CAZyme Information: HMPREF1541_01906-t46_1-p1

Basic Information

• Species: Cyphellophora europaea
• Lineage: Ascomycota; Eurotiomycetes; ; Cyphellophoraceae; Cyphellophora; Cyphellophora europaea
• CAZyme ID: HMPREF1541_01906-t46_1-p1
• CAZy Family: AA6
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
523	KB822718|CGC4	57518.14	4.5298

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CeuropaeaCBS101466	11153	1220924	59	11094

• Gene Location: location=KB822718:1091357-1093287(-)

Full Sequence      

MKTPSKLALSALVAFSASATASWQDAGEGSQHCCQALADAGLGDRLILPDTADYEDRVDV
HWSLAARLTPYCFVRPETAGEVAKVVNTLVEANKTSPCQFAIRSGGHTTWAGSANIEDGV
TVDLGYMNSTTYNAENKTASVQPGARWKGVYSTLDALGIAAAGGRASTVGVAGLATGGGN
SFYGAREGFVCDNVVRFEVVLASGEIVEADRDNNVDLWQSLKGGSNNFGIVTRLDLATLE
GIDLWGGVVTYSNDTTKQQIQAMYNFGEEATNDRYASAITIWQYSTTTDTNMVINAYDYT
KPVARAPIFDEFLAIPGNTSDSLRFTNMTDLTIELEQAEGFRDSFFTLTFKNDIRVMEKA
IELHHQYLERLKAADIKGNWTLQDMFQPVPTFFAEHGEEKGGNVLGLGRFTDNLQLWQTY
LAWEDAAQDDMFHSWGMEYIAELDEFAKSVGADNSWIYLDYAYKTQDPLASYGEENLQKL
RDVSKKYDPEGVFQTMVPGGFKVSKAGKPEQTRGSKKMRKREL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	59	278	4.9e-49	0.47161572052401746

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	4.79e-24	42	493	6	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.29e-22	70	210	1	139	FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.
273751	FAD_lactone_ox	2.95e-08	61	289	6	231	sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.
215242	PLN02441	7.13e-07	67	233	62	233	cytokinin dehydrogenase
178402	PLN02805	1.59e-04	51	236	111	302	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA72155.1|AA7	5.36e-14	70	493	95	542
UJO18775.1|AA7	1.10e-13	34	242	38	242
QGA17347.1|AA7	3.03e-12	45	238	23	214
UJO16207.1|AA7	5.02e-12	62	502	120	556
ANH22774.1|AA7	3.17e-11	54	240	45	235

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO4_A	3.60e-16	35	233	16	210	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	3.60e-16	35	233	16	210	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6FYE_A	4.51e-16	36	235	12	205	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	1.06e-15	36	235	12	205	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
6FYG_A	1.88e-15	36	235	12	205	The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|C8VPE5|SDCF_EMENI	2.88e-120	30	506	5	479	FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	2.50e-118	28	511	39	521	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	5.26e-62	70	504	79	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A2G5ICA0|CTB5_CERBT	9.16e-61	30	503	41	524	FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1
sp|A0ST43|CTB5_CERNC	3.24e-56	68	503	12	456	FAD-dependent monooxygenase CTB5 OS=Cercospora nicotianae OX=29003 GN=CTB5 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000496	0.999455	CS pos: 21-22. Pr: 0.7823

TMHMM  Annotations     

There is no transmembrane helices in HMPREF1541_01906-t46_1-p1.