CAZyme Information: EPE03349.1

Basic Information

• Species: Ophiostoma piceae
• Lineage: Ascomycota; Sordariomycetes; ; Ophiostomataceae; Ophiostoma; Ophiostoma piceae
• CAZyme ID: EPE03349.1
• CAZy Family: AA7
• CAZyme Description: alpha-1,2-Mannosidase [Source:UniProtKB/TrEMBL;Acc:S3BPU7]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1073		116941.63	4.5734

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_OpiceaeUAMH11346	8884	1262450	0	8884

• Gene Location: location=KE148168:97557-100778(+)

Full Sequence      

MALLRFRRYRVFVFGAAAFLFLLYQLSQSSQLNDSTQKIIYKGYSPPAEPGSVGNSGGAS
DGKSEGGSLGDGIASTSPKDVVQDAENAAPQEPVRAPELPSSLSVKGASSLPTENSAPEP
STPQQTDASVPVSAPAPVDENGIADTERVHRVNPPAAFQETVLPQQPATAAPNRPVPTTS
IIHWKKMPEHFPIPEESLIPLPTGSPKVIPRIQHRFEDETIAQREVRESRLDAVRREMQH
AWSGYRQFAWTHDELGPVSQTFRDPFCGWAASMVDALDTLWIMGMFEEFDEAYAAVKEID
FTTTPYRSEIPVFETIIRYLGGLIAAYDVSGGASGNYPALLTKATELAEILMGVFDTPNR
MPILYYNWKPAFSSQPAAASSSSSIAEIGSMTMEFTRLAQLTGNNKYYDAIARIVDAIEE
WQSRPGGTALPGIFPEQVDASGCNRTAAALQKARLANEKLASDLAKAQIEAAADSDAKTE
PVGYQPSQADPDPMDAADQVKAKATDESEPGLEFRVSPASSPEEGEFVNVYHKRDVGDVS
ESQAAPAAQAEAVAAAPVAAPATPPVVPVAKPPVAASHAPIKADGTNADFQCIPMNLTAG
GYGRDSFSMGGSQDSTYEYFPKQFLLLGGLVEKYQTMHEKVADAVLKYLLYRPMIEDSGR
EILFSAKVMAKDGNDENLSYHYELTHLTCFLGGMFAMGGRIFDRPDDVHIGSMLADGCAW
AYEVMPTGIMPEGATMLPCEDSTDCAWNQTVWHGMLDSNRAYRDEQMLQYDKKMQQWEVD
KNEVRRKQEERVARKQREKAAADAARKEAEANPVAGSSAPSTDNVAKRDIGNTGALAPPP
PAAAKVDAQEAATDAAEKTADNDDDDDDVAKAAAAKKLEQAAEETSSTRVIAPGSGFRNR
NKGGSAKPASQTQLDGDGDDDDDKALVTPPMPRKPESHEEYVKSRIERDNLQPGFMTIND
RRYILRPEAIESVWYMYRITGDPSWQAKGWRMFEAVIRATRTDAGHSAIGDVTRRPQTPS
EGADSTPAKMDNMESFWLAETLKYFYLLFTPPDVISLDEYVLNTEAHPFKRPV

Enzyme Prediction     

EC	3.2.1.113:7

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH47	238	1071	2.6e-171	0.9955156950672646

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396217	Glyco_hydro_47	2.37e-111	237	777	1	380	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	3.35e-63	189	1072	28	519	glycoside hydrolase family 47 protein; Provisional
396217	Glyco_hydro_47	2.37e-57	955	1071	347	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).
237057	PRK12323	0.002	54	195	367	510	DNA polymerase III subunit gamma/tau.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ERT02678.1|GH47|3.2.1.113	0.0	1	1072	1	1042
AEO67971.1|GH47	3.05e-275	94	1072	106	881
AEO60003.1|GH47	1.43e-263	94	1072	88	897
QBZ62321.1|GH47	2.76e-249	3	1072	1	1024
UQC81050.1|GH47	3.34e-247	178	1073	174	1027

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5KIJ_A	8.02e-31	240	427	15	193	Crystal structure of the class I human endoplasmic reticulum 1,2-alpha-mannosidase and Man9GlcNAc2-PA complex [Homo sapiens]
5KK7_A	8.38e-31	240	427	15	193	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	8.75e-31	240	427	20	198	Crystal Structure Of Human Class I Alpha1,2-Mannosidase [Homo sapiens]
1FO2_A	9.01e-31	240	427	20	198	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]
1KKT_A	1.30e-30	186	732	2	375	Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KKT_B Structure of P. citrinum alpha 1,2-mannosidase reveals the basis for differences in specificity of the ER and Golgi Class I enzymes [Penicillium citrinum],1KRE_A Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRE_B Structure Of P. Citrinum Alpha 1,2-Mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_A Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum],1KRF_B Structure Of P. Citrinum Alpha 1,2-mannosidase Reveals The Basis For Differences In Specificity Of The Er And Golgi Class I Enzymes [Penicillium citrinum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B2GUY0|MA1B1_RAT	1.85e-30	240	427	217	395	Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Rattus norvegicus OX=10116 GN=Man1b1 PE=2 SV=2
sp|A2AJ15|MA1B1_MOUSE	3.28e-30	240	427	218	396	Endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase OS=Mus musculus OX=10090 GN=Man1b1 PE=1 SV=1
sp|P31723|MAN12_PENCI	6.71e-30	186	732	2	375	Mannosyl-oligosaccharide alpha-1,2-mannosidase OS=Penicillium citrinum OX=5077 GN=MSDC PE=1 SV=2
sp|Q2ULB2|MNS1B_ASPOR	2.85e-29	213	732	24	375	Mannosyl-oligosaccharide alpha-1,2-mannosidase 1B OS=Aspergillus oryzae (strain ATCC 42149 / RIB 40) OX=510516 GN=mns1B PE=1 SV=1
sp|B8N417|MNS1B_ASPFN	2.85e-29	213	732	24	375	Probable mannosyl-oligosaccharide alpha-1,2-mannosidase 1B OS=Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC 167) OX=332952 GN=mns1B PE=3 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000021	0.000001

TMHMM  Annotations     

There is no transmembrane helices in EPE03349.1.