CAZyme Information: SPSK_01456-t39_1-p1

Basic Information

• Species: Sporothrix schenckii
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Sporothrix; Sporothrix schenckii
• CAZyme ID: SPSK_01456-t39_1-p1
• CAZy Family: AA8
• CAZyme Description: beta-mannosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
893	AXCR01000005|CGC9	99720.50	4.9543

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Sschenckii1099-18	10434	1397361	141	10293

• Gene Location: location=AXCR01000005:1209202-1211883(-)

Full Sequence      

MASSPSHPRVVVPVDQGWSFKQADQDDTHWLPVGQFPTNVHLDLLAHERIPDPFVGKNEE
LVQWIGETTWVYKTTFALDKAASSSGGNKTVLAFDGLDTFATVVLNGKTILESDNMFLPY
RVDVTDSVRADGPNDLVITFDSAYLRGWDLVEQHPDHKWGCWNGDNSRLAVRKSQYHWGW
DWGPVLLTCGPWRPIHVEVYDARLSDLSFDTTVDESLRSATVAARAEVEAGSVAGTRVRF
DVSLDGVAVASETVDVAAKEKSSDDDNDNTDDTPDGIATATFLINSPALWYPARYGKQPL
YTVRATLLVGVTEADKATKKIGLRRSRLVQQPLEGQPGTSFFFEVNNVPIFCGGSDWIPA
DNFVPRISGQRYHDWVKLAVDGHQAMIRVWGGGIYEEQAFYDACDELGVLVWQDFMFGCG
NYPAWPALRDSIRREAAANVRLLRHHPSIVIWAGNNEDYQYQESEGLTYDYANKDAESWL
QTDFPARYIYEKILADVCRALIPGTPYHYGSPWGGGVDTHDPTVGDIHQWNVWHGTQEKY
QNFDRLVGRFVSEFGMEAFPSVRTIDQFLPNGRDDADRYPQSATLDFHNKADGHERRIAL
YLVENLRYAPDPLEQFVYCTQLMQAECLASAYRLWKRQWQGPGRAYCGGALVWQLNDCWP
VTSWSICDYYLRPKHAYFTVKREMAPVTVGMTRREHAHSRAGGHSHSRIDIARRTQIEIW
GSNLTLHDIDGVDCVVRAWDVETGKLTYEGTVAEGIVLKANRSTELAALDVPGVKGDEAK
TVVAAYLEASSKQIARYVNWPEPLKYLHLAKPDLTVDVVTSSGDAVVAVAVRSDVPVKGV
AVEVHEDTPNAEADAVRFDDNLVDLVPGETVQLGVTGATASTRFTTRYLGLSS

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	11	791	1.9e-95	0.7167553191489362

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	6.18e-84	3	681	4	627	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
407658	Mannosidase_ig	2.16e-15	715	806	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.
236673	ebgA	2.16e-10	69	459	110	452	cryptic beta-D-galactosidase subunit alpha; Reviewed
395572	Glyco_hydro_2	2.51e-08	202	324	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
407625	Ig_mannosidase	7.84e-05	811	883	1	64	Ig-fold domain. This Ig-like fold domain is found in mannosidase enzymes.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UQC87618.1|GH2	0.0	9	891	29	875
AFJ59925.1|GH2|3.2.1.25	0.0	8	891	3	854
AEO53082.1|GH2	0.0	8	891	3	854
AEO69937.1|GH2	0.0	8	891	3	850
EAA35570.1|GH2	0.0	8	891	3	853

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	3.60e-129	11	691	26	660	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	4.97e-112	11	876	8	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	5.21e-112	11	876	10	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	5.33e-112	11	876	10	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	1.38e-111	11	876	8	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	8	891	3	854	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
sp|A1D911|MANBB_NEOFI	4.37e-293	13	877	8	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|A1CGA8|MANBB_ASPCL	1.00e-291	13	877	8	830	Beta-mannosidase B OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=mndB PE=3 SV=1
sp|Q4WAH4|MANBB_ASPFU	8.10e-291	13	877	8	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	1.15e-290	13	877	8	830	Beta-mannosidase B OS=Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) OX=451804 GN=mndB PE=3 SV=1

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 SPSK_01456-t39_1-p1.