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Conserved domains on  [gi|2024489651|ref|XP_040523407|]
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mannosyl-oligosaccharide 1,2-alpha-mannosidase IA isoform X4 [Gallus gallus]

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 ...
1-439 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: 635.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651   1 MMKYAWDNYKRYAWGLNELKPISKQGHSSnlFGNIqGATIVDALDTLFIMEMKEEFKEAKEWVEKNLDFNVNA-EISVFE 79
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGGW-GATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651  80 VNIRFVGGLLSAYYLS--GEEIFRKKAVELGEKLLPAFNTPTGIPWALLNIKSGIGRNWPWAsGGSSILAEFGTLHLEFV 157
Cdd:pfam01532  78 TTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHVA-GGASSLAEAGTLQLEFT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 158 HLSHLSGNPVFAEKVMNIRKVLSRLD---KPEGLYPNYLNPSSGQWGQHHVSIGGLGDSFYEYLLKAWLMSDKTDEEGKK 234
Cdd:pfam01532 157 RLSQLTGDPKYEDLAQKIMDVLWKNQsrtPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGTDPEYRD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 235 MYYDAVQAIETHLIRKSS--GGLTYIAEWK---GGLLEHKMGHLTCFAGGMFALGADGAPSDKtgHHIELGAEIARTCHE 309
Cdd:pfam01532 237 MYEEAMDAIKKHLLFRPStpSDLLFIGELDsggGGKLSPKMDHLSCFAGGMLALGATLGLPRE--GDLELAEKLTEGCYK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 310 SYDRTSMKLGPEAFRFDGGVE---------AIATRQNEKYYILRPEVIETYMYMWRLTHDPKYRQWAWEAVEALEKHCRV 380
Cdd:pfam01532 315 TYDSTPTGLGPEIFYFDPCDEdcpwdedkwDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTRT 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024489651 381 DGGYSGIRDVYSNHESHDDVQQSFFLSETLKYLYLLFSDDDLLPFEHWVFNTEAHPFPI 439
Cdd:pfam01532 395 ECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEWVFNTEAHPLPV 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 ...
1-439 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: 635.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651   1 MMKYAWDNYKRYAWGLNELKPISKQGHSSnlFGNIqGATIVDALDTLFIMEMKEEFKEAKEWVEKNLDFNVNA-EISVFE 79
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGGW-GATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651  80 VNIRFVGGLLSAYYLS--GEEIFRKKAVELGEKLLPAFNTPTGIPWALLNIKSGIGRNWPWAsGGSSILAEFGTLHLEFV 157
Cdd:pfam01532  78 TTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHVA-GGASSLAEAGTLQLEFT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 158 HLSHLSGNPVFAEKVMNIRKVLSRLD---KPEGLYPNYLNPSSGQWGQHHVSIGGLGDSFYEYLLKAWLMSDKTDEEGKK 234
Cdd:pfam01532 157 RLSQLTGDPKYEDLAQKIMDVLWKNQsrtPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGTDPEYRD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 235 MYYDAVQAIETHLIRKSS--GGLTYIAEWK---GGLLEHKMGHLTCFAGGMFALGADGAPSDKtgHHIELGAEIARTCHE 309
Cdd:pfam01532 237 MYEEAMDAIKKHLLFRPStpSDLLFIGELDsggGGKLSPKMDHLSCFAGGMLALGATLGLPRE--GDLELAEKLTEGCYK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 310 SYDRTSMKLGPEAFRFDGGVE---------AIATRQNEKYYILRPEVIETYMYMWRLTHDPKYRQWAWEAVEALEKHCRV 380
Cdd:pfam01532 315 TYDSTPTGLGPEIFYFDPCDEdcpwdedkwDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTRT 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024489651 381 DGGYSGIRDVYSNHESHDDVQQSFFLSETLKYLYLLFSDDDLLPFEHWVFNTEAHPFPI 439
Cdd:pfam01532 395 ECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEWVFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
1-439 0e+00

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 590.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651   1 MMKYAWDNYKRYAWGLNELKPISKQGHssNLFGniQGATIVDALDTLFIMEMKEEFKEAKEWVEKNL--DFNVNAEISVF 78
Cdd:PTZ00470   79 AMKHAWEGYKEYAWGHDELRPLTKRHH--EWFG--LGLTIIDSLDTLKIMGLKKEYKEGRDWVANNLkqSKDTGLGVSVF 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651  79 EVNIRFVGGLLSAYYLSGEEIFRKKAVELGEKLLPAFNTPTGIPWALLNIKSGIGRNWPWAsGGSSILAEFGTLHLEFVH 158
Cdd:PTZ00470  155 ETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLATGRKSYPGWA-GGCSILSEVGTLQLEFNY 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 159 LSHLSGNPVFAEKVMNIRKVLSRLDKP-EGLYPNYLNPSSGQWGQHHVSIGGLGDSFYEYLLKAWLMSDKTDEEGKKMYY 237
Cdd:PTZ00470  234 LSEITGDPKYAEYVDKVMDALFSMKPAiNGLYPIFLNPDAGRFCGNHISLGALGDSYYEYLLKQWLYTNGREERYRRLFV 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 238 DAVQAIETHLIRKSSGGLTYIAEWKGGLLEHKMGHLTCFAGGMFALGADG--APSD-KTGHHIELGAEIARTCHESYDRT 314
Cdd:PTZ00470  314 ESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLACFAGGMFALGAAIniTPDDeKSARYMEVGEEVTKTCYETYATS 393
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 315 SMKLGPEAFRFDGGVEAIATRQNEKYYILRPEVIETYMYMWRLTHDPKYRQWAWEAVEALEKHCRVDGGYSGIRDVYSNH 394
Cdd:PTZ00470  394 PTGLGPEIFHFDPNSGDISPNVHDSHYILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYSGLKNVLTVH 473
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2024489651 395 ESHDDVQQSFFLSETLKYLYLLFSDDDLLPFEHWVFNTEAHPFPI 439
Cdd:PTZ00470  474 PQQDDFQESFFLAETLKYLYLLFQPDHVIPLDKYVFNTEAHPIPI 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 ...
1-439 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: 635.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651   1 MMKYAWDNYKRYAWGLNELKPISKQGHSSnlFGNIqGATIVDALDTLFIMEMKEEFKEAKEWVEKNLDFNVNA-EISVFE 79
Cdd:pfam01532   1 AFLHAWDGYKKYAWGHDELRPISGGGNDT--FGGW-GATIVDSLDTLIIMGLTDEFEEAVDWVEKTLDFDKDStEVSVFE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651  80 VNIRFVGGLLSAYYLS--GEEIFRKKAVELGEKLLPAFNTPTGIPWALLNIKSGIGRNWPWAsGGSSILAEFGTLHLEFV 157
Cdd:pfam01532  78 TTIRYLGGLLSAYDLSgdGDDVLLEKAVDLADRLLPAFDTPTGIPYPRVNLKTGKGGNGHVA-GGASSLAEAGTLQLEFT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 158 HLSHLSGNPVFAEKVMNIRKVLSRLD---KPEGLYPNYLNPSSGQWGQHHVSIGGLGDSFYEYLLKAWLMSDKTDEEGKK 234
Cdd:pfam01532 157 RLSQLTGDPKYEDLAQKIMDVLWKNQsrtPLPGLVPIYIDPDTGKFVGSNIGLGARGDSYYEYLLKQYLLTGGTDPEYRD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 235 MYYDAVQAIETHLIRKSS--GGLTYIAEWK---GGLLEHKMGHLTCFAGGMFALGADGAPSDKtgHHIELGAEIARTCHE 309
Cdd:pfam01532 237 MYEEAMDAIKKHLLFRPStpSDLLFIGELDsggGGKLSPKMDHLSCFAGGMLALGATLGLPRE--GDLELAEKLTEGCYK 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 310 SYDRTSMKLGPEAFRFDGGVE---------AIATRQNEKYYILRPEVIETYMYMWRLTHDPKYRQWAWEAVEALEKHCRV 380
Cdd:pfam01532 315 TYDSTPTGLGPEIFYFDPCDEdcpwdedkwDFYVKIEDPHYLLRPETIESLFYLYRATGDPKYREWGWEIFQAIEKYTRT 394
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024489651 381 DGGYSGIRDVYSNHESHDDVQQSFFLSETLKYLYLLFSDDDLLPFEHWVFNTEAHPFPI 439
Cdd:pfam01532 395 ECGYSGLQDVTSPPGEKEDNMESFWLAETLKYLYLLFSDDDLLSLDEWVFNTEAHPLPV 453
PTZ00470 PTZ00470
glycoside hydrolase family 47 protein; Provisional
1-439 0e+00

glycoside hydrolase family 47 protein; Provisional


Pssm-ID: 240427  Cd Length: 522  Bit Score: 590.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651   1 MMKYAWDNYKRYAWGLNELKPISKQGHssNLFGniQGATIVDALDTLFIMEMKEEFKEAKEWVEKNL--DFNVNAEISVF 78
Cdd:PTZ00470   79 AMKHAWEGYKEYAWGHDELRPLTKRHH--EWFG--LGLTIIDSLDTLKIMGLKKEYKEGRDWVANNLkqSKDTGLGVSVF 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651  79 EVNIRFVGGLLSAYYLSGEEIFRKKAVELGEKLLPAFNTPTGIPWALLNIKSGIGRNWPWAsGGSSILAEFGTLHLEFVH 158
Cdd:PTZ00470  155 ETTIRVLGGLLSAYDLTGDEMYLEKAREIADRLLPAFNEDTGFPASEINLATGRKSYPGWA-GGCSILSEVGTLQLEFNY 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 159 LSHLSGNPVFAEKVMNIRKVLSRLDKP-EGLYPNYLNPSSGQWGQHHVSIGGLGDSFYEYLLKAWLMSDKTDEEGKKMYY 237
Cdd:PTZ00470  234 LSEITGDPKYAEYVDKVMDALFSMKPAiNGLYPIFLNPDAGRFCGNHISLGALGDSYYEYLLKQWLYTNGREERYRRLFV 313
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 238 DAVQAIETHLIRKSSGGLTYIAEWKGGLLEHKMGHLTCFAGGMFALGADG--APSD-KTGHHIELGAEIARTCHESYDRT 314
Cdd:PTZ00470  314 ESAKGIIEHLYKRSPKGLTYIAEMDGGSLTNKMEHLACFAGGMFALGAAIniTPDDeKSARYMEVGEEVTKTCYETYATS 393
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024489651 315 SMKLGPEAFRFDGGVEAIATRQNEKYYILRPEVIETYMYMWRLTHDPKYRQWAWEAVEALEKHCRVDGGYSGIRDVYSNH 394
Cdd:PTZ00470  394 PTGLGPEIFHFDPNSGDISPNVHDSHYILRPETVESIFILYRLTGDPKYREWAWKIFQAIEKHCKTENGYSGLKNVLTVH 473
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2024489651 395 ESHDDVQQSFFLSETLKYLYLLFSDDDLLPFEHWVFNTEAHPFPI 439
Cdd:PTZ00470  474 PQQDDFQESFFLAETLKYLYLLFQPDHVIPLDKYVFNTEAHPIPI 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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