CAZyme Information: KAG2013741.1

Basic Information

• Species: Coprinopsis cinerea
• Lineage: Basidiomycota; Agaricomycetes; ; Psathyrellaceae; Coprinopsis; Coprinopsis cinerea
• CAZyme ID: KAG2013741.1
• CAZy Family: GH18
• CAZyme Description: mannosyl-oligosaccharide 1,2-alpha-mannosidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
878		98263.12	4.8832

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Ccinerea326	15250	N/A	238	15012

• Gene Location: location=JAAGWA010000005:1935628-1939093(-)

Full Sequence      

MKWESYWSGCLIAVITVVLPRLPLFQTTDASDALVNPGWTAQRKLAAREKTRDLWYHGFD
NYMTHAFPMDELAPLSCAGQGPDWNNPANIARNDVAGNFSLTLVDVLDSFVILDDRPGFE
LAVKKVIEHVSFDVNTKPQVFETTIRVLGGLLSGHLYASQPDQPFYLPWYRGQLLELAYD
LGDRLLPAFSTPTGIPYARINLRQGIMKGETTETCTAGAGSLILEFGLLSRLTGDDRFEK
AAKKAYFGIWNRRSDLGIVGNTINSWNGQWTPPEVSGIGAGVDSFYEYALKWYIMSGEIE
FLDIWDDAYAAIMRYSRSLDGYWYRPVNMNTGDLAYYTVDSLSAFWPGLQVLAGDVEAAI
KLHMLYYNLWKHHAGLPEVYDTSFKVATSHQYPLRPEFIESTWYLYRATKDPFYLDVGER
VLFDLTTRAKVPCGLTGIADLRSNKRDDRMESFALSETLKYLYLLFDEDNALHRDDSDFV
LTTEGHIFKLPEVLKRASPPPSRKFISHQCPAYSPQEKGSKLPGLLQGVRYRPHVEYARS
LVGASASETDKKWWSADGWCEKPKLDVYSYEFILSVNGGTVPEDPSPSLKKLDVVSDGFV
INNVTGIRTKIVQRMDGKGFDVRKLGPYNVRPGQVVYINDTELFASPANGQLAQTAIWDR
DRTVDLHFMDFDTLSPQSTLESDSNVPRPADVDVVVTASTAQFGAHFLDVVKSETSSAPE
YLPIFYDKDNDRGCEPYQYSYPGSVLMVHRGTCSFLEKLKQARDASAVAVLVISDGDEPI
NPSAGAEDLLVAGKVNETAVVLVTNKVGLALLDLLEAAEAEGNKQLAVSSFSLPPTPNTK
TQEEEPKLKESKQEEEEDPRSRILYINSHPLLNTRLLI

Enzyme Prediction     

EC	3.2.1.113:6

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	56	489	3e-137	0.9910313901345291

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	2.76e-144	56	490	3	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	5.40e-76	48	491	73	519	glycoside hydrolase family 47 protein; Provisional
238300	PA	2.26e-13	703	808	2	109	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.
240120	PA_SaNapH_like	4.57e-07	733	799	31	104	PA_SaNapH_like: Protease-associated domain containing proteins like Streptomyces anulatus N-acetylpuromycin N-acetylhydrolase (SaNapH).This group contains various PA domain-containing proteins similar SaNapH. Proteins in this group belong to the peptidase M28 family. NapH is a terminal enzyme in the puromycin biosynthetic pathway; NapH hydrolyzes N-acetylpuromycin to the active antibiotic. 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.
239047	PA_GO-like	1.48e-06	696	778	19	95	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
QRW05174.1|GH47	1.11e-271	1	817	1	820
QRV76268.1|GH47	2.85e-270	1	878	1	865
CCA68810.1|GH47	1.48e-262	36	830	22	829
QRW19457.1|GH47	7.61e-248	1	878	1	910
CDZ96368.1|GH47	7.75e-201	24	824	13	904

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	3.50e-52	53	486	11	447	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	3.99e-52	53	486	16	452	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	4.17e-52	53	486	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]
5KK7_A	1.78e-51	53	486	11	447	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]
1X9D_A	2.05e-51	53	486	94	530	Crystal Structure Of Human Class I alpha-1,2-Mannosidase In Complex With Thio-Disaccharide Substrate Analogue [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|O94726|MNL1_SCHPO	5.44e-172	9	647	2	625	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	1.23e-143	29	521	112	610	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	1.63e-142	29	507	107	595	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q9FG93|MNS4_ARATH	2.97e-129	48	490	41	473	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	1.80e-125	43	486	33	474	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
0.148484	0.851492	CS pos: 30-31. Pr: 0.7347

TMHMM  Annotations     

There is no transmembrane helices in KAG2013741.1.