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Conserved domains on  [gi|72534766|ref|NP_001026910|]
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glycoprotein endo-alpha-1,2-mannosidase-like protein isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH99_GH71_like super family cl01529
Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside ...
 105-249 2.03e-77

Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside hydrolases contains families GH71 and GH99 (following the CAZY nomenclature), as well as other members with undefined function and specificity.


The actual alignment was detected with superfamily member cd11574:

Pssm-ID: 470237  Cd Length: 338  Bit Score: 237.21  E-value: 2.03e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534766 105 LHAFYYSWYGSPRREGHYIHWDHVMVPHWDpkISASYPRGRHSPPDDLGSSFYPELGPYSSRDPEVLREHMTQLKEAAIG 184
Cdd:cd11574   1 VHIFYYAWYGNPEFDGKYGHWNHKILPHWD--IAKKYPQGRHDPPDDIGSNFYPKLGPYSSSDPSVIDDHMKQIREAGIG 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 72534766 185 VLVLSWYPPGMADDNGEPSDDLVPAILDTAHQYSIQVAFHIQPYKGRDDITVHDNIKYIIDTTGK 249
Cdd:cd11574  79 VVVVSWYGPGSSDDNGKPSDDTIPLLLDIAHEYGLKVAFHIEPYEGRTAASLREDIKYILDKYGS 143
 
Name Accession Description Interval E-value
GH99 cd11574
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
 105-249 2.03e-77

Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside hydrolases 99 (following the CAZY nomenclature) includes endo-alpha-1,2-mannosidase (EC 3.2.1.130), which is an important membrane-associated eukaryotic enzyme involved in the maturation of N-linked glycans. Specifically, it cleaves mannoside linkages internal to N-linked glycan chains by hydrolyzing an alpha-1,2-mannosidic bond between a glucose-substituted mannose and the remainder of the chain. The biological function and significance of the soluble bacterial orthologs, which may have obtained the genes via horizontal transfer, is not clear.


Pssm-ID: 211415  Cd Length: 338  Bit Score: 237.21  E-value: 2.03e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534766 105 LHAFYYSWYGSPRREGHYIHWDHVMVPHWDpkISASYPRGRHSPPDDLGSSFYPELGPYSSRDPEVLREHMTQLKEAAIG 184
Cdd:cd11574   1 VHIFYYAWYGNPEFDGKYGHWNHKILPHWD--IAKKYPQGRHDPPDDIGSNFYPKLGPYSSSDPSVIDDHMKQIREAGIG 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 72534766 185 VLVLSWYPPGMADDNGEPSDDLVPAILDTAHQYSIQVAFHIQPYKGRDDITVHDNIKYIIDTTGK 249
Cdd:cd11574  79 VVVVSWYGPGSSDDNGKPSDDTIPLLLDIAHEYGLKVAFHIEPYEGRTAASLREDIKYILDKYGS 143
Glyco_hydro_99 pfam16317
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
 105-248 4.24e-62

Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some uncharacterized proteins from bacteroides to human. Some proteins in this family, annotated as endo-alpha-mannosidases cleave mannoside linkages internally within an N-linked glycan chain, short circuiting the classical N-glycan biosynthetic pathway. This domain reveals a (beta-alpha)(8) barrel fold in which the catalytic centre is present in a long substrate-binding groove, consistent with cleavage within the N-glycan chain, providing a foundation upon which to develop new enzyme inhibitors targeting the hijacking of N-glycan synthesis in viral disease and cancer.


Pssm-ID: 435273  Cd Length: 341  Bit Score: 198.20  E-value: 4.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534766   105 LHAFYYSWYGSPRREGHYIHWDHVMVPHWDPKISAS-YPRGRHSPPDDLGSSFYPELGPYSSRDPEVLREHMTQLKEAAI 183
Cdd:pfam16317   6 LHVFYYSWYGNPQFDGKYQHWNHPVLEHWDPRIGKLnYPGARHGPPDDIGSNFYPELGSYSSRDPEIIETHMRMMRSASI 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 72534766   184 GVLVLSWYppgmaDDNGEPSdDLVPAILDTAHQYSIQVAFHIQPYKGRDDITVHDNIKYIIDTTG 248
Cdd:pfam16317  86 GVLSVSWY-----GENDEAT-RSVPTILDKAAKYGLKVTFHIEPYNNRSDQNMHANIKYIIDKYG 144
 
Name Accession Description Interval E-value
GH99 cd11574
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
 105-249 2.03e-77

Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside hydrolases 99 (following the CAZY nomenclature) includes endo-alpha-1,2-mannosidase (EC 3.2.1.130), which is an important membrane-associated eukaryotic enzyme involved in the maturation of N-linked glycans. Specifically, it cleaves mannoside linkages internal to N-linked glycan chains by hydrolyzing an alpha-1,2-mannosidic bond between a glucose-substituted mannose and the remainder of the chain. The biological function and significance of the soluble bacterial orthologs, which may have obtained the genes via horizontal transfer, is not clear.


Pssm-ID: 211415  Cd Length: 338  Bit Score: 237.21  E-value: 2.03e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534766 105 LHAFYYSWYGSPRREGHYIHWDHVMVPHWDpkISASYPRGRHSPPDDLGSSFYPELGPYSSRDPEVLREHMTQLKEAAIG 184
Cdd:cd11574   1 VHIFYYAWYGNPEFDGKYGHWNHKILPHWD--IAKKYPQGRHDPPDDIGSNFYPKLGPYSSSDPSVIDDHMKQIREAGIG 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 72534766 185 VLVLSWYPPGMADDNGEPSDDLVPAILDTAHQYSIQVAFHIQPYKGRDDITVHDNIKYIIDTTGK 249
Cdd:cd11574  79 VVVVSWYGPGSSDDNGKPSDDTIPLLLDIAHEYGLKVAFHIEPYEGRTAASLREDIKYILDKYGS 143
Glyco_hydro_99 pfam16317
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
 105-248 4.24e-62

Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some uncharacterized proteins from bacteroides to human. Some proteins in this family, annotated as endo-alpha-mannosidases cleave mannoside linkages internally within an N-linked glycan chain, short circuiting the classical N-glycan biosynthetic pathway. This domain reveals a (beta-alpha)(8) barrel fold in which the catalytic centre is present in a long substrate-binding groove, consistent with cleavage within the N-glycan chain, providing a foundation upon which to develop new enzyme inhibitors targeting the hijacking of N-glycan synthesis in viral disease and cancer.


Pssm-ID: 435273  Cd Length: 341  Bit Score: 198.20  E-value: 4.24e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534766   105 LHAFYYSWYGSPRREGHYIHWDHVMVPHWDPKISAS-YPRGRHSPPDDLGSSFYPELGPYSSRDPEVLREHMTQLKEAAI 183
Cdd:pfam16317   6 LHVFYYSWYGNPQFDGKYQHWNHPVLEHWDPRIGKLnYPGARHGPPDDIGSNFYPELGSYSSRDPEIIETHMRMMRSASI 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 72534766   184 GVLVLSWYppgmaDDNGEPSdDLVPAILDTAHQYSIQVAFHIQPYKGRDDITVHDNIKYIIDTTG 248
Cdd:pfam16317  86 GVLSVSWY-----GENDEAT-RSVPTILDKAAKYGLKVTFHIEPYNNRSDQNMHANIKYIIDKYG 144
GH99_GH71_like_3 cd11575
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
 101-199 3.29e-07

Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism.


Pssm-ID: 211416  Cd Length: 376  Bit Score: 50.42  E-value: 3.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534766 101 VYSDLHAFYYSwygspRREGHYIHWdHVMVPHWDPkiSASYPRGRHsppdDLGSSFYPELGPYSSRDPEVLREHMTQLKE 180
Cdd:cd11575   9 VYAHYMPWFET-----RPDDGKWGW-HWTMANFDP--DHIDASGKR----QIASHYYPLIGPYSSGDPDVIEYQLLLMKL 76

                        90       100
                ....*....|....*....|
gi 72534766 181 AAI-GVLVlSWYppGMADDN 199
Cdd:cd11575  77 AGIdGVIV-DWY--GTGHFS 93
GH99_GH71_like cd11573
Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside ...
 163-246 3.72e-05

Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside hydrolases contains families GH71 and GH99 (following the CAZY nomenclature), as well as other members with undefined function and specificity.


Pssm-ID: 211414  Cd Length: 284  Bit Score: 44.02  E-value: 3.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534766 163 YSSRDPEVLREHMTQLKEAAIGVLVLSWYPPGMADDNGEpSDDLVPAILDTAHQYSIQVAFHIQPYKGRDDITVHDNIKY 242
Cdd:cd11573   5 YQPWTPEVMRKHIRWAQEAGIDGFAVDWYPEADTSPLAE-TTAILNKALDAAEEENFTIFFMLDPASLREAGELDVVLER 83


                ....
gi 72534766 243 IIDT 246
Cdd:cd11573  84 ITRL 87
GH99_GH71_like_1 cd11578
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
 107-198 9.44e-04

Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside hydrolases resembles glycosyl hydrolase families 71 and 99 (following the CAZY nomenclature) and may share a similar catalytic site and mechanism.


Pssm-ID: 211419  Cd Length: 313  Bit Score: 39.70  E-value: 9.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 72534766 107 AFYYSWYGSprreghYIHWDhvmvphwdpkisasyprgrhsppddLGSSFYPELGPYSSRDPEVLREHMTQLKEAAIGVL 186
Cdd:cd11578   3 AYYYNWTSS------GLDWN-------------------------KKYPEEPLLGEYDALDPAVIEQHIDWADQAGIDFF 51

                        90
                ....*....|..
gi 72534766 187 VLSWYPPGMADD 198
Cdd:cd11578  52 IVSWWGPDNDNV 63
 
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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