ID A0A0V1HQ47_9BILA Unreviewed; 1248 AA.
AC A0A0V1HQ47;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN Name=Mtif2 {ECO:0000313|EMBL:KRZ12888.1};
GN ORFNames=T11_12146 {ECO:0000313|EMBL:KRZ12888.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ12888.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ12888.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ12888.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion
CC {ECO:0000256|ARBA:ARBA00004173}.
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 -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|ARBA:ARBA00006666,
CC ECO:0000256|RuleBase:RU003857}.
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:KRZ12888.1}.
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DR EMBL; JYDP01000036; KRZ12888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1HQ47; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0034702; C:monoatomic ion channel complex; 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:0005267; F:potassium channel activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 1.10.287.70; -; 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 InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR005410; 2pore_dom_K_chnl_THIK.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR027417; P-loop_NTPase.
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 NCBIfam; TIGR00487; IF-2; 1.
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 PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01588; THIKCHANNEL.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:KRZ12888.1}; Ion channel {ECO:0000256|RuleBase:RU003857};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003857};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857};
KW Voltage-gated channel {ECO:0000256|ARBA:ARBA00022882}.
FT TRANSMEM 865..886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 947..965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 977..996
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1044..1064
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1076..1094
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1106..1126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 144..314
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 1248 AA; 140677 MW; CBD080B7391EBAAF CRC64;
MLRKGILAYS RNVCRDFLPL SCTSDISVSY RYDRNLHTTL PKLKRIYKKR DPIQFNKKSE
KPQAKVWQSM SINDLAIVLK CDVDDIFECI MTTKYADLFE NVSDKIEDLN LIVHIVRQFG
YSINTDEELD VSPLPLPPLE QCKPRPPVVT IMGHVDHGKT TLLDSLRHSH IVDEEFGAIT
QHIGAFSVKL PNDRVITFLD TPGHAVFKKM RFRGAQVTDM VILVVAADDG VMEQTVESIR
MAQESHVPIV VAINKCDKFG VDLDSVKRQL LEYDVVGEQY GGDVQIIPIS ALKGTNLDLL
CEAVLTQADL MELVADYEGP VEGVVLESKT AHGQGKVCFA LVKRGCLRKG VVLVAGSCWC
KVRSLFDENK VELKMAKPSF PVEITGWKGD EIPSAGEAIL QVENERRAKQ VTNLRKRKQM
IKKALDEKHI IDQRRAEERL EYLKIRERKH QSGYIKYDPL ADYRRKKEAV SSYDGPILPF
VLKADVDGSL EAILDVYETY NSTKCNFDLV HFGIGDVTEN DLEIADTFKA LADSKGIQLR
KHNVIYSLID DFRKELNSRL PPVNKEVIIG EGSVIKEFMV SDIGRKKVPI AGCSVKKGIL
TKNDRIRFLR NGEVIYDGSV ISMRREKDLV SSSQVGQEVG IRIENSDVRF NVDDQVICYK
LVEEQQWKGS MKVMKNEKGR CLSMAVVRRP VCETMRWPVT RRINFLTNLS WFASCLPAFD
WRSQLFEAIG QSWHCWTAST WRGALNGHAA AIIVSSISSN SRGDNNSISS NCLLLVHCLS
SGYWFISFAT GCSYCWSRWA GRSAALMKLA AQLAKRNALL VMDRLAYRRQ SLLRSRNPWG
KWPSEPELRL GFCSSLRIAE ENIRMLLLAV LLVIYLVIGA MLFSVIERKQ EALERLLYSE
KLEHFKMQHC TTGGLTLVNC SALDELLEMR GKMSAAGMSE HRSSWDFFGS FYFVSTVVTT
IGFGMTTPRT AIGKAVVILY GFVGCSSSIL FFNLFLERIL TFLSCLFRVG HRIRLPQSNS
SNCGRRGSDE QSGSLETEWR PNLYFFWIGL LILSSTTITL AALLYQYAED WSYLEAVYFC
FVSFATIGFG DFISSQRTSE ISSYKLYSIL NFAILFVGCC CIYSLFNVTS IVIRSLLDQI
IASLDCRCRL FGRFRHHKAS VARRPVDGLH TTLDQNAKGA YLASVQTGDG LLSLKEFLDQ
TQDNLLSVPD QLLLPTEHDL RKSSVSASSV GPMAIVNEVI VPVADDDF
//
