Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_9990400g0010 |
Family | GT47 |
Protein Properties | Length: 576 Molecular Weight: 66116.4 Isoelectric Point: 6.3829 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT47 | 158 | 495 | 0 |
QCRGRQIYVYDLPKKFNAELLEQCQSLIPWFNLCDYVTNEGMGKPIGNFYRRWYQTNQYTLELVFHSRISKHPCLVSSPAEANLFYIPYYGGLDVTRWNF RKNISNEKRDELGLELVNWLQGQPWWRRHGGRDHVLVLTKISWDFRRSNDADKWGSRLLHLPEMKSVTKLLVERYPWDMNEIGIPHPTFFHPRSDEDIWL WQRVISTSPRPYLISFAGAPRPNSTESIRSILIEQCLGKPEACEFLNCNAGVCLSPESTVKLFMKSEFCLQPVGDSPTRRSVFDSLIAGCIPVLFNPFTA YYQYPWHLPANQSSYSVYIPEEAVRQREINVVEALQKI |
Full Sequence |
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Protein Sequence Length: 576 Download |
MGTVIRRALL LPPLFLMLII CFWVTTSLLP VSVLRACFPS RRLNVYCVVL EDDKINLGDD 60 EEMQRLSVAN HGLKTESQLL NESVNAHGAA LKWEIPTSDV EISSQEKFGN VSNESTTMGN 120 QSLNAENGTI DHNVLKMKME AIRSASMPIG MKDPSQKQCR GRQIYVYDLP KKFNAELLEQ 180 CQSLIPWFNL CDYVTNEGMG KPIGNFYRRW YQTNQYTLEL VFHSRISKHP CLVSSPAEAN 240 LFYIPYYGGL DVTRWNFRKN ISNEKRDELG LELVNWLQGQ PWWRRHGGRD HVLVLTKISW 300 DFRRSNDADK WGSRLLHLPE MKSVTKLLVE RYPWDMNEIG IPHPTFFHPR SDEDIWLWQR 360 VISTSPRPYL ISFAGAPRPN STESIRSILI EQCLGKPEAC EFLNCNAGVC LSPESTVKLF 420 MKSEFCLQPV GDSPTRRSVF DSLIAGCIPV LFNPFTAYYQ YPWHLPANQS SYSVYIPEEA 480 VRQREINVVE ALQKIPEDQR KEMRRTIIQE IMPGLVYGDA DSKFDKFQDA FMISLNNIFW 540 RLEKAGISSS QNEAISIHDG EDNTAEVKYA ENSTDS |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam03016 | Exostosin | 7.0e-63 | 158 | 495 | 353 | + 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. |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI34680.1 | 0 | 117 | 549 | 573 | 996 | unnamed protein product [Vitis vinifera] |
RefSeq | NP_176534.2 | 0 | 11 | 545 | 74 | 663 | catalytic [Arabidopsis thaliana] |
RefSeq | XP_002269913.1 | 0 | 116 | 549 | 117 | 541 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002299537.1 | 0 | 33 | 544 | 59 | 571 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002509789.1 | 0 | 109 | 544 | 111 | 565 | Xyloglucan galactosyltransferase KATAMARI1, putative [Ricinus communis] |