CAZyme Information: RQM15764.1

Basic Information

• Species: Peronospora effusa
• Lineage: Oomycota; NA; ; Peronosporaceae; Peronospora; Peronospora effusa
• CAZyme ID: RQM15764.1
• CAZy Family: GT2
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1526	QKXF01000144|CGC1	172551.69	6.4872

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PeffusaR13	8603	N/A	0	8603

• Gene Location: location=QKXF01000144:67531-72506(-)

Full Sequence      

MTTEANTSHGALWAAAFGLQGDIQLAQRERYERLKQHMVFQIDATGTTDPLTVTKDVVNS
SSNWSQYFTDETLLEEIKTDLDRLYPFGNENLFQNERCMTMLRHVLFVWCRLHPDVAYRQ
GMHDVVAVVLFALMQTQETESVDVKKLPESTEADTFLLFEAVMLFLKPFYEIVEMRQKGE
DEEEERRLFASFSFQKDDSRNGVQSFETTTEKQKQPALHRLCHHIQYELLQQKDPQLYYH
LKNLEIIPETYCLRWIRLLFAREYTLKDLLCVWDALILDSRRAVIDFPVINMTEKSDNDL
LQLPKLVAGSEETTWTGFPLLRYVCAARLLQMSTQLRQSDNTDCLRILMRTCQEKDLNST
DLERQSRAVELTKFARILQTPMTEETVESENGIKSNDEEEVVAPDGGSKLVEVVLFREGS
LGIVLAMAEAPYENRLAVKAFTKDPNRSDGAGQAKASGKVHLGDLLQSINGVPIVDVTTE
EVKRRLQLIDRPVYIAFSRYKGAYDNCEVTTSEHSAAVKDSDAPDSPPSLEITMTELVQP
ALLPGELCYANVETSMQRLVLSHDGSCLSHYISGKLFITNYRCFFTRLLGRGEVEWQIPV
LSILSIDRIDPRAISSAVGSTTLSVENAQVAFGFTPDDSYKVVIRCKDTQVARLSIADHD
EYEKLVQCLSFLAFPKSLLDAFCFAYSPTVAPSEEVRFNIRQEYKRIGLLSFPDHLRCID
QSSKYTLCETYPRHLIVPADISDIRLKAAAAFRSHQRLPVISWIHPSTGATIVRSSQPLV
GLKSARNGEDELLVFLLCCSSNTKAFGRYVIMDARSQLAAVRNKALGKGTENSSNYHGAK
LIFMNVENIHAVRQSQLALAATFEPKRSANEDTSSFYGRIESSGWLRHVRLVLKASVDLA
YTVHNGRSVLTHCSDGWDRTAQMVALAELMLDPYYRTLCGFQVLVEKEWCAFGHQFALRC
GHARSDVSNDQRSPVFLLWIDCVWQYIRQYPTECEFNESFLLALADHVYSCKFGTFMFDC
ERQRKDLFTKHRVLSIWSEINSQSDRFTNHMYAPSEQATVLAPSTLSKNIKLWKGYFCRW
DPTFVPPVPAFQCIFIVWAFFRGLSCSIPRAVRPSEEITRLRVGFLHPDFGIGGAENLVV
NAAVALQHRGAYVTVFTAHHDVNHCFEETRDNGPLASHVRVYGDWLPRTILGKLYAFCAL
LRVLYVTLCIAVYDIDDLDVFVVDQVSISIPFLRAMGKPVLFYGHFPDKLLCIPSDSPWK
RMYRVPLDFLEEITTASSDIIVANSKFSRGVFHEVFPRLQMKKVGILYPPVDIKAYKATA
EASVERDSGLFVSLNRFERKKNVALAIEALVELRHKVPSEEFKRVKLIVAGGYDPLNTEN
QEHLIELQDVVAKHGLGDHVEFRTSVSNSMKLELLRKAHAILYTPDREHFGIVPIEAMAC
GTPVIAVSSGGPLESIADGETGFLCEQKPKAFAKAMAKLCGPKHSTRVVEMGVCGRLRAQ
KLFSLETFGDALLELVNEAVYGEKAA

Enzyme Prediction     

EC	2.4.1.257:6	2.4.1.132:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT4	1330	1480	5.3e-39	0.8625

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
340834	GT4_ALG2-like	5.80e-177	1121	1512	1	392	alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.
399535	Myotub-related	6.86e-165	698	1025	8	330	Myotubularin-like phosphatase domain. This family represents the phosphatase domain within eukaryotic myotubularin-related proteins. Myotubularin is a dual-specific lipid phosphatase that dephosphorylates phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bi-phosphate. Mutations in gene encoding myotubularin-related proteins have been associated with disease.
350357	PTP-MTM-like	1.76e-116	756	985	1	226	protein tyrosine phosphatase-like domain of myotubularins. Myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. Not all members are catalytically active proteins, some function as adaptors for the active members.
350380	PTP-MTMR6-like	3.00e-112	700	1010	1	301	protein tyrosine phosphatase-like domain of myotubularin related phosphoinositide phosphatases 6, 7, and 8. This subgroup of enzymatically active phosphatase domains of myotubularins consists of MTMR6, MTMR7 and MTMR8, and related domains. Beside the phosphatase domain, they contain a C-terminal coiled-coil domain and an N-terminal PH-GRAM domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively. MTMR6, MTMR7 and MTMR8 form complexes with catalytically inactive MTMR9, and display differential substrate preferences. In cells, the MTMR6/R9 complex significantly increases the cellular levels of PtdIns(5)P, the product of PI(3,5)P(2) dephosphorylation, whereas the MTMR8/R9 complex reduces cellular PtdIns(3)P levels. The MTMR6/R9 complex serves to inhibit stress-induced apoptosis while the MTMR8/R9 complex inhibits autophagy.
350383	PTP-MTM1-like	1.81e-90	757	1009	2	249	protein tyrosine phosphatase-like domain of myotubularin, and myotubularin related phosphoinositide phosphatases 1 and 2. This subgroup of enzymatically active phosphatase domains of myotubularins consists of MTM1, MTMR1 and MTMR2. All contain an additional N-terminal PH-GRAM domain and C-terminal coiled-coiled domain and PDZ binding site. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. They dephosphorylate the D-3 position of phosphatidylinositol 3-phosphate [PI(3)P] and phosphatidylinositol 3,5-bisphosphate [PI(3,5)P2], generating phosphatidylinositol and phosphatidylinositol 5-phosphate [PI(5)P], respectively.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ22829.1|GT4	7.65e-300	1094	1526	21	453
CCA25726.1|GT4	7.37e-150	1094	1518	20	447
AWO96647.1|GT4	1.11e-104	1122	1512	4	397
AAH92211.1|GT4	2.44e-103	1125	1521	7	404
AAH77444.1|GT4	1.65e-102	1120	1512	2	395

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1ZSQ_A	7.96e-104	534	1082	1	516	Chain A, Myotubularin-related protein 2 [Homo sapiens],1ZVR_A Chain A, Myotubularin-related protein 2 [Homo sapiens]
1LW3_A	9.24e-104	506	1089	44	595	Chain A, Myotubularin-related protein 2 [Homo sapiens],1M7R_A Chain A, Myotubularin-related Protein-2 [Homo sapiens],1M7R_B Chain B, Myotubularin-related Protein-2 [Homo sapiens]
5GNH_A	1.47e-103	539	1089	3	520	Myotubularin-related protein 2 [Homo sapiens],5GNH_B Myotubularin-related protein 2 [Homo sapiens]
5C16_A	1.35e-102	542	1092	6	522	Myotubularin-related proetin 1 [Homo sapiens],5C16_B Myotubularin-related proetin 1 [Homo sapiens],5C16_C Myotubularin-related proetin 1 [Homo sapiens],5C16_D Myotubularin-related proetin 1 [Homo sapiens]
2YF0_A	3.99e-95	642	1083	68	505	Human Myotubularin related protein 6 (MTMR6) [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q13496|MTM1_HUMAN	2.35e-109	572	1082	59	543	Myotubularin OS=Homo sapiens OX=9606 GN=MTM1 PE=1 SV=2
sp|Q5R9S3|MTM1_PONAB	2.35e-109	572	1082	59	543	Myotubularin OS=Pongo abelii OX=9601 GN=MTM1 PE=2 SV=1
sp|A6QLT4|MTM1_BOVIN	8.43e-109	572	1082	59	543	Myotubularin OS=Bos taurus OX=9913 GN=MTM1 PE=2 SV=2
sp|Q9Z2C5|MTM1_MOUSE	2.04e-107	543	1082	38	543	Myotubularin OS=Mus musculus OX=10090 GN=Mtm1 PE=1 SV=2
sp|Q52KU6|MTM1_XENLA	2.34e-105	572	1082	58	542	Myotubularin OS=Xenopus laevis OX=8355 GN=mtm1 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000053	0.000000

TMHMM  Annotations     

There is no transmembrane helices in RQM15764.1.