ID A0A1B8DD54_9PEZI Unreviewed; 1017 AA.
AC A0A1B8DD54;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, 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=VE04_04366 {ECO:0000313|EMBL:OBT56827.1};
OS Pseudogymnoascus sp. 24MN13.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622150 {ECO:0000313|EMBL:OBT56827.1, ECO:0000313|Proteomes:UP000092157};
RN [1] {ECO:0000313|EMBL:OBT56827.1, ECO:0000313|Proteomes:UP000092157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24MN13 {ECO:0000313|EMBL:OBT56827.1,
RC ECO:0000313|Proteomes:UP000092157};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=24MN13 {ECO:0000313|Proteomes:UP000092157};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(2018).
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; KV456087; OBT56827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B8DD54; -.
DR STRING; 1622150.A0A1B8DD54; -.
DR Proteomes; UP000092157; 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; 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.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000092157}.
FT DOMAIN 481..649
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 41..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 748..803
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 43..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1017 AA; 111178 MW; 62431D4F22AA9EAE CRC64;
MGRIPSLFDL RVLRPWAGTS QGTVTYRTTL PTNIELETEF IGGCGSGQSQ GSDDRSQLPR
SQSAGAAFST GGGFGRPAFG SRPAFGNTGG GGGGAVAGSG RPAFGSGQIE LTEDEKRLRD
ALKTQGEAEA QTQAQSKPLK IRRPLKIYGG AGPEASRAGR PEPLDRVQNA TVMAKEARLE
RARQMSAGRR KRNDALPKDT ADGTPRSWNQ LNRRVLTQGE GSDNIPKAGL QDGDHHESRG
YTSPSARNPY TRQQQQPEFS SHRQISINKS SSDVSTPGPA PEPQLTTWRA APQRVEPELS
PAVLRLRQEE IERAADLEQR QKLREQRPLQ RSAEHSASSS RESENLGFKG RGKDKKKDRR
REEFATEEDD HVNAVVDRKA ELKKERKAAK AAKKAAAPTP VLLPEYISVA NLATVLKVRL
EHFVEKMEEL GFEETGTDYV LNGETAGLIA QEYNFEPLID RSESEDLKAR PAAEDPSIFP
QRAPVVTIMG HVDHGKTTIL DYLRKSSVAA GEAGGITQHI GAFSVPMPSG KVITFLDTPG
HAAFLNMRQR GANVTDIVVL VVAADDSVKP QTIEAINHAT GARVPIIVAI NKIDKEDTNI
DRVKQDLARH GVDIEDYGGD TQVVCVSGKT GQGMDELEEA ALTLSDVLDM RADTKGAAEG
WVLEASIKSM GKVATVLVRC GTMRPGDFIV AGKTWARIRC MRNEAGIEIT EAGPGTPVEI
DGWKEQPLAG DEVLQAPTEQ KAKNVVDYRV EKEERDRLAE DMEAINEDRK ITHEKRTKEK
LELEASKKRT AEENAEHDAL EEVVEEEHGP KQVYFILKGD VSGSVEAVTD SIAAIGSSEI
RPVILRSGVG NLSEFDVEHA AVAKGFLISF NNTIDPMIQK KADAAKVKIL DHNIIYRLVD
DVKGTLSEFL PPIVSHKVLG EAEVAQVFNI TIKGRKQKPI AGCKVRNGVI GRNTKIRVFR
QGKKVFDGDL ESLKNVKKDV AEARKGGECG MGFEGWHEFE VGDQVQCYEV KEEKRFL
//
