Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna19637.1-v1.0-hybrid |
Family | CBM43 |
Protein Properties | Length: 860 Molecular Weight: 94845 Isoelectric Point: 4.888 |
Chromosome | Chromosome/Scaffold: 3 Start: 550097 End: 556750 |
Description | O-Glycosyl hydrolases family 17 protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM43 | 571 | 652 | 1e-33 |
CIAMDGVDAKSLQAALDWACGPGRANCTEIQPGENCYSPNNVKNHASYAFDSYYQKQGKAAGSCDFKGVATITTTDPSKGSC | |||
GH17 | 233 | 552 | 0 |
VGVNIGTDVSNLLSPSELVSFLELQKITHIRLYDADPDILKALAKTKIRVIISVPNNQLIAIGSSNTTAASWVGRNVVAFYPQTLITGIAVGDEVLTTVP SSAPMLVPAIESLYSALVAANLHTQVKISTPNAASIILDPFPPSQAFFNQSLADIVVPLLRFLSKTGAPLMMNLYPYYVFMQNKGVVPLDNALFKPLTPS KEMVDPNTLLHYTNVLDAMIDAAYFSMKNLNVTDVMVLVTESGWPSKADSKEPYATVDNADTYNSNLIKHVFDRSGTPLHPETTSSVYIYELFNEDLRSP PVSEANWGLFYGNSSAVYLL |
Full Sequence |
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Protein Sequence Length: 860 Download |
MTMYMRRIAD LDLEDRRRWE RPRGGLSEHL WDQGLVSVSY LEYFGALTEK LEKEGIKLEG 60 SFVPSVEQKQ SSCLILPIGL ATVAVSPTGV DNVPLSVINP NQTNDAGTSN EIVLYDESVL 120 NVEVESMFLV ECIIFQSIHF PCLASFNLVQ VPFTYGQLNQ KQQQRKKRNQ PSSTSTSSPM 180 AFTNLHLPTL YFFFFSLLLT LLLSTSSIAA ESSQLYATLK QQIQDTDSKE PFVGVNIGTD 240 VSNLLSPSEL VSFLELQKIT HIRLYDADPD ILKALAKTKI RVIISVPNNQ LIAIGSSNTT 300 AASWVGRNVV AFYPQTLITG IAVGDEVLTT VPSSAPMLVP AIESLYSALV AANLHTQVKI 360 STPNAASIIL DPFPPSQAFF NQSLADIVVP LLRFLSKTGA PLMMNLYPYY VFMQNKGVVP 420 LDNALFKPLT PSKEMVDPNT LLHYTNVLDA MIDAAYFSMK NLNVTDVMVL VTESGWPSKA 480 DSKEPYATVD NADTYNSNLI KHVFDRSGTP LHPETTSSVY IYELFNEDLR SPPVSEANWG 540 LFYGNSSAVY LLHVSGSGTF LANDTTNQTF CIAMDGVDAK SLQAALDWAC GPGRANCTEI 600 QPGENCYSPN NVKNHASYAF DSYYQKQGKA AGSCDFKGVA TITTTDPSKG SCIFPGSKQA 660 SNVTRQVVNS THESGAAERL KFIGFNSKRP SGISWLLYVI FVGRNMDVGQ MQRQWVDYIK 720 SLFLEGFLDG QFLHLQKLQD ESTPDFVVEV VSIFFDETEK LLNDVTTALE QPSVDFRIIG 780 GHVYRFKGSS SSVGAQRVKD GCIAFRNYCE EENIEGCIGC LQELKQEYYL VKDKLQTLFA 840 MEQQIVAAGG SIPMLKLDI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01627 | Hpt | 2.0e-5 | 749 | 808 | 61 | + Hpt domain. The histidine-containing phosphotransfer (HPt) domain is a novel protein module with an active histidine residue that mediates phosphotransfer reactions in the two-component signaling systems. A multistep phosphorelay involving the HPt domain has been suggested for these signaling pathways. The crystal structure of the HPt domain of the anaerobic sensor kinase ArcB has been determined. The domain consists of six alpha helices containing a four-helix bundle-folding. The pattern of sequence similarity of the HPt domains of ArcB and components in other signaling systems can be interpreted in light of the three-dimensional structure and supports the conclusion that the HPt domains have a common structural motif both in prokaryotes and eukaryotes. In S. cerevisiae ypd1p this domain has been shown to contain a binding surface for Ssk1p (response regulator receiver domain containing protein pfam00072). | ||
cd00088 | HPT | 4.0e-6 | 749 | 808 | 62 | + Histidine Phosphotransfer domain, involved in signalling through a two part component systems in which an autophosphorylating histidine protein kinase serves as a phosphoryl donor to a response regulator protein; the response regulator protein is modulated by phosphorylation and dephosphorylation of a conserved aspartic acid residue; two-component proteins are abundant in most eubacteria; In E. coli there are 62 two-component proteins involved in a variety of processes such as chemotaxis, osmoregulation, metabolism and transport 1; also present in both Gram positive and Gram negative pathogenic bacteria where they regulate basic housekeeping functions and control expression of toxins and other proteins important for pathogenesis; in archaea and eukaryotes, two-component pathways constitute a very small number of all signaling systems; in fungi they mediate environmental stress responses and, in pathogenic yeast, hyphal development. In Dictyostelium and in plants, they are involved in important processes such as osmoregulation, cell growth, and differentiation; to date two-component proteins have not been identified in animals; in most prokaryotic systems, the output response is effected directly by the RR, which functions as a transcription factor while in eukaryotic systems, two-component proteins are found at the beginning of signaling pathways where they interface with more conventional eukaryotic signaling strategies such as MAP kinase and cyclic nucleotide cascades | ||
pfam07983 | X8 | 2.0e-25 | 569 | 641 | 78 | + X8 domain. The X8 domain domain contains at least 6 conserved cysteine residues that presumably form three disulphide bridges. The domain is found in an Olive pollen allergen as well as at the C-terminus of several families of glycosyl hydrolases. This domain may be involved in carbohydrate binding. This domain is characteristic of GPI-anchored domains. | ||
smart00768 | X8 | 1.0e-42 | 569 | 654 | 86 | + Possibly involved in carbohydrate binding. The X8 domain, which may be involved in carbohydrate binding, is found in an Olive pollen antigen as well as at the C terminus of family 17 glycosyl hydrolases. It contains 6 conserved cysteine residues which presumably form three disulfide bridges. | ||
pfam00332 | Glyco_hydro_17 | 1.0e-82 | 233 | 550 | 318 | + Glycosyl hydrolases family 17. |
Gene Ontology | |
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GO Term | Description |
GO:0000160 | phosphorelay signal transduction system |
GO:0004553 | hydrolase activity, hydrolyzing O-glycosyl compounds |
GO:0004871 | signal transducer activity |
GO:0005975 | carbohydrate metabolic process |
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 | 3us6_A | 0 | 706 | 858 | 1 | 153 | A Chain A, Crystal Structure Of Histidine-Containing Phosphotransfer Protein Mthpt1 From Medicago Truncatula |
PDB | 2cyg_A | 0 | 233 | 550 | 1 | 308 | A Chain A, Crystal Structure At 1.45- Resolution Of The Major Allergen Endo-Beta-1,3-Glucanase Of Banana As A Molecular Basis For The Latex-Fruit Syndrome |
PDB | 4euk_B | 0 | 705 | 857 | 5 | 157 | B Chain B, Crystal Structure |
PDB | 3ur8_B | 0 | 233 | 555 | 3 | 315 | B Chain B, Crystal Structure |
PDB | 3ur8_A | 0 | 233 | 555 | 3 | 315 | B Chain B, Crystal Structure |