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Conserved domains on  [gi|19114765|ref|NP_593853|]
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dolichol-P-Man-dependent alpha(1-3) mannosyltransferase Alg3 [Schizosaccharomyces pombe]

Protein Classification

glycosyltransferase family 58 protein( domain architecture ID 10525167)

glycosyltransferase family 58 protein similar to Dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase that adds the first Dol-P-Man derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-Dol

CAZY:  GT58
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ALG3 pfam05208
ALG3 protein; The formation of N-glycosidic linkages of glycoproteins involves the ordered ...
30-384 4.20e-170

ALG3 protein; The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl pyrophosphate. Whereas early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9GlcNAc2-PP-Dol on the lumenal side use Dol-P-Man. ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase.


:

Pssm-ID: 461587  Cd Length: 358  Bit Score: 479.66  E-value: 4.20e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765    30 LLLLEIPFVFAIISKVPYTEIDWIAYMEQVNSFLLGERDYKSLVGCTGPLVYPGGHVFLYTLLYYLTDGGTNIVRAQYIF 109
Cdd:pfam05208   3 LLLAEAVLCKLIIWKVPYTEIDWKAYMQQVEGFLNGERDYSKIKGDTGPLVYPAGHVYIYSALYYLTDGGRNIRLAQYIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765   110 AFVYWITTAIVGYLFKIVRAPFYIYVLLILSKRLHSIFILRLFNDGFNSLFSSLFILSSCKKKWVRASILLSVACSVKMS 189
Cdd:pfam05208  83 AGLYLLTLALVFAIYRRAKVPPYVLPLLCLSKRLHSIFVLRLFNDCFAMLFLYLAILLFQRRRWTLGSLLYSLAVSIKMN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765   190 SLLYVPAYLVLLLQILGPKKTWMHIFVIIIVQILFSIPFLAYF-WSYWTQAFDFGRAFDYKWTVNWRFIPRSIFESTSFS 268
Cdd:pfam05208 163 ALLFLPALLVLLLLNLGLLGTLRQLAVIALVQVLLGLPFLLTNpRSYLSRAFDFSRQFLYKWTVNWRFVPEEIFLSKEFA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765   269 TSILFLHVALLVAFTCKHWNKLSRATPFAMVNSMLTLKPLPKLQLATPNFIFTALATSNLIGILCARSLHYQFYAWFAWY 348
Cdd:pfam05208 243 LALLALHLALLLLFALTRWLRPSGGLDFVLKLLLIRPLLKPASPPLSPDLILTTLFTSNLIGILFARSLHYQFYSWYAWT 322
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 19114765   349 SPYLCYQASFPAPIVIGLWMLQEYAWNVFPSTKLSS 384
Cdd:pfam05208 323 LPFLLWRTGLPPVLRLALWAAIEYCWNVYPSTPLSS 358
 
Name Accession Description Interval E-value
ALG3 pfam05208
ALG3 protein; The formation of N-glycosidic linkages of glycoproteins involves the ordered ...
30-384 4.20e-170

ALG3 protein; The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl pyrophosphate. Whereas early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9GlcNAc2-PP-Dol on the lumenal side use Dol-P-Man. ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase.


Pssm-ID: 461587  Cd Length: 358  Bit Score: 479.66  E-value: 4.20e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765    30 LLLLEIPFVFAIISKVPYTEIDWIAYMEQVNSFLLGERDYKSLVGCTGPLVYPGGHVFLYTLLYYLTDGGTNIVRAQYIF 109
Cdd:pfam05208   3 LLLAEAVLCKLIIWKVPYTEIDWKAYMQQVEGFLNGERDYSKIKGDTGPLVYPAGHVYIYSALYYLTDGGRNIRLAQYIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765   110 AFVYWITTAIVGYLFKIVRAPFYIYVLLILSKRLHSIFILRLFNDGFNSLFSSLFILSSCKKKWVRASILLSVACSVKMS 189
Cdd:pfam05208  83 AGLYLLTLALVFAIYRRAKVPPYVLPLLCLSKRLHSIFVLRLFNDCFAMLFLYLAILLFQRRRWTLGSLLYSLAVSIKMN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765   190 SLLYVPAYLVLLLQILGPKKTWMHIFVIIIVQILFSIPFLAYF-WSYWTQAFDFGRAFDYKWTVNWRFIPRSIFESTSFS 268
Cdd:pfam05208 163 ALLFLPALLVLLLLNLGLLGTLRQLAVIALVQVLLGLPFLLTNpRSYLSRAFDFSRQFLYKWTVNWRFVPEEIFLSKEFA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765   269 TSILFLHVALLVAFTCKHWNKLSRATPFAMVNSMLTLKPLPKLQLATPNFIFTALATSNLIGILCARSLHYQFYAWFAWY 348
Cdd:pfam05208 243 LALLALHLALLLLFALTRWLRPSGGLDFVLKLLLIRPLLKPASPPLSPDLILTTLFTSNLIGILFARSLHYQFYSWYAWT 322
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 19114765   349 SPYLCYQASFPAPIVIGLWMLQEYAWNVFPSTKLSS 384
Cdd:pfam05208 323 LPFLLWRTGLPPVLRLALWAAIEYCWNVYPSTPLSS 358
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
143-232 3.00e-03

Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 39.59  E-value: 3.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765 143 LHSIFILrlfnDGFNSLFSSLFILSSCKKKWVRASILLSVACSVKMSSLLYVPAYLVLLLQI-LGPKKTWMHIFVI-IIV 220
Cdd:COG4346 146 MSSIAML----DIYVAFFTALALYFAVSGRLLLSSIALGLAAASKYSGLFLLIPLLLYLREIeKSPIKRFLYGILIpLAV 221
                        90
                ....*....|..
gi 19114765 221 QILFSIPFLAYF 232
Cdd:COG4346 222 FLIVSIPLIIYF 233
 
Name Accession Description Interval E-value
ALG3 pfam05208
ALG3 protein; The formation of N-glycosidic linkages of glycoproteins involves the ordered ...
30-384 4.20e-170

ALG3 protein; The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl pyrophosphate. Whereas early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9GlcNAc2-PP-Dol on the lumenal side use Dol-P-Man. ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase.


Pssm-ID: 461587  Cd Length: 358  Bit Score: 479.66  E-value: 4.20e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765    30 LLLLEIPFVFAIISKVPYTEIDWIAYMEQVNSFLLGERDYKSLVGCTGPLVYPGGHVFLYTLLYYLTDGGTNIVRAQYIF 109
Cdd:pfam05208   3 LLLAEAVLCKLIIWKVPYTEIDWKAYMQQVEGFLNGERDYSKIKGDTGPLVYPAGHVYIYSALYYLTDGGRNIRLAQYIF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765   110 AFVYWITTAIVGYLFKIVRAPFYIYVLLILSKRLHSIFILRLFNDGFNSLFSSLFILSSCKKKWVRASILLSVACSVKMS 189
Cdd:pfam05208  83 AGLYLLTLALVFAIYRRAKVPPYVLPLLCLSKRLHSIFVLRLFNDCFAMLFLYLAILLFQRRRWTLGSLLYSLAVSIKMN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765   190 SLLYVPAYLVLLLQILGPKKTWMHIFVIIIVQILFSIPFLAYF-WSYWTQAFDFGRAFDYKWTVNWRFIPRSIFESTSFS 268
Cdd:pfam05208 163 ALLFLPALLVLLLLNLGLLGTLRQLAVIALVQVLLGLPFLLTNpRSYLSRAFDFSRQFLYKWTVNWRFVPEEIFLSKEFA 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765   269 TSILFLHVALLVAFTCKHWNKLSRATPFAMVNSMLTLKPLPKLQLATPNFIFTALATSNLIGILCARSLHYQFYAWFAWY 348
Cdd:pfam05208 243 LALLALHLALLLLFALTRWLRPSGGLDFVLKLLLIRPLLKPASPPLSPDLILTTLFTSNLIGILFARSLHYQFYSWYAWT 322
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 19114765   349 SPYLCYQASFPAPIVIGLWMLQEYAWNVFPSTKLSS 384
Cdd:pfam05208 323 LPFLLWRTGLPPVLRLALWAAIEYCWNVYPSTPLSS 358
COG4346 COG4346
Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase ...
143-232 3.00e-03

Predicted membrane-bound dolichyl-phosphate-mannose-protein mannosyltransferase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443487 [Multi-domain]  Cd Length: 379  Bit Score: 39.59  E-value: 3.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114765 143 LHSIFILrlfnDGFNSLFSSLFILSSCKKKWVRASILLSVACSVKMSSLLYVPAYLVLLLQI-LGPKKTWMHIFVI-IIV 220
Cdd:COG4346 146 MSSIAML----DIYVAFFTALALYFAVSGRLLLSSIALGLAAASKYSGLFLLIPLLLYLREIeKSPIKRFLYGILIpLAV 221
                        90
                ....*....|..
gi 19114765 221 QILFSIPFLAYF 232
Cdd:COG4346 222 FLIVSIPLIIYF 233
 
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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