CAZyme Information: H257_18485-t26_1-p1

Basic Information

• Species: Aphanomyces astaci
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces astaci
• CAZyme ID: H257_18485-t26_1-p1
• CAZy Family: GT8
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
754		84599.74	7.5192

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=KI913282:4098-7014(-)

Full Sequence      

MLHRARRPGFQAIKRERCIQWACSGQRSFSEGHQASIPMSLVQGGERILRESSPTNKVLQ
SLNVQALWQTGKLPLIHTSTWSPNPPDFPSRPPQPLLYDPKDMPSEKGFPIPVAILHALA
HIELGAMDNYWDTIVRFGPSQSDGLCELPRAFYDDFLNVACDEARHFELVTGRLHELGSF
YGQLPAHQALLAHAHNTQNCLAARLAVIPLVQEARGLDAGPRLVHKLKSLGDRESADIVA
QIVFEERGHVSCGIKWFKHLCASTKRDPVGYFHELVKGTFPEGLPGPFDLEARLAANMDP
TWYQPLEMPKKPTIILDKPVNPVIPLRKKNGKAILIAGSVWPERTSSAAGVRTCDMIDIL
LDEGWDVVCISPSRLNAHTRALAATGVHCEQVDPNKEEALEAFMCSRETPVHVALFDRYI
AEEMYGWQVTKLAPHALRVLDLQDVHFLRKAREFHVCTDKKDYRTTLQPSIDVEPVASVV
LRELASVYRSHVTLYVSEFEKTMLTTRFDVPPRRLRKLDYIVPDDKLNQFPLNFKDRRHV
AVVGSFKHAPNVDGLHWLKDTLWPTMRQSLPPHTELHMYGSYASAKAIKSLHNPHMNVHV
MGFCDDVHETLASYRVSLAPLRFGAGIKGKIIDSWAAGTPVVSTSVGAEGMHYHPNQPWG
GAVADSPAEFADRVAALYGNADEWTAAYEGGKVLCRTHYDLDSQRRTLLDVVGSPTDVDN
WVGRVLESSQFRATEYMSRFIQEKNKNLTRTPQL

Enzyme Prediction     

No EC number prediction in H257_18485-t26_1-p1.

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
398135	DUF455	1.79e-97	50	304	1	243	Protein of unknown function (DUF455).
225389	COG2833	1.80e-61	39	307	3	263	Uncharacterized conserved protein, contains ferritin-like DUF455 domain [Function unknown].
404563	Glyco_trans_1_4	3.28e-18	537	680	1	138	Glycosyl transferases group 1.
340831	GT4_PimA-like	4.28e-17	334	711	2	364	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.
153097	Ferritin_like	6.64e-10	114	257	1	130	Ferritin-like superfamily of diiron-containing four-helix-bundle proteins. Ferritin-like, diiron-carboxylate proteins participate in a range of functions including iron regulation, mono-oxygenation, and reactive radical production. These proteins are characterized by the fact that they catalyze dioxygen-dependent oxidation-hydroxylation reactions within diiron centers; one exception is manganese catalase, which catalyzes peroxide-dependent oxidation-reduction within a dimanganese center. Diiron-carboxylate proteins are further characterized by the presence of duplicate metal ligands, glutamates and histidines (ExxH) and two additional glutamates within a four-helix bundle. Outside of these conserved residues there is little obvious homology. Members include bacterioferritin, ferritin, rubrerythrin, aromatic and alkene monooxygenase hydroxylases (AAMH), ribonucleotide reductase R2 (RNRR2), acyl-ACP-desaturases (Acyl_ACP_Desat), manganese (Mn) catalases, demethoxyubiquinone hydroxylases (DMQH), DNA protecting proteins (DPS), and ubiquinol oxidases (AOX), and the aerobic cyclase system, Fe-containing subunit (ACSF).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UIZ27514.1|GT4	7.25e-215	111	750	13	665
CCA13921.1|GT4	2.33e-103	298	744	1	450
SDV03690.1|GT4	6.11e-87	334	747	9	429
ARU90469.1|GT4	4.23e-86	334	746	4	425
BBP59536.1|GT4	3.93e-82	334	747	9	429

PDB Hits     

H257_18485-t26_1-p1 has no PDB hit.

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P43935|Y077_HAEIN	3.33e-25	92	297	60	266	Uncharacterized protein HI_0077 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_0077 PE=4 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_18485-t26_1-p1.