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Conserved domains on  [gi|1720398289|ref|XP_030105470|]
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endoplasmic reticulum mannosyl-oligosaccharide 1,2-alpha-mannosidase isoform X2 [Mus musculus]

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.-
Gene Ontology:  GO:0006486
PubMed:  17116466|34777906
SCOP:  3000996

Graphical summary

 Zoom to residue level

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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 ...
1-398 0e+00

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: 563.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289   1 MWILGLKQEFKQARKWVSENLDF-QKNVDVNLFESTIRILGGLLSTYHLS--GDSLFLTKAEDFGKRLMPAFTTPSKIPY 77
Cdd:pfam01532  44 LIIMGLTDEFEEAVDWVEKTLDFdKDSTEVSVFETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289  78 SDVNIGTGFAHSPQWTS-DSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHS--LSGKKDGLVPMFINTNSGLFT 154
Cdd:pfam01532 124 PRVNLKTGKGGNGHVAGgASSLAEAGTLQLEFTRLSQLTGDPKYEDLAQKIMDVLWKnqSRTPLPGLVPIYIDPDTGKFV 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 155 HpGVFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVKAIEGIKAHLL-RQSQPRKLTFVGEL---AHGRFSAKMDHLVC 230
Cdd:pfam01532 204 G-SNIGLGARGDSYYEYLLKQYLLTGGTDPEYRDMYEEAMDAIKKHLLfRPSTPSDLLFIGELdsgGGGKLSPKMDHLSC 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 231 FLPGTLALGVHHGLP-ADHMDLARALMETCYQMNQQMETGLSPEIAHFNM-----YPRADHKDVEVKPADRHNLLRPETV 304
Cdd:pfam01532 283 FAGGMLALGATLGLPrEGDLELAEKLTEGCYKTYDSTPTGLGPEIFYFDPcdedcPWDEDKWDFYVKIEDPHYLLRPETI 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 305 ESLFYLYRVTRDRKYQDWGWEILQSFNKYTRVPSgGYSSINNVqNSHKPEPRDKMESFFVGETLKYLYLLFSDDlELLSL 384
Cdd:pfam01532 363 ESLFYLYRATGDPKYREWGWEIFQAIEKYTRTEC-GYSGLQDV-TSPPGEKEDNMESFWLAETLKYLYLLFSDD-DLLSL 439
                         410
                  ....*....|....
gi 1720398289 385 DSCVFNTEAHPLPI 398
Cdd:pfam01532 440 DEWVFNTEAHPLPV 453
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
1-398 0e+00

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: 563.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289   1 MWILGLKQEFKQARKWVSENLDF-QKNVDVNLFESTIRILGGLLSTYHLS--GDSLFLTKAEDFGKRLMPAFTTPSKIPY 77
Cdd:pfam01532  44 LIIMGLTDEFEEAVDWVEKTLDFdKDSTEVSVFETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289  78 SDVNIGTGFAHSPQWTS-DSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHS--LSGKKDGLVPMFINTNSGLFT 154
Cdd:pfam01532 124 PRVNLKTGKGGNGHVAGgASSLAEAGTLQLEFTRLSQLTGDPKYEDLAQKIMDVLWKnqSRTPLPGLVPIYIDPDTGKFV 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 155 HpGVFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVKAIEGIKAHLL-RQSQPRKLTFVGEL---AHGRFSAKMDHLVC 230
Cdd:pfam01532 204 G-SNIGLGARGDSYYEYLLKQYLLTGGTDPEYRDMYEEAMDAIKKHLLfRPSTPSDLLFIGELdsgGGGKLSPKMDHLSC 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 231 FLPGTLALGVHHGLP-ADHMDLARALMETCYQMNQQMETGLSPEIAHFNM-----YPRADHKDVEVKPADRHNLLRPETV 304
Cdd:pfam01532 283 FAGGMLALGATLGLPrEGDLELAEKLTEGCYKTYDSTPTGLGPEIFYFDPcdedcPWDEDKWDFYVKIEDPHYLLRPETI 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 305 ESLFYLYRVTRDRKYQDWGWEILQSFNKYTRVPSgGYSSINNVqNSHKPEPRDKMESFFVGETLKYLYLLFSDDlELLSL 384
Cdd:pfam01532 363 ESLFYLYRATGDPKYREWGWEIFQAIEKYTRTEC-GYSGLQDV-TSPPGEKEDNMESFWLAETLKYLYLLFSDD-DLLSL 439
                         410
                  ....*....|....
gi 1720398289 385 DSCVFNTEAHPLPI 398
Cdd:pfam01532 440 DEWVFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
1-398 1.44e-167

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 479.60  E-value: 1.44e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289   1 MWILGLKQEFKQARKWVSENLDFQKNVD--VNLFESTIRILGGLLSTYHLSGDSLFLTKAEDFGKRLMPAFTTPSKIPYS 78
Cdd:PTZ00470  121 LKIMGLKKEYKEGRDWVANNLKQSKDTGlgVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPAS 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289  79 DVNIGTGFAHSPQWT-SDSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHSLSGKKDGLVPMFINTNSGLFtHPG 157
Cdd:PTZ00470  201 EINLATGRKSYPGWAgGCSILSEVGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAINGLYPIFLNPDAGRF-CGN 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 158 VFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVKAIEGIKAHLLRQSqPRKLTFVGELAHGRFSAKMDHLVCFLPGTLA 237
Cdd:PTZ00470  280 HISLGALGDSYYEYLLKQWLYTNGREERYRRLFVESAKGIIEHLYKRS-PKGLTYIAEMDGGSLTNKMEHLACFAGGMFA 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 238 LG------VHHGLPADHMDLARALMETCYQMNQQMETGLSPEIAHFNmyprADHKDVEVKPADRHNLLRPETVESLFYLY 311
Cdd:PTZ00470  359 LGaainitPDDEKSARYMEVGEEVTKTCYETYATSPTGLGPEIFHFD----PNSGDISPNVHDSHYILRPETVESIFILY 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 312 RVTRDRKYQDWGWEILQSFNKYTRVPSgGYSSINNVQNSHkPEPRDKMESFFVGETLKYLYLLFSDDlELLSLDSCVFNT 391
Cdd:PTZ00470  435 RLTGDPKYREWAWKIFQAIEKHCKTEN-GYSGLKNVLTVH-PQQDDFQESFFLAETLKYLYLLFQPD-HVIPLDKYVFNT 511

                  ....*..
gi 1720398289 392 EAHPLPI 398
Cdd:PTZ00470  512 EAHPIPI 518
 
Name Accession Description Interval E-value
Glyco_hydro_47 pfam01532
Glycosyl hydrolase family 47; Members of this family are alpha-mannosidases that catalyze the ...
1-398 0e+00

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: 563.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289   1 MWILGLKQEFKQARKWVSENLDF-QKNVDVNLFESTIRILGGLLSTYHLS--GDSLFLTKAEDFGKRLMPAFTTPSKIPY 77
Cdd:pfam01532  44 LIIMGLTDEFEEAVDWVEKTLDFdKDSTEVSVFETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289  78 SDVNIGTGFAHSPQWTS-DSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHS--LSGKKDGLVPMFINTNSGLFT 154
Cdd:pfam01532 124 PRVNLKTGKGGNGHVAGgASSLAEAGTLQLEFTRLSQLTGDPKYEDLAQKIMDVLWKnqSRTPLPGLVPIYIDPDTGKFV 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 155 HpGVFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVKAIEGIKAHLL-RQSQPRKLTFVGEL---AHGRFSAKMDHLVC 230
Cdd:pfam01532 204 G-SNIGLGARGDSYYEYLLKQYLLTGGTDPEYRDMYEEAMDAIKKHLLfRPSTPSDLLFIGELdsgGGGKLSPKMDHLSC 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 231 FLPGTLALGVHHGLP-ADHMDLARALMETCYQMNQQMETGLSPEIAHFNM-----YPRADHKDVEVKPADRHNLLRPETV 304
Cdd:pfam01532 283 FAGGMLALGATLGLPrEGDLELAEKLTEGCYKTYDSTPTGLGPEIFYFDPcdedcPWDEDKWDFYVKIEDPHYLLRPETI 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 305 ESLFYLYRVTRDRKYQDWGWEILQSFNKYTRVPSgGYSSINNVqNSHKPEPRDKMESFFVGETLKYLYLLFSDDlELLSL 384
Cdd:pfam01532 363 ESLFYLYRATGDPKYREWGWEIFQAIEKYTRTEC-GYSGLQDV-TSPPGEKEDNMESFWLAETLKYLYLLFSDD-DLLSL 439
                         410
                  ....*....|....
gi 1720398289 385 DSCVFNTEAHPLPI 398
Cdd:pfam01532 440 DEWVFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
1-398 1.44e-167

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 479.60  E-value: 1.44e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289   1 MWILGLKQEFKQARKWVSENLDFQKNVD--VNLFESTIRILGGLLSTYHLSGDSLFLTKAEDFGKRLMPAFTTPSKIPYS 78
Cdd:PTZ00470  121 LKIMGLKKEYKEGRDWVANNLKQSKDTGlgVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPAS 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289  79 DVNIGTGFAHSPQWT-SDSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHSLSGKKDGLVPMFINTNSGLFtHPG 157
Cdd:PTZ00470  201 EINLATGRKSYPGWAgGCSILSEVGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAINGLYPIFLNPDAGRF-CGN 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 158 VFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVKAIEGIKAHLLRQSqPRKLTFVGELAHGRFSAKMDHLVCFLPGTLA 237
Cdd:PTZ00470  280 HISLGALGDSYYEYLLKQWLYTNGREERYRRLFVESAKGIIEHLYKRS-PKGLTYIAEMDGGSLTNKMEHLACFAGGMFA 358
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 238 LG------VHHGLPADHMDLARALMETCYQMNQQMETGLSPEIAHFNmyprADHKDVEVKPADRHNLLRPETVESLFYLY 311
Cdd:PTZ00470  359 LGaainitPDDEKSARYMEVGEEVTKTCYETYATSPTGLGPEIFHFD----PNSGDISPNVHDSHYILRPETVESIFILY 434
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720398289 312 RVTRDRKYQDWGWEILQSFNKYTRVPSgGYSSINNVQNSHkPEPRDKMESFFVGETLKYLYLLFSDDlELLSLDSCVFNT 391
Cdd:PTZ00470  435 RLTGDPKYREWAWKIFQAIEKHCKTEN-GYSGLKNVLTVH-PQQDDFQESFFLAETLKYLYLLFQPD-HVIPLDKYVFNT 511

                  ....*..
gi 1720398289 392 EAHPLPI 398
Cdd:PTZ00470  512 EAHPIPI 518
 
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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