CAZyme Information: FUN_010688-T1-p1

Basic Information

• Species: Rhizophagus irregularis
• Lineage: Mucoromycota; Glomeromycetes; ; Glomeraceae; Rhizophagus; Rhizophagus irregularis
• CAZyme ID: FUN_010688-T1-p1
• CAZy Family: GH5
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
861		99236.08	6.9233

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_RirregularisC2	25634	N/A	90	25544

• Gene Location: location=CP080906:2437673-2441875(+)

Full Sequence      

MQPLNRPSHKRAFHYISLYNFAYIIFWIIFMLSVVVNKVNGMSEQRSNDLKSQAKDMFYH
AFNNYMKYAFPDDELNPLQCTGRGSDKNDPHNTIINDVLGDYSLTLVDCLDTFVVFNDRK
GFEKAVRDVIKYVSFDQDNKVQVFEVNIRALGALLSAHLFITDPRFGYSIKGYNNELLKL
AHDLGKRLLPAFQKSKTGIPYARVNLKYGVPINETHETCTAAAGTLIIEFGVLSRLTNDT
RFEDAAKKALFGLWNRRTDLNLLGNVINVQTGQWIHTASSTGAGIDSFYEYLLKAYVLFG
ETEYLDMFNEAYNSVLRYVKDETGYLYRNVNMMNGGLMSNWVDSLSAYFPGLQVLAGDLD
NAIKSHLLYYNIWKKYNAMPERFNFHLRNVELATYPLRPEFIESTYFLYRATRDPFYLQV
GEMVLKDLEYYARVNCGFASIKDVLTKSLDERMESFLLSETFKYLYLLFDTENKINSMDD
NFIFTTEAHLIFLPQKYLKKHSKIRPSMSGAERSFCSIYEKPSPSKHLFTTSVITSRSDA
DFARELVGFEERTLPLLDPKGICEVPKSDPQVIEVSFGGLQESHEDDLIYQGQEQQQQII
KYVDGLIANRLKGLKLELTKRVDKKGYDVTKVDNYRYTFRYYIFPGQTFEIRDPAVKDFW
VKQQTYQTSVLRVYFYNENNYNAYNYADYIAAVASFGPKITGELPIRTLVSVSSSLYGCV
DYNIEETKLIEGNIIFVKRGNCTFVDKVLKAQQAGAKGIVIWSNENYLFQPASAAEKNDI
WKFEIPCVLITYENGVELSRILEENEKYIQEGKNSSNIKVKILSHEREPTTNIKTNENNE
LLLTIYGHAIRKNVLCTNFKT

Enzyme Prediction     

No EC number prediction in FUN_010688-T1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	57	491	2.7e-145	0.9932735426008968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	8.65e-148	57	489	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	7.30e-77	38	496	60	521	glycoside hydrolase family 47 protein; Provisional
238300	PA	5.46e-15	717	807	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	2.40e-13	691	807	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	8.61e-13	694	806	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	5.45e-228	57	631	1	574
QRW05174.1|GH47	4.25e-196	43	803	45	819
QRV76268.1|GH47	3.33e-192	43	803	45	819
QRW19457.1|GH47	6.24e-188	40	803	41	862
CCA68810.1|GH47	5.19e-180	45	776	30	785

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KKB_A	2.15e-51	51	489	23	463	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	2.60e-51	51	489	21	461	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	5.53e-49	56	489	11	447	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	6.28e-49	56	489	16	452	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	6.55e-49	56	489	16	452	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|Q92611|EDEM1_HUMAN	1.12e-170	50	491	130	584	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	1.34e-170	50	496	125	584	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|O94726|MNL1_SCHPO	2.13e-166	39	567	24	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	1.65e-137	27	832	15	797	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q2HXL6|EDEM3_MOUSE	5.38e-136	42	807	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
1.000020	0.000002

TMHMM  Annotations     

Start	End
13	35