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CAZyme Information: POV94369.1

You are here: Home > Sequence: POV94369.1

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 Puccinia striiformis
Lineage Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis
CAZyme ID POV94369.1
CAZy Family AA1
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
914 102328.00 8.1082
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Pstriiformis93-210 15090 N/A 0 15090
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 2.4.1.16:26 2.4.1.16:26

CAZyme Signature Domains help

Family Start End Evalue family coverage
GT2 206 382 3.3e-71 0.9938650306748467
GT2 359 629 2.5e-20 0.47058823529411764

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396286 Chitin_synth_1 6.38e-98 206 382 1 163
Chitin synthase. This region is found commonly in chitin synthases classes I, II and III. Chitin a linear homopolymer of GlcNAc residues, it is an important component of the cell wall of fungi and is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases.
133033 Chitin_synth_C 7.48e-90 202 538 1 244
C-terminal domain of Chitin Synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin. Chitin synthase, also called UDP-N-acetyl-D-glucosamine:chitin 4-beta-N-acetylglucosaminyltransferase, catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of GlcNAc residues formed by covalent beta-1,4 linkages. Chitin is an important component of the cell wall of fungi and bacteria and it is synthesized on the cytoplasmic surface of the cell membrane by membrane bound chitin synthases. Studies with fungi have revealed that most of them contain more than one chitin synthase gene. At least five subclasses of chitin synthases have been identified.
400626 Chitin_synth_1N 4.35e-30 131 205 1 70
Chitin synthase N-terminal. This is the N-terminal domain of Chitin synthase (pfam01644).
224136 BcsA 5.28e-27 331 665 115 413
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility].
367353 Chitin_synth_2 1.35e-16 348 629 187 451
Chitin synthase. Members of this family are fungal chitin synthase EC:2.4.1.16 enzymes. They catalyze chitin synthesis as follows: UDP-N-acetyl-D-glucosamine + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N) <=> UDP + {(1,4)-(N-acetyl-beta-D-glucosaminyl)}(N+1).

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 37 862 5 835
0.0 10 861 24 881
0.0 18 861 29 873
0.0 96 864 113 877
0.0 96 864 113 877

PDB Hits      help

POV94369.1 has no PDB hit.

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 92 847 88 848
Chitin synthase 7 OS=Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487) OX=235443 GN=CHS7 PE=2 SV=2
0.0 29 861 57 885
Chitin synthase 1 OS=Ustilago maydis (strain 521 / FGSC 9021) OX=237631 GN=CHS1 PE=3 SV=3
3.89e-302 8 848 20 867
Chitin synthase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=chsB PE=2 SV=2
5.40e-302 113 842 115 854
Chitin synthase 3 OS=Exophiala dermatitidis OX=5970 GN=CHS3 PE=3 SV=2
5.31e-301 70 848 80 862
Chitin synthase G OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=chsG PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000072 0.000000

TMHMM  Annotations      download full data without filtering help

Start End
568 590
610 632
642 664
685 707
722 744