ID A0A061DS06_THECC Unreviewed; 1387 AA.
AC A0A061DS06;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Eukaryotic translation initiation factor 5B {ECO:0000256|ARBA:ARBA00013824};
DE AltName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00032478};
GN ORFNames=TCM_001618 {ECO:0000313|EMBL:EOX92723.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOX92723.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOX92723.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001879; EOX92723.1; -; Genomic_DNA.
DR EnsemblPlants; EOX92723; EOX92723; TCM_001618.
DR Gramene; EOX92723; EOX92723; TCM_001618.
DR HOGENOM; CLU_002656_2_1_1; -.
DR Proteomes; UP000026915; Chromosome 1.
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; cd03703; aeIF5B_II; 1.
DR CDD; cd16266; IF2_aeIF5B_IV; 1.
DR CDD; cd01887; IF2_eIF5B; 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; IPR029459; EFTU-type.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
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:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF14578; GTP_EFTU_D4; 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; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000313|EMBL:EOX92723.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000026915}.
FT DOMAIN 795..1011
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..33
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..144
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..347
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..656
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..689
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..790
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1387 AA; 153351 MW; EE92EE924DE103C0 CRC64;
MFGGSAFDAL ANDDDGEVVD DSLKEEDNVG EEEEENDKHA LAKALRGKKK KSKGAKKGGS
WFTAAALDEL DDDTGEKDDE KKDEEEDTPS LSFSGKKKKS SKSSKKSGGM FGGSAFDAIA
NEDDNGEMVE DESKVEEEED DDDVLAKAFT GKKKKSKGGK KSGMFGRSAF DSIADEDDNG
QMVEEESKVE EEEDVHAKAF TGKKKNSRGG KKGGSWFAAA ALDELDDEAG EKEDEKKDEE
DDVPSFFFSD KKKKSARSSK KSGNSFSAAL LDEEDDGEAS VSEPAVVDDF DDVSAIAFSG
KKKKSSKKKS NSAFAILTDG TEPQSEVTDM VESEQPSLGT SNVEADDSKT NNKSEGIAET
SKNKKKKKKN KSGRTAQEED DLDKILAELG EGPTVSKPAA PPPAEENVQV LPETVIPADA
TGEKEGEEEG VESAAAKKKK KKKEKEKEKK AAAAAAATAS ADVKEESQEE MKIETSDTKK
KDAKSKAADK KLPKHVREMQ EALARRQEAE ERKKREEEER LRKEEEERRR QEELERQAEE
ARRRKKEREK ERLLKKKQEG KLLTGKQKEE ARRLEAMRNQ ILGNKGGLPL PSADKDGAPT
KRPIYQSKRS KTAHHHANGA ASSKPEEKVQ AKEKQQEEQE TKDEVDTLED EKVDEVESNN
TEEKSVVADA AEDIGMEEED DDDGEWDEKS WDDVNLNVKG AFDDEEADFE PKHVVQKDIK
SAAPASRNAA PPAVAKPTVE TKKASASRSI KSQDDESKKP QPEAEAPDKN MKKNTAAKNK
APRSDAPPKQ SEENLRSPIC CIMGHVDTGK TKLLDCIRGT NVQEGEAGGI TQQIGATYFP
AENIRERTRE LKADAKLKVP GLLVIDTPGH ESFTNLRSRG SGLCDIAILV VDIMHGLEPQ
TIESLNLLKM RNTEFIVALN KVDRLYGWKV LRNAPILKSL KQQSKDVQNE FNMRLTHIVT
QFKEQGLNTE LYYKNREMGE TFSIVPTSAI TGEGIPDLLL LLVQWAQKTM VEKLTFNDEV
QCTVLEVKVI EGLGTTIDVV LVNGVLHEGD QIVVSGLQGP IVTTVRALLT PHPMKELRVK
GTYMQHKEIK AAMGIKIAAQ NLEHAIAGTG LYVVGPDDDL EDVKEAVRED MQSVMSRIDK
SGEGVYVQAS TLGSLEALLE FLKTPEVNIP VSGIGIGPVH KKDVMKASVM LEKKNEYATI
LAFDVKVTPE ARELADELGV RIFIADIIYH LFDQFKAYID GLKEERKKES ADEAVFPCVL
KILPNCIFNK KDPIVLGVDV LEGIARVGTP ICIPQREFID IGRLASIENN HRPVEVAKKG
QKVAIKIAGS NPEEQQKMYG RHFELEDELV SHISRRSIDV LKANYRDDLT LEEWRLVQRL
KILFKIP
//
