CAZyme Information: PIW_T008323-RA-p1

Basic Information

• Species: Globisporangium iwayamae
• Lineage: Oomycota; NA; ; Pythiaceae; Globisporangium; Globisporangium iwayamae
• CAZyme ID: PIW_T008323-RA-p1
• CAZy Family: GH72
• CAZyme Description: ER degradation-enhancing alpha-mannosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
731	PiwaDAOMBR242034_SC01479|CGC1	80624.87	6.3163

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_GiwayamaeDAOMBR242034	14874	1223558	0	14874

• Gene Location: location=PiwaDAOMBR242034_SC01479:207-2402(+)

Full Sequence      

MYFMCTLLTSVLLVGSGGVAVADAKMHASEMSHLQEQAREMFYHGYRNYMEHAFPWDELK
PLSCEGRRWDKRERGDLDDVLGGYSLTLIDSLDMLAIIGDRDEFVRAVKLVIEHVSFDRD
VVVSVFESTIRVIGGLISAHMLASSDHLGIMTAQEYDGELLDLAVDLGTRLLPAFDTPTG
LPVHRINLKHGVVKNTPTITCPAAAGSLLVELSYLSRLSSLPLFEEKASNAVMALWLRRS
DLDLLGSAIDVASGEWVHSHVSIGAGLDSYFEYLLKYHLVSGNSVWLEMFNMSYNAVETH
VNHDDMHIEVDMNYGKQYVRSRRVSALQAFWPGLQVLAGEVSSAIRSHDKLFSLWDKFGA
MPELFDLAGAGSVISWARTSPLRPELIESTYHLYQATRDHKYLKIGRKLLQDIQRVSRVS
CGYAAVGNIHTLDVEDRMDSYFLSETVKYLYLLFNENPDVIVPSFQLTNSSTLSSSTNTS
SRNASSQCTSRDSTRALKSSQVIFSTEGHLLMLDSTLFARGNETQNVLPHAECENSNLLS
KMQSTSDSETASSKVVAPSQQIGISVRLDDVHVMTLVAWPAVFGLQISPPIHIEAPLMLY
AKSVGDACLEISKADAKRVKGKIVMVTRGVCPFSEKALRMQSAGAAGVIIVNSKTSKSRH
PDRKYVLTDGKRGLGRQVVIPVMLVSREDAAQLHRHVANLQSVTPEAEDGSSGGSDPESS
LLLGSLSSWLY

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	41	511	6.4e-131	0.9932735426008968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	6.76e-124	41	511	1	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	1.11e-65	36	463	74	503	glycoside hydrolase family 47 protein; Provisional
240122	PA_subtilisin_1	7.46e-16	580	693	2	104	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.
238300	PA	2.99e-14	590	704	15	123	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.
240120	PA_SaNapH_like	2.48e-11	589	695	13	110	PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. The significance of the PA domain to these proteins has not been ascertained. 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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA23124.1|GH47	1.08e-269	25	731	21	727
AIG56058.1|GH47	2.96e-244	26	700	24	681
CAD7086284.1|GH47	1.74e-129	26	705	33	752
AGB92969.1|GH47	2.39e-128	4	685	23	738
BAD52943.1|GH47	8.44e-128	18	462	33	463

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	3.75e-46	31	461	2	435	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A	3.99e-46	31	461	2	435	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]
1FMI_A	4.23e-46	31	461	7	440	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	4.40e-46	31	461	7	440	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]
1X9D_A	1.80e-45	31	461	85	518	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|Q9FG93|MNS4_ARATH	4.89e-121	30	511	36	471	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q92611|EDEM1_HUMAN	5.29e-119	34	460	130	568	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	3.55e-118	34	458	125	562	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q2HXL6|EDEM3_MOUSE	2.75e-113	24	720	43	809	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Mus musculus OX=10090 GN=Edem3 PE=1 SV=2
sp|Q9BZQ6|EDEM3_HUMAN	3.93e-113	13	658	30	741	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
0.000280	0.999652	CS pos: 22-23. Pr: 0.9581

TMHMM  Annotations     

There is no transmembrane helices in PIW_T008323-RA-p1.