Basic Information | |
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Species | Aquilegia coerulea |
Cazyme ID | Aquca_072_00077.3 |
Family | GT41 |
Protein Properties | Length: 619 Molecular Weight: 68643.6 Isoelectric Point: 6.6151 |
Chromosome | Chromosome/Scaffold: 72 Start: 505113 End: 517929 |
Description | Tetratricopeptide repeat (TPR)-like superfamily protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT41 | 60 | 550 | 0 |
SIKPNFSQSLNNLGVVYTVQGKMDAAASMIEKAIVANPSYAEAYNNLGVLYRDAGNISLAIEAYEQCLKIDPDSRNAGQNRLLAMNYINEDIDDKLFEAH RDWGRRFMRLFSQYTSWDNPKDPERPLVIGYVSPDYFTHSVSYFIEAPLVYHDYGKYKVVVYSGVVKGDAKTNRFRDKVVKKGGLWRDIYGIDEKKVASM VREDKVDILVELTGHTANNKLGMMACRPAPVQATWIGYPNTTGLPTIDYRITDSLADPPDTRQKHVEELVRLPKCFLCYTPSSEAGPVCPTPALSNGFVT FGSFNNLAKITPKVLQVWARILCSVPNSRLVVKCKPFCCDSVRQRFLSTLEQLGLESVRVDLLPLILLNHDHMQAYSLMDISLDTFPYAGTTTTCESLYM GVPCVTMAGSVHAHNVGVSLLSNVGLGHLIAKTEDEYIQSAVELASNITSLSELRLSLRGLMTNSPVCDGRSFILGLESTYRHLWHRYCRG |
Full Sequence |
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Protein Sequence Length: 619 Download |
MYNLGVAYGE MLQFDMAIVF YELALHFNPH CAEACNNLGV IYKDRDNLDK AVECYQLALS 60 IKPNFSQSLN NLGVVYTVQG KMDAAASMIE KAIVANPSYA EAYNNLGVLY RDAGNISLAI 120 EAYEQCLKID PDSRNAGQNR LLAMNYINED IDDKLFEAHR DWGRRFMRLF SQYTSWDNPK 180 DPERPLVIGY VSPDYFTHSV SYFIEAPLVY HDYGKYKVVV YSGVVKGDAK TNRFRDKVVK 240 KGGLWRDIYG IDEKKVASMV REDKVDILVE LTGHTANNKL GMMACRPAPV QATWIGYPNT 300 TGLPTIDYRI TDSLADPPDT RQKHVEELVR LPKCFLCYTP SSEAGPVCPT PALSNGFVTF 360 GSFNNLAKIT PKVLQVWARI LCSVPNSRLV VKCKPFCCDS VRQRFLSTLE QLGLESVRVD 420 LLPLILLNHD HMQAYSLMDI SLDTFPYAGT TTTCESLYMG VPCVTMAGSV HAHNVGVSLL 480 SNVGLGHLIA KTEDEYIQSA VELASNITSL SELRLSLRGL MTNSPVCDGR SFILGLESTY 540 RHLWHRYCRG DLPSLKTIEM QQSEAVVPDN IAVNLSESSR ITSLAGNLGS IKANGFRFGL 600 SSTPTLKPCE GNGKIESG* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00189 | TPR | 9.0e-15 | 67 | 158 | 92 | + Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here | ||
cd00189 | TPR | 5.0e-19 | 2 | 98 | 97 | + Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here | ||
pfam13844 | Glyco_transf_41 | 3.0e-21 | 358 | 544 | 187 | + Glycosyl transferase family 41. This family of glycosyltransferases includes O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, an enzyme which catalyzes the addition of O-GlcNAc to serine and threonine residues. In addition to its function as an O-GlcNAc transferase, human OGT, also appears to proteolytically cleave the epigenetic cell-cycle regulator HCF-1. | ||
cd00189 | TPR | 1.0e-24 | 33 | 132 | 100 | + Tetratricopeptide repeat domain; typically contains 34 amino acids [WLF]-X(2)-[LIM]-[GAS]-X(2)-[YLF]-X(8)-[ASE]-X(3)-[FYL]-X(2)-[ASL]-X(4)-[PKE] is the consensus sequence; found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans in various subcellular locations; involved in a variety of functions including protein-protein interactions, but common features in the interaction partners have not been defined; involved in chaperone, cell-cycle, transciption, and protein transport complexes; the number of TPR motifs varies among proteins (1,3-11,13 15,16,19); 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accomodate an alpha-helix of a target protein; it has been proposed that TPR proteins preferably interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes; examples of TPR-proteins include, Cdc16p, Cdc23p and Cdc27p components of the cyclosome/APC, the Pex5p/Pas10p receptor for peroxisomal targeting signals, the Tom70p co-receptor for mitochondrial targeting signals, Ser/Thr phosphatase 5C and the p110 subunit of O-GlcNAc transferase; three copies of the repeat are present here | ||
COG3914 | Spy | 3.0e-92 | 15 | 547 | 562 | + Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones] |
Gene Ontology | |
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GO Term | Description |
GO:0005515 | protein binding |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002281883.1 | 0 | 1 | 613 | 301 | 912 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002281883.1 | 6e-20 | 2 | 160 | 193 | 356 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002281883.1 | 0.0000000000002 | 3 | 144 | 119 | 267 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002281883.1 | 0.005 | 13 | 131 | 61 | 186 | 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 | 4gz6_D | 1e-35 | 3 | 336 | 14 | 386 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |
PDB | 4gz6_D | 4e-22 | 352 | 559 | 518 | 723 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |
PDB | 4gz6_D | 0.000000000002 | 29 | 139 | 6 | 116 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |
PDB | 4gz6_C | 1e-35 | 3 | 336 | 14 | 386 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |
PDB | 4gz6_C | 4e-22 | 352 | 559 | 518 | 723 | A Chain A, Unusual Structural Features In The Parallel Beta-Helix In Pectate Lyases |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
DY295408 | 383 | 128 | 508 | 0 |
DT769000 | 296 | 147 | 442 | 0 |
GT041789 | 337 | 43 | 379 | 0 |
HO781209 | 357 | 195 | 551 | 0 |
GT041789 | 64 | 342 | 405 | 8.1 |
Sequence Alignments (This image is cropped. Click for full image.) |
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