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Conserved domains on  [gi|1867988472|ref|NP_001372113|]
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mannosyl-oligosaccharide 1,2-alpha-mannosidase IC isoform 5 [Homo sapiens]

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.-

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 ...
213-449 1.93e-119

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: 356.87  E-value: 1.93e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 213 DHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEAIETYLLNV--SPGGLTYIAE---WRGGILDHKMGHLACFS 287
Cdd:pfam01532 205 SNIGLGARGDSYYEYLLKQYLLTGGTDPEYRDMYEEAMDAIKKHLLFRpsTPSDLLFIGEldsGGGGKLSPKMDHLSCFA 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 288 GGMIALGAedAKEEKRAHYRELAAQITKTCHESYARSDTKLGPEAFWFN---------SGREAVATQLSESYYILRPEVV 358
Cdd:pfam01532 285 GGMLALGA--TLGLPREGDLELAEKLTEGCYKTYDSTPTGLGPEIFYFDpcdedcpwdEDKWDFYVKIEDPHYLLRPETI 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 359 ESYMYLWRQTHNPIYREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDLLSLEDW 438
Cdd:pfam01532 363 ESLFYLYRATGDPKYREWGWEIFQAIEKYTRTECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEW 442
                         250
                  ....*....|.
gi 1867988472 439 VFNTEAHPLPV 449
Cdd:pfam01532 443 VFNTEAHPLPV 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 ...
213-449 1.93e-119

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: 356.87  E-value: 1.93e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 213 DHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEAIETYLLNV--SPGGLTYIAE---WRGGILDHKMGHLACFS 287
Cdd:pfam01532 205 SNIGLGARGDSYYEYLLKQYLLTGGTDPEYRDMYEEAMDAIKKHLLFRpsTPSDLLFIGEldsGGGGKLSPKMDHLSCFA 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 288 GGMIALGAedAKEEKRAHYRELAAQITKTCHESYARSDTKLGPEAFWFN---------SGREAVATQLSESYYILRPEVV 358
Cdd:pfam01532 285 GGMLALGA--TLGLPREGDLELAEKLTEGCYKTYDSTPTGLGPEIFYFDpcdedcpwdEDKWDFYVKIEDPHYLLRPETI 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 359 ESYMYLWRQTHNPIYREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDLLSLEDW 438
Cdd:pfam01532 363 ESLFYLYRATGDPKYREWGWEIFQAIEKYTRTECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEW 442
                         250
                  ....*....|.
gi 1867988472 439 VFNTEAHPLPV 449
Cdd:pfam01532 443 VFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
208-449 2.98e-112

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 340.55  E-value: 2.98e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 208 EGNMF--DHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEAIETYLLNVSPGGLTYIAEWRGGILDHKMGHLAC 285
Cdd:PTZ00470  272 DAGRFcgNHISLGALGDSYYEYLLKQWLYTNGREERYRRLFVESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLAC 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 286 FSGGMIALGAE---DAKEEKRAHYRELAAQITKTCHESYARSDTKLGPEAFWFNSGREAVATQLSESYYILRPEVVESYM 362
Cdd:PTZ00470  352 FAGGMFALGAAiniTPDDEKSARYMEVGEEVTKTCYETYATSPTGLGPEIFHFDPNSGDISPNVHDSHYILRPETVESIF 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 363 YLWRQTHNPIYREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDLLSLEDWVFNT 442
Cdd:PTZ00470  432 ILYRLTGDPKYREWAWKIFQAIEKHCKTENGYSGLKNVLTVHPQQDDFQESFFLAETLKYLYLLFQPDHVIPLDKYVFNT 511

                  ....*..
gi 1867988472 443 EAHPLPV 449
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 ...
213-449 1.93e-119

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: 356.87  E-value: 1.93e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 213 DHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEAIETYLLNV--SPGGLTYIAE---WRGGILDHKMGHLACFS 287
Cdd:pfam01532 205 SNIGLGARGDSYYEYLLKQYLLTGGTDPEYRDMYEEAMDAIKKHLLFRpsTPSDLLFIGEldsGGGGKLSPKMDHLSCFA 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 288 GGMIALGAedAKEEKRAHYRELAAQITKTCHESYARSDTKLGPEAFWFN---------SGREAVATQLSESYYILRPEVV 358
Cdd:pfam01532 285 GGMLALGA--TLGLPREGDLELAEKLTEGCYKTYDSTPTGLGPEIFYFDpcdedcpwdEDKWDFYVKIEDPHYLLRPETI 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 359 ESYMYLWRQTHNPIYREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDLLSLEDW 438
Cdd:pfam01532 363 ESLFYLYRATGDPKYREWGWEIFQAIEKYTRTECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEW 442
                         250
                  ....*....|.
gi 1867988472 439 VFNTEAHPLPV 449
Cdd:pfam01532 443 VFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
208-449 2.98e-112

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 340.55  E-value: 2.98e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 208 EGNMF--DHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEAIETYLLNVSPGGLTYIAEWRGGILDHKMGHLAC 285
Cdd:PTZ00470  272 DAGRFcgNHISLGALGDSYYEYLLKQWLYTNGREERYRRLFVESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLAC 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 286 FSGGMIALGAE---DAKEEKRAHYRELAAQITKTCHESYARSDTKLGPEAFWFNSGREAVATQLSESYYILRPEVVESYM 362
Cdd:PTZ00470  352 FAGGMFALGAAiniTPDDEKSARYMEVGEEVTKTCYETYATSPTGLGPEIFHFDPNSGDISPNVHDSHYILRPETVESIF 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1867988472 363 YLWRQTHNPIYREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDLLSLEDWVFNT 442
Cdd:PTZ00470  432 ILYRLTGDPKYREWAWKIFQAIEKHCKTENGYSGLKNVLTVHPQQDDFQESFFLAETLKYLYLLFQPDHVIPLDKYVFNT 511

                  ....*..
gi 1867988472 443 EAHPLPV 449
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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