CAZyme Information: EDK41928.1

Basic Information

• Species: Lodderomyces elongisporus
• Lineage: Ascomycota; Saccharomycetes; ; Debaryomycetaceae; Lodderomyces; Lodderomyces elongisporus
• CAZyme ID: EDK41928.1
• CAZy Family: AA2
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
945	CH981524|CGC1	109298.81	5.3477

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LelongisporusNRRLYB-4239	5908	379508	109	5799

• Gene Location: location=CH981524:296321-299158(+)

Full Sequence      

MRQLSNWQFQLPSFQNFSHITNADNFYPQSTPPLFYNYKDDIPMQIVLDKWYDSDPHGNG
GHQIHLDLLYNKLIVDPFSNDFAEGMQWIGKVQWVYRCRFNISDISTIGSAMGTTVGSTM
TATTQIQNSLGTVDDDTFTQNATLIFEGLDTIAHVTLNNESILDSHNAFHNHIVPVNLLQ
ANELIIHFESSWSYGKEMENRHGKIPEDHCWNGDCSRLYVRKPQYQYGWDWGPKLLTCGP
WKPVKLVVEEYLIENSIEDLIPAFIEDFFVNYELIDNDAKVWFLLRWLQPTKRKVTTTNI
AAKIIVKLEHDVVLNKVLSIEEFDNTFGSNKANRNKSATVFTLQNVKLWYPYKLGKPTLY
TIQLYFNDKLVSTQQVGFRKVELIQKPDTYGESFYFKINNIPVQMLGSNWIPPHYFHNKV
NLTTYENLLELVVKSNQNMIRVWGGGQYENNEFYAKCDEMGIMVWQDFMFACGVYPNNPF
FLELVQKEVEDQLIKLHHFASIVIFAGNNEDYQIADALQLDIHNSTQFPAGVIYETLIPD
LVKEFCNQVVYRFGSPYSDTNHSSYDLSIGDSHQWEVWHGSRKPYQNWPELAARFISEFG
MLAFPSEGLLAKYISFKELYLNLTILQYHNKAMNGAVNLEHYVLSNFDKPTHLKLSKWIY
LTQLMQMEATSQAFRYWRRKWQDYQVGGVLVWQLNDCWPAISWSIIDFLGVPKLSYYGLK
RELADSAISAYRHQSNSKTISKEANSEEKRQIVLKNNEAFYQVETTLLDVWAFVCDDTDL
TLEIQAFDANSGDHVLTYRKSNLSLVPHSVNELLVDQRFDWLGKDNKILCLRLIDNHGEV
IARSSDWPQPLKLINFTKLGKGLEISILEVSQDEGSRNGENCQVDIQLTTNKPVKGLELY
IEGHNQCICDENGIDLFPNDPQIVSINGLCEEDVHKVKYRHLGDL

Enzyme Prediction     

EC	3.2.1.25:3

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	132	778	4.5e-70	0.5917553191489362

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
225789	LacZ	1.96e-52	144	768	84	681	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
395572	Glyco_hydro_2	5.46e-09	263	379	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
407658	Mannosidase_ig	5.88e-07	768	852	3	90	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCG20510.1|GH2	2.06e-275	1	943	1	832
CCE41561.1|GH2	8.94e-268	49	943	26	828
AOW31022.1|GH2	2.00e-260	46	945	21	816
CAX39789.1|GH2	1.42e-257	35	942	10	812
ABN65300.2|GH2	4.39e-211	44	942	1	837

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	5.26e-99	64	729	52	659	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	2.49e-87	45	729	19	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	2.58e-87	45	729	21	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	2.63e-87	45	729	21	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	6.67e-87	45	729	19	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	5.89e-149	64	943	35	853	Beta-mannosidase B OS=Thermothelomyces thermophilus OX=78579 GN=man9 PE=1 SV=1
sp|Q5B7W2|MANBB_EMENI	1.19e-138	64	943	36	842	Beta-mannosidase B OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=mndB PE=1 SV=2
sp|Q0CCA0|MANBB_ASPTN	1.89e-136	64	943	36	842	Beta-mannosidase B OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=mndB PE=3 SV=2
sp|A1CGA8|MANBB_ASPCL	2.96e-135	64	943	36	844	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|A1D911|MANBB_NEOFI	8.63e-134	64	943	36	844	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000012	0.000056

TMHMM  Annotations     

There is no transmembrane helices in EDK41928.1.