CAZyme Information: MGYG000001269_00319

Basic Information

• Species: Rothia mucilaginosa
• Lineage: Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Rothia; Rothia mucilaginosa
• CAZyme ID: MGYG000001269_00319
• CAZy Family: CBM13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
531	MGYG000001269_5|CGC2	55580.71	9.2524

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001269	2178797	MAG	Italy	Europe

• Gene Location: Start: 40158; End: 41753 Strand: -

Full Sequence      

MQSIDELLNIKTSYVRSTALDASVVTTSAELTPAQAQQYMNALSANSKVASVSPDMRRYA
TVDNTAETVKINDPKMNRMWSLTGEKGVSALEAWGTTRGKGVTVAVLDSGITAHPDLDAN
VLPGYDFIAESAFSNDGNGRDSDPTDAGNWTVDNQCFTGSKATASDWHGTHVAGTIAAIA
NNNEGIAGVAPEAKIVPVRVLGACGGFDSDITDGIIWAAGGSVRGVPANQNPAQVINMSI
GSEGTCTTPYRQAIAQANKRGSIVVVAAGNNNFDASKSSPGNCEDVINVGATDKNGKRSY
FSNYGSRVDVSAPGGDRRYWGGGILSTLNAGKTAPGKADYAEYQGTSMAAPHVAGIVALM
KAVDPKLTYAQAKKALQSTSQGVECDQSACGSGIVNAARAVQQVRSDREAADAAAAEAAR
KKAEEEAARKKAAEEAARKKAEEDAKRQQAPAPKVTPAPKVTPAPKVTPAPKASRPVTRP
SRPVTRPSYPSRPRHGHTSRYRSWYGASVNTYPSNTYPSSGYLGFATGNHR

Enzyme Prediction     

No EC number prediction in MGYG000001269_00319.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd07496	Peptidases_S8_13	8.94e-124	101	379	1	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.
cd07484	Peptidases_S8_Thermitase_like	3.15e-73	72	381	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	2.80e-67	101	379	1	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	1.82e-66	100	380	2	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.
pfam00082	Peptidase_S8	6.53e-62	99	381	1	273	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
AIY26234.1	3.22e-107	72	406	129	468
QZY84418.1	5.53e-104	15	376	104	450
CAG23448.1	3.41e-100	72	402	130	465
ALN86161.1	1.46e-99	15	406	94	479
ATE72186.1	2.05e-99	15	406	94	479

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5YL7_A	5.71e-110	72	398	4	332	Proteasesfrom Pseudoalteromonas arctica PAMC 21717 (Pro21717) [Pseudoalteromonas arctica]
3LPC_A	4.48e-92	72	404	3	338	Crystalstructure of a subtilisin-like protease [Dichelobacter nodosus]
3LPA_A	4.48e-92	72	404	3	338	Crystalstructure of a subtilisin-like protease [Dichelobacter nodosus VCS1703A]
3TI7_A	2.59e-91	72	408	4	343	Crystalstructure of the basic protease BprV from the ovine footrot pathogen, Dichelobacter nodosus [Dichelobacter nodosus VCS1703A]
3TI9_A	2.59e-91	72	408	4	343	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
P23314	2.47e-107	15	401	90	465	Extracellular protease OS=Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25) OX=190485 GN=XCC0851 PE=3 SV=1
P42780	1.30e-92	14	404	83	471	Extracellular subtilisin-like protease OS=Dichelobacter nodosus OX=870 PE=3 SV=1
P42779	9.45e-91	1	411	72	478	Extracellular basic protease OS=Dichelobacter nodosus OX=870 GN=bprV PE=1 SV=1
Q99405	6.79e-42	99	402	134	380	M-protease OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=aprE PE=1 SV=2
P29600	1.70e-41	99	402	23	269	Subtilisin Savinase OS=Lederbergia lentus OX=1467 PE=1 SV=1

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
1.000040	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001269_00319.