CAZyme Information: PV06_09655-t43_1-p1

Basic Information

• Species: Exophiala oligosperma
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala oligosperma
• CAZyme ID: PV06_09655-t43_1-p1
• CAZy Family: GT20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2442	KN847341.1|CGC5	273072.56	6.3308

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EoligospermaCBS72588	11938	N/A	45	11893

• Gene Location: location=KN847341.1:1334590-1342113(+)

Full Sequence      

MTARGGSLSIFFFLFFTTCFGYRYDPNYSQWNLNQNQTAVDPLDYWGEWSGHEYTPSPTN
WRFPFYTLFLDRFVNGDPSNDNINGTAYEHDTNSNQMRHGGDLQGLVDTLDYLRGMGIKG
IYIAGSPFINTPWGYDQYSPLDLSILDQHFGDIEMWRTAINEIHERGMYVLLDNTFATMG
DLIGFDGYLNTTTPFSLAEHQVQFKSDRHYYDFSFGNNYNQTCNYPKFWLETGYPAGEDV
TNNLKGCYDSDFDQYGDTEAFGVFPDWRRQLSKFASVQDRLREWHEPVRHKLENFYCILI
ASLDVDGFRYDKATQSTIDAMGFMNEAMRTCAKRFGKENFFTPGEITGGNVFGSLYLGRG
RQPDMLPDNLTAAVTMTNNSADKYFLRAPEHGALDAAAFHYTVYRTLTRFLGMDGNLEAG
YDAPPNWVDMWNNFLLTNDFVNPNTGLFDPRHLMGTTNQDVFRWPAITNGVHRQLLGHFI
TTIEMPGAPLLLWGEEQAFYVLDNTASNYIFGRQAMSSATAWYTHGCYHLNSTQFFKMPL
NASRHGCKDITVSYDHRDPSHPVRNIIHHMNQLREQFPVLQDGFFLQQLSNQTEQIQYPG
SGKVTTETGMWSVMRSGFPGVQDLGTTGAGNLPIWLLYSNANSSTTYNFDCNDNATALNT
TSLIAPYDAGTTVKNLFYPYDEHTLEDSVHQLGINGSTSANGCLRSLDMAAYDFRAYVPI
DDWVGPQPMITKFNPGHDIRLRSTVNSTGTETVDIALEFSVEMDCDSVTNSILFNSTTEL
GTVPTIDRDSVKCTLMNNPETPPYVGAISSVWSWSASIEDVANGIHAITVRNASAQGGGQ
TDAVDRFLFRIGQTDNPMVFTTSANYSSSLLSRSDNGSLMVSHSAAGADKWRYSTNWGST
FSSWMPYKGGKAEIEEQPWSGTKLQSWKGTHVRVEYFSRLAGSSDHIQQGDLGYHTSRRF
PHLFLNGPYNQYGYDAGLDNEMTLSENSTWHHHFMTEWSPSPSGVLAQINVWGVNPDGKP
DQTIVMGDADGDSILDRLPPSSLSSVILNITDAPPKPYLGWRVVINDGTLRFEIVPSGSM
WNQLILYILLWVVPIITAAFGVWSFMQSFYQVKFNEIGISEKAGMIPAAIKKQFKKLKDE
ESSPGFLSKINRKPKFLQQSDTVIDQQRRRTVLIATMEYDIEDWEIKIKIGGLGVMAQLM
GKNLGHQDLIWCVPCVGGVEYPEDTKADPMTVVVLGKPYEVQVQYHVLRNITYVLLDAPV
FRQQTKSEPYPPRMDDLSSAIYYSAWNQCIAQAINRFPVDLYHINDYHGSVAPLYLLPRT
IPACLSLHNAEFQGLWPMRTKQEREEVCSVFNLSTELVQRYVQFGEVFNLLHAGASYLRL
HQHGFGAVGVSKKYGKRSYARYPIFWGLKKVGKLPNPDPSDTGEWDKKLPKESDIRIDPT
FEAGRPELKRQAQEWAGLEQNPQAELFVFVGRWSMQKGIDLIADVFPSILESNPNVQLIT
VGPVIDLYGKFAALKLDRMMKLYPGRVFSKPVFTALPPFIFSGAEFALIPSRDEPFGLVA
VEFGRKGALGVGARVGGLGQMPGWWYTVESMTTSHLLHQFKQAIDEALHSKTEIRALMRA
RSAKQRFPVAQWVEDLEILQSTAIQLHDKVEASKRHAAAGEIIWGHSGWSTPGGSGAVTP
GLANSRVSSSSALNSLTSRLRGLAHSREQSHDVSTRSGSTLARSASLGSHQGPGHINAHD
AHDGEVTYAPNTLATVPDVEGNDATGLGTPNTPNFPEDDDDSSDSDYDADDAITMPTRTR
GRYERVPVHEDFPFTPHHLDNLTSPRSPGLEMASMQSQLAMPHGSSPVPPSPPAESGFLI
PPPPVRAETNNRISASPSMLSVNSIVGEKTDFKLQKVDPFFTDSNGEFAKTFEKKLENLN
GSTSESSACIEEFLVKSEKQWFDTFRNVKLGRYNALSPRPSFQATRESRPPSSYAGDSEH
SSGGHDSNNLGNEFLLGDDYKPPTGLRKWMQLRVGDWPVYAFFMGFGQIIAANSYQITLL
TGEVGQTADKLYSIASIYLVTSICWWFLFRRFSSMLCLSLPFFFYGLAFILIGTAHYAST
ASGRGWVQNVGTGMYAVASSSGSIFFALNFGDEGGAQVKAWVFRACVIQGTQQIYVVALW
YWGAYLNKRTSDGLLTSSDSVSSTWKITAITLPIAILLWVIGLLMWFGLPNYYRQAPGKM
PSFYHSLLRRKIVLWFFFTVIIQNFFLSAPYGRNWSFLWSSSHAKTWQIVLLVLLFFVGV
WAGFLWLFALLSKRHSWILPLFAIGLGAPRWAQIWWGTSNIGLFLPWAGGYTSSALVSRA
LWLWLGTLDAIQGVGLGMILLSTLTRVHVAFTLIIAQVLGSVATIVARACAPNKIGPGPI
SPDISGSVSTIWQAWFWVGLALNLSVCFGYFMFYRKEQLSKP

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	497	2.6e-176	0.995
GH13	1172	1635	1.9e-75	0.98

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
200462	AmyAc_AGS	0.0	23	577	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	1.13e-106	1172	1627	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.
223443	AmyA	3.06e-29	65	592	3	460	Glycosidase [Carbohydrate transport and metabolism].
223374	GlgA	1.96e-27	2010	2406	115	468	Glycogen synthase [Carbohydrate transport and metabolism].
200489	AmyAc_5	2.20e-22	65	370	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCR88082.1|GH13_22|GT5	0.0	4	2442	2	2432
QKX60599.1|GH13_22|GT5	0.0	17	2442	14	2421
UJO14671.1|GH13_22|GT5	0.0	22	2442	20	2401
QSS70070.1|GH13_22|GT5	0.0	24	2442	23	2417
QSS52092.1|GH13_22|GT5	0.0	24	2442	23	2417

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7D9B_A	2.47e-16	65	424	145	442	Chain A, Alpha-glycosidase [Weissella cibaria]
7D9C_A	3.26e-16	65	181	145	259	Chain A, Alpha-glycosidase [Weissella confusa],7DCG_A Chain A, Alpha-glycosidase [Weissella cibaria],7DCH_A Chain A, Alpha-glycosidase [Weissella cibaria]
7EHH_A	3.26e-16	65	181	145	259	Chain A, alpha-glucosidase [Weissella cibaria],7EHI_A Chain A, alpha glucosidase [Weissella cibaria]
5A2A_A	9.33e-15	66	173	12	112	Crystal Structure of Anoxybacillus Alpha-amylase Provides Insights into a New Glycosyl Hydrolase Subclass [Anoxybacillus ayderensis]
5A2B_A	1.15e-14	66	173	46	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q09854|MOK11_SCHPO	0.0	29	2442	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	14	2442	19	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	7	2440	8	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|Q9Y719|MOK13_SCHPO	0.0	23	2442	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	1.40e-292	1031	2442	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
0.240490	0.759500	CS pos: 21-22. Pr: 0.7298

TMHMM  Annotations     

Start	End
2076	2098
2113	2130
2142	2164
2187	2209
2232	2251
2266	2288
2295	2317
2340	2362
2369	2391
2411	2433
7	24
1084	1106
2017	2039
2052	2069