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IF2P_PYRHO
ID   IF2P_PYRHO              Reviewed;        1044 AA.
AC   O58822;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=Probable translation initiation factor IF-2;
DE   Contains:
DE     RecName: Full=Pho infB intein;
DE     AltName: Full=Pho IF2 intein;
GN   Name=infB; OrderedLocusNames=PH1095;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA30194.1; -; Genomic_DNA.
DR   PIR; H71049; H71049.
DR   AlphaFoldDB; O58822; -.
DR   SMR; O58822; -.
DR   STRING; 70601.3257511; -.
DR   MEROPS; N10.004; -.
DR   EnsemblBacteria; BAA30194; BAA30194; BAA30194.
DR   KEGG; pho:PH1095; -.
DR   eggNOG; arCOG01560; Archaea.
DR   eggNOG; arCOG03151; Archaea.
DR   OMA; DHGKCLL; -.
DR   Proteomes; UP000000752; 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.
FT   CHAIN           1..22
FT                   /note="Probable translation initiation factor IF-2, 1st
FT                   part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014493"
FT   CHAIN           23..466
FT                   /note="Pho infB intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014494"
FT   CHAIN           467..1044
FT                   /note="Probable translation initiation factor IF-2, 2nd
FT                   part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014495"
FT   DOMAIN          173..265
FT                   /note="DOD-type homing endonuclease"
FT   DOMAIN          451..668
FT                   /note="tr-type G"
FT   BINDING         524..528
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         578..581
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1044 AA;  118951 MW;  907C7A84D0ACB3F4 CRC64;
     MSYVKRIRQP IIAVLGHVDH GKCLLPEERV ILPDYGPITL EELFNMTKET VFKDEEKEVR
     KLGIRMPVAG VDGRVRLLEG PYVWKVRYKG KMLRVKLKDW HSVAVTPEHP FLTTRGWVRA
     DQLKPGDYVA VPKILPGKDD KEKFLQYVHE KLKGKVHIKL PSSDEEWETF FYFAGTIFGR
     ENSVNPEGLT HEVKALLELF KVLFEYPREV LRVLFMAPVR YVANFLRGFF DINGYVNGEE
     LRVEVRGAPH EVLEELSLIL LRLGIVSKIY PTSLAISGRR NLELFRRYIG FSEKQKAKEL
     EGIIRRSENS ESYPIFEELR RIRLLFGFTR AELSSTIPLY SKYESKEAPS YEILMKILNT
     IEKGSKDLNK KITILEGRVR DHEYIEEFKR EGLIKDGKLT ELGKELLEVW RNREFDSRDV
     NYLRNIIENF VFLPVEKIEE FEYDGYVYDV TTETHNFIAN GILVHNTTLL DKIRKTNVAA
     KEAGGITQHI GATEVPIDVV KKIAGPLIKL WKAEIRLPGL LFIDTPGHEA FTSLRARGGS
     LADLAVLVID VNEGFQPQTI ESIEILRRYR TPFVVAANKI DRIRGWVIEE DEPFLMNIKR
     QDQRAIQELE TKLWELIGKF YEFGFQANRF DRVQNFTREL AIVPISAKYG IGIAELLVLI
     AGLSQKYLEE KLKIEVEGPA RGTILEVREE PGLGHTIDVI IYDGTLHKDD TIVVGGKDKA
     IVTKVRALLK PKPLDEIRDP RFRFDYVDEV TAAAGVKIAA PGLEEALAGS PVIAAPTPED
     VERAKEEIMR QIESVVISTD KVGVIVKADT LGSLEALSKE LQEKEIPIRK ADVGNISKTD
     VMEALSVKEE NPKYGVILGF NVKVNEDAKE VAKAKEVPIF VGNIIYKLIE DYEAWIKEEE
     EKRKRELLAK VTFPGVIKLY PDERYVFRRS NPAIVGIEVL EGRIKPGVTL IKQNGQKVGT
     IRSIKSRDEF LQEARKGQAV AIAIEGAIVG RHIHPGETLY VDLSRDDAII LLKHLRDVLE
     DTDIKALKMI AQVKAKEDPF WRAV
 
 
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