CAZyme Information: MGYG000002381_01293

Basic Information

• Species: Stenotrophomonas bentonitica_A
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas bentonitica_A
• CAZyme ID: MGYG000002381_01293
• CAZy Family: CBM13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
581		58071.86	6.679

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002381	4114425	Isolate	not provided	not provided

• Gene Location: Start: 40330; End: 42075 Strand: +

Full Sequence      

MSHVSQHRLRQRALVVLGASVLSPLLLATPAFAGDVQLSGLSSAPTHQRFIVKYKDGSTE
VATPTALASSLKAAAAAVPAAQGRALGLQKLRQLAIGPTVVKADRPLDRAEAELLMRRLA
ADPSVEYVEVDQLMQATLVPNDTRFSEQWGFGTSNASINVRPAWDKATGAGVVVAVIDTG
ITNHPDLNANLLPGYDFISDAAMARDGGGRDNNPNDEGDWYAANECGSGIPASNSSWHGT
HVAGTVVAVTNNSTGVAGTAFNAKVVPVRVLGKCGGYTSDIADAIVWASGGTVSGVPANA
NPAEVINMSLGGGGSCSTTYQTAINGAVSRGTTVVVAAGNSNTNVSSSVPANCANVIAVA
ATTSAGARASFSNYGTGIDISAPGQGILSTLNSGTTVPGSASYASYNGTSMAAPHVAGVV
ALVQSVAPTALSPAAIESLLKSTARPLPGACSGGCGAGIVDADAAVTAALNGTGPGPGTG
TVLQNNVPVTGLGAASGASLAYTVTVPSGSSQLKVTIAGGSGDADLYVRNGSAPTDTVYT
CRPYLSGNNETCTISAPAAGTWHVRVKAYSTFSGVTLTAQY

Enzyme Prediction     

No EC number prediction in MGYG000002381_01293.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07496	Peptidases_S8_13	1.34e-130	171	443	1	285	Peptidase S8 family domain, uncharacterized subfamily 13. 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.
cd07484	Peptidases_S8_Thermitase_like	9.08e-83	139	447	1	259	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	3.23e-65	171	443	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	5.78e-65	171	445	3	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.
cd04077	Peptidases_S8_PCSK9_ProteinaseK_like	2.88e-60	165	446	20	255	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ALN86161.1	4.02e-164	26	472	29	480
ATE72186.1	5.69e-164	26	472	29	480
QZY84418.1	1.04e-133	43	440	63	450
CAG23448.1	1.36e-120	91	466	80	464
AIY26234.1	1.03e-116	91	467	79	464

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5YL7_A	9.75e-124	140	462	3	331	Proteasesfrom Pseudoalteromonas arctica PAMC 21717 (Pro21717) [Pseudoalteromonas arctica]
3LPA_A	1.02e-106	140	470	2	339	Crystalstructure of a subtilisin-like protease [Dichelobacter nodosus VCS1703A]
3LPC_A	2.04e-106	140	470	2	339	Crystalstructure of a subtilisin-like protease [Dichelobacter nodosus]
3LPD_A	3.12e-105	140	470	2	339	Crystalstructure of a subtilisin-like protease [Dichelobacter nodosus VCS1703A]
3TI7_A	5.96e-103	140	470	3	340	Crystalstructure of the basic protease BprV from the ovine footrot pathogen, Dichelobacter nodosus [Dichelobacter nodosus VCS1703A]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23314	4.62e-295	8	581	7	580	Extracellular protease OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=XCC0851 PE=3 SV=1
P42780	8.80e-114	49	472	45	474	Extracellular subtilisin-like protease OS=Dichelobacter nodosus OX=870 PE=3 SV=1
P42779	6.74e-112	49	470	48	472	Extracellular basic protease OS=Dichelobacter nodosus OX=870 GN=bprV PE=1 SV=1
P16588	3.85e-58	116	581	114	534	Alkaline serine exoprotease A OS=Vibrio alginolyticus OX=663 GN=proA PE=3 SV=1
Q45670	1.68e-42	113	425	97	362	Thermophilic serine proteinase OS=Bacillus sp. (strain AK1) OX=268807 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
0.000826	0.997495	0.000324	0.000907	0.000244	0.000180

TMHMM  Annotations     

start	end
13	32