CAZyme Information: PHYCI_229961T0-p1

Basic Information

• Species: Phytophthora cinnamomi
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora cinnamomi
• CAZyme ID: PHYCI_229961T0-p1
• CAZy Family: GH123
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
710	PcinCBS144-22_SC0062|CGC2	78133.71	6.4709

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PcinnamomiCBS144-22	26201	1048749	70	26131

• Gene Location: location=PcinCBS144-22_SC0062:148732-150864(+)

Full Sequence      

MEHAFPWDELKPLSCSGRRWDRRERGDLDDVLGGFSLTLVDSLDMLAVLGDRDEFARAVR
LVASSVSFDRDVTVSVFESTIRVIGGLVSAHMLASPEYFGMMGADEYNGELLSLAEDLGR
RLLPAFDTPTGIPVHRVNLRSGVLPKDRAAKLTCPAAAGSLLVEMAYLSRLTGDHRFEER
AKEAVVAIWDRRSDIDLLGSAIDVASGEWVHSHGGIGAGLDSFFEYLLKYHLVSGDSQWL
AMFNASYQAVETHVNHDDVYIEVDMNGGKDQVRARRVSALQAFWPGLQVLAGDVSGAIRT
HEHMFPLWDEFGAMPELLDLAPRGMSKPGNRGTVISWARTSPLRPELIESTYHLYQATRD
HKYLKMGRQMLQDIRRVSEVPCGYAAVGNIHTLDIEDRMDSYFLSETAKYLYLLFSDEPD
VIVPAPIVRQRKNASSLSSPSSATDSTTKPRTLEPSLDCKNDSTNANSTYVRRNKKPLKA
SDVVFSTEGHILMVDSHLFREPQHKASLASPKCENGKLQVRKRNVELAAARDIQQTSPVI
PVGMAVRLGDVHVMTLVASPAKFGLQVTTPSAVEAPLLLFMPEIGEACGAIDTKQVRGKI
VLVARGTCTFAEKALRLQNAGAAGVVVVNSKAAYSRYPNRKYSLADDKRGLGRYVTIPVV
LVSREDATQLHRHASLKRLFSDDDGDSEGDDGVHGDSNDALIGSLSPWLY

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	1	493	3.1e-129	0.9753363228699552

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	7.93e-131	1	422	10	437	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	1.88e-70	2	424	89	503	glycoside hydrolase family 47 protein; Provisional
240122	PA_subtilisin_1	2.15e-18	560	670	2	104	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.
239041	PA_EDEM3_like	3.40e-17	558	673	2	121	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.
238300	PA	1.60e-13	585	672	30	114	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CCA23124.1|GH47	7.30e-242	1	710	46	727
AIG56058.1|GH47	9.24e-217	1	672	48	676
AGB92969.1|GH47	9.02e-125	1	662	66	738
AAM50976.1|GH47	3.39e-123	1	662	66	747
NP_609611.1|GH47	3.39e-123	1	662	66	747

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	2.99e-56	5	422	23	435	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A	3.21e-56	5	422	23	435	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]
1FMI_A	3.44e-56	5	422	28	440	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	3.60e-56	5	422	28	440	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	1.89e-55	5	422	106	518	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|Q925U4|EDEM1_MOUSE	4.27e-117	1	421	141	563	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|Q92611|EDEM1_HUMAN	2.69e-116	1	421	146	568	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q9FG93|MNS4_ARATH	2.98e-116	1	415	56	445	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q6GQB9|EDEM3_XENLA	3.48e-116	1	682	54	778	ER degradation-enhancing alpha-mannosidase-like protein 3 OS=Xenopus laevis OX=8355 GN=edem3 PE=2 SV=2
sp|Q2HXL6|EDEM3_MOUSE	7.21e-116	1	682	69	792	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
1.000062	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PHYCI_229961T0-p1.