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IF2P_PYRAB
ID   IF2P_PYRAB              Reviewed;         992 AA.
AC   Q9UZK7; G8ZKB1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Probable translation initiation factor IF-2;
DE   Contains:
DE     RecName: Full=Pab infB intein;
DE     AltName: Full=Pab IF2 intein;
GN   Name=infB; OrderedLocusNames=PYRAB11390; ORFNames=PAB0755;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248286; CAB50050.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70554.1; -; Genomic_DNA.
DR   PIR; E75093; E75093.
DR   AlphaFoldDB; Q9UZK7; -.
DR   SMR; Q9UZK7; -.
DR   STRING; 272844.PAB0755; -.
DR   MEROPS; N10.004; -.
DR   EnsemblBacteria; CAB50050; CAB50050; PAB0755.
DR   KEGG; pab:PAB0755; -.
DR   PATRIC; fig|272844.11.peg.1195; -.
DR   eggNOG; arCOG01560; Archaea.
DR   eggNOG; arCOG03151; Archaea.
DR   HOGENOM; CLU_002656_3_4_2; -.
DR   OMA; DHGKCLL; -.
DR   PhylomeDB; Q9UZK7; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; 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; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
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   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   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..20
FT                   /note="Probable translation initiation factor IF-2, 1st
FT                   part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014487"
FT   CHAIN           21..414
FT                   /note="Pab infB intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014488"
FT   CHAIN           415..992
FT                   /note="Probable translation initiation factor IF-2, 2nd
FT                   part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000014489"
FT   DOMAIN          96..220
FT                   /note="DOD-type homing endonuclease"
FT   DOMAIN          399..616
FT                   /note="tr-type G"
FT   BINDING         472..476
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         526..529
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   992 AA;  112225 MW;  9838BADA50E6F1C6 CRC64;
     MTKRIRQPII AVLGHVDHGK CLLPDEKVVV PSVGFVTLKE LFETASKVVE RDDEKEIREL
     DERITSVNGD GKTGLVKASY VWKVRHKGKV IRVKLKNWHG VTVTPEHPFL TTKGWKRADQ
     LRPGDYVAVP RFIHGNEDEK IFLSYVKVKK SGEEWKEYFY LAGRKGNIDV NLLFVAPKRY
     VVEFLRGYFE ERSEVKGESV IVEARELVEP LSLALLRFGI FSKIQGSKLI VTGKRNLEAF
     KDYIGFKDER EKALEEAIEK VKGSEVYPIF EEIRRLRLLF GFTREELGSY AKYENSEAPT
     YEELMEILDF IERGSPSLSK KIAILEGKLK AELRVLEEEG LIKDGKLTPL GRELLEVWRN
     REFDSKDVDY IRNIAETLVF IPVENVEEEE YDGYVYDLTT ETHNFIANGI LVHNTTLLDR
     IRKTNVAAKE AGGITQHIGA TEVPIEVVKK IAGPLIKLWK AEIKLPGLLF IDTPGHEAFT
     SLRARGGSLA DLAVLVVDIN EGFQPQTIES IEILRKYRTP FVVAANKIDR IKGWVIEEDE
     PFLMNIKKQD QRAVQELETK LWELIGKFYE FGFQANRFDR VQNFTRELAI VPISAKYGIG
     IAELLVLIAG LSQRYLEEKL KIEVEGPARG TILEVREEPG LGHTIDVIIY DGTLHKDDTI
     VVGGKDKAIV TKIRALLKPK PLDEIRDPRF RFDYVDEVTA AAGVKIAAPG LEEALAGSPV
     IAAPTPEDVE KAKQEILEQI ERVVISTDKV GVIVKADTLG SLEALSKELQ EKEIPIRKAD
     VGNVSKTDVM EALSVKEEEP KYGVILGFNV KVNEDAEEVA KAKDVKIFVG NVIYKLIEDY
     EEWVKEEEEK KKRELLSKVT FPGVIRLYPD ERYVFRRSNP AIVGIEVIEG RIKPGVTLIK
     QNGQKVGVIR SIKSRDEFLQ EAKKGQAVAI AIEGAIVGRH IHPGETLYVD LSRDDAITLL
     KHLRDTLEDT DIKALKMIAK VKAKEDPFWR AI
 
 
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