ID A0AAI9WZZ6_9ASCO Unreviewed; 1665 AA.
AC A0AAI9WZZ6;
DT 24-JUL-2024, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2024, sequence version 1.
DT 08-OCT-2025, entry version 7.
DE RecName: Full=Translation initiation factor IF-2, mitochondrial {ECO:0000256|ARBA:ARBA00044200};
GN ORFNames=KGF56_000711 {ECO:0000313|EMBL:KAI3406579.2};
OS Candida oxycetoniae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Pichiomycetes;
OC Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=497107 {ECO:0000313|EMBL:KAI3406579.2, ECO:0000313|Proteomes:UP001202479};
RN [1] {ECO:0000313|EMBL:KAI3406579.2}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 10844 {ECO:0000313|EMBL:KAI3406579.2};
RX PubMed=35438177; DOI=10.1093/dnares/dsac010;
RA Mixao V., Del Olmo V., Hegedusova E., Saus E., Pryszcz L., Cillingova A.,
RA Nosek J., Gabaldon T.;
RT "Genome analysis of five recently described species of the CUG-Ser clade
RT uncovers Candida theae as a new hybrid lineage with pathogenic potential in
RT the Candida parapsilosis species complex.";
RL DNA Res. 29:dsac010-dsac010(2022).
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:KAI3406579.2}.
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DR EMBL; JAHUZD010000023; KAI3406579.2; -; Genomic_DNA.
DR RefSeq; XP_049182324.1; XM_049326651.1.
DR GeneID; 73378328; -.
DR Proteomes; UP001202479; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-ARBA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0032543; P:mitochondrial translation; IEA:UniProtKB-ARBA.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR FunFam; 2.40.30.10:FF:000126; Mitochondrial translation initiation factor; 1.
DR FunFam; 6.10.250.3410:FF:000001; Protein DBF4 homolog A; 1.
DR FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.10050:FF:000001; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.300:FF:000019; Translation initiation factor IF-2; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 6.10.250.3410; DBF zinc finger; 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; IPR036420; BRCT_dom_sf.
DR InterPro; IPR055116; DBF4_BRCT.
DR InterPro; IPR053905; EF-G-like_DII.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013939; Regulatory_Dfp1/Him1.
DR InterPro; IPR005225; Small_GTP-bd.
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; IPR006572; Znf_DBF.
DR InterPro; IPR038545; Znf_DBF_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; PF22437; DBF4_BRCT; 1.
DR Pfam; PF08630; Dfp1_Him1_M; 1.
DR Pfam; PF22042; EF-G_D2; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 1.
DR Pfam; PF07535; zf-DBF; 1.
DR SMART; SM00586; ZnF_DBF; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 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; PS51265; ZF_DBF4; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP001202479};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00600}.
FT DOMAIN 782..831
FT /note="DBF4-type"
FT /evidence="ECO:0000259|PROSITE:PS51265"
FT DOMAIN 1133..1302
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 23..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..974
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1029..1049
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..82
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..313
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..400
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..699
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..896
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..965
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1005..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1665 AA; 188893 MW; D4D95BC2E53F3D9B CRC64;
MEDNNLSDKD YSASNDHDIF KKKFTSLSRP RQPLRETNSN LPISSFKRQG KHDKSVGIHS
PKTQSPCENF GKRKHSPLRK SRSSLSPLKK IVEDLVVKDS NSAQRAQIDT PLGNLDKAGK
PIKIVEGEST QPGGNPGGNP EGHHQMKEKG HHQQKEKEQH QQKEREQYQH QQHQQKEREQ
HQSQGNHLPS QIPKTNPNSS HEQTAEPVFE TPKKRGRAAS DDRMEHKRFV KPKTEEIATN
LLNKYIDKRP QIGIASTNQT YESEKYTTKK LDSTVTNKHS ISLNEQKEQS RIKNDVQLHS
PFQSQSKQTF SQQCKEKNIP HHKQNGSKST IDDSTSQGGL KYNKSSLKML DLNRLDQRHQ
EKSVENKSRK LQSQSQQQQQ HQQQQQHQQQ QQQQQQQQQQ KANGRLSGDE LLQWQQSWRK
IMKESTVFFE GYHDTQSSEY RRAIKYLKYV GCEVAPFYGN DVTIIISKRP YDDKAHYPAH
DIFSNVSRLK VKVWNYDKLF RFMKNLGLTT TTVSEEQSVN THTILPPSLS NNNLYSLLKG
EKIYGSTDRD PNARRDDFHY FGKNYLYVYD LSQAVRPIAI KEWGQDYPTL SLTLDGKCPF
IYDPLDQNSE KKRLKRLRKF EATKAHRQAL RAASNKVIHG ITLSVEGFTG TSTSTDNTEE
ASNEEASNEE EEEEEEEEEE EEEEEEEEEE EEEEEEEEAV EFRQPLTRNS SNMQSRAVEN
MASGYNGVSN ALQFSMDSNL NSNALAAGNG LGPIGSQVPS KNLNNLKKRI FLKRKVAERK
DKEMTPGYCE NCRIKYDSFD DHIMSNRHRN FACKDSNFKD IDELILTLKE SKSLGHVTSN
AKSPTESPSP SPSQQQQQQP RVNRFAQQYA QSEQQSSHKS SSGQQNRPRN RSSLSNSHDD
SRNSKNYEYQ KNATPRSGFN RTQYEPNDRS QQSQFNNGHF RSNNQGNNGQ PRRDKAPFQS
RDNHQQRHTP GFGHQLKQIV PQLTKEEIEQ QKTLKFQELQ KEIARQDAAK DNNRDTQQIK
SPMFQKKIIN SKKMQRNNNN NNKKKKKKKA LVKIQLPPFI SVSNLATVMQ VPLNDVFKKL
EGLGFEDIRH SYILDKENAA MIADEYDLEV ETVKESKNLD LFPAPVKQEL LKERPPVVTI
MGHVDHGKTT ILDYLRKSSI VKGEFGGITQ HIGAFSVIAP QSNKKITFLD TPGHAAFLKM
RERGAIITDI VILVVAADDS VMPQTIEAIK HAKKAGVPMI VAINKCDKPG INVDKVLADL
SAQGVDVEDY GGETQTVQVS GKTGLNMDKL EEAIVTLSEL NEFKAETKDV PAEGWIIESE
VLKGMGNVAT VLVRRGSLKT GDIIVAGETF CKIRGMKDEY NKVIKIAGPS TPVQVWGWKN
LPDSGDQILQ ASTEHVAKKV IDYRVARSQE IQVSRDIEDI NVKNAEAIKE AERLDKIAEM
KKAGLDPSEL EKAVEENGIK KCEYIIKADV FGSAEAIKES IDGLGNDEVK ASVLSHSAGP
PTESDIELAK TFGATIFCFN IQVPKTIHLK AEREKVEIKE HNIIYRLIED VTEKLSTLLT
PRIETKILAE VEVKDVFTIS QGKSKMKVAG CKVSTGIIKR SSQVKVLRDG TQVFKGNLSS
LKHVKEDIAE ARKGGECGIT FSDWNKFEQG DIIQAFEDVE HKQYL
//
