CAZyme Information: evm.model.AC2VRR_s00227g207-p1

Basic Information

• Species: Albugo candida
• Lineage: Oomycota; NA; ; Albuginaceae; Albugo; Albugo candida
• CAZyme ID: evm.model.AC2VRR_s00227g207-p1
• CAZy Family: GT41
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
629		72028.40	5.0513

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Acandida2VRR	15896	911350	72	15824

• Gene Location: location=Acan2VRR_SC227:405792-407681(-)

Full Sequence      

MGLLGKHIDNRNGDWYETLSGPGSNSDSVYEYFLKMYMNFGDVEFLHIFEELYDAIMTYN
RVGDWFFDMNMYDESQIRRSQMIFENLVAFFPGLQVAFGQLSAASNSLNAFHKVWRELGF
TPERFDVQSWDLQWNRRDYVLRPELAESTFYMHEATQDSSWLRAGAHIVESIENHCKTDC
GYASVKDVKTKSLKDEMPSFFLAETCKYLYLLFNTSSFIRNGNFVFTTEAHPFPISQVTA
GLELIQKLVKSKSGTLTDRNDDTCSEAPFWLAYSYQEDYHVITEKENTRLYDEAFYPWSS
CELHTKKKSSKVVQSHVVNGGEKLGDFYVHRVGQFTRVTQEQTQQWIDFVRYGQNQLLVA
MMPAQELITTSNSGISKAPLVPVYRTFQLHTAPSTVIKLLSFTCSVQVLLDLKSLNKEHH
DETTAFRFPCMQSKFGGYSFLPHSIAFAMAGLVIADPIDACTTLQGNHYRGKYVLANQVK
CSYEEKSANVDASGAFGLLIWIAEKLETDIDDVLVEVWTSNRPDGTKFPDNITIPIIMVS
HSLGKWLDSIKDTDIGIRLDLETFVYSNFDISQLWQMKSQDREDDLFFMISAKHYDKVWL
CGPQWSVEVKLSATSVIAILENAPSTNDQ

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	2	235	5.1e-64	0.57847533632287

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	2.98e-59	2	235	189	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	4.15e-37	2	235	263	518	glycoside hydrolase family 47 protein; Provisional
239047	PA_GO-like	5.46e-07	452	561	42	137	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.
238300	PA	1.75e-06	435	554	9	120	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.
239038	PA_C_RZF_like	2.88e-05	452	559	44	145	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA28112.1|GH47	3.55e-315	1	610	33	643
AIG56334.1|GH47	5.17e-95	1	562	382	918
UIZ27914.1|GH47	1.02e-93	1	547	281	945
AIG55397.1|GH47	2.61e-92	1	615	378	934
CAG1852391.1|GH47	1.54e-52	1	235	252	482

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KKB_A	3.01e-21	2	235	215	467	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	3.21e-21	2	235	213	465	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	8.29e-16	23	235	215	451	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	8.54e-16	23	235	220	456	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	8.62e-16	23	235	220	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|Q9FG93|MNS4_ARATH	5.08e-51	1	236	236	474	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	5.60e-50	1	235	248	478	Alpha-mannosidase I MNS5 OS=Arabidopsis thaliana OX=3702 GN=MNS5 PE=1 SV=1
sp|Q9BV94|EDEM2_HUMAN	2.28e-43	1	232	232	479	ER degradation-enhancing alpha-mannosidase-like protein 2 OS=Homo sapiens OX=9606 GN=EDEM2 PE=1 SV=2
sp|Q6GQB9|EDEM3_XENLA	4.41e-43	3	552	255	768	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q8BJT9|EDEM2_MOUSE	1.07e-42	1	232	232	479	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 OTHER

Other	SP_Sec_SPI	CS Position
1.000028	0.000001

TMHMM  Annotations     

There is no transmembrane helices in evm.model.AC2VRR_s00227g207-p1.