CAZyme Information: PUG3_T001561-RA-p1

Basic Information

• Species: Globisporangium ultimum
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium ultimum
• CAZyme ID: PUG3_T001561-RA-p1
• CAZy Family: AA17|AA17
• CAZyme Description: 3'5'-cyclic nucleotide phosphodiesterase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1551	PultBR650_SC0063|CGC1	171859.39	5.9703

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GultimumBR650	14086	1223559	0	14086

• Gene Location: location=PultBR650_SC0063:2999-9601(-)

Full Sequence      

MACAGGDARLPAVDAAFQEPLLQIVCFSMDRVFQLSEYLRTLHNHLTLHGSTLRDAAFAR
VAVICRCSTQEIREYYDALAREYAARVAFLYESEQQSFADCLLLSLANGGGVLKDNDGMG
QGARAVCEPQPPTVPFKLAYHVFNPARGCLDWNYPWELSGSVYLHSTVQRVVTEIQAAFG
KQGINHPNHLELRGHQIVQKWAATKLECACPLQPKMHVFAINQVQDVFNNRLYEDEVEAN
GHAGGGDLTNLLRLYQANETLDEAFYRRNRLSSVHIGTLVLEAKDSPIAACEESSDLISV
VMPVHNVEKYIEQALVSVMTQTYTHLEILVIDDASTDATPEVVARLRDQDPRIQYVRNET
NIGVAASLNKGFALAKGKYVARMDGDDISLPERIERQWNYLQEHPDVSIVGTSVLLLRER
DDDSFRSMQRLETAVYPTSPLVTKWRMLFGCFVAHPSVMLRYQVLETLARHGEACYSSSQ
TSSEDYELWLRCLFHHKLRIQSMGDALLIHRKHASNVSTTHRDRQIEETQIIAARVIQSI
VATTSKADGVVGSSSPNLHRVLHPLFDVDACESVDALQHAIEVLQQLQSTVCSTPKALTT
KTQIEAFECETEAILQDAAAREGQLALQAMLLDPIRGTQLWGAFAARHPQILNVTSCSKV
GIVGFQVPLEKFAMDMLLRGDGLQQQSEPSASSMDNASNEPVYLANLQTRASYDPLSDVD
SVVGVKTSSILAGTIVAETGKPIFVVEARSARETHRFSTSMFCAALATLENIVYHYDLQQ
VLTKTLESSASLNEFLQDAILQPAVASKSKKAAQQESSELTPPPRLASSPSGSRIESLRP
DIEIEELLVEIAPDLSKLVGHLRTLSSSDAVCLLEFNAVNESCVAIANASAASTDELFDA
ANINAPPATTTTDTGGNAGTTDAPVLPLFHRLLECIQKAQPLDVSGDAELRSLVHGEETF
QTLVFVPIPSTSAACAMHAGILLLSSREHHGYDLRSLRSFMSALALAVVMKRKSDDMHTS
TMQKLKLIHLYNSQFEIETINDPSTLVNMICEIGCQTFNTNRVTLYVADPIKSELWSLST
LGSVNGLRIPYGKGIAGTVASTKETLIVRNAYDDPRFDRSFDVKFGFKTDSLITFPVVDK
NGETLGVIQAINTQQFLDPNAHPLITRFDERVLNVFNHMVSHALQINSSLIMFAKVQADY
WANRVVLDIKDDEDSTRVPRNKWSTFAYACWVLGKFLIAGYRKHRESSNNNDMKSDLSGK
WAVDDSVFGKETSECAIRRRSRKTSIFEGLMLITTFRIEEPMLRCFIDTLVSKYRPVAYH
SFYHGFDVAMNAYCLIRKTSVISVIKEFEALSLIIAALGHDADHPGNDNQFEIDSSSPLA
LCYNDISVLENHHASTTFSVLKHLSASAKVSVRTAIVRCILATGTNAFNVHHSRLISDLS
VVRDVSGFEQVTDGRQLMLNMIIHGADLSSVAHPLPITIKWVELVCQEFTDQAKKSEAIG
IFVPPHLVNLDDEVGRSRLQVNFIDYLVAPLWNTIATILPDARPTHYEQSR

Enzyme Prediction     

No EC number prediction in PUG3_T001561-RA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT74	143	271	1.8e-34	0.42857142857142855
GT2	299	412	7.8e-34	0.6705882352941176

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395177	PDEase_I	2.00e-67	1319	1544	1	230	3'5'-cyclic nucleotide phosphodiesterase.
395426	Glycos_transf_2	2.72e-37	299	465	1	164	Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.
132997	Glyco_tranf_GTA_type	7.06e-36	300	418	1	120	Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.
133055	GT_2_WfgS_like	1.68e-28	299	497	1	181	WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
223539	WcaA	8.75e-28	294	437	1	134	Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA24176.1|GT2|GT74	7.74e-117	22	661	3	728
AOW99803.1|GT2	9.37e-44	297	535	9	234
QOV89439.1|GT2	1.17e-43	295	541	8	239
UFH42939.1|GT2	1.79e-42	292	523	10	228
BBM62240.1|GT2	4.17e-42	292	540	3	231

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2QYM_A	1.25e-37	1285	1543	47	316	crystal structure of unliganded PDE4C2 [Homo sapiens]
3O0J_A	8.50e-37	1285	1543	37	306	PDE4B In complex with ligand an2898 [Homo sapiens],5K6J_A Human Phospodiesterase 4B in complex with pyridyloxy-benzoxaborole based inhibitor [Homo sapiens]
2QYL_A	1.18e-36	1285	1543	48	317	Crystal structure of PDE4B2B in complex with inhibitor NPV [Homo sapiens]
4KP6_A	1.27e-36	1285	1543	51	320	Crystal structure of human phosphodiesterase 4B (PDE4B) in complex with a [1,3,5]triazine derivative [Homo sapiens]
3D3P_A	1.71e-36	1285	1543	48	317	Chain A, cAMP-specific 3',5'-cyclic phosphodiesterase 4B [Homo sapiens],3FRG_A Chain A, cAMP-specific 3',5'-cyclic phosphodiesterase 4B [Homo sapiens],3GWT_A Chain A, cAMP-specific 3',5'-cyclic phosphodiesterase 4B [Homo sapiens],3O56_A Catalytic domain of human phosphodiesterase 4b2b in complex with a 5-heterocycle pyrazolopyridine inhibitor [Homo sapiens],3O57_A Catalytic domain of human phosphodiesterase 4b2b in complex with a 5-heterocycle pyrazolopyridine inhibitor [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q3UEI1|PDE4C_MOUSE	2.69e-35	1285	1543	353	622	cAMP-specific 3',5'-cyclic phosphodiesterase 4C OS=Mus musculus OX=10090 GN=Pde4c PE=1 SV=1
sp|P14644|PDE4C_RAT	5.40e-35	1292	1543	225	487	cAMP-specific 3',5'-cyclic phosphodiesterase 4C (Fragment) OS=Rattus norvegicus OX=10116 GN=Pde4c PE=2 SV=2
sp|Q08493|PDE4C_HUMAN	1.02e-34	1285	1543	352	621	cAMP-specific 3',5'-cyclic phosphodiesterase 4C OS=Homo sapiens OX=9606 GN=PDE4C PE=1 SV=2
sp|Q07343|PDE4B_HUMAN	1.52e-33	1285	1543	370	639	cAMP-specific 3',5'-cyclic phosphodiesterase 4B OS=Homo sapiens OX=9606 GN=PDE4B PE=1 SV=1
sp|P14646|PDE4B_RAT	3.54e-33	1285	1543	370	639	cAMP-specific 3',5'-cyclic phosphodiesterase 4B OS=Rattus norvegicus OX=10116 GN=Pde4b PE=1 SV=4

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000062	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PUG3_T001561-RA-p1.