NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|398365365|ref|NP_014369|]
View 

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

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
6-499 7.55e-175

Mannosyltransferase [Carbohydrate transport and metabolism];


:

Pssm-ID: 227353  Cd Length: 399  Bit Score: 498.06  E-value: 7.55e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365   6 RTINAFLGCIHCNLTATCILIaFVITMYVVLVSEPASVDGTMG-NFLPFSKMDLATKRDRPFYSNCVNTQ-DYLLNPSYI 83
Cdd:COG5020    1 KKIRRFLLLIPRSVLYVLFLV-SLFAIYVFYVGEPSSIQSQDEpNELPSSEGDAIRNRDSKFSINCYNDElLYLEAPSYP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365  84 KQNASFVMLTRNGELEDVIKTINSIEEHFNQWFHYPYVFLNDQPFEEDFKAKVRDVTVGaLVEFGTIDEISWNFPSDVkD 163
Cdd:COG5020   80 RENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSG-LTEFGLIPKDEWNFPEWI-D 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 164 TFEFYNAIEDQGDRSILYGNLESYHKMCRFYSGLFYKHPLVQKYEWYWRLEPDVEFFCDITYDPFLEMLRTNKKYGFTII 243
Cdd:COG5020  158 EDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKDNNKVYGFVIS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 244 IPELYWTVPNLFRHTKSFISQKGVTL--GSLWKLFTKDYdifesddpelrdwinydfqakakisekiaieqllkkgddfq 321
Cdd:COG5020  238 LYEYEETIPTLWRTTKKFIKKNPGYLseNNLWKFISNDD----------------------------------------- 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 322 qinddkegimnlihkarsrkhivedkffNEEYNLCHFWSNFEIARLSVFDNDIYNSFFQYLEKSGGFWKERWGDAPVHSI 401
Cdd:COG5020  277 ----------------------------GIDYNLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVHSI 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 402 GLSLTLDLDDVHYFRDIGYRHSTIQHCPHNAmgneefsylasdskfkrknaaydegrEFGCGCRCRCPKKKrEIEDSMGF 481
Cdd:COG5020  329 AASLFLDKDQIHYFRDIGYHHSPFHHCPLNA--------------------------GTRLGCRCNCDPGK-DITDSSGS 381
                        490
                 ....*....|....*...
gi 398365365 482 CVNIWVNLLNQQRGHERH 499
Cdd:COG5020  382 CLGKWFNLLNGDKPEGWE 399
 
Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
6-499 7.55e-175

Mannosyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 227353  Cd Length: 399  Bit Score: 498.06  E-value: 7.55e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365   6 RTINAFLGCIHCNLTATCILIaFVITMYVVLVSEPASVDGTMG-NFLPFSKMDLATKRDRPFYSNCVNTQ-DYLLNPSYI 83
Cdd:COG5020    1 KKIRRFLLLIPRSVLYVLFLV-SLFAIYVFYVGEPSSIQSQDEpNELPSSEGDAIRNRDSKFSINCYNDElLYLEAPSYP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365  84 KQNASFVMLTRNGELEDVIKTINSIEEHFNQWFHYPYVFLNDQPFEEDFKAKVRDVTVGaLVEFGTIDEISWNFPSDVkD 163
Cdd:COG5020   80 RENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSG-LTEFGLIPKDEWNFPEWI-D 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 164 TFEFYNAIEDQGDRSILYGNLESYHKMCRFYSGLFYKHPLVQKYEWYWRLEPDVEFFCDITYDPFLEMLRTNKKYGFTII 243
Cdd:COG5020  158 EDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKDNNKVYGFVIS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 244 IPELYWTVPNLFRHTKSFISQKGVTL--GSLWKLFTKDYdifesddpelrdwinydfqakakisekiaieqllkkgddfq 321
Cdd:COG5020  238 LYEYEETIPTLWRTTKKFIKKNPGYLseNNLWKFISNDD----------------------------------------- 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 322 qinddkegimnlihkarsrkhivedkffNEEYNLCHFWSNFEIARLSVFDNDIYNSFFQYLEKSGGFWKERWGDAPVHSI 401
Cdd:COG5020  277 ----------------------------GIDYNLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVHSI 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 402 GLSLTLDLDDVHYFRDIGYRHSTIQHCPHNAmgneefsylasdskfkrknaaydegrEFGCGCRCRCPKKKrEIEDSMGF 481
Cdd:COG5020  329 AASLFLDKDQIHYFRDIGYHHSPFHHCPLNA--------------------------GTRLGCRCNCDPGK-DITDSSGS 381
                        490
                 ....*....|....*...
gi 398365365 482 CVNIWVNLLNQQRGHERH 499
Cdd:COG5020  382 CLGKWFNLLNGDKPEGWE 399
Glyco_transf_15 pfam01793
Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases ...
84-422 6.56e-94

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: 288.58  E-value: 6.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365   84 KQNASFVMLTRNGELEDVIKTINSIEEHFNQWFHYPYVFLNDQPFEEDFKAKVRDVtVGALVEFGTIDEISWNFPsDVKD 163
Cdd:pfam01793  42 EYNATILTLVRNSELRKILRSIKQVEKRFNKKFNYPYVFINDEPFTEKFKAKITKL-VSADVEFGTIPPEHWSYP-DFID 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365  164 TFEFYNAIEDQGDRSILYGNLESYHKMCRFYSGLFYKHPLVQKYEWYWRLEPDVEFFCDITYDPFLEMLRTNKKYGFTII 243
Cdd:pfam01793 120 STKAAKARIDLADANIPYGDSESYRHMCRFYSGFFYKHPELQKYDYYWRIEPGIKFNCDINYDIFKYMQDNNKIYGFTLS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365  244 IPELYWTVPNLFRHTKSFISQkgvtlgslwklftkdydifesddpelrdwiNYDFqakakisekiaieqllkkgddfqqi 323
Cdd:pfam01793 200 LYEIEETIPTLWDSTLNFMKQ------------------------------NPEF------------------------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365  324 nddkegimnlIHKARSRKHIVEDKffNEEYNLCHFWSNFEIARLSVFDNDIYNSFFQYLEKSGGFWKERWGDAPVHSIGL 403
Cdd:pfam01793 225 ----------IAKNNNRSWLSDDG--GNTYNTCHFWSNFEIGDLDFFRSEAYEKYFEYLDSKGGFFYERWGDAPVHSIAV 292
                         330
                  ....*....|....*....
gi 398365365  404 SLTLDLDDVHYFRDIGYRH 422
Cdd:pfam01793 293 SLFLPKDDIHFFRDIGYYH 311
 
Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
6-499 7.55e-175

Mannosyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 227353  Cd Length: 399  Bit Score: 498.06  E-value: 7.55e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365   6 RTINAFLGCIHCNLTATCILIaFVITMYVVLVSEPASVDGTMG-NFLPFSKMDLATKRDRPFYSNCVNTQ-DYLLNPSYI 83
Cdd:COG5020    1 KKIRRFLLLIPRSVLYVLFLV-SLFAIYVFYVGEPSSIQSQDEpNELPSSEGDAIRNRDSKFSINCYNDElLYLEAPSYP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365  84 KQNASFVMLTRNGELEDVIKTINSIEEHFNQWFHYPYVFLNDQPFEEDFKAKVRDVTVGaLVEFGTIDEISWNFPSDVkD 163
Cdd:COG5020   80 RENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSG-LTEFGLIPKDEWNFPEWI-D 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 164 TFEFYNAIEDQGDRSILYGNLESYHKMCRFYSGLFYKHPLVQKYEWYWRLEPDVEFFCDITYDPFLEMLRTNKKYGFTII 243
Cdd:COG5020  158 EDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKDNNKVYGFVIS 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 244 IPELYWTVPNLFRHTKSFISQKGVTL--GSLWKLFTKDYdifesddpelrdwinydfqakakisekiaieqllkkgddfq 321
Cdd:COG5020  238 LYEYEETIPTLWRTTKKFIKKNPGYLseNNLWKFISNDD----------------------------------------- 276
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 322 qinddkegimnlihkarsrkhivedkffNEEYNLCHFWSNFEIARLSVFDNDIYNSFFQYLEKSGGFWKERWGDAPVHSI 401
Cdd:COG5020  277 ----------------------------GIDYNLCHFWSNFEIANLDFFRSEAYRKYFDYLDKSGGFFYERWGDAPVHSI 328
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365 402 GLSLTLDLDDVHYFRDIGYRHSTIQHCPHNAmgneefsylasdskfkrknaaydegrEFGCGCRCRCPKKKrEIEDSMGF 481
Cdd:COG5020  329 AASLFLDKDQIHYFRDIGYHHSPFHHCPLNA--------------------------GTRLGCRCNCDPGK-DITDSSGS 381
                        490
                 ....*....|....*...
gi 398365365 482 CVNIWVNLLNQQRGHERH 499
Cdd:COG5020  382 CLGKWFNLLNGDKPEGWE 399
Glyco_transf_15 pfam01793
Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases ...
84-422 6.56e-94

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: 288.58  E-value: 6.56e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365   84 KQNASFVMLTRNGELEDVIKTINSIEEHFNQWFHYPYVFLNDQPFEEDFKAKVRDVtVGALVEFGTIDEISWNFPsDVKD 163
Cdd:pfam01793  42 EYNATILTLVRNSELRKILRSIKQVEKRFNKKFNYPYVFINDEPFTEKFKAKITKL-VSADVEFGTIPPEHWSYP-DFID 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365  164 TFEFYNAIEDQGDRSILYGNLESYHKMCRFYSGLFYKHPLVQKYEWYWRLEPDVEFFCDITYDPFLEMLRTNKKYGFTII 243
Cdd:pfam01793 120 STKAAKARIDLADANIPYGDSESYRHMCRFYSGFFYKHPELQKYDYYWRIEPGIKFNCDINYDIFKYMQDNNKIYGFTLS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365  244 IPELYWTVPNLFRHTKSFISQkgvtlgslwklftkdydifesddpelrdwiNYDFqakakisekiaieqllkkgddfqqi 323
Cdd:pfam01793 200 LYEIEETIPTLWDSTLNFMKQ------------------------------NPEF------------------------- 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365365  324 nddkegimnlIHKARSRKHIVEDKffNEEYNLCHFWSNFEIARLSVFDNDIYNSFFQYLEKSGGFWKERWGDAPVHSIGL 403
Cdd:pfam01793 225 ----------IAKNNNRSWLSDDG--GNTYNTCHFWSNFEIGDLDFFRSEAYEKYFEYLDSKGGFFYERWGDAPVHSIAV 292
                         330
                  ....*....|....*....
gi 398365365  404 SLTLDLDDVHYFRDIGYRH 422
Cdd:pfam01793 293 SLFLPKDDIHFFRDIGYYH 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH