CAZyme Information: H257_07704-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_07704-t26_1-p1
• CAZy Family: GH43
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
951		104936.38	6.4742

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AastaciAPO3	19584	N/A	465	19119

• Gene Location: location=KI913129:677642-681029(-)

Full Sequence      

MKPPMRLLVLVALHLVPTWCRRGHRPIVQPDGNNGGCMLAFGIDGLQMPCQVADFGGFVR
PSVSQPVRVVLADPLHACPSSSSNVVPSINADDEPTDVLVVVVRGDCSFVDKMEYVERWG
GRYMVLVNSDNTFLRMQTPQWVESGTVAVAVRQNDGVRLIDLARNSTTLSFLSPLFTITL
QPNVLQCLHRIEALLAINAPRTAVDTFALCAPHATITSVVSKFPPRLDQTPSPNEEYAGF
YNQVASLFRQSPFHSTDFVRHVLLESSYFAVYYAASATALQYHNLGTASLLTGHFHMAAS
NFVLTSTANSVTTCDAALAFFLAGDYIPAHKWYSQCNIGLLPLLSTQRLNMLTYCSSAAS
STHSYDVPAASLRSLFASPLTPSDVACLVAATTADTQPSNATCCSPRWDVHMGVTLHFDS
VFVQNLYETITLMGVFLDELGAFHESLVHFGHGLRLCGKASGLHIRMATSVPIVFDSKVD
MDTFILDFPRRVLSLDMLGVSHDVARYNRPEFAGHLQWTITPPTMFVGYQGVDVAPLQAA
VATMYDRLYPVLSRPLDSLPPPPLQIPNKTTVGFVSSWFRTHSVGKLIQRVIESLDRDRF
EVVVFAASHFFPLKGDDDPITTAIERAANRFVQLPSDQEMAMHVLLREDLDVLVYPEVGM
DAWVYFLAGRRLARVQCMFWGHPITTGLSTIDYFIASEYFFSDFYDAGGQPNPHSDYHMY
GGASYSEQLVLFADLSTYFPPPAAAVPPDPSSSVRAMLHLPPSPSRIYLCPQTLMKLHVD
FDAAILGILDRDPGGTIVLLYSNKQVLWKDQVHRRLRQSTLGRRVVFIETMPYAMFMQLL
AAVDVMVDPFPFGGGVTTLDALAVGLPVITLPSRQTVLQLAAGFYRYMSVSDSLVAASVD
EFVTFAVAMATNATLKGATQAAIRHRYHVLFHDDNSSKTHTEWNTFLANIT

Enzyme Prediction     

No EC number prediction in H257_07704-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT41	425	927	7.2e-60	0.47375886524822697

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
226428	Spy	2.11e-32	565	926	255	591	Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones].
239039	PA_PoS1_like	1.56e-05	91	171	48	129	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.
238300	PA	1.87e-05	89	171	39	124	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	3.01e-05	572	870	2	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.
239042	PA_hPAP21_like	2.88e-04	54	131	1	69	PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted glycoprotein hPAP21 (human protease-associated domain-containing protein, 21kDa). This group contains various PA domain-containing proteins similar to hPAP21. Complex N-glycosylation may be required for the secretion of hPAP21. The significance of the PA domain to hPAP21 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	8.28e-195	30	950	25	874
UEM20219.1|GT41	4.01e-60	458	936	236	673
BBO34148.1|GT41	1.43e-58	464	934	513	937
UEM04243.1|GT41	1.55e-57	432	936	380	842
UEM20228.1|GT41	1.55e-57	450	936	398	842

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5DJS_A	9.53e-12	546	909	145	475	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	1.49e-11	594	912	289	588	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	7.57e-11	594	912	278	577	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	7.57e-11	652	912	341	577	UDP-glucose:protein N-beta-glucosyltransferase OS=Actinobacillus pleuropneumoniae serotype 7 (strain AP76) OX=537457 GN=APP7_1697 PE=1 SV=1
sp|Q9M8Y0|SEC_ARATH	3.97e-08	568	912	590	914	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SEC OS=Arabidopsis thaliana OX=3702 GN=SEC PE=1 SV=1
sp|Q96301|SPY_ARATH	8.78e-08	545	924	463	815	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Arabidopsis thaliana OX=3702 GN=SPY PE=1 SV=1
sp|Q8RVB2|SPY_SOLLC	2.63e-07	565	924	482	820	Probable UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase SPINDLY OS=Solanum lycopersicum OX=4081 GN=SPY PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000390	0.999585	CS pos: 20-21. Pr: 0.9771

TMHMM  Annotations     

There is no transmembrane helices in H257_07704-t26_1-p1.