CAZyme Information: SPRG_11439-t26_1-p1

Basic Information

• Species: Saprolegnia parasitica
• Lineage: Oomycota; NA; ; Saprolegniaceae; Saprolegnia; Saprolegnia parasitica
• CAZyme ID: SPRG_11439-t26_1-p1
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
598		65770.13	6.0124

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=KK583253:172856-174652(+)

Full Sequence      

MLRVVFLLAALATCCIADTDDRAALRARVKAWKESGPGQEAQARGLASGLEATDIDAELD
AFQETLDMVATLNAQYPQARFSEQNPFALMTQAAFEKWVRGNKPARNETWSRTSTEDATV
LPASTATTSIDWSTSGCMAPVRNQGVCGSCFAYAAVAAAESAYCLVNNRQLTLFSDQQAL
SCGPGNGCYGGWSDLSLGWMAANGMCTLDAYPNTNEWTMTTAACEKNCAPTKMPFTTVAS
TVGEVELEQALNLQPVAVDIGSSSPVFKNYAGGVITGGCDTWFDHVLLGVGYGNDDAGLP
YFKMKNSWGTWWGENGYVRLQRGVGGVGTCGLARHAAYPVVFTPQFNLVTSSGHVLSEYY
SNLFAGPSRGPSPNEQWNYDSRTHHIKVNSNHECLDAYYDGSAFKVHTYTCDASNGNQRW
RIDSANHRIAHRTHPNLCLDVDPSQNNKVQVWACGNPAPNQWLAVSEERVKLYSFNNRFL
SSNGEMIQFPPEGSYPYEWVVSNADNTWRARSNTGDPQRCLDAYQPWNGGVVHLYACDAT
NANQKWRYDPSTKQLRHLTHLGFCLDMRTADGSQAHLWRCNAPTNDLQRFTYASQSFP

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM13	370	473	4.8e-17	0.5691489361702128

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
239068	Peptidase_C1A	2.47e-46	128	339	2	210	Peptidase C1A subfamily (MEROPS database nomenclature); composed of cysteine peptidases (CPs) similar to papain, including the mammalian CPs (cathepsins B, C, F, H, L, K, O, S, V, X and W). Papain is an endopeptidase with specific substrate preferences, primarily for bulky hydrophobic or aromatic residues at the S2 subsite, a hydrophobic pocket in papain that accommodates the P2 sidechain of the substrate (the second residue away from the scissile bond). Most members of the papain subfamily are endopeptidases. Some exceptions to this rule can be explained by specific details of the catalytic domains like the occluding loop in cathepsin B which confers an additional carboxydipeptidyl activity and the mini-chain of cathepsin H resulting in an N-terminal exopeptidase activity. Papain-like CPs have different functions in various organisms. Plant CPs are used to mobilize storage proteins in seeds. Parasitic CPs act extracellularly to help invade tissues and cells, to hatch or to evade the host immune system. Mammalian CPs are primarily lysosomal enzymes with the exception of cathepsin W, which is retained in the endoplasmic reticulum. They are responsible for protein degradation in the lysosome. Papain-like CPs are synthesized as inactive proenzymes with N-terminal propeptide regions, which are removed upon activation. In addition to its inhibitory role, the propeptide is required for proper folding of the newly synthesized enzyme and its stabilization in denaturing pH conditions. Residues within the propeptide region also play a role in the transport of the proenzyme to lysosomes or acidified vesicles. Also included in this subfamily are proteins classified as non-peptidase homologs, which lack peptidase activity or have missing active site residues.
395062	Peptidase_C1	8.71e-42	128	340	3	212	Papain family cysteine protease.
214761	Pept_C1	1.62e-32	128	339	3	175	Papain family cysteine protease.
240310	PTZ00200	1.45e-26	130	332	238	436	cysteine proteinase; Provisional
239111	Peptidase_C1A_CathepsinB	3.99e-24	132	324	10	224	Cathepsin B group; composed of cathepsin B and similar proteins, including tubulointerstitial nephritis antigen (TIN-Ag). Cathepsin B is a lysosomal papain-like cysteine peptidase which is expressed in all tissues and functions primarily as an exopeptidase through its carboxydipeptidyl activity. Together with other cathepsins, it is involved in the degradation of proteins, proenzyme activation, Ag processing, metabolism and apoptosis. Cathepsin B has been implicated in a number of human diseases such as cancer, rheumatoid arthritis, osteoporosis and Alzheimer's disease. The unique carboxydipeptidyl activity of cathepsin B is attributed to the presence of an occluding loop in its active site which favors the binding of the C-termini of substrate proteins. Some members of this group do not possess the occluding loop. TIN-Ag is an extracellular matrix basement protein which was originally identified as a target Ag involved in anti-tubular basement membrane antibody-mediated interstitial nephritis. It plays a role in renal tubulogenesis and is defective in hereditary tubulointerstitial disorders. TIN-Ag is exclusively expressed in kidney tissues.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG55540.1|CBM13	7.08e-280	10	598	12	599
AIG56318.1|CBM13	3.54e-185	25	575	19	558
AIG56282.1|CBM13	6.04e-182	17	594	20	580
AIG55595.1|CBM13|GH17	3.49e-54	348	592	305	558
AIG56230.1|CBM13|GH17	1.64e-51	315	592	221	506

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6MIS_A	9.92e-36	129	341	4	214	Native ananain in complex with E-64 [Ananas comosus],6MIS_B Native ananain in complex with E-64 [Ananas comosus],6OKJ_A Native ananain from Ananas comosus [Ananas comosus],6OKJ_B Native ananain from Ananas comosus [Ananas comosus]
6YCC_A	1.02e-35	129	341	4	214	Structure the ananain protease from Ananas comosus covalently bound to the E64 inhibitor [Ananas comosus],6YCC_B Structure the ananain protease from Ananas comosus covalently bound to the E64 inhibitor [Ananas comosus],6YCD_A Structure the ananain protease from Ananas comosus covalently bound to the TLCK inhibitor [Ananas comosus],6YCD_B Structure the ananain protease from Ananas comosus covalently bound to the TLCK inhibitor [Ananas comosus]
3P5W_A	1.14e-35	130	342	5	218	Actinidin from Actinidia arguta planch (Sarusashi) [Actinidia arguta]
6Y6L_A	2.49e-34	129	341	4	214	Structure the ananain protease from Ananas comosus with a thiomethylated catalytic cysteine [Ananas comosus],6Y6L_B Structure the ananain protease from Ananas comosus with a thiomethylated catalytic cysteine [Ananas comosus],6YCB_A Structure the ananain protease from Ananas comosus covalently bound to with the E64 inhibitor [Ananas comosus],6YCB_B Structure the ananain protease from Ananas comosus covalently bound to with the E64 inhibitor [Ananas comosus]
3P5U_A	2.77e-34	130	342	5	218	Actinidin from Actinidia arguta planch (Sarusashi) [Actinidia arguta],3P5V_A Actinidin from Actinidia arguta planch (Sarusashi) [Actinidia arguta],3P5X_A Actinidin from Actinidia arguta planch (Sarusashi) [Actinidia arguta]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q7XWK5|SAG39_ORYSJ	6.08e-35	85	339	83	337	Senescence-specific cysteine protease SAG39 OS=Oryza sativa subsp. japonica OX=39947 GN=SAG39 PE=2 SV=2
sp|A5HII1|ACTN_ACTDE	7.45e-35	56	345	60	347	Actinidain OS=Actinidia deliciosa OX=3627 PE=1 SV=1
sp|A2XQE8|SAG39_ORYSI	8.35e-35	85	339	83	337	Senescence-specific cysteine protease SAG39 OS=Oryza sativa subsp. indica OX=39946 GN=OsI_14861 PE=3 SV=1
sp|P80884|ANAN_ANACO	8.59e-34	62	341	61	336	Ananain OS=Ananas comosus OX=4615 GN=AN1 PE=1 SV=2
sp|P43156|CYSP_HEMSP	7.61e-33	52	340	50	345	Thiol protease SEN102 OS=Hemerocallis sp. OX=29711 GN=SEN102 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000264	0.999692	CS pos: 17-18. Pr: 0.9793

TMHMM  Annotations     

There is no transmembrane helices in SPRG_11439-t26_1-p1.