| Basic Information | |
|---|---|
| Species | Vitis vinifera |
| Cazyme ID | GSVIVT01019767001 |
| Family | GT47 |
| Protein Properties | Length: 999 Molecular Weight: 114536 Isoelectric Point: 6.6305 |
| Chromosome | Chromosome/Scaffold: 2 Start: 3144644 End: 3153646 |
| Description | root hair specific 8 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| GT47 | 607 | 932 | 0 |
| CNGRGVFVYDLPPKFNKELVDHCYDMIPWMDFCKYLSNEALGEPILKLGKGWHQTHQYSLEPIFHSRVLKHPCRVYNQNEAKLFYVPFYGGLDILRWHFK NVSSDVKDTLGLELIQWLESQQPWIRNSGKDHVFVLGKISWDFRRNNKISWGTRFLELDQMQNPIKLLIERQPWHMNDIGIPHPTHFHPHSDDDIITWQL KIMRSKRKNLVSFAGAARPGAPENIRSILIKQCTSSDTGKCQFLNCDSGDCRQPESIIELFMESEFCLQPPGDSPTRKSVFDSLVSGCIPVLFDSFTAYY QYPWHLPEDHTRYSVFIDQEDVRSMK | |||
| Full Sequence |
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| Protein Sequence Length: 999 Download |
| MNNLKLGVDV VSAHNLMPKD GQGSSSAFVE LYFDGQKFRT TIKEKDLNPV WNESFYFNIS 60 DPSNLHYLTL DTASTYDLVE QMQFLFVRVV KARELPAMDV TGSLDPYVEV KIGNYKGVTK 120 HMEKKQNPEW NVVFAFSRDR MQASVLEVVV KDKDLVKDDF VGRARFDLNE VPMRVPPDSP 180 LAPEWYRLED KKGEKIKGEL MLAAQDLVPT EKNRFPDVYV KVHIGNQVMK TKTVQARSLT 240 TLWNEDLLFV AAEPFEDHLI LSVEDRVGPG KDEILGRVII PLSTVDRHGK GTSDTYCVAK 300 YVAARLGRAE PPLRKEVVEY MSDVDSHLWS MRRSKANFFR LMSIFSGLFA VGKWFGDICM 360 YPPHMNTRIS QADAVHPDEL DEEFDTFPTS RSPELVIAAL AGFYMMRHPR FRYRLPSAPI 420 NFFRRLPART DSMLWNHPRV ENQEQNLEET ILSPEMAISV SKKRSRLPKK AEAEELGSFI 480 SVLSKLLCRI PAVLLVLVLL FLWSSSTTII SGNIVHVCVS SRRLNNLYCL SAGTQPNFEI 540 PVSIVHNTSS STSTTPEMVD VFVENPVPIA DNSTGNERDE VENAVKIVEE QLRAHRSWTA 600 NGNTGDCNGR GVFVYDLPPK FNKELVDHCY DMIPWMDFCK YLSNEALGEP ILKLGKGWHQ 660 THQYSLEPIF HSRVLKHPCR VYNQNEAKLF YVPFYGGLDI LRWHFKNVSS DVKDTLGLEL 720 IQWLESQQPW IRNSGKDHVF VLGKISWDFR RNNKISWGTR FLELDQMQNP IKLLIERQPW 780 HMNDIGIPHP THFHPHSDDD IITWQLKIMR SKRKNLVSFA GAARPGAPEN IRSILIKQCT 840 SSDTGKCQFL NCDSGDCRQP ESIIELFMES EFCLQPPGDS PTRKSVFDSL VSGCIPVLFD 900 SFTAYYQYPW HLPEDHTRYS VFIDQEDVRS MKMNVVERLM KVSVREREDM RRYIVYELLP 960 GLVYGDSSSE FDKFQDAFSI SMNNLLERIS RLDSTSVN* 1020 |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| cd08378 | C2B_MCTP_PRT_plant | 0.009 | 217 | 285 | 69 | + C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset. MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology. | ||
| cd04019 | C2C_MCTP_PRT_plant | 6.0e-40 | 202 | 287 | 86 | + C2 domain third repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset. MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the third C2 repeat, C2C, and has a type-II topology. | ||
| cd08378 | C2B_MCTP_PRT_plant | 1.0e-47 | 84 | 203 | 120 | + C2 domain second repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset. MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-II topology. | ||
| pfam03016 | Exostosin | 9.0e-67 | 607 | 942 | 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 | |
|---|---|
| GO Term | Description |
| GO:0005515 | protein binding |
| GO:0016020 | membrane |
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| EMBL | CBI34680.1 | 0 | 1 | 998 | 1 | 998 | unnamed protein product [Vitis vinifera] |
| RefSeq | NP_176534.2 | 0 | 455 | 991 | 23 | 662 | catalytic [Arabidopsis thaliana] |
| RefSeq | XP_002269913.1 | 0 | 456 | 998 | 1 | 543 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299537.1 | 0 | 456 | 992 | 1 | 572 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002509789.1 | 0 | 456 | 992 | 1 | 566 | Xyloglucan galactosyltransferase KATAMARI1, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3hn8_C | 0.000000001 | 85 | 290 | 23 | 254 | A Chain A, Crystal Structure Of Synaptotagmin |
| PDB | 3hn8_C | 0.0000008 | 5 | 165 | 22 | 243 | A Chain A, Crystal Structure Of Synaptotagmin |
| PDB | 3hn8_B | 0.000000001 | 85 | 290 | 23 | 254 | A Chain A, Crystal Structure Of Synaptotagmin |
| PDB | 3hn8_B | 0.0000008 | 5 | 165 | 22 | 243 | A Chain A, Crystal Structure Of Synaptotagmin |
| PDB | 3hn8_A | 0.000000001 | 85 | 290 | 23 | 254 | A Chain A, Crystal Structure Of Synaptotagmin |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HS567391 | 267 | 72 | 286 | 0 |
| FC346433 | 254 | 690 | 941 | 0 |
| CO091625 | 250 | 92 | 289 | 0 |
| EX917484 | 260 | 73 | 282 | 0 |
| FC451292 | 239 | 691 | 927 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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