ID K5W8G3_PHACS Unreviewed; 618 AA.
AC K5W8G3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, 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=PHACADRAFT_95981 {ECO:0000313|EMBL:EKM55470.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM55470.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM55470.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM55470.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(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}.
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DR EMBL; JH930472; EKM55470.1; -; Genomic_DNA.
DR RefSeq; XP_007395794.1; XM_007395732.1.
DR AlphaFoldDB; K5W8G3; -.
DR STRING; 650164.K5W8G3; -.
DR GeneID; 18920912; -.
DR KEGG; pco:PHACADRAFT_95981; -.
DR HOGENOM; CLU_006301_5_2_1; -.
DR InParanoid; K5W8G3; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000008370; 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; cd01887; IF2_eIF5B; 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 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 PRINTS; PR00315; ELONGATNFCT.
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 Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370}.
FT DOMAIN 91..267
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT COILED 368..404
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 618 AA; 66363 MW; 5317EEA1652D874C CRC64;
MHLKTIQADV YIPGLVSIEN LSRLLNVRLD RLQHKMSQVG MKEQSSYDHM LTAEYASLIA
LEFNRNPVVN DEAAFDIYPP PPTVSRESLP SRPPVVTIMG HVDHGKTTLL DTLRSASVAK
GEAGGITQHI GAFSVPVPNP GGEKRTITFL DTPGHAAFSA MRARGASVTD IVVLVVAADD
GIMPQTREVL KLVNRESNNV GLVVAINKID KPGADVSKVE TALLAEGVQL ETFDGDVPVV
HVSGLTGQGL PTLIETISLV AEMQDLRAEQ TGPIHGYVLE SKVDKGLGPV ATVLLLRGQL
TPGTSIICGL AHGKVRLLKS SSGQSFKAVM PGTAALVSGW KELPKAGDEV LLGTESEIKK
ALANRRRKAD LEATIQDAEA INESRRAERE LQQLEAQGEL VSQQMNGEDE KKELRLVVKG
DVSGTVEAVC GAVSGIGNHL AGAKIVAQGV GEVSESDVMR AKAAEGIILA FSVNTPRSVK
AIASSQGVKI IESNVIYALM DEVKKNVIEL LPTVTEKRVT GEANVLQIFE IQLKAKQTMK
VAGCRVVNGI VEKNKKARVV RNGENVFEGN LETLKHLKRD IMEAGKGLEC GMAFEGWDDL
REGDLIQMYQ EIVKPGQL
//
