CAZyme Information: EAQ90369.1

Basic Information

• Species: Chaetomium globosum
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Chaetomium; Chaetomium globosum
• CAZyme ID: EAQ90369.1
• CAZy Family: GH55
• CAZyme Description: zf-3CxxC domain-containing protein [Source:UniProtKB/TrEMBL;Acc:Q2HBV0]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
711		77963.29	6.7027

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_CglobosumCBS148.51	11232	306901	184	11048

• Gene Location: location=CH408030:563969-568568(+)

Full Sequence      

MASTTKPKKQKAPKRKNPPATTATFPSLHEDIKNVLASEDVILDPKPWFNLTGGDAEATK
EHDTNIMGRFECRNNQCSQRGWGSKKIAIHIRGFPGNGYNAVVYKQRCRTCERLGILRLD
ENSPNTTTPSQHHPLTMTTPTVFITGATGSQGSALAHHLRRLNWAVHSTARNLSSPAAQA
LTAIGVQLTPGSWDDEAALASAMAGCSKMFLCLLPDFGDPTRELRQAGVMVRVAREAGVK
QVVASTSLGVFTLEEEGVGGGGDGEGRGGVVAGSVMAGHLANKKGIEEVVRGGGFERWAF
LRPAFFMANFLEPKVARYPEPREKGTWTTAMTPEAPLALIDHVDIAAFAAAVFQQPDRFH
DRAFGLASELLTVQETLDALGEAAGRSLKAVFMTDEEIAEKQRTSNVFTNSQVSLRYAAK
YIDMEEVASVIRPTSFKDFLEREKEGVKKTQPSSYPWLLEDQQAKGIQRRWWPDPIQSVD
HPQLSCNRGNPLEKNLPTMHAVIQAGTNITAYYIPPKCPPGYNQPTEVLAPEFQDPSPPM
RCAGPEYSWVHSTGPLLVYMAACNGPCDQFNPEGKKVWFKVYESGLKNGGKVNEWGQKID
VASGEGWDQIRFANNGWSITIPKNLKPGNYLIRHEIIMIELMPPQFYPECANLEVTGDGT
ELPGEEYLVSFPGAYSLEDPGLALSGDLYSQKGHSTYNYTIPGPAVWTGEK

Enzyme Prediction     

EC	1.14.99.54:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA9	465	684	8.1e-41	0.8136363636363636

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
410622	LPMO_AA9	1.36e-54	467	707	22	216	lytic polysaccharide monooxygenase (LPMO) auxiliary activity family 9 (AA9). AA9 proteins are copper-dependent lytic polysaccharide monooxygenases (LPMOs) involved in the cleavage of cellulose chains with oxidation of carbons C1 and/or C4 and C6. Activities include lytic cellulose monooxygenase (C1-hydroxylating) (EC 1.14.99.54) and lytic cellulose monooxygenase (C4-dehydrogenating) (EC 1.14.99.56). The family used to be called GH61 because weak endoglucanase activity had been demonstrated in some family members.
397484	Glyco_hydro_61	8.70e-51	467	697	26	211	Glycosyl hydrolase family 61. Although weak endoglucanase activity has been demonstrated in several members of this family, they lack the clustered conserved catalytic acidic amino acids present in most glycoside hydrolases. Many members of this family lack measurable cellulase activity on their own, but enhance the activity of other cellulolytic enzymes. They are therefore unlikely to be true glycoside hydrolases. The subsrate-binding surface of this family is a flat Ig-like fold.
187561	NmrA_like_SDR_a	3.68e-45	142	401	1	237	NmrA (a transcriptional regulator) and HSCARG (an NADPH sensor) like proteins, atypical (a) SDRs. NmrA and HSCARG like proteins. NmrA is a negative transcriptional regulator of various fungi, involved in the post-translational modulation of the GATA-type transcription factor AreA. NmrA lacks the canonical GXXGXXG NAD-binding motif and has altered residues at the catalytic triad, including a Met instead of the critical Tyr residue. NmrA may bind nucleotides but appears to lack any dehydrogenase activity. HSCARG has been identified as a putative NADP-sensing molecule, and redistributes and restructures in response to NADPH/NADP ratios. Like NmrA, it lacks most of the active site residues of the SDR family, but has an NAD(P)-binding motif similar to the extended SDR family, GXXGXXG. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Atypical SDRs are distinct from classical SDRs. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
187578	TMR_SDR_a	1.82e-26	144	403	3	230	triphenylmethane reductase (TMR)-like proteins, NMRa-like, atypical (a) SDRs. TMR is an atypical NADP-binding protein of the SDR family. It lacks the active site residues of the SDRs but has a glycine rich NAD(P)-binding motif that matches the extended SDRs. Proteins in this subgroup however, are more similar in length to the classical SDRs. TMR was identified as a reducer of triphenylmethane dyes, important environmental pollutants. This subgroup also includes Escherichia coli NADPH-dependent quinine oxidoreductase (QOR2), which catalyzes two-electron reduction of quinone; but is unlikely to play a major role in protecting against quinone cytotoxicity. Atypical SDRs are distinct from classical SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.
398829	NmrA	2.43e-25	142	392	1	236	NmrA-like family. NmrA is a negative transcriptional regulator involved in the post-translational modification of the transcription factor AreA. NmrA is part of a system controlling nitrogen metabolite repression in fungi. This family only contains a few sequences as iteration results in significant matches to other Rossmann fold families.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC96956.1|AA9	6.37e-42	455	708	34	249
AEO68577.1|AA9	9.49e-39	456	709	48	250
UPO25274.1|AA9	1.40e-37	465	709	58	256
CBX97718.1|AA9	3.23e-37	450	709	42	252
CCA94932.1|AA9	3.50e-37	467	709	54	255

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5NNS_A	1.53e-36	467	709	29	225	Crystal structure of HiLPMO9B [Heterobasidion irregulare TC 32-1],5NNS_B Crystal structure of HiLPMO9B [Heterobasidion irregulare TC 32-1]
5UFV_A	8.96e-30	472	709	32	227	Crystal Structure of a Cellulose-active Polysaccharide Monooxygenase from M. thermophila (MtPMO3*) [Thermothelomyces thermophilus ATCC 42464],5UFV_B Crystal Structure of a Cellulose-active Polysaccharide Monooxygenase from M. thermophila (MtPMO3*) [Thermothelomyces thermophilus ATCC 42464],5UFV_C Crystal Structure of a Cellulose-active Polysaccharide Monooxygenase from M. thermophila (MtPMO3*) [Thermothelomyces thermophilus ATCC 42464],5UFV_D Crystal Structure of a Cellulose-active Polysaccharide Monooxygenase from M. thermophila (MtPMO3*) [Thermothelomyces thermophilus ATCC 42464],5UFV_E Crystal Structure of a Cellulose-active Polysaccharide Monooxygenase from M. thermophila (MtPMO3*) [Thermothelomyces thermophilus ATCC 42464],5UFV_F Crystal Structure of a Cellulose-active Polysaccharide Monooxygenase from M. thermophila (MtPMO3*) [Thermothelomyces thermophilus ATCC 42464]
7NTL_A	5.32e-25	554	709	83	222	Chain A, LPMO9F [Malbranchea cinnamomea]
4EIS_A	6.65e-24	554	708	84	224	Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases (PMO-3) [Neurospora crassa OR74A]
4EIS_B	6.65e-24	554	708	84	224	Structural basis for substrate targeting and catalysis by fungal polysaccharide monooxygenases (PMO-3) [Neurospora crassa OR74A]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q00023|CEL1_AGABI	1.40e-31	467	707	58	254	Cellulose-growth-specific protein OS=Agaricus bisporus OX=5341 GN=cel1 PE=3 SV=1
sp|G2Q9T3|CEL61_MYCTT	7.18e-20	545	709	100	245	Polysaccharide monooxygenase Cel61a OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=Cel61a PE=1 SV=1
sp|Q7Z9M7|GUN7_HYPJQ	1.20e-19	549	709	106	249	Endoglucanase-7 OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=cel61b PE=1 SV=3
sp|O14405|GUN4_HYPJE	1.07e-18	549	709	105	248	Endoglucanase-4 OS=Hypocrea jecorina OX=51453 GN=cel61a PE=1 SV=1
sp|Q8KU07|AZOB_XENAZ	2.05e-10	142	397	2	224	NAD(P)H azoreductase OS=Xenophilus azovorans OX=151755 GN=azoB PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000060	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EAQ90369.1.