CAZyme Information: TRIREDRAFT_62166-t26_1-p1

Basic Information

• Species: Trichoderma reesei
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma reesei
• CAZyme ID: TRIREDRAFT_62166-t26_1-p1
• CAZy Family: GH47
• CAZyme Description: Hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
854	GL985065|CGC7	97437.06	5.0718

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TreeseiQM6a	9138	431241	7	9131

• Gene Location: location=GL985065:258215-260779(-)

Full Sequence      

MAPRKIIPIDANWQFGRTDVEKPDFRPVSQFPTNVHLDLLHHKLIPDPFIGKNELDVQWV
GEVRAWQYRTSFKSPTIGSQEKAVLAFDGLDTFAEVLLNDKKILETDNMFIPERVDVTAL
LNETDKDNQLVITFDSAYLRGWERVEQIPEHKWGTWNGDHSRLAVRKAQYHWGWDWGPTL
LTCGPWKPINLEIYESRLSDLYANVTLDESLNNAKIELHAETDGKASKVRFELSLGKTIL
SDTVDVSKGAAVATLSISKPELWYPARYGKQPLYTAKATLLDGDEEVDTLSKRIGIRKVE
LVQKPLEDQPGTSFFFKVNNIPIFCGGSCWIPADNFTPRITNEKYQNWIRLMVEGNQSMI
RIWGGGIYEDERLLDACDEQGILVWVDFLFACGNYPCNPEMLQSVEREARANIKIMRHHP
SIVIYAGNNEDYQFQESEGLTYDVQDKDPQSWLKSDFPARYIYEHLLVQVCQELVPETFY
HYGSPWGGKTSSDPTVGDIHQWNVWHGSQARYQDFDKLIGRFVSEFGLEAFPSARTIDAA
LPKGKDDPDRHPQSDIVDFHNKADGHERRIALYLAENIPYVTSPLEQYIYSTQLLQAECL
SSAFRLWRRQWKGPGREYCSGALLWQLNDCWPVTSWAICDYYLRPKLAYYTVKRELLPVT
VGIKRTEHRHPKSKYTRVDVEVSTKLEIWASNFTLNEVKVDCVVKAWDVETAEEVYSETI
ASSQQLPDNRTTELKTMEVPVKTSNAGLEGRTVVAAYLYQDGKLLARYVDWPQPLKHVHL
QQPQSLKVRISEDGSSVTLSSDAPVKGVALEVDDEDVKFDDNLVDLVPGEEVVIGVTGAS
KSTVFTTRYLGMSS

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	4	773	1.5e-91	0.7446808510638298

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	8.98e-80	1	653	7	627	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
407658	Mannosidase_ig	1.25e-14	684	777	1	91	Mannosidase Ig/CBM-like domain. This domain corresponds to domain 4 in the structure of Bacteroides thetaiotaomicron beta-mannosidase, BtMan2A. This domain has an Ig-like fold.
407625	Ig_mannosidase	3.15e-11	787	844	7	64	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.
236657	PRK10150	1.74e-10	58	324	62	293	beta-D-glucuronidase; Provisional
395572	Glyco_hydro_2	1.78e-10	197	297	2	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ49429.1|GH2	0.0	1	852	1	851
UKZ64740.1|GH2	0.0	1	852	1	850
UKZ90237.1|GH2	0.0	1	854	1	852
UKZ75961.1|GH2	0.0	61	852	3	770
UQC87618.1|GH2	0.0	1	852	26	875

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	5.72e-142	1	664	21	661	Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_B Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_C Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_D Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12]
2VJX_A	1.55e-118	5	837	7	817	Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482]
2JE8_A	1.63e-118	5	837	9	819	Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
7OP6_A	1.67e-118	5	837	9	819	Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482]
2WBK_A	4.36e-118	5	837	7	817	Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I2C092|MANBB_THETO	0.0	1	852	1	854	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
sp|A1D911|MANBB_NEOFI	8.28e-278	1	838	1	830	Beta-mannosidase B OS=Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) OX=331117 GN=mndB PE=3 SV=1
sp|Q4WAH4|MANBB_ASPFU	9.46e-277	1	838	1	830	Beta-mannosidase B OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=mndB PE=3 SV=1
sp|B0YBU9|MANBB_ASPFC	1.90e-276	1	838	1	830	Beta-mannosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=mndB PE=3 SV=1
sp|Q0CCA0|MANBB_ASPTN	7.13e-276	13	851	13	842	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000054	0.000000

TMHMM  Annotations     

There is no transmembrane helices in TRIREDRAFT_62166-t26_1-p1.