CAZyme Information: jhhlp_001580-t41_1-p1

Basic Information

• Species: Lomentospora prolificans
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
• CAZyme ID: jhhlp_001580-t41_1-p1
• CAZy Family: AA7
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
238	NLAX01000004|CGC7	24820.86	8.4689

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LprolificansJHH5317	8768	N/A	208	8560

• Gene Location: location=NLAX01000004:2382576-2383559(+)

Full Sequence      

MKPIFALQALLGLVAAVPTASEASHGIEKRQATLTKWCSPTTSLCYNQYTTGGGSAFRIA
IADSSTTAGAFDIAIQLVAPTGQGWVGLSWGGGMSQAPLTVAWPNGQDVTLSSRWANAHT
MPTMYNDATYTVLADTGVNGTHYTLSVVCKGCSTWTRPTGTRTLSPNGGVRLAWAQNTQA
ASVAQPANPASNFNYHQYLGYFDASFQDSKVPAAQFSAAVAMTKAGVNSAAATPVPSF

Enzyme Prediction     

No EC number prediction in jhhlp_001580-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA8	39	211	2.8e-47	0.9505494505494505

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
406418	CDH-cyt	1.79e-55	37	212	1	176	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.
187688	CDH_like_cytochrome	8.67e-45	37	204	2	166	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.
187689	DOMON_DOH	2.31e-06	72	197	20	134	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.
397434	DOMON	7.18e-04	72	175	15	118	DOMON domain. The DOMON (named after dopamine beta-monooxygenase N-terminal) domain is 110-125 residues long. It is predicted to form an all beta fold with up to 11 strands and is secreted to the extracellular compartment. The beta-strand folding produces a hydrophobic pocket which appears to bind soluble haem. This is consistent with the predominant architectures where the protein is associated with cytochromes or enzymatic domains whose activity involves redox or electron transfer reactions potentially as a direct participant in the electron transfer process. The DOMON domain superfamily, of which this is just one member, shows (1) multiple hydrophobic residues that contribute to the hydrophobic core of the strands of the beta-sandwich, and small residues found at the boundaries of strands and loops, (2) a strongly conserved charged residue (usually arginine/lysine) at the end of strand 9, which possibly stabilizes the loop between 9 and 10, and (3) a polar residue (usually histidine, lysine or arginine), that interacts or coordinates with ligands. The suggested superfamily includes both haem- and sugar-binding members: the haem-binding families being the ethyl-Benzoate dehydrogenase family EB_dh, pfam09459, the cellobiose dehydrogenase family CBDH and this family, and the sugar-binding families being the xylanases, CBM_4_9, pfam02018. The common feature of the superfamily is the 11-beta-strand structure, although the first and eleventh strands are not well conserved either within families or between families.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO69821.1|AA8	4.84e-47	16	220	24	227
AEO59519.1|AA8	4.58e-46	20	216	27	217
VBB87352.1|AA8	1.27e-37	24	221	22	211
CDP32865.1|AA8	5.05e-37	24	221	22	211
CDP24536.1|AA8	5.53e-36	17	218	27	219

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1D7B_A	1.73e-20	76	206	47	173	Chain A, CELLOBIOSE DEHYDROGENASE [Phanerodontia chrysosporium],1D7B_B Chain B, CELLOBIOSE DEHYDROGENASE [Phanerodontia chrysosporium],1D7D_A Chain A, CELLOBIOSE DEHYDROGENASE [Phanerodontia chrysosporium],1D7D_B Chain B, CELLOBIOSE DEHYDROGENASE [Phanerodontia chrysosporium]
1D7C_A	1.89e-20	76	206	47	173	Chain A, CELLOBIOSE DEHYDROGENASE [Phanerodontia chrysosporium],1D7C_B Chain B, CELLOBIOSE DEHYDROGENASE [Phanerodontia chrysosporium]
1PL3_A	1.80e-19	76	206	47	173	Chain A, Cellobiose dehydrogenase [Phanerodontia chrysosporium],1PL3_B Chain B, Cellobiose dehydrogenase [Phanerodontia chrysosporium]
6JT6_A	2.36e-14	31	202	1	170	Chain A, Extracellular PQQ-dependent sugar dehydrogenase [Coprinopsis cinerea]
4QI3_A	1.38e-12	51	189	29	165	Chain A, Cellobiose dehydrogenase [Thermothelomyces myriococcoides],4QI3_B Chain B, Cellobiose dehydrogenase [Thermothelomyces myriococcoides]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q01738|CDH_PHACH	3.14e-18	76	206	65	191	Cellobiose dehydrogenase OS=Phanerodontia chrysosporium OX=2822231 GN=CDH-1 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000221	0.999750	CS pos: 30-31. Pr: 0.5168

TMHMM  Annotations     

There is no transmembrane helices in jhhlp_001580-t41_1-p1.