DYVRNIVENL VFLPVEKVER IEYEGYVYDV TTETHNFVAN GILVHNTTLL DRIRKTNVAA
KEAGGITQHI GATEVPIDVV KEIAGPLIKL WKAEIKLPGL LFIDTPGHEA FTSLRARGGS
LADLAVLVVD INEGFQPQTI ESIEILRRYK TPFVVAANKI DRIKGWVIQE DEPFLLNSKR
QDQRAIQELE TKLWELIGKF YEFGFQANRF DRVQNFTREL AIVPISAKYG IGIAELLVLI
AGLSQKYLEE RLKIEVEGPA RGTILEVREE PGLGHTIDVI IYEGTLHKDD TIVVGGKDKA
IVTKVRALLK PKPLDEIRDP RFRFDYVDEV TAAAGVKIAA PGLEEALAGS PVIAAPTPEA
VEKAKEEIMR QIQSVVISTD KMGVIIKADT LGSLEALSKE LQEKGIPIRK ADVGNISKTD
VMEALSVREE DPKYGVIIGF NVKVNEDAQE IAKAKGVPIF VGNIIYKLIE DYEAWVKEEE
EKKKRELLAK VTFPGVIRLY PDERYVFRRS NPAIVGIEVI EGRIKPGVTL IKQNGQKVGT
IKSIKSRDEF LQEAKKGQAV AVAIEGAIVG RHIHPGETLY VDISRDDAIT LLKYLRDVLE
DSDIKALKII AQIKAKEDPF WRAI
