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CAZyme Information: MGYG000000395_00327

You are here: Home > Sequence: MGYG000000395_00327

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 CAG-217 sp900547275
Lineage Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Acutalibacteraceae; CAG-217; CAG-217 sp900547275
CAZyme ID MGYG000000395_00327
CAZy Family GH23
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2588 293567.95 4.7212
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000000395 2097770 MAG Sweden Europe
Gene Location Start: 321676;  End: 329442  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000000395_00327.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4646 COG4646 3.80e-64 1672 2212 1 540
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair].
pfam18824 LPD11 1.43e-30 1248 1314 1 69
Large polyvalent protein-associated domain 11. This is an alpha-helical domain with conserved hydrophobic residues. It is found in polyvalent proteins of conjugative elements.
COG4646 COG4646 2.57e-28 2353 2544 439 637
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair].
pfam02384 N6_Mtase 6.81e-11 1436 1646 17 247
N-6 DNA Methylase. Restriction-modification (R-M) systems protect a bacterial cell against invasion of foreign DNA by endonucleolytic cleavage of DNA that lacks a site specific modification. The R-M system is a complex containing three polypeptides: M (this family), S (pfam01420), and R. This family consists of N-6 adenine-specific DNA methylase EC:2.1.1.72 from Type I and Type IC restriction systems. These methylases have the same sequence specificity as their corresponding restriction enzymes.
cd18011 DEXDc_RapA 2.57e-10 2158 2217 1 62
DEXH-box helicase domain of RapA. In bacteria, RapA is an RNA polymerase (RNAP)-associated SWI2/SNF2 (switch/sucrose non-fermentable) protein that mediates RNAP recycling during transcription. The ATPase activity of RapA is stimulated by its interaction with RNAP and inhibited by its N-terminal domain. The conformational changes of RapA and its interaction with RNAP are essential for RNAP recycling. RapA is part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
ASV45029.1 4.46e-235 1360 2580 1548 2781
AEY69616.1 2.27e-234 1360 2580 1689 2921
AXF51455.1 2.31e-234 1360 2580 1782 3014
QIW86704.1 6.41e-234 1360 2580 1616 2849
QIW86628.1 6.41e-234 1360 2580 1616 2849

PDB Hits      help

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
Q71TF8 2.42e-33 1378 2511 50 1224
Defense against restriction protein B OS=Escherichia phage P1 OX=2886926 GN=darB PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000045 0.000001 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000000395_00327.