dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: HUMAN GUT

help

CAZyme Information: MGYG000004667_04489

You are here: Home > Sequence: MGYG000004667_04489

Basic Information help

Species

Clostridium beijerinckii

Lineage

Bacteria; Firmicutes_A; Clostridia; Clostridiales; Clostridiaceae; Clostridium; Clostridium beijerinckii

CAZyme ID

MGYG000004667_04489

CAZy Family

GH24

CAZyme Description

hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
541		62402.88	4.3875

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000004667	6180974	Isolate	United States	North America

Gene Location

Start: 4632; End: 6257 Strand: -

Full Sequence Download help

Enzyme Prediction help

No EC number prediction in MGYG000004667_04489.

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
GH24	389	528	1.5e-36	0.9927007299270073

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd00737	lyz_endolysin_autolysin	1.36e-43	393	533	1	136	endolysin and autolysin. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
COG3772	RrrD	9.65e-29	389	537	7	152	Phage-related lysozyme (muramidase), GH24 family [Cell wall/membrane/envelope biogenesis].
cd16901	lyz_P1	3.49e-24	396	531	9	138	P1 lysozyme Lyz-like proteins. Enterobacteria phage P1 lysozyme Lyz is secreted to the Escherichia coli periplasm where it is membrane bound and inactive. Activation involves the release from the membrane, an intramolecular thiol-disulfide isomerization and extensive structural rearrangement of the N-terminal region. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division. Endolysins and autolysins are found in viruses and bacteria, respectively. Both endolysin and autolysin enzymes cleave the glycosidic beta 1,4-bonds between the N-acetylmuramic acid and the N-acetylglucosamine of the peptidoglycan.
NF033930	pneumo_PspA	6.65e-19	257	391	442	569	pneumococcal surface protein A. The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.
NF033840	PspC_relate_1	5.26e-18	259	356	511	603	PspC-related protein choline-binding protein 1. Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALS16930.1	1.07e-165	1	538	1	542
QMW91761.1	7.95e-163	1	538	1	542
BBK76021.1	7.95e-163	1	538	1	542
QGH24680.1	1.78e-159	1	538	1	544
QGH20639.1	1.78e-159	1	538	1	544

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6ET6_A	2.91e-20	390	533	53	194	ChainA, Lysozyme [Acinetobacter baumannii]
2ANV_A	9.95e-13	389	534	4	146	ChainA, Lysozyme [Lederbergvirus P22],2ANV_B Chain B, Lysozyme [Lederbergvirus P22],2ANX_A Chain A, Lysozyme [Lederbergvirus P22],2ANX_B Chain B, Lysozyme [Lederbergvirus P22]
7M5I_A	1.18e-11	389	537	9	158	ChainA, Endolysin [Escherichia coli O157 typing phage 15],7M5I_B Chain B, Endolysin [Escherichia coli O157 typing phage 15]
3HDF_A	6.55e-11	401	533	10	136	ChainA, Lysozyme [Enterobacteria phage P21],3HDF_B Chain B, Lysozyme [Enterobacteria phage P21]
4ZPU_A	1.01e-10	401	533	35	161	Thestructure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_B The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_C The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12],4ZPU_D The structure of DLP12 endolysin exhibits likely active and inactive conformations. [Escherichia coli K-12]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q37896	6.76e-16	389	536	3	146	Endolysin OS=Bacillus phage B103 OX=10778 GN=15 PE=3 SV=1
P07540	8.42e-16	389	532	3	142	Endolysin OS=Bacillus phage PZA OX=10757 GN=15 PE=3 SV=1
P11187	8.42e-16	389	532	3	142	Endolysin OS=Bacillus phage phi29 OX=10756 GN=15 PE=1 SV=1
Q9T1T5	1.76e-15	389	535	3	146	Endolysin OS=Acyrthosiphon pisum secondary endosymbiont phage 1 OX=2682836 GN=13 PE=3 SV=1
P09963	2.94e-12	389	534	4	146	Endolysin OS=Salmonella phage P22 OX=10754 GN=19 PE=1 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
1.000088	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM Annotations help

There is no transmembrane helices in MGYG000004667_04489.