CAZyme Information: KEF56290.1

Basic Information

• Species: Exophiala aquamarina
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala aquamarina
• CAZyme ID: KEF56290.1
• CAZy Family: GH154
• CAZyme Description: DOMON domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A072PLC8]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
949	AMGV01000006|CGC7	103407.47	4.6785

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EaquamarinaCBS119918	13118	1182545	0	13118

• Gene Location: location=AMGV01000006:1448754-1451603(+)

Full Sequence      

MLLAHYATLLSRFTKSDLLLTSLALAAFAVAQSSNDLDWVPFDREQFNGNVALDAEGNVQ
LFWKTANQSSTFGVASRSSGYLALGFSETGAMTGADMAVGYRDQDDNFVFENRHAMGFVT
PQVSQDQENNMRLQESHQADGVTAFVFEKQNKAGCLQTQADVAKDAWQWFIYAFSDENTF
AMHAPGNMGKEYVKLGTGKSVSLNEIRDIDGTQNFTIMQPELTIPTAETTYCYTLHKMPA
GDKNYLLGERPTASSQLLHHLVIYACYGLPDEYMDMLGKEPNCDYEEFSNPCNGFVTEWA
PGMSGRTFEPGYGKPFGTEYYEYVMLETHYNNPEGLEGEKDTASYTFLYTDQPVDTEIGT
LTLGDLQVEGWFLDPGQPLVAHSTVCTPECTERWPSDGITAVSVFHHMHYRGRHARVQII
RDGKEITPLSSLRNFEYDFQFSKSLNSVELLPGDKLITTCEYDTSNDTEPVPGGLPSKHE
MCFAWVDYYPANGVLACTQTSRGETAAICLESSADGLDVYESPFLTSSFQNLPVSGNTCP
AEDSGSGASNQAAVLNTCPETDVCFSLNVPEQSASSGTGDIYFQLSAPVTYSWVALAQGT
MMSNANMFVMYSSADGTNVTLSPRTAPGHTMPTHNEAADVSLLDGSGISNGRMTANVRCG
NCDSWDTGTMSLQGSNSDWLYAYSQGSPINSDDTNVPILQHDRQGGFQWDLSRATGGSDT
NPFTDAATTTTTTSVGGQNSWQRLSTQTQRRFVQVHGALASLAFVAILPIGAILVRLTSF
RGLVWTHGGVQVFGYVVFVVAAGLGIFIARGVTYLQEPHAIIGLILLGIFFFMPFIGIIH
HRIYKKVQERTVWSYGHIFTGRVGVILGMINGGLGLQLADARRSHAIVYGVFAGLIGAVY
IGAIVIGEHKRAKRSSQNGMASSSVYPKSKPLDQDDSDSGNGASHEAAN

Enzyme Prediction     

No EC number prediction in KEF56290.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA8	560	715	9.5e-20	0.8736263736263736

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187688	CDH_like_cytochrome	1.68e-55	557	711	15	168	Heme-binding cytochrome domain of fungal cellobiose dehydrogenases. Cellobiose dehydrogenase (CellobioseDH or CDH) is an extracellular fungal oxidoreductase that degrades both lignin and cellulose. Specifically, CDHs oxidize cellobiose, cellodextrins, and lactose to corresponding lactones, utilizing a variety of electron acceptors. Class-II CDHs are monomeric hemoflavoenzymes that are comprised of a b-type cytochrome domain linked to a large flavodehydrogenase domain. The cytochrome domain of CDH and related enzymes, which this model describes, folds as a beta sandwich and complexes a heme molecule. It is found at the N-terminus of this family of enzymes, and belongs to the DOMON domain superfamily, a ligand-interacting motif found in all three kingdoms of life.
176490	Cyt_b561_FRRS1_like	4.44e-36	710	905	8	191	Eukaryotic cytochrome b(561), including the FRRS1 gene product. Cytochrome b(561), as found in eukaryotes, similar to and including the human FRRS1 gene product (ferric-chelate reductase 1), also called SDR-2 (stromal cell-derived receptor 2). This family comprises a variety of domain architectures, many of which contain dopamine beta-monooxygenase (DOMON) domains. The protein might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.
406418	CDH-cyt	1.07e-31	559	715	16	174	Cytochrome domain of cellobiose dehydrogenase. CDH-cyt is the cytochrome domain, at the N-terminus, of cellobiose dehydrogenase. CDH-cyt folds as a beta sandwich with the topology of the antibody Fab V(H) domain and binds iron. The haem iron is ligated by Met83 and His181 in UniProtKB:Q01738.
395859	Cu2_monooxygen	6.07e-29	215	337	1	130	Copper type II ascorbate-dependent monooxygenase, N-terminal domain. The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.
397669	Cu2_monoox_C	6.41e-21	359	491	4	138	Copper type II ascorbate-dependent monooxygenase, C-terminal domain. The N and C-terminal domains of members of this family adopt the same PNGase F-like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAE7013938.1|AA8	1.30e-116	547	913	15	386
SMR42136.1|AA0	3.04e-108	548	915	17	389
SMR44317.1|AA0	3.04e-108	548	915	17	389
SMR55355.1|AA0	1.81e-104	563	930	25	385
SMR57731.1|AA0	1.81e-104	563	930	25	385

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZEL_A	3.70e-31	50	497	11	464	Human dopamine beta-hydroxylase [Homo sapiens],4ZEL_B Human dopamine beta-hydroxylase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q08CS6|MOXD2_DANRE	3.06e-40	53	497	38	472	DBH-like monooxygenase protein 2 homolog OS=Danio rerio OX=7955 GN=moxd2 PE=2 SV=2
sp|Q6UVY6|MOXD1_HUMAN	5.37e-39	53	497	31	480	DBH-like monooxygenase protein 1 OS=Homo sapiens OX=9606 GN=MOXD1 PE=1 SV=1
sp|Q9CXI3|MOXD1_MOUSE	1.83e-36	51	498	29	481	DBH-like monooxygenase protein 1 OS=Mus musculus OX=10090 GN=Moxd1 PE=1 SV=1
sp|Q5TZ24|MOXD1_DANRE	4.43e-36	46	497	26	482	DBH-like monooxygenase protein 1 homolog OS=Danio rerio OX=7955 GN=moxd1 PE=2 SV=2
sp|Q6NP60|MOX12_DROME	9.88e-36	52	490	112	573	MOXD1 homolog 2 OS=Drosophila melanogaster OX=7227 GN=olf413 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000320	0.999642	CS pos: 31-32. Pr: 0.9749

TMHMM  Annotations     

Start	End
758	780
792	814
818	840
853	875
885	907