ID A0A830HWT3_9CHLO Unreviewed; 908 AA.
AC A0A830HWT3;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 08-OCT-2025, entry version 14.
DE RecName: Full=Translation initiation factor IF-2, chloroplastic {ECO:0000256|ARBA:ARBA00044105};
GN ORFNames=PPROV_001063300 {ECO:0000313|EMBL:GHP11906.1};
OS Pycnococcus provasolii.
OC Eukaryota; Viridiplantae; Chlorophyta; Pseudoscourfieldiophyceae;
OC Pseudoscourfieldiales; Pycnococcaceae; Pycnococcus.
OX NCBI_TaxID=41880 {ECO:0000313|EMBL:GHP11906.1, ECO:0000313|Proteomes:UP000660262};
RN [1] {ECO:0000313|EMBL:GHP11906.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIES 2893 {ECO:0000313|EMBL:GHP11906.1};
RA Suzuki S., Kawachi M.;
RT "Unveiling of a novel bifunctional photoreceptor, Dualchrome1, isolated
RT from a cosmopolitan green alga.";
RL Submitted (OCT-2020) 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 -!- 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:GHP11906.1}.
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DR EMBL; BNJQ01000037; GHP11906.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A830HWT3; -.
DR OrthoDB; 361630at2759; -.
DR Proteomes; UP000660262; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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 FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1.
DR FunFam; 2.40.30.10:FF:000054; 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; 3.40.50.300; 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; IPR053905; EF-G-like_DII.
DR InterPro; IPR044145; IF2_II.
DR InterPro; IPR006847; IF2_N.
DR InterPro; IPR027417; P-loop_NTPase.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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 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 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:UP000660262}.
FT DOMAIN 377..548
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 129..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..163
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..183
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..221
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..249
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 908 AA; 94969 MW; 59CA603165EC398A CRC64;
MSATMSAITA AASASNNKGG ILRRRGMMAG RGGGMMAGRG GGGMIGGRSG RGGGGMMMYS
NAQGYYYSPA SSSRHFSMSA SCLAHQRSST VVPALGATAM EASLAPAFAA RRNSTFCAHF
GGGVGVCCPS PSSSSSSSSS SSSSLSSTKL YATPQAQQKQ APTDVGRGQG QGRGQGRGQG
RGQGRGRGRG GRGGRGGGRG GGGRGQGQGG GGYGGGGGGY QNQGDSSAGP RGGRGGGRGR
GRGRGRGGRG GRNGIGRRPF TTPTAAQKRK GRAMRKAERE ANRETKVAQE IIEVGEEGML
VGDLAEMLAV NATEVVKTLF LKGVMCSVNQ VLDIDAVKLV AESYEVEVLE EGEKSIYDEA
KKVESYDEDD GDDDLLPRAP VVCVMGHVDH GKTSLLDYMR KASVADGEAG GITQGIGAYR
VDVEGREDSL VFLDTPGHEA FSSMRARGAR VTDVAIVVVA ADDGVMPQTK EAISHAQAAE
VPIVIAYTKS DKSDANLDRV RTGLSEIGVV DEAWGGDFTC IPVSSKTGEG IPELLESVML
VAELEELKAN PDKLARGTVL EANLDKTVGA KATVLVQTGT LRIGDNIVSG ASFGKVRSMM
DDRGNKLEEA GPSTAVQITG WGEVPVAGAT FEACETDAEM RAMAEASADE NRLARLAERA
GGRAMSVSLT ALPNVTETGE LTKINVVLRT DASGSVEAVK AALDALPQDS VALRYLFASP
GEIAQSDVDL ATASEGIILG FNVQPSDDIQ SYAKDQGVEI RTYDVIYNLI DDVRAAMEGK
LLDKTVKDPL GSAKVLAVFG SGKRRAAGCS IEDGLLRKGC TIEVKRKKRV VYEGVMDSLR
KVREDVFELE EGNECGVQVE KFWDWKEGDR IFAYQLVTQS RTLEQASEEK VVVVSSTQSM
DDDDDGDE
//
