CAZyme Information: PADG_04264-t30_1-p1

Basic Information

• Species: Paracoccidioides brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; NA; Paracoccidioides; Paracoccidioides brasiliensis
• CAZyme ID: PADG_04264-t30_1-p1
• CAZy Family: GH27
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
875		100586.96	5.8686

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PbrasiliensisPb18	8522	502780	132	8390

• Gene Location: location=KN275960:2353103-2356036(+)

Full Sequence      

MRFALRRRAVGSPRSLVEIIERSVIPLDQGWVFKQADDQEAQFLSVSQFPTNVHLDLMHH
GLIPDPFIGKNELHVQWVGEKSWIYKTSFDTPTIGDGQKAVLAFDGLDTYATVLLNDTKI
LETENMFVPERVDVTELLRKSTGPNVLHITFSSTFLIGKKIQEQYPKHFWGSWNGDPSRL
AVRKAQYHYSWDWGPTLMTCGPWRPINLEIYNARISDLHVRQNVEKSLKHAILAATAEVE
GDAEKVIFKFLLDGKEICSETTEVEYGVATATLNVHNPQLWYPSRYGKQPLYTLSASLLS
SNGVEVDSASQRFGLRRAELVQRKLDDAEGTSFFFEINNIPVFCGGSNWIPADNFIPRIS
PQKYRDWVKLMVNGNQVMARVWGGGIFEEQVFYDACDELGLLVWQDFLFSCGNYPAFPSF
LENVKREAVANVKILRHHPSIVIWAGNNEDYQYAESENLEYDPKDINPNNWLKSSFPARY
IYEKILVDVTKELIPDTYYHFGSPWGGNTTKDPTIGDIHQWNVWHGTQEKYQNFDKLSGR
FVSEFGMQAFPAMETIDGYLLEGIDNPDRYPQSSTVEFHNKAAGHERRMALYLAENVKYT
TDPFERYVYCTQLMQAECLASAFRLWKRQWKGPGREYCAGALLWQINDCWPGTSWSIVDY
HLRPKLAYYAVKREMNPITIGLKRTTHTEYVDKYTHAYYKTTHKIEMWATNFTLETKNVS
VLIKGWDVVTAQRTYFQELPDCVVLEQNRSTEIIEFELPVESSGEGSEGWKDKAPRTVVA
AYLFDDGKQIARYVNWPEPLKYVPLQHRDLKLIQSAEPNLLELSAEVPIKGVVLYADDDR
KVFDDNFMDLVPEETVYIHTKGPGKICSVRHLGKD

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	20	717	1.3e-94	0.648936170212766

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	8.16e-82	13	672	1	627	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
395572	Glyco_hydro_2	2.35e-13	213	316	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
236657	PRK10150	4.60e-12	22	343	10	293	beta-D-glucuronidase; Provisional
407658	Mannosidase_ig	4.38e-11	704	802	2	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	0.003	821	859	17	55	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
QSS62028.1|GH2	0.0	21	873	3	858
QSS71278.1|GH2	0.0	21	873	3	858
UQC87618.1|GH2	0.0	14	873	21	874
EAA35570.1|GH2	0.0	22	873	4	852
ATZ49691.1|GH2	0.0	6	873	13	877

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	3.41e-143	24	863	26	813	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	7.13e-118	24	681	8	657	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	7.48e-118	24	681	10	659	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	7.66e-118	24	681	10	659	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	2.00e-117	24	681	8	657	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	22	873	4	853	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
sp|A1D911|MANBB_NEOFI	5.33e-279	26	862	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	1.73e-277	26	862	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	3.96e-276	26	862	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|Q0CCA0|MANBB_ASPTN	5.24e-276	27	858	9	826	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
1.000034	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PADG_04264-t30_1-p1.