CAZyme Information: KFA46534.1

Basic Information

• Species: Stachybotrys chartarum
• Lineage: Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
• CAZyme ID: KFA46534.1
• CAZy Family: AA7
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
406	KL651648|CGC1	43100.66	5.2907

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SchartarumIBT40293	11453	1280524	0	11453

• Gene Location: location=KL651648:940-2229(+)

Full Sequence      

MYRSPWLLTTSRRLVAAVSNAAIASHCPGDSDDLCFQWGVPEASASAGSGNVYIQLRAST
SLSWAGLGIGSRMAGADIFLIYQDGNGNVTLSTRAGSGHMMPQYEARQGVELIEGSGIVD
GHMVANIRCSGCSSLDLAGSNNWIAAWLPGDSLDSSDPAEPINIHSDNTMFQVDMAEATI
SSDQNPFLASSGNNGSSGNDGDDQNDGDRGGAVTEQDSDDNNTLRSAHGVIMTIVFVVAY
PVGALLMPIFGKWFIHAGWQMIAFLGMWIGFALGYILTEREGESLDEAHMGLGTFIVALL
GLQPILGWLHHRHYLKHQARGVAGKAHIWYGRVLTILGIVNGGLGLQLSGADAGFVIAYS
VIAGAICIAWIAFCALTAFRRSPRARPAAKQSPHGVNATELEERIP

Enzyme Prediction     

No EC number prediction in KFA46534.1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA8	32	180	1.8e-16	0.8736263736263736

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187688	CDH_like_cytochrome	7.39e-47	14	175	2	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	1.95e-35	217	373	28	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	9.66e-21	36	182	20	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	4.16e-07	228	346	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.
214768	DoH	1.86e-06	47	179	11	147	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).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK98553.1|AA0	6.30e-134	7	391	8	397
UKZ96621.1|AA0	9.51e-132	10	377	11	368
UKZ85812.1|AA0	8.47e-123	19	382	21	400
UPK99964.1|AA0	3.44e-118	7	362	8	353
QPC76823.1|AA0	2.68e-106	15	361	20	350

PDB Hits     

KFA46534.1 has no PDB hit.

Swiss-Prot Hits     

KFA46534.1 has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.998785	0.001242

TMHMM  Annotations     

Start	End
228	250
255	277
287	309
329	351
355	377