CAZyme Information: PTTG_01202-t43_1-p1

Basic Information

• Species: Puccinia triticina
• Lineage: Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia triticina
• CAZyme ID: PTTG_01202-t43_1-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
597	ADAS02000009.1|CGC1	66632.84	8.2680

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

• Gene Location: location=ADAS02000009.1:731881-734453(-)

Full Sequence      

MLTIFQARSLLVLLTVAIHHQAHGSPQASPPGQPLTKADPQTNTLSAATSTYFGWSSWSL
QANKGKGYGYDWLNEKNIKAQADVMFKEFSHLGYDRINLDSGWQDDAVDKYGRTVLNHDK
FPSGIEHLSSYLAQRKLKLGLFYLPGIDSRAVNDQAVVMNTKYTANQIIQCPDREALGCN
RMMPNAFNTGLALNYSHPGAQMYINSVVDGLYSWGVSFVKLAGVVPGSGVDPVEWWKYNT
TGDLMAWRKAIDDMYQQKWQKQGREPIWLAVSWKIPTVAGSTMDKYADSFRIEQDIEAYV
GTMTTSFYRVIRSVKTSALWSSVDANREWKGIRDLDSILISDMTVAECKTMITIWAMSGS
VIYLGDDLTKLPEARKALVKNPEVLKVAIIASTKQARLDGYDPKAYGTRTTTAQPLGQRL
NSVDQLGVNEVTEAYQIIASDCDEMALKRQLVVESGLKQKVDNSDNLYQSCMKASANEKS
THLRTRSTTESEGVNPDPWILQTWVLEQGQGDIYVAVVNAGEQIDEDKPAKVQISLSKLK
TLQKSPRIKQMTRVRYAVRDLWANKNLSNVAFQGAIDATLETHGPILLKFSPIFPLN

Enzyme Prediction     

No EC number prediction in PTTG_01202-t43_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH27	211	397	6.5e-22	0.6899563318777293

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
269893	GH27	3.45e-60	54	387	4	268	glycosyl hydrolase family 27 (GH27). GH27 enzymes occur in eukaryotes, prokaryotes, and archaea with a wide range of hydrolytic activities, including alpha-glucosidase (glucoamylase and sucrase-isomaltase), alpha-N-acetylgalactosaminidase, and 3-alpha-isomalto-dextranase. All GH27 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH27 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
269892	GH36	7.88e-14	54	380	5	291	glycosyl hydrolase family 36 (GH36). GH36 enzymes occur in prokaryotes, eukaryotes, and archaea with a wide range of hydrolytic activities, including alpha-galactosidase, alpha-N-acetylgalactosaminidase, stachyose synthase, and raffinose synthase. All GH36 enzymes cleave a terminal carbohydrate moiety from a substrate that varies considerably in size, depending on the enzyme, and may be either a starch or a glycoprotein. GH36 members are retaining enzymes that cleave their substrates via an acid/base-catalyzed, double-displacement mechanism involving a covalent glycosyl-enzyme intermediate. Two aspartic acid residues have been identified as the catalytic nucleophile and the acid/base, respectively.
178770	PLN03231	5.98e-13	54	387	4	345	putative alpha-galactosidase; Provisional
166449	PLN02808	3.45e-11	54	387	35	292	alpha-galactosidase
178295	PLN02692	1.49e-10	54	400	59	332	alpha-galactosidase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCM93998.1|GH27	2.31e-55	52	392	35	364
BCL77684.1|CBM35|GH27	2.16e-54	42	387	42	380
SDS59418.1|CBM35|GH27	4.87e-52	48	387	65	391
QNE35833.1|GH27	3.44e-49	48	417	99	452
QIZ00458.1|CBM35|GH27	1.02e-48	36	387	53	386

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1UAS_A	2.42e-12	54	387	12	269	Chain A, alpha-galactosidase [Oryza sativa]
3A21_A	8.48e-11	50	387	11	291	Crystal Structure of Streptomyces avermitilis beta-L-Arabinopyranosidase [Streptomyces avermitilis],3A21_B Crystal Structure of Streptomyces avermitilis beta-L-Arabinopyranosidase [Streptomyces avermitilis],3A22_A Crystal Structure of beta-L-Arabinopyranosidase complexed with L-arabinose [Streptomyces avermitilis],3A22_B Crystal Structure of beta-L-Arabinopyranosidase complexed with L-arabinose [Streptomyces avermitilis],3A23_A Crystal Structure of beta-L-Arabinopyranosidase complexed with D-galactose [Streptomyces avermitilis],3A23_B Crystal Structure of beta-L-Arabinopyranosidase complexed with D-galactose [Streptomyces avermitilis]
3CC1_A	1.83e-10	41	387	3	340	Chain A, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125],3CC1_B Chain B, Putative alpha-N-acetylgalactosaminidase [Halalkalibacterium halodurans C-125]
6F4C_B	4.19e-09	54	387	12	269	Nicotiana benthamiana alpha-galactosidase [Nicotiana benthamiana]
3HG3_A	6.19e-08	73	387	33	288	Chain A, Alpha-galactosidase A [Homo sapiens],3HG3_B Chain B, Alpha-galactosidase A [Homo sapiens],3TV8_A Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens],3TV8_B Pharmacological Chaperoning in Human alpha-Galactosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q92451|AGAL3_HYPJE	8.74e-21	21	310	154	426	Alpha-galactosidase 3 OS=Hypocrea jecorina OX=51453 GN=agl3 PE=1 SV=1
sp|Q8RX86|AGAL2_ARATH	4.86e-12	48	419	37	328	Alpha-galactosidase 2 OS=Arabidopsis thaliana OX=3702 GN=AGAL2 PE=1 SV=1
sp|Q9FXT4|AGAL_ORYSJ	1.68e-11	54	387	67	324	Alpha-galactosidase OS=Oryza sativa subsp. japonica OX=39947 GN=Os10g0493600 PE=1 SV=1
sp|Q8VXZ7|AGAL3_ARATH	1.32e-10	48	387	70	332	Alpha-galactosidase 3 OS=Arabidopsis thaliana OX=3702 GN=AGAL3 PE=1 SV=1
sp|P14749|AGAL_CYATE	1.59e-10	54	387	59	316	Alpha-galactosidase OS=Cyamopsis tetragonoloba OX=3832 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000269	0.999704	CS pos: 24-25. Pr: 0.9752

TMHMM  Annotations     

There is no transmembrane helices in PTTG_01202-t43_1-p1.