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Conserved domains on  [gi|442614829|ref|NP_001259152|]
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ER degradation enhancer, mannosidase alpha-like 1, isoform E [Drosophila melanogaster]

Protein Classification

glycoside hydrolase family 47 protein( domain architecture ID 10479221)

glycoside hydrolase family 47 protein such as ER class I alpha1,2-mannosidase, which is a critical enzyme in the maturation of N-linked oligosaccharides and ER-associated degradation

CATH:  1.50.10.10
CAZY:  GH47
EC:  3.2.1.-
SCOP:  3000996

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
48-486 2.98e-144

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).


:

Pssm-ID: 460241  Cd Length: 453  Bit Score: 438.14  E-value: 2.98e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829    48 MFQHAYDGYLRHASNYDELRPLTCDGHDTWGSYSLTLIDALDTLATMGNFTEFRRAARLLEEKMDFDRD-INVSVFETNI 126
Cdd:pfam01532    1 AFLHAWDGYKKYAWGHDELRPISGGGNDTFGGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDsTEVSVFETTI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   127 RIVGGLLSAHLLSkragvelepgWPCKGPLLRLAEDVARRLLPAFVTNTGMPYGTVNL--RYGVPKGETSI-TCTAGVGT 203
Cdd:pfam01532   81 RYLGGLLSAYDLS----------GDGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLktGKGGNGHVAGGaSSLAEAGT 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   204 FLIEFGTLSRLTGKTIYEDVAMKAVHALWA---YRSPIGLFGNHIDVQSGRWTALDSGIGAGVDSLFEYLVKASVLLNR- 279
Cdd:pfam01532  151 LQLEFTRLSQLTGDPKYEDLAQKIMDVLWKnqsRTPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGt 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   280 -PELLELFHEARAAIDKYM----RKEDWYVWVGMNK--GRVTL-PVFQSLEAFWPGIL--------SIIGDTEPALRTIS 343
Cdd:pfam01532  231 dPEYRDMYEEAMDAIKKHLlfrpSTPSDLLFIGELDsgGGGKLsPKMDHLSCFAGGMLalgatlglPREGDLELAEKLTE 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   344 RYIGVWKKY--GFLPEFYNIAAGEA-------------SPNREVYPLRPELIESAMYLYRATGNEYLLEFGEHMLETLEF 408
Cdd:pfam01532  311 GCYKTYDSTptGLGPEIFYFDPCDEdcpwdedkwdfyvKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEK 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   409 SAKTKCGYATIRNV--VTHEKENRMESFFLAETSKYLYLLFDEENFLHNDgsggellsteddvcvvqagAYIFNTEAHPM 486
Cdd:pfam01532  391 YTRTECGYSGLQDVtsPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLD-------------------EWVFNTEAHPL 451
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
48-486 2.98e-144

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).


Pssm-ID: 460241  Cd Length: 453  Bit Score: 438.14  E-value: 2.98e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829    48 MFQHAYDGYLRHASNYDELRPLTCDGHDTWGSYSLTLIDALDTLATMGNFTEFRRAARLLEEKMDFDRD-INVSVFETNI 126
Cdd:pfam01532    1 AFLHAWDGYKKYAWGHDELRPISGGGNDTFGGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDsTEVSVFETTI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   127 RIVGGLLSAHLLSkragvelepgWPCKGPLLRLAEDVARRLLPAFVTNTGMPYGTVNL--RYGVPKGETSI-TCTAGVGT 203
Cdd:pfam01532   81 RYLGGLLSAYDLS----------GDGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLktGKGGNGHVAGGaSSLAEAGT 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   204 FLIEFGTLSRLTGKTIYEDVAMKAVHALWA---YRSPIGLFGNHIDVQSGRWTALDSGIGAGVDSLFEYLVKASVLLNR- 279
Cdd:pfam01532  151 LQLEFTRLSQLTGDPKYEDLAQKIMDVLWKnqsRTPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGt 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   280 -PELLELFHEARAAIDKYM----RKEDWYVWVGMNK--GRVTL-PVFQSLEAFWPGIL--------SIIGDTEPALRTIS 343
Cdd:pfam01532  231 dPEYRDMYEEAMDAIKKHLlfrpSTPSDLLFIGELDsgGGGKLsPKMDHLSCFAGGMLalgatlglPREGDLELAEKLTE 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   344 RYIGVWKKY--GFLPEFYNIAAGEA-------------SPNREVYPLRPELIESAMYLYRATGNEYLLEFGEHMLETLEF 408
Cdd:pfam01532  311 GCYKTYDSTptGLGPEIFYFDPCDEdcpwdedkwdfyvKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEK 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   409 SAKTKCGYATIRNV--VTHEKENRMESFFLAETSKYLYLLFDEENFLHNDgsggellsteddvcvvqagAYIFNTEAHPM 486
Cdd:pfam01532  391 YTRTECGYSGLQDVtsPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLD-------------------EWVFNTEAHPL 451
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
31-486 4.26e-85

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 284.31  E-value: 4.26e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   31 KQYSKARKL--ELREDVRRMFQHAYDGYLRHASNYDELRPLTCDGHDtWGSYSLTLIDALDTLATMGNFTEFRRAARLLE 108
Cdd:PTZ00470   60 EVYYQNEKLniKRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHHE-WFGLGLTIIDSLDTLKIMGLKKEYKEGRDWVA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  109 EKMDFDRDIN--VSVFETNIRIVGGLLSAHLLSKRagvELepgwpckgpLLRLAEDVARRLLPAFVTNTGMPYGTVNLRY 186
Cdd:PTZ00470  139 NNLKQSKDTGlgVSVFETTIRVLGGLLSAYDLTGD---EM---------YLEKAREIADRLLPAFNEDTGFPASEINLAT 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  187 GVPK-----GETSITCTagVGTFLIEFGTLSRLTGKTIYEDVAMKAVHALWAYRSPI-GLFGNHIDVQSGRWTALDSGIG 260
Cdd:PTZ00470  207 GRKSypgwaGGCSILSE--VGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAInGLYPIFLNPDAGRFCGNHISLG 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  261 AGVDSLFEYLVKASVLLNRPE--LLELFHEARAAIDKYM--RKEDWYVWVGMNKGRVTLPVFQSLEAFWPGILSIIGDTE 336
Cdd:PTZ00470  285 ALGDSYYEYLLKQWLYTNGREerYRRLFVESAKGIIEHLykRSPKGLTYIAEMDGGSLTNKMEHLACFAGGMFALGAAIN 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  337 PALRTIS--RYIGVWKKY-------------GFLPEFYNIA--AGEASPN--REVYPLRPELIESAMYLYRATGNEYLLE 397
Cdd:PTZ00470  365 ITPDDEKsaRYMEVGEEVtktcyetyatsptGLGPEIFHFDpnSGDISPNvhDSHYILRPETVESIFILYRLTGDPKYRE 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  398 FGEHMLETLEFSAKTKCGYATIRNVVTHEK--ENRMESFFLAETSKYLYLLFDEENFLHNDgsggellsteddvcvvqag 475
Cdd:PTZ00470  445 WAWKIFQAIEKHCKTENGYSGLKNVLTVHPqqDDFQESFFLAETLKYLYLLFQPDHVIPLD------------------- 505
                         490
                  ....*....|.
gi 442614829  476 AYIFNTEAHPM 486
Cdd:PTZ00470  506 KYVFNTEAHPI 516
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
199-289 4.51e-03

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.


Pssm-ID: 271200 [Multi-domain]  Cd Length: 836  Bit Score: 41.14  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  199 AGVGTFLIEfgtLSRLTGKTIYEDVAMKAVHALwayrspiglfGNHIDVQSGRWTALDSGIGAGVDSLFEYLVKASVLLN 278
Cdd:cd04792   497 SGIALFLAA---LAALTGDEKYRDLARKALRPL----------RKLLRDLAADPRSLGIGGFTGLGSILYALSHLARLLG 563
                          90
                  ....*....|.
gi 442614829  279 RPELLELFHEA 289
Cdd:cd04792   564 DPELLEDALEL 574
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
48-486 2.98e-144

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).


Pssm-ID: 460241  Cd Length: 453  Bit Score: 438.14  E-value: 2.98e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829    48 MFQHAYDGYLRHASNYDELRPLTCDGHDTWGSYSLTLIDALDTLATMGNFTEFRRAARLLEEKMDFDRD-INVSVFETNI 126
Cdd:pfam01532    1 AFLHAWDGYKKYAWGHDELRPISGGGNDTFGGWGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDsTEVSVFETTI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   127 RIVGGLLSAHLLSkragvelepgWPCKGPLLRLAEDVARRLLPAFVTNTGMPYGTVNL--RYGVPKGETSI-TCTAGVGT 203
Cdd:pfam01532   81 RYLGGLLSAYDLS----------GDGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLktGKGGNGHVAGGaSSLAEAGT 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   204 FLIEFGTLSRLTGKTIYEDVAMKAVHALWA---YRSPIGLFGNHIDVQSGRWTALDSGIGAGVDSLFEYLVKASVLLNR- 279
Cdd:pfam01532  151 LQLEFTRLSQLTGDPKYEDLAQKIMDVLWKnqsRTPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGt 230
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   280 -PELLELFHEARAAIDKYM----RKEDWYVWVGMNK--GRVTL-PVFQSLEAFWPGIL--------SIIGDTEPALRTIS 343
Cdd:pfam01532  231 dPEYRDMYEEAMDAIKKHLlfrpSTPSDLLFIGELDsgGGGKLsPKMDHLSCFAGGMLalgatlglPREGDLELAEKLTE 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   344 RYIGVWKKY--GFLPEFYNIAAGEA-------------SPNREVYPLRPELIESAMYLYRATGNEYLLEFGEHMLETLEF 408
Cdd:pfam01532  311 GCYKTYDSTptGLGPEIFYFDPCDEdcpwdedkwdfyvKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEK 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   409 SAKTKCGYATIRNV--VTHEKENRMESFFLAETSKYLYLLFDEENFLHNDgsggellsteddvcvvqagAYIFNTEAHPM 486
Cdd:pfam01532  391 YTRTECGYSGLQDVtsPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLD-------------------EWVFNTEAHPL 451
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
31-486 4.26e-85

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 284.31  E-value: 4.26e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829   31 KQYSKARKL--ELREDVRRMFQHAYDGYLRHASNYDELRPLTCDGHDtWGSYSLTLIDALDTLATMGNFTEFRRAARLLE 108
Cdd:PTZ00470   60 EVYYQNEKLniKRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHHE-WFGLGLTIIDSLDTLKIMGLKKEYKEGRDWVA 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  109 EKMDFDRDIN--VSVFETNIRIVGGLLSAHLLSKRagvELepgwpckgpLLRLAEDVARRLLPAFVTNTGMPYGTVNLRY 186
Cdd:PTZ00470  139 NNLKQSKDTGlgVSVFETTIRVLGGLLSAYDLTGD---EM---------YLEKAREIADRLLPAFNEDTGFPASEINLAT 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  187 GVPK-----GETSITCTagVGTFLIEFGTLSRLTGKTIYEDVAMKAVHALWAYRSPI-GLFGNHIDVQSGRWTALDSGIG 260
Cdd:PTZ00470  207 GRKSypgwaGGCSILSE--VGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAInGLYPIFLNPDAGRFCGNHISLG 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  261 AGVDSLFEYLVKASVLLNRPE--LLELFHEARAAIDKYM--RKEDWYVWVGMNKGRVTLPVFQSLEAFWPGILSIIGDTE 336
Cdd:PTZ00470  285 ALGDSYYEYLLKQWLYTNGREerYRRLFVESAKGIIEHLykRSPKGLTYIAEMDGGSLTNKMEHLACFAGGMFALGAAIN 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  337 PALRTIS--RYIGVWKKY-------------GFLPEFYNIA--AGEASPN--REVYPLRPELIESAMYLYRATGNEYLLE 397
Cdd:PTZ00470  365 ITPDDEKsaRYMEVGEEVtktcyetyatsptGLGPEIFHFDpnSGDISPNvhDSHYILRPETVESIFILYRLTGDPKYRE 444
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  398 FGEHMLETLEFSAKTKCGYATIRNVVTHEK--ENRMESFFLAETSKYLYLLFDEENFLHNDgsggellsteddvcvvqag 475
Cdd:PTZ00470  445 WAWKIFQAIEKHCKTENGYSGLKNVLTVHPqqDDFQESFFLAETLKYLYLLFQPDHVIPLD------------------- 505
                         490
                  ....*....|.
gi 442614829  476 AYIFNTEAHPM 486
Cdd:PTZ00470  506 KYVFNTEAHPI 516
LanM-like cd04792
Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; ...
199-289 4.51e-03

Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins; LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.


Pssm-ID: 271200 [Multi-domain]  Cd Length: 836  Bit Score: 41.14  E-value: 4.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442614829  199 AGVGTFLIEfgtLSRLTGKTIYEDVAMKAVHALwayrspiglfGNHIDVQSGRWTALDSGIGAGVDSLFEYLVKASVLLN 278
Cdd:cd04792   497 SGIALFLAA---LAALTGDEKYRDLARKALRPL----------RKLLRDLAADPRSLGIGGFTGLGSILYALSHLARLLG 563
                          90
                  ....*....|.
gi 442614829  279 RPELLELFHEA 289
Cdd:cd04792   564 DPELLEDALEL 574
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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