CAZyme Information: MGYG000001700_02654

Basic Information

• Species: Citrobacter_A sedlakii
• Lineage: Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Citrobacter_A; Citrobacter_A sedlakii
• CAZyme ID: MGYG000001700_02654
• CAZy Family: CBM5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
683		72780	6.3984

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000001700	4631466	Isolate	not provided	not provided

• Gene Location: Start: 114808; End: 116859 Strand: -

Full Sequence      

MKKSILSMLICAAVTCAAYAQTGTALQHVHQAQEVQEGVSYDAIVVKLKPGKSQTSPLKL
DDPALVATRMYHADNLSRERAAEIAELNARYGFDRYLRIELPENKKQDRNYIEHVINTIQ
QNQDVETVYPEAMPVGFQAEKQEAGQSSTLLKSTVNSGLSAVSVPDYRQQQDYLKAPDDK
RSGYYIGGVNRDSVNQYIGNEGEDITIVSSENCGWNANHVNLPPASFVQGPNKDTCNERE
HNTASVGILAARDIGSGVRGLSYKSKVGYAAWPASNLFNVIPLLKAGDVVSLNMQTYGGE
ITGTCKSACYIPIEYLDSYFNVIKALTDKGVFVITSAGNGNINLDSPAFNGRWDTQVRDS
GAIIAGAFCSKDGKKANFSTYGSRVTSSSRGCSDVTTTGYGNLYNRTNANYTGSFGGTSS
ATPIVAGVVASLSGIAKANGITVTPRQMRQILAETGTPIANGDSAKVGTQPDMARAVARI
LALKNGSDIPAIPAPTAAAGADYTMVSPTTGVSTYPLDGSKSLNATSYNWSVTKGVGTFF
LEEKLNGVQVNSIDNAHAYAVIPANTEGQATFTLTTTGADGRTAQDSMTIMVSKPATPAK
EDTPTKDDTPANDDAPANDDVPATNTAPAYNGKIAYPTKCTKVSYNGKIWFNQWYVNPGQ
ETPGTGGQWGAWREQGTSNNSCK

Enzyme Prediction     

No EC number prediction in MGYG000001700_02654.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd04843	Peptidases_S8_11	9.69e-71	198	457	11	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	1.07e-14	231	455	32	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.
cd00306	Peptidases_S8_S53	5.25e-13	210	455	15	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.
cd04077	Peptidases_S8_PCSK9_ProteinaseK_like	7.03e-13	318	458	134	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.
cd04059	Peptidases_S8_Protein_convertases_Kexins_Furin-like	2.39e-11	237	455	82	295	Peptidase S8 family domain in Protein convertases. Protein convertases, whose members include furins and kexins, are members of the peptidase S8 or Subtilase clan of proteases. They have an Asp/His/Ser catalytic triad that is not homologous to trypsin. Kexins are involved in the activation of peptide hormones, growth factors, and viral proteins. Furin cleaves cell surface vasoactive peptides and proteins involved in cardiovascular tissue remodeling in the TGN, at cell surface, or in endosomes but rarely in the ER. Furin also plays a key role in blood pressure regulation though the activation of transforming growth factor (TGF)-beta. High specificity is seen for cleavage after dibasic (Lys-Arg or Arg-Arg) or multiple basic residues in protein convertases. There is also strong sequence conservation.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUC29609.1	0.0	1	683	1	683
BBT92306.1	0.0	1	683	1	681
QWC66401.1	0.0	1	683	1	681
QXM21696.1	0.0	1	683	1	681
QIK15526.1	0.0	1	683	1	649

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3TI9_A	1.75e-06	241	455	105	313	Crystalstructure of the basic protease BprB from the ovine footrot pathogen, Dichelobacter nodosus [Dichelobacter nodosus]
3TI7_A	5.41e-06	241	455	105	313	Crystalstructure of the basic protease BprV from the ovine footrot pathogen, Dichelobacter nodosus [Dichelobacter nodosus VCS1703A]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P23314	4.78e-06	241	486	237	471	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

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
0.001178	0.833721	0.164212	0.000318	0.000278	0.000258

TMHMM  Annotations     

There is no transmembrane helices in MGYG000001700_02654.