CAZyme Information: MGYG000002821_00274

Basic Information

• Species: Finegoldia magna_F
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Peptoniphilaceae; Finegoldia; Finegoldia magna_F
• CAZyme ID: MGYG000002821_00274
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
769	MGYG000002821_2|CGC2	85628.79	9.844

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002821	1823789	MAG	United States	North America

• Gene Location: Start: 78240; End: 80549 Strand: +

Full Sequence      

MKNLKEIAKVSFVALSVSLMISTGSMAQTENDKKDVENELSAKYTSISTHNQSKLTKKAK
LGYANVDNLQNEKKENDDLNREDLKSTDLNKHIKEKEGKTEVSDSTKDQEESEKVVAPEK
SVSKENSEEQSSEEKEQETDGKESEDSEVKALNSAGQIIPTRIAGKNRYESAAKISREQF
TNAKKVIVVNAQKYADALSATTLSDGKYSILYTEKDSLPTATRNEIQRLNPVEVYLLGGQ
QSISAGIENILKKYSNKVTRIAGRDRYETSAKVAAMSKKKNVVIASGENFSDPLYASSYA
YSNNAKILLSSGKTLSRETRDYLLRNKSSIGKVTVVGGGQSISSATVRYIQSVTGKNVSR
ISGRNRYDGSVKVANSMKKDKVFIASGEDFADALAISPLAQKLNAPILLSSKGKLDTSVI
AFLNNFKNSIKDVFIVGGYRTIDNNVYGTVQNVLKKQIAKPKPQPKPQPKPKPPVVKDQS
DIIEEDKAIGLHDFVVAKHATTLYNAANSSAKSVRNINTSTVMQVINILDNGWMQLDING
FKGYAKVSDFGMFNPNKYRLVFQQGADLSKFNRNVNMKLAKQNGMDFVILKAGSGYSGED
PKFQQNYNNAKAAGLNVGAYWYSYAVNVEEAKEEAVRFMKILGKKQFEYPVYLDFEDPSQ
RKIPKKTKTDMAIAFMSILEKNGFYTGLYSSGSWINNQFERERLKDYDIWIAHWHVTSPN
CFTPDYGMWQFTNKSKIKGVPDTGEGGVDMNYSYKNYPKIIKDAKLNNF

Enzyme Prediction     

No EC number prediction in MGYG000002821_00274.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	567	740	3e-44	0.9887005649717514

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	1.65e-75	563	754	1	191	The LytC lysozyme of Streptococcus pneumoniae is a bacterial cell wall hydrolase that cleaves the beta1-4-glycosydic bond located between the N-acetylmuramoyl-N-glucosaminyl residues of the cell wall polysaccharide chains. LytC is composed of a C-terminal glycosyl hydrolase family 25 (GH25) domain and an N-terminal choline-binding module (CBM) consisting of eleven homologous repeats that specifically recognizes the choline residues of pneumococcal lipoteichoic and teichoic acids. This domain arrangement is the reverse of the major pneumococcal autolysin, LytA, and the CPL-1-like lytic enzymes of the pneumococcal bacteriophages, in which the CBM (consisting of six repeats) is at the C-terminus. This model represents the C-terminal catalytic domain of the LytC-like enzymes.
cd00599	GH25_muramidase	2.66e-37	564	752	1	185	Endo-N-acetylmuramidases (muramidases) are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues. This family of muramidases contains a glycosyl hydrolase family 25 (GH25) catalytic domain and is found in bacteria, fungi, slime molds, round worms, protozoans and bacteriophages. The bacteriophage members are referred to as endolysins which are involved in lysing the host cell at the end of the replication cycle to allow release of mature phage particles. Endolysins are typically modular enzymes consisting of a catalytically active domain that hydrolyzes the peptidoglycan cell wall and a cell wall-binding domain that anchors the protein to the cell wall. Endolysins generally have narrow substrate specificities with either intra-species or intra-genus bacteriolytic activity.
pfam01183	Glyco_hydro_25	8.22e-31	567	740	2	180	Glycosyl hydrolases family 25.
cd06525	GH25_Lyc-like	5.18e-28	564	752	1	183	Lyc muramidase is an autolytic lysozyme (autolysin) from Clostridium acetobutylicum encoded by the lyc gene. Lyc has a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.
cd06413	GH25_muramidase_1	2.90e-22	564	751	4	187	Uncharacterized bacterial muramidase containing a glycosyl hydrolase family 25 (GH25) catalytic domain. Endo-N-acetylmuramidases are lysozymes (also referred to as peptidoglycan hydrolases) that degrade bacterial cell walls by catalyzing the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAG07790.1	0.0	1	769	1	780
QKH79509.1	0.0	1	769	1	785
QQK08229.1	1.15e-52	565	769	5	217
QAR21437.1	8.18e-44	564	769	5	206
QLI94930.1	1.09e-43	564	769	5	206

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5J72_A	4.11e-27	162	412	134	396	ChainA, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630],5J72_B Chain B, Putative N-acetylmuramoyl-L-alanine amidase,autolysin cwp6 [Clostridioides difficile 630]
7ACZ_B	1.89e-21	163	430	43	360	ChainB, SLPH (HMW SLP) [Clostridioides difficile R20291],7ACZ_D Chain D, SLPH (HMW SLP) [Clostridioides difficile R20291]
7ACY_B	2.22e-20	148	411	29	329	ChainB, S-layer protein [Clostridioides difficile 630],7ACY_D Chain D, S-layer protein [Clostridioides difficile 630],7QGQ_B Chain B, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_D Chain D, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_J Chain J, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_K Chain K, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_L Chain L, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_M Chain M, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_N Chain N, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_T Chain T, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_U Chain U, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_V Chain V, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_W Chain W, Precursor of the S-layer proteins [Clostridioides difficile 630],7QGQ_X Chain X, Precursor of the S-layer proteins [Clostridioides difficile 630]
7ACX_B	2.98e-20	148	411	29	329	ChainB, S-layer protein [Clostridioides difficile],7ACX_D Chain D, S-layer protein [Clostridioides difficile]
5A6S_A	5.61e-20	566	762	25	210	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q02114	1.33e-29	162	452	30	315	N-acetylmuramoyl-L-alanine amidase LytC OS=Bacillus subtilis (strain 168) OX=224308 GN=lytC PE=1 SV=1
Q02113	1.57e-25	159	408	61	302	Amidase enhancer OS=Bacillus subtilis (strain 168) OX=224308 GN=lytB PE=1 SV=1
P26836	2.00e-13	564	769	10	207	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
Q8X7H0	1.35e-11	524	751	30	252	Uncharacterized protein YegX OS=Escherichia coli O157:H7 OX=83334 GN=yegX PE=3 SV=2
P76421	1.81e-11	524	751	30	252	Uncharacterized protein YegX OS=Escherichia coli (strain K12) OX=83333 GN=yegX PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000406	0.998808	0.000281	0.000161	0.000162	0.000154

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002821_00274.