CAZyme Information: H310_12683-t26_2-p1

Basic Information

• Species: Aphanomyces invadans
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces invadans
• CAZyme ID: H310_12683-t26_2-p1
• CAZy Family: GT41
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1777		193742.37	5.4244

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AinvadansNJM9701	15416	N/A	168	15248

• Gene Location: location=KI913993:29732-36556(+)

Full Sequence      

MRRQGFVMCAWVAAVLGQGPSARDFTNALIQSTRCTPTSTTSACLAYERCKATHRCARGS
EEYTIGDAKLEAFDQEFDQGRRSQVQLVNDFEDWKTGVHHWSVPLEWKAPTKFGFDTFHY
PLLGSLELASGTVYIDTTTAGMSGDVSFQGMLLQTPQRTTVAVFNFLTIHLGANVQVKLK
GRHALCLLSRSSAVVNTHLVSPPGMLGGFPGGGTIAQHNINGPGSSSVRVYTHTVQTSGA
LEPTVMEIQTSVAAGQTMRGTFTLSNGANVTARIRYDASAEEMQAQLELGLGGVGRVQVT
RAGQEVASVGRIWRVSFLTAVGNVPLLTPTSYLTGLDSTVQTRLVAVGNQLSGVFRLRFL
GQTSPDLPYNISADGMAAALRAAFDVQQVAVTKDVPTSIERGCTWRIQMTTLRGNEAPTS
PSAPVVDAPLTFMTASAADVVVDPVTHATTTQPYLIGKRAQVTISDTAGFSLSYGGKGGR
LAANGDLIGGSGGGGGGDSPTDFGQFPRPIFGGAGGGAIYLAAVNDMTLGPNASLAVHGE
AGESGIFAGGGGSGGSIVLTSGTSIHIMGTLAATGGLGGRSTQSPGENGSDGEISLHAHA
VAYSGAGAIVGGTIHLDIQTQLQLTTDPFVGAAQTAKSLYLAKSVIDPTPTLEGPSFRVF
PSQPSRVSYFVRVGATKIGSLQTNRGALFGVHHSSDPTLFVVAIGMMQGALTYSTNARGF
PVQALLPAIHPWQWYQVDIFLNWHVLELEIRVNGVSRVAHVPFAADTVDLIGLYTYDAMQ
TWWDELYVGLDRTMSFHCPTVDSNGRVVVSQPRQRPLWSPAVVGPPTQYSPPIRHYSHLS
RRAVYAYDNGGLAPNDGPLHRVYSNDIRDDVFDADASALGMGELVAIAISPDVSIVYPVD
SNAERIASTATTLPKESQYWFSEVQLVDANHVVVGGGIGACSTTDLISWRNEGIMLHFAN
LTDPFGVHQRLVATRPKVVLTRPGAEQQFVMWMHVDNAQNEMGLSGVATADFPNGPYRFQ
ASMYPPGATEAPGGQTITETHDQTVLVSPTNDAYLIQSYYKTVEYWLPRPIMDPLWESVK
RMDGSVDYSLNFHRAFFTKDYDNVDDIYLQRFRSEDAPWAITCCDRVTNVCDDSVLIHNE
GCPPPYRKQVNGLAQLHEPIRSRYKDPHDPQNNAFRPHSVPSHTDWGFQVYNIKTWRGNY
FDALSTNITLAVFKLFAGMASAYAIPSTQEVTYPFASESAAFINTTDPPNMMDFILDTLG
VPMSPSFLEKFDDFDMKHMDVNLDGKLTLDEVAEMMKSGQKTLSATAFDAFLVELEALKR
EEALKLDPDRDGRITYGEFDAWVGLDPALAFDRFDLDKSGYLDENELSRFLMDRQLPRLD
AIAIMLDPDFDGRVYYEMFEQFVFQASSVVFRSYDFDNSNDLNASEVALLQADIGVSFLN
APVMLSLLPTNTSTMRLDTYMTWMTASASELRDRVQAFKVDNGLHPTRPDRMTGPQHVVE
QRRAKYVSVSKLTPDYVGIEALLVELEGDLDGQGALQDIASLVLQLNFPPTTQSLVPFRQ
FLAPAAFGQYASYWNGRTWEPRPSAPPAFTYGKSTRWMCYRARVTDAAGQQCTDQVRNPD
CLPCLTQSPYLSTTVAVYRNIEPTLAHCDNNKELDAYLKQFDHQVSFPLRFQQVARVSSA
GVQPHYSPCLNQSESVPCDVLKVYEATAVTPWSLAWESRPVNQGTSVKIRAGPMQLESIG
QTFQERFPRRVAEPPFAMCEINSTVVPDQYQHVLGGG

Enzyme Prediction     

No EC number prediction in H310_12683-t26_2-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH43	919	1058	2.2e-17	0.5040650406504065

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
350146	GH43_CtGH43-like	1.68e-20	919	1058	16	155	Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350099	GH43_CtGH43-like	2.22e-20	919	1058	16	142	Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350142	GH43_Pc3Gal43A-like	1.30e-15	919	1056	16	135	Glycosyl hydrolase family 43 protein such as Phanerochaete chrysosporium exo-beta-1,3-galactanase (Pc1, 3Gal43A, 1,3Gal43A). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), Fusarium oxysporum 12S Fo/1 (3Gal), and Streptomyces sp. 19(2012) SGalase1 and SGalase2. It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350143	GH43_CtGH43-like	7.37e-11	919	1058	16	138	Glycosyl hydrolase family 43 protein such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43). This glycosyl hydrolase family 43 (GH43) subgroup includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43), Streptomyces avermitilis MA-4680 = NBRC 14893 (Sa1,3Gal43A;SAV2109) (1,3Gal43A), and Ruminiclostridium thermocellum ATCC 27405 (Ct1,3Gal43A;CtGH43;Cthe_0661) (1,3Gal43A). It belongs to the GH43_CtGH43 subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. GH43_CtGH43 includes proteins such as Clostridium thermocellum exo-beta-1,3-galactanase (Ct1,3Gal43A or CtGH43) which is comprised of the GH43 domain, a CBM13 domain, and a dockerin domain, exhibits an unusual ability to hydrolyze beta-1,3-galactan in the presence of a beta-1,6 linked branch, and is missing an essential acidic residue suggesting a mechanism by which it bypasses beta-1,6 linked branches in the substrate. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.
350147	GH43_CtGH43-like	3.48e-10	936	1062	34	168	Glycosyl hydrolase family 43 protein similar to Clostridium thermocellum exo-beta-1,3-galactanase CtGH43 and Ruminococcus champanellensis arabinanase Ara43A. This uncharacterized glycosyl hydrolase family 43 (GH43) subgroup belongs to a subgroup which includes characterized enzymes with exo-beta-1,3-galactanase (EC 3.2.1.145, also known as galactan 1,3-beta-galactosidase) activity such as Clostridium thermocellum (Ct1,3Gal43A or CtGH43) and Phanerochaete chrysosporium 1,3Gal43A (Pc1, 3Gal43A), and arabinanase (EC 3.2.1.99) activity such as Ruminococcus champanellensis Ara43A. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG55746.1|GH0	0.0	7	1777	3	1775
CCA15423.1|GH0	4.14e-263	171	1592	1	1566
BAX82392.1|GH43_24	4.06e-12	899	1025	36	169
QHO10394.1|GH43_24	5.94e-12	919	1058	165	299
QHO10393.1|GH43_24	5.94e-12	919	1058	165	299

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7BYS_A	1.39e-06	919	1028	32	133	Chain A, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYS_B Chain B, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYT_A Chain A, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]
7BYX_A	1.39e-06	919	1028	32	133	Chain A, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYX_B Chain B, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYX_C Chain C, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium],7BYX_D Chain D, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]
7BYV_A	1.40e-06	919	1028	33	134	Chain A, Galactan 1,3-beta-galactosidase [Phanerodontia chrysosporium]

Swiss-Prot Hits     

H310_12683-t26_2-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.010532	0.989462	CS pos: 17-18. Pr: 0.9549

TMHMM  Annotations     

There is no transmembrane helices in H310_12683-t26_2-p1.