ID A0A0G4KC97_9PEZI Unreviewed; 779 AA.
AC A0A0G4KC97;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=BN1708_000066 {ECO:0000313|EMBL:CRJ79653.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRJ79653.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRJ79653.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRJ79653.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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; CVQH01000001; CRJ79653.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4KC97; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
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; 1.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
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 SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000044602}.
FT DOMAIN 520..590
FT /note="Tr-type G"
FT /evidence="ECO:0000259|Pfam:PF00009"
FT DOMAIN 596..664
FT /note="Translation initiation factor IF- 2"
FT /evidence="ECO:0000259|Pfam:PF11987"
FT REGION 46..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 85028 MW; C4F3F0D79CCA6845 CRC64;
MLQCRTLRVW NLRRCFWPYA DLPQDRGNSY ICALCRHHGA ARPSHLTIRS YSSDPKSSSH
APHGRSGGLG GGWSSSASSA MPRRTSGPSN AGWGAPAFGA SNASAVNGSD STTTPSSNTP
TDTSSTPSPD DGLLPHERAA RQRLAAQRTS DSEPTKPAPQ PAKPHQHRTP PHKQEGLPSL
GRRPRQHFGS LDDSIGRTRA GPRPVAPIPH RSTPRAANPM GLDEKPGLRG SLGGLDGPPG
SSDPFARLAD SVDKKARTPR ARPHESGSSD WGLLSKRAPR QGPRGPRAQG SSAQGAAGSF
WERFKDHVHP SSGQGAEKQG LGDAQQENEI DYSAWDTAVA EPEETQPRRR NRESTFDASY
QIDRDARKRG KVGRDDKKAK RFGARNRSRF EEEEGDWDDE AAQRDRERRE RKAEKKMQRQ
LEAAEALEAA GPPKITLPEF INLTNLAYGL KLKPDFLLAS LEEMGFENMT LDSIFTGDTA
ALVAQEFGFE PTVDMGGDRE LRPRPEPEDP SSLPPRPPVV TIMGHVDHGK TTLLDYLRKS
SVAAQEHGGI TQHIGAFVVN MSSGRHITFL DTPGHAAFLT MRQRGAHVTD XQDGHELGNH
EVKPRILRSA VGQVSESDVE HAATSGSVIV NFNAAVAPHI KRLADAAGVR LIAHSVIYHL
ADEVRQTLSD QLADVVSTKV VGEAEVLQIF PINTKGRAFR NIAGCKIRNG LVSRTGMVRV
LRRGETVFEG KIDALKHGKK DVTEMRKGTE CGISFEGYQD FQVGDQVQTY EEVREKRTL
//
