Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | Medtr1g102430.1 |
Family | GT47 |
Protein Properties | Length: 878 Molecular Weight: 99422.7 Isoelectric Point: 8.7411 |
Chromosome | Chromosome/Scaffold: 1 Start: 30479354 End: 30485407 |
Description | glycosyltransferase 18 |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT47 | 100 | 442 | 0 |
CSSGRIFVYDLPKFFNQEILDNCDNLNPWSSRCNALSNDGLGEIATGLAGIVPENLLPSWYWTDQFVSEIIFHNRMLNHKCRTMEPESAAGFYVPFYVGL AVGKYLWMNTSTAKDRDSHCEKMLIWLNEQPYYKESNGWDHFITMGRITWDFRRSKDEDWGSSCIYKPGLRNITRLLIERNPWDYFDIGIPYPTGFHPSS FSDITRWQSFVRNRRRKSLFCFAGAPRRSFRNDFRAVLLNQCRNSGGSCHAVDCGGSKCANGTSAITETFLDSDFCLQPRGDSFTRRSIFDCMVAGSIPV FFWRRTAYLQYQWFLPEEPGSYSVYIDRNAVKNGTSVKAVLES |
Full Sequence |
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Protein Sequence Length: 878 Download |
MLPKSPPHSP ESQPFKLSTT KTSFKTTFQS LFNLQNPRAW IFLIFVFIQI LLFFNLRRFP 60 ASIPAPHHNF PTRLAVVDGG RRIQNYTVLD SIPTINSDEC SSGRIFVYDL PKFFNQEILD 120 NCDNLNPWSS RCNALSNDGL GEIATGLAGI VPENLLPSWY WTDQFVSEII FHNRMLNHKC 180 RTMEPESAAG FYVPFYVGLA VGKYLWMNTS TAKDRDSHCE KMLIWLNEQP YYKESNGWDH 240 FITMGRITWD FRRSKDEDWG SSCIYKPGLR NITRLLIERN PWDYFDIGIP YPTGFHPSSF 300 SDITRWQSFV RNRRRKSLFC FAGAPRRSFR NDFRAVLLNQ CRNSGGSCHA VDCGGSKCAN 360 GTSAITETFL DSDFCLQPRG DSFTRRSIFD CMVAGSIPVF FWRRTAYLQY QWFLPEEPGS 420 YSVYIDRNAV KNGTSVKAVL ESFTKEEVRK MREKVIEYIP RMVYAKHNEG IEGVKDAFDY 480 ATEGVLTRFK EQLQPGFHKR CLGVGLKNCF MPFLRVVLES ERVHKAEFGI WIPVPLFSPI 540 LAVRYLCCIS LPFAHPMLRS QLIPDIIRCY SSEGQTIIFT ETKESASQLA ELLHGARALN 600 GDIQQAQREV WEIHDISCHV VAAQDLYIND VQLIIQCEPP RDVKANIHRS GRTGSAGNTG 660 VVVMLYDPRR SNIPKIESQV LNLNINLPLK PMILPKLLAE NVIPAFKSAA EELLNNSGLS 720 VVDLFAKALA KVVVSLSCNL QGYTDIKKRS LLTSMENYVT LLLENRKPYL YPNKVEAVKG 780 LTITADGNGV VFDVAAEDLD TYLAGKEDAS YVRLKVLKEL PRLQQRDQSR GVRFGDGSGR 840 GGGSRFSGCG RNGRFSSDRF SNDGGRGRGG NWVGNIW* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
cd00079 | HELICc | 3.0e-10 | 571 | 665 | 108 | + Helicase superfamily c-terminal domain; associated with DEXDc-, DEAD-, and DEAH-box proteins, yeast initiation factor 4A, Ski2p, and Hepatitis C virus NS3 helicases; this domain is found in a wide variety of helicases and helicase related proteins; may not be an autonomously folding unit, but an integral part of the helicase; 4 helicase superfamilies at present according to the organization of their signature motifs; all helicases share the ability to unwind nucleic acid duplexes with a distinct directional polarity; they utilize the free energy from nucleoside triphosphate hydrolysis to fuel their translocation along DNA, unwinding the duplex in the process | ||
COG0513 | SrmB | 4.0e-14 | 573 | 677 | 119 | + Superfamily II DNA and RNA helicases [DNA replication, recombination, and repair / Transcription / Translation, ribosomal structure and biogenesis] | ||
cd12937 | GUCT_RH7_like | 1.0e-23 | 749 | 821 | 86 | + RNA-binding GUCT domain found in plant DEAD-box ATP-dependent RNA helicase 7 (RH7) and similar proteins. This subfamily corresponds to the Gu C-terminal (GUCT) domain of RH7 and similar proteins. RH7, also termed plant RNA helicase 75 (PRH75), is a new nucleus-localized member of the DEAD-box protein family from higher plants. It displays a weak ATPase activity which is barely stimulated by RNA ligands. RH7 contains an N-terminal KDES domain rich in lysine, glutamic acid, aspartic acid, and serine residues, seven highly conserved helicase motifs in the central region, a GUCT domain, and a C-terminal GYR domain harboring a large number of glycine residues interrupted by either arginines or tyrosines. RH7 is RNA specific and harbors two possible RNA-binding motifs, the helicase motif VI (HRIGRTGR) and the C-terminal glycine-rich GYR domain. | ||
pfam08152 | GUCT | 5.0e-26 | 742 | 825 | 97 | + GUCT (NUC152) domain. This is the C terminal domain found in the RNA helicase II / Gu protein family. | ||
pfam03016 | Exostosin | 1.0e-51 | 100 | 443 | 359 | + 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 | |
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GO Term | Description |
GO:0003723 | RNA binding |
GO:0004386 | helicase activity |
GO:0005524 | ATP binding |
GO:0005634 | nucleus |
GO:0016020 | membrane |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAA97186.1 | 0 | 1 | 492 | 1 | 510 | unnamed protein product [Arabidopsis thaliana] |
RefSeq | XP_002270309.1 | 0 | 3 | 492 | 8 | 483 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002318866.1 | 0 | 1 | 497 | 1 | 510 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002321855.1 | 0 | 3 | 497 | 19 | 514 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002510893.1 | 0 | 38 | 492 | 48 | 490 | Xyloglucan galactosyltransferase KATAMARI1, putative [Ricinus communis] |
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 | 2jgn_C | 0.0000000007 | 559 | 675 | 32 | 159 | A Chain A, Ddx3 Helicase Domain |
PDB | 2jgn_B | 0.0000000007 | 559 | 675 | 32 | 159 | A Chain A, Ddx3 Helicase Domain |
PDB | 2jgn_A | 0.0000000007 | 559 | 675 | 32 | 159 | A Chain A, Ddx3 Helicase Domain |
PDB | 2i4i_A | 0.000000009 | 565 | 675 | 268 | 389 | A Chain A, Crystal Structure Of Human Dead-Box Rna Helicase Ddx3x |
PDB | 2db3_D | 0.000001 | 559 | 670 | 289 | 408 | A Chain A, Structural Basis For Rna Unwinding By The Dead-Box Protein Drosophila Vasa |