CAZyme Information: VBB72615.1

Basic Information

• Species: Podospora comata
• Lineage: Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora comata
• CAZyme ID: VBB72615.1
• CAZy Family: AA3
• CAZyme Description: Putative Glycoside Hydrolase Family 47

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
627	LR026964|CGC23	69899.29	5.2551

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcomataTmat	13100	N/A	2652	10448

• Gene Location: location=LR026964:3939319-3941202(+)

Full Sequence      

MAILTARRFQRLALLTVVALVFYILLDQADYVAIPLVPKTGQYVQSTYDWARRRMKYPFD
ESKLIKLPEGIPLELPRIQYDFSQDEASESHIKTQKERQEAVKQAAKKSWNAYRKYAWGR
DELLPEKLTGKDTFAGWGATLVDSLDTLWIMGLKDEYKEAVQKTATINWDKTTSSHCSLF
ETTIRYLGGLLSAYDLNGDQVLLDKAVELGDMLYAGFDTPNHMPANSFNFREAKAGSLRP
SMGESSAAAGTLSLEFTRLAQLTGDPKYFNAISGVTRALEKTQDDTNLPGMWPVFIDVSR
NEPENPISAKGSSFSLGASADSAYEYFSKMYVLLGGLDPTYKKLHMKSMATARNHLLFRP
MLPDLYPATPPDVLLSGNVYANGQDIVDLQPQVQHLGCFAGGMFALGGKLFHEPAHVKIG
EQLARGCAWAYEAFPSGIMPEVSEIIPCPAPSSAPSSKDEEEEFPRCKWDDATYKEANTA
PGRYPKPFRAVQDPSYLLRPEAIESIFIAYRITGKKDLLDIAWRMFTAVQKATETNEAYT
AISDVNVAPGEEQADAHGRGGTRSRTKNSMESFWIAETLKYYYLIFSEPDLISLDDYVFN
TEAHPLKIPKPGKGAEGKEGLDTEKEA

Enzyme Prediction     

EC	3.2.1.113:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	107	608	1.5e-158	0.9932735426008968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	0.0	105	608	1	453	Glycosyl hydrolase family 47. Members of this family are alpha-mannosidases that catalyze the hydrolysis of the terminal 1,2-linked alpha-D-mannose residues in the oligo-mannose oligosaccharide Man(9)(GlcNAc)(2).
240427	PTZ00470	9.46e-134	61	611	43	521	glycoside hydrolase family 47 protein; Provisional
271200	LanM-like	0.004	187	272	598	676	Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VBB72615.1|GH47	0.0	1	627	1	627
CDP23506.1|GH47	0.0	1	627	1	628
CAP69486.1|GH47	0.0	1	627	1	628
AEO54071.1|GH47	5.67e-259	1	616	1	604
CAE76560.1|GH47	6.94e-236	5	627	6	656

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1FO2_A	1.60e-67	98	611	10	459	Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With 1-Deoxymannojirimycin [Homo sapiens],1FO3_A Crystal Structure Of Human Class I Alpha1,2-Mannosidase In Complex With Kifunensine [Homo sapiens]
5KIJ_A	2.55e-67	98	608	5	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1KKT_A	2.86e-67	65	610	1	510	Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KKT_B Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KRE_A Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRE_B Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_A Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_B Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum]
1FMI_A	2.97e-67	98	608	10	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
5KK7_A	7.49e-67	98	611	5	454	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens],5KK7_B Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase T688A mutant and Thio-disaccharide substrate analog complex [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q8H116|MNS2_ARATH	6.18e-77	50	608	44	537	Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS2 OS=Arabidopsis thaliana OX=3702 GN=MNS2 PE=1 SV=1
sp|Q9C512|MNS1_ARATH	1.26e-76	96	608	95	536	Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS1 OS=Arabidopsis thaliana OX=3702 GN=MNS1 PE=1 SV=1
sp|D4AV26|MNS1B_ARTBC	3.63e-68	100	608	42	507	Probable mannosyl-oligosaccharide alpha-1,2-mannosidase ARB_00035 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_00035 PE=1 SV=1
sp|B2GUY0|MA1B1_RAT	6.17e-67	97	611	206	656	Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Rattus norvegicus OX=10116 GN=Man1b1 PE=2 SV=2
sp|P31723|MAN12_PENCI	1.47e-66	65	610	1	510	Mannosyl-oligosaccharide alpha-1,2-mannosidase OS=Penicillium citrinum OX=5077 GN=MSDC PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000017	0.000003

TMHMM  Annotations     

Start	End
12	34