CAZyme Information: EPrPVT00000017090-p1

Basic Information

• Species: Phytopythium vexans
• Lineage: Oomycota; NA; ; Pythiaceae; Phytopythium; Phytopythium vexans
• CAZyme ID: EPrPVT00000017090-p1
• CAZy Family: GH16
• CAZyme Description: Tetratricopeptide repeat domain protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1052		116381.38	4.4229

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PvexansDAOMBR484	11991	1223560	34	11957

• Gene Location: location=PvexDAOMBR484_SC0186:17997-21535(+)

Full Sequence      

MVLSRWTRWTCLAAALCLAVSAEEAATLDDEVMDEEIDLEEEMEEETEEDAVVEDPLLPA
GHCKLVAPVELALDCRLGAIGKFLPAQDDGVASVLRVVALPEDQWQACSPLEGKEPNYYK
DAVVVARRGECSFQDKVRVGALSSYAPCSGWLTRLHEQLKHVASAGGAAMIVVNTEDEPL
DLGALDTDEISAIAVSMALSQGEELLAQVTADTDARLEICAPVSEVEQARLRLQHFAETN
TQVAAFHTFWQAVHNLPELQALGSFEEIVAAISQIDKAEKVANESPVGVAPMSDDAFEFL
VSSSFALSWWTFADEAVLHGSTLAAASLMLGSRGKDSPLSSKDKLLLQLAAQQLISAGYF
VPGRVLLSRLLEEEAQDATEEVELHCRIAITRFLEADLLQSIPVLPKECAEVELSLGNVV
PSLLVGEQALYNTAAVERTPEDDVCLSQAAGESKAADNSCCKYVAIETEIEGEDNSTTIK
RELRFKSQFVGKLYNSLNLMGVFLDEIGAFDESLRFFDHAERLCPYHDGQSVQLRRATAV
PVVFSSNDEVDSFFTKELPKKLQKLDAVGRKSAAPVVVSAAGETAEADYVWRPEKATHLS
WSSHFDKVVCVLDVVVDHKGHDVLPVQRALYDLRSKLFPSLTSTFAPSPSTTATGKKRIA
FISSWFRDHSVGKLLLGVLERLDRSQFEVIVYRCTHFLRNEDDWTEAFAEAADEYDELPE
DQEEAIRLLRNERIDVVVFPELGMDAWTVFLSHHRIAPVQCVFWGHPITTGNPNIDYFIS
SRYFTQDGGVADGNKRFQIEQNDKYSEKLAVFNGLSTIFTEPTADDDLLQPVSRADLHLP
ENRRLYVCPQHTIDNWSSGAAQTLMKFHPRFDTVLAGILKRDPEGVIVLVASDKQQMWTE
QLRRRFRSQFGKDAYRVRFLPTLPFEEFQALLSHSSVMLDPFPFGGGVTALDALNLGIPV
VTLPSEQSVVQLAAGFLRYLNVTDGIVTSADEYVEFAVEVATKPDVREQIRTQLLASHGA
IYKDESAVHDWNAFLTTVADSTRSATPVRDEL

Enzyme Prediction     

No EC number prediction in EPrPVT00000017090-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT41	475	1043	1.8e-69	0.5205673758865248

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226428	Spy	3.59e-51	656	1014	259	588	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
340831	GT4_PimA-like	9.54e-11	658	1011	1	341	phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.
238300	PA	2.73e-09	107	219	32	126	PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.
239038	PA_C_RZF_like	3.13e-09	82	206	25	134	PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. The significance of the PA domain to these proteins has not been ascertained. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.
404688	Glyco_transf_41	5.99e-06	811	1013	331	523	Glycosyl transferase family 41. This family of glycosyltransferases includes O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase, an enzyme which catalyzes the addition of O-GlcNAc to serine and threonine residues. In addition to its function as an O-GlcNAc transferase, human OGT also appears to proteolytically cleave the epigenetic cell-cycle regulator HCF-1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG55953.1|GT41	1.04e-116	50	1038	19	874
QDU81044.1|GT41	3.53e-69	618	1045	622	1030
QDT74414.1|GT41	1.28e-68	658	1039	599	949
BBO34148.1|GT41	3.66e-67	656	1037	599	949
BAP54338.1|GT41	1.12e-63	611	1037	185	584

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5DJS_A	7.28e-18	618	1014	111	493	Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum],5DJS_B Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum],5DJS_C Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum],5DJS_D Thermobaculum terrenum O-GlcNAc transferase mutant - K341M [Thermobaculum terrenum]
2JLB_A	8.47e-18	627	1039	177	560	Xanthomonas campestris putative OGT (XCC0866), complex with UDP- GlcNAc phosphonate analogue [Xanthomonas campestris pv. campestris],2JLB_B Xanthomonas campestris putative OGT (XCC0866), complex with UDP- GlcNAc phosphonate analogue [Xanthomonas campestris pv. campestris],2VSY_A Xanthomonas campestris putative OGT (XCC0866), apostructure [Xanthomonas campestris pv. campestris str. ATCC 33913],2VSY_B Xanthomonas campestris putative OGT (XCC0866), apostructure [Xanthomonas campestris pv. campestris str. ATCC 33913],2XGM_A Substrate and product analogues as human O-GlcNAc transferase inhibitors. [Xanthomonas campestris],2XGM_B Substrate and product analogues as human O-GlcNAc transferase inhibitors. [Xanthomonas campestris],2XGO_A XcOGT in complex with UDP-S-GlcNAc [Xanthomonas campestris],2XGO_B XcOGT in complex with UDP-S-GlcNAc [Xanthomonas campestris],2XGS_A XcOGT in complex with C-UDP [Xanthomonas campestris],2XGS_B XcOGT in complex with C-UDP [Xanthomonas campestris]
2VSN_A	8.47e-18	627	1039	177	560	Structure and topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation [Xanthomonas campestris pv. campestris str. 8004],2VSN_B Structure and topological arrangement of an O-GlcNAc transferase homolog: insight into molecular control of intracellular glycosylation [Xanthomonas campestris pv. campestris str. 8004]
3Q3E_A	3.37e-15	736	1019	352	604	Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3E_B Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3H_A Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in complex with UDP-GLC [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3H_B Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in complex with UDP-GLC [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3I_A Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in the presence of peptide N1131 [Actinobacillus pleuropneumoniae serovar 1 str. 4074],3Q3I_B Crystal structure of the Actinobacillus pleuropneumoniae HMW1C glycosyltransferase in the presence of peptide N1131 [Actinobacillus pleuropneumoniae serovar 1 str. 4074]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A3N2T3|NGT_ACTP2	1.70e-14	736	1019	341	593	UDP-glucose:protein N-beta-glucosyltransferase OS=Actinobacillus pleuropneumoniae serotype 5b (strain L20) OX=416269 GN=APL_1635 PE=1 SV=1
sp|Q9M8Y0|SEC_ARATH	3.23e-14	658	1017	593	928	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
sp|B3H2N2|NGT_ACTP7	3.89e-14	736	1019	341	593	UDP-glucose:protein N-beta-glucosyltransferase OS=Actinobacillus pleuropneumoniae serotype 7 (strain AP76) OX=537457 GN=APP7_1697 PE=1 SV=1
sp|Q8RVB2|SPY_SOLLC	1.62e-13	636	1014	470	819	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Solanum lycopersicum OX=4081 GN=SPY PE=2 SV=1
sp|Q96301|SPY_ARATH	3.63e-13	659	1014	485	814	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Arabidopsis thaliana OX=3702 GN=SPY PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000369	0.999584	CS pos: 22-23. Pr: 0.9702

TMHMM  Annotations     

There is no transmembrane helices in EPrPVT00000017090-p1.