CAZyme Information: KAE8541922.1

Basic Information

• Species: Cryptococcus cf. gattii
• Lineage: Arthropoda; Insecta; ; Eriococcidae; Cryptococcus; Cryptococcus cf. gattii
• CAZyme ID: KAE8541922.1
• CAZy Family: GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1130	CM018865|CGC8	125239.12	6.2561

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccf.gattiiMF34	6321	N/A	114	6207

Full Sequence      

MAPSQPSVRLLLLPFIKSRFLALLILPLVVLILYKNQLSKPPSLKVKVKEAPQGGSWEAL
ADVDDDWGIHEGSWGGGVKDWFGWKDKGRRSIIITGGAGQLAQALIPELISNYTVHVQDI
VPRPPSLPSSVIYHRSSLSPAEAYKSIFPSNIFDGVIHLAGISLGAWCAAKEDQCHEVNV
GGTKALMDEVIAVNKQSKRGKMRKNVRVPWVILGSTMEVFGPEGTDEDSPKNPTSVIGRT
KLEAEQVFEEAILDGASEGIRGLVLRFPEVYGYSSASSIPEAFIPSLLTNSLTSLPIQYS
SDQIPYDLLHAEDAINGFVKAISYIEATPGGGVSSINLVSGQRTPARDIVELVRKETTSM
SPVWDIGDNRNPSANEYSRAKAAEILSWQAEITPLVGLGKAITQLTEDIGTYSRSYLHEH
CPPSADFPASDDDLAVSFIEDERNKPLWKLAGCTVNLGFNHEGWFRHLKCQDGKHCKVDD
VKVTALNWNQSTFIIEKVGKKQRERVVRVMLREQTGMGYLGMTKTEGEVGLELYKDSREG
QTVFDLEVRRDSSSLRLLVPDSEMQLHAVSNNTDGSTWFTVEPITRWVDPHFDMRINVLC
CPFEGDWPLLLDDYESADVRFGSTGQIPFDSTRRSHLCARAEQAVRYNFKHLSTARQAVN
KVTSTAGHAFFRETGPKTDPHPHGWALKDLPACWNDCGSPTVCVQTGNCKCVQADHCKPR
RENPLLKIYPSNPLHPDENKLTLGSLAGYSPVLAKAVEAIDWKDVLLPTAQAALEAHPDF
VKVHVADGYKGQEEIEAASCHKLQESDCFSADSIMYRAFRHMSVPADEAELVVVPAYQQC
EGTQFLLHDAMHHASETIQGVKNGEKKVALVLTHDWGICVDFAWDIWSARGERALHPDGI
LNNVLVWSVMGDYDSPCYRPHQDVVIPARTCRSNTLRETFPNVGAIKPMRERSNLLMWSG
TYSGTGKSERIRLTCNRGGAGDRELIKGGGKQSNFANSDYMKDLNNARFCPQPRGIAGWS
SQTSDAIYAGCIPVFISEGTHYPFADFLDWSKLSVRVAPTELDKIEKVLAAIPLSKVEEL
QANLVSVREAFLYSGDQKPEDELERRGPMFFALHEAGMRIRTRYPVKGEE

Enzyme Prediction     

No EC number prediction in KAE8541922.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT47	781	1072	2e-42	0.9831081081081081

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
397245	Exostosin	1.63e-64	777	1072	1	290	Exostosin family. The EXT family is a family of tumor suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear.
223528	WcaG	2.84e-28	92	402	3	305	Nucleoside-diphosphate-sugar epimerase [Cell wall/membrane/envelope biogenesis].
396097	Epimerase	6.97e-24	92	330	1	233	NAD dependent epimerase/dehydratase family. This family of proteins utilize NAD as a cofactor. The proteins in this family use nucleotide-sugar substrates for a variety of chemical reactions.
212494	SDR_e	3.30e-22	92	338	1	199	extended (e) SDRs. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
187549	Gne_like_SDR_e	4.44e-17	91	321	2	224	Escherichia coli Gne (a nucleoside-diphosphate-sugar 4-epimerase)-like, extended (e) SDRs. Nucleoside-diphosphate-sugar 4-epimerase has the characteristic active site tetrad and NAD-binding motif of the extended SDR, and is related to more specifically defined epimerases such as UDP-glucose 4 epimerase (aka UDP-galactose-4-epimerase), which catalyzes the NAD-dependent conversion of UDP-galactose to UDP-glucose, the final step in Leloir galactose synthesis. This subgroup includes Escherichia coli 055:H7 Gne, a UDP-GlcNAc 4-epimerase, essential for O55 antigen synthesis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
KGB76296.2|GT47	KGB76296.2|GT47	0.0	1	1130	1	1130
ADV23625.1|GT47	ADV23625.1|GT47	0.0	1	1130	1	1130
AAW44475.1|GT47	AAW44475.1|GT47	0.0	1	1130	1	1132
UOH83106.1|GT47	UOH83106.1|GT47	0.0	1	1130	1	1125
AFR96705.1|GT47	AFR96705.1|GT47	0.0	1	1130	1	1125

PDB Hits     

KAE8541922.1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8S1X9|GT13_ORYSJ	sp|Q8S1X9|GT13_ORYSJ	4.83e-14	827	1101	104	381	Probable glucuronosyltransferase Os01g0926400 OS=Oryza sativa subsp. japonica OX=39947 GN=Os01g0926400 PE=2 SV=1
sp|Q3EAR7|GLYT2_ARATH	sp|Q3EAR7|GLYT2_ARATH	1.83e-12	999	1101	348	450	Probable glycosyltransferase At3g42180 OS=Arabidopsis thaliana OX=3702 GN=At3g42180 PE=2 SV=2
sp|Q94AA9|XGD1_ARATH	sp|Q94AA9|XGD1_ARATH	1.89e-11	999	1101	378	480	Xylogalacturonan beta-1,3-xylosyltransferase OS=Arabidopsis thaliana OX=3702 GN=XGD1 PE=1 SV=2
sp|Q3E9A4|GLYT5_ARATH	sp|Q3E9A4|GLYT5_ARATH	2.24e-11	997	1103	343	449	Probable glycosyltransferase At5g20260 OS=Arabidopsis thaliana OX=3702 GN=At5g20260 PE=3 SV=3
sp|Q6NMM8|F8H_ARATH	sp|Q6NMM8|F8H_ARATH	3.97e-11	806	1101	133	438	Probable glucuronoxylan glucuronosyltransferase F8H OS=Arabidopsis thaliana OX=3702 GN=F8H PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999959	0.000061

TMHMM  Annotations     

Start	End
12	34