CAZyme Information: ALNC14_092670:RNA-p1

Basic Information

• Species: Albugo laibachii
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo laibachii
• CAZyme ID: ALNC14_092670:RNA-p1
• CAZy Family: GH5
• CAZyme Description: ER degradationenhancing alphamannosidaselike protein putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
727		81946.82	7.2950

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AlaibachiiNc14	14629	890382	180	14449

• Gene Location: location=FR824226:25818-28001(+)

Full Sequence      

MRLHAVVLLLMCIFRELYARKFHSSERIHLKNKAREMFYHGYNNYMEHAFPWDELKPLTC
EGRRWDRRERGDLDQTLGGFSLTLIDSLDMLAILGDHEEFRHAVKLVIQHVTFDRNVTVS
VFESAIRVIGGLLSAHVLASSSYVGLMPPSEYKSELLDMAIDLATRLLPAFDTPTGIPVD
RINLLHGLNKHGSSLTCPAAGSVLVEFSYLSRLSKNPIFEQKARKAVLAVWERRSHLDLL
GSSIDVLSGTWESSHVGIGAGTDSFYEYLLKYHILTGEASWLEIFNSSYTAVEAHTKFND
LHVEVDMHHGNRKIRYPRISALQAFWPGLQVLAGDVVNAVKSHDRLFELWVKFGAMPELF
DLRGAGVVVDWARASPLRPELIESTYHLYQATRDHKYLKIGRKLLHDIESVSRVPCGYAA
VKDIYTLEVEDRMDSYFLSETIKYLYLLFSDNPSVIVPSIYVGSIHTTLNVSVFGTSNCI
DGEGYWTRPVKSSQVIFSTEGHILLTAPELYRRNPSHRMSNSYQCQSSTGFDDHLVDSLS
SKKSSFSGYMPLGLSVRHKNIHVGTILASPAKFGKQIYNTKVTVESLFDLEPVGNGCDTI
SPSSLLGERIFGKLVMVYRGNCTFARKALNLEQAGASGVIIINTARVPYKKYRNQFYLIW
DDRSKAGRNVSIPVLMVLAEDVTRLVGLIRDQELNSILTTRNGIKNEIPTLEDEEDGIVA
SLSSWLW

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	37	504	3.2e-134	0.9932735426008968

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	1.71e-133	37	504	1	451	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	1.58e-72	15	458	57	503	glycoside hydrolase family 47 protein; Provisional
239041	PA_EDEM3_like	2.93e-11	568	675	2	102	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	5.71e-11	570	693	2	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.
239042	PA_hPAP21_like	1.50e-09	577	681	5	98	PA_hPAP21_like: Protease-associated domain containing proteins like the human secreted glycoprotein hPAP21 (human protease-associated domain-containing protein, 21kDa). This group contains various PA domain-containing proteins similar to hPAP21. Complex N-glycosylation may be required for the secretion of hPAP21. The significance of the PA domain to hPAP21 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
CCA23124.1|GH47	0.0	1	727	1	727
AIG56058.1|GH47	2.93e-217	23	685	25	674
QCQ78383.1|GH47	7.35e-133	30	510	46	483
QCE07576.1|GH47	1.18e-132	30	510	35	472
BAT94804.1|GH47	2.52e-131	25	510	30	472

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KKB_A	9.25e-49	33	452	25	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	1.11e-48	33	452	23	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]
1FMI_A	3.28e-47	28	462	5	446	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	3.42e-47	28	462	5	446	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]
5KIJ_A	5.46e-47	36	462	11	441	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q9FG93|MNS4_ARATH	4.17e-129	25	510	35	477	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q9BZQ6|EDEM3_HUMAN	4.47e-122	25	715	47	804	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Homo sapiens OX=9606 GN=EDEM3 PE=1 SV=2
sp|Q2HXL6|EDEM3_MOUSE	6.46e-121	25	715	48	805	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Mus musculus OX=10090 GN=Edem3 PE=1 SV=2
sp|Q9BV94|EDEM2_HUMAN	5.86e-118	29	502	34	478	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Homo sapiens OX=9606 GN=EDEM2 PE=1 SV=2
sp|Q8BJT9|EDEM2_MOUSE	2.23e-117	29	502	34	478	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Mus musculus OX=10090 GN=Edem2 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000212	0.999745	CS pos: 19-20. Pr: 0.9794

TMHMM  Annotations     

There is no transmembrane helices in ALNC14_092670:RNA-p1.