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CAZyme Information: EPE05345.1

You are here: Home > Sequence: EPE05345.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Ophiostoma piceae
Lineage Ascomycota; Sordariomycetes; ; Ophiostomataceae; Ophiostoma; Ophiostoma piceae
CAZyme ID EPE05345.1
CAZy Family GH17
CAZyme Description DYNc domain-containing protein [Source:UniProtKB/TrEMBL;Acc:S3CWZ4]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1083 KE148156|CGC4 120592.82 6.1825
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_OpiceaeUAMH11346 8884 1262450 0 8884
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in EPE05345.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 679 913 5.9e-50 0.9898477157360406

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
206738 DLP_1 2.45e-48 45 354 5 273
Dynamin_like protein family includes dynamins and Mx proteins. The dynamin family of large mechanochemical GTPases includes the classical dynamins and dynamin-like proteins (DLPs) that are found throughout the Eukarya. These proteins catalyze membrane fission during clathrin-mediated endocytosis. Dynamin consists of five domains; an N-terminal G domain that binds and hydrolyzes GTP, a middle domain (MD) involved in self-assembly and oligomerization, a pleckstrin homology (PH) domain responsible for interactions with the plasma membrane, GED, which is also involved in self-assembly, and a proline arginine rich domain (PRD) that interacts with SH3 domains on accessory proteins. To date, three vertebrate dynamin genes have been identified; dynamin 1, which is brain specific, mediates uptake of synaptic vesicles in presynaptic terminals; dynamin-2 is expressed ubiquitously and similarly participates in membrane fission; mutations in the MD, PH and GED domains of dynamin 2 have been linked to human diseases such as Charcot-Marie-Tooth peripheral neuropathy and rare forms of centronuclear myopathy. Dynamin 3 participates in megakaryocyte progenitor amplification, and is also involved in cytoplasmic enlargement and the formation of the demarcation membrane system. This family also includes interferon-induced Mx proteins that inhibit a wide range of viruses by blocking an early stage of the replication cycle. Dynamin oligomerizes into helical structures around the neck of budding vesicles in a GTP hydrolysis-dependent manner.
404513 Glyco_trans_2_3 1.24e-45 679 914 1 194
Glycosyl transferase family group 2. Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.
197491 DYNc 5.01e-21 38 274 20 233
Dynamin, GTPase. Large GTPases that mediate vesicle trafficking. Dynamin participates in the endocytic uptake of receptors, associated ligands, and plasma membrane following an exocytic event.
395279 Dynamin_N 1.82e-18 46 240 1 167
Dynamin family.
224136 BcsA 1.18e-08 677 1008 138 426
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 32 1083 9 1016
0.0 32 1083 9 1034
0.0 32 1083 9 1034
0.0 142 1083 1 912
4.83e-305 487 1083 52 642

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.48e-18 46 271 29 234
CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_1 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_2 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_3 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_4 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_5 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_6 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_7 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_8 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_9 CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_A CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_B CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_C CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_D CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_E CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_F CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_G CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_H CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_I CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_J CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_K CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_L CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_M CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_N CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_O CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_P CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_Q CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_R CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_S CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_T CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_U CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_V CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_W CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_X CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_Y CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_Z CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_a CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_b CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_c CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_d CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_e CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_f CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_g CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_h CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_i CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_j CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_k CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_l CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_m CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_n CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_o CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_p CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_q CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_r CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_s CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_t CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_u CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_v CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_w CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_x CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_y CryoEM structure of the helical assembly of full length MxB [Homo sapiens],5UOT_z CryoEM structure of the helical assembly of full length MxB [Homo sapiens]
1.58e-18 46 271 52 257
Myxovirus Resistance Protein 2 (MxB) [Homo sapiens],4WHJ_B Myxovirus Resistance Protein 2 (MxB) [Homo sapiens]
1.61e-18 46 271 16 222
GMPPCP-bound stalkless-MxA [Homo sapiens]
3.03e-18 46 271 31 237
GMPPCP-bound stalkless-MxA [Homo sapiens]
3.61e-18 46 271 37 243
GDP-bound stalkless-MxA [Homo sapiens]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.58e-19 46 271 36 242
Interferon-induced GTP-binding protein Mx OS=Epinephelus coioides OX=94232 GN=mx PE=2 SV=1
8.31e-19 46 271 36 242
Interferon-induced GTP-binding protein Mx OS=Solea senegalensis OX=28829 GN=mx PE=2 SV=1
9.07e-19 46 271 66 272
Interferon-induced GTP-binding protein Mx2 OS=Mus musculus OX=10090 GN=Mx2 PE=2 SV=2
5.30e-18 46 271 117 323
Interferon-induced GTP-binding protein Mx OS=Gallus gallus OX=9031 GN=MX PE=2 SV=1
5.39e-18 46 271 121 326
Interferon-induced GTP-binding protein Mx2 OS=Macaca mulatta OX=9544 GN=MX2 PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000043 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
433 455
891 913
928 950
971 993
1026 1048
1055 1074