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Conserved domains on  [gi|375298735|ref|NP_001243551|]
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mannosyl-oligosaccharide 1,2-alpha-mannosidase IB [Danio rerio]

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 ...
191-630 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: 639.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  191 MMKHAWDSYRQYGWGHNELKPLAKKGHSTniFGNsqMGATIVDALDTLYIMGLHDEFKDGQEWIEQNLDFSVNA-EVSVF 269
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGG--WGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  270 EVNIRFIGGLLAAYYLS--GQEVFKLKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVGRNWGWAsGGSSILAEFGTLHMEF 347
Cdd:pfam01532  77 ETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHVA-GGASSLAEAGTLQLEF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  348 VHLTYLTGNPAYYQKVMHIRKLLAKMD---RPNGLYPNYLNPRTGRWGQHHTSVGGLGDSFYEYLLKAWLMSDKTDAEAR 424
Cdd:pfam01532 156 TRLSQLTGDPKYEDLAQKIMDVLWKNQsrtPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGTDPEYR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  425 KTYDDAIEAIERHLIRK--SNGGLTFIGEWK---NGHLERKMGHLTCFAGGMFALGADGSPDDKagHYLQLGAEIAHTCH 499
Cdd:pfam01532 236 DMYEEAMDAIKKHLLFRpsTPSDLLFIGELDsggGGKLSPKMDHLSCFAGGMLALGATLGLPRE--GDLELAEKLTEGCY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  500 ESYDRTVLKLGPEAFKF---------DSGLEAVAVRQNEKYYILRPEVIETYWYMWRFTHDPKYRQWGWEAAQAIDKHCR 570
Cdd:pfam01532 314 KTYDSTPTGLGPEIFYFdpcdedcpwDEDKWDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTR 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  571 VSGGFSGVKDVYSSNPTYDDVQQSFFLAETLKYLYLLFSSDELLPLENWVFNTEAHPLPV 630
Cdd:pfam01532 394 TECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEWVFNTEAHPLPV 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 ...
191-630 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: 639.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  191 MMKHAWDSYRQYGWGHNELKPLAKKGHSTniFGNsqMGATIVDALDTLYIMGLHDEFKDGQEWIEQNLDFSVNA-EVSVF 269
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGG--WGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  270 EVNIRFIGGLLAAYYLS--GQEVFKLKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVGRNWGWAsGGSSILAEFGTLHMEF 347
Cdd:pfam01532  77 ETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHVA-GGASSLAEAGTLQLEF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  348 VHLTYLTGNPAYYQKVMHIRKLLAKMD---RPNGLYPNYLNPRTGRWGQHHTSVGGLGDSFYEYLLKAWLMSDKTDAEAR 424
Cdd:pfam01532 156 TRLSQLTGDPKYEDLAQKIMDVLWKNQsrtPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGTDPEYR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  425 KTYDDAIEAIERHLIRK--SNGGLTFIGEWK---NGHLERKMGHLTCFAGGMFALGADGSPDDKagHYLQLGAEIAHTCH 499
Cdd:pfam01532 236 DMYEEAMDAIKKHLLFRpsTPSDLLFIGELDsggGGKLSPKMDHLSCFAGGMLALGATLGLPRE--GDLELAEKLTEGCY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  500 ESYDRTVLKLGPEAFKF---------DSGLEAVAVRQNEKYYILRPEVIETYWYMWRFTHDPKYRQWGWEAAQAIDKHCR 570
Cdd:pfam01532 314 KTYDSTPTGLGPEIFYFdpcdedcpwDEDKWDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTR 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  571 VSGGFSGVKDVYSSNPTYDDVQQSFFLAETLKYLYLLFSSDELLPLENWVFNTEAHPLPV 630
Cdd:pfam01532 394 TECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEWVFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
182-630 0e+00

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 596.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 182 KEKRDKIREMMKHAWDSYRQYGWGHNELKPLAKKGHstNIFGnsqMGATIVDALDTLYIMGLHDEFKDGQEWIEQNLDFS 261
Cdd:PTZ00470  70 IKRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHH--EWFG---LGLTIIDSLDTLKIMGLKKEYKEGRDWVANNLKQS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 262 --VNAEVSVFEVNIRFIGGLLAAYYLSGQEVFKLKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVGRNWGWAsGGSSILAE 339
Cdd:PTZ00470 145 kdTGLGVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLATGRKSYPGWA-GGCSILSE 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 340 FGTLHMEFVHLTYLTGNPAYYQKVMHIRKLLAKMDRP-NGLYPNYLNPRTGRWGQHHTSVGGLGDSFYEYLLKAWLMSDK 418
Cdd:PTZ00470 224 VGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAiNGLYPIFLNPDAGRFCGNHISLGALGDSYYEYLLKQWLYTNG 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 419 TDAEARKTYDDAIEAIERHLIRKSNGGLTFIGEWKNGHLERKMGHLTCFAGGMFALGADGS--PDD-KAGHYLQLGAEIA 495
Cdd:PTZ00470 304 REERYRRLFVESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLACFAGGMFALGAAINitPDDeKSARYMEVGEEVT 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 496 HTCHESYDRTVLKLGPEAFKFDSGLEAVAVRQNEKYYILRPEVIETYWYMWRFTHDPKYRQWGWEAAQAIDKHCRVSGGF 575
Cdd:PTZ00470 384 KTCYETYATSPTGLGPEIFHFDPNSGDISPNVHDSHYILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGY 463
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 375298735 576 SGVKDVYSSNPTYDDVQQSFFLAETLKYLYLLFSSDELLPLENWVFNTEAHPLPV 630
Cdd:PTZ00470 464 SGLKNVLTVHPQQDDFQESFFLAETLKYLYLLFQPDHVIPLDKYVFNTEAHPIPI 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 ...
191-630 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: 639.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  191 MMKHAWDSYRQYGWGHNELKPLAKKGHSTniFGNsqMGATIVDALDTLYIMGLHDEFKDGQEWIEQNLDFSVNA-EVSVF 269
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGG--WGATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  270 EVNIRFIGGLLAAYYLS--GQEVFKLKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVGRNWGWAsGGSSILAEFGTLHMEF 347
Cdd:pfam01532  77 ETTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHVA-GGASSLAEAGTLQLEF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  348 VHLTYLTGNPAYYQKVMHIRKLLAKMD---RPNGLYPNYLNPRTGRWGQHHTSVGGLGDSFYEYLLKAWLMSDKTDAEAR 424
Cdd:pfam01532 156 TRLSQLTGDPKYEDLAQKIMDVLWKNQsrtPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGTDPEYR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  425 KTYDDAIEAIERHLIRK--SNGGLTFIGEWK---NGHLERKMGHLTCFAGGMFALGADGSPDDKagHYLQLGAEIAHTCH 499
Cdd:pfam01532 236 DMYEEAMDAIKKHLLFRpsTPSDLLFIGELDsggGGKLSPKMDHLSCFAGGMLALGATLGLPRE--GDLELAEKLTEGCY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  500 ESYDRTVLKLGPEAFKF---------DSGLEAVAVRQNEKYYILRPEVIETYWYMWRFTHDPKYRQWGWEAAQAIDKHCR 570
Cdd:pfam01532 314 KTYDSTPTGLGPEIFYFdpcdedcpwDEDKWDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTR 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735  571 VSGGFSGVKDVYSSNPTYDDVQQSFFLAETLKYLYLLFSSDELLPLENWVFNTEAHPLPV 630
Cdd:pfam01532 394 TECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEWVFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
182-630 0e+00

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 596.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 182 KEKRDKIREMMKHAWDSYRQYGWGHNELKPLAKKGHstNIFGnsqMGATIVDALDTLYIMGLHDEFKDGQEWIEQNLDFS 261
Cdd:PTZ00470  70 IKRRESVREAMKHAWEGYKEYAWGHDELRPLTKRHH--EWFG---LGLTIIDSLDTLKIMGLKKEYKEGRDWVANNLKQS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 262 --VNAEVSVFEVNIRFIGGLLAAYYLSGQEVFKLKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVGRNWGWAsGGSSILAE 339
Cdd:PTZ00470 145 kdTGLGVSVFETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLATGRKSYPGWA-GGCSILSE 223
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 340 FGTLHMEFVHLTYLTGNPAYYQKVMHIRKLLAKMDRP-NGLYPNYLNPRTGRWGQHHTSVGGLGDSFYEYLLKAWLMSDK 418
Cdd:PTZ00470 224 VGTLQLEFNYLSEITGDPKYAEYVDKVMDALFSMKPAiNGLYPIFLNPDAGRFCGNHISLGALGDSYYEYLLKQWLYTNG 303
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 419 TDAEARKTYDDAIEAIERHLIRKSNGGLTFIGEWKNGHLERKMGHLTCFAGGMFALGADGS--PDD-KAGHYLQLGAEIA 495
Cdd:PTZ00470 304 REERYRRLFVESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLACFAGGMFALGAAINitPDDeKSARYMEVGEEVT 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 375298735 496 HTCHESYDRTVLKLGPEAFKFDSGLEAVAVRQNEKYYILRPEVIETYWYMWRFTHDPKYRQWGWEAAQAIDKHCRVSGGF 575
Cdd:PTZ00470 384 KTCYETYATSPTGLGPEIFHFDPNSGDISPNVHDSHYILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGY 463
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 375298735 576 SGVKDVYSSNPTYDDVQQSFFLAETLKYLYLLFSSDELLPLENWVFNTEAHPLPV 630
Cdd:PTZ00470 464 SGLKNVLTVHPQQDDFQESFFLAETLKYLYLLFQPDHVIPLDKYVFNTEAHPIPI 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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