CAZyme Information: ZTRI_10.23.mRNA-p1

Basic Information

• Species: Zymoseptoria tritici
• Lineage: Ascomycota; Dothideomycetes; ; Mycosphaerellaceae; Zymoseptoria; Zymoseptoria tritici
• CAZyme ID: ZTRI_10.23.mRNA-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1078		117171.01	6.6590

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_ZtriticiIPO323	11839	336722	13	11826

• Gene Location: location=Ztri_chr_10:75298-78784(+)

Full Sequence      

MFFLSTTLCTLAFAALVAAQSSTDLAWIPFDRDQFSNNTALDNDGNVQLFWKIGDDYSSY
GIASRSNGYLALGFSETGAMTGADMALGYKADNGSFMLENRHAQGFVRPDVSPDQTVNMR
FKEGDQSDNLTHFIFDKKNMADCLETQVDVMRDSWQWFIYAHSDSNTFAQHKDGQMGKKY
VKLGTGKDVSLNVVSNVNNAKNFTVLQPELTIPAKETSYCYTLHKMPAGKKNFLVGEQPG
EAGSMLHHLVLYACYDLPDSYLDMLGKEANCDARAVKNPCNGFVTEWAPGMAGRTFEPGF
GKPFGEDLYQYAMLEVHYNNPDLIEGVKDTTGYSFSWTDQQVETEIGSLTTGALQGDGWF
LEPGKELVTISRVCTPDCTRNWPEEGITAVAVFHHMHFRGVNTWVQIIRDGKEIMPLSTL
RHFEYGYQFSKTLNEIKLLPGDRLITTCQYNTMNDTQPVPGGPSSADEMCFAWIDYYPAN
SILACTEVDLSLIPSSPINGSAGFCLDYTKDDPIFSSASTLTADYEHLPPSGNNCSATDG
GTATGPAILQTCPETDVCFSLNVPASSKTNLERRAEPGDIFFQLSAPTSYSWVALGQGTT
MSNANIFVMHSSADGKNVTLSPRTATGHVMPTHDTAASISLLEGSGISNGKMTANVRCSN
CKNTMALSGGDSDWIYAHLKGPSIASDDLETPVSQHDDHGAFKWDLSKATGGSSPNPFLA
AGSSTTSSSSSSSQPSLRLVQAHGAMASLAFVGIFPIGAILVRLANLSHLAWVHGAIQLL
GYAIFIAAAGIGISLAKQGSYLSKPHAGIGLFLLAVLFFMPIVGALQHRLYKKVHKRTVW
SYGHIFTGRVAVVLGMINGGLGLKLADAPSRYKIVYGVFAGLMGLFYIGAMIFGERKSAK
ERKQAVALEKESSGSSTECRRSPTTLFATSCFMASRSIFFLAHPNCFFFRILPRSPTNNR
FASRSPCSLLIRIYRVTSVVVRITWPVLSRVDEWSASASSITAVATLALIFLTTEEDMKL
HLLTIPGLIVLATPARATGVTHGDSCTRDELGQKRCEKDGGHVMLCSNKNACVKYPAQ

Enzyme Prediction     

No EC number prediction in ZTRI_10.23.mRNA-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA8	555	710	7.5e-16	0.8681318681318682

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
187688	CDH_like_cytochrome	3.06e-49	551	706	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	5.73e-39	698	888	1	187	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.
395859	Cu2_monooxygen	7.41e-30	203	325	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.
406418	CDH-cyt	7.31e-28	553	710	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.
397669	Cu2_monoox_C	1.08e-25	347	485	4	144	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
SMR42136.1|AA0	3.81e-104	547	905	22	392
SMR44317.1|AA0	3.81e-104	547	905	22	392
CAE7013938.1|AA8	3.17e-96	548	912	22	395
SMR55355.1|AA0	2.16e-88	557	905	25	372
SMR57731.1|AA0	2.16e-88	557	905	25	372

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4ZEL_A	1.06e-26	198	485	170	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|Q6UVY6|MOXD1_HUMAN	3.01e-38	35	488	25	483	DBH-like monooxygenase protein 1 OS=Homo sapiens OX=9606 GN=MOXD1 PE=1 SV=1
sp|Q61P40|TBH1_CAEBR	6.92e-38	46	485	32	477	Tyramine beta-hydroxylase OS=Caenorhabditis briggsae OX=6238 GN=tbh-1 PE=3 SV=1
sp|Q08CS6|MOXD2_DANRE	2.54e-37	41	488	38	475	DBH-like monooxygenase protein 2 homolog OS=Danio rerio OX=7955 GN=moxd2 PE=2 SV=2
sp|Q9CXI3|MOXD1_MOUSE	5.52e-37	35	488	25	483	DBH-like monooxygenase protein 1 OS=Mus musculus OX=10090 GN=Moxd1 PE=1 SV=1
sp|Q5TZ24|MOXD1_DANRE	2.38e-36	34	488	26	485	DBH-like monooxygenase protein 1 homolog OS=Danio rerio OX=7955 GN=moxd1 PE=2 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000221	0.999766	CS pos: 19-20. Pr: 0.9790

TMHMM  Annotations     

Start	End
743	765
770	792
807	826
839	861
874	893