CAZyme Information: MGYG000001298_02463

Basic Information

• Species: Listeria grayi
• Lineage: Bacteria; Firmicutes; Bacilli; Lactobacillales; Listeriaceae; Listeria; Listeria grayi
• CAZyme ID: MGYG000001298_02463
• CAZy Family: CBM13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
714		77900.73	10.2682

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001298	2589961	Isolate	not provided	Europe

• Gene Location: Start: 953104; End: 955248 Strand: +

Full Sequence      

MKKGYALFCSMILSIGILVTPATAQAEPNQAMTAESKQIIQTVQTAEKEDYQDQRVIVTL
KDTTPAYIEENYPLVQAEMIKTDTYLFKIKKSAGTLETLIKQLLADRTHISIAEPNYKAT
ISSSSTDKKLWAKNNSSYPEFDINYNKIDPAQSKKKIKIAVVDTGIDYNHPALKNVISKT
KSGAVNGRDFGDNDNDPMDKDSHGTHVAGTIAGANGIGLDTNVEIMPLKVERSDGNIYVS
DIIAAMDYAVKNKAAIVNLSLITPFKSQEMKKTIDKAKNVLFIAAAGNNGGNNDKEAGGT
NVNLMTPLYPASFDSPNIISVANLKQNGFLEESSNYGKTSVDLAAPGTNIYSTLPNGKYG
YKTGTSMAAPQVTGIAALLEGKYTSDSAVQIKSRILKNVHKLSALNGKMTTGGLLDAYKA
FSPDTLTSDRYYYIRSVGSGLYMNVKGNSSKENTALWQSGMNGKAGEQWKIVKNSNGSVY
LQSRLGKVLQLKNNSKNPNTVLQINKKNTKNNAQQFYLSKIANGRYSIESWKKQTNVAGV
SGNTKASKSAILAKRNQESLSEQWEFKPVAIQSGKTYNLISKKSGKALEISSTSKLAGAK
LYQNTSKNSISQQFILKKDSKGIQIVSKANPKYALEIAGNKMAKRTKLSMQTQKNTKGQH
FTFKFQSDGSVTIAALSSTKYGLDVKGASTKNKTAIQLYSLKNLDNQKWFLIPR

Enzyme Prediction     

No EC number prediction in MGYG000001298_02463.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM13	575	710	3.2e-16	0.675531914893617

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07473	Peptidases_S8_Subtilisin_like	4.65e-87	154	399	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.
cd07477	Peptidases_S8_Subtilisin_subset	1.20e-61	157	398	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.
cd07484	Peptidases_S8_Thermitase_like	9.11e-59	134	403	2	260	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.
cd00306	Peptidases_S8_S53	9.99e-54	157	398	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.
cd07474	Peptidases_S8_subtilisin_Vpr-like	4.97e-45	155	420	2	295	Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VEI36172.1	0.0	1	714	1	714
BAY62672.1	7.05e-49	154	421	66	349
QIR40666.1	7.73e-49	152	428	61	358
BAY27877.1	9.78e-49	149	421	57	350
BAY12514.1	1.57e-48	149	421	172	443

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1DBI_A	5.06e-37	158	420	34	277	CrystalStructure Of A Thermostable Serine Protease [Bacillus sp. Ak1]
3VV3_A	2.16e-35	155	420	42	324	Crystalstructure of deseasin MCP-01 from Pseudoalteromonas sp. SM9913 [Pseudoalteromonas sp. SM9913],3VV3_B Crystal structure of deseasin MCP-01 from Pseudoalteromonas sp. SM9913 [Pseudoalteromonas sp. SM9913]
1AK9_A	1.66e-34	157	402	26	257	ChainA, SUBTILISIN 8321 [Bacillus amyloliquefaciens]
1S01_A	2.26e-34	157	402	26	257	LARGEINCREASES IN GENERAL STABILITY FOR SUBTILISIN BPN(PRIME) THROUGH INCREMENTAL CHANGES IN THE FREE ENERGY OF UNFOLDING [Bacillus amyloliquefaciens]
1AQN_A	2.26e-34	157	402	26	257	ChainA, SUBTILISIN 8324 [Bacillus amyloliquefaciens],1AU9_A Chain A, SUBTILISIN BPN' [Bacillus amyloliquefaciens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q45670	2.08e-37	10	420	8	398	Thermophilic serine proteinase OS=Bacillus sp. (strain AK1) OX=268807 PE=1 SV=1
P00781	1.71e-31	157	395	26	249	Subtilisin DY OS=Bacillus licheniformis OX=1402 GN=apr PE=1 SV=1
P00782	6.45e-31	157	402	133	364	Subtilisin BPN' OS=Bacillus amyloliquefaciens OX=1390 GN=apr PE=1 SV=1
P11018	2.18e-30	155	380	42	260	Major intracellular serine protease OS=Bacillus subtilis (strain 168) OX=224308 GN=isp PE=1 SV=2
P00780	1.26e-29	157	395	131	354	Subtilisin Carlsberg OS=Bacillus licheniformis OX=1402 GN=subC PE=1 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
0.000269	0.999033	0.000179	0.000188	0.000167	0.000150

TMHMM  Annotations     

start	end
5	24