ID C5FV79_ARTOC Unreviewed; 1024 AA.
AC C5FV79;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=MCYG_06632 {ECO:0000313|EMBL:EEQ33813.1};
OS Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Microsporum.
OX NCBI_TaxID=554155 {ECO:0000313|EMBL:EEQ33813.1, ECO:0000313|Proteomes:UP000002035};
RN [1] {ECO:0000313|Proteomes:UP000002035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4605 / CBS 113480 {ECO:0000313|Proteomes:UP000002035};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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}.
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DR EMBL; DS995706; EEQ33813.1; -; Genomic_DNA.
DR RefSeq; XP_002844668.1; XM_002844622.1.
DR AlphaFoldDB; C5FV79; -.
DR STRING; 554155.C5FV79; -.
DR GeneID; 9226986; -.
DR VEuPathDB; FungiDB:MCYG_06632; -.
DR eggNOG; KOG1145; Eukaryota.
DR HOGENOM; CLU_006301_8_4_1; -.
DR OMA; QCQKANP; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000002035; 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: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 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.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:EEQ33813.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000002035}.
FT DOMAIN 499..669
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1024 AA; 112403 MW; B2D753F9583DB0B0 CRC64;
MRRHSILKGI RCRYCYSLGR LPLKYTGNHE LLGQQIRQLS SSSNNVGGPD NNNGDEKPQS
AGSAFGRGWG SPAFGAPMTF TPAELKQREA LLAKQPRQKP SPPAEVTHGS HGQNENTTRD
QRATWVCAQC QKVNLMKLAF CPDCHWRPSQ TYLRSSTPRP PQRKPLGPRA SSEGEQKPGS
TKHQKQSKFT ITRFWATEQP PQRSDRSRQP PRHVNPSTQT PSSDSPSRIS TAREGADAAT
QKSQQNGDVQ NISLKPGRSL DSQTQALGGN ISWPLSGFRS LPPQSEQPQL SDIAPHSEAL
PARSKPKWDE MGTNTSTEEH ITTPTSSRGG YRKNNKDFTP YEEAGNDISF KPKKRKGRHA
ASKKDFDEPE IRPKHHSSKR DQDSDLMDLA EEYGMGQRRR KGDKKKVAQR LREQSGPTPI
VLPDFISVGN LADAINVRRP QFIKSLENLG FDNVTNDHVL DSETAGLIVT EFNFEPVAES
NDIDLVAAPA PEDTSNLPPK PPVVTIMGHV DHGKTTLLDY LRKSSVVATE HGGITQHIGA
FSVTMPSGKQ ITFLDTPGHA AFLEMRKRGA DVTDIVILVV AADDSVKPQT IEAIKHAKGA
DVPIIVAINK IDKEDTDIER VKQDLARHNV SVEDYGGDVQ AIGVSGKTGQ GMLKLEEAVI
TLSEMLDLRA DKECNFEGWV IEASTRKGGR AATVLVRQGT LRPGDVIVAG TSWAKIRTLR
NEAGVQVNEA LPGTPVEVDG WKDQPVAGSE ALQAPDEQRA KDVVMFRLEK EETQRLGGDV
EAINQTRRQE REKRQLQAAQ EDNGGTMADI ADKSGPEPIP FIVKADVSGS AEAIVNAVSA
IGNNEVFAKI LRFNVGKIGE SDIRLASAAN AAVISFNQSV EPDIMKLAIA EGVNILNHNI
IYELIDDVKM RLSEHLPPTV TQRVSGEAEI GEIFEIKLKG KKTASVAGCK VRNGVIYRSH
NVRVLRGKNV IYDGTLSSLK NVKKDVTEMR KGTECGMAFE NWADFAVGDE IQTYEVVHEK
RYLD
//
