CAZyme Information: KAG6615961.1

Basic Information

• Species: Phytophthora cinnamomi
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
• CAZyme ID: KAG6615961.1
• CAZy Family: GT2
• CAZyme Description: putative serine protease family S08A

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
912	JAFJYM010000023|CGC2	100924.80	5.2571

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcinnamomiGKB4	19981	N/A	0	19981

• Gene Location: location=JAFJYM010000023:679317-682823(-)

Full Sequence      

MSRIHLALFLASLSLALGLIRGLNDRVLLVHLHPPLDARSLALSPALGASQRRRLVFQSF
SRAVDGAQRSVASFIEAQSVGDAVVSRLWLQNTLVVRYNDNNTDLKTFFFSDKGLRGLPG
VLQVEEDAPVLRLIGAQREEDFGEQRGGEEPQSNVKLLHAPQLWALGAKGKGVVVASIDS
GVRYTHEALRDTFRGTKQDGTVDFDYSFWFTPGTDMSKETPDTADEVGHGTHTMGTAVGG
KGVGVAPEATWITARAFDIWGAANKSDFLLAAQWVLCPTKMDGTGADCSLGADVVTNSFG
VDRSTPAYPQWTWLSKVIDTWRAAGVYPVFASGNTNGFLCGSVYYPGSHEDTIAVGALIG
GSSLWGASGKGPSLEEDFGESVTATSGKYVIKPDFVAPGVGIRSAMSVKDGAYTRLTGTS
MATPHVAGAIALLLSLYNSSEESSLVKPPEYEKVLQSLTETTTRKLHKPFLVPSECGNTT
YQEYPNNIYVLLCDAIPSEEKKRLNYQAIVCRETFGADWANPFVYLPPLQLTVQALKAPH
PVDSQLDVTMGEDWAYMESLRPPVYICLRRKVDRAGYEPMPLDGRVDKEDWAHVPWSDAF
VDIEGSQRKPKEHPFTRFKMMYDDDTLYVGAELIEPKIWGTITEKNSTMYHENDFEVFFN
PDGSRHHYYELEVNCLNTIWELLLHRPYKDGYSIENPFNLVSLRSAVFVDGLTNSPETES
VRWCIEMSWSLAELQQFDKLRSRGKVGEPPSATGLPSGRATPRPPSSSGQTSRPAVTSTS
TVAGDVWRVNFSRVQYELETVVNVDTQQLQYQKVPDKREDNIVWAPTGVIDIHRPERWGF
VFFSSENELPGGEMELSSAMTGFLEERMAIERILDAVYYRQRAFHAFHGGFASTMEMLYT
ATEKLAGTTPPR

Enzyme Prediction     

No EC number prediction in KAG6615961.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM9	583	735	2.6e-26	0.7307692307692307

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173807	Peptidases_S8_BacillopeptidaseF-like	8.13e-77	170	435	1	243	Peptidase S8 family domain in BacillopeptidaseF-like proteins. Bacillus subtilis produces and secretes proteases and other types of exoenzymes at the end of the exponential phase of growth. The ones that make up this group is known as bacillopeptidase F, encoded by bpr, a serine protease with high esterolytic activity which is inhibited by PMSF. Like other members of the peptidases S8 family these have a 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 these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity.
187678	CBM9_like_3	9.30e-59	582	840	1	200	DOMON-like type 9 carbohydrate binding module. Family 9 carbohydrate-binding modules (CBM9) play a role in the microbial degradation of cellulose and hemicellulose (materials found in plants). The domain has previously been called cellulose-binding domain. The polysaccharide binding sites of CBMs with available 3D structure have been found to be either flat surfaces with interactions formed by predominantly aromatic residues (tryptophan and tyrosine), or extended shallow grooves. CBM9 domains found in this uncharacterized heterogeneous subfamily may co-occur with various other domains.
173787	Peptidases_S8_S53	1.58e-44	173	439	1	228	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.
173812	Peptidases_S8_1	5.09e-44	170	435	1	245	Peptidase S8 family domain, uncharacterized subfamily 1. 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.
173803	Peptidases_S8_Subtilisin_subset	3.26e-41	172	439	1	216	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UOK64684.1|CBM0	3.02e-67	562	898	15	297
QOT09656.1|CBM0	4.16e-66	562	898	15	298
QLG42346.1|CBM0	1.96e-64	562	898	15	297
UPK45153.1|CBM9	2.71e-64	562	898	15	297
QZN78207.1|CBM9	9.86e-64	562	898	15	297

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2ZWO_A	5.48e-20	115	437	51	341	Chain A, Tk-subtilisin [Thermococcus kodakarensis],2ZWO_B Chain B, Tk-subtilisin [Thermococcus kodakarensis],2ZWO_C Chain C, Tk-subtilisin [Thermococcus kodakarensis]
2Z2Z_A	1.27e-19	115	437	48	338	Chain A, Tk-subtilisin precursor [Thermococcus kodakarensis KOD1]
4JP8_A	1.31e-19	115	437	51	341	Crystal structure of Pro-F17H/S324A [Thermococcus kodakarensis KOD1]
3WIU_A	1.31e-19	115	437	51	341	Crystal structure of Pro-S324A/L349A [Thermococcus kodakarensis KOD1],3WIU_B Crystal structure of Pro-S324A/L349A [Thermococcus kodakarensis KOD1],3WIU_C Crystal structure of Pro-S324A/L349A [Thermococcus kodakarensis KOD1]
3WIV_A	1.31e-19	115	437	51	341	Crystal structure of Pro-S324A/D356A [Thermococcus kodakarensis KOD1],3WIV_B Crystal structure of Pro-S324A/D356A [Thermococcus kodakarensis KOD1],3WIV_C Crystal structure of Pro-S324A/D356A [Thermococcus kodakarensis KOD1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P16397|SUBF_BACSU	2.24e-36	38	489	90	501	Bacillopeptidase F OS=Bacillus subtilis (strain 168) OX=224308 GN=bpr PE=1 SV=2
sp|P11018|ISP1_BACSU	1.77e-19	150	461	21	284	Major intracellular serine protease OS=Bacillus subtilis (strain 168) OX=224308 GN=isp PE=1 SV=2
sp|P58502|TKSU_THEKO	3.60e-19	115	437	75	365	Tk-subtilisin OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1675 PE=1 SV=1
sp|P29139|ISP_PAEPO	1.27e-17	144	456	16	280	Intracellular serine protease OS=Paenibacillus polymyxa OX=1406 GN=isp PE=1 SV=1
sp|P00782|SUBT_BACAM	1.89e-17	139	470	99	368	Subtilisin BPN' OS=Bacillus amyloliquefaciens OX=1390 GN=apr PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.938578	0.061428

TMHMM  Annotations     

There is no transmembrane helices in KAG6615961.1.