CAZyme Information: SPRG_21856-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_21856-t26_1-p1
• CAZy Family: GT60
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
663		71407.45	6.4986

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SparasiticaCBS223-65	20435	695850	314	20121

• Gene Location: location=KK583637:4733-6979(-)

Full Sequence      

MKAFLILATAAATVSAKVASSVLRQLEVDGKSDVFVRFADPSAALEAATLENKPLERQEV
FDILSEVTTTGHKSIEAVTAGYKVTPTWLVTGAFIDGADKDLIAKLSLNKAIKSVEHLPD
IELEPLLTKEIDAPAANITNQWGVNTVGAPEVWKNFNGKGVVIGSIDTGARHTHNLIKDS
WRADRGWYDPYNQTALPEDLGGHGTHTIGTMTGKDGYGVAPGAQWIACRGLYIKSGSSQA
LMQCLQFMMCPTRTDGTHPDCSKGAHVINNSWGSAKFNPVYEEAVAALRKAGITPVFSNG
NSGPACGTTGNPGTYPNVISVGAIGSYTDEPTKLAFFSSKGPGTYIDAHNVQQTIVKPTI
SAPGFFTLSAYNTGDSAVKYMAGTSMAAPHVAGVVALLKSAKIDLTYEEIYAYLTQTADQ
KMLEGEPKEWVVPNNKNGTDIYPGAPNCGGVDDTKWPNNRYGYGRVNVANILKDGKFVSI
STPAPTTKAPAPEPVGAKFCTYKKTVLSEWNNQLFIDTIKNNKNEGFVIDLKYNIIQSAS
SEDGCLSLIKDATNTNSVALAKCTGDATQIWKFDTVAKRIVHPHNGECLDAFRDGDKFGL
HTYACDATNANQKWLIDAAGHKIKHATHNNLCLDVDPTNPTHAAQVWECHDWNTNQWIDA
VAY

Enzyme Prediction     

No EC number prediction in SPRG_21856-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM13	537	657	3e-17	0.6436170212765957

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173807	Peptidases_S8_BacillopeptidaseF-like	6.20e-94	158	419	1	264	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.
173800	Peptidases_S8_subtilisin_Vpr-like	1.91e-44	158	431	1	282	Peptidase S8 family domain in Vpr-like proteins. The maturation of the peptide antibiotic (lantibiotic) subtilin in Bacillus subtilis ATCC 6633 includes posttranslational modifications of the propeptide and proteolytic cleavage of the leader peptide. Vpr was identified as one of the proteases, along with WprA, that are capable of processing subtilin. Asp, Ser, His triadPeptidases S8 or Subtilases are a 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	3.80e-42	160	417	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.
395035	Peptidase_S8	7.37e-42	158	419	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.
173790	Peptidases_S8_PCSK9_ProteinaseK_like	5.65e-40	158	418	24	253	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
AIG56170.1|CBM13	0.0	1	663	1	745
AIG56438.1|CBM13	0.0	1	663	1	748
AIG56171.1|CBM13	2.04e-250	1	663	1	751
AIG56439.1|CBM13	6.01e-249	9	663	8	748
SCG17872.1|CBM57	1.91e-56	14	467	41	471

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3AFG_A	1.67e-22	59	419	53	393	Chain A, Subtilisin-like serine protease [Thermococcus kodakarensis],3AFG_B Chain B, Subtilisin-like serine protease [Thermococcus kodakarensis]
1WMD_A	1.45e-20	158	399	21	269	Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.30 angstrom, 100 K) [Bacillus sp. KSM-KP43],1WME_A Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.50 angstrom, 293 K) [Bacillus sp. KSM-KP43]
5FAX_A	4.58e-20	158	399	21	268	Chain A, Subtilase SubHal from Bacillus halmapalus [Sutcliffiella halmapala],5FAX_B Chain B, Subtilase SubHal from Bacillus halmapalus [Sutcliffiella halmapala],5FBZ_A Chain A, Enzyme subtilase SubHal from Bacillus halmapalus [Sutcliffiella halmapala],5FBZ_C Chain C, Enzyme subtilase SubHal from Bacillus halmapalus [Sutcliffiella halmapala]
1MPT_A	1.41e-19	142	418	6	248	Chain A, M-PROTEASE [Alkalihalobacillus clausii KSM-K16],1WSD_A Chain A, M-protease [Alkalihalobacillus clausii KSM-K16]
2IXT_A	2.08e-19	142	425	8	290	SPHERICASE [Lysinibacillus sphaericus],2IXT_B SPHERICASE [Lysinibacillus sphaericus],3D43_A The crystal structure of Sph at 0.8A [Lysinibacillus sphaericus],3D43_B The crystal structure of Sph at 0.8A [Lysinibacillus sphaericus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P16397|SUBF_BACSU	1.62e-38	141	419	200	486	Bacillopeptidase F OS=Bacillus subtilis (strain 168) OX=224308 GN=bpr PE=1 SV=2
sp|Q5JIZ5|TKSP_THEKO	5.80e-22	59	419	76	416	Subtilisin-like serine protease OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1689 PE=1 SV=1
sp|Q99405|PRTM_ALKCK	1.40e-19	114	418	86	359	M-protease OS=Alkalihalobacillus clausii (strain KSM-K16) OX=66692 GN=aprE PE=1 SV=2
sp|P00780|SUBC_BACLI	4.48e-19	38	418	23	358	Subtilisin Carlsberg OS=Bacillus licheniformis OX=1402 GN=subC PE=1 SV=2
sp|P27693|ELYA_ALKAL	4.53e-19	114	418	86	359	Alkaline protease OS=Alkalihalobacillus alcalophilus OX=1445 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.003383	0.996594	CS pos: 16-17. Pr: 0.9224

TMHMM  Annotations     

There is no transmembrane helices in SPRG_21856-t26_1-p1.