CAZyme Information: MGYG000002490_03292

Basic Information

• Species: Paenibacillus_B thiaminolyticus
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus_B; Paenibacillus_B thiaminolyticus
• CAZyme ID: MGYG000002490_03292
• CAZy Family: CBM5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
434	MGYG000002490_30|CGC2	45498.59	4.2816

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002490	6537383	Isolate	Japan	Asia

• Gene Location: Start: 56561; End: 57865 Strand: +

Full Sequence      

MKKFLSSVLAAILLMATLVTGVAFGSPDQGYSGDYIEGQLVVSVEEPFMDSIQSVDELLM
EAESLTESGFTIADSLFGQDAGSFSVQSLDSDVRATAIEKMGLVYLVEYSVEDYNSIDSA
KITLEETLDNLGFNVRYVTENRKMYALETATVQDVSPQDIHNNQRWHYDMIKVPQAWEIT
TGSSSVRIGVLDTGIDSNHPNLKNLVNTSLGSSFVGGTTNDGNGHGTHVAGTIASYGSVS
GVMQNATLIPIKVLNDSGSGSLYGVQQGIVYAANVRADVINMSLGGGGYDQGMDEAIQTA
VGLGTIVVAAAGNDGLPKISYPAAYSGSIAVGSVTSSRTRSSFSNYGPGLDVMAPGSNIY
STYKNGQYATLSGTSMSTPHVTGVLGLMRSVNPNLTSAEAEEILKNTAQPAGSSDQYGHG
IVDAHAAVLAASQR

Enzyme Prediction     

No EC number prediction in MGYG000002490_03292.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07484	Peptidases_S8_Thermitase_like	2.14e-90	157	412	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.
cd07477	Peptidases_S8_Subtilisin_subset	2.43e-74	186	407	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.
cd07473	Peptidases_S8_Subtilisin_like	2.18e-64	183	408	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	3.93e-60	180	410	21	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.
cd00306	Peptidases_S8_S53	1.31e-56	186	407	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	5.19e-273	1	432	1	432
ATX75767.1	1.37e-51	84	434	105	490
QCD67055.1	1.36e-48	135	432	60	360
QFR21865.1	1.36e-48	135	432	60	360
ACV48841.1	2.69e-48	135	432	114	414

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AH2_A	8.18e-65	166	427	6	267	ChainA, SERINE PROTEASE PB92 [Alkalihalobacillus alcalophilus]
1GCI_A	4.54e-64	166	427	6	267	ChainA, SUBTILISIN [Lederbergia lenta],1JEA_A Chain A, Subtilisin [Lederbergia lenta],1NDQ_A Chain A, Subtilisin Savinase [Lederbergia lenta],1SVN_A Chain A, Savinase (tm) [Lederbergia lenta],1TK2_A Chain A, Subtilisin Savinase [Lederbergia lenta],3BX1_A Chain A, Subtilisin Savinase [Lederbergia lenta],3BX1_B Chain B, Subtilisin Savinase [Lederbergia lenta],4CFY_A Chain A, Subtilisin Savinase [Lederbergia lenta],4CFZ_A Chain A, SUBTILISIN SAVINASE [Lederbergia lenta],4CG0_A Chain A, Subtilisin Savinase [Lederbergia lenta],5AQE_A Chain A, SUBTILISIN SAVINASE [Lederbergia lenta],6Y5S_A Chain A, Subtilisin Savinase [Lederbergia lenta],6Y5T_A Chain A, Subtilisin Savinase [Lederbergia lenta]
1IAV_A	4.54e-64	166	427	6	267	ChainA, SUBTILISIN SAVINASE [Lederbergia lenta]
1MPT_A	4.54e-64	166	427	6	267	ChainA, M-PROTEASE [Alkalihalobacillus clausii KSM-K16],1WSD_A Chain A, M-protease [Alkalihalobacillus clausii KSM-K16]
1NDU_A	1.27e-63	166	427	6	267	ChainA, Subtilisin Savinase [Lederbergia lenta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P29600	2.48e-63	166	427	6	267	Subtilisin Savinase OS=Lederbergia lentus OX=1467 PE=1 SV=1
P27693	1.08e-62	166	427	117	378	Alkaline protease OS=Alkalihalobacillus alcalophilus OX=1445 PE=1 SV=1
Q99405	5.93e-62	166	427	117	378	M-protease OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=aprE PE=1 SV=2
P41362	5.93e-62	166	427	117	378	Alkaline protease OS=Alkalihalobacillus clausii OX=79880 PE=1 SV=1
P29599	7.64e-62	166	427	6	267	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
0.000368	0.998954	0.000196	0.000165	0.000153	0.000153

TMHMM  Annotations     

start	end
5	27