ID A0A0J9V4B9_FUSO4 Unreviewed; 1032 AA.
AC A0A0J9V4B9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=FOXG_08101 {ECO:0000313|EMBL:KNB06003.1};
OS Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS / NRRL 34936) (Fusarium vascular wilt of tomato).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=426428 {ECO:0000313|EMBL:KNB06003.1, ECO:0000313|Proteomes:UP000009097};
RN [1] {ECO:0000313|EMBL:KNB06003.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=4287 {ECO:0000313|EMBL:KNB06003.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KNB06003.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4287 {ECO:0000313|EMBL:KNB06003.1};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS231703; KNB06003.1; -; Genomic_DNA.
DR RefSeq; XP_018244048.1; XM_018386849.1.
DR AlphaFoldDB; A0A0J9V4B9; -.
DR GeneID; 28949754; -.
DR KEGG; fox:FOXG_08101; -.
DR VEuPathDB; FungiDB:FOXG_08101; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000009097; 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:KNB06003.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000009097}.
FT DOMAIN 508..676
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 127..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 113231 MW; 5F68FAC17AFBCD64 CRC64;
MLRVRTLQER GNSYVCAFCR HKLSPRDSQP RDRHVSSVGA PITSARAIRP SSCHSLRLPG
VRALSTSSIL HGPNDNGKPG GFPGSGFPGG FGAGLGSFGA FANKPSPDAS KQSVDLLPHE
LEARKKMGLP LKKPTPNVKA APTPPSAQSN IKKPPGLQNA NQNQSQKKNT PQARVNQQPN
RSNDGNNYAR QQQQRDAKPT TPPSNLLSSS ILAEAFRTDR TPAPVATPKS WSTNESPKPA
APPWGAFSAR KVDTHIPLIS RQTEAKPAEN QNKNKPQNVA PATGQEDDES VWGQLKRSRK
LKEKPGREND GFWDALESRV TNIRSRPGPS DQYKDALQGA DGMLQDSQQS QEDQIRRKSR
FEMEEDDVFD RRRDKKDKRP KNVRRNEAED DDFDEDSIRR WEARQRKKAE RDARKRLEEA
AEAAPVPIFL PEYISISNLA GALQIRITDF LHDLESMGFE DLSEETIMTG DTAALVAQEY
GYDPTVDTGS QRDLQPRPAP EDPSLLPSRP PVVTIMGHVD HGKTTLLDWL RKSSIAAQEH
GGITQHIGAF VVQMSSGKQI TFLDTPGHAA FLSMRQRGAN VTDIVVLVVA ADDSVMPQTL
EALKHATAAK VPIIVAINKI DKEDARVDQV KADLARHGVE IEDYGGDVQV VPVSGKTGKG
MQDLEENIVT LSEILDVRAE ADGMAEGWVL ESSIKQTGKT ATVLVKRGTL RLGDIIVAGK
SWAKIRGLRN EAGVEVPEAP PGTPVQILGW RELPDAGEQV LQAPDEGKAR TAVEYREEMA
ERLESSKQLA EQEQRQREKE AAEEAAAAAE AEGTEAEPAK TEPGILYQNF IVKADVAGSV
EAVCGTVQEL GNNEVQSKLL RSGVGAISEY DVDHAAASKS IIVNFNMPIL PHIRQRAEEA
GVRIIDHSVI YHVVDDVKSA LSDLLPHNIT HKVLGEADVL QVFAINVRKR LQKNIAGCKI
RNGTIKRTSM VRVIRGGEVV YDGKIDTLKH VKKDVMEMGK GTECGIGLED FQELQIDDQI
QTYEVIKERR TL
//
