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Conserved domains on  [gi|19920762|ref|NP_608937|]
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uncharacterized protein Dmel_CG14015 [Drosophila melanogaster]

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 ...
130-453 1.64e-72

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: 232.98  E-value: 1.64e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 130 VHIFYtapVPWYKSKKPPPP-------PAEHPNDV---PLTTPRPVRILNTAFYPALGLYKPSG-SLLAQHFENIRSCGI 198
Cdd:cd11574   1 VHIFY---YAWYGNPEFDGKyghwnhkILPHWDIAkkyPQGRHDPPDDIGSNFYPKLGPYSSSDpSVIDDHMKQIREAGI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 199 GVLILSFSG-------GKPaEAALLHQILELAPQHNLSVTFELSVAGNQSVEFVRQQLQEIA-TYTSLAGFYKVwsqSRG 270
Cdd:cd11574  78 GVVVVSWYGpgssddnGKP-SDDTIPLLLDIAHEYGLKVAFHIEPYEGRTAASLREDIKYILdKYGSHPAFYKY---KKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 271 VSLPVLYVSNAYKLSDS-LGRLLCRSPSLVEPDglrRILDALFIGHIRLKSHADVLRRLCFDGFYSKLPSNGAVFASTWK 349
Cdd:cd11574 154 RGLPVFYIYDSYLTPPSdWAKLLSPNGKLTIRN---TAYDAIFIGLLVESDHKSDILEAGFDGFYTYFAANGFTYGSTPK 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 350 NWSYLKSFALSYKMLFVPTVGPGFAERNKFPRHGDIQRHRSNGRYYGVAWRTAILNHVGFINIASYNNWPDGSQIEEVMP 429
Cdd:cd11574 231 NWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMWKAALKVDPDIISITSFNEWHEGTQIEPAVP 310
                       330       340
                ....*....|....*....|....*...
gi 19920762 430 RAGF----LDYNPGSRTKYLDLTAHWVG 453
Cdd:cd11574 311 KKGGeftyLDYSPNDPDFYLELTRKWVE 338
 
Name Accession Description Interval E-value
GH99 cd11574
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
130-453 1.64e-72

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: 232.98  E-value: 1.64e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 130 VHIFYtapVPWYKSKKPPPP-------PAEHPNDV---PLTTPRPVRILNTAFYPALGLYKPSG-SLLAQHFENIRSCGI 198
Cdd:cd11574   1 VHIFY---YAWYGNPEFDGKyghwnhkILPHWDIAkkyPQGRHDPPDDIGSNFYPKLGPYSSSDpSVIDDHMKQIREAGI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 199 GVLILSFSG-------GKPaEAALLHQILELAPQHNLSVTFELSVAGNQSVEFVRQQLQEIA-TYTSLAGFYKVwsqSRG 270
Cdd:cd11574  78 GVVVVSWYGpgssddnGKP-SDDTIPLLLDIAHEYGLKVAFHIEPYEGRTAASLREDIKYILdKYGSHPAFYKY---KKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 271 VSLPVLYVSNAYKLSDS-LGRLLCRSPSLVEPDglrRILDALFIGHIRLKSHADVLRRLCFDGFYSKLPSNGAVFASTWK 349
Cdd:cd11574 154 RGLPVFYIYDSYLTPPSdWAKLLSPNGKLTIRN---TAYDAIFIGLLVESDHKSDILEAGFDGFYTYFAANGFTYGSTPK 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 350 NWSYLKSFALSYKMLFVPTVGPGFAERNKFPRHGDIQRHRSNGRYYGVAWRTAILNHVGFINIASYNNWPDGSQIEEVMP 429
Cdd:cd11574 231 NWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMWKAALKVDPDIISITSFNEWHEGTQIEPAVP 310
                       330       340
                ....*....|....*....|....*...
gi 19920762 430 RAGF----LDYNPGSRTKYLDLTAHWVG 453
Cdd:cd11574 311 KKGGeftyLDYSPNDPDFYLELTRKWVE 338
Glyco_hydro_99 pfam16317
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
172-457 2.55e-50

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: 174.70  E-value: 2.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762   172 FYPALGLYKPSG-SLLAQHFENIRSCGIGVLILSFSGGKPAEAALLHQILELAPQHNLSVTFELSVAGNQSVEFVRQQLQ 250
Cdd:pfam16317  58 FYPELGSYSSRDpEIIETHMRMMRSASIGVLSVSWYGENDEATRSVPTILDKAAKYGLKVTFHIEPYNNRSDQNMHANIK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762   251 EIA-TYTSLAGFYKVWSQsrgvslPVLYVSNAYKLSDSlgrllcRSPSLVEPDGLRRI----LDALFIGHIRLKSHADVL 325
Cdd:pfam16317 138 YIIdKYGNHPAFYRYKGK------PLFYVYDSYITKPS------EWAKLLTPGGELSVrnspYDGLFIGLLVEEKEKYDI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762   326 RRLCFDGFYSKLPSNGAVFASTWKNWSYLKSFALSYKMLFVPTVGPGFAERNKFPRHGDIQRHRSNGRYYGVAWRTAILN 405
Cdd:pfam16317 206 LQSGFDGFYTYFATNGFTYGSTHQNWPSLKGWASKHNKLFIPSVGPGYIDTRIRPWNGQNTRNRENGKYYDRMLSAALQT 285
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19920762   406 HVGFINIASYNNWPDGSQIEEVMPRAG----FLDYNPGSRTKYLDLTAHWVGNFLK 457
Cdd:pfam16317 286 KPSLISITSFNEWHEGTQIEPAVPKRTpntvYLDYRPLKPDYYLERTRKWSEKYSK 341
 
Name Accession Description Interval E-value
GH99 cd11574
Glycoside hydrolase family 99, an endo-alpha-1,2-mannosidase; This family of glycoside ...
130-453 1.64e-72

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: 232.98  E-value: 1.64e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 130 VHIFYtapVPWYKSKKPPPP-------PAEHPNDV---PLTTPRPVRILNTAFYPALGLYKPSG-SLLAQHFENIRSCGI 198
Cdd:cd11574   1 VHIFY---YAWYGNPEFDGKyghwnhkILPHWDIAkkyPQGRHDPPDDIGSNFYPKLGPYSSSDpSVIDDHMKQIREAGI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 199 GVLILSFSG-------GKPaEAALLHQILELAPQHNLSVTFELSVAGNQSVEFVRQQLQEIA-TYTSLAGFYKVwsqSRG 270
Cdd:cd11574  78 GVVVVSWYGpgssddnGKP-SDDTIPLLLDIAHEYGLKVAFHIEPYEGRTAASLREDIKYILdKYGSHPAFYKY---KKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 271 VSLPVLYVSNAYKLSDS-LGRLLCRSPSLVEPDglrRILDALFIGHIRLKSHADVLRRLCFDGFYSKLPSNGAVFASTWK 349
Cdd:cd11574 154 RGLPVFYIYDSYLTPPSdWAKLLSPNGKLTIRN---TAYDAIFIGLLVESDHKSDILEAGFDGFYTYFAANGFTYGSTPK 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 350 NWSYLKSFALSYKMLFVPTVGPGFAERNKFPRHGDIQRHRSNGRYYGVAWRTAILNHVGFINIASYNNWPDGSQIEEVMP 429
Cdd:cd11574 231 NWKQLSKFARERGLLFIPSVGPGYDDTRVRPWNASNTRSRENGKYYEKMWKAALKVDPDIISITSFNEWHEGTQIEPAVP 310
                       330       340
                ....*....|....*....|....*...
gi 19920762 430 RAGF----LDYNPGSRTKYLDLTAHWVG 453
Cdd:cd11574 311 KKGGeftyLDYSPNDPDFYLELTRKWVE 338
Glyco_hydro_99 pfam16317
Glycosyl hydrolase family 99; This domain, around 350 residues, is mainly found in some ...
172-457 2.55e-50

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: 174.70  E-value: 2.55e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762   172 FYPALGLYKPSG-SLLAQHFENIRSCGIGVLILSFSGGKPAEAALLHQILELAPQHNLSVTFELSVAGNQSVEFVRQQLQ 250
Cdd:pfam16317  58 FYPELGSYSSRDpEIIETHMRMMRSASIGVLSVSWYGENDEATRSVPTILDKAAKYGLKVTFHIEPYNNRSDQNMHANIK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762   251 EIA-TYTSLAGFYKVWSQsrgvslPVLYVSNAYKLSDSlgrllcRSPSLVEPDGLRRI----LDALFIGHIRLKSHADVL 325
Cdd:pfam16317 138 YIIdKYGNHPAFYRYKGK------PLFYVYDSYITKPS------EWAKLLTPGGELSVrnspYDGLFIGLLVEEKEKYDI 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762   326 RRLCFDGFYSKLPSNGAVFASTWKNWSYLKSFALSYKMLFVPTVGPGFAERNKFPRHGDIQRHRSNGRYYGVAWRTAILN 405
Cdd:pfam16317 206 LQSGFDGFYTYFATNGFTYGSTHQNWPSLKGWASKHNKLFIPSVGPGYIDTRIRPWNGQNTRNRENGKYYDRMLSAALQT 285
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19920762   406 HVGFINIASYNNWPDGSQIEEVMPRAG----FLDYNPGSRTKYLDLTAHWVGNFLK 457
Cdd:pfam16317 286 KPSLISITSFNEWHEGTQIEPAVPKRTpntvYLDYRPLKPDYYLERTRKWSEKYSK 341
GH99_GH71_like cd11573
Glycoside hydrolase families 71, 99, and related domains; This superfamily of glycoside ...
189-453 4.31e-16

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: 78.31  E-value: 4.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 189 HFENIRSCGIGVLILSF-----SGGKPAEAALLHQILELAPQHNLSVTFELSVA---GNQSVEFVRQQLQE-IATYTSLA 259
Cdd:cd11573  16 HIRWAQEAGIDGFAVDWypeadTSPLAETTAILNKALDAAEEENFTIFFMLDPAslrEAGELDVVLERITRlINEYRNPS 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 260 GFYKVwsQSRgvslPVLYV-SNAYKLSDSLGRLLCRSPslvepdglrRILDALFIGhirLKSHADVLRRLC----FDGFY 334
Cdd:cd11573  96 SYYKV--GGK----PLVFIwGPGLAYTASEWEALKAQL---------RAGCPYMIG---LWTPWRVPNRDMitdmFDGAS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 335 SKLP----SNGAVFASTWKNWSYLKSFALSYKMLFVPTVGPGFAERNKFP-RHGDIQRHRSnGRYYGVAWRTAILNHVGF 409
Cdd:cd11573 158 PWTPwrgtNPEEAYGHGVKNWRPDQEWMGANGKGYIPTVSPGFSDINRRPgDPGDIILRRD-GQRLHSMLEAALKAGPAM 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 19920762 410 INIASYNNWPDGSQIEEV----MPRAGFLDYNPGSRTKYLDLTAHWVG 453
Cdd:cd11573 237 IQIASWNDWGEGTYIEPCeeygPRDRKFVTYEGRPPDAYLKRTPRALG 284
GH99_GH71_like_1 cd11578
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
339-433 4.34e-08

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: 54.72  E-value: 4.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 339 SNGAVFASTW--KNWSYLKSFALSYKMLFVPTVGPGFAERNKFPR-HGDIQRHRSNGRYY-GVAWRTaiLNHVGFINIAS 414
Cdd:cd11578 203 SKEFLAFYSFvdLNWRNWTESLGKWNVDFIPCISPGFNDTVDNLFqSYKLERNPSSFKKMcNVALRN--DGACNIVLITS 280
                        90
                ....*....|....*....
gi 19920762 415 YNNWPDGSQIEEVMPRAGF 433
Cdd:cd11578 281 FNEWNEGTNIEPSEEAYGF 299
GH99_GH71_like_3 cd11575
Uncharacterized glycoside hydrolase family 99-like domain; This family of putative glycoside ...
331-425 5.54e-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: 5.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920762 331 DGFYSKLPSNGAVFASTWKNWSYLKSF---ALSYKMLfVPTVGPGFaerNKFPRHGDIQRH-----RSNGRYYGVAWRTA 402
Cdd:cd11575 210 DGEFAWVPARLRVSTARLEGLDYLDNFytnFADWPIA-IGSAYPGF---DDFYCEGGGGGSywyipRNNGETFLRTLDLA 285
                        90       100
                ....*....|....*....|...
gi 19920762 403 ILNHVGFINIASYNNWPDGSQIE 425
Cdd:cd11575 286 LASGLDIIQIATWNDYGEGTMIE 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.
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