CAZyme Information: PV07_04108-t44_1-p1

Basic Information

• Species: Cladophialophora immunda
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora immunda
• CAZyme ID: PV07_04108-t44_1-p1
• CAZy Family: GH127
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1499	KN847041.1|CGC4	166227.79	7.5544

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CimmundaCBS83496	12879	N/A	49	12830

• Gene Location: location=KN847041.1:5406285-5413818(-)

Full Sequence      

MDRLTSWASSMIVLFFIVSLKQVRAGPATYCKPIPSSSNWPAQSAWQELNMTVSGKLFVD
IPPGSVCHPENILFDNTTCALVLSQWTNSSFHANNPISIDYNDDGCLPSPLAPCTLSAYP
SFVVHATKASDVQAAVDFAANTGVRLIVKGTGHDLLSRSSGGQSLSIWTHNIVGISVNTS
DTRALPYGGVGSVKIAAGSRMAEVYQAVAKYNLTVIAGGDMSVGIGGWVLGGGHSPISST
YGLGADQVLEMEVVTPDGKFLTINEKSYPDLFWAMRGGGGSTFGVLISVTMKVYPTLPGS
LTIFTANTTSNSDTFWSISTYFTSQVPSLSDQGANGYHYFIPYAPPNPPDQAGIIIGGYF
FPNKTPAQVNAIMDPVITKINTTNWGDKVFVANETIPVPDFNKFWMTNQPEAVGPSERLG
SRLLTRGALTGNQTELENALRTASNGTWTLLNHLVAGKGVRDAKIPGGNNSVCPAWRNNT
YIHFVTYRTWTPLNQTEKTSVTNELRNSAVEALRILDPYTGAYVNEADPTEPNWQTTFWG
SNYPRLLALKKKYDPEGIFWCKPCVGNELWNVTGSSATQDEPPMRSTDFEDDDLLETILT
AAGRLCLDDQGGWDYHGHSSGPAFLQGLRKRFLDKGATNGDDATILSPLQSVPWSPRSPP
PPPEPRIAPPLPPKELAQKLVECALGSGCAVLSFIHRPTFSQLLDTFYETDPENYGIQEA
RVRAFLYSVFALGWLFLRTKSVDLRSNISMREGKYVCVSFLYRGDGSSFASNRPTQVFTR
RVFDAVEQETRKRVFWTVRNMEAYICAILGLPTAIKEDDVDQELPLEVDDACIARYGISV
CPAKHLPPTVAINAHTRLMQIFAKILRYVYPVHHSGHGHGLADQPGEYRVKYKRMCEVEH
ELQLWSANLPLELSNDNDNTPNPLRFQRALLFIAYAHTRLILYRPFLLSVSHYTMKNQSD
TRAHTYVMACLDASRDVIIGMRNMRERDILSGPFFFTSYSTFFAAISLISYAWERTQGED
IQAVLRYAEIGRDILSLLGQRSVAAARCSKALEALFGLLNKRLSETNEVAVTARPHAEPT
LMHRGPESVTGTFTHNPSFTPGLKDVSGKEAYFLGDAGVDGYISVADSTNPEFDTVKLTL
EGLLVTTIRCLDWYADTLIQRAQKLLQLHDVKRATDFIGFEDQRKSTAKCFFHFDVPKCL
QSELLGQNRGFLRDLPPSLPQFEVGQRHPVLQPRRQGQCDVTYTLRVQALMQDKVVTSWS
RSIQIIPALDVSPPFCVTDFAGEYLLERSRRRRRWLPGGRTTGDLRIEACQPPPVILSQL
TGDTVLSTTLSLTQGDRSTGNVREESRTPAQGRCRASLMFSTFISSDPRESAPTLKDLSS
PGALCRNFGVYATVEVPVQFSKWTKTSATLQGDNHNLELEHQWKADAHVTLNFGKLKYPV
PSFESSLVSRRYRVDLRVRIAAPYRCTLRLALPIQILYRTDSGQSPRRFREIDCPPYVA

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	116	309	3.5e-48	0.39956331877729256

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
213391	fungal_TF_MHR	2.04e-38	672	1055	1	405	fungal transcription factor regulatory middle homology region. This domain is present in the large family of fungal zinc cluster transcription factors that contain an N-terminal GAL4-like C6 zinc binuclear cluster DNA-binding domain. Examples of members of this large fungal group are the following Saccharomyces cerevisiae transcription factors, GAL4, STB5, DAL81, CAT8, RDR1, HAL9, PUT3, PPR1, ASG1, RSF2, PIP2, as well as the C-terminal domain of the Cep3, a subunit of the yeast centromere-binding factor 3. It has been suggested that this region plays a regulatory role.
396238	FAD_binding_4	4.01e-15	120	264	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.
369658	BBE	2.46e-14	522	560	1	39	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.
223354	GlcD	5.62e-14	118	559	30	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
397964	Fungal_trans	1.13e-08	692	905	12	260	Fungal specific transcription factor domain.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	4.17e-62	31	571	500	1055
QKD57322.1|CBM91|GH43_11	4.17e-62	31	571	500	1055
QRW06655.1|AA7	3.39e-19	120	580	68	510
QRV77710.1|AA7	3.39e-19	120	580	68	510
QRW27390.1|AA7	7.33e-19	116	566	62	491

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	3.51e-69	31	572	28	565	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	4.72e-63	31	568	30	585	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]
6FYD_A	1.51e-20	115	559	40	453	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]
6FYE_A	2.68e-20	115	559	40	453	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	3.58e-20	115	559	40	453	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4AS41|A7056_ARTBC	6.38e-87	3	574	2	584	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|A0A0E0RTV6|ZEB1_GIBZE	6.89e-83	19	572	15	554	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	2.78e-76	9	572	7	559	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
sp|G0R6T3|SORD_HYPJQ	8.05e-73	25	573	33	565	FAD-linked oxidoreductase sor8 OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=sor8 PE=3 SV=1
sp|A0A075TR33|PATO_PENEN	2.41e-70	13	572	10	558	FAD-linked oxidoreductase patO OS=Penicillium expansum OX=27334 GN=patO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000205	0.999748	CS pos: 25-26. Pr: 0.9768

TMHMM  Annotations     

There is no transmembrane helices in PV07_04108-t44_1-p1.