CAZyme Information: ZTRI_1.1789.mRNA-p1

Basic Information

• Species: Zymoseptoria tritici
• Lineage: Ascomycota; Dothideomycetes; ; Mycosphaerellaceae; Zymoseptoria; Zymoseptoria tritici
• CAZyme ID: ZTRI_1.1789.mRNA-p1
• CAZy Family: AA3
• CAZyme Description: similar to alpha 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2410		270063.32	6.3206

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ZtriticiIPO323	11839	336722	13	11826

• Gene Location: location=Ztri_chr_1:5063435-5071105(+)

Full Sequence      

MFAQRVVAVFLILLGVVPAYRYDPEYTEYNLNQNQFTENPLEYWGYWHEDAADYTPSPEN
WRMPFYTLFLDRFVNGDPYNDEINGTAFERDPNSNQMRHGGDLQGLIDTLDYLSGMGIKA
LYIAGSPFMNQPWGYDQYSPIDLTLLEPHFGTLETWRRAVMEIHKRVFTALGMRVVLDNT
IATLGDLIGFEGYLNTSTPFTVKEHRAQWKTDRRYLDFDFGNTYNETCTYPRFWNETGYP
IDQPIRDQLVGCYDSDFDQYGDTEAFGVYPDWRRQITKFASVQDRLREWHPPVRAKLENF
YCMLIAQLDIDGFRYDKATQGTPDAIAAMSASFRECARRHGKQNFYITGEITGGNTFASI
YVGRGRQPDQLPENLTQAVTLKHNSSHQYFLRAEQESAMDSGAFHYTIYRTLTRFLGMDG
NLEAGYDAPRNWVDMWNTLLLTNDMTNANTGDFDPRHMYGVTNQDVFRWPAIRQGLHRQI
VGHFITTLLMPGIPKLLWGEEQAFYVLDSTNSNYMFGRQPLSAATAWQTHGCYGLDSTQY
YQMPLEAARNGCNDDTVSQDHRDPSAPVRNILRRMYHLREVYPVLNDGFFLQQLSNMTEG
MVYRGSSGVVTDTGLWSVMRSTFVGVQDLNKNTQANTTVTTTSDETSEDAIDVMVDALGG
NATVATSKGNTTIFTSGENTTITTTDNTTDSAIANRNANLPIWLIFTNLNETKRFEFNCS
DNATDLNTTALISPYPAGTKIKNLFHPYDEHTLINSTQTLYISNSTEPNGCLRELEVPPF
GFAAYVPASDWVGPEPVITKFSPGHDASILSTRDKRVEVQLEFSQSMDCNNVTRSITFES
STDNGDIRPTVDRDTIKCGAIANPENSTLVAGIPSAWFWSAKLRNVEDGVHRLTVPVVKT
LSGSQLTKSRDHFLIRVGQPNNPIVFTRTANYSSTLLVQASDDKLMLNHSAAGADLFRYS
TNFGTSFSDWTPYTGGMTEVEKQPWSGTKKQAWKGEHVRVEYFSRFRGSSDHVQQADLDS
KPRRLPNLFLNGPYNSYGYDAGLDNTFKLSNDGEWSIPWMTEWSASGSVAQLNVWGMNPD
GQPDQTIVLGDIDGDSVLDRLPPSSLAKLVLNITMPPPKPHLAWKIAVNDGNMRFALIPT
GNMWHQLTLYVLLWTVPLITAALSAWVFVLGFYKVKFNKIGATEKIRSVLPVAIRKPLRK
LFHRRTPSSERFLQEVAKPSLENSLENQRTVLIATMEYNIDDWNIKIKIGGLGVMSQLMG
NNVPNLIWVVPCVGGIDYPIDEEAPPMNVTILGSTYTVNVQYHTVKNITYVLLDAPVFRK
QTKAEPYPARMDDMESAIYYSAWNQCIAQAIQRFPEVDIYHINDYHGTVAPLYLLPRTIP
VCLSLHNAEFQGLWPMRKSAEKEEICMVFNLPVDTVTKYVQFGQVFNLLHAGASLLRLHQ
EGFGAVGVSTKYGKRSHARYSIFWGLGEVKALQNPDPSDLGAIEEPSDTPADITVDAEWE
QSRLQLRVEAQEWAGLEINPNAELFVFVGRWSMQKGVDLIADAFPSILEKNPNVQLITIG
PVIDLYGKFAALKLDKLMEKYPGRVCSKPVFTQLPPCVFTGAEFALIPSRDEPFGLVAVE
FGRKGALGVGARVGGLGQMPGWWFTVESTSTSHMLNQFKGAIREAMASSFETRAKMRAIS
AKQRFPVAQWRKELDELQSKAIRMHDKIRNRKSMGSSSTASTLVPSEPSLPSEPSLSSET
SLSPPASAAASRRQSFDFEFQTASEEDGLNMSSRSRRYSSTSQVSSLEVSDEDDVRGHPG
GDIVPDLPPIPAPARYSTSNMSSLSPLPRTESSRRISRLPTELSMEKVVGEKTDYNLQEV
DPFFTDSNGTFFKKFEKMLENLNGKNSETSNCIEEYLLKSEKDWASNVRNARLGRNKSET
NLSIWNKRTVSVNVSPVITELFDSDSDLEMNGSPLPTNGEYQLAPGYTPPRGLRNWMQIR
LGTWPLYSFLLALAQVISANSYQITLLTGEVGQPAGKLYAIASIYLATSIGWWIMYRRLS
SHYALSLPFLFYGLAFFFIGIAHYAGYNGANWIQNVGTGCYAVASSSGSLYFALNFGDDA
GGRVHNWVFRACMIQGTQQVWVVALWYWGRVITHQSTLGHVTSVGDGFAGTWKITAVALP
IAALLWAIGLILYFGLPAYYRQSPGDTPAFYSSIIRRKVVIMFGVMVLVQNFFMSAPYGR
NWTFLFSSSHVPNWQIFLLAMGFFIGVWGVSLWILGYYSRAHTWLMPVFAIGLGAPRFVQ
IWWGTSGLGLWLPWAGGTFISSVFASRSVWLWLGVLDSLQGVGLGMILLSTLTRSHVAFT
VTGCQVIGAAVTILARAVAPNRIGPGLISPDISGGLEAILQPWFWVGLILQLLLCVGFFK
VYRKEQLQKP

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	100	502	1.5e-179	0.995
GH13	1231	1694	6.5e-70	0.9825

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200462	AmyAc_AGS	0.0	6	582	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	3.79e-95	1231	1697	2	471	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.
223443	AmyA	9.57e-29	65	596	3	459	Glycosidase [Carbohydrate transport and metabolism].
200489	AmyAc_5	2.67e-24	65	375	2	314	Alpha amylase catalytic domain found in an uncharacterized protein family. 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.
223374	GlgA	2.97e-23	1977	2385	115	484	Glycogen synthase [Carbohydrate transport and metabolism].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
SMY20404.1|GH13_22|GT5	0.0	1	2410	2	2411
SMR45241.1|GH13_22|GT5	0.0	1	2410	2	2411
SMR43075.1|GH13_22|GT5	0.0	1	2410	2	2406
SMQ46717.1|GH13_22|GT5	0.0	1	2410	2	2405
UJO14671.1|GH13_22|GT5	0.0	7	2410	7	2401

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2A_A	2.31e-16	66	185	12	119	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	2.98e-16	66	185	46	153	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis],5A2C_A Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
7D9B_A	6.69e-15	65	533	145	503	Chain A, Alpha-glycosidase [Weissella cibaria]
3D1J_A	1.37e-14	1347	1636	120	401	Chain A, Glycogen synthase [Escherichia coli]
2QZS_A	1.43e-14	1347	1636	120	401	Crystal Structure of Wild-type E.coli GS in complex with ADP and Glucose(wtGSb) [Escherichia coli],2R4T_A Crystal Structure of Wild-type E.coli GS in Complex with ADP and Glucose(wtGSc) [Escherichia coli],2R4U_A Crystal Structure of Wild-type E.coli GS in complex with ADP and Glucose(wtGSd) [Escherichia coli],3GUH_A Crystal Structure of Wild-type E.coli GS in complex with ADP and DGM [Escherichia coli K-12]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9UUL4|MOK12_SCHPO	0.0	6	2407	9	2350	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	27	2410	30	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|Q9USK8|AGS1_SCHPO	0.0	2	2410	9	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|Q9Y719|MOK13_SCHPO	0.0	21	2410	23	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	6.29e-296	1094	2410	125	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
0.025943	0.974020	CS pos: 21-22. Pr: 0.5600

TMHMM  Annotations     

Start	End
1151	1173
1981	2003
2018	2036
2043	2062
2072	2094
2107	2129
2154	2176
2199	2216
2236	2258
2278	2300
2310	2332
2337	2359
2379	2401