CAZyme Information: MGYG000001473_00205

Basic Information

• Species: Anaerosalibacter massiliensis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Tissierellales; Sporanaerobacteraceae; Anaerosalibacter; Anaerosalibacter massiliensis
• CAZyme ID: MGYG000001473_00205
• CAZy Family: CBM5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
442	MGYG000001473_7|CGC1	48395.39	5.0053

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001473	3196506	Isolate	not provided	not provided

• Gene Location: Start: 15484; End: 16812 Strand: -

Full Sequence      

MKKFLSLFMIVVVLTTLSTSVSADKFSMKDSKVVEGELIVSIEKPVGKYSIQSFDNQVEK
HTDTLNETGFEVKDSLLSSVFDGEVTISSKNNDFISEVIEEVGYIYLVKYEDTGESIEKV
IQRLEDKLTEKGLKVKLIEPNYVVKMDGQIDSLQDFRSIRTEKIHEDQAWHYEMINIPKA
WEISSGNRNVKMAVLDTGIDYNHKNLKNYVNKSLGKNFTSNDTSDFMDRQGHGTHVAGTI
ASYGEISGVMQEATLVPVKVLGDNGSGSTYNIMQGLIHATNEDVDVVNMSIRGWNYSEGM
DNACRTAESRGVIVVAATGNDSMSQIGYPARYDSVLSVGAVDSSGRRASFSNYGEGGVGV
MAPGVDIYSTFLNNKYMYMSGTSMATPHVAGVAGLIKSVNRNISASKAKEIIKNTANYAG
DQYEYGSGIVDAYKALEAVSGH

Enzyme Prediction     

No EC number prediction in MGYG000001473_00205.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07484	Peptidases_S8_Thermitase_like	1.14e-93	167	416	8	256	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.
cd07477	Peptidases_S8_Subtilisin_subset	2.14e-87	189	415	1	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.
cd07473	Peptidases_S8_Subtilisin_like	2.82e-75	187	416	1	258	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.
cd04077	Peptidases_S8_PCSK9_ProteinaseK_like	5.87e-65	194	417	31	254	Peptidase S8 family domain in ProteinaseK-like proteins. The peptidase S8 or Subtilase clan of proteases have a Asp/His/Ser catalytic triad that is not homologous to trypsin. This CD contains several members of this clan including: PCSK9 (Proprotein convertase subtilisin/kexin type 9), Proteinase_K, Proteinase_T, and other subtilisin-like serine proteases. PCSK9 posttranslationally regulates hepatic low-density lipoprotein receptors (LDLRs) by binding to LDLRs on the cell surface, leading to their degradation. The binding site of PCSK9 has been localized to the epidermal growth factor-like repeat A (EGF-A) domain of the LDLR. Characterized Proteinases K are secreted endopeptidases with a high degree of sequence conservation. Proteinases K are not substrate-specific and function in a wide variety of species in different pathways. It can hydrolyze keratin and other proteins with subtilisin-like specificity. The number of calcium-binding motifs found in these differ. Proteinase T is a novel proteinase from the fungus Tritirachium album Limber. The amino acid sequence of proteinase T as deduced from the nucleotide sequence is about 56% identical to that of proteinase K.
cd00306	Peptidases_S8_S53	1.83e-60	190	415	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
ACX42259.1	9.68e-120	1	441	1	433
QCD67055.1	4.39e-42	173	440	88	360
QFR21865.1	4.39e-42	173	440	88	360
ACV48841.1	7.49e-42	173	440	142	414
QGA83116.1	9.86e-40	173	440	142	414

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1SCN_E	8.35e-62	189	438	25	275	INACTIVATIONOF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE [Bacillus licheniformis]
1AF4_A	3.08e-61	189	437	25	274	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]
1C3L_A	3.08e-61	189	437	25	274	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]
1YU6_A	3.18e-61	189	437	26	275	CrystalStructure of the Subtilisin Carlsberg:OMTKY3 Complex [Bacillus licheniformis],1YU6_B Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex [Bacillus licheniformis]
3QTL_A	4.34e-61	189	437	25	274	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P00780	6.34e-59	132	437	47	379	Subtilisin Carlsberg OS=Bacillus licheniformis OX=1402 GN=subC PE=1 SV=2
Q99405	1.46e-56	87	435	37	378	M-protease OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=aprE PE=1 SV=2
P27693	2.87e-56	87	435	37	378	Alkaline protease OS=Alkalihalobacillus alcalophilus OX=1445 PE=1 SV=1
P41362	2.87e-56	87	435	37	378	Alkaline protease OS=Alkalihalobacillus clausii OX=79880 PE=1 SV=1
P00782	3.02e-56	106	437	40	382	Subtilisin BPN' OS=Bacillus amyloliquefaciens OX=1390 GN=apr PE=1 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
0.000301	0.998992	0.000216	0.000156	0.000150	0.000145

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001473_00205.