CAZyme Information: PPTG_08735-t26_1-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_08735-t26_1-p1
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
909		102679.44	5.2191

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PparasiticaINRA-310	23240	761204	119	23121

• Gene Location: location=KI669576:220308-223373(+)

Full Sequence      

MVLAPNDKMLGCSQVSDKKFSNFENTAVIVRRGECSFQEKIVNVAVKDAALMILVNSEDT
LIPLSSLEYEHVTTAAVSVTLSDGEKLIEMVKRRDELTGIELKIETISLANQARTRLQFL
VDINAPVAVYEEFKYVMEQLEPMVGTLDGLLSMIWTEEYERVGTVHSDAEAKELMEFLPF
CVKQLSKWSFASEAALHASVAAAVLQIQLWNNESQTDSRKERLLVRTAARKLMESGYYSH
SFSLLQKIPASSDNRSDTSIQCMLSFLKFLQGDVITSLSETSACQTLKFDAGTPSLKVAE
GAFNRLTKLERSSHDEECLGLAAGLVNDTNLALACCYPNERTGTLSREFSSEFTKEFFHS
LVMMGVFLDELGPFEESLRFFGYAARMCPGDSTTLELRQLLAVPVVFSSQNELDLFIAEL
KSKLNIFTETLAIKHELEERVVSPLEIADESNEAALSITGPVLRPEEAAYLQYTITPPTM
FIGYQGVDVLPIQEAINRLRSLVYPSLTSSFEPQNPDRSEETLIPGDDHKRRRVGFISSW
FRSHSVGKLLLGVVQNLDRAKFHVIIYRCVHFLRDGDKISELFKHTADEYVELPETQDPA
VHILRQAQLDIAIFPELGMDEWTVLLSHHRVAPIQCVFWGHPITTGNPNIDYFISSEHFV
SDNFDEPTESTPVNEQLKLSGYRRSSFSEQIVLFRGLSTIFTEPNPLTIESREITRSRLY
LPTNRRLYVCPQTLMKLHPAFDEALARILERDNKATIVLLASNTQLVWMEKVRRRFRQRF
GRNHRLVLFLPTLPFTEFQALLAHADVVLDPFPFGGGVTTLDALHLGIPVITLPAAQSVV
HLAAGFLRYMNASDCIAKSLDEYVHLAVSVAMDHQDIRKRLLLHRNDIYQDVSTIDDWNT
FLDTVYPLH

Enzyme Prediction     

No EC number prediction in PPTG_08735-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT41	353	878	2.2e-65	0.46382978723404256

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226428	Spy	4.00e-38	475	899	201	599	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
238300	PA	1.17e-06	2	98	23	123	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.
340831	GT4_PimA-like	5.55e-06	533	832	1	296	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.
239039	PA_PoS1_like	1.36e-05	4	92	39	120	PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 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.
239044	PA_hSPPL_like	2.36e-05	16	73	36	94	PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AIG55953.1|GT41	6.25e-147	7	905	64	874
QDU81044.1|GT41	9.97e-73	475	905	627	1023
QDU48009.1|GT41	1.88e-67	475	904	526	921
QDV15686.1|GT41	1.88e-67	475	904	526	921
QDT25015.1|GT41	1.88e-67	475	904	526	921

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5DJS_A	5.13e-22	522	873	153	478	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]
3Q3E_A	6.79e-16	612	885	351	597	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]
2VSN_A	1.65e-14	533	909	207	563	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]
2JLB_A	6.61e-14	533	909	207	563	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]
5NPR_A	8.39e-09	715	879	507	668	The human O-GlcNAc transferase in complex with a thiol-linked bisubstrate inhibitor [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A3N2T3|NGT_ACTP2	3.42e-15	612	885	340	586	UDP-glucose:protein N-beta-glucosyltransferase OS=Actinobacillus pleuropneumoniae serotype 5b (strain L20) OX=416269 GN=APL_1635 PE=1 SV=1
sp|B3H2N2|NGT_ACTP7	7.84e-15	612	885	340	586	UDP-glucose:protein N-beta-glucosyltransferase OS=Actinobacillus pleuropneumoniae serotype 7 (strain AP76) OX=537457 GN=APP7_1697 PE=1 SV=1
sp|Q96301|SPY_ARATH	7.44e-14	527	873	478	803	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Arabidopsis thaliana OX=3702 GN=SPY PE=1 SV=1
sp|Q9M8Y0|SEC_ARATH	1.55e-12	530	873	590	914	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
sp|O82039|SPY_PETHY	3.44e-12	527	873	483	808	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Petunia hybrida OX=4102 GN=SPY PE=2 SV=1

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 PPTG_08735-t26_1-p1.