ID A0A0V1PH43_9BILA Unreviewed; 2217 AA.
AC A0A0V1PH43;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN Name=MTIF2 {ECO:0000313|EMBL:KRZ95528.1};
GN ORFNames=T08_13806 {ECO:0000313|EMBL:KRZ95528.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ95528.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ95528.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ95528.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: One of the essential components for the initiation of protein
CC synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC and promotes its binding to the 30S ribosomal subunits. Also involved
CC in the hydrolysis of GTP during the formation of the 70S ribosomal
CC complex. {ECO:0000256|ARBA:ARBA00025162}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ95528.1}.
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DR EMBL; JYDM01000012; KRZ95528.1; -; Genomic_DNA.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
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:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR CDD; cd09857; PIN_EXO1; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 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_B; IF_2_B; 1.
DR InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR InterPro; IPR008918; HhH2.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029060; PIN-like_dom_sf.
DR InterPro; IPR044752; PIN-like_EXO1.
DR InterPro; IPR021757; Ribosomal_mL46_N.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR000178; TF_IF2_bacterial-like.
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; IPR006086; XPG-I_dom.
DR InterPro; IPR006084; XPG/Rad2.
DR InterPro; IPR019974; XPG_CS.
DR InterPro; IPR006085; XPG_DNA_repair_N.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF20; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR Pfam; PF11788; MRP-L46; 1.
DR Pfam; PF00867; XPG_I; 1.
DR Pfam; PF00752; XPG_N; 1.
DR PRINTS; PR00853; XPGRADSUPER.
DR SMART; SM00279; HhH2; 1.
DR SMART; SM00484; XPGI; 1.
DR SMART; SM00485; XPGN; 1.
DR SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF88723; PIN domain-like; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS00842; XPG_2; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:KRZ95528.1}; Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1706..1730
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1742..1760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1839..1860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1922..1940
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1952..1971
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2019..2039
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2051..2069
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2081..2101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1013..1183
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 399..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2217 AA; 250461 MW; 741984B88999B666 CRC64;
MASISRRMLS SILAYKISHL TAKTYQIKQL QILGQHYSFA PENLMVLITR LIASSVYKWR
ADHSYATLIK TDALGEASKA QTLNYKWKIM VSLCIERFPV IARGLNSIEK HYKDLMDRIE
FENSLYSQHE LRLLEDEKRL ALKKTGEMHD HDSVMTAADF EDACAQKLEE FNQKYNKKAD
DDGTNTHSLW RNLDRKLLLA VNHAEKKHWL LPEIPVENGE TLHDASVRLL TSIVEPNNAM
PYAYAPVGFF KFKYPKPVAT KCHAIGEKIF FFKCHLKSKY PEEIVPKVEN YMWLNHDELV
SIFPPKYYKS ISVMGIKTLL PVVKAACRDV NIEEFRGKTV AVDASCWLHR ALFGCAYQLA
TGIETDSYVK FCCKWIKVLL SYNIRVIMVF DGRNVPAKKD TNNARKERRQ SLKEKGQALS
KSGKHREARQ CFQQATEITF DMIVNLIKAI KSIPNVDYLV APYEADAQLA YLAQNGIVHL
VISEDSDLIP FGCSKVLFKM DMLGNGVLYE KEKLHLAMSV PEESFSFQNF RRSCILSGCD
YLENLPGIGI KKSIKFFQKT FDVDIRKALP KIPSYLNMPN LEVNESYIER FIEAENAFLY
QLVFDPRKKQ LVSLNAYPVG MNASDFPYAG LVFEKHVAIQ IARGMINPHT LQHVSEISGL
VPNKKSPKNI KSTPVEYAFS FSVPEASVSM KGKLIVMPDL DIKVEANAEQ LEETTEIQDV
YETYAVSPED GCLFEKQSSN NEESILEQWN YRRDDEKLVL RSSYFLNAEH KKEMPSPPEA
FNPCKVYQTR SVCKIMENIE LAEGRTSKSF NPFKVSDVSD LPQEDSSSEE VVCTEQQDAQ
ATLGKRKLQT KSELFQPLKK TTAKKMRGKN SKKNNPTSPC PAKKTLFQYF SNQPAQSALS
YDRNLHTTLP KLKRIHKQRD PIQFNKKSEK PQAKVWQSMS INDLAKVLKC DVDDIFECIM
TTKYADMFEN VSDKIEDLNL IVHIVRQFGY SSNTDEELDA SPLPLPPLEQ CKPRPPVVTI
MGHVDHGKTT LLDSLRHSHI VDEEFGAITQ HIGAFSVKLQ NDRVITFLDT PGHAVFKKMR
FRGAQVTDMV ILVVAADDGV MEQTVESIRM AQESHVPIVV AVNKCDKFGV DLDRVKRQLL
EYDVVGEQYG GDVQIIPISA LKGTNLDLLC DAVLTQADLM ELVADYEGPV EGVVLESKTA
HGQGKVCFAL VKRGCLRKGV VLVAGSCWCK VRSLFDENKV ELKMATPSFP VEITGWKGDE
IPSAGEEILQ VENERRAKQV TNLRKKKQLI NKALDEKNII DQRRAEERLE YLKIRERKLQ
SGYIRYDPQA DYRRKKEVIS SSDGPILPFV LKADVDGSLE AILDVYRTYN STKCNFDLVH
FGIGDVTEND LEIADTFKAA VAFAAIIFCF NVSIGQKEKA LADSKAIQLR KHNVIYSLID
DFKKELNSRL PPVSKEIIIG EGTVIKEFMV SDIGRKKVPV AGCSVKKGVL TKNDRIRFIR
NGEVIYDGSV ISMRREKDLV SSSQVGQEVG IKIENRDVRF NEDDQVICYK LVEEQHIHIG
HLSKEIVCND NDGISLISSS SSVSVCQFRI KAFNNQKFIE VFMQMKNEKG RRLSMSVVRR
PACATMRWPV TRRINFPTNL IDWGGVSWKQ LVRAGVVGPL QPGVALWTAM PPRSVMHKAT
VEQLNRAEQE VSSAGTHLVH FAPDKFTLSL AIVVVLLLLL LLTVVVAVVV GSSISNNSGI
SISSNCLLLV YCLSSRYWFI SFATGCSYCW SRWAGRSAAL MKLAVQLAKR NALLVMDRLA
HRRQSLLRSR NPWGKWPSEP ELRLGFCSSL RIAEENIRMV LLAILLVIYL VIGAMLFSVI
ERKQEALERL LYSEKLERFK MQHCTTGGGL TLVNCSALDE LLEMRGKMSA AGISEHRSSW
DFFGSFYFVS TVVTTIGFGM TTPRTAIGKA AVILYGFVGC SSSILFFNLF LERILTFLSC
LFRVVHRIRL PQSNRSNCGR RASDEQSCSL EAEWRPNLYF FWFGLLILSS TTITLAALLY
QYAEDWSYLE AVYFCFVSFA TIGFGDFISS QRTSEISSYK LYSILNFAIL FVGCCCIYSF
FNVTSIVIRS LLDQIIASLD CRCRLLGRFR HDKARRPVDG LHTTLDQNAK GAYLASAQTG
DGLLSLKEFL DQTQDNLLSV PDQLLLPAEH DLRKSSVSAS SVGPMAIVNE MIGTADI
//
