CAZyme Information: Bcin08g02140.1:RNA-p1

Basic Information

• Species: Botrytis cinerea
• Lineage: Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Botrytis; Botrytis cinerea
• CAZyme ID: Bcin08g02140.1:RNA-p1
• CAZy Family: GH3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2467	bcin_chr_8|CGC11	275311.67	5.9774

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_BcinereaB05-10	12073	332648	366	11707

• Gene Location: location=bcin_chr_8:812541-820088(+)

Full Sequence      

MLARTFVALCSVLLSTQVDALRYEEEFVGYNLNTNQTATSPFDYYGKWEDHEFFQSPDNW
RFPFYSFFLDKFVNGDPTNDDINGTKFETDFMQTQLRHGGDLQGLIDSLDYIQGMGIKGI
YIAGSPMINAPWGADQYSPLDFSLLDQHFGDIDLWRKTTTAIHDRGMYVMLDNTMGTMGD
LIAFKGYENSSTPFTLTEHEVLWRNDNRQYLDFSFGSKYNETCNYPRFWLDTGYTVKEDV
TDLMNGCYDSEFDQYGDTEAFGVFPDWQRQLSKFASVQDRLREWVPSVRTKIEIFTCMII
QQLDIDGLRVDKATQITVDALGSFSHAIRECARDVNKTNFMVTGEITGGNTFGSIYLGRG
RQPDMLPSSMADAVKLTSNSSLAYFIRDHDQNALDSAAFHYSVYRTLTRFLGMDGNLASG
YDTPTNWVDAWNEMLVTNDFVNPNTGVFDPRHMYGVSNQDVFRWPAIQNGTQKQLLGFFI
TTIHMPGIPLLLWGEEQAFYVLDNTADNYLFGRQAMSPSQAWQTHGCYALGSGTYYQFPN
DSCTRGCNDDWNSRDHRDPSHPVRNIVKAMYQMRDNYPVLTDGAFLRQLSNQTIEILLPG
SNGTATETGMWSTMRGQYDGIQDLSKAGGQANQSVWMVYHNNYDTVTYSFDCSSNETSLV
APFLDGVTVKNLFYPYEEVTLKAGPFQLGIANQTGFNGCLDSLTLVPYEYKAYVPKKSWV
GPSPMITSFSPGHDARLVSTVAPGEQETIEIEFGFSAEMKCSDLISKMVITSATEDGQVA
TLANATGEYSCTLLPSAVNVTEFVGSIPTMWTFKGNLTNVSNGVHSITLANITSNSGNSS
TGATDTFLFRVGQVDNPIAFPGSANFTRELLHKYDNGTLYVSHKAAGADRFKYSLNWGSS
WSEWLPYVGGNTTLEPQAWTGTSKQKWDGDHVIMQYWSKLTGSSDVVQHADLETNKWSRR
LPHLFANGPYNQYGYDTGIDNGFTLNKKDSLWEYKFMTEWPAVMQVNVWGMNPDGQPDET
IVLGDIDNDNILDRMPPSSLSTALINITRVPPSPYLGYKIAIDDGNYRYYQIPYGNRSYQ
MLMVVLFWIVPVLSGGLSIWLFMKSFYAVKLNSVGVKEAKNYIPLALRRKLKREKKEDPS
EKEMTVMGGLHSMFHENATQLGLQADVAATGRRTVLIATMEYDIEDWAIKIKIGGLGVMA
QLMGKNLGHQDLIWVVPCVGGIDYPIDHQAEPMDVTILGNSYTVQVQYHTLRNITYVLLD
APVFRAQSKSEPYPARMDDLDSAVYYSAWNQCIALTIKRFPVDLYHINDYHGAVAPVHLL
PETIPCCLSLHNAEFQGLWPMRNQKERSEVCQVYNIPEEVAIKYVQFGDVFNLLHAGSSY
LRIHQKGFGAVGVSKKYGKRSWARYPIFWGLSKIGNLPNPDPSDTGDWNGTQDSTGKTIV
NQDFESQRADLKRQAQEWAGLEQNPKAELLVFVGRWSMQKGIDLIADVMPAVLEENPNVQ
LICVGPVIDLYGKFAALKLDVMMTKYKGRVFSKPEFTALPPFIFSGAEFALIPSRDEPFG
LVAVEFGRKGALGIGARVGGLGQMPGWWFTVESTTTTHMLHQFKQAIKEALASKLETRQI
MRARSAKQRFPVAQWVNDLEILQSKAIKIHDKEEAKHSGRPRSRGRDGGNIFYSSAKRLS
SFGTSFASTSQLDVASTIGGSTRPSSPTRVEQPPAGGGLSRKLSLGYRAGPGHRVTKNRF
NGSNAPGAGIKNDEGLTDVDEDSDDEDARIRDDIYDEYVLTPEELEAQRQQEQWRGQAES
PAAGGAFLAPQPGFLDSPRRSPSANTGSLHINDSELSLPRLKDGSNIYSTHSIPGSPGLE
SPGTPGAHDSLLPPPSIFGAGGDNANRASMLSLSSVIGDKTDFKLQKVDPFFTDTQGEYY
QQFARNLDNLDGKNSEGQLCIEEYLIKSEKKWFDRFRDAKLGRNSVAPSFSALGSGRRSH
DSRGRSNSRDSFTNDTITHSRQNSSQDNMALTGGSTANDQFLLGKDYKPPTGLRLVMQYR
FFDWPVYSFLLAFGQIIAANSYQITLLTGTVGQSAEKLYITATIYLVTSIMWWEVFSFFK
SIYVLSIPFIFYGLAFFLLGMAPFVDGADGRGWVQNVATGLYAVAASSGSIFFALNFGDE
GGSPVKAWVFRACIIQGTQQAYVVILWFWGSYLNRRQADGLGTSFTSASPKMSAVVLPIA
VLMWAVGLITFLGLPEYYRQAPGKVPSFYASLFRRKIVMWFFVTVLIQNFFLSTLYGRNW
LYLFSSNHAPTWAIILLIIFFFGFLWAGFLWFFAILSKDHSWVLPIFAIGLGAPRWCQML
WSCTPIGQYVPWVGGGLASAIFSRSLWLWLGMLDALQGVGFGMLLLQTLTRVHIAFTLIA
AQVLGSIATMVARACAPNKIGPGTVFPDFSDGAAGLGNGWFWIGLILQLVICGGFFTFFR
KEQLSKP

Enzyme Prediction     

EC	2.4.1.183:18	2.4.1.-:2	2.4.1.183:36	2.4.1.-:11

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH13	99	497	5.6e-184	0.995
GH13	1174	1637	2.5e-73	0.98

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200462	AmyAc_AGS	0.0	7	577	1	569	Alpha amylase catalytic domain found in Alpha 1,3-glucan synthase (also called uridine diphosphoglucose-1,3-alpha-glucan glucosyltransferase and 1,3-alpha-D-glucan synthase). Alpha 1,3-glucan synthase (AGS, EC 2.4.1.183) is an enzyme that catalyzes the reversible chemical reaction of UDP-glucose and [alpha-D-glucosyl-(1-3)]n to form UDP and [alpha-D-glucosyl-(1-3)]n+1. AGS is a component of fungal cell walls. The cell wall of filamentous fungi is composed of 10-15% chitin and 10-35% alpha-1,3-glucan. AGS is triggered in fungi as a response to cell wall stress and elongates the glucan chains in cell wall synthesis. This group includes proteins from Ascomycetes and Basidomycetes. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
340822	GT5_Glycogen_synthase_DULL1-like	1.10e-103	1175	1630	2	459	Glycogen synthase GlgA and similar proteins. This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.
223374	GlgA	5.13e-31	2036	2445	108	487	Glycogen synthase [Carbohydrate transport and metabolism].
223443	AmyA	3.08e-22	64	556	3	414	Glycosidase [Carbohydrate transport and metabolism].
200458	AmyAc_euk_AmyA	1.97e-21	99	499	39	335	Alpha amylase catalytic domain found in eukaryotic Alpha-amylases (also called 1,4-alpha-D-glucan-4-glucanohydrolase). AmyA (EC 3.2.1.1) catalyzes the hydrolysis of alpha-(1,4) glycosidic linkages of glycogen, starch, related polysaccharides, and some oligosaccharides. This group includes eukaryotic alpha-amylases including proteins from fungi, sponges, and protozoans. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCD46749.1|GH13_22|GT5	0.0	1	2467	1	2467
ATZ52517.1|GH13_22|GT5	0.0	1	2467	1	2467
APA10928.1|GH13_22|GT5	0.0	1	2467	1	2460
QSZ37320.1|GH13_22|GT5	0.0	1	2467	1	2458
BCR88082.1|GH13_22|GT5	0.0	23	2467	22	2432

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D9B_A	6.83e-18	53	180	127	259	Chain A, Alpha-glycosidase [Weissella cibaria]
7EHH_A	6.83e-18	53	180	127	259	Chain A, alpha-glucosidase [Weissella cibaria],7EHI_A Chain A, alpha glucosidase [Weissella cibaria]
7D9C_A	6.83e-18	53	180	127	259	Chain A, Alpha-glycosidase [Weissella confusa],7DCG_A Chain A, Alpha-glycosidase [Weissella cibaria],7DCH_A Chain A, Alpha-glycosidase [Weissella cibaria]
6GNG_A	8.61e-14	1192	1592	54	491	Granule Bound Starch Synthase I from Cyanophora paradoxa bound to acarbose and ADP [Cyanophora paradoxa],6GNG_B Granule Bound Starch Synthase I from Cyanophora paradoxa bound to acarbose and ADP [Cyanophora paradoxa]
3D1J_A	1.33e-13	1303	1581	131	401	Chain A, Glycogen synthase [Escherichia coli]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9USK8|AGS1_SCHPO	0.0	4	2467	11	2410	Cell wall alpha-1,3-glucan synthase ags1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=ags1 PE=1 SV=3
sp|Q9UUL4|MOK12_SCHPO	0.0	18	2465	20	2351	Cell wall alpha-1,3-glucan synthase mok12 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok12 PE=3 SV=1
sp|Q09854|MOK11_SCHPO	0.0	30	2467	32	2397	Cell wall alpha-1,3-glucan synthase mok11 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok11 PE=3 SV=2
sp|Q9Y719|MOK13_SCHPO	0.0	18	2467	19	2358	Cell wall alpha-1,3-glucan synthase mok13 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok13 PE=3 SV=2
sp|Q9Y704|MOK14_SCHPO	4.33e-275	1034	2467	131	1369	Cell wall alpha-1,3-glucan synthase mok14 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mok14 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000286	0.999698	CS pos: 20-21. Pr: 0.9793

TMHMM  Annotations     

Start	End
1080	1102
2046	2068
2078	2096
2101	2123
2133	2155
2168	2190
2212	2234
2257	2276
2291	2313
2320	2339
2349	2371
2392	2414
2440	2459