CAZyme Information: MGYG000003745_00320

Basic Information

• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; CAG-1427
• CAZyme ID: MGYG000003745_00320
• CAZy Family: GH25
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1232		128835.79	4.5229

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003745	1293229	MAG	Canada	North America

• Gene Location: Start: 123; End: 3821 Strand: +

Full Sequence      

MLNAVLNELRKRTQIRHTHSDEPFCPRYDAAKAHAPWRTVMSVFISLTLVCGLLPIIPRQ
SYADETVSSDAIAQSAQISEDEIVIVYQDEVLDLDEEVATTSTDAEDRVADSAEDVDADS
DGEVSNSSDEQSTTTASAETTLQECGVVDQEEVTAATDDKGAVAVAQLEEGVSTEGAIEA
LESVEGIASVQPNYRYSLLTTTTSDMYATSDTTAEYNQYYLAASGITDAWDYAQAEGSVT
IATIDTGCNLQHEDLQGVVDTEHAYDVTTNSLLAAAGVANNGDANGHGTLVAGVLAAQAN
NGIGIAGASYNATIVPIKVFDDNDQCTTAQLIAAYEYLDGLLDQGELSSLHVINMSLGYY
ASGDDQADDALRAVIADMRDEHNVLTVCAGGNGTASGEARTATCYPSDFDECLSVTALNE
DGSVARFSDYNAAKDISAAGVNVLSTTATGGYATATGTSMAAPQVSAAAALLWAVDSSLT
TSQVVDALTNTADSVEGMQADNGSAGSLNAAAAVASVLGISLDDEQLADGDGAAEATTDD
ETTGSTTGTDSTSDDATSDASGVDGAADEKDAVDSGSSAQEGDQESDDSDGTTNDLSDRS
VVTLDDDADAATSSDSTSTNSTEADDNANSWRYTNGELLSEDLKQVQSILPLAAANNAYS
CATWYASNKTTSYTYKATPTSSKSTVKVSGVKKVGIDVSHHNGTINWKKAKADGISFAII
RCGYGSNFTAQDDTQFLANVKGALANDIEIGIYLYSYATKTTGSDSSATSEAQHVIRLLK
AAGLDPSKVTYPIFLDMEDKSQAALVDDASNKTTGRKLLGSIATTFCNALEAEGYTVGIY
ANKNWWDTYLTDSAFSNETWVKWVARYPVSKLTSSGVDGVDMWQFSDCGNVSGVGGLVDV
NFDYTYDYVGNSVVRATTSSVATQVYSGKALTPSPTVKLKGKTLVKGTDYTLSYKNNTNV
GTATITITGIGNYTGTKTVTFKIAKSLSSATVSSVSSKTYTGAAIKPTPTVKVGSTTLKN
GTDYTLSYKNNKSVGTATITITGKGSYTGTKSVTFKITKASLSKATIASIGTKTYTGKAL
KPTPTVKLSGNKLTTADYTVSYKNNTKTGTATVTIKGKGNCSGSKSITFKIKPAKVTSVS
VKSTSKGKITVKWSNTKGKAAGVTGYKIVVKYGSKTIKTQYVSGKSAKSKTVSVSSKYRG
KKVKVYVYAYKTINKSKVCSAASSVKTVKVKK

Enzyme Prediction     

No EC number prediction in MGYG000003745_00320.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH25	696	894	9.1e-41	0.9943502824858758

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd06414	GH25_LytC-like	5.27e-69	693	904	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.
cd07484	Peptidases_S8_Thermitase_like	1.51e-45	217	493	9	257	Peptidase S8 family domain in Thermitase-like proteins. Thermitase is a non-specific, trypsin-related serine protease with a very high specific activity. It contains a subtilisin like domain. The tertiary structure of thermitase is similar to that of subtilisin BPN'. It contains a Asp/His/Ser catalytic triad. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) clan include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53 the it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.
cd07473	Peptidases_S8_Subtilisin_like	7.31e-45	237	493	2	259	Peptidase S8 family domain in Subtilisin-like proteins. This family is a member of the Peptidases S8 or Subtilases serine endo- and exo-peptidase clan. They have an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The stability of subtilases may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd07477	Peptidases_S8_Subtilisin_subset	6.76e-41	239	491	2	229	Peptidase S8 family domain in Subtilisin proteins. This group is composed of many different subtilisins: Pro-TK-subtilisin, subtilisin Carlsberg, serine protease Pb92 subtilisin, and BPN subtilisins just to name a few. Pro-TK-subtilisin is a serine protease from the hyperthermophilic archaeon Thermococcus kodakaraensis and consists of a signal peptide, a propeptide, and a mature domain. TK-subtilisin is matured from pro-TK-subtilisin upon autoprocessing and degradation of the propeptide. Unlike other subtilisins though, the folding of the unprocessed form of pro-TK-subtilisin is induced by Ca2+ binding which is almost completed prior to autoprocessing. Ca2+ is required for activity unlike the bacterial subtilisins. The propeptide is not required for folding of the mature domain unlike the bacterial subtilases because of the stability produced from Ca2+ binding. Subtilisin Carlsberg is extremely similar in structure to subtilisin BPN'/Novo thought it has a 30% difference in amino acid sequence. The substrate binding regions are also similar and 2 possible Ca2+ binding sites have been identified recently. Subtilisin Carlsberg possesses the highest commercial importance as a proteolytic additive for detergents. Serine protease Pb92, the serine protease from the alkalophilic Bacillus strain PB92, also contains two calcium ions and the overall folding of the polypeptide chain closely resembles that of the subtilisins. Members of the peptidases S8 and S35 clan include endopeptidases, exopeptidases and also a tripeptidyl-peptidase. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. The S53 family contains a catalytic triad Glu/Asp/Ser. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values.
cd00306	Peptidases_S8_S53	3.51e-37	239	491	1	241	Peptidase domain in the S8 and S53 families. Members of the peptidases S8 (subtilisin and kexin) and S53 (sedolisin) family include endopeptidases and exopeptidases. The S8 family has an Asp/His/Ser catalytic triad similar to that found in trypsin-like proteases, but do not share their three-dimensional structure and are not homologous to trypsin. Serine acts as a nucleophile, aspartate as an electrophile, and histidine as a base. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of subtilisin. The serine residue here is the nucleophilic equivalent of the serine residue in the S8 family, while glutamic acid has the same role here as the histidine base. However, the aspartic acid residue that acts as an electrophile is quite different. In S53, it follows glutamic acid, while in S8 it precedes histidine. The stability of these enzymes may be enhanced by calcium; some members have been shown to bind up to 4 ions via binding sites with different affinity. There is a great diversity in the characteristics of their members: some contain disulfide bonds, some are intracellular while others are extracellular, some function at extreme temperatures, and others at high or low pH values.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAK44097.1	2.32e-229	36	915	38	834
BCA89043.1	4.91e-66	629	905	160	417
BCS56855.1	3.64e-49	628	905	156	441
AEB07228.1	7.96e-49	629	904	67	320
QUF79171.1	1.97e-48	688	893	75	259

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3QTL_A	2.84e-25	231	492	14	253	StructuralBasis for Dual-inhibition Mechanism of a Non-classical Kazal-type Serine Protease Inhibitor from Horseshoe Crab in Complex with Subtilisin [Bacillus licheniformis],3QTL_B Structural Basis for Dual-inhibition Mechanism of a Non-classical Kazal-type Serine Protease Inhibitor from Horseshoe Crab in Complex with Subtilisin [Bacillus licheniformis],3QTL_C Structural Basis for Dual-inhibition Mechanism of a Non-classical Kazal-type Serine Protease Inhibitor from Horseshoe Crab in Complex with Subtilisin [Bacillus licheniformis],4HX2_A Crystal structure of Streptomyces caespitosus sermetstatin in complex with Bacillus licheniformis subtilisin [Bacillus licheniformis],4HX2_C Crystal structure of Streptomyces caespitosus sermetstatin in complex with Bacillus licheniformis subtilisin [Bacillus licheniformis]
1C3L_A	2.84e-25	231	492	14	253	Subtilisin-CarlsbergComplexed With Xenon (8 Bar) [Bacillus licheniformis],3UNX_A Bond length analysis of asp, glu and his residues in subtilisin Carlsberg at 1.26A resolution [Bacillus licheniformis]
4GI3_A	2.91e-25	231	492	15	254	Crystalstructure of Greglin in complex with subtilisin [Bacillus licheniformis]
1AF4_A	7.08e-25	231	492	14	253	CRYSTALSTRUCTURE OF SUBTILISIN CARLSBERG IN ANHYDROUS DIOXANE [Bacillus licheniformis],1BE6_A TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE [Bacillus licheniformis],1BE8_A TRANS-CINNAMOYL-SUBTILISIN IN WATER [Bacillus licheniformis],1BFK_A Crystal Structure Of Subtilisin Carlsberg In 40% Acetonitrile [Bacillus licheniformis],1BFU_A SUBTILISIN CARLSBERG IN 20% DIOXANE [Bacillus licheniformis],1CSE_E THE HIGH-RESOLUTION X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN SUBTILISIN CARLSBERG AND EGLIN C, AN ELASTASE INHIBITOR FROM THE LEECH HIRUDO MEDICINALIS. STRUCTURAL ANALYSIS, SUBTILISIN STRUCTURE AND INTERFACE GEOMETRY [Bacillus subtilis],1OYV_A Chain A, Subtilisin Carlsberg [Bacillus licheniformis],1OYV_B Chain B, Subtilisin Carlsberg [Bacillus licheniformis],1R0R_E 1.1 Angstrom Resolution Structure of the Complex Between the Protein Inhibitor, OMTKY3, and the Serine Protease, Subtilisin Carlsberg [Bacillus licheniformis],1SBC_A The Refined Crystal Structure Of Subtilisin Carlsberg At 2.5 Angstroms Resolution [Bacillus subtilis],1SCA_A ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT [Bacillus licheniformis],1SCB_A ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT [Bacillus licheniformis],1SCD_A X-RAY CRYSTAL STRUCTURE OF CROSS-LINKED SUBTILISM CARLSBERG IN WATER VS. ACETONITRILE [Bacillus licheniformis],2SEC_E STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO [Bacillus licheniformis],2WUV_A Crystallographic analysis of counter-ion effects on subtilisin enzymatic action in acetonitrile [Bacillus licheniformis],2WUW_E Crystallographic analysis of counter-ion effects on subtilisin enzymatic action in acetonitrile (native data) [Bacillus licheniformis],4C3U_A Extensive counter-ion interactions with subtilisin in aqueous medium, Cs derivative [Bacillus licheniformis],4C3V_A Extensive counter-ion interactions with subtilisin in aqueous medium, no Cs soak [Bacillus licheniformis]
1YU6_A	7.24e-25	231	492	15	254	CrystalStructure of the Subtilisin Carlsberg:OMTKY3 Complex [Bacillus licheniformis],1YU6_B Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q45670	2.58e-24	173	497	95	383	Thermophilic serine proteinase OS=Bacillus sp. (strain AK1) OX=268807 PE=1 SV=1
P00780	1.48e-23	231	492	119	358	Subtilisin Carlsberg OS=Bacillus licheniformis OX=1402 GN=subC PE=1 SV=2
P00781	1.09e-22	231	492	14	253	Subtilisin DY OS=Bacillus licheniformis OX=1402 GN=apr PE=1 SV=1
P04072	7.49e-22	229	497	23	261	Thermitase OS=Thermoactinomyces vulgaris OX=2026 PE=1 SV=1
P54423	2.63e-20	241	503	458	694	Cell wall-associated protease OS=Bacillus subtilis (strain 168) OX=224308 GN=wprA PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.810127	0.173044	0.012714	0.002930	0.000480	0.000687

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003745_00320.