CAZyme Information: KDQ29257.1

Basic Information

• Species: Pleurotus ostreatus
• Lineage: Basidiomycota; Agaricomycetes; ; Pleurotaceae; Pleurotus; Pleurotus ostreatus
• CAZyme ID: KDQ29257.1
• CAZy Family: GH31
• CAZyme Description: glycoside hydrolase family 47 protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
884		98690.59	5.4322

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PostreatusPC15	12460	1137138	164	12296

• Gene Location: location=KL198007:1900285-1903773(-)

Full Sequence      

MLWKYWPEALFAGVLISLRCLAWGTDSSATNLSTSSYDPWTTQRKIAVRERTRQLWYHGF
DNYMTFAFPLDELSPLSCTGRGPDWDNPSNIATNDVAGNFSLTLIDVLDTLVVLNDRPRF
EIAVRNVIDWVNFDVNTKPQVFETTIRVLGGLLSGHIFASQTGQPFHLPWYKGELLKMAK
DLGERLLPAFATPTGMPYARVNLRHGVMKGETQETCTAGAGSLILEFATLSRLTGDDRFE
KAAYKAFFALWNRKSDIGLVGNTINTFSGLWSHPEITGIGAGIDSFYEYALKWYILIGEV
EFLDVWKDSYAALMRYSRAVDGYWYRNVNIHSGDVSYYTIDSLSAFWPGLQVLSGDVQNA
IKSHMMYWNLWRAHSGLPEVYDTNFKTATSFQYPLRPELAESTWYLYRATRDTFYLDVGE
RIFEDLENRAKVGCGLTGIADLRTNKRDDRMESFALSETLKYLYLLFDEENPLHSDDSNY
VFTTEGHLLTLPRHLLRPVPPARLQFRQNESHQCPAYHPFVHSYPNQKKPKRGRGLTLGI
RSRSDIDYSRELLALLPDSADRDASSPDGWCEQPKVETYSYDFILSADGQATPEDPLPSQ
LKLAAISGGYIIHNITGIRTHIVRRLDGKGYDITKLGPHAVKTGQIVYINDTALFGPKKD
VEQTPLPPAPHSDGVVPLRFFVDLMDPTLRANTIDGSSELDAVMTAWTSTFGGKLVSEPG
SEPIQFAHGEGVVVASEDSNLLGCNPYERDFDGAAVLVRRGECTFVEKLLHAKSAGASGV
IVISDIESRLNPSADAEDLDQAGDISDVALVVLPPSSGFVVDQLLKLTESTGMGRLVVTL
VPEGQPAMHDEGHIPAELPSRTQQTKKRILYLNGHPLVNTQLLN

Enzyme Prediction     

EC	3.2.1.113:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	57	490	9.7e-141	0.9910313901345291

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	3.35e-148	57	489	3	451	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	1.43e-76	49	494	73	521	glycoside hydrolase family 47 protein; Provisional
238300	PA	3.51e-12	738	805	27	99	PA: Protease-associated (PA) domain. The PA domain is an insert domain in a diverse fraction of proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following: i) various signal peptide peptidases including, hSPPL2a and 2b which catalyze the intramembrane proteolysis of tumor necrosis factor alpha, ii) various proteins containing a C3H2C3 RING finger including, Arabidopsis ReMembR-H2 protein and various E3 ubiquitin ligases such as human GRAIL (gene related to anergy in lymphocytes), iii) EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein), iv) various plant vacuolar sorting receptors such as Pisum sativum BP-80, v) glutamate carboxypeptidase II (GCPII), vi) yeast aminopeptidase Y, vii) Vibrio metschnikovii VapT, a sodium dodecyl sulfate (SDS) resistant extracellular alkaline serine protease, viii) lactocepin (a cell envelope-associated protease from Lactobacillus paracasei subsp. paracasei NCDO 151), ix) various subtilisin-like proteases such as melon Cucumisin, and x) human TfR (transferrin receptor) 1 and 2.
240122	PA_subtilisin_1	1.07e-10	708	798	2	88	PA_subtilisin_1: Protease-associated domain containing subtilisin-like proteases, subgroup 1. A subgroup of PA domain-containing subtilisin-like proteases. The significance of the PA domain to many of the proteins in which it is inserted is undetermined. It may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate. Proteins into which the PA domain is inserted include the following subtilisin-like proteases: i) melon cucumisin, ii) Arabidopsis thaliana Ara12, iii) Alnus glutinosa ag12, iv) members of the tomato P69 family, and v) tomato LeSBT2. However, these proteins belong to other subtilisin-like subgroups. Relatively little is known about proteins in this subgroup.
239047	PA_GO-like	2.22e-09	692	825	9	129	PA_GO-like: Protease-associated domain containing proteins like Arabidopsis thaliana growth-on protein GRO10. This group contains various PA domain-containing proteins similar to the functionally uncharacterized Arabidopsis GRO10. The PA domain may be a protein-protein interaction domain. At peptidase active sites, the PA domain may participate in substrate binding and/or promoting conformational changes, which influence the stability and accessibility of the site to substrate.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA68810.1|GH47	6.83e-281	40	833	27	822
QRW05174.1|GH47	2.40e-272	1	851	1	841
QRV76268.1|GH47	1.10e-271	1	882	1	863
QRW19457.1|GH47	1.60e-262	1	883	1	909
CDZ96368.1|GH47	2.11e-215	34	824	18	889

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	2.36e-51	58	491	15	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	2.69e-51	58	491	20	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	2.81e-51	58	491	20	456	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]
5KK7_A	1.19e-50	58	491	15	451	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]
1X9D_A	1.35e-50	58	491	98	534	Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O94726|MNL1_SCHPO	9.19e-165	44	651	31	616	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mnl1 PE=3 SV=2
sp|Q925U4|EDEM1_MOUSE	2.10e-141	43	495	120	585	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q92611|EDEM1_HUMAN	2.44e-141	43	495	125	590	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q6GQB9|EDEM3_XENLA	2.98e-125	41	814	31	750	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q9BZQ6|EDEM3_HUMAN	3.32e-125	28	814	32	763	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Homo sapiens OX=9606 GN=EDEM3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.218040	0.781940	CS pos: 24-25. Pr: 0.7621

TMHMM  Annotations     

There is no transmembrane helices in KDQ29257.1.