CAZyme Information: SDRG_14636-t26_1-p1

Basic Information

• Species: Saprolegnia diclina
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia diclina
• CAZyme ID: SDRG_14636-t26_1-p1
• CAZy Family: GT69
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
653		69708.19	5.9880

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SdiclinaVS20	17448	1156394	89	17359

• Gene Location: location=JH767206:114493-116722(+)

Full Sequence      

MKAFLILSTMAAAASAKVASSVLRALEIDGNADVFVRFADASSALEAATLESNKPLERQE
VFEILSDATATGQKSIEAATAGFEVTPTWIVSGAFIKAADKALIEKLTRNQVIKSVEQVP
DMQLDPVLSKPTTEAVAAAAASPNQWGIDAIGASDVWKYANGSGIGADVINNSWGGKTFH
PVYEEAIASIRKAGITPIFANGNEGPACGTTGSPGTYPNVISVGAIGSYTNEPNKLAFFS
SKGPGKYIDAHNVPQTIVKPTVSAPGFFTLSAYNNSDTGLAYLAGTSMAAPHVAGVVALL
KSIKRDLTYDEIYAYLTQTADRTLEGEPKEWLVPNKTSNGTDVYPGAFNCGGVDDTTWPN
NRYGYGRVNVAKILAGGKFASVATPTPVPRTTPPAPLETNFCTYKKTALSEWNHGLYIDT
IKNNKNEGFTIDRVGNLIAAYAPPKEDSFCLALTKDTTNTNTATLTKCKGDETQIWKFDA
AAKRIVHPASGFCLTFNAAKLGAGPSVAPCSPSAVSQYFDACDNVKAKSYVKLITKSNKV
ISEFYSGVYADWVSDSANELFTYDSNAKTLQAASNGQCLDAFRDGDKFGLHTYACDATND
NQKWIIDAANHKIKHATHNNLCLDVDPTNPSHVAQVWECHNANTNQWIDAVAY

Enzyme Prediction     

EC	-	-

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
173807	Peptidases_S8_BacillopeptidaseF-like	5.81e-40	166	321	119	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	3.66e-32	166	319	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	7.15e-32	166	321	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	3.46e-28	149	321	108	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.
173812	Peptidases_S8_1	8.91e-28	149	321	90	264	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG56170.1|CBM13	0.0	1	653	1	745
AIG56438.1|CBM13	7.65e-304	1	653	1	748
AIG56171.1|CBM13	4.18e-200	1	653	1	751
AIG56439.1|CBM13	2.52e-195	16	653	15	748
AIG56036.1|CBM13|GH17	1.15e-77	396	653	442	691

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1WMD_A	1.93e-17	166	301	122	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	3.41e-17	166	301	121	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]
1WMF_A	2.56e-16	166	301	122	269	Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (oxidized form, 1.73 angstrom) [Bacillus sp. KSM-KP43]
1DUI_A	3.26e-13	157	322	104	247	Chain A, PROTEIN (SUBTILISIN BPN') [Bacillus amyloliquefaciens]
1SUE_A	3.26e-13	157	322	104	247	Chain A, SUBTILISIN BPN' [Bacillus amyloliquefaciens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P16397|SUBF_BACSU	1.25e-14	168	369	341	507	Bacillopeptidase F OS=Bacillus subtilis (strain 168) OX=224308 GN=bpr PE=1 SV=2
sp|P72186|PLS_PYRFU	7.65e-13	166	328	449	634	Pyrolysin OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=pls PE=1 SV=2
sp|Q5JIZ5|TKSP_THEKO	6.42e-12	157	321	254	416	Subtilisin-like serine protease OS=Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OX=69014 GN=TK1689 PE=1 SV=1
sp|P00782|SUBT_BACAM	9.20e-12	157	322	220	363	Subtilisin BPN' OS=Bacillus amyloliquefaciens OX=1390 GN=apr PE=1 SV=1
sp|Q45670|THES_BACSJ	2.41e-11	154	322	238	380	Thermophilic serine proteinase OS=Bacillus sp. (strain AK1) OX=268807 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.028765	0.971234	CS pos: 16-17. Pr: 0.8085

TMHMM  Annotations     

There is no transmembrane helices in SDRG_14636-t26_1-p1.