CAZyme Information: MGYG000001101_00303

Basic Information

• Species: HGM11523 sp900756545
• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA1381; HGM11523; HGM11523 sp900756545
• CAZyme ID: MGYG000001101_00303
• CAZy Family: CBM50
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
3224	MGYG000001101_5|CGC1	361203.47	4.4042

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001101	2035203	MAG	China	Asia

• Gene Location: Start: 6568; End: 16242 Strand: +

Full Sequence      

MKKKIIICLSVAMCMLLTIGFAAQNYLSAEEETISVMIRAKNNISAQTFSADAQEETAGE
ITVEDIAPSELGDLKENPNVFVEPNSKVVKSTLADNWYLDYDNISAVYDDLTVRGQNVKI
AVLDTGISGDGFSTAGGINILDTSGDYIDNNGHGSAMANIIHTIAPEAQLYSVKVLDETG
TGYYSDVISGINWAVENDMDIICMSFGSYEYSYFLEEAVNNAFCNNIAMIAAAGNDGNEN
IHYPAAYNQVLSVGACDKSGNIASFSNGGDKADVYAPGVDINTADHRHVKMQGKGTSVSA
AQTAGVAVLMKSAVSEYDVSKLYTVLKHAANQDENIPILNGYASMSKMNAFIENQDIYVP
TLDKNVVETENGRVAISYKYDAYDYQTVSVNDPVTVRAGFYSAHDYCDITVYKSTNTSNI
LYSTRYYDISGDAYLTFTCPQDILTSAGTYYIRYHGSENSSTQYDDIFTVYVEDIAPDKY
EPNDTFSAAYEIDRTGYRITANIGSAADKDYYKIYLNAGETIELELTNLPRDYDLALYNP
SKRQVEDSVNSGLRAETITYSAAKNGYHYIYIYSFEGMCSADTYRLNYSISVPKDEYEEH
KNYANITVDNNDTYDARNLLYFTNNITLTPTISYMGDVDWFQFTAPKGQVTITLEDMPYD
YDLYLYTDKNTQAAKSNNGGTNAESITYEISGDYQTLYIKVTGYDDYFSILPYTLTISYN
YIKTNTVQPEKNTAAVIWTTAFSGDSTVNYGTTSSVAQTKSSSAWTKNHSISLTGLSPAK
QYFYKVKTTGYTSSESETASFCTKDRYEDNNTLDSATPISWAGEIFNGTIHDSNDEDYYT
VSLDKTGIIYLTLEDIPADCDYDLWLADQDGNALAYSSNYGDVDEAIVYIAEPGTYYAVI
ECYRRYKGDAPYSFTYDFEPLNLNSAEVIDELHYGGDGVYSATGNYSKTFSDLNFTNTAY
DYYIGRTYNSKDQTNKHFGRGWIFSFEGKVNDLERTFEYSNGNIGTYTDENYKMVKLPDG
RVYIFEKQSNGTFQAQDSRATLVKNGTGYLFTAKDKSKYFFNDQGILTSMEDKYGNTMTI
TVNTDGKVQSFTDPTQNQYTVAYGENGYISDITETATGRNVSYQYTGDDLTTVVDAAGII
THYAYDTDHYLTAIKNDQEAALETLTYTAMENEPKKISTLTDMYGNNFSYTYESTENKTI
ITDSNGRTTAQSYDEKKFITSILDQAGRTKTIQYTLDEAGKNKYGEEAAITDENGNTFTY
IRDENGNITKETKPDGTYKDYFYDSNDNLIWERDSTGNFIRYEYDSKGIQMTKKARYLEK
VSENQVVELNSENYGLFAVEEYIYYPDAKAKIKGLLQKCINADGIATEYDYDGNGNPISV
KDPQTGLSTAYTYNTLNYKLTRTTPRGYTTQYMYDNAGNLVKETDTTDGAVRRIVYDVNG
RKTLEINPEQYDASADYLNAAENINSYSVSADGAAYEYYPNGLLKKETSPEGDVKAYTYD
LYGNVTTETLPSQYDVTGNRKLDCGQYIYEYDNLNRMTAKKYKETPDAESVLLESTVYSV
EQNTDTGEFYTVRSITKYYSPENSSATVYKSNYDDKTVFVGYDNGSTEHFSYYPDGELKS
YTDGNENTVHYRYDSFDNVKNVTYDEVWSPAEGGYSYARIDYSLNGDKAAEYKSADIVEL
YAVPENLYVKNYSYYANGLLKTEADTEGRKTEYEYDADGNTAKVSVYRDETNKNVTEFVN
NHKGHVITETKHVSTGTFYGDERTSLVTAYTYDLNGNKISVTAPDGAVTSYVYDKKNRLI
STSQFLTNEDGIIQNAVVEQQYNCNDEPYFRKDALGNTTRYVYDNRGFCIKEVDALGGTV
FNVRDYAGRITNTVKPRFYNASVDISEMNRTELVYNSRDWVIRQTEHYDDGTGEEEKDVT
VKEYTYDNNGNVLTETDALGNITRYTYTPSNHLKTRLDQETFDKGLEFSVKFSYNGMYQQ
VSEYNSAGVRIDTEYNTRGQVLRKTVISGADIAVLERNTYDGAGNRLSEMDANGNTTSYT
YNELNAVQNIVYPHDESIPENTVSKKYGLNSKAAYETDSLGKEILYSYDEAGRLVATTVQ
SANSSPLTVYTKYDLNGNKRREIDGAGNVTENTFDALNHITSMVKAGKSTSYTYDANGNL
VSTTDWLGNTTATEYDALDRVCAEYDAYGKAVSRKQYNANGVQISNTDALGAVTSYEYDK
NNRLVKTIDPNNNITLKSYDNLGNVASETDANGNVKYYTYDKLNNLTSVRQTVGGVEEAT
GYTYDNCGNLLSQTDGNGNVTEYEYNALNLVSRKIYPGGGENPHSQESYTYYADGTLAAF
TDRNGNTVSYTYDAAGRQLSQTASGLSVSSVYDGAGNKLVLADDTGNTERTYDAYGRAVS
KTQPRIGTFTYTYDVTTDVTEGEFAEITNDPHNNVTKKVFDKAGRLHFVYDNAALAAKYT
YYDNGALQKIEYGSGASEEYTYFSNGWLQTLVNKNSSGEVTDSYSYTYDANGNQTSKNEI
IGGINKGTTAYIYDEQNRLKSVLEPSGRQTVYTYDKAGNRLSETIIEEGSNIVTNYIYDN
QNRLIATLTIIDGAKIRYDYQYDYNGNLVSKTKTVTGGSEALQKMIGMTIAGETENGVSQ
YAEFYEYDALNRLVKAAIGGKTSCYAYNGEGLRVQKTMDGAVTDIGYDFDNPVIEQEGTE
YTVNLYGTNLVSRTAGGQKLYYQFNGHADVVALTDASGNVVASYYYDAFGVQTEQNGNAE
NPFRYGGYVYDEETGLYYIKSRFYDAAVARFIQEDVYTGDKKDPLSLNLYTYVVNNPLKY
LDPTGRIPNEIKINGKSIGYLKGYGTGVYGSMRDIVSAYGGYISRQDNVYYAQIGDVKLT
FNLKDAKIGQTYAFQAKGNKTKFDYNYFVLTEDVEQKGAVKILVNIESFVKVFSSNPNDM
QKIYWNLNTFFSDINQLEAAAKDYKKNKNHSYYAQLVLQQMRKHNYDGIMWDRVAGNIDE
GFTKYLKKNNKLYLSFMGDVVLYDFTTGGAVDLPHFAATLNALLYETHPTVLTGAPALGA
GRSEQDVDDLAGWAGDLQSAIRDLHDYENLYKVDATDYGAVYSIAKEFIGNRGQFSQPDM
LADVDAVNINAAMKYGHSLYATLRGYYRDTFNTNKVNKRYTAFINNQFHTTDKEKIRSYV
NHFVSDDSTGYIFNNFKRRDITNAERRALRDAFINYIYNINSGR

Enzyme Prediction     

No EC number prediction in MGYG000001101_00303.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07477	Peptidases_S8_Subtilisin_subset	4.38e-58	117	313	1	213	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	5.19e-46	114	313	26	240	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	2.10e-44	118	328	1	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.
cd07473	Peptidases_S8_Subtilisin_like	1.21e-41	116	320	2	248	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	3.18e-36	115	332	24	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ATW25298.1	8.88e-173	1025	2827	3	1798
ATW25288.1	1.18e-73	2437	2827	18	390
ATW25292.1	3.49e-64	2503	2827	16	323
ATW25294.1	3.60e-60	2356	2827	268	721
AKG34398.1	1.33e-43	2449	2825	1158	1480

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AF4_A	6.03e-38	114	330	22	253	CRYSTALSTRUCTURE OF SUBTILISIN CARLSBERG IN ANHYDROUS DIOXANE [Bacillus licheniformis],1BE6_A TRANS-CINNAMOYL-SUBTILISIN IN ANHYDROUS ACETONITRILE [Bacillus licheniformis],1BE8_A TRANS-CINNAMOYL-SUBTILISIN IN WATER [Bacillus licheniformis],1BFK_A Crystal Structure Of Subtilisin Carlsberg In 40% Acetonitrile [Bacillus licheniformis],1BFU_A SUBTILISIN CARLSBERG IN 20% DIOXANE [Bacillus licheniformis],1CSE_E THE HIGH-RESOLUTION X-RAY CRYSTAL STRUCTURE OF THE COMPLEX FORMED BETWEEN SUBTILISIN CARLSBERG AND EGLIN C, AN ELASTASE INHIBITOR FROM THE LEECH HIRUDO MEDICINALIS. STRUCTURAL ANALYSIS, SUBTILISIN STRUCTURE AND INTERFACE GEOMETRY [Bacillus subtilis],1OYV_A Chain A, Subtilisin Carlsberg [Bacillus licheniformis],1OYV_B Chain B, Subtilisin Carlsberg [Bacillus licheniformis],1R0R_E 1.1 Angstrom Resolution Structure of the Complex Between the Protein Inhibitor, OMTKY3, and the Serine Protease, Subtilisin Carlsberg [Bacillus licheniformis],1SBC_A The Refined Crystal Structure Of Subtilisin Carlsberg At 2.5 Angstroms Resolution [Bacillus subtilis],1SCA_A ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT [Bacillus licheniformis],1SCB_A ENZYME CRYSTAL STRUCTURE IN A NEAT ORGANIC SOLVENT [Bacillus licheniformis],1SCD_A X-RAY CRYSTAL STRUCTURE OF CROSS-LINKED SUBTILISM CARLSBERG IN WATER VS. ACETONITRILE [Bacillus licheniformis],2SEC_E STRUCTURAL COMPARISON OF TWO SERINE PROTEINASE-PROTEIN INHIBITOR COMPLEXES. EGLIN-C-SUBTILISIN CARLSBERG AND CI-2-SUBTILISIN NOVO [Bacillus licheniformis],2WUV_A Crystallographic analysis of counter-ion effects on subtilisin enzymatic action in acetonitrile [Bacillus licheniformis],2WUW_E Crystallographic analysis of counter-ion effects on subtilisin enzymatic action in acetonitrile (native data) [Bacillus licheniformis],4C3U_A Extensive counter-ion interactions with subtilisin in aqueous medium, Cs derivative [Bacillus licheniformis],4C3V_A Extensive counter-ion interactions with subtilisin in aqueous medium, no Cs soak [Bacillus licheniformis]
1YU6_A	6.19e-38	114	330	23	254	CrystalStructure of the Subtilisin Carlsberg:OMTKY3 Complex [Bacillus licheniformis],1YU6_B Crystal Structure of the Subtilisin Carlsberg:OMTKY3 Complex [Bacillus licheniformis]
1SCN_E	6.36e-38	114	330	22	253	INACTIVATIONOF SUBTILISIN CARLSBERG BY N-(TERT-BUTOXYCARBONYL-ALANYL-PROLYL-PHENYLALANYL)-O-BENZOL HYDROXYLAMINE: FORMATION OF COVALENT ENZYME-INHIBITOR LINKAGE IN THE FORM OF A CARBAMATE DERIVATIVE [Bacillus licheniformis]
1BH6_A	2.06e-37	114	330	22	253	SubtilisinDy In Complex With The Synthetic Inhibitor N- Benzyloxycarbonyl-Ala-Pro-Phe-Chloromethyl Ketone [Bacillus licheniformis]
1AV7_A	2.79e-37	114	330	22	253	SubtilisinCarlsberg L-Naphthyl-1-Acetamido Boronic Acid Inhibitor Complex [Bacillus licheniformis],1AVT_A Subtilisin Carlsberg D-Para-Chlorophenyl-1-Acetamido Boronic Acid Inhibitor Complex [Bacillus licheniformis],1SEL_A Crystal Structure Of Selenosubtilisin At 2.0-angstroms Resolution [Bacillus subtilis],1SEL_B Crystal Structure Of Selenosubtilisin At 2.0-angstroms Resolution [Bacillus subtilis],1VSB_A Subtilisin Carlsberg L-Para-Chlorophenyl-1-Acetamido Boronic Acid Inhibitor Complex [Bacillus licheniformis],3VSB_A Subtilisin Carlsberg D-Naphthyl-1-Acetamido Boronic Acid Inhibitor Complex [Bacillus licheniformis],6DWQ_A Subtilisin serine protease modified with the protease inhibitor cyanobenzylsulfonylfluoride [Bacillus licheniformis]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P41363	3.97e-43	21	317	17	327	Thermostable alkaline protease OS=Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) OX=272558 GN=BH0855 PE=1 SV=2
P16396	2.63e-39	17	311	19	340	Minor extracellular protease Epr OS=Bacillus subtilis (strain 168) OX=224308 GN=epr PE=2 SV=1
P00781	9.63e-36	114	330	22	253	Subtilisin DY OS=Bacillus licheniformis OX=1402 GN=apr PE=1 SV=1
P00780	1.98e-35	114	330	127	358	Subtilisin Carlsberg OS=Bacillus licheniformis OX=1402 GN=subC PE=1 SV=2
Q99405	6.76e-35	56	330	76	359	M-protease OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=aprE PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.745501	0.227201	0.025251	0.000502	0.000331	0.001219

TMHMM  Annotations     

start	end
5	27