IF2P_METJA
ID IF2P_METJA Reviewed; 1155 AA.
AC Q57710;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Probable translation initiation factor IF-2;
DE Contains:
DE RecName: Full=Mja infB intein;
DE AltName: Full=Mja IF2 intein;
GN Name=infB; OrderedLocusNames=MJ0262;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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; L77117; AAB98248.1; -; Genomic_DNA.
DR PIR; G64332; G64332.
DR RefSeq; WP_010869759.1; NC_000909.1.
DR AlphaFoldDB; Q57710; -.
DR SMR; Q57710; -.
DR STRING; 243232.MJ_0262; -.
DR EnsemblBacteria; AAB98248; AAB98248; MJ_0262.
DR GeneID; 1451116; -.
DR KEGG; mja:MJ_0262; -.
DR eggNOG; arCOG01560; Archaea.
DR eggNOG; arCOG03151; Archaea.
DR eggNOG; arCOG03157; Archaea.
DR HOGENOM; CLU_002656_3_4_2; -.
DR InParanoid; Q57710; -.
DR OMA; DHGKCLL; -.
DR OrthoDB; 604at2157; -.
DR PhylomeDB; Q57710; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
DR CDD; cd00093; HTH_XRE; 1.
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; IPR001387; Cro/C1-type_HTH.
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 InterPro; IPR039518; WhiA_LAGLIDADG_dom.
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 Pfam; PF14527; LAGLIDADG_WhiA; 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; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Protein splicing; Reference proteome.
FT CHAIN 1..30
FT /note="Probable translation initiation factor IF-2, 1st
FT part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014484"
FT CHAIN 31..576
FT /note="Mja infB intein"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014485"
FT CHAIN 577..1155
FT /note="Probable translation initiation factor IF-2, 2nd
FT part"
FT /evidence="ECO:0000255"
FT /id="PRO_0000014486"
FT DOMAIN 237..367
FT /note="DOD-type homing endonuclease"
FT DOMAIN 561..781
FT /note="tr-type G"
FT BINDING 634..638
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 688..691
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1155 AA; 132299 MW; 6653FA355E7EE0D3 CRC64;
MAKKNTKKDN KNQNLRCPIV CVLGHVDHGK CLMPHEKVLT EYGEIKIEDL FKIGKEIVEK
DELKEIRKLN IKVHTLNENG EIKIINAPYV WKLKHKGKMI KVKLKNWHSI TTTPEHPFLT
NNGWIKAENI KKGMYVAIPR KIYGNEDFEK FIEFINSKIL TNELIVKVNE KDLKNVELPS
TKIYKKQKNV FRSEDIIEHN LNIEKISFSP RIHRCGKPQH YIKLPKSLNE WKAIFYFAGV
MFGDGCVDRI ANNDEEVFNK LKSLNNLGIE VERIKRKSSY EIIFKNGKNA LINLLKILFD
YPSEKKSHNI KIPQILYIAP KELVAEFIKG YFDADGYVNL RQNRIEVISA SKEFIEGLSI
LLLRFEITSK IYEIKKSYKE TKKKYYQLNI VGKRNLKNFK NIGFSIKYKE ENLNKIIEKS
RKSEKYPINK DMKRLRILFG MTRNEVNVSY YAKYENGKEI PSYEIVKKFL NSLKPKNLDK
KIKVLEGKER DVNYLKAFES DGLIENGRLT KLGREALNIW KNHEFGKENI DYMKSLIENI
AFVEVEDVEI IDYDGYVYDL TTETHNFIAN GIVVHNTTLL DKIRKTRVAK REAGGITQHI
GASEIPIDVI KRLCGDLLKM LKADLKIPGL LVIDTPGHEA FTSLRKRGGA LADIAILVVD
INEGFKPQTV EAVNILRQCK TPFVVAANKI DLIPGWNSKE GPFILNFNEK NQHPNALTEF
EIRLYENIIK PLNELGFDAD LYSRVQDVTK TVCIIPVSAV TGEGIPDLLM MVAGLAQKFL
EDRLKLNVEG YAKGTILEVK EEKGLGTTID AIIYDGIAKR GDYLVVGLPD DVLVTRVKAL
LKPKPLDEMR DPRDKFKPVN EVTAAAGVKI AAPELDKVIA GCPIRIVPKD KIEEAKEEVM
KEVEEAKIEV DDEGILIKAD TLGSLEALAN ELRKAGVKIK KAEVGDVTKK DVIEVASYKQ
SNPLHGAIVA FNVKILPEAQ KEIEKYDIKV FLDNIIYKLV EDFTEWIKKE EERIKYGEFE
KLIKPAIIRI LPDCIFRQKD PAICGVEVLC GTLRVGAPLM REDGMQLGYV REIKDRGENV
KEAKAGKAVS IAIDGRVVLK RHVDEGDYMY VAVPESHVRE LYHKYMDRLR NDEKEALLRY
MELMQKLTNN IFWGR