CAZyme Information: MGYG000001063_00675

Basic Information

• Species: Robinsoniella sp900540475
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Robinsoniella; Robinsoniella sp900540475
• CAZyme ID: MGYG000001063_00675
• CAZy Family: GH25
• CAZyme Description: Cell division suppressor protein YneA

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
406	MGYG000001063_24|CGC3	44800.4	4.4784

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001063	7637037	MAG	Sweden	Europe

• Gene Location: Start: 85913; End: 87133 Strand: -

Full Sequence      

MLKKTLSVLLSMVLLFSFFPVFMVSAIPPSSHPLYRGIDVSFYQEDIDFEQVADSGIQIV
YIRSSLGGDYIDPKFEDNYHKASAAGLSIGFYHYVTARSISQAQYQAQFFVNTIQGKDFD
CRLAMDFEDLQYLTDTEINAIGLAFIQTVEQLSGKKAVVYSDSYNAGYSFSGAVTNYPLW
VAEYGVSSPSDTSNWSFWVGWQYSDTGSVPGISTAVDLDYFTDGIFLNSSGPITSVPPPT
SPSTSYVDYEVKPGDTLWSIAHLYHTSITAIANENALSDPNLIYPGQILRIPIADDTPSD
ETYLTYTVKPGDTLWAIAHQYHTSIANLVSLNQIQNENLIYPGQRLKIPCKPNAGSQNPV
VWYTVKAGDTLWAIAVRYHTTVGALASINHLSNPGFILVGEKLLIP

Enzyme Prediction     

No EC number prediction in MGYG000001063_00675.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	38	212	8.6e-47	0.9943502824858758
CBM50	306	349	1.7e-17	0.975

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06525	GH25_Lyc-like	1.03e-72	36	221	1	184	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.
cd00599	GH25_muramidase	6.69e-50	36	221	1	186	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	2.78e-48	38	212	1	180	Glycosyl hydrolases family 25.
cd06414	GH25_LytC-like	3.94e-47	36	221	2	190	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.
COG3757	Acm	4.66e-43	35	229	63	261	Lyzozyme M1 (1,4-beta-N-acetylmuramidase), GH25 family [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QIB56830.1	9.31e-155	24	405	23	402
QMW80393.1	9.31e-155	24	405	23	402
QBE96304.1	3.06e-153	24	405	23	402
ANU77129.1	4.68e-150	24	403	23	400
QJU17248.1	4.68e-150	24	403	23	400

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4KRU_A	1.32e-44	36	230	21	216	X-raystructure of catalytic domain of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
4KRT_A	3.21e-43	36	230	21	216	X-raystructure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101],4KRT_B X-ray structure of endolysin from clostridium perfringens phage phiSM101 [Clostridium phage phiSM101]
5A6S_A	2.53e-23	27	223	15	203	Crystalstructure of the CTP1L endolysin reveals how its activity is regulated by a secondary translation product [Clostridium phage phiCTP1]
4B8V_A	8.92e-23	243	406	38	217	ChainA, Extracellular Protein 6 [Fulvia fulva],4B9H_A Chain A, Extracellular Protein 6 [Fulvia fulva]
1JFX_A	2.17e-20	36	221	6	202	Crystalstructure of the bacterial lysozyme from Streptomyces coelicolor at 1.65 A resolution [Streptomyces coelicolor]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P26836	4.04e-39	36	225	10	200	Probable autolytic lysozyme OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=lyc PE=3 SV=2
P34020	5.46e-32	36	230	2	189	Autolytic lysozyme OS=Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787) OX=272562 GN=lyc PE=1 SV=1
Q49UX4	8.03e-25	249	403	29	191	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41) OX=342451 GN=sle1 PE=3 SV=1
Q8CMN2	1.98e-24	249	406	29	191	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) OX=176280 GN=sle1 PE=3 SV=1
Q5HRU2	1.98e-24	249	406	29	191	N-acetylmuramoyl-L-alanine amidase sle1 OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=sle1 PE=3 SV=1

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
0.000314	0.998992	0.000180	0.000180	0.000158	0.000155

TMHMM  Annotations     

start	end
5	27