CAZyme Information: MGYG000001536_00885

Basic Information

• Species: Enterobacter_A timonensis
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Enterobacter_A; Enterobacter_A timonensis
• CAZyme ID: MGYG000001536_00885
• CAZy Family: CBM5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
656	MGYG000001536_10|CGC3	70005.43	6.812

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001536	4199690	Isolate	not provided	not provided

• Gene Location: Start: 413222; End: 415192 Strand: +

Full Sequence      

MKKSLLSLLICATVSCSAYAETLTHVEYAHDGITYDAIVVKLKPVKPLLKSTGGTTANTL
TLSEPSLVPSTMFRPTLLRGSEASEMAQLNTRYGFDRYLRITLPEGRSQDKDYINQVIAE
IEQKPNVETVYPESLPVSLEEYRHSDSFAPPKLKSTINQNLGAAAVPDFRHLQDYLKSPT
EKRQGYFLGGVNRDSVNQYAGNDGAGVTIVSEENCAWNPAHINLPPIAFSQGNKQWQSCG
NHDSASVGIMAARDIGAGVKGLAWNTRVGFASWQVNNLYNTIPLLKAGDVLQMGMQTGGG
EVTGCKSECYMPQESAQAYYDLIKALTDKGVYVIEAAGNGNINLDNPVFNGKFDVNVRDS
GAILAGAACAKEGKRAYFSTYGSRVTSASWGCWDVVSTGYGDLWQNGVNNYTNTFAGTSS
ANPIIAGVVASLSGIAKANGITVTPLQMRQILQETGTPLAGNESAKIGTQPDMERAVAKI
MALKDGDSTAPAPTAEAGADKSMVSSANSVTTWPLDGSKSLNVKSFSWRISKGGDKFGLQ
AKQNGALVESVEAPQAWAVIPANAEGDVTYTLTTTGADGRTAQDSVTLHVSKPNAPATDV
PAYSARTVYSKNCTKVAYGGKIWQNQWYVNSGQETPGTGGQWGAWREVGASNNSCR

Enzyme Prediction     

No EC number prediction in MGYG000001536_00885.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04843	Peptidases_S8_11	1.36e-69	190	457	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.
cd07498	Peptidases_S8_15	3.26e-11	219	455	19	242	Peptidase S8 family domain, uncharacterized subfamily 15. 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	1.12e-10	317	458	133	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	2.60e-10	232	455	36	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.
cd07473	Peptidases_S8_Subtilisin_like	3.61e-10	248	457	71	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QDK17979.1	0.0	1	656	1	659
QGU16820.1	0.0	1	656	1	659
QCZ26615.1	0.0	1	656	1	660
AFM61610.1	0.0	1	656	1	670
QFQ10755.1	5.62e-307	1	656	1	674

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3TI7_A	9.41e-07	242	469	105	327	Crystalstructure of the basic protease BprV from the ovine footrot pathogen, Dichelobacter nodosus [Dichelobacter nodosus VCS1703A]
3TI9_A	1.25e-06	242	469	105	327	Crystalstructure of the basic protease BprB from the ovine footrot pathogen, Dichelobacter nodosus [Dichelobacter nodosus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P42780	1.67e-07	225	487	225	475	Extracellular subtilisin-like protease OS=Dichelobacter nodosus OX=870 PE=3 SV=1
P42779	7.99e-06	242	469	237	459	Extracellular basic protease OS=Dichelobacter nodosus OX=870 GN=bprV 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
0.000758	0.598640	0.399901	0.000245	0.000228	0.000206

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001536_00885.