ID K2RD10_MACPH Unreviewed; 791 AA.
AC K2RD10;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=MPH_12118 {ECO:0000313|EMBL:EKG10807.1};
OS Macrophomina phaseolina (strain MS6) (Charcoal rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Macrophomina.
OX NCBI_TaxID=1126212 {ECO:0000313|EMBL:EKG10807.1, ECO:0000313|Proteomes:UP000007129};
RN [1] {ECO:0000313|EMBL:EKG10807.1, ECO:0000313|Proteomes:UP000007129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS6 {ECO:0000313|EMBL:EKG10807.1,
RC ECO:0000313|Proteomes:UP000007129};
RX PubMed=22992219; DOI=10.1186/1471-2164-13-493;
RA Islam M.S., Haque M.S., Islam M.M., Emdad E.M., Halim A., Hossen Q.M.M.,
RA Hossain M.Z., Ahmed B., Rahim S., Rahman M.S., Alam M.M., Hou S., Wan X.,
RA Saito J.A., Alam M.;
RT "Tools to kill: Genome of one of the most destructive plant pathogenic
RT fungi Macrophomina phaseolina.";
RL BMC Genomics 13:493-493(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}.
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:EKG10807.1}.
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DR EMBL; AHHD01000503; EKG10807.1; -; Genomic_DNA.
DR AlphaFoldDB; K2RD10; -.
DR STRING; 1126212.K2RD10; -.
DR VEuPathDB; FungiDB:MPH_12118; -.
DR eggNOG; KOG1145; Eukaryota.
DR HOGENOM; CLU_006301_8_5_1; -.
DR InParanoid; K2RD10; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000007129; 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:UP000007129}.
FT DOMAIN 252..420
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 71..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 519..562
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 114..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 86173 MW; B49F73CA61D10526 CRC64;
MEADALRAQF GLQRVAESVS SRQQFQSQPK LHQSVERDAL ASRFAKPSGV AEHGPSEDQE
WRKLAVDQEA ALEKGEGMER VEEDSLEEEQ GMERIRAAAQ QVRERERAGR FSKFADVEED
DAPRKRKTKG GWSKASAYED EEADFGRAER KSKKKDKRKQ RVVQVAPPTP IYLPEYLSVV
NLANMLRVRT EDLVRKMEEL GFEDINNDDI LNSENAGLIA MEYNFEPAAA DPSQDLDLYP
APEPEDLASL PARPPVITIM GHVDHGKTTL LDFLRKSSVA ATEFGGITQH IGAFSVPLSG
GKTITFLDTP GHAAFLSMRE RGANVTDIVI LVVAADDSVK PQTIEAIKHA KAARVPMIVA
INKVDKEGAN IERVKQDLAR HGVDIEDFGG DVQAIPVSGK TGQGMQDLEE AAITLSEILD
HRADPEGPVE GWILEAATKK SGKAATILVR RGTLKVGSIV VAGRTFARVR SIRNEAGVDI
PSVGPGMPAE IDGWRGQPEA GDEVLEAPDE QRATEVVEYR EANAERVQMA KDMEAINEAR
RLEHERRERE EAIAAAAKAG EEDPEAAVAA AAAAEAAENA KSGVIEVPFI VKADVSGSVE
AVVDYVMTVG NGEVRPRVIR SGVGPVGEFD IDYAATAGGH VVSFNVGLDP RLARMAESKG
VRVLEQNVIY RLVDDVKDVL SEKLEPTVVQ RVSGEAAVLQ VFSIALGRKQ SLNIAGCRVT
NGSVARGAKV RVFRGEEKVY DGTVSSLKQV KKDVSEMRKG SECGMAFEGW GDFQPGDTIQ
CYEERFEKRS L
//
