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Conserved domains on  [gi|398364323|ref|NP_012181|]
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putative mannosyltransferase [Saccharomyces cerevisiae S288C]

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];
7-490 1.26e-180

Mannosyltransferase [Carbohydrate transport and metabolism];


:

Pssm-ID: 227353  Cd Length: 399  Bit Score: 512.70  E-value: 1.26e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323   7 PKVRRFLLDKCRQKRYGfLFLGCIFAILYCMGTWPFFAKDIvHDPNNLPYSLQDYSTDKDEPFFRGCTDTK-LYLQNPAY 85
Cdd:COG5020    1 KKIRRFLLLIPRSVLYV-LFLVSLFAIYVFYVGEPSSIQSQ-DEPNELPSSEGDAIRNRDSKFSINCYNDElLYLEAPSY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323  86 SKMNASFVMLTRNEEIEDVLKTMRSIEGHFNKWFKYPYVFLNDDPFTDHFKDQIQAATNATVEFGTVDEIMWEFPAKVrN 165
Cdd:COG5020   79 PRENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLTEFGLIPKDEWNFPEWI-D 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 166 SLQFKASLEDQNDRGIMYGNMESYHKMCRFYSGIFYKHPLVSKYEWYWRIEPDVDFFCDISYDPFFEMAKHNKKYGFTVL 245
Cdd:COG5020  158 EDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKDNNKVYGFVIS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 246 ITELYWTVPNLFRTTKSFIKKTAGLKENlGTLWKLFTFNynildtddeeisrwvnfpwdakpklteklmvdfllenhgqv 325
Cdd:COG5020  238 LYEYEETIPTLWRTTKKFIKKNPGYLSE-NNLWKFISND----------------------------------------- 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 326 nneedlegiqylverarskvpmledslEGEDYNLCHFWSNFEIARVDLFDNEIYNAYFKFLEESGGFWTERWGDAPIHSI 405
Cdd:COG5020  276 ---------------------------DGIDYNLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVHSI 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 406 GLGMTLDLEDVHYFRDIGYRHSSLQHCPKNAlqsqenlntfdeGYNFGCGCRCvcpKKGEDIEDHSTPCMDIFFELLHGR 485
Cdd:COG5020  329 AASLFLDKDQIHYFRDIGYHHSPFHHCPLNA------------GTRLGCRCNC---DPGKDITDSSGSCLGKWFNLLNGD 393

                 ....*
gi 398364323 486 EYEKE 490
Cdd:COG5020  394 KPEGW 398
 
Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
7-490 1.26e-180

Mannosyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 227353  Cd Length: 399  Bit Score: 512.70  E-value: 1.26e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323   7 PKVRRFLLDKCRQKRYGfLFLGCIFAILYCMGTWPFFAKDIvHDPNNLPYSLQDYSTDKDEPFFRGCTDTK-LYLQNPAY 85
Cdd:COG5020    1 KKIRRFLLLIPRSVLYV-LFLVSLFAIYVFYVGEPSSIQSQ-DEPNELPSSEGDAIRNRDSKFSINCYNDElLYLEAPSY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323  86 SKMNASFVMLTRNEEIEDVLKTMRSIEGHFNKWFKYPYVFLNDDPFTDHFKDQIQAATNATVEFGTVDEIMWEFPAKVrN 165
Cdd:COG5020   79 PRENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLTEFGLIPKDEWNFPEWI-D 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 166 SLQFKASLEDQNDRGIMYGNMESYHKMCRFYSGIFYKHPLVSKYEWYWRIEPDVDFFCDISYDPFFEMAKHNKKYGFTVL 245
Cdd:COG5020  158 EDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKDNNKVYGFVIS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 246 ITELYWTVPNLFRTTKSFIKKTAGLKENlGTLWKLFTFNynildtddeeisrwvnfpwdakpklteklmvdfllenhgqv 325
Cdd:COG5020  238 LYEYEETIPTLWRTTKKFIKKNPGYLSE-NNLWKFISND----------------------------------------- 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 326 nneedlegiqylverarskvpmledslEGEDYNLCHFWSNFEIARVDLFDNEIYNAYFKFLEESGGFWTERWGDAPIHSI 405
Cdd:COG5020  276 ---------------------------DGIDYNLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVHSI 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 406 GLGMTLDLEDVHYFRDIGYRHSSLQHCPKNAlqsqenlntfdeGYNFGCGCRCvcpKKGEDIEDHSTPCMDIFFELLHGR 485
Cdd:COG5020  329 AASLFLDKDQIHYFRDIGYHHSPFHHCPLNA------------GTRLGCRCNC---DPGKDITDSSGSCLGKWFNLLNGD 393

                 ....*
gi 398364323 486 EYEKE 490
Cdd:COG5020  394 KPEGW 398
Glyco_transf_15 pfam01793
Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases ...
86-426 5.99e-90

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: 278.18  E-value: 5.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323   86 SKMNASFVMLTRNEEIEDVLKTMRSIEGHFNKWFKYPYVFLNDDPFTDHFKDQIQAATNATVEFGTVDEIMWEFPAKVrN 165
Cdd:pfam01793  41 NEYNATILTLVRNSELRKILRSIKQVEKRFNKKFNYPYVFINDEPFTEKFKAKITKLVSADVEFGTIPPEHWSYPDFI-D 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323  166 SLQFKASLEDQNDRGIMYGNMESYHKMCRFYSGIFYKHPLVSKYEWYWRIEPDVDFFCDISYDPFFEMAKHNKKYGFTVL 245
Cdd:pfam01793 120 STKAAKARIDLADANIPYGDSESYRHMCRFYSGFFYKHPELQKYDYYWRIEPGIKFNCDINYDIFKYMQDNNKIYGFTLS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323  246 ITELYWTVPNLFRTTKSFIKKtaglkenlgtlwklftfNYnildtddEEISRWVNFPWdakpklteklmvdfllenhgqv 325
Cdd:pfam01793 200 LYEIEETIPTLWDSTLNFMKQ-----------------NP-------EFIAKNNNRSW---------------------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323  326 nneedlegiqylverarskvpmLEDSLeGEDYNLCHFWSNFEIARVDLFDNEIYNAYFKFLEESGGFWTERWGDAPIHSI 405
Cdd:pfam01793 234 ----------------------LSDDG-GNTYNTCHFWSNFEIGDLDFFRSEAYEKYFEYLDSKGGFFYERWGDAPVHSI 290
                         330       340
                  ....*....|....*....|.
gi 398364323  406 GLGMTLDLEDVHYFRDIGYRH 426
Cdd:pfam01793 291 AVSLFLPKDDIHFFRDIGYYH 311
 
Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
7-490 1.26e-180

Mannosyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 227353  Cd Length: 399  Bit Score: 512.70  E-value: 1.26e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323   7 PKVRRFLLDKCRQKRYGfLFLGCIFAILYCMGTWPFFAKDIvHDPNNLPYSLQDYSTDKDEPFFRGCTDTK-LYLQNPAY 85
Cdd:COG5020    1 KKIRRFLLLIPRSVLYV-LFLVSLFAIYVFYVGEPSSIQSQ-DEPNELPSSEGDAIRNRDSKFSINCYNDElLYLEAPSY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323  86 SKMNASFVMLTRNEEIEDVLKTMRSIEGHFNKWFKYPYVFLNDDPFTDHFKDQIQAATNATVEFGTVDEIMWEFPAKVrN 165
Cdd:COG5020   79 PRENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLTEFGLIPKDEWNFPEWI-D 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 166 SLQFKASLEDQNDRGIMYGNMESYHKMCRFYSGIFYKHPLVSKYEWYWRIEPDVDFFCDISYDPFFEMAKHNKKYGFTVL 245
Cdd:COG5020  158 EDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKDNNKVYGFVIS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 246 ITELYWTVPNLFRTTKSFIKKTAGLKENlGTLWKLFTFNynildtddeeisrwvnfpwdakpklteklmvdfllenhgqv 325
Cdd:COG5020  238 LYEYEETIPTLWRTTKKFIKKNPGYLSE-NNLWKFISND----------------------------------------- 275
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 326 nneedlegiqylverarskvpmledslEGEDYNLCHFWSNFEIARVDLFDNEIYNAYFKFLEESGGFWTERWGDAPIHSI 405
Cdd:COG5020  276 ---------------------------DGIDYNLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVHSI 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323 406 GLGMTLDLEDVHYFRDIGYRHSSLQHCPKNAlqsqenlntfdeGYNFGCGCRCvcpKKGEDIEDHSTPCMDIFFELLHGR 485
Cdd:COG5020  329 AASLFLDKDQIHYFRDIGYHHSPFHHCPLNA------------GTRLGCRCNC---DPGKDITDSSGSCLGKWFNLLNGD 393

                 ....*
gi 398364323 486 EYEKE 490
Cdd:COG5020  394 KPEGW 398
Glyco_transf_15 pfam01793
Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases ...
86-426 5.99e-90

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: 278.18  E-value: 5.99e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323   86 SKMNASFVMLTRNEEIEDVLKTMRSIEGHFNKWFKYPYVFLNDDPFTDHFKDQIQAATNATVEFGTVDEIMWEFPAKVrN 165
Cdd:pfam01793  41 NEYNATILTLVRNSELRKILRSIKQVEKRFNKKFNYPYVFINDEPFTEKFKAKITKLVSADVEFGTIPPEHWSYPDFI-D 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323  166 SLQFKASLEDQNDRGIMYGNMESYHKMCRFYSGIFYKHPLVSKYEWYWRIEPDVDFFCDISYDPFFEMAKHNKKYGFTVL 245
Cdd:pfam01793 120 STKAAKARIDLADANIPYGDSESYRHMCRFYSGFFYKHPELQKYDYYWRIEPGIKFNCDINYDIFKYMQDNNKIYGFTLS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323  246 ITELYWTVPNLFRTTKSFIKKtaglkenlgtlwklftfNYnildtddEEISRWVNFPWdakpklteklmvdfllenhgqv 325
Cdd:pfam01793 200 LYEIEETIPTLWDSTLNFMKQ-----------------NP-------EFIAKNNNRSW---------------------- 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364323  326 nneedlegiqylverarskvpmLEDSLeGEDYNLCHFWSNFEIARVDLFDNEIYNAYFKFLEESGGFWTERWGDAPIHSI 405
Cdd:pfam01793 234 ----------------------LSDDG-GNTYNTCHFWSNFEIGDLDFFRSEAYEKYFEYLDSKGGFFYERWGDAPVHSI 290
                         330       340
                  ....*....|....*....|.
gi 398364323  406 GLGMTLDLEDVHYFRDIGYRH 426
Cdd:pfam01793 291 AVSLFLPKDDIHFFRDIGYYH 311
 
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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