CAZyme Information: MGYG000001712_03730

Basic Information

• Species: Bacillus_A thuringiensis_S
• Lineage: Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae_G; Bacillus_A; Bacillus_A thuringiensis_S
• CAZyme ID: MGYG000001712_03730
• CAZy Family: CBM13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
613		67810.73	4.9288

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001712	5736823	Isolate	United States	North America

• Gene Location: Start: 3693117; End: 3694958 Strand: -

Full Sequence      

MKIFQKMYASTVIITTLLGTGGTINSVHADSIEQQSKLGIEQETDKQIIVKFKADLDFPY
EDGIEKQIQSQTNDKVIKDLLTEYPDVTFTRLFTSVSPEQIQNLEVKAPNHVSTSLLNYY
ILQNQNSGYEEEIVDKLKASSLIEDAYMKKQEKIMPPEVQSSSVALNPNKNPRFKKQGYL
EAAPYGINAPFAWGVQGGNGNGITFVDMEYGWLLNHEDLLHQNIELMSGRNINQHVGHGT
SVLGIVSSEDNEVGNIGIAPKAKAKVISQIRDNGQYNTADAILSAVNQLEAGDVLLLEAQ
ASFDGYGDKYLPVEVQPDIFDAIRAGTDKGIVIIEAGANGWNDLDQFKDRKGKQVLNRNS
KDFKDSGAIMVGAGSSSFPHERMWFSNYGSRIDVYGWGENVDTTTAEQSRSAVNLYTSSF
SGTSSASPIIAGAATLVQSIAKENLGQPYRPSELRAILSNQSTGTKSKDPYADKIGVLPD
LKSILVNLGYEQRKLNGGNELQVTENEPNNEPRQANKVNFHTPVKGTLHNSDRVDVFTFQ
IDSPENINISLLNEQNIGMTWVLHHESDLNNYVAYGENEGNVVKGTYNAKPGKYYLYVYK
YENKDGSYVLNIK

Enzyme Prediction     

No EC number prediction in MGYG000001712_03730.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04843	Peptidases_S8_11	1.14e-115	186	463	1	277	Peptidase S8 family domain, uncharacterized subfamily 11. 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	2.80e-11	168	460	2	254	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	4.12e-11	211	460	9	240	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.
cd07477	Peptidases_S8_Subtilisin_subset	1.43e-10	211	458	10	226	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	7.84e-10	200	439	40	240	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QWH75751.1	1.27e-217	1	490	1	500
QWG59428.1	1.79e-217	1	490	1	500
QWG76020.1	1.79e-217	1	490	1	500
QWG81795.1	1.79e-217	1	490	1	500
QEL88395.1	1.79e-217	1	490	1	500

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5SV5_A	1.13e-37	509	613	1	105	1.0Angstrom Crystal Structure of pre-Peptidase C-terminal Domain of Collagenase from Bacillus anthracis. [Bacillus anthracis]
4HPK_B	1.70e-18	498	612	3	116	ChainB, Collagenase [Hathewaya histolytica]
1NQJ_A	1.74e-18	498	612	4	117	ChainA, class 1 collagenase [Hathewaya histolytica],1NQJ_B Chain B, class 1 collagenase [Hathewaya histolytica]
1NQD_A	1.89e-18	498	612	7	120	ChainA, class 1 collagenase [Hathewaya histolytica],1NQD_B Chain B, class 1 collagenase [Hathewaya histolytica],2O8O_A Chain A, Collagenase [Hathewaya histolytica],2O8O_B Chain B, Collagenase [Hathewaya histolytica]
4HPK_A	5.13e-18	502	612	1	111	ChainA, Collagenase [Hathewaya histolytica]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q899Y1	6.56e-21	502	608	880	986	Collagenase ColT OS=Clostridium tetani (strain Massachusetts / E88) OX=212717 GN=colT PE=1 SV=1
P43153	3.74e-20	503	613	864	976	Collagenase ColA OS=Clostridium perfringens (strain 13 / Type A) OX=195102 GN=colA PE=1 SV=2
Q9X721	1.90e-15	487	612	992	1116	Collagenase ColG OS=Hathewaya histolytica OX=1498 GN=colG PE=1 SV=1
P29139	2.40e-10	187	458	29	278	Intracellular serine protease OS=Paenibacillus polymyxa OX=1406 GN=isp PE=1 SV=1
P29599	1.47e-09	181	471	2	257	Subtilisin BL OS=Lederbergia lentus OX=1467 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
0.000280	0.999002	0.000212	0.000184	0.000157	0.000132

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001712_03730.