ID G3J440_CORMM Unreviewed; 960 AA.
AC G3J440;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=CCM_01269 {ECO:0000313|EMBL:EGX96611.1};
OS Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX96611.1, ECO:0000313|Proteomes:UP000001610};
RN [1] {ECO:0000313|EMBL:EGX96611.1, ECO:0000313|Proteomes:UP000001610}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM01 {ECO:0000313|EMBL:EGX96611.1,
RC ECO:0000313|Proteomes:UP000001610};
RX PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT valued traditional Chinese medicine.";
RL Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
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; JH126399; EGX96611.1; -; Genomic_DNA.
DR RefSeq; XP_006666488.1; XM_006666425.1.
DR AlphaFoldDB; G3J440; -.
DR STRING; 983644.G3J440; -.
DR GeneID; 18163300; -.
DR KEGG; cmt:CCM_01269; -.
DR VEuPathDB; FungiDB:CCM_01269; -.
DR eggNOG; KOG1145; Eukaryota.
DR HOGENOM; CLU_006301_8_3_1; -.
DR InParanoid; G3J440; -.
DR OMA; DPFVAGN; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000001610; 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; 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 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.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:EGX96611.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000001610}.
FT DOMAIN 435..603
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 106..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 104328 MW; 13C8DE01A774ED7A CRC64;
MLRTHAWQQR GPFVCAACRQ GRSVAQTPPR IAWSARLPGV ASPCTTEFGG RRLFSTSNIL
GDDSKPSFPG GFSGGAAKFG SFGAFASKAK PAATSGLLPH ELAARKTATI EPPKPATSTD
KAEQAKPRQP RKPRPVDPAR DQKTLKSKSV LADILRSDRQ PRDPATPASW SSTDRKAHAN
DPGRKPGDSN VWQELTKKRR DPVPHGKGTL GTRALKNGAK KEPNQEPIGL WADLDDQQGL
SEAQKKRNAR ERQVPKKMQG KYAGVHSHPS HVGDDLAPSK TPTDIPTKQK KSRFDDAPPI
RDDKKSKKGK HHGSSRRGTD EWEDDGDRWE ELEERKRAKE ARKAAKAEKP VAVPIFLPEY
ISATDLAQSL KQPLTSFMTD MEEMGFENIT GDTVMTGETA ALVAMEYGFE PTVDDGARRD
LQPAPMPEDM SSLPPRPPVV TIMGHVDHGK TTLLDYLRKS SVAAQEHGGI TQHIGAFVVS
MSTGKQITFL DTPGHAAFLS MRQRGANVTD IVVLVVAADD SVKPQTLEAL KHARAAKVPI
IVAINKIDKE DARVDQVKAD LSRHGVEIED YGGDVQVVCV SGKTGQGMDE LEENIVTLSE
ILDVRAETDG MASGWILESS IRQDGKAATV LVKRGTLRLG DHIVAGKTWA RVRLLRNEAG
VEMREAPPGT PVEILGWREL PPAGDMVLQA PDEARAKTAV AYRSEMADRE ANSANIAEQE
QRQRAKVAAD TLAAEKAELG EDGEEEAATA TGPLTQSFIV KADVAGSVEA VVGSILEQGN
HEVRSRVLRS SAGQVTEYDV DLAAASGSLI VNFNTAVAPH IKQRADEARV RILDHTVIYH
VVDDVRAALG ALLPPLVTQR VQGEADILQV FPINVTRRVV RNIAGCRVRN GALKKGSKVK
VLRKGKVIFE GIIDTIKHGK KDVQEMGKGT ECGIGLEDFE SFQEDDQLQT YEVISEKRQL
//
