CAZyme Information: SPRG_22267-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_22267-t26_1-p1
• CAZy Family: GT8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
525		56605.76	8.7626

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=KK583264:126912-130129(-)

Full Sequence      

MICPTRTDGTHPDCSKGADVINNSWGGKKYHPVYEEAIASIRKAGITPIFANGNEGPACG
TTGSPGTYPNVISVGAIGSYTNEPNKLAFFSSKGPGKYVDAHNVRQTIVKPTISAPGFFT
LSAYNNSDTELTYLAGTSMAAPHVAGVVALLKSIKRDLTYDEIYAYLTQTADRALEGEPK
EWLVPNKTSNSTNVYPGAFNCGGVDDTKWPNNRYGYGRVNVAKILAGGKFASVVTPTPVP
RTTPPAPVETNFCTYKKTALSEWNQGLYIDTIKNNKNEGFTIDRVNNIIAAYAPPKKDSY
CLALTKDATNTNTATLTKCKGDETQIWKFDSAAKRIVHPASGFCLTSNAAKLGAGPSVAP
CSPGAVSQYFDACDNVKEKSYVKLITKTNKVISEFYSGVYADWVSDSVNELFTYDSAAKT
LQAASNGQCLDAYRDGNNWKPPRAWVLCKLLANAETLRVLISQSLNRTLGTPARMQARRT
CGAHFLCSPKYSQLFHATDSSCADRVAKSSHTRIAQADGFDVQGA

Enzyme Prediction     

No EC number prediction in SPRG_22267-t26_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173807	Peptidases_S8_BacillopeptidaseF-like	5.53e-48	1	172	103	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.
173803	Peptidases_S8_Subtilisin_subset	1.17e-34	17	170	96	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.
173800	Peptidases_S8_subtilisin_Vpr-like	3.45e-32	17	172	119	270	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.
173799	Peptidases_S8_Subtilisin_like	9.00e-30	16	172	119	259	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.
173790	Peptidases_S8_PCSK9_ProteinaseK_like	1.14e-27	11	171	114	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	1.92e-237	1	439	246	680
AIG56438.1|CBM13	4.22e-227	1	439	244	683
AIG56171.1|CBM13	8.23e-149	1	439	255	686
AIG56439.1|CBM13	1.18e-144	1	439	252	683
AIG56036.1|CBM13|GH17	2.47e-49	247	440	442	627

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5FAX_A	2.10e-19	15	152	119	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]
1WMD_A	5.06e-19	15	152	120	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]
1WMF_A	6.91e-18	15	152	120	269	Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (oxidized form, 1.73 angstrom) [Bacillus sp. KSM-KP43]
1DBI_A	3.84e-13	17	173	127	259	Crystal Structure Of A Thermostable Serine Protease [Bacillus sp. Ak1]
1SBN_E	4.86e-13	19	173	120	256	REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES [Bacillus subtilis],1SIB_E REFINED CRYSTAL STRUCTURES OF SUBTILISIN NOVO IN COMPLEX WITH WILD-TYPE AND TWO MUTANT EGLINS. COMPARISON WITH OTHER SERINE PROTEINASE INHIBITOR COMPLEXES [Bacillus subtilis],1SUP_A Subtilisin Bpn' At 1.6 Angstroms Resolution: Analysis Of Discrete Disorder And Comparison Of Crystal Forms [Bacillus amyloliquefaciens],2SIC_E REFINED CRYSTAL STRUCTURE OF THE COMPLEX OF SUBTILISIN BPN' AND STREPTOMYCES SUBTILISIN INHIBITOR AT 1.8 ANGSTROMS RESOLUTION [Bacillus amyloliquefaciens],2ST1_A The Three-dimensional Structure Of Bacillus Amyloliquefaciens Subtilisin At 1.8 Angstroms And An Analysis Of The Structural Consequences Of Peroxide Inactivation [Bacillus amyloliquefaciens],3SIC_E MOLECULAR RECOGNITION AT THE ACTIVE SITE OF SUBTILISIN BPN': CRYSTALLOGRAPHIC STUDIES USING GENETICALLY ENGINEERED PROTEINACEOUS INHIBITOR SSI (STREPTOMYCES SUBTILISIN INHIBITOR) [Bacillus amyloliquefaciens],5SIC_E MOLECULAR RECOGNITION AT THE ACTIVE SITE OF SUBTILISIN BPN': CRYSTALLOGRAPHIC STUDIES USING GENETICALLY ENGINEERED PROTEINACEOUS INHIBITOR SSI (STREPTOMYCES SUBTILISIN INHIBITOR) [Bacillus amyloliquefaciens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P16397|SUBF_BACSU	8.38e-17	1	220	324	507	Bacillopeptidase F OS=Bacillus subtilis (strain 168) OX=224308 GN=bpr PE=1 SV=2
sp|P72186|PLS_PYRFU	1.43e-12	17	179	449	634	Pyrolysin OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=pls PE=1 SV=2
sp|E4UZP9|SUB2_ARTGP	2.47e-12	16	155	256	375	Subtilisin-like protease 2 OS=Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) OX=535722 GN=SUB2 PE=3 SV=1
sp|Q5JIZ5|TKSP_THEKO	3.15e-12	17	172	263	416	Subtilisin-like serine protease OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1689 PE=1 SV=1
sp|C5NZ70|SUB2C_COCP7	4.08e-12	16	165	248	377	Subtilisin-like protease CPC735_013710 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CPC735_013710 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000049	0.000014

TMHMM  Annotations     

There is no transmembrane helices in SPRG_22267-t26_1-p1.