CAZyme Information: CCE32761.1

Basic Information

• Species: Claviceps purpurea
• Lineage: Ascomycota; Sordariomycetes; ; Clavicipitaceae; Claviceps; Claviceps purpurea
• CAZyme ID: CCE32761.1
• CAZy Family: GT1
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
393		42051.39	9.6963

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Cpurpurea20.1	8979	1111077	156	8823

• Gene Location: location=CAGA01000046:50439-51843(-)

Full Sequence      

MRFPSSKEAVAAGVILNAAKVLAVPTSYCSVDKEVCFQWAVPEAAAASGTGNVYFQLRAP
TSYAWISVAIGPQMVGSDMFVVYDNGNGNVTLSTRPGLKHAMPEYKAHPGVALLAGSGIV
DGQMVANVRCSSCSTLSLKSTNSWSSAWKKGASLASTNEAARIPYHDAHDSFSVDFSKAT
VSSDRNPFVGNTAAVVSGSGVSQQDSSSSDNKGLLYAHGIIMSLVFLIGFPVGSMLMPLL
GKWLVHASWQIVAFILMWAGFGVGYVLSRRWDMFFTQAHTRLGLVLCILISFQPVLGWLH
HQYYVQHQRRGAISNAHVWFGRILIILGMINGGLGLQLAGNDRAFVIAYCVILAVFAASY
LASVMLGAVSRRTKRGRQSSSDDSNGIGVAQSK

Enzyme Prediction     

No EC number prediction in CCE32761.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA8	31	182	2.2e-16	0.8901098901098901

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187688	CDH_like_cytochrome	2.49e-43	27	176	13	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	2.23e-37	168	362	1	188	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	1.53e-20	27	183	12	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.
214769	B561	1.17e-09	218	336	2	129	Cytochrome b-561 / ferric reductase transmembrane domain. Cytochrome b-561 recycles ascorbate for the generation of norepinephrine by dopamine-beta-hydroxylase in the chromaffin vesicles of the adrenal gland. It is a transmembrane heme protein with the two heme groups being bound to conserved histidine residues. A cytochrome b-561 homologue, termed Dcytb, is an iron-regulated ferric reductase in the duodenal mucosa. Other homologues of these are also likely to be ferric reductases. SDR2 is proposed to be important in regulating the metabolism of iron in the onset of neurodegenerative disorders.
187689	DOMON_DOH	9.31e-07	27	117	1	85	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
UKZ96621.1|AA0	1.28e-128	4	364	3	365
UPK98553.1|AA0	2.02e-121	23	377	23	392
UKZ85812.1|AA0	5.93e-117	1	375	1	402
UPK99964.1|AA0	2.11e-113	10	374	9	375
QPC76823.1|AA0	8.16e-102	25	351	28	350

PDB Hits     

CCE32761.1 has no PDB hit.

Swiss-Prot Hits     

CCE32761.1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.978198	0.021806

TMHMM  Annotations     

Start	End
214	236
246	268
318	340
345	367