CAZyme Information: H310_00419-t26_3-p1

Basic Information

• Species: Aphanomyces invadans
• Lineage: Oomycota; NA; ; Saprolegniaceae; Aphanomyces; Aphanomyces invadans
• CAZyme ID: H310_00419-t26_3-p1
• CAZy Family: CBM13
• CAZyme Description: hypothetical protein, variant 1

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
586		64407.37	7.0553

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AinvadansNJM9701	15416	N/A	168	15248

• Gene Location: location=KI913952:1427180-1429469(-)

Full Sequence      

MLALVDPVEFEAAVTRVIHTVSFDRDVTVSVFETTIRVIGGLLSAHMLATSGAVGSIHLT
YQGELVDLAVEVGTRLLPAFKTKTGLPVHRVNLKHGLVRNAPALTCPAAAGSLLLEFSVL
SRLSNIPDFEDAALDAVLALWDRRSELNLLGSTINVHTGEWVHTHTGIGAGLDSFYEYLL
KYYVMSGDSDFLDMFNQSYVSIEKHLLHPRDGYHREVDMSLGNQFVHSNRVSALQAFWPG
LQVLAGDLAAAVYSHQQLFDLWNEFGALPELYDRSGTGSVVEWAKHYPLRPELAESTYHL
YAATKDDKYLQIGRKLLQDIDDTSRVSCGYAAVGNVHDKRLEDRMDSFFLSETVKYLYLL
FSNDTSVVIPKTAVNRNALPASHVVFTTEGHLFPVVPSLYQDATSKRRKFRKPHQDRTCA
APYSLGRLTSKNAHLDAAVTIRHGNLHIKTLSASPAQFGYKLSDGRIDGALYAALDDVQT
ACQDLSALAQAIRGKIVLVKRGNCSFTRKALYVQQVGGIGMIAVNSKSSGGRDRTAHRLY
SLSDDGAGTHVTIPVVMVSKRDGLLLQNDVAHCDQELVVSLSMLLT

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	8	395	3.7e-111	0.8834080717488789

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	1.11e-115	9	395	52	453	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	9.53e-65	22	397	144	520	glycoside hydrolase family 47 protein; Provisional
239038	PA_C_RZF_like	2.95e-19	436	579	9	146	PA_C-RZF_ like: Protease-associated (PA) domain C_RZF-like. This group includes various PA domain-containing proteins similar to C-RZF (chicken embryo RING zinc finger) protein. These proteins contain a C3H2C3 RING finger. C-RZF is expressed in embryo cells and is restricted mainly to brain and heart, it is localized to both the nucleus and endosomes. Additional C3H2C3 RING finger proteins belonging to this group, include Arabidopsis ReMembR-H2 protein and mouse sperizin. ReMembR-H2 is likely to be an integral membrane protein, and to traffic through the endosomal pathway. Sperizin is expressed in haploid germ cells and localized in the cytoplasm, it may participate in spermatogenesis. 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.
239041	PA_EDEM3_like	8.44e-17	453	566	2	112	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	3.70e-16	455	571	2	109	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
AIG56058.1|GH47	2.28e-243	1	586	92	697
CCA23124.1|GH47	2.45e-174	1	562	90	681
CDS05465.1|GH47	3.06e-117	9	423	65	462
CAG1852391.1|GH47	1.29e-102	9	401	112	488
CAB4078645.1|GH47	3.59e-102	9	396	113	482

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1NXC_A	5.50e-42	9	408	81	478	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]
5KKB_A	8.89e-42	9	396	83	468	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]
5KIJ_A	1.24e-41	9	395	62	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	1.38e-41	9	395	67	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	1.43e-41	9	395	67	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q6GQB9|EDEM3_XENLA	3.03e-99	9	575	108	771	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q92611|EDEM1_HUMAN	2.54e-98	9	395	201	586	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	6.20e-98	9	395	196	581	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	1.74e-97	9	401	110	484	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1
sp|Q2HXL6|EDEM3_MOUSE	2.36e-96	9	575	123	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
1.000096	0.000000

TMHMM  Annotations     

There is no transmembrane helices in H310_00419-t26_3-p1.