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CAZyme Information: PHYCI_112571T0-p1

You are here: Home > Sequence: PHYCI_112571T0-p1

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 Phytophthora cinnamomi
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
CAZyme ID PHYCI_112571T0-p1
CAZy Family AA17
CAZyme Description Vesicle coat complex COPII, subunit SEC23
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
1452 163856.41 6.8156
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PcinnamomiCBS144-22 26201 1048749 70 26131
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.12:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 1063 1280 4.5e-19 0.8883248730964467

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
215083 PLN00162 0.0 30 518 227 706
transport protein sec23; Provisional
227380 SEC23 3.26e-177 29 518 221 700
Vesicle coat complex COPII, subunit SEC23 [Intracellular trafficking and secretion].
238755 Sec23-like 3.96e-78 29 191 105 267
Sec23-like: Protein and membrane traffic in eukaryotes is mediated by at least in part by the budding and fusion of intracellular transport vesicles that selectively carry cargo proteins and lipids from donor to acceptor organelles. The two main classes of vesicular carriers within the endocytic and the biosynthetic pathways are COP- and clathrin-coated vesicles. Formation of COPII vesicles requires the ordered assembly of the coat built from several cytosolic components GTPase Sar1, complexes of Sec23-Sec24 and Sec13-Sec31. The process is initiated by the conversion of GDP to GTP by the GTPase Sar1 which then recruits the heterodimeric complex of Sec23 and Sec24. This heterodimeric complex generates the pre-budding complex. The final step leading to membrane deformation and budding of COPII-coated vesicles is carried by the heterodimeric complex Sec13-Sec31. The members of this CD belong to the Sec23-like family. Sec 23 is very similar to Sec24. The Sec23 and Sec24 polypeptides fold into five distinct domains: a beta-barrel, a zinc finger, a vWA or trunk, an all helical region and a carboxy Gelsolin domain. The members of this subgroup lack the consensus MIDAS motif but have the overall Para-Rossmann type fold that is characteristic of this superfamily.
398467 Sec23_trunk 7.79e-51 29 193 81 241
Sec23/Sec24 trunk domain. COPII-coated vesicles carry proteins from the endoplasmic reticulum to the Golgi complex. This vesicular transport can be reconstituted by using three cytosolic components containing five proteins: the small GTPase Sar1p, the Sec23p/24p complex, and the Sec13p/Sec31p complex. This domain is known as the trunk domain and has an alpha/beta vWA fold and forms the dimer interface.
200443 Sec23_C 8.87e-50 422 518 1 97
C-terminal Actin depolymerization factor-homology domain of Sec23. The C-terminal domain of the Sec23 subunit of the coat protein complex II (COPII) is distantly related to gelsolin-like repeats and the actin depolymerizing domains found in cofilin and similar proteins. Sec23 forms a tight complex with Sec24. The cytoplasmic Sec23/24 complex is recruited together with Sar1-GTP and Sec13/31 to induce coat polymerization and membrane deformation in the forming of COPII-coated endoplasmic reticulum vesicles. The function of the Sec23 C-terminal domain is unclear.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 515 1452 89 1026
0.0 515 1452 89 1026
0.0 515 1452 89 1028
0.0 515 1452 80 1019
0.0 515 1452 89 1028

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.75e-161 24 518 221 706
Crystal structure of the mammalian COPII-coat protein Sec23/24 bound to the transport signal sequence of membrin [Homo sapiens],3EGD_A Crystal structure of the mammalian COPII-coat protein Sec23a/24a complexed with the SNARE protein Sec22 and bound to the transport signal sequence of vesicular stomatitis virus glycoprotein [Homo sapiens],3EGX_A Crystal structure of the mammalian COPII-coat protein Sec23a/24a complexed with the SNARE protein Sec22b and bound to the transport signal sequence of the SNARE protein Bet1 [Homo sapiens],5VNE_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with Emp24 sorting motif [Homo sapiens],5VNF_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal VV sorting motif [Homo sapiens],5VNG_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal II sorting motif [Homo sapiens],5VNH_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal SV sorting motif [Homo sapiens],5VNI_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal FA sorting motif [Homo sapiens],5VNJ_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal FF sorting motif (ERGIC-53) [Homo sapiens],5VNK_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with a C-terminal LL sorting motif [Homo sapiens],5VNL_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with 4-phenylbutyric acid (1mM soaking) [Homo sapiens],5VNM_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with 4-phenylbutyric acid (15mM soaking) [Homo sapiens],5VNN_A Crystal structure of Sec23a/Sec24a/Sec22 complexed with 4-phenylbutyric acid (50mM soaking) [Homo sapiens],5VNO_A Crystal structure of Sec23a/Sec24a/Sec22 [Homo sapiens]
2.83e-161 24 518 221 706
Crystal Structure of the mammalian COPII-coat protein Sec23/24 bound to the transport signal sequence of syntaxin 5 [Homo sapiens]
2.83e-161 24 518 221 706
Structure of Sec23 and TANGO1 complex [Homo sapiens],5KYN_B Structure of Sec23 and TANGO1 complex [Homo sapiens],5KYU_A crystal structure of Sec23 and TANGO1 peptide2 complex [Homo sapiens],5KYW_A crystal structure of Sec23 and TANGO1 peptide3 complex [Homo sapiens],5KYX_A crystal structure of Sec23 and TANGO1 peptide1 complex [Homo sapiens],5KYY_A Crystal structure of Sec23 and TANGO1 peptide4 complex [Homo sapiens]
3.19e-161 24 518 225 710
Crystal Structure of the human Sec23a/24a heterodimer, complexed with the SNARE protein Sec22b [Homo sapiens],2NUT_A Crystal Structure of the human Sec23a/24a heterodimer, complexed with the SNARE protein Sec22b [Homo sapiens]
9.32e-136 31 518 225 711
Cryo-tomography and subtomogram averaging of Sar1-Sec23-Sec24 - fitted model. [Saccharomyces cerevisiae S288C],6ZGA_A Chain A, Protein transport protein SEC23 [Saccharomyces cerevisiae],6ZGA_E Chain E, Protein transport protein SEC23 [Saccharomyces cerevisiae]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.69e-163 1 519 203 709
Protein transport protein Sec23B OS=Homo sapiens OX=9606 GN=SEC23B PE=1 SV=2
7.34e-163 1 519 203 709
Protein transport protein Sec23B OS=Mus musculus OX=10090 GN=Sec23b PE=1 SV=1
2.80e-162 1 518 203 708
Protein transport protein Sec23B OS=Bos taurus OX=9913 GN=SEC23B PE=2 SV=1
1.07e-161 1 518 203 708
Protein transport protein Sec23A OS=Gallus gallus OX=9031 GN=SEC23A PE=2 SV=1
7.69e-161 1 519 203 708
Protein transport protein Sec23B OS=Pongo abelii OX=9601 GN=SEC23B PE=2 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000044 0.000001

TMHMM  Annotations      download full data without filtering help

Start End
637 659
724 746
1242 1264
1276 1295
1310 1329
1350 1372
1382 1404
1425 1444