NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1720408096|ref|XP_030109256|]
View 

glycoprotein endo-alpha-1,2-mannosidase-like protein isoform X2 [Mus musculus]

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 8.32e-118

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: 339.29  E-value: 8.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096  24 RYGSHGAFYRYKNsmGKSLPLFYIYDSYLTSPEAWAHLLTQNGPHSIRNTPYDGVFIALLVEESHTHDILAAGFDGMYTY 103
Cdd:cd11574   140 KYGSHPAFYKYKK--GRGLPVFYIYDSYLTPPSDWAKLLSPNGKLTIRNTAYDAIFIGLLVESDHKSDILEAGFDGFYTY 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096 104 FASNGFSFGSSHQNWKAVKNFCDTNNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:cd11574   218 FAANGFTYGSTPKNWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMWKAALKVDPDIISITSFN 297
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720408096 184 EWHEGTQIEKAVPKTTPTRLYLDYLPHQSSLYLELTRRWAE 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 8.32e-118

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: 339.29  E-value: 8.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096  24 RYGSHGAFYRYKNsmGKSLPLFYIYDSYLTSPEAWAHLLTQNGPHSIRNTPYDGVFIALLVEESHTHDILAAGFDGMYTY 103
Cdd:cd11574   140 KYGSHPAFYKYKK--GRGLPVFYIYDSYLTPPSDWAKLLSPNGKLTIRNTAYDAIFIGLLVESDHKSDILEAGFDGFYTY 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096 104 FASNGFSFGSSHQNWKAVKNFCDTNNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:cd11574   218 FAANGFTYGSTPKNWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMWKAALKVDPDIISITSFN 297
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720408096 184 EWHEGTQIEKAVPKTTPTRLYLDYLPHQSSLYLELTRRWAE 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 1.34e-106

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: 311.06  E-value: 1.34e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096  24 RYGSHGAFYRYKnsmGKslPLFYIYDSYLTSPEAWAHLLTQNGPHSIRNTPYDGVFIALLVEESHTHDILAAGFDGMYTY 103
Cdd:pfam16317 142 KYGNHPAFYRYK---GK--PLFYVYDSYITKPSEWAKLLTPGGELSVRNSPYDGLFIGLLVEEKEKYDILQSGFDGFYTY 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096 104 FASNGFSFGSSHQNWKAVKNFCDTNNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:pfam16317 217 FATNGFTYGSTHQNWPSLKGWASKHNKLFIPSVGPGYIDTRIRPWNGQNTRNRENGKYYDRMLSAALQTKPSLISITSFN 296
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720408096 184 EWHEGTQIEKAVPKTTPTRLYLDYLPHQSSLYLELTRRWAEHFIK 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 8.32e-118

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: 339.29  E-value: 8.32e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096  24 RYGSHGAFYRYKNsmGKSLPLFYIYDSYLTSPEAWAHLLTQNGPHSIRNTPYDGVFIALLVEESHTHDILAAGFDGMYTY 103
Cdd:cd11574   140 KYGSHPAFYKYKK--GRGLPVFYIYDSYLTPPSDWAKLLSPNGKLTIRNTAYDAIFIGLLVESDHKSDILEAGFDGFYTY 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096 104 FASNGFSFGSSHQNWKAVKNFCDTNNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:cd11574   218 FAANGFTYGSTPKNWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMWKAALKVDPDIISITSFN 297
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1720408096 184 EWHEGTQIEKAVPKTTPTRLYLDYLPHQSSLYLELTRRWAE 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 1.34e-106

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: 311.06  E-value: 1.34e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096  24 RYGSHGAFYRYKnsmGKslPLFYIYDSYLTSPEAWAHLLTQNGPHSIRNTPYDGVFIALLVEESHTHDILAAGFDGMYTY 103
Cdd:pfam16317 142 KYGNHPAFYRYK---GK--PLFYVYDSYITKPSEWAKLLTPGGELSVRNSPYDGLFIGLLVEEKEKYDILQSGFDGFYTY 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096 104 FASNGFSFGSSHQNWKAVKNFCDTNNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYETALQAALTVRPEIVSITSFN 183
Cdd:pfam16317 217 FATNGFTYGSTHQNWPSLKGWASKHNKLFIPSVGPGYIDTRIRPWNGQNTRNRENGKYYDRMLSAALQTKPSLISITSFN 296
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1720408096 184 EWHEGTQIEKAVPKTTPTRLYLDYLPHQSSLYLELTRRWAEHFIK 228
Cdd:pfam16317 297 EWHEGTQIEPAVPKRTPNTVYLDYRPLKPDYYLERTRKWSEKYSK 341
GH99_GH71_like cd11573
Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside ...
10-223 1.11e-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: 127.61  E-value: 1.11e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096  10 WYLPFWTlpiSTTSRYGSHGAFYRYKnsmGKslPLFYIYDSYL-TSPEAWAHLLTQNgphsirnTPYDGVFIALLVEES- 87
Cdd:cd11573    79 VVLERIT---RLINEYRNPSSYYKVG---GK--PLVFIWGPGLaYTASEWEALKAQL-------RAGCPYMIGLWTPWRv 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096  88 HTHDILAAGFDGMYTYFASNGFS----FGSSHQNWKAVKNFCDTNNLMFIPSVGPGYIDTSIRPWNNHNTRNRVNGKYYE 163
Cdd:cd11573   144 PNRDMITDMFDGASPWTPWRGTNpeeaYGHGVKNWRPDQEWMGANGKGYIPTVSPGFSDINRRPGDPGDIILRRDGQRLH 223
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096 164 TALQAALTVRPEIVSITSFNEWHEGTQIEKAVPKTTPTRLYLDYLPHQSSLYLELTRRWA 223
Cdd:cd11573   224 SMLEAALKAGPAMIQIASWNDWGEGTYIEPCEEYGPRDRKFVTYEGRPPDAYLKRTPRAL 283
GH99_GH71_like_1 cd11578
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
116-192 9.54e-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: 57.42  E-value: 9.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096 116 QNWKAVKNFCDTNNLMFIPSVGPGYIDTSIRPWNNHN-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 1.30e-05

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: 45.32  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096 115 HQNWKAVKNFCDTNNLMFIPSVGPGyidTSIRPWNNHNTRN---RVNGKYYETALQAALTVRPEIVSITSFNEWHEGTQI 191
Cdd:cd11576   257 TNVIKPDKAWCNANGIDYQPVVFPG---FSWHNLKGGSPLNqipRLGGDFLWRQAYNAKKAGAKMIYVAMFDEYDEGTAI 333
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720408096 192 EKAV--PKTTPTRLYL-------DYLPhqSSLYLELT 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 1.56e-03

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: 38.86  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096  43 PLFYIY-DSYLTSPEAWAHLLTqngphSIRNTPYdgvFIALlveESHTHDILAAGFDGMYTYFASNGFSFGSSHQNWKAV 121
Cdd:cd11575   165 PLLLLFgPQFLKSEEEWTVIFS-----ALKPKPV---FLTL---WGETNEVGANLADGEFAWVPARLRVSTARLEGLDYL 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720408096 122 KNFCDTNNL--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