CAZyme Information: EAQ90278.1

Basic Information

• Species: Chaetomium globosum
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Chaetomium; Chaetomium globosum
• CAZyme ID: EAQ90278.1
• CAZy Family: GH55
• CAZyme Description: Cellulase domain-containing protein [Source:UniProtKB/TrEMBL;Acc:Q2HC41]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1272		139580.40	6.0391

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=CH408030:237418-242835(-)

Full Sequence      

MKLLNLLLGAVATSSALAAPASVAPTLTTKEKRAGKFKFVGVNQSGAEFGKDTLPGQLGK
HYTWPAKSSIDVSFVLLLCCSWERSRYYERIITDVDGFKAWWTTTAKIFSSNDKVIFDTN
NEYHDMDDKLVFNLNQAAIDGIRGAGATSQLIFVEGNSWTGAWTWVSSGNGASLINLSDP
AGSDKLVYEMHQYLDSDGSGTSEACVSGTIGQERLREATAWLKASGKRGILGETAGGANA
QCIAALTGMLAHMAENADVWMGWLWWGGGPWWGTYMYSIRAKWGSAGWRLCAQHRWGTAQ
CGLCAEHMEDLYQLSLVNRRLLSVVEPILYARGIGYHFATPLAWAAKFGIAATLHKVLAA
GASPDRKLRCQMTRHFWHFANDAHQATLDWAAGDPKYWPPLSNDRVEALDDEEEIWAKDM
TSGLADFDVGYPAEVCPSAGLAGNGSPDSSTVDFAQSPRDPPPELYEADRLLREYTALHL
AAREGHTDFVNLLLANGASVDSSSRWFCPCRPHRGLWQTMLDRPTLGHLLKPVHWLPLHA
AICSSRIETAKSLLSAGATVLRNSHNGSASYGALHQAAAAGHVDLVRYILDTHPDIDVDV
PDELGMTPFYHAYINARWDSTIPILMARGANINSRVRVVFDRRHGDVQTNVRLDATPLAE
ACRLGRFEDALKLIDLGANVTMGVQLGNDSAINMNIPPLHLCCMDFGLDNEFYPTGEAIW
SRAPGQRAFRGAVIARLVAAGVSPDAKMGFIGFGVETALTVAVRHTNVAAVEALLAAGAD
VGIRNLKGRNALMVSVEPPTIDSPSEMSLGFLSYAPAYLASFRIAHSDAWAITKLLIEAG
VSLVDGDEDGDTVLHLLFDSLDEGDRFRIESPSDMGILRLLLARGADPCLRNKKGVPALH
VAVRNGRLAAVQCIAAQGRIDLVKTFPMEVVGALFDAVQFEDDIEDATTDPDWEALMGDP
HRFSAATLRLIDALVDMDRSGRLSSNVSFICSRLHNRHRKDPALEVAEVLCYRGLAADTF
DGEAKLTILRAAIKAARWDMARALLRDVPETDINSLDPEGHTLLSLVTSSRRMHDGGFAW
ELIEAGADIHIRVAPSLSCGEDTTPLKQALICSDTYPIERMLQKQPIRGNPRAIEHRYLH
WAVTLPWNPSLEEEWSESVWSDRDTIVRALLVAGADPTQLDSNGDTPLLRAAREMDENKH
DVCREIGHWVKPLSRGVDGHRKNKQGRSIVDHLTNIINERELSDLEFMYSVMVFNLTEDG
KSVKRAIRWPPK

Enzyme Prediction     

EC	3.2.1.4:38

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH5	82	276	1.5e-73	0.6914893617021277

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
395098	Cellulase	1.62e-40	86	259	94	262	Cellulase (glycosyl hydrolase family 5).
293786	ANK	5.49e-14	473	598	1	96	ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.
293786	ANK	7.10e-13	535	635	3	97	ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.
293786	ANK	9.16e-11	573	682	5	96	ankyrin repeats. Ankyrin repeats are one of the most abundant repeat motifs, and generally function as scaffolds for protein-protein interactions in processes including cell cycle, transcriptional regulation, signal transduction, vesicular trafficking, and inflammatory response. Although predominantly found in eukaryotic proteins, they are also found in some bacterial and viral proteins. Less is known of their physiological roles in prokaryotes. Some bacterial ANK proteins play key roles in microbial pathogenesis by mimicking or manipulating host function(s). The pathogen Providencia alcalifaciens N-formyltransferase ankyrin repeats function in small molecule binding and allosteric control. Ankyrin-repeat proteins have been associated with a number of human diseases.
403870	Ank_2	1.02e-10	478	598	1	89	Ankyrin repeats (3 copies).

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO58455.1|GH5_5	5.82e-132	1	286	1	325
AEO68519.1|GH5_5	7.56e-129	1	286	1	329
VBB80589.1|GH5_5	2.33e-110	1	279	1	324
CDP28876.1|GH5_5	3.46e-110	1	279	1	326
CAP61800.1|GH5_5	3.46e-110	1	279	1	326

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1GZJ_A	4.81e-85	37	286	3	292	Structure of Thermoascus aurantiacus family 5 endoglucanase [Thermoascus aurantiacus],1GZJ_B Structure of Thermoascus aurantiacus family 5 endoglucanase [Thermoascus aurantiacus]
1H1N_A	1.20e-83	37	286	4	293	Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus [Thermoascus aurantiacus],1H1N_B Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus [Thermoascus aurantiacus]
6T9F_A	2.16e-79	31	286	7	302	CRYSTAL STRUCTURE OF EN ENDOGLUCANASE S308P FROM PENICILLIUM VERRUCULOSUM [Talaromyces verruculosus],6T9F_B CRYSTAL STRUCTURE OF EN ENDOGLUCANASE S308P FROM PENICILLIUM VERRUCULOSUM [Talaromyces verruculosus],6T9F_C CRYSTAL STRUCTURE OF EN ENDOGLUCANASE S308P FROM PENICILLIUM VERRUCULOSUM [Talaromyces verruculosus],6T9F_D CRYSTAL STRUCTURE OF EN ENDOGLUCANASE S308P FROM PENICILLIUM VERRUCULOSUM [Talaromyces verruculosus]
5L9C_A	2.16e-79	31	286	7	302	Crystal structure of an endoglucanase from Penicillium verruculosum in complex with cellobiose [Talaromyces verruculosus],5L9C_B Crystal structure of an endoglucanase from Penicillium verruculosum in complex with cellobiose [Talaromyces verruculosus],5L9C_C Crystal structure of an endoglucanase from Penicillium verruculosum in complex with cellobiose [Talaromyces verruculosus],5L9C_D Crystal structure of an endoglucanase from Penicillium verruculosum in complex with cellobiose [Talaromyces verruculosus]
6YON_A	1.97e-78	31	286	7	302	Chain A, Endoglucanase [Talaromyces verruculosus],6YON_B Chain B, Endoglucanase [Talaromyces verruculosus],6YON_C Chain C, Endoglucanase [Talaromyces verruculosus],6YON_D Chain D, Endoglucanase [Talaromyces verruculosus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A1DME8|EGLB_NEOFI	2.93e-84	1	286	1	316	Probable endo-beta-1,4-glucanase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=eglB PE=3 SV=1
sp|Q12624|GUN3_HUMIN	6.08e-82	35	279	84	368	Endoglucanase 3 OS=Humicola insolens OX=34413 GN=CMC3 PE=1 SV=1
sp|Q7SDR1|GUN3_NEUCR	8.13e-81	35	285	86	376	Endoglucanase gh5-1 OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=gh5-1 PE=1 SV=1
sp|Q2UPQ4|EGLB_ASPOR	1.18e-79	1	286	1	320	Probable endo-beta-1,4-glucanase B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=eglB PE=3 SV=1
sp|B8MW97|EGLB_ASPFN	1.18e-79	1	286	1	320	probable endo-beta-1,4-glucanase B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=eglB PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000601	0.999366	CS pos: 18-19. Pr: 0.9696

TMHMM  Annotations     

There is no transmembrane helices in EAQ90278.1.