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Conserved domains on  [gi|19112730|ref|NP_595938|]
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alpha-1,2-mannosyltransferase Omh2 [Schizosaccharomyces pombe]

Protein Classification

glycosyltransferase family 15 protein( domain architecture ID 10009030)

glycosyltransferase family 15 protein similar to alpha 1,2-mannosyltransferase, which transfers a mannose residue from GDP-mannose to a range of acceptors in vitro, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage

CATH:  3.90.550.10
CAZY:  GT15
EC:  2.4.1.-
Gene Ontology:  GO:0006486|GO:0016757
PubMed:  9334165
SCOP:  4001169

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
1-372 0e+00

Mannosyltransferase [Carbohydrate transport and metabolism];


:

Pssm-ID: 227353  Cd Length: 399  Bit Score: 522.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730   1 MRISRLLIRVLLGfVILFITYILFPS-------------IPKALVNTLNVYKLEERLNYYNDRLLDGNLKSKELENATFV 67
Cdd:COG5020   8 LLIPRSVLYVLFL-VSLFAIYVFYVGepssiqsqdepneLPSSEGDAIRNRDSKFSINCYNDELLYLEAPSYPRENATFV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730  68 TLARNADLYDLIETINIYENRFNSKHNYPWVFLNDEPFTRTFEVVMSRLTSGPTYFGVVNSSEWDIPKWIDMDIAHSNWN 147
Cdd:COG5020  87 MLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLTEFGLIPKDEWNFPEWIDEDKAAESLD 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730 148 RLSREGVLYGGMKSYRQMCRYFSGFFWRHPLLDPYKYYWRVEPSTKLLCEVNKDPFRQLRLLNKTYGFVITLFEIGQTVP 227
Cdd:COG5020 167 DMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKDNNKVYGFVISLYEYEETIP 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730 228 SLWNSTLEFIEKYPETLAKNNLWEWISDDNGKKFSHCHFWSNFEIADLDFFRSDSYRKYFDFLDKKGGFFYERWGDAPVH 307
Cdd:COG5020 247 TLWRTTKKFIKKNPGYLSENNLWKFISNDDGIDYNLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVH 326
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112730 308 SIALSLFLDRNKLHYFDEIGYSHAPLLHCPRK------GRCFCKPEEIDLSSNSSCIARFINLTNEDYDEL 372
Cdd:COG5020 327 SIAASLFLDKDQIHYFRDIGYHHSPFHHCPLNagtrlgCRCNCDPGKDITDSSGSCLGKWFNLLNGDKPEG 397
 
Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
1-372 0e+00

Mannosyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 227353  Cd Length: 399  Bit Score: 522.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730   1 MRISRLLIRVLLGfVILFITYILFPS-------------IPKALVNTLNVYKLEERLNYYNDRLLDGNLKSKELENATFV 67
Cdd:COG5020   8 LLIPRSVLYVLFL-VSLFAIYVFYVGepssiqsqdepneLPSSEGDAIRNRDSKFSINCYNDELLYLEAPSYPRENATFV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730  68 TLARNADLYDLIETINIYENRFNSKHNYPWVFLNDEPFTRTFEVVMSRLTSGPTYFGVVNSSEWDIPKWIDMDIAHSNWN 147
Cdd:COG5020  87 MLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLTEFGLIPKDEWNFPEWIDEDKAAESLD 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730 148 RLSREGVLYGGMKSYRQMCRYFSGFFWRHPLLDPYKYYWRVEPSTKLLCEVNKDPFRQLRLLNKTYGFVITLFEIGQTVP 227
Cdd:COG5020 167 DMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKDNNKVYGFVISLYEYEETIP 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730 228 SLWNSTLEFIEKYPETLAKNNLWEWISDDNGKKFSHCHFWSNFEIADLDFFRSDSYRKYFDFLDKKGGFFYERWGDAPVH 307
Cdd:COG5020 247 TLWRTTKKFIKKNPGYLSENNLWKFISNDDGIDYNLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVH 326
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112730 308 SIALSLFLDRNKLHYFDEIGYSHAPLLHCPRK------GRCFCKPEEIDLSSNSSCIARFINLTNEDYDEL 372
Cdd:COG5020 327 SIAASLFLDKDQIHYFRDIGYHHSPFHHCPLNagtrlgCRCNCDPGKDITDSSGSCLGKWFNLLNGDKPEG 397
Glyco_transf_15 pfam01793
Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases ...
62-332 1.08e-126

Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases involved in N-linked and O-linked glycosylation of proteins. Some of the enzymes in this family have been shown to be involved in O- and N-linked glycan modifications in the Golgi.


Pssm-ID: 396385  Cd Length: 313  Bit Score: 366.78  E-value: 1.08e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730    62 ENATFVTLARNADLYDLIETINIYENRFNSKHNYPWVFLNDEPFTRTFEVVMSRLTSGPTYFGVVNSSEWDIPKWIDMDI 141
Cdd:pfam01793  43 YNATILTLVRNSELRKILRSIKQVEKRFNKKFNYPYVFINDEPFTEKFKAKITKLVSADVEFGTIPPEHWSYPDFIDSTK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730   142 AHSNWNRLSREGVLYGGMKSYRQMCRYFSGFFWRHPLLDPYKYYWRVEPSTKLLCEVNKDPFRQLRLLNKTYGFVITLFE 221
Cdd:pfam01793 123 AAKARIDLADANIPYGDSESYRHMCRFYSGFFYKHPELQKYDYYWRIEPGIKFNCDINYDIFKYMQDNNKIYGFTLSLYE 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730   222 IGQTVPSLWNSTLEFIEKYPETLAKNNLWEWISDDNGKKFSHCHFWSNFEIADLDFFRSDSYRKYFDFLDKKGGFFYERW 301
Cdd:pfam01793 203 IEETIPTLWDSTLNFMKQNPEFIAKNNNRSWLSDDGGNTYNTCHFWSNFEIGDLDFFRSEAYEKYFEYLDSKGGFFYERW 282
                         250       260       270
                  ....*....|....*....|....*....|.
gi 19112730   302 GDAPVHSIALSLFLDRNKLHYFDEIGYSHAP 332
Cdd:pfam01793 283 GDAPVHSIAVSLFLPKDDIHFFRDIGYYHDP 313
 
Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
1-372 0e+00

Mannosyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 227353  Cd Length: 399  Bit Score: 522.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730   1 MRISRLLIRVLLGfVILFITYILFPS-------------IPKALVNTLNVYKLEERLNYYNDRLLDGNLKSKELENATFV 67
Cdd:COG5020   8 LLIPRSVLYVLFL-VSLFAIYVFYVGepssiqsqdepneLPSSEGDAIRNRDSKFSINCYNDELLYLEAPSYPRENATFV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730  68 TLARNADLYDLIETINIYENRFNSKHNYPWVFLNDEPFTRTFEVVMSRLTSGPTYFGVVNSSEWDIPKWIDMDIAHSNWN 147
Cdd:COG5020  87 MLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLTEFGLIPKDEWNFPEWIDEDKAAESLD 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730 148 RLSREGVLYGGMKSYRQMCRYFSGFFWRHPLLDPYKYYWRVEPSTKLLCEVNKDPFRQLRLLNKTYGFVITLFEIGQTVP 227
Cdd:COG5020 167 DMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKDNNKVYGFVISLYEYEETIP 246
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730 228 SLWNSTLEFIEKYPETLAKNNLWEWISDDNGKKFSHCHFWSNFEIADLDFFRSDSYRKYFDFLDKKGGFFYERWGDAPVH 307
Cdd:COG5020 247 TLWRTTKKFIKKNPGYLSENNLWKFISNDDGIDYNLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVH 326
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19112730 308 SIALSLFLDRNKLHYFDEIGYSHAPLLHCPRK------GRCFCKPEEIDLSSNSSCIARFINLTNEDYDEL 372
Cdd:COG5020 327 SIAASLFLDKDQIHYFRDIGYHHSPFHHCPLNagtrlgCRCNCDPGKDITDSSGSCLGKWFNLLNGDKPEG 397
Glyco_transf_15 pfam01793
Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases ...
62-332 1.08e-126

Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases involved in N-linked and O-linked glycosylation of proteins. Some of the enzymes in this family have been shown to be involved in O- and N-linked glycan modifications in the Golgi.


Pssm-ID: 396385  Cd Length: 313  Bit Score: 366.78  E-value: 1.08e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730    62 ENATFVTLARNADLYDLIETINIYENRFNSKHNYPWVFLNDEPFTRTFEVVMSRLTSGPTYFGVVNSSEWDIPKWIDMDI 141
Cdd:pfam01793  43 YNATILTLVRNSELRKILRSIKQVEKRFNKKFNYPYVFINDEPFTEKFKAKITKLVSADVEFGTIPPEHWSYPDFIDSTK 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730   142 AHSNWNRLSREGVLYGGMKSYRQMCRYFSGFFWRHPLLDPYKYYWRVEPSTKLLCEVNKDPFRQLRLLNKTYGFVITLFE 221
Cdd:pfam01793 123 AAKARIDLADANIPYGDSESYRHMCRFYSGFFYKHPELQKYDYYWRIEPGIKFNCDINYDIFKYMQDNNKIYGFTLSLYE 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19112730   222 IGQTVPSLWNSTLEFIEKYPETLAKNNLWEWISDDNGKKFSHCHFWSNFEIADLDFFRSDSYRKYFDFLDKKGGFFYERW 301
Cdd:pfam01793 203 IEETIPTLWDSTLNFMKQNPEFIAKNNNRSWLSDDGGNTYNTCHFWSNFEIGDLDFFRSEAYEKYFEYLDSKGGFFYERW 282
                         250       260       270
                  ....*....|....*....|....*....|.
gi 19112730   302 GDAPVHSIALSLFLDRNKLHYFDEIGYSHAP 332
Cdd:pfam01793 283 GDAPVHSIAVSLFLPKDDIHFFRDIGYYHDP 313
 
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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