Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000315108 |
Family | GT47 |
Protein Properties | Length: 1037 Molecular Weight: 117551 Isoelectric Point: 9.076 |
Chromosome | Chromosome/Scaffold: 019152104 Start: 2390 End: 8963 |
Description | Translation elongation factor EF1B, gamma chain |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT47 | 170 | 501 | 0 |
SCSGRYIYVYDLPKRFNQDLLKNCHSLVRWNDMCSHLSNMGLGPRIHNSKGKLVGNGWFATNQFSLEVIFHNRMKXYRCLTNDSSLASAIFVPFYAGLDV GRYLWDYNTSVRDASPLELVKWLSRRPEWKAMWGRDHFLVGGRIAWDFRRLTDNNSDWGSKLMFLPESKNMTLLSIESGSWNNEQAIPYPTYFHPSKXSE VFEWQRRMRNRKRRYLFSFAGAPRSDSKDNIRDTIINQCRSSATCKLVSCYNGAKKCDDPLNVMKVFEASVFCLQPSGDSYTRRSTFDSILAGCIPVFFH PGSAYVQYLWHFPNTPSKYSVFISENDIKDQK |
Full Sequence |
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Protein Sequence Length: 1037 Download |
MKRLLVLMEK SRVAGRCHNQ PWFFLLIASF LLVFVLLLSD YSALSAGRNT QQVTYFITNF 60 ANVIVNQDNS TSLPYHDHST PISSNQTEIW LTLNVTNSST SNAIPAQFFG HGREENHSVK 120 SVVISKSPPA QPISPPPVQS ISSPPVQSIS SPPAQPISNE IGKNNSDADS CSGRYIYVYD 180 LPKRFNQDLL KNCHSLVRWN DMCSHLSNMG LGPRIHNSKG KLVGNGWFAT NQFSLEVIFH 240 NRMKXYRCLT NDSSLASAIF VPFYAGLDVG RYLWDYNTSV RDASPLELVK WLSRRPEWKA 300 MWGRDHFLVG GRIAWDFRRL TDNNSDWGSK LMFLPESKNM TLLSIESGSW NNEQAIPYPT 360 YFHPSKXSEV FEWQRRMRNR KRRYLFSFAG APRSDSKDNI RDTIINQCRS SATCKLVSCY 420 NGAKKCDDPL NVMKVFEASV FCLQPSGDSY TRRSTFDSIL AGCIPVFFHP GSAYVQYLWH 480 FPNTPSKYSV FISENDIKDQ KAIINETXLR IPKHQVVAMR KEVXRLIPRV IYANPMAPRX 540 ETVEDAFDIA VKGMLDKVEK IRRDMKEGKD PGVAFSELNG RKFDMPAVVV SDCTVVQFFL 600 RSQLSIXVSI ASQKXRNSVI VLHAGKTNKN GYKALITAEY TGVKVELAPN FXMGVSNKTP 660 EYLKLNPIGK VPLLVTPDGP IFESNAIARY VARLKADNPL YGCSLIDYAH IEQWIDFGSM 720 EIDANISKWY YPRLGYGVYL PPAEEAAISA LKRALGALNT HIASNTYLVG HSVTLADIVV 780 VCNLYVGFAN VMTKSFTSEF PHVERYFWTL VNQPNFKKVL GDVEQAVSVP PVASAKKPAQ 840 PAKGKIKEEP KKEAKKEPAK PKAEAAEEVE EAPKPKPKNP LDLLPPSKMV LDDWKRLYSN 900 TKSNFREVAI KGFWDMYDPE GYSLWFCEYK YNDENTVSFV TLNKVGGFLQ RMDLARKYAF 960 GKMLVIGSEA PFKVKGLWLF RGQEIPKFVM XECYDMELYS WTKVDISDEN QKERVNQMIE 1020 DQEPFEGEAL LDAKCFK |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd03044 | GST_N_EF1Bgamma | 8.0e-21 | 622 | 694 | 74 | + GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal TRX-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. | ||
COG0625 | Gst | 5.0e-27 | 630 | 819 | 195 | + Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones] | ||
pfam00647 | EF1G | 1.0e-43 | 887 | 984 | 98 | + Elongation factor 1 gamma, conserved domain. | ||
cd03181 | GST_C_EF1Bgamma_like | 2.0e-46 | 707 | 826 | 120 | + Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins. Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF. | ||
pfam03016 | Exostosin | 1.0e-67 | 170 | 506 | 351 | + Exostosin family. The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear. |
Gene Ontology | |
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GO Term | Description |
GO:0003746 | translation elongation factor activity |
GO:0005515 | protein binding |
GO:0005853 | eukaryotic translation elongation factor 1 complex |
GO:0006414 | translational elongation |
GO:0016020 | membrane |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ABK25057.1 | 0 | 620 | 1037 | 3 | 424 | unknown [Picea sitchensis] |
GenBank | ACU18062.1 | 0 | 620 | 1037 | 4 | 420 | unknown [Glycine max] |
EMBL | CAN75785.1 | 0 | 619 | 1037 | 2 | 423 | hypothetical protein [Vitis vinifera] |
Swiss-Prot | Q9FUM1 | 0 | 620 | 1037 | 3 | 422 | EF1G_PRUAV RecName: Full=Elongation factor 1-gamma; Short=EF-1-gamma; AltName: Full=eEF-1B gamma |
RefSeq | XP_002264400.1 | 0 | 619 | 1037 | 2 | 423 | PREDICTED: hypothetical protein [Vitis vinifera] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 1pbu_A | 2e-24 | 878 | 1037 | 2 | 162 | A Chain A, Solution Structure Of The C-Terminal Domain Of The Human Eef1bgamma Subunit |
PDB | 1aw9_A | 0.000000000001 | 642 | 831 | 25 | 214 | A Chain A, Structure Of Glutathione S-Transferase Iii In Apo Form |
PDB | 1bye_D | 0.000000000004 | 622 | 819 | 5 | 205 | A Chain A, Glutathione S-Transferase I From Mais In Complex With Atrazine Glutathione Conjugate |
PDB | 1bye_C | 0.000000000004 | 622 | 819 | 5 | 205 | A Chain A, Glutathione S-Transferase I From Mais In Complex With Atrazine Glutathione Conjugate |
PDB | 1bye_B | 0.000000000004 | 622 | 819 | 5 | 205 | A Chain A, Glutathione S-Transferase I From Mais In Complex With Atrazine Glutathione Conjugate |