CAZyme Information: PTTG_27250-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_27250-t43_1-p1
• CAZy Family: GT39
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2323		260175.04	7.6824

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ptriticina1-1BBBDRace1	15692	630390	814	14878

Full Sequence      

MATITISSRTRLICLTILLLGLQLSLIHSYPYDPAFSDYNININSSAGNNILDYYSDWPE
KSQNGSRYTPSPANWRELPIYTVILDRFMDGNPSNNDFYKSRSEWDFLSNQLRHGGDIEG
FAQDRVLDYIYGMGYRTIYIAGTPWLNMPWQSDGYSALDFTLLDPHFGTLSEWRAAIDKI
HSKGMYVMLDTTTTTLSDFLEFKGNSGGAAPFNLHGYEVEYKTTVQKPWNINQYAEFKFT
NSRDQSCRLPKFYNPNGTDVLPPTDWDGCYAGDFNQFGDSSPAGKAPGWQDQLTKYSGVQ
DRLRDWDSGVAAKLEKLACMTVKALDMDALRVDKATQQTLEFMGKWGGSLRTCAKDLGKN
NFFITGEISDGNTFGSLYIGRGRQPAHYANLEFDTAALVTANQTENFMRPIGENALDSAA
FHYSIYRSLTRFLGMDGELDSPYDIPVNWVEAWRQIFVTNDLFNQETQQLDPRHLYGTTN
QDNFRWASLINGTERFLLGQLVTNLIMPGIPFAFYGEEQDLHIFDSQANDYLYGRQPMSS
SKAWQTHGCYKLGSKKYPTMPLGKALNGCKDDWNSLDHYDPTSNTRNMLAHFAYLRSQYA
SLQDGFNLTQLGNWTHFGELPASSHTPTEWGLWSVSRSSLKSQNLSGPNSQLPVWILYSN
VNQTTTFSYDCSSKLAITSPYPGPSTVRNLFYPYETYDLDPSSTSSTWDDAPPFLGCLKS
ITMDPLSYKVLVPASNWVSPQPRLVGFVPGHDARILSQADNDNETIPISLSFSDELSCEG
VSSSLSLSYTIDPNSKASPRIDLEHANCSKIESPSNSTQSALPAVWQWSASIVGAADGIY
ELILNNATGQNGIHTNSIDHLLLRKGRKLNPITFSDVSYSESLLENKDGKYTLRSDAPGA
DMMRYSVDFGKTYSNWTRYSSDHVRVQYWSRLTGSAAPTIDADINFDGGFKRRFPQLILR
GAYNKWGFDEGIPGLLSPRSENMTIDVITSWPHEFQLAVFEARDKVFYGDVDNDGVLDLL
PPNSQARNFLSLPPPSKPYLGWRIMINPRDLTWGAQPVGHQKIVIMLLFLLLFIPPTTAL
LACWLYQRIFYKIKHNQYGFQTAGLNSFLPFQHLPKSMLNSQIPSTLKHAITPQLGSKKE
TPHFSFANTWPENINSRRKVLIATLEYEIIDWGIKVKIGGLGVMTSLMGKVMEDLDLLWV
IPKVSGLEYPEAERAEPIPVVVFGEKYLVELQIHKFKNITYFLLDSPIFRANSKMNPYPA
RMDDLDSAIFYSYWNQSIAEICRRTPDLTIYHINDYHGALAPLYLLPKIIPVALSLHNAE
FQGQWPLGTPEEENEVCQSFNISSKVCSKYARYGSVFNLLHSAASYISHHQNSVGVAGVS
EKYGKRSWARYPVLWTLKSIEPLPNPDPTDVESLDVIPPDMRRIQIDQEAEAKRPGNKLK
LQEWAGLHEDPKAQVFVFVGRWSFQKGVDLIADVFPLLLETRKDVQLVAIGPVIDLYGKL
AALKLNRLMESYPDRVYSKPEFTALPDFRDEPFGLVAVEFGRKGALGVGSRLGGLGLMPG
WWFPVESDSTAHLHSQFAKTLNAALECPEEERAVLRARSVHQRFPVLEWRMKMEDIHSRS
VKASRKYAGRLTMNINQNEVIKPDESSSASHDQGNPRQAHLSATESNKPGQICTSSTGNQ
SNTFGSHLNPTRPSSDVSRILSSTNQLAVQLSEAVKRLIITKNRSSTPPSRLSGRITDKA
SVDGAITPSGRPQNNDQEILTSVVTLDKNNGNTGEHNPADFQRTYCGQDDRNSPLNQGVK
DFTDEDGKASQEFVRRLQTLDASNSQRELCIARYIVAAHKAHFNQVRKGTLALAKTKYGS
SPTLSVTSIIPRAMLGISSHANDLHDFSDQVKNEKNDTVDVTAALSMNRWQIRLQRRVFG
WPVYTVLLAIGQILGATSFQLSLLSGTSSNGSFDFYVIGAVNILGSAWWYGWSRKKPSTW
SLSMPWIFFGLAFIFIGLPSLSENLKQYSRRHSLAVAASGFYSFASSAGFLFFSSNFGRR
PLVLGIQTPKRDPTNAALAPPGWINAITLSLGAGCFSIAYILFTGLPKYYRNVPGTVPNF
TRALFRRKLVLWYLAAEILRNYWLSGPYGRNWNFLWTRETSFGVTLFLLLFFFVGVWGLA
IWGLSRASKSHTWIVAIFAIGLGAPRWCQMLWGTSSVASYISWGGSAGSHIATSLWLWLG
VLDAVQGVGLGMILLQTLSRVHVAATLCLAQIIGSTAVLVARATAPDRIGPGGVFPDLAL
WNPKFSYLDSPLANWQFWIALICQLIIVTGYFVLFRREQLSKP

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	115	519	7.5e-145	0.995
GH13	1159	1526	8.9e-62	0.7775

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200462	AmyAc_AGS	0.0	31	599	16	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	7.34e-91	1159	1604	1	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.
223443	AmyA	3.30e-25	80	618	3	464	Glycosidase [Carbohydrate transport and metabolism].
200478	AmyAc_bac_CMD_like_2	7.77e-21	76	190	1	118	Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. 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.
200459	AmyAc_AmyMalt_CGTase_like	3.66e-19	80	540	7	369	Alpha amylase catalytic domain found in maltogenic amylases, cyclodextrin glycosyltransferase, and related proteins. Enzymes such as amylases, cyclomaltodextrinase (CDase), and cyclodextrin glycosyltransferase (CGTase) degrade starch to smaller oligosaccharides by hydrolyzing the alpha-D-(1,4) linkages between glucose residues. In the case of CGTases, an additional cyclization reaction is catalyzed yielding mixtures of cyclic oligosaccharides which are referred to as alpha-, beta-, or gamma-cyclodextrins (CDs), consisting of six, seven, or eight glucose residues, respectively. CGTases are characterized depending on the major product of the cyclization reaction. Besides having similar catalytic site residues, amylases and CGTases contain carbohydrate binding domains that are distant from the active site and are implicated in attaching the enzyme to raw starch granules and in guiding the amylose chain into the active site. The maltogenic alpha-amylase from Bacillus is a five-domain structure, unlike most alpha-amylases, but similar to that of cyclodextrin glycosyltransferase. In addition to the A, B, and C domains, they have a domain D and a starch-binding domain E. Maltogenic amylase is an endo-acting amylase that has activity on cyclodextrins, terminally modified linear maltodextrins, and amylose. 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
QRW14378.1|GH13_22|GT5	QRW14378.1|GH13_22|GT5	0.0	31	2323	23	2353
QRV85802.1|GH13_22|GT5	QRV85802.1|GH13_22|GT5	0.0	31	2323	23	2353
QRV99867.1|GH13_22|GT5	QRV99867.1|GH13_22|GT5	0.0	31	2323	23	2353
AAW44814.1|GH13_22|GT5|2.4.1.183	AAW44814.1|GH13_22|GT5|2.4.1.183	0.0	15	2323	16	2430
AAR97368.1|GH13_22|GT5|2.4.1.183	AAR97368.1|GH13_22|GT5|2.4.1.183	0.0	15	2323	6	2420

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5A2B_A	5A2B_A	6.60e-12	63	190	28	146	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]
5A2A_A	5A2A_A	1.73e-11	75	190	6	112	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
6SAO_A	6SAO_A	4.99e-11	73	190	4	109	Structural and functional characterisation of three novel fungal amylases with enhanced stability and pH tolerance [Thamnidium elegans]
4E2O_A	4E2O_A	5.29e-11	75	190	7	113	Crystal structure of alpha-amylase from Geobacillus thermoleovorans, GTA, complexed with acarbose [Geobacillus thermoleovorans CCB_US3_UF5]
3VM7_A	3VM7_A	5.98e-11	71	229	23	184	Chain A, Alpha-amylase [Malbranchea cinnamomea]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9Y719|MOK13_SCHPO	sp|Q9Y719|MOK13_SCHPO	0.0	17	2323	6	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|Q09854|MOK11_SCHPO	sp|Q09854|MOK11_SCHPO	0.0	31	2323	24	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	sp|Q9USK8|AGS1_SCHPO	0.0	13	2323	7	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	sp|Q9UUL4|MOK12_SCHPO	0.0	39	2321	32	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|Q9Y704|MOK14_SCHPO	sp|Q9Y704|MOK14_SCHPO	1.10e-250	1035	2323	148	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
0.000222	0.999729	CS pos: 29-30. Pr: 0.9799

TMHMM  Annotations     

Start	End
12	31
1063	1085
1918	1940
1955	1972
1979	2001
2016	2038
2061	2083
2142	2164
2171	2193
2213	2235
2242	2264
2293	2315