CAZyme Information: NEUDI_140163T0-p1

Basic Information

• Species: Neurospora discreta
• Lineage: Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora discreta
• CAZyme ID: NEUDI_140163T0-p1
• CAZy Family: GH11
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
415		43748.59	8.8854

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_NdiscretaFGSC8579	10345	510953	397	9948

• Gene Location: location=NdisFGSC8579_SC007:1313226-1314688(-)

Full Sequence      

MKAIKVSLLASGLSASIVVHATTPKYCATGADNVCFRFGIPQSSANSGSGNIYFQIQAPS
TYSWVALGTGDQMKGSNMFVMYQDGTGNLTLSPRLGTGHSMPEEDTSSSAADLGLLAGSG
VANGVMVANVVCPNCETWDGGSLSLTDTASKWIAAWKSGSSLATTSKSARISQHDDHDQF
QLDLTQATVSSDSNPFLEADIEDPGTGSGGGSNGGGGGSSDNPGDVVGPGNPFAPVVGGR
RRDAALVAHSGIMTATFAALYPLGSMLMPLAGSWIAHAAWQTVAFIMMWVGFGLGIHVAQ
DRNMPVLGVMHHKYFVKYRERGAISYAHIWWGRILLILAVVNGGLGLKLTNAGNSAVIAY
CIVAAVCFGIYAIVKSWAVVRRGRQGGAHFRKSDNFTHQQRYPVGRQPYRPRNRV

Enzyme Prediction     

No EC number prediction in NEUDI_140163T0-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA8	32	190	4.4e-18	0.8791208791208791

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187688	CDH_like_cytochrome	4.77e-57	21	184	6	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	7.91e-26	225	374	15	189	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	6.33e-25	28	191	14	177	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.
214768	DoH	5.70e-07	48	161	12	124	Possible catecholamine-binding domain present in a variety of eukaryotic proteins. A predominantly beta-sheet domain present as a regulatory N-terminal domain in dopamine beta-hydroxylase, mono-oxygenase X and SDR2. Its function remains unknown at present (Ponting, Human Molecular Genetics, in press).
187689	DOMON_DOH	6.07e-06	47	128	16	93	DOMON-like domain of copper-dependent monooxygenases and related proteins. This diverse family characterizes DOMON domains found in dopamine beta-hydroxylase (DBH), monooxygenase X (MOX), and various other proteins, some of which contain DOMON domains exclusively; the family is not restricted to eukaryotes. DBH is a membrane-bound enzyme that converts dopamine to L-norepinephrine, and plays a central role in the metabolism of catecholamine neurotransmitters. DOMON domains were initially thought to confer protein-protein interactions. They were subsequently found as a heme-binding motif in cellobiose dehydrogenase, an extracellular fungal oxidoreductase that degrades both lignin and cellulose, and in ethylbenzene dehydrogenase, an enzyme that aids in the anaerobic degradation of hydrocarbons. The domain interacts with sugars in the type 9 carbohydrate binding modules (CBM9), which are present in a variety of glycosyl hydrolases, and it can also be found at the N-terminus of sensor histidine kinases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK98553.1|AA0	5.22e-92	8	371	8	376
UKZ96621.1|AA0	4.09e-90	16	371	17	361
UPK99964.1|AA0	1.94e-89	21	384	22	377
UKZ85812.1|AA0	2.75e-84	2	385	5	402
QPC76823.1|AA0	7.17e-77	20	371	25	359

PDB Hits     

NEUDI_140163T0-p1 has no PDB hit.

Swiss-Prot Hits     

NEUDI_140163T0-p1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000232	0.999751	CS pos: 21-22. Pr: 0.9614

TMHMM  Annotations     

Start	End
246	268
278	300
324	346
356	378