ID A0A0M8NYQ8_9EURO Unreviewed; 1012 AA.
AC A0A0M8NYQ8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=ACN38_g11476 {ECO:0000313|EMBL:KOS37714.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS37714.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS37714.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS37714.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-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}.
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:KOS37714.1}.
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DR EMBL; LHQQ01000299; KOS37714.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8NYQ8; -.
DR STRING; 229535.A0A0M8NYQ8; -.
DR OrthoDB; 169393at2759; -.
DR Proteomes; UP000037696; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Gene3D; 4.10.1060.10; Zinc finger, RanBP2-type; 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 InterPro; IPR001876; Znf_RanBP2.
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 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.
DR PROSITE; PS01176; IF2; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000037696};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00322};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00322}.
FT DOMAIN 224..253
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 492..660
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1012 AA; 112954 MW; FDD48EBB62EE953F CRC64;
MMHRRPVCRL SRRAEWSNSA YRTPTLTALT LRRTLQLSAT RWNSSDPSSG NDDGTASNTA
PVKPKFGSRW GPKQHTPSAG LSFAEQAMRQ TLVANSQPPP PPPAPAPPQR KREQSNQQFN
SGQSNQQNKP YVRRVPPRDN QDVYMKWPRG TSRNQERTPS TQEQNPFKKE NADSHMRWPK
GTSRNQQRNP SIRGTKPTFE EENPFAPEKT QNRYQGQTRD HPMARDDWNC PQCMKHVFAT
KQVCPFCKTS RPDDAQPKFR ITREYSDSPG PSQSRQSRSP SEYDRKFQRL GDSVLSELEQ
DVQPSTTDTT GRHPKESDRP QTKEEAEDFK KNQWSWDMSA LEQLEGLETQ EQPPPKPMKR
RDGRKGRQSE SDEVDFDSED RERLRTERRR QQKEKDAQRA AKKAAAPAAP APLYLPEFIS
VSNLADVVGV RPAQFVQRME DMGFEEITYR DILDAETAGL VAAEFNYEAI FDSGKEDLYA
APEPEDTSDL PSRPPVVTIM GHVDHGKTTI LDWLRKSSVA ASEHGGITQH IGAFSVMMPS
GKAITFLDTP GHSAFLEMRR RGADVTDIVV LVVAADDSVK PQTIEAIKHA TQANVPVIVA
ISKIDKEGSN PDRVKGDLSV HGIHVEDYGG EVQAIGVSGK TGQGMVELEE AVIALSELLD
HRAATTCNVE GWVIEASTKS YGRVASVLIR RGTLRPGDII VAGTAWARVR TLRNEAGVTI
GEATPGMPVE IDGWREQPGA GTELLQAPTE QKAKDVVDYR LEKSDTQKMG VDIVAINEAR
REVLEKRRRD KEEEEITKEV EPTGPKSVNF VLKGDVDGSV EAVLNSVAAV GNNEVFANII
RSGVGPVSEF DIEHAGSAKG KIISFNQVID PNIMRIAETE GVEILDHNII YKLIDDIKAI
LSEKLPPSVT MRVTGEAEIQ QVFEITIKGR EKTAIAGSRV RNGLIHKTRK VRVLRGEEII
YDGTMASLKN VKKDVIEMRK DTECGIAFEN WTDFAPGDHI QCYEEISEKR YL
//
