CAZyme Information: MGYG000001163_01109

Basic Information

• Species: CAG-1427 sp900542265
• Lineage: Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Eggerthellaceae; CAG-1427; CAG-1427 sp900542265
• CAZyme ID: MGYG000001163_01109
• CAZy Family: CBM13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1061	MGYG000001163_17|CGC2	111266.76	5.3781

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001163	1959348	MAG	Austria	Europe

• Gene Location: Start: 35829; End: 39014 Strand: -

Full Sequence      

MEIRAPRLLNLVLSIILVSTLFLPTNIAYADSVSEADSNKVTFVGSDADSELEANEGDSE
LENALDDAVPDDAASDNTVIADNDSLEDNHAVLISEEEKAAALQELNTPEEELGYVPGEM
IVVYDETATEREMAEAASSIDAELDSAAGGISAGTVSLVTISEDMTVATAIEAIEKDNAV
VYAEPNYTVSLFDDDPVAFTQSNDAGYSNVRDYLNAISAEQAWNYLATQSISTTRIASID
TGAKVDHEDLKNVLNLTLSKEIVATGEGANRKTTFEKLQGDGLVNGKIHSTITSSSTHGT
HVAGIMAAQSNNGVGSAGVASGGSTKYSNKIVDLFAIDAFNGVSSDNKETANIYDVVSAM
QYAKNNKARVVNLSLGLFEDSSTLQTACKDLYTNNVVMVCAAGNYNSTQKVYPAAYDTTI
AVINCKNDGSRATYDSGAGGSTYGTWCDVAAPGYQIYSTTSSSTSAYGYLTGTSMAAPVV
SSAAAMMIAVNPSLTPSGVKTILTETARNTQKNEQTAWGMINAEKAVKEAVSNKTGTGQS
QIGASTDVSKAMITGVSASYTYTGSAVSPVPTVRIGTKTLVKNKDYTLTYSNNNRLGTAQ
VIVKGMGSYSGTKTVSFVIKAANAVDELAIKNKSVIANGIYSIKSLGSSVHVLDVSGGST
SNGANVQLYANNYSGAQKWRVTHDALGYITLTNVQSGKVLDVAGGKSTRGTNVQQYQSNG
SKAQKWIAVKSGSGFIVRSALNTNMVLDISGGKFANKSNVQIYTANNTNAQKFVFASIPQ
MADIKQGTYIISSALGNNQVLDISGARLTNGGNAQIYAFNGTAAQKWYVRPAGSGYYTLQ
NVNSGMYLGVNGSNVCQQPLQGDATKWVIIASGAKYVLSNAATGKVLDVSGAKKSSGTNV
QVYVSNSSAAQQWTFAATDLFTPGVYTVVTAVNPNYALDVSGASKANGAPITLYSRNGTA
AQKFRISKNSDGTYTFININSGKVIDIPGASKTNGKAIQQYTSNGTAAQHWKISIGSRGF
VLTSPLGKTLDVSGAKAYNKAKVQTYSPNGTLAQCWLLVKS

Enzyme Prediction     

No EC number prediction in MGYG000001163_01109.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM13	876	1013	1.3e-27	0.6702127659574468
CBM13	638	776	6e-26	0.6914893617021277
CBM13	743	869	9.5e-19	0.6329787234042553

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07484	Peptidases_S8_Thermitase_like	1.33e-36	203	508	3	257	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	1.54e-36	235	506	3	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	7.01e-31	236	508	6	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.
cd07496	Peptidases_S8_13	3.62e-30	236	506	4	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.
pfam00082	Peptidase_S8	2.79e-27	236	513	6	278	Subtilase family. Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see pfam00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAK44097.1	2.17e-47	154	982	160	1064
BAK44091.1	6.90e-29	784	983	596	802
QRT49576.1	7.14e-29	635	983	580	928
QRT50581.1	8.79e-27	783	983	125	341
QRT49575.1	1.54e-26	784	981	583	784

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1THM_A	4.27e-26	203	528	4	278	CRYSTALSTRUCTURE OF THERMITASE AT 1.4 ANGSTROMS RESOLUTION [Thermoactinomyces vulgaris]
1BH6_A	2.37e-25	244	528	12	274	SubtilisinDy In Complex With The Synthetic Inhibitor N- Benzyloxycarbonyl-Ala-Pro-Phe-Chloromethyl Ketone [Bacillus licheniformis]
1C3L_A	3.22e-25	232	528	24	274	Subtilisin-CarlsbergComplexed With Xenon (8 Bar) [Bacillus licheniformis],3UNX_A Bond length analysis of asp, glu and his residues in subtilisin Carlsberg at 1.26A resolution [Bacillus licheniformis]
3QTL_A	3.22e-25	232	528	24	274	StructuralBasis for Dual-inhibition Mechanism of a Non-classical Kazal-type Serine Protease Inhibitor from Horseshoe Crab in Complex with Subtilisin [Bacillus licheniformis],3QTL_B Structural Basis for Dual-inhibition Mechanism of a Non-classical Kazal-type Serine Protease Inhibitor from Horseshoe Crab in Complex with Subtilisin [Bacillus licheniformis],3QTL_C Structural Basis for Dual-inhibition Mechanism of a Non-classical Kazal-type Serine Protease Inhibitor from Horseshoe Crab in Complex with Subtilisin [Bacillus licheniformis],4HX2_A Crystal structure of Streptomyces caespitosus sermetstatin in complex with Bacillus licheniformis subtilisin [Bacillus licheniformis],4HX2_C Crystal structure of Streptomyces caespitosus sermetstatin in complex with Bacillus licheniformis subtilisin [Bacillus licheniformis]
4GI3_A	3.29e-25	232	528	25	275	Crystalstructure of Greglin in complex with subtilisin [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q45670	1.45e-29	98	487	31	360	Thermophilic serine proteinase OS=Bacillus sp. (strain AK1) OX=268807 PE=1 SV=1
P00781	5.22e-25	244	528	12	274	Subtilisin DY OS=Bacillus licheniformis OX=1402 GN=apr PE=1 SV=1
P00780	1.21e-23	232	528	129	379	Subtilisin Carlsberg OS=Bacillus licheniformis OX=1402 GN=subC PE=1 SV=2
P04072	3.01e-23	203	528	4	278	Thermitase OS=Thermoactinomyces vulgaris OX=2026 PE=1 SV=1
I3R794	1.36e-22	171	507	95	379	Halolysin OS=Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) OX=523841 GN=hly 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
0.000329	0.998905	0.000211	0.000193	0.000187	0.000166

TMHMM  Annotations     

start	end
7	29