NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|22749033|ref|NP_689709|]
View 

glycoprotein endo-alpha-1,2-mannosidase-like protein isoform 2 [Homo sapiens]

Protein Classification

glycoside hydrolase family 99 protein( domain architecture ID 10184038)

glycoside hydrolase family 99 protein similar to glycoprotein endo-alpha-1,2-mannosidase that catalyzes the hydrolysis of the terminal alpha-D-glucosyl- (1->3)-D-mannosyl unit from the GlcMan(9)(GlcNAc)(2) oligosaccharide component of N-glucosylated proteins during their processing in the Golgi apparatus

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GH99 cd11574
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
 24-224 3.16e-120

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: 345.45  E-value: 3.16e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033  24 RYGSHGAFYRYKNsmGKSLPLFYIYDSYLTSPEAWAHLLTPNGPHSIRNTPYDGVFIALLVEEGHTHDILAAGFDGMYTY 103
Cdd:cd11574 140 KYGSHPAFYKYKK--GRGLPVFYIYDSYLTPPSDWAKLLSPNGKLTIRNTAYDAIFIGLLVESDHKSDILEAGFDGFYTY 217

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033 104 FASNGFSFGSSHQNWKAVKNFCDANNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:cd11574 218 FAANGFTYGSTPKNWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMWKAALKVDPDIISITSFN 297

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 22749033 184 EWHEGTQIEKAIPKKTPTRLYLDYLPHQPSLYLELTRRWAE 224
Cdd:cd11574 298 EWHEGTQIEPAVPKKGGEFTYLDYSPNDPDFYLELTRKWVE 338
 
Name Accession Description Interval E-value
GH99 cd11574
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
 24-224 3.16e-120

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: 345.45  E-value: 3.16e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033  24 RYGSHGAFYRYKNsmGKSLPLFYIYDSYLTSPEAWAHLLTPNGPHSIRNTPYDGVFIALLVEEGHTHDILAAGFDGMYTY 103
Cdd:cd11574 140 KYGSHPAFYKYKK--GRGLPVFYIYDSYLTPPSDWAKLLSPNGKLTIRNTAYDAIFIGLLVESDHKSDILEAGFDGFYTY 217

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033 104 FASNGFSFGSSHQNWKAVKNFCDANNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:cd11574 218 FAANGFTYGSTPKNWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMWKAALKVDPDIISITSFN 297

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 22749033 184 EWHEGTQIEKAIPKKTPTRLYLDYLPHQPSLYLELTRRWAE 224
Cdd:cd11574 298 EWHEGTQIEPAVPKKGGEFTYLDYSPNDPDFYLELTRKWVE 338
Glyco_hydro_99 pfam16317
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
 24-228 1.50e-109

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: 318.38  E-value: 1.50e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033    24 RYGSHGAFYRYKnsmGKslPLFYIYDSYLTSPEAWAHLLTPNGPHSIRNTPYDGVFIALLVEEGHTHDILAAGFDGMYTY 103
Cdd:pfam16317 142 KYGNHPAFYRYK---GK--PLFYVYDSYITKPSEWAKLLTPGGELSVRNSPYDGLFIGLLVEEKEKYDILQSGFDGFYTY 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033   104 FASNGFSFGSSHQNWKAVKNFCDANNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:pfam16317 217 FATNGFTYGSTHQNWPSLKGWASKHNKLFIPSVGPGYIDTRIRPWNGQNTRNRENGKYYDRMLSAALQTKPSLISITSFN 296

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 22749033   184 EWHEGTQIEKAIPKKTPTRLYLDYLPHQPSLYLELTRRWAEHFIK 228
Cdd:pfam16317 297 EWHEGTQIEPAVPKRTPNTVYLDYRPLKPDYYLERTRKWSEKYSK 341
 
Name Accession Description Interval E-value
GH99 cd11574
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
 24-224 3.16e-120

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: 345.45  E-value: 3.16e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033  24 RYGSHGAFYRYKNsmGKSLPLFYIYDSYLTSPEAWAHLLTPNGPHSIRNTPYDGVFIALLVEEGHTHDILAAGFDGMYTY 103
Cdd:cd11574 140 KYGSHPAFYKYKK--GRGLPVFYIYDSYLTPPSDWAKLLSPNGKLTIRNTAYDAIFIGLLVESDHKSDILEAGFDGFYTY 217

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033 104 FASNGFSFGSSHQNWKAVKNFCDANNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:cd11574 218 FAANGFTYGSTPKNWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMWKAALKVDPDIISITSFN 297

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 22749033 184 EWHEGTQIEKAIPKKTPTRLYLDYLPHQPSLYLELTRRWAE 224
Cdd:cd11574 298 EWHEGTQIEPAVPKKGGEFTYLDYSPNDPDFYLELTRKWVE 338
Glyco_hydro_99 pfam16317
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
 24-228 1.50e-109

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: 318.38  E-value: 1.50e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033    24 RYGSHGAFYRYKnsmGKslPLFYIYDSYLTSPEAWAHLLTPNGPHSIRNTPYDGVFIALLVEEGHTHDILAAGFDGMYTY 103
Cdd:pfam16317 142 KYGNHPAFYRYK---GK--PLFYVYDSYITKPSEWAKLLTPGGELSVRNSPYDGLFIGLLVEEKEKYDILQSGFDGFYTY 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033   104 FASNGFSFGSSHQNWKAVKNFCDANNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:pfam16317 217 FATNGFTYGSTHQNWPSLKGWASKHNKLFIPSVGPGYIDTRIRPWNGQNTRNRENGKYYDRMLSAALQTKPSLISITSFN 296

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 22749033   184 EWHEGTQIEKAIPKKTPTRLYLDYLPHQPSLYLELTRRWAEHFIK 228
Cdd:pfam16317 297 EWHEGTQIEPAVPKRTPNTVYLDYRPLKPDYYLERTRKWSEKYSK 341
GH99_GH71_like cd11573
Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside ...
 19-223 4.58e-35

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: 126.07  E-value: 4.58e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033  19 ISTASRYGSHGAFYRYKnsmGKslPLFYIYDSYL-TSPEAWAHLLTPNgphsirnTPYDGVFIALLV-EEGHTHDILAAG 96
Cdd:cd11573  85 TRLINEYRNPSSYYKVG---GK--PLVFIWGPGLaYTASEWEALKAQL-------RAGCPYMIGLWTpWRVPNRDMITDM 152

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033  97 FDGMYTYFASNGFS----FGSSHQNWKAVKNFCDANNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTV 172
Cdd:cd11573 153 FDGASPWTPWRGTNpeeaYGHGVKNWRPDQEWMGANGKGYIPTVSPGFSDINRRPGDPGDIILRRDGQRLHSMLEAALKA 232

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 22749033 173 RPEIVSITSFNEWHEGTQIEKAIPKKTPTRLYLDYLPHQPSLYLELTRRWA 223
Cdd:cd11573 233 GPAMIQIASWNDWGEGTYIEPCEEYGPRDRKFVTYEGRPPDAYLKRTPRAL 283
GH99_GH71_like_1 cd11578
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
 116-192 6.23e-10

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: 58.19  E-value: 6.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033 116 QNWKAVKNFCDANNLMFIPSVGPGYIDTSIRPWNNHN-TRNRVNGKYYetaLQAALTVRPE--IVSITSFNEWHEGTQIE 192
Cdd:cd11578 215 LNWRNWTESLGKWNVDFIPCISPGFNDTVDNLFQSYKlERNPSSFKKM---CNVALRNDGAcnIVLITSFNEWNEGTNIE 291
GH99_GH71_like_2 cd11576
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
 115-219 2.24e-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. The domain may co-occur with other domains involved in the binding/processing of glycans.


Pssm-ID: 211417  Cd Length: 378  Bit Score: 41.47  E-value: 2.24e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033 115 HQNWKAVKNFCDANNLMFIPSVGPGyidTSIRPWNNHNTRN---RVNGKYYETALQAALTVRPEIVSITSFNEWHEGTQI 191
Cdd:cd11576 257 TNVIKPDKAWCNANGIDYQPVVFPG---FSWHNLKGGSPLNqipRLGGDFLWRQAYNAKKAGAKMIYVAMFDEYDEGTAI 333

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 22749033 192 EKAIPKK--TPTRLYL-------DYLPhqPSLYLELT 219
Cdd:cd11576 334 FKVAEDPpvPPNGQYFltldadgDGLP--SDFYLRLT 368
GH99_GH71_like_3 cd11575
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
 43-192 5.34e-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: 211416  Cd Length: 376  Bit Score: 40.40  E-value: 5.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033  43 PLFYIY-DSYLTSPEAWAHLLTPngphsIRNTPYdgvFIALlveEGHTHDILAAGFDGMYTYFASNGFSFGSSHQNWKAV 121
Cdd:cd11575 165 PLLLLFgPQFLKSEEEWTVIFSA-----LKPKPV---FLTL---WGETNEVGANLADGEFAWVPARLRVSTARLEGLDYL 233

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22749033 122 KNFCDANNL--MFIPSVGPGYIDTSIRPWNN-------HNtrnrvNGKYYETALQAALTVRPEIVSITSFNEWHEGTQIE 192
Cdd:cd11575 234 DNFYTNFADwpIAIGSAYPGFDDFYCEGGGGgsywyipRN-----NGETFLRTLDLALASGLDIIQIATWNDYGEGTMIE 308
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH