CAZyme Information: H310_03448-t26_1-p1

Basic Information

• Species: Aphanomyces invadans
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces invadans
• CAZyme ID: H310_03448-t26_1-p1
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1426		156480.39	8.0384

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AinvadansNJM9701	15416	N/A	168	15248

• Gene Location: location=KI913956:1347842-1353447(-)

Full Sequence      

MAAASMRKTLFRNKAAASNVIFVNGIPLSKDILEDPSNNDAPVQEHEAFLDAAEMFKKYD
RDKSGGIDMAEFMVLLQDLNFDIPDGKAVVYFRKCDVAQKGYITFDEFRVALFTCDPSNP
ARTGGFCPGKALTPKDIFTMFDADDSGEIGRDEFERVLKFLSIKMPLDKMESIFSQHENP
DSEALDYKSFRTIWLTLVDVRKELQLRNIPHNKLLPKSVLAKKLEGILDKEDAQEQYTID
EAKWNIQWEQIRSDRDQLVRKAKRFANYILGDTLDAAGQVYVFGRGSFNRFDGAPATKDF
VECPYFEKLLALWTARVRGADEWSPLVASHPSTKSAGWESAAKKQEQELQAKLAAVAAKK
LDAVETQQLSFQNRMVAVNTAWLWGRRIKHVSCGSTVAYALTDTGELYCWGGSQRRWNYL
YEPNDETVPLANRPFTARTEQLKLVAPAQVRRDAHMHEQNYVRNMFRANAPPAPPVVSPD
QQRKGAVAIVEYFNLGQTMPPDVRAALPLDKLQEIIEFDLSADLAANAMRLRGLAVHDAG
KQAIVDDLSKVLALEIECMGAPFHDRMKRLDLKYKQALHNNNAKLVAELLKRGATTWRGM
RKLHHAIDDVVKAEFQAKQDNWNAKRDEIRRVRLKQDRIGRENAEPASTNPALRTIEVSG
LTSRGPPQKQFHGGHALQEISVGAKHALAVHASGKIYGWGFGTFGRLGTGVHADLPVPQP
MAQLDSMRFRSVAAGYSHSLALRNDGQVFVWGSAATGKLGLEPDVPLRPRTTPVGHRHMS
KQPASSLLSTNGVDLDITDCFTIMPLPLSLPAAVRKIACGPSHSAAVTANGELFVWGSGD
GGRLGLGDGRIMDTDNELKGGLLGVLTAPTLVTSLTGQFIVDVSCGVSHTAALTAIEADM
ARGSKGGHLYVCGSAHALGKFCPVFVALPQLKGVPISNVSCGNAHTAAVSTDGEIYTWGN
NTGGCTGHTLVHRYVKAPTKLHCMYQMPENMARHTKYTVAAVQSSVNSGYSAAMALDGNT
DGQFESSCSQTFCEICPFWQVDLGVHCRVDTIRVWNRTGADGQRLFPCCVMVSESPFEPE
SGKFMLRTCKAQSVWTKFGDDCAAQNPLVWHAPEGTLGRFVRVQVEATTTLSLAQVEVLG
VEASKCVGPKASSVACGDDVTMVVCRPNVVQSEIDKKFLRALCADIDHLDVLKEYLAFAP
SVQKFAGDVRPHITPCLLCTAQYTCPICVLFKQIPSTSLPPDVRATTSLDTFSDMLLSHR
PPRTFATSAATVMMTDDANRLLQIAVDDEKPESDLAKAQDAVFATVHKAVTTTAHLVQSN
STAVQKIHAAAADHLQKLQDQARPMSRSFLRNAMASSKETWQKYTSGKPPREKYTPSGQG
GNADVIRVQPKSASRPPLDDDTAPLNKPRTRHAATSRLLNGRPVAE

Enzyme Prediction     

No EC number prediction in H310_03448-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
CBM47	1003	1136	1.1e-21	0.9765625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
227511	ATS1	4.16e-21	685	968	59	318	Alpha-tubulin suppressor and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton].
227511	ATS1	1.44e-20	679	961	108	419	Alpha-tubulin suppressor and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton].
227511	ATS1	7.67e-17	680	886	236	455	Alpha-tubulin suppressor and related RCC1 domain-containing proteins [Cell cycle control, cell division, chromosome partitioning, Cytoskeleton].
395335	RCC1	7.81e-13	693	742	1	50	Regulator of chromosome condensation (RCC1) repeat.
320029	EFh_PI-PLC	1.06e-09	54	190	4	129	EF-hand motif found in eukaryotic phosphoinositide-specific phospholipase C (PI-PLC, EC 3.1.4.11) isozymes. PI-PLC isozymes are signaling enzymes that hydrolyze the membrane phospholipids phosphatidylinositol-4,5-bisphosphate (PIP2) to generate two important second messengers in eukaryotic signal transduction cascades, Inositol 1,4,5-trisphosphate (InsP3) and diacylglycerol (DAG). InsP3 triggers inflow of calcium from intracellular stores, while DAG, together with calcium, activates protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity. Calcium is required for the catalysis. This family corresponds to the four EF-hand motifs containing PI-PLC isozymes, including PI-PLC-beta (1-4), -gamma (1-2), -delta (1,3,4), -epsilon (1), -zeta (1), eta (1-2). Lower eukaryotes such as yeast and slime molds contain only delta-type isozymes. In contrast, other types of isoforms present in higher eukaryotes. This family also includes 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1 (PLC1) from fungi. Some homologs from plants contain only two atypical EF-hand motifs and they are not included. All PI-PLC isozymes except sperm-specific PI-PLC-zeta share a core set of domains, including an N-terminal pleckstrin homology (PH) domain, four atypical EF-hand motifs, a PLC catalytic core, and a single C2 domain. PI-PLC-zeta lacks the PH domain. The PLC catalytic core domain is a TIM barrel with two highly conserved regions (X and Y) split by a highly degenerate linker sequence. Most of EF-hand motifs found in PI-PLCs consist of a helix-loop-helix structure, but lack residues critical to metal binding. Moreover, the EF-hand region of most of PI-PLCs may have an important regulatory function, but it has yet to be identified. However, PI-PLC-zeta is a key exception. It is responsible for Ca2+ oscillations in fertilized oocytes and exhibits a high sensitivity to Ca2+ mediated through its EF-hand domain. In addition, PI-PLC-eta2 shows a canonical EF-loop directing Ca2+-sensitivity and thus can amplify transient Ca2+ signals. Also it appears that PI-PLC-delta1 can regulate the binding of PH domain to PIP2 in a Ca2+-dependent manner through its functionally important EF-hand domains. PI-PLCs can be activated by a variety of extracellular ligands, such as growth factors, hormones, cytokines and lipids. Their activation has been implicated in tumorigenesis and/or metastasis linked to migration, proliferation, growth, inflammation, angiogenesis and actin cytoskeleton reorganization. PI-PLC-beta isozymes are activated by G-protein coupled receptor (GPCR) through different mechanisms. However, PI-PLC-gamma isozymes are activated by receptor tyrosine kinase (RTK), such as Rho and Ras GTPases. In contrast, PI-PLC-epsilon are activated by both GPCR and RTK. PI-PLC-delta1 and PLC-eta 1 are activated by GPCR-mediated calcium mobilization. The activation mechanism for PI-PLC-zeta remains unclear.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ARF14915.1|CBM48	4.40e-18	680	964	41	328
ARF18102.1|CBM48	3.91e-17	680	964	39	326
BAK17762.1|CBM48	1.36e-15	651	976	23	334
ARD48911.1|CBM48	2.12e-14	658	964	84	339
ARK25401.1|CBM48	1.09e-13	658	964	84	339

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4DNU_A	6.08e-30	666	967	49	300	Crystal structure of the W285A mutant of UVB-resistance protein UVR8 [Arabidopsis thaliana]
4DNV_A	1.07e-29	666	967	47	298	Crystal structure of the W285F mutant of UVB-resistance protein UVR8 [Arabidopsis thaliana],4DNV_B Crystal structure of the W285F mutant of UVB-resistance protein UVR8 [Arabidopsis thaliana],4DNV_C Crystal structure of the W285F mutant of UVB-resistance protein UVR8 [Arabidopsis thaliana],4DNV_D Crystal structure of the W285F mutant of UVB-resistance protein UVR8 [Arabidopsis thaliana]
4NC4_A	1.22e-29	666	967	46	297	Crystal structure of photoreceptor AtUVR8 mutant W285F and light-induced structural changes at 120K [Arabidopsis thaliana],4NC4_B Crystal structure of photoreceptor AtUVR8 mutant W285F and light-induced structural changes at 120K [Arabidopsis thaliana],4NC4_C Crystal structure of photoreceptor AtUVR8 mutant W285F and light-induced structural changes at 120K [Arabidopsis thaliana],4NC4_D Crystal structure of photoreceptor AtUVR8 mutant W285F and light-induced structural changes at 120K [Arabidopsis thaliana]
4DNW_A	1.55e-29	666	967	47	298	Crystal structure of UVB-resistance protein UVR8 [Arabidopsis thaliana],4DNW_B Crystal structure of UVB-resistance protein UVR8 [Arabidopsis thaliana]
4NAA_A	1.64e-29	666	967	46	297	Crystal structure of UVB photoreceptor UVR8 from Arabidopsis thaliana and UV-induced structural changes at 120K [Arabidopsis thaliana],4NAA_B Crystal structure of UVB photoreceptor UVR8 from Arabidopsis thaliana and UV-induced structural changes at 120K [Arabidopsis thaliana],4NAA_C Crystal structure of UVB photoreceptor UVR8 from Arabidopsis thaliana and UV-induced structural changes at 120K [Arabidopsis thaliana],4NAA_D Crystal structure of UVB photoreceptor UVR8 from Arabidopsis thaliana and UV-induced structural changes at 120K [Arabidopsis thaliana],4NBM_A Crystal structure of UVB photoreceptor UVR8 and light-induced structural changes at 180K [Arabidopsis thaliana],4NBM_B Crystal structure of UVB photoreceptor UVR8 and light-induced structural changes at 180K [Arabidopsis thaliana],4NBM_C Crystal structure of UVB photoreceptor UVR8 and light-induced structural changes at 180K [Arabidopsis thaliana],4NBM_D Crystal structure of UVB photoreceptor UVR8 and light-induced structural changes at 180K [Arabidopsis thaliana],6DD7_A Crystal structure of plant UVB photoreceptor UVR8 from in situ serial Laue diffraction [Arabidopsis thaliana],6DD7_B Crystal structure of plant UVB photoreceptor UVR8 from in situ serial Laue diffraction [Arabidopsis thaliana],6DD7_C Crystal structure of plant UVB photoreceptor UVR8 from in situ serial Laue diffraction [Arabidopsis thaliana],6DD7_D Crystal structure of plant UVB photoreceptor UVR8 from in situ serial Laue diffraction [Arabidopsis thaliana]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9FN03|UVR8_ARATH	2.40e-28	666	967	58	309	Ultraviolet-B receptor UVR8 OS=Arabidopsis thaliana OX=3702 GN=UVR8 PE=1 SV=1
sp|Q9FJG9|RUG3_ARATH	5.40e-25	680	984	106	363	RCC1 domain-containing protein RUG3, mitochondrial OS=Arabidopsis thaliana OX=3702 GN=RUG3 PE=1 SV=1
sp|Q9VR91|HERC2_DROME	1.23e-24	679	981	4086	4340	Probable E3 ubiquitin-protein ligase HERC2 OS=Drosophila melanogaster OX=7227 GN=HERC2 PE=1 SV=3
sp|O95714|HERC2_HUMAN	3.60e-24	679	968	3989	4231	E3 ubiquitin-protein ligase HERC2 OS=Homo sapiens OX=9606 GN=HERC2 PE=1 SV=2
sp|Q4U2R1|HERC2_MOUSE	4.71e-24	679	968	3991	4233	E3 ubiquitin-protein ligase HERC2 OS=Mus musculus OX=10090 GN=Herc2 PE=1 SV=3

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000043	0.000000

TMHMM  Annotations     

There is no transmembrane helices in H310_03448-t26_1-p1.