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Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna02487.1-v1.0-hybrid |
Family | GT61 |
Protein Properties | Length: 626 Molecular Weight: 71169.2 Isoelectric Point: 9.1588 |
Chromosome | Chromosome/Scaffold: 6 Start: 15918137 End: 15921222 |
Description | Glycosyltransferase family 61 protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT61 | 205 | 478 | 0 |
CDRSSMRSDVCTMKGDVRTHSPSSSIFVYASQDQAVKNEEDLQHEKIKPYTRKWETIIMDTIVELDLIAKKRTLIMNHHNCDVQHDVPAVFFSTGGYTGN VYHEFNDGIMPLYITSQHFNKKVVFVILEFHNWWVMKYSDILSHLSDYPVIDFHTDERVHCFPEAIVGLKIHDELTVDSSLMEGNKSIVDFRELLDRAYQ PQIRSLMHMHEHAKVSDVLSKSKRPSRIRRNVQERAFNNEPKLVIISRNGSRAITNENLLVKMAEKIGFHVQVL |
Full Sequence |
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Protein Sequence Length: 626 Download |
MKGLVYLSNP AALTSDQATS LSHHLAVLQV FEDCRRHLHT TRSPQFLGLR NQRGLWSESD 60 YGSDINVGVF DTGVWPKRQS FSDLNLGPMP KQWRSVCETG DRFAASNCNK KLIGARIFIK 120 GHEAAANAGG PMTAIDQRLD GIPVRKRHCR KKKERRYVVV GEGEKSGGRE NSGDRSPAPE 180 TGDWSPTVGD QSPVIFRPTA GAICCDRSSM RSDVCTMKGD VRTHSPSSSI FVYASQDQAV 240 KNEEDLQHEK IKPYTRKWET IIMDTIVELD LIAKKRTLIM NHHNCDVQHD VPAVFFSTGG 300 YTGNVYHEFN DGIMPLYITS QHFNKKVVFV ILEFHNWWVM KYSDILSHLS DYPVIDFHTD 360 ERVHCFPEAI VGLKIHDELT VDSSLMEGNK SIVDFRELLD RAYQPQIRSL MHMHEHAKVS 420 DVLSKSKRPS RIRRNVQERA FNNEPKLVII SRNGSRAITN ENLLVKMAEK IGFHVQVLRP 480 DSRTMLAEIY WALNSSDVMI GVHGAAMTHF LFMKPGSVFI QVIPLGIEWA AEAYYGEPAK 540 KLGLNYIGYQ ILTKESSLCD KYNKDDPVLK DPRSVTRKGW QYTKMIYLEG QTVRLDLPRF 600 RKQLVGAYNY TIDRLKQQRS NIQSH* 660 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam04577 | DUF563 | 3.0e-13 | 445 | 549 | 107 | + Protein of unknown function (DUF563). Family of uncharacterized proteins. | ||
cd04852 | Peptidases_S8_3 | 4.0e-31 | 37 | 136 | 105 | + Peptidase S8 family domain, uncharacterized subfamily 3. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. |
Gene Ontology | |
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GO Term | Description |
GO:0016757 | transferase activity, transferring glycosyl groups |
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 | 3i74_B | 3e-17 | 40 | 121 | 1 | 82 | C Chain C, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 In Complex With A Chloromethylketone Inhibitor |
PDB | 3i74_A | 3e-17 | 40 | 121 | 1 | 82 | C Chain C, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 In Complex With A Chloromethylketone Inhibitor |
PDB | 3i6s_B | 3e-17 | 40 | 121 | 1 | 82 | A Chain A, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 |
PDB | 3i6s_A | 3e-17 | 40 | 121 | 1 | 82 | A Chain A, Crystal Structure Of The Plant Subtilisin-Like Protease Sbt3 |
PDB | 3vta_B | 0.00000000009 | 40 | 118 | 1 | 74 | A Chain A, Crystal Structure Of Cucumisin, A Subtilisin-Like Endoprotease From Cucumis Melo L |
Sequence Alignments (This image is cropped. Click for full image.) |
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