ID A0A178ET16_TRIRU Unreviewed; 1023 AA.
AC A0A178ET16;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=A7C99_5487 {ECO:0000313|EMBL:OAL63099.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL63099.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL63099.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) 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: Mitochondrion {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 -!- 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:OAL63099.1}.
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DR EMBL; LHPM01000018; OAL63099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178ET16; -.
DR VEuPathDB; FungiDB:TERG_00894; -.
DR OMA; QCQKANP; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000243015; Unassembled WGS sequence.
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 CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 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; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
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 InterPro; IPR001876; Znf_RanBP2.
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; PF04760; IF2_N; 1.
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 PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:OAL63099.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000243015}.
FT DOMAIN 498..668
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 38..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 149..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 798..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..396
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1023 AA; 111956 MW; 5C4046FE9A8E2C69 CRC64;
MRRHSILKGI RCQNCCSPRR FPVKPVGNHE LSAQQLRQLS SSSNTVNGSD NNNSSNKTQP
SNPTFGRGWG APAFGGQVSC TAAELKQREA LLALQVSQKQ SHPTAESETK NGNTAREQHA
TWICAQCQKA NPVKSVSCPG CNWRPSQAYL TSSRSRPAQP KPSSPKASPG NGRTSSDTRN
QKQSKFTITR SWAPEQSLYR SARGRQQPQS TGQSSRDPRF GASGASSRAS GNTDTDHQEP
WQETGFRSIS RKPRSSLDSQ KQDSSVSGLW QLSGFRSLPP QSEQVRSSDI APESEAPPVR
SKPRRDELDS GNYTNEYHVG RQSSWAVRGR AQDFTPPSED ADNEFSSKPR KQKGRRATTE
DDLDEPPTRS NRRGASHARD LDIMDRELEY SVGRPKRKDK KGKKKAAQRV QEQSGPTPIV
LPDFISVGNL ADAINVRRTQ FIKSLESLGF DDVTNDHVLD SETAGLIVTE FNFEPVAESN
DVDLVAAPRP DDTSNLPPRP PVVTIMGHVD HGKTTLLDYL RKSSVVAAEH GGITQHIGAF
SVTMPSGKQI TFLDTPGHAA FLEMRKRGAD VTDIVILVVA ADDSVKPQTI EAIKHAKGAD
VPIIVAINKI DKEDINIDRV KQDLARHNVS VEDYGGDVQA IGVSGKTGQG MLKLEEAVIT
LSEMLDLRAD KECNFEGWII EASTKRAGRT ATVLVRQGTL RPGDVIVAGT SWAKVRTLRN
ESGIQVVEAL PGTPVEVDGW RDQPVAGFEV LQAPDEQRAK DVVAFRAEKE EVQRLGGDVE
AINQTRRETR ERRQLQAALE ENGDTPPDTT DKAGPQPIPF IIKADVSGSA EAIVNAMSAV
GNNEVFAKIL RFSVGKIGES DIRHASAANA AVISFNQSVD PDIMKLAVAE GVDILNHNII
YELIDDVKMR LSEHLPPTVT QRVSGEAEIG EIFEIKLKGK KTTFVAGCKV SNGVINRSHN
VRVLRGKNII YDGTLSSLKN VKKDVTEMRK GTECGMAFEG WADFAIGDEI QTYEVVREKR
QLD
//
