CAZyme Information: TPX50818.1

Basic Information

• Species: Synchytrium endobioticum
• Lineage: Chytridiomycota; Chytridiomycetes; ; Synchytriaceae; Synchytrium; Synchytrium endobioticum
• CAZyme ID: TPX50818.1
• CAZy Family: GT2
• CAZyme Description: alpha-1,2-Mannosidase [Source:UniProtKB/TrEMBL;Acc:A0A507DIT4]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
923		102033.50	5.7792

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SendobioticumMB42	8031	N/A	0	8031

• Gene Location: location=QEAN01000062:63229-66670(-)

Full Sequence      

MRPHPHWLHIIALWRLLFASLDVCDAMTTRRRLDLRDKVQEMFYHGWDSYIKYAYPQDEL
NPLSCTARSRNDSDPDAFHVNDVLAGVSVTLLDTLDTFAVMNDRANFSRLVHLVISRGPT
QLDVPSRVQVFETTIRVLGGLLSAHLLATNSDLGFAVPAYSGELLSLAQDLGRKLLPAFD
ASPTDIPFARVNLMHGVLPWEVNDTCTAGAGTLILEFGILSRLTNDPTFEKVAKKALMAI
WDKRSELDLVGNTLSVQTGKWIHRMAGIECLETFESAYAAVMSHIRDSNGFVYKNVNMDS
GQLVTTWIDSLAAFFPGLQVLYGDVESAARLHHLYFALWRRFKSLPERFDWTTQSAVLAH
YPLRPELVESTFMLYRATKHPHYLQVGEEILQDLNSLMRVKCGFASLADVVKKTTTDRME
SFFLSETLKYLYLLFDEDNVFNHLDSNFVFSTEGHVFVLPHNYSRTPSATDKSDMSQPTQ
LNTSRPETTVCPLNKGIWGMLETYEFRNHITPDAKRLYPPIDLESTKAIHRFVGLPEDMD
PVVDTMPMCNTGALLNQQPLIILAGQTFTVAIDAPSGANVPLAHLTQFSHGFTTSSVAGL
QLNLQVDIASPDAFMITSITDPTRDVSLVVRPGHVVRVPKQGRDYAGVLAAFGRDIAAGE
WMDVVLQPLLDGHGILWDGCTPYQGVDVAGRVPLVLRGACMFAAKAKHAEAAGAVGLVVV
ARDNRPFTMSSANETWSEEEANIGIPVIMVGISFLRHLLSLPYEAVDGIICGPRLNSEIE
CGVPIDSETQLSHLYEADTQIQFNNLKVRNFEVVLVLSGRERRVLDSGRPLANSVSGILD
PGQGIGCAGGCIADTRMCCRDLVGLGLGVGGMGSSRASHVRNVVASDAPGPLISGSRLSE
SNNGQEKEQSTWWDWLELHFKYL

Enzyme Prediction     

EC	3.2.1.113:20

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	42	268	7.1e-66	0.4641255605381166
GH47	270	457	1.1e-55	0.4730941704035874

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	3.24e-132	42	457	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	1.27e-60	36	455	73	514	glycoside hydrolase family 47 protein; Provisional
240122	PA_subtilisin_1	1.78e-04	678	751	28	97	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.
240120	PA_SaNapH_like	0.008	678	728	30	82	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.
239044	PA_hSPPL_like	0.009	665	750	20	100	PA_hSPPL_like: Protease-associated domain containing human signal peptide peptidase-like (hSPPL)-like. This group contains various PA domain-containing proteins similar to hSPPL2a and 2b. These SPPLs are GxGD aspartic proteases. SPPL2a is sorted to the late endosomes, SPPL2b to the plasma membrane. In activated dendritic cells, hSPPL2a and 2b catalyze the intramembrane proteolysis of tumor necrosis factor alpha triggering IL-12 production. hSPPL2a and 2b may have a broad substrate spectrum. The significance of the PA domain to these SPPLs 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
CDS05465.1|GH47	6.03e-159	42	466	1	444
AAH64866.1|GH47	2.82e-141	32	459	67	526
AFE70442.1|GH47	2.72e-140	26	467	54	527
AAI53844.1|GH47	2.82e-140	25	535	121	657
AAI51306.1|GH47	2.82e-140	25	535	121	657

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4AYO_A	8.02e-41	39	437	17	415	Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 [Caulobacter sp. K31],4AYP_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with thiomannobioside [Caulobacter sp. K31],4AYQ_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with mannoimidazole [Caulobacter sp. K31],4AYR_A Structure of The GH47 processing alpha-1,2-mannosidase from Caulobacter strain K31 in complex with noeuromycin [Caulobacter sp. K31],5MEH_A Crystal structure of alpha-1,2-mannosidase from Caulobacter K31 strain in complex with 1-deoxymannojirimycin [Caulobacter sp. K31],5NE5_A Crystal structure of family 47 alpha-1,2-mannosidase from Caulobacter K31 strain in complex with kifunensine [Caulobacter sp. K31]
5KIJ_A	8.81e-41	33	455	2	447	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
1FMI_A	9.85e-41	33	455	7	452	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	1.02e-40	33	455	7	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]
1X9D_A	3.69e-40	33	455	85	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|Q92611|EDEM1_HUMAN	5.28e-140	26	467	121	594	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Homo sapiens OX=9606 GN=EDEM1 PE=1 SV=1
sp|Q925U4|EDEM1_MOUSE	6.94e-139	26	456	116	578	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Mus musculus OX=10090 GN=Edem1 PE=1 SV=1
sp|O94726|MNL1_SCHPO	9.05e-120	17	457	17	475	ER degradation-enhancing alpha-mannosidase-like protein 1 OS=Schizosaccharomyces pombe (strain 972 / ATCC 24843) OX=284812 GN=mnl1 PE=3 SV=2
sp|Q9FG93|MNS4_ARATH	1.15e-114	35	456	40	470	Alpha-mannosidase I MNS4 OS=Arabidopsis thaliana OX=3702 GN=MNS4 PE=1 SV=1
sp|Q9SXC9|MNS5_ARATH	3.28e-105	4	455	6	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
0.000212	0.999763	CS pos: 26-27. Pr: 0.9656

TMHMM  Annotations     

There is no transmembrane helices in TPX50818.1.