CAZyme Information: evm.model.AC2VRR_s00060g40-p1

Basic Information

• Species: Albugo candida
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo candida
• CAZyme ID: evm.model.AC2VRR_s00060g40-p1
• CAZy Family: GH28
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
690		77791.96	7.0328

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Acandida2VRR	15896	911350	72	15824

• Gene Location: location=Acan2VRR_SC060:76394-78466(+)

Full Sequence      

MFYHGYNNYMEHAFPWDELKPLTCEGRRWDRRERGDLDQTLGGFSLTLIDSLDMLAILGD
HKEFRRAVKLVIQHVTFDRNVTVSVFESAIRVIGGLLSAHVLASSDYVGLMPPPEYTNEL
LELAVDLATRLLPAFDTPTGIPMDRINLMHGISKHGPFVTCPAAGSVLVEFSYLSRLSKN
PIFEKKARVAVLAVWERRSQLDLLGSSIDVLSGTWTSSHVGIGAGTDSFYEYLLKYHILT
GEASWLDIFNSSYTAVEAHTKFNDLHVEVDMHYGNRRIRYPRVSALQAFWPGLQVLAGDV
INAVKSHDKLFDLWVKFGAMPELFDLRGGGAVVEWARASPLRPELIESTYHLYQATRNHK
YLKVGRKLLHDIEAVSRVPCGYAAVKDIYTLEVEDRMDSYFLSETIKYLYLLFSDDPSVI
VPSTYIGKTHTVSNVSAFGTTNCFDGEGYWTRPVKSSEIIFSTEGHILLTAPELYRRNSS
HQMAILHQCESSTGFENNQVESLSSRKYSSSGYMPLGLSVRYKNTHVGTILASPAKFGQQ
IINTKLTLEAFFDLEPVGNGCDTISPSSLLSERISGKMVMVYRGNCTFARKALNLEQAGA
AGVVIINTARVPYKKYRTQFYLIWDDRSKIGQNVSIPVLMVLAEDVNRLVQLIKDHELKS
LLTVKNHRKHKQSFLEEEDEIVVSLSSWLW

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	1	468	2e-131	0.9932735426008968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	4.94e-133	1	468	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	1.01e-73	1	420	79	502	glycoside hydrolase family 47 protein; Provisional
239041	PA_EDEM3_like	6.28e-12	532	657	2	120	PA_EDEM3_like: protease associated domain (PA) domain-containing EDEM3-like proteins. This group contains various PA domain-containing proteins similar to mouse EDEM3 (ER-degradation-enhancing mannosidase-like 3 protein). EDEM3 contains a region, similar to Class I alpha-mannosidases (gylcosyl hydrolase family 47), N-terminal to the PA domain. EDEM3 accelerates glycoprotein ERAD (ER-associated degradation). In transfected mammalian cells, overexpression of EDEM3 enhances the mannose trimming from the N-glycans, of a model misfolded protein [alpha1-antitrypsin null (Hong Kong)] as well as, from total glycoproteins. Mannose trimming appears to be involved in the selection of ERAD substrates. EDEM3 has a different specificity of trimming than ER alpha-mannosidase 1. The significance of the PA domain to EDEM3 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.
238300	PA	2.96e-10	574	657	45	120	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.
239047	PA_GO-like	4.11e-10	535	641	24	117	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
CCA23124.1|GH47	0.0	1	690	37	727
AIG56058.1|GH47	2.99e-215	1	649	39	674
QCQ78383.1|GH47	2.36e-130	1	474	53	483
QCE07576.1|GH47	5.37e-130	1	474	42	472
BAT94804.1|GH47	1.61e-128	1	474	42	472

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KKB_A	1.58e-48	1	416	29	448	Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus],5KKB_B Structure of mouse Golgi alpha-1,2-mannosidase IA and Man9GlcNAc2-PA complex [Mus musculus]
1NXC_A	1.89e-48	1	416	27	446	Structure of mouse Golgi alpha-1,2-mannosidase IA reveals the molecular basis for substrate specificity among Class I enzymes (family 47 glycosidases) [Mus musculus]
5KIJ_A	1.96e-47	1	429	12	444	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	2.22e-47	1	429	17	449	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	2.31e-47	1	429	17	449	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9FG93|MNS4_ARATH	2.43e-127	1	474	47	477	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q2HXL6|EDEM3_MOUSE	1.99e-117	1	680	60	806	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Mus musculus OX=10090 GN=Edem3 PE=1 SV=2
sp|Q9BZQ6|EDEM3_HUMAN	5.57e-117	1	680	59	805	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Homo sapiens OX=9606 GN=EDEM3 PE=1 SV=2
sp|Q9BV94|EDEM2_HUMAN	3.87e-115	1	466	42	478	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Homo sapiens OX=9606 GN=EDEM2 PE=1 SV=2
sp|Q8BJT9|EDEM2_MOUSE	7.44e-115	1	466	42	478	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Mus musculus OX=10090 GN=Edem2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000045	0.000000

TMHMM  Annotations     

There is no transmembrane helices in evm.model.AC2VRR_s00060g40-p1.