CAZyme Information: H257_04761-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_04761-t26_1-p1
• CAZy Family: GH18
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
663	KI913121|CGC2	72523.09	7.4596

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=KI913121:957752-961328(-)

Full Sequence      

MATPGRKKAATGASLLDALSPQLMSLVEASLGHSLAAPSSVRNGLSSANASPPPQRSTVQ
PPANRGESVIPQSRSSDYIRVGVLNPSEIFLLRQADSPGFVVREHFLGPAAATAVHDACL
GLTESTPMRPAQVGVGKSTAVTCHVADARGDQLVWLPHDKTALPPPLQHLLAQIERLMHG
LAKAAPELGVRNVKSTQLAVFPGHNTRFVPHVDTYDHNNNAKQHLSRRITCLYYLNPSWE
SSHGGALRMHLQDGTTWDIPPVLDTLVVFRSTDVLHEVLPTTVHRLALTTWYYGGGSATT
IPSTPPSATSPTPTTPSFATNIATRTTSSCVTGSNQPLEVAGGDATSTIFVSIPSYCDSE
CQPTVAHLFATAAAPSRVFVGLCLQHEQDDQSMDMYGEHVRIKRMRPADATGPCLARWET
QQLWKGEAFYLQIDSHMRFRRGWDVYLIDQLRRCSNSPQGRPRKAILTTYPLGYTLPNEI
PNDTRPTLLCASAFDSHGMLRQCGKVLKTSPSSPVPSAFWAAGFAFSRACVIQEVPYDPS
LAHLFFGEENVMAARLWTHGYDFYAPCEAVVYHLWSRSHRPTFTSPQRVDQAAKNASLER
VLALLLQAKENEPMVACGLGRERSIQDFHAAQGVNWSTHEIQWTSLWGHRDPIEFDLTAA
VDT

Enzyme Prediction     

EC	2.4.1.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GT60	348	635	1.3e-88	0.990909090909091

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
371506	GlcNAc	5.53e-68	348	628	1	341	Glycosyltransferase (GlcNAc). GlcNAc is an enzyme that carries out the first glycosylation step of hydroxylated Skp1, a ubiquitous eukaryotic protein, in the cytoplasm.
404519	2OG-FeII_Oxy_3	1.74e-21	197	293	2	94	2OG-Fe(II) oxygenase superfamily. This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.
214780	P4Hc	1.48e-14	134	292	20	164	Prolyl 4-hydroxylase alpha subunit homologues. Mammalian enzymes catalyse hydroxylation of collagen, for example. Prokaryotic enzymes might catalyse hydroxylation of antibiotic peptides. These are 2-oxoglutarate-dependent dioxygenases, requiring 2-oxoglutarate and dioxygen as cosubstrates and ferrous iron as a cofactor.
379319	2OG-FeII_Oxy_4	4.26e-10	226	292	22	92	2OG-Fe(II) oxygenase superfamily. This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily.
226274	EGL9	1.57e-09	146	292	88	238	Proline 4-hydroxylase (includes Rps23 Pro-64 3,4-dihydroxylase Tpa1), contains SM-20 domain [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA15104.1|GT60	7.52e-122	14	662	37	642
BDA44136.1|GT60	7.16e-72	149	641	107	588
AAK56291.1|GT60|2.4.1.-	6.96e-67	347	604	4	279
CAG4710602.1|GT60	1.83e-60	91	603	62	561
QNJ16416.1|GT60	1.57e-48	346	641	2	313

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4IW3_A	2.70e-15	99	297	43	226	Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) in complex with elongation factor Tu (EF-Tu) [Pseudomonas putida KT2440],4IW3_J Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) in complex with elongation factor Tu (EF-Tu) [Pseudomonas putida KT2440],4J25_A Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) [Pseudomonas putida KT2440],4J25_B Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) [Pseudomonas putida KT2440],4J25_C Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) [Pseudomonas putida KT2440],4J25_D Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) [Pseudomonas putida KT2440],4J25_E Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) [Pseudomonas putida KT2440],4J25_F Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) [Pseudomonas putida KT2440],4J25_G Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) [Pseudomonas putida KT2440],4J25_H Crystal structure of a Pseudomonas putida prolyl-4-hydroxylase (P4H) [Pseudomonas putida KT2440]
6EY1_A	1.30e-12	91	293	53	244	prolyl hydroxylase from Trichoplax adhaerens [Trichoplax adhaerens]
6F0W_A	1.30e-12	91	293	53	244	prolyl hydroxylase in complex with hypoxia inducible factor oxygen degradation domain peptide fragment from Trichoplax adhaerens [Trichoplax adhaerens]
6NMQ_A	2.16e-12	99	293	27	212	Hypoxia-Inducible Factor (HIF) Prolyl Hydroxylase 2 (PHD2) in Complex with the Carboxamide Analog JNJ43058171 [Homo sapiens]
3OUI_A	2.16e-12	99	293	27	212	PHD2-R717 with 40787422 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8T1C6|GNT1_DICDI	1.73e-67	347	583	4	257	[Skp1-protein]-hydroxyproline N-acetylglucosaminyltransferase OS=Dictyostelium discoideum OX=44689 GN=gnt1 PE=1 SV=2
sp|Q91UZ4|EGLN3_MOUSE	9.68e-17	99	293	27	213	Prolyl hydroxylase EGLN3 OS=Mus musculus OX=10090 GN=Egln3 PE=1 SV=1
sp|Q9H6Z9|EGLN3_HUMAN	2.40e-16	99	293	27	213	Prolyl hydroxylase EGLN3 OS=Homo sapiens OX=9606 GN=EGLN3 PE=1 SV=1
sp|Q62630|EGLN3_RAT	5.97e-16	99	293	27	213	Prolyl hydroxylase EGLN3 OS=Rattus norvegicus OX=10116 GN=Egln3 PE=1 SV=2
sp|G5EBV0|EGL9_CAEEL	1.01e-12	91	292	367	564	Hypoxia-inducible factor prolyl hydroxylase OS=Caenorhabditis elegans OX=6239 GN=egl-9 PE=1 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 H257_04761-t26_1-p1.