CAZyme Information: APA10045.1

Basic Information

• Species: Sclerotinia sclerotiorum
• Lineage: Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Sclerotinia; Sclerotinia sclerotiorum
• CAZyme ID: APA10045.1
• CAZy Family: GH28
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1421	CP017818|CGC14	150976.64	4.2134

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ssclerotiorum1980UF-70	11368	665079	238	11130

• Gene Location: location=CP017818:2661400-2667292(+)

Full Sequence      

MAQGDSTNDAQVPLAFAAAEASGFSLFFSFDYAGNGAWPQSTVLSFLNKYISSSAYYYVG
DKPFVSTFEGPAALSAGGGAEINGLFSWAAWPWGNTDMGPYVDASYAQYLDDEFGGSGSD
FSHYMMAISPWFFTNLPGYDKNWLWRGDSLWYDRWIQANYLQPEYAARWLASTSTLSHRY
LQKQYFHNYPGNSRGMVSTEPGCRKLLRNWRHIWKHPQSIPGRVPTGTLFKDNIFYSALL
SGPGATVTVTIGGNTVLGGWAKTPFDGVGIYHGNVSMNGYTGAVTITLSRGDAVITGKDI
STTCTHDIQNWNAWVGYAYGETVTATPTSLSKQVCIAGTGAGNFLGLCQFTCSYGYCPVG
SCVCTQMSTQRTLPKSLDVNGYPAAGLSASYEGVCAFACNYGYCPATTCGTTKEPESIPT
ISPFLPEACTAGSGSGNLGGLCGFACGYGFCPIIACSCDSKGALGTLPAYTCDDSGVPVA
GLDEAVYSDLCRFVYQYGYDPPPTDVCISSTSSSGGSTTACVGGTGPDNVIGLCDFSCED
DSYDVLCDFACTHNYCPPTACSRSPPAGDGGVIYLPPSVWDPSSDPFGCNGNSICTLIIP
PSSLPGPETINWPSLTTTLLASSAGSVYTKTTVLSVEPFTITETNFWSVTITAGDANHAT
FIPEQSFMPPAFILNLPGSELTFPPSAYPSYSNPLPLPTTTSATPIPTFFSTSHGVTILP
MPTITHLLPHNLPVPLVAEATSVSFSDAVELVESLAVVEAVVYLVVEVVADFLDAAEVAI
HRVAACRCPGSGTGDGDGDPDPTSASSCEPSTCATKTSCEAPKETVGCNIDPETGEEGDG
FSHLYIVYPLDGTTSTGTDPIISLLKSYGTQSVTGLTTQASTIIGIMFWSLHLTPDQLTE
VTNHELVASCTPQCTTSCPKIYERVLQRTPRNVTLQDDFSRLNSRELGLIRQDDALTGLV
MISQEEGHDLDDYDGNYIYDKEEMPQTLVYVIDSYINTTDSQFDKFRSQITDMSPGEPPE
PSDEDEDPMAHGTYVLSLIASKRFRVSKNISPVLIGLDNVDAQHTEVSQETFLIALNVAV
QHYRLLGGSAEAGMAIVNLSLNFRETQVTDAWIDDVRNLLREFVNLGVLPVVSSGNEGLD
SVRKYPVMFAASDIPEMLVVGAVDLDGSKTEYSNIDTFVSVHVFGATFCPNGLGGTQYQY
GTSFSAPLVSGLAAYFLGLSSLREKFEAESKPALKVAALKAYIVKLAWSRDKSAIETIYN
GVEWSEVDLTCPADANGQDGTDTCATSTTSTSTTTSTTTASTSAATNTFKVYEWECEGKQ
QITKLGAAAASALTYCASQSSFLSNEGGITQGDTFTVCGSKYTVATTGVGFAISGGGKTG
TCSSVGPPDFANGKSCLGQSGDIISLACQVTVAYKCDIAAC

Enzyme Prediction     

EC	-	-

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM24	334	409	1.2e-27	0.9868421052631579
CBM24	428	502	9.5e-17	0.9473684210526315

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397634	Glyco_hydro_71	7.92e-75	5	295	40	370	Glycosyl hydrolase family 71. Family of alpha-1,3-glucanases.
211418	GH71	7.38e-52	1	165	43	228	Glycoside hydrolase family 71. This family of glycoside hydrolases 71 (following the CAZY nomenclature) function as alpha-1,3-glucanases (mutanases, EC 3.2.1.59). They appear to have an endo-hydrolytic mode of enzymatic activity and bacterial members are investigated as candidates for the development of dental caries treatments.The member from fission yeast, endo-alpha-1,3-glucanase Agn1p, plays a vital role in daughter cell separation, while Agn2p has been associated with endolysis of the ascus wall.
173790	Peptidases_S8_PCSK9_ProteinaseK_like	9.70e-25	974	1247	14	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.
173787	Peptidases_S8_S53	1.19e-19	989	1244	3	239	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.
211414	GH99_GH71_like	1.75e-15	14	169	50	242	Glycoside hydrolase families 71, 99, and related domains. This superfamily of glycoside hydrolases contains families GH71 and GH99 (following the CAZY nomenclature), as well as other members with undefined function and specificity.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APA10045.1|CBM24|GH71	0.0	1	1421	1	1421
APA15443.1|CBM24|GH71	2.22e-88	1	707	216	937
BCS05636.1|CBM24|GH71	1.10e-87	1	389	32	475
CAK44988.1|CBM24|GH71	1.24e-87	1	389	46	501
VBB73755.1|CBM24|GH71	2.23e-87	1	725	1	744

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4H6V_A	1.59e-07	1030	1217	60	235	Structure of Patellamide maturation protease PatA [Prochloron didemni]
3ZXX_A	1.60e-07	1030	1217	69	244	Structure of self-cleaved protease domain of PatA [Prochloron didemni]
4H6W_A	2.12e-07	1031	1223	64	244	Structure of Prenylagaramide maturation protease PagA [Planktothrix agardhii NIES-596],4H6W_B Structure of Prenylagaramide maturation protease PagA [Planktothrix agardhii NIES-596]
3ZXY_A	3.15e-07	1030	1217	50	225	Structure of S218A mutant of the protease domain of PatA [Prochloron didemni]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B6GX22|MU71A_PENRW	2.92e-12	5	320	78	432	Mutanase Pc12g07500 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=PCH_Pc12g07500 PE=1 SV=1
sp|C5PCB1|SUB4A_COCP7	2.88e-11	976	1223	140	363	Subtilisin-like protease CPC735_066880 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CPC735_066880 PE=3 SV=1
sp|C5PCX1|SUB7B_COCP7	1.19e-10	949	1222	118	363	Subtilisin-like protease CPC735_015300 OS=Coccidioides posadasii (strain C735) OX=222929 GN=CPC735_015300 PE=3 SV=1
sp|Q5VJ77|SUB1_TRIVC	1.20e-10	975	1222	140	364	Subtilisin-like protease 1 (Fragment) OS=Trichophyton verrucosum OX=63417 GN=SUB1 PE=3 SV=1
sp|Q64K30|SUB1_ARTBE	1.20e-10	975	1222	140	364	Subtilisin-like protease 1 (Fragment) OS=Arthroderma benhamiae OX=63400 GN=SUB1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000065	0.000002

TMHMM  Annotations     

There is no transmembrane helices in APA10045.1.