CAZyme Information: PV10_06518-t45_1-p1

Basic Information

• Species: Exophiala mesophila
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala mesophila
• CAZyme ID: PV10_06518-t45_1-p1
• CAZy Family: GT15
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
2044		227535.13	6.0683

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EmesophilaCBS40295	9237	N/A	56	9181

• Gene Location: location=KN847523:4052954-4061084(-)

Full Sequence      

MLLQTFLFFVLLELGLATAPRPRQRYRYGDAGWPDDRTWQAFNESISGRLVRTFPSAAVC
HQDQYDADRCAEARADWSNSFWRTNQSGAYTAMAWELGDQQCFTNGSDTDPCEQGLVPYF
SVAAESVEDIQAAVKFASKKDLYLAVKNTGHDHLGRSSGQGSFSIWTHNLKGREWTNAFT
AQGAPPGTEGVPAVTLQAGEQWLDVYEAAAKQGVIVVGGHARTVGAAGGWLTGGGHSAWS
NLYGLGVDNLLQATLVNSCGDHVTINQYTDPDHFWALRGGGGSAWGVITSVTYKTHPEPA
NGIQVAVVQINATNQGSLRPVLEKALGAIVNVTDAGYTGYGFLLGGISAILIRPGGTEED
LEKCFASFSEVAQIEGASPVFFNITYPRWTDYTVDFLSDPNVAHNVMDASRLLTPSMAFD
KANEIVDLILEVGEEHAPFFNFIGHVNSDQREATSVHPVWREGRGVLSFGTDWEDTASED
EKKSKRDWLVKISQRWDEIAGATGGTYMNEANPYEPNWENAFWGSNYDRLLQIKRKLDPT
NLWGLYPAPDEASTDVDQHRDRDRQAGSAVNKRSPRFGHRFGHQQPTRNHPPSDSLHTSR
FRSTRENPRVDTDDEPLPASRERFAPVQKQHESAPQSAGHAQWSLIDADDDIYELTEIPH
LSNVTILPGDTAANEQLSDVQHPTSDRDHYFRGPASDIDFTTPSPVQTPILNPASDVDFT
TPSPIQTPILNPAFDVAFTTPSPIQSPILNPAGCLGKRTASSNELVANKRRLRVTQQAQK
ILSSPLTDNLDAKPYSLMSARHDDFLDYGTRARQSSIAPFLSTRISGRPDSATTMPDKEQ
SQDTQTSKNTRDDSGILNFDLDMPYNFLGTSQESIDPGLITTSPTLEEQEASAQKSRMLR
EKALGRASNLNVAMSTYDSITPESHPDQPPSDAHESTTQASSPGIGGDTRHVEEEGHSEN
QVDRHLQESDATHNDETPVNDIRQPQKSNAPDNETLLNDIRHSQESHPTNNDAPLNEMRR
PRPRPHGSHATNLEKHLNDIQRSHESNASDRGTHLKDIRRPRESHATNLEKHLNDIQRLH
ESNAVARGTHLKDIRRSHESNSTNLERPLNDIQPAHKSNNAAARETYLKDIRRPHESHAT
NGERPLNDIQRAHESNNAADPQTHLNNETHLNDIHCPQGSHPKNHDAPMNDIRRPPPPES
HATNHDIRRPRPPERHATNHGPSLKDILQPRPHKGHALDHPAPLNDRAHESHATNHDIRR
PQGSHPNNRDAPVNDVRRSESHATNNDAPLNNNQQHHRMSNTVDHGTHLNNIRRPHQSDV
TERERPLNDIHSTSATGKANDIHPTTSTREASDVHTTISPNTPNVAPRPSGFEMLAVRRG
NHFWSTNDHRGAAPAPVAVTHQDKANTPSKQKQPFGTRIPTQVADNLTEVLPNASPVKET
EQRLNHRLPLMNRNGGGRQATRATDVPDRPARGITLGEHSPSQDRPREVGGSSIEIARDA
VELTLPHRFDTWSEEGQQIIREHEIAKEANRDLEALFVAVGRIAQLRSFGFLKAIEEKEL
CSVQQFLDLVGRRRLSGKRQRPDISKISSRMRQRVTAAGGSLPTQNVVEQNIALLFPIEA
IQDARNQMADLKAKIERLGAKRQNISKHRALPSIQVTANRDNRESEGSQNLDIPANIPVN
ASRHSRTPQLETLGTPLALTVPSPRSSPPAAAAPALPTPVAAPRIRGSQGFDQGLLDRMR
KQSLAKQSQPEENQSGEEDEAASSSAETTTESDDDEADSDSDGETSGPSELFEYTVSSIY
AGVEDYDSGDEYICLKTTDVKKANQKVDKLATEFEKKYPPEEGLRFGRRSNRSSWENGLV
ERYVSLGEDEVREARFFVKRQIASVARSAYRIARTRDPVISRIFYKVEWEKVTEYEEQQE
QEEGEAQAEINWGPPERSTIPLHEILSFTTSAQANRHAADVWLAWYFRYFPGLEMEQQRR
LDAEEIERELEMKADFGLFAKEDSFYSGQVPENDGDGGELQTPQRVRETFKIWVRKDHVY
GPPN

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	122	303	1.6e-39	0.36681222707423583

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.48e-19	122	542	36	449	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	3.71e-19	122	266	5	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.
369658	BBE	9.34e-11	506	543	1	38	Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.
215242	PLN02441	0.005	126	289	73	232	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	3.98e-43	30	545	506	1046
QKD57322.1|CBM91|GH43_11	3.98e-43	30	545	506	1046
UJO23499.1|AA7	4.60e-13	100	543	43	477
QRW22693.1|AA7	1.21e-10	118	543	61	476
UQC87672.1|AA7	2.88e-10	118	547	70	492

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	1.71e-76	29	557	33	566	Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6F74_A	1.31e-56	29	543	35	576	Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6FYE_A	1.87e-14	118	545	45	455	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	3.28e-14	118	545	45	455	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]
6FYD_A	4.35e-14	118	545	45	455	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B1Z7|A2478_ARTBC	3.30e-191	29	543	32	551	Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02478 PE=1 SV=1
sp|D4AS41|A7056_ARTBC	2.40e-77	33	543	35	569	Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07056 PE=1 SV=2
sp|G2QDQ9|VAO15_MYCTT	8.79e-76	29	557	33	566	VAO-type flavoprotein oxidase VAO615 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=MYCTH_2305637 PE=1 SV=1
sp|A0A0E0RTV6|ZEB1_GIBZE	4.93e-74	29	543	32	541	FAD-linked oxidoreductase ZEB1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=ZEB1 PE=2 SV=2
sp|A1CFM2|PATO_ASPCL	6.63e-68	29	539	34	542	FAD-linked oxidoreductase patO OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=patO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000184	0.999779	CS pos: 17-18. Pr: 0.9724

TMHMM  Annotations     

There is no transmembrane helices in PV10_06518-t45_1-p1.