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CAZyme Information: MGYG000002195_00551

You are here: Home > Sequence: MGYG000002195_00551

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 Emergencia sp900551775
Lineage Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Anaerovoracaceae; Emergencia; Emergencia sp900551775
CAZyme ID MGYG000002195_00551
CAZy Family GH23
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
2216 251588.53 5.3334
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000002195 4665652 MAG Spain Europe
Gene Location Start: 14944;  End: 21594  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000002195_00551.

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4646 COG4646 2.24e-63 931 1455 1 540
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair].
COG4646 COG4646 6.22e-28 1596 1785 439 635
Adenine-specific DNA methylase, N12 class [Replication, recombination and repair].
COG0286 HsdM 1.11e-09 716 908 157 375
Type I restriction-modification system, DNA methylase subunit [Defense mechanisms].
pfam02384 N6_Mtase 2.11e-09 716 993 17 295
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 4.17e-09 1401 1666 1 190
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 8.79e-312 642 2181 1554 3182
QIW86704.1 1.21e-308 642 2196 1622 3265
QIW86628.1 1.21e-308 642 2196 1622 3265
AEY69616.1 1.55e-306 640 2181 1693 3326
AXF51455.1 1.85e-306 625 2141 1770 3380

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 2.37e-38 655 1972 51 1567
Defense against restriction protein B OS=Escherichia phage P1 OX=2886926 GN=darB PE=3 SV=1
P52284 2.19e-08 727 849 26 135
Type II methyltransferase M.CvrRI OS=Paramecium bursaria Chlorella virus XZ-6E OX=36360 GN=CVIRIM 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
1.000071 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000002195_00551.