CAZyme Information: mRNA_M_BR32_EuGene_00024461-p1

Basic Information

• Species: Pyricularia oryzae
• Lineage: Ascomycota; Sordariomycetes; ; Pyriculariaceae; Pyricularia; Pyricularia oryzae
• CAZyme ID: mRNA_M_BR32_EuGene_00024461-p1
• CAZy Family: AA8
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1124	BR32_scaffold00002|CGC16	122600.89	6.3176

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PoryzaeBR32	14781	N/A	432	14349

• Gene Location: location=BR32_scaffold00002:2319451-2322903(-)

Full Sequence      

MDQGRSSAMSGCVILGPRAAPVPAIRLVLLPLLLLLSCFSFCEGMRPAQIADLRRETVEL
FYHGFDNYMEIAFPEDELRPVTCAPLTRDPKDPTNISLNDVLGNYSLTLVDSLSTLAILA
SAPKEDGDVGPKALRDFQDGVKALVEQYGDGTDGPSGQGLRARGFDVDSKVQVFETVIRG
VGGLLSAHLFAAGELPIRGYEPLPVFEGQEPKPWPNGMTYNGQLLRLANDLADRLLPAFY
TQTGMPYPRVNLRHGIPFYRNSPLHDTSGINDEPNGRGGAPEITETCSAGAGSLVLEFTV
LSRLTGDPKYEQLAKRAFWAVWYRRSDIGLIGAGVDAEHGKWIGAYSVIGAGADSFFEYA
MKTHILLSGHAPPKKASSTDSTPGKGNTNNSKRGLDPNILFPPLTDEENSPDSFLEAWHH
AHAATKRHLYNDRGHPHYVSVNLWTGSLASQWIDSLGAYYSGLLTLAGELDEAIETNLLY
AAVWTKYAALPERWNVRDKIVEGGLGWWPLRPEFVESTYFLYLATKDPWYLHVGEMVLRD
VTRRCKTSCGWAGLQNVIDGEMSDRMESFFLGETAKYMYLMYDENHPLNKIDAPFVFTTE
GHPLIIPKATEPGKSHPKASATRKHKAAASYYDPGFTNSCPVPKAPMPLTGSLTAARKDI
FHAAKMVNLHQTPVHSGRTVVEDTPGRKRATKENHSVFPWTLPSRLIPEDGICSKVHEPT
EITLEFASNAQQAVGGSSFNYMVGTQNLERLTVDKIRVLSISGLKLTLRLEDRAAGSSSP
TSYWRITKVNGLPLGRDESLVLNRATLGDVSDPRFNMVRDPVVVKLHHLHQVDLVYNVTA
AAEAAEGEGDVEIKERITLQQTQTESGVPMASAAVNAPDLGNRMKSFFQQIMSSLEEAGA
EPTYTPRSGNGVSTTPGTAAPPYNVLMNLTGITPTGLGAAPLPSVDMPPGAHIPHMGPFT
ASYLPWSTVFAAGDACGGPLPEMAPRDHHVIVIRRGGCSFSTKLANIPAHKRSSASLQLV
VVVSDDDEDDGFFRDGREGGGMAARDYDRIVRPLLDVMQTTPSGMVRHNPLSMLLVGGGD
AAYHQISQAERLGLTRRYYIESHGVRVRNILIDDGDSGELTLKA

Enzyme Prediction     

No EC number prediction in mRNA_M_BR32_EuGene_00024461-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	61	605	1.5e-142	0.9932735426008968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	1.06e-129	60	606	1	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	2.33e-57	54	608	72	520	glycoside hydrolase family 47 protein; Provisional
239039	PA_PoS1_like	0.002	971	1009	39	77	PA_PoS1_like: Protease-associated (PA) domain PoS1-like. This group includes various PA domain-containing proteins similar to Pleurotus ostreatus (Po)S1. PoSl, the main extracellular protease in P. ostreatus is a subtilisin-like serine protease belonging to the peptidase S8 family. Ca2+ and Mn2+ both stimulate the protease activity of (Po)S1. Ca2+ protects PoS1 from autolysis. PoS1 is a monomeric glycoprotein, which may play a role in the regulation of laccases in lignin formation. (Po)S1 participates in the degradation of POXA1b, and in the activation of POXA3, (POXA1b and POXA3 are laccase isoenzymes), but its effect may be indirect. The significance of the PA domain to PoS1 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
QBZ62593.1|GH47	0.0	1	1124	1	1124
VBB71678.1|GH47	0.0	44	1120	73	1143
AEO53259.1|GH47	0.0	33	1115	52	1107
CDP22661.1|GH47	0.0	44	1120	73	1156
AEO70189.1|GH47	0.0	45	1116	1	1023

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1FMI_A	1.49e-32	47	606	4	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	1.53e-32	47	606	4	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]
1X9D_A	4.33e-32	47	606	82	534	Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]
5KIJ_A	4.44e-32	54	606	6	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A	2.04e-31	54	606	6	451	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O94726|MNL1_SCHPO	1.26e-117	33	676	12	535	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mnl1 PE=3 SV=2
sp|Q92611|EDEM1_HUMAN	4.40e-113	43	606	119	586	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	5.34e-113	43	608	114	583	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|P38888|MNL1_YEAST	8.41e-108	28	608	7	504	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) OX=559292 GN=MNL1 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	5.87e-92	26	606	8	478	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.022802	0.977175	CS pos: 44-45. Pr: 0.8929

TMHMM  Annotations     

There is no transmembrane helices in mRNA_M_BR32_EuGene_00024461-p1.