Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna24144.1-v1.0-hybrid |
Family | GT47 |
Protein Properties | Length: 622 Molecular Weight: 70503.5 Isoelectric Point: 8.9297 |
Chromosome | Chromosome/Scaffold: 1 Start: 10451191 End: 10460205 |
Description | Exostosin family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GT47 | 292 | 571 | 0 |
KLFKIYVYEEGEVPLFHAGPCKSIYSSEGRFIHEMEKGKLYRTKDPDEADVYFIPVSVTNLVEYLYVHGTPDRDPIKRAFIDYIKVIADRHPFWNRSLGA DHFMLSCHDWGPVTSSSVPDFFHNSIRVLCNANTSEGFNPSKDASFPEINLLTGEISSLGGPPPSTRTVLAFFAGRLHGHIRYLLLNEWKGKDEDVQVYE VLPKKVSYENKLKSSKFCLCPSGYEVASPRVVEAIYAECVPVLISDAYVPPFSDVLNWRSFSVQIPVQNISDIKNILMGI |
Full Sequence |
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Protein Sequence Length: 622 Download |
MEEQGLNVET AKNEDHYGAL IHHLSLVRNK RCLMAYLYNR AEILRTLMWK VGSLIPEEIE 60 EKLSYSEKEY IRKHSASLKK YMASVELDLE VDMVPPKDPY IKVRVLDDLG GDILLSDDKK 120 ANFTRHSMHF LKRTDAEQLI SQPLSSRSSS SSSSETWAVG NSSSTSRNFS YSRALSAAPA 180 EAPLTSFLYG SPSPAPAPAP APQISTGAIQ VGGIRRVKSW RSMKLDKLEE SLSKARSSIR 240 EAAATSLALK NKINSTSKSV QLVHDQDPDY VPHGRIYRNA QAFHRSYLLM EKLFKIYVYE 300 EGEVPLFHAG PCKSIYSSEG RFIHEMEKGK LYRTKDPDEA DVYFIPVSVT NLVEYLYVHG 360 TPDRDPIKRA FIDYIKVIAD RHPFWNRSLG ADHFMLSCHD WGPVTSSSVP DFFHNSIRVL 420 CNANTSEGFN PSKDASFPEI NLLTGEISSL GGPPPSTRTV LAFFAGRLHG HIRYLLLNEW 480 KGKDEDVQVY EVLPKKVSYE NKLKSSKFCL CPSGYEVASP RVVEAIYAEC VPVLISDAYV 540 PPFSDVLNWR SFSVQIPVQN ISDIKNILMG ISHRQYLRMQ RNVKQVQRHF VVNGPPKRYD 600 VFHMIVHSIW LRRLNIRVHD F* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam05916 | Sld5 | 0.001 | 24 | 68 | 46 | + GINS complex protein. The eukaryotic GINS complex is essential for the initiation and elongation phases of DNA replication. It consists of four paralogous protein subunits (Sld5, Psf1, Psf2 and Psf3), all of which are included in this family. The GINS complex is conserved from yeast to humans, and has been shown in human to bind directly to DNA primase. | ||
COG5230 | COG5230 | 1.0e-15 | 19 | 142 | 125 | + Uncharacterized conserved protein [Function unknown] | ||
cd11710 | GINS_A_psf1 | 2.0e-26 | 11 | 87 | 77 | + Alpha-helical domain of GINS complex protein Psf1. Psf1 is a component of the GINS tetrameric protein complex. Psf1 is mainly expressed in highly proliferative tissues, such as blastocysts, adult bone marrow, and testis, in which the stem cell system is active. Loss of Psf1 causes embryonic lethality. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3. | ||
pfam03016 | Exostosin | 2.0e-63 | 290 | 571 | 303 | + 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:0016020 | membrane |
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 | 2q9q_G | 1e-19 | 21 | 142 | 64 | 188 | C Chain C, The Crystal Structure Of Full Length Human Gins Complex |
PDB | 2q9q_C | 1e-19 | 21 | 142 | 64 | 188 | C Chain C, The Crystal Structure Of Full Length Human Gins Complex |
PDB | 2eho_J | 0.00000000000005 | 23 | 104 | 67 | 152 | A Chain A, Crystal Structure Of Human Gins Complex |
PDB | 2eho_F | 0.00000000000005 | 23 | 104 | 67 | 152 | A Chain A, Crystal Structure Of Human Gins Complex |
PDB | 2eho_B | 0.00000000000005 | 23 | 104 | 67 | 152 | A Chain A, Crystal Structure Of Human Gins Complex |
Sequence Alignments (This image is cropped. Click for full image.) |
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