CAZyme Information: RhiirA1_401688-t46_1-p1

Basic Information

• Species: Rhizophagus irregularis
• Lineage: Mucoromycota; Glomeromycetes; ; Glomeraceae; Rhizophagus; Rhizophagus irregularis
• CAZyme ID: RhiirA1_401688-t46_1-p1
• CAZy Family: CE4
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
777		89198.42	6.8193

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RirregularisA1DAOM664342	26582	N/A	106	26476

• Gene Location: location=LLXH01001938:3350-7112(-)

Full Sequence      

MSEQRSNDLKSQAKDMFYHAFNNYMKYAFPDDELNPLQCTGRGSDKNDPQVFNDRKGFEK
AVRDVIKYVSFDQDNKVQVFEVNIRALGALLSAHLFITDPRFGYSIKGYNNELLKLAHDL
GKRLLPAFQKSKTGIPYARVNLKYGVPINETHETCTAAAGTLIIEFGVLSRLTNDTRFED
AAKKALFGLWNRRTDLNLLGNVINVQTGQWIHTASSTGAGIDSFYEYLLKAYVLFGETEY
LDMFNEAYNSVLRYVKDETGYLYRNVNMMNGGLMSNWVDSLSAYFPGLQVLAGDLDNAIK
SHLLYYNIWKKYNAMPERFNFHLRNVELATYPLRPEFIESTYFLYRATRDPFYLQVGEMV
LKDLEYYARVNCGFASIKDVLTKSLDERMESFLLSETFKYLYLLFDTEAHLIFLPQKYLK
KHSKIRPSMSGAERSFCSIYEKPSPSKHLFTTSVITSRSDADFARELVGFEERTLPLLDP
KGICEVPKSDPQVIEVSFGGLQESHEDDLIYQGQEQQQQIIKYVDGLIANRLKGLKLELT
KRVDKKGYDVTKVDNYRVFPGQTFEIRDPAVKDFWVKQQTYQTSVLRVYFYNENNYNAYN
YADYIAAVASFGPKITGELPIRTLVSVSSSLYGCVDYNIEETKLIEGNIIFVKRGNCTFV
DKVLKAQQAGAKGIVIWSNENYLFQPASAAEKNDIWKFEIPCVLITYENGVELSRILEEN
EKYIQEGKNSSNIKVKILSHEREPTTNIKTNENNELLLTIYGHAIRNIRLNLNLNGN

Enzyme Prediction     

EC	3.2.1.113:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	16	409	1.5e-125	0.9573991031390134

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	1.00e-132	16	410	1	449	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	6.66e-66	2	417	65	521	glycoside hydrolase family 47 protein; Provisional
238300	PA	5.75e-15	632	722	35	121	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.
239041	PA_EDEM3_like	2.14e-13	606	722	2	121	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.
240122	PA_subtilisin_1	7.70e-13	609	721	3	112	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CDS05465.1|GH47	8.40e-198	16	552	1	574
QRW05174.1|GH47	2.02e-175	2	718	45	819
QRV76268.1|GH47	2.43e-172	2	774	45	867
QRW19457.1|GH47	2.63e-167	2	718	44	862
CCA68810.1|GH47	3.07e-156	4	691	30	785

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KKB_A	2.04e-43	10	408	23	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	2.40e-43	10	408	21	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	2.04e-41	15	414	11	437	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A	2.16e-41	15	414	11	437	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	2.28e-41	15	414	16	442	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q92611|EDEM1_HUMAN	1.47e-147	9	408	130	565	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	3.54e-147	9	408	125	560	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|O94726|MNL1_SCHPO	3.69e-141	8	488	34	548	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mnl1 PE=3 SV=2
sp|Q6GQB9|EDEM3_XENLA	6.26e-121	9	747	38	797	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q2HXL6|EDEM3_MOUSE	1.93e-119	1	722	45	785	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Mus musculus OX=10090 GN=Edem3 PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000056	0.000000

TMHMM  Annotations     

There is no transmembrane helices in RhiirA1_401688-t46_1-p1.