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Conserved domains on  [gi|398365497|ref|NP_009764|]
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mannosyltransferase KTR3 [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];
1-404 0e+00

Mannosyltransferase [Carbohydrate transport and metabolism];


:

Pssm-ID: 227353  Cd Length: 399  Bit Score: 572.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497   1 MSVHHKKKLMPKSALLIRkyqkgirssfiGLIIVLSFLFFMSGSRSP--------EVPIAQGTSVSRVASKDYLMPFTDK 72
Cdd:COG5020    1 KKIRRFLLLIPRSVLYVL-----------FLVSLFAIYVFYVGEPSSiqsqdepnELPSSEGDAIRNRDSKFSINCYNDE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497  73 SQGVIHPVDDgkKEKGVMVTLARNSDLWNLVKSIRHVEDRFNNRYHYDWVFLNDQPFSDEFKRVTSALVSGKAKYGTIPK 152
Cdd:COG5020   70 LLYLEAPSYP--RENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLTEFGLIPK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497 153 DHWSIPSWIDTEKFDEKRLAMGKLDIPYGSSVPYRHMCRFQSGFIWRHPLLEEYEWFWRVDTDITLFCDIQYDIFKFLKV 232
Cdd:COG5020  148 DEWNFPEWIDEDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKD 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497 233 NNKKYGFILSVSEYERTIPTLWETTKKFIKKNPKFLHKNNLMKFISNDDGDTYNMCHFWTNFEIGSLDFFRSDAYREYFD 312
Cdd:COG5020  228 NNKVYGFVISLYEYEETIPTLWRTTKKFIKKNPGYLSENNLWKFISNDDGIDYNLCHFWSNFEIANLDFFRSEAYRKYFD 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497 313 YLDSSGGFFYERWGDAPVHSIAASLFLDKSEIHFFDGLGFHHPDFTSCPIEQKIRLQNKCICEPSKDVTWTPdYFCTRKY 392
Cdd:COG5020  308 YLDKSGGFFYERWGDAPVHSIAASLFLDKDQIHYFRDIGYHHSPFHHCPLNAGTRLGCRCNCDPGKDITDSS-GSCLGKW 386
                        410
                 ....*....|..
gi 398365497 393 FSAGNYKLPPGI 404
Cdd:COG5020  387 FNLLNGDKPEGW 398
 
Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
1-404 0e+00

Mannosyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 227353  Cd Length: 399  Bit Score: 572.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497   1 MSVHHKKKLMPKSALLIRkyqkgirssfiGLIIVLSFLFFMSGSRSP--------EVPIAQGTSVSRVASKDYLMPFTDK 72
Cdd:COG5020    1 KKIRRFLLLIPRSVLYVL-----------FLVSLFAIYVFYVGEPSSiqsqdepnELPSSEGDAIRNRDSKFSINCYNDE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497  73 SQGVIHPVDDgkKEKGVMVTLARNSDLWNLVKSIRHVEDRFNNRYHYDWVFLNDQPFSDEFKRVTSALVSGKAKYGTIPK 152
Cdd:COG5020   70 LLYLEAPSYP--RENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLTEFGLIPK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497 153 DHWSIPSWIDTEKFDEKRLAMGKLDIPYGSSVPYRHMCRFQSGFIWRHPLLEEYEWFWRVDTDITLFCDIQYDIFKFLKV 232
Cdd:COG5020  148 DEWNFPEWIDEDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKD 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497 233 NNKKYGFILSVSEYERTIPTLWETTKKFIKKNPKFLHKNNLMKFISNDDGDTYNMCHFWTNFEIGSLDFFRSDAYREYFD 312
Cdd:COG5020  228 NNKVYGFVISLYEYEETIPTLWRTTKKFIKKNPGYLSENNLWKFISNDDGIDYNLCHFWSNFEIANLDFFRSEAYRKYFD 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497 313 YLDSSGGFFYERWGDAPVHSIAASLFLDKSEIHFFDGLGFHHPDFTSCPIEQKIRLQNKCICEPSKDVTWTPdYFCTRKY 392
Cdd:COG5020  308 YLDKSGGFFYERWGDAPVHSIAASLFLDKDQIHYFRDIGYHHSPFHHCPLNAGTRLGCRCNCDPGKDITDSS-GSCLGKW 386
                        410
                 ....*....|..
gi 398365497 393 FSAGNYKLPPGI 404
Cdd:COG5020  387 FNLLNGDKPEGW 398
Glyco_transf_15 pfam01793
Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases ...
68-355 8.27e-142

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: 406.45  E-value: 8.27e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497   68 PFTDKSQGVIHPVD-DGKKEKGVMVTLARNSDLWNLVKSIRHVEDRFNNRYHYDWVFLNDQPFSDEFKRVTSALVSGKAK 146
Cdd:pfam01793  24 ANLPKSASGRKPMPnDENEYNATILTLVRNSELRKILRSIKQVEKRFNKKFNYPYVFINDEPFTEKFKAKITKLVSADVE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497  147 YGTIPKDHWSIPSWIDTEKFDEKRLAMGKLDIPYGSSVPYRHMCRFQSGFIWRHPLLEEYEWFWRVDTDITLFCDIQYDI 226
Cdd:pfam01793 104 FGTIPPEHWSYPDFIDSTKAAKARIDLADANIPYGDSESYRHMCRFYSGFFYKHPELQKYDYYWRIEPGIKFNCDINYDI 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497  227 FKFLKVNNKKYGFILSVSEYERTIPTLWETTKKFIKKNPKFLHKNNLMKFISNDDGDTYNMCHFWTNFEIGSLDFFRSDA 306
Cdd:pfam01793 184 FKYMQDNNKIYGFTLSLYEIEETIPTLWDSTLNFMKQNPEFIAKNNNRSWLSDDGGNTYNTCHFWSNFEIGDLDFFRSEA 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 398365497  307 YREYFDYLDSSGGFFYERWGDAPVHSIAASLFLDKSEIHFFDGLG-FHHP 355
Cdd:pfam01793 264 YEKYFEYLDSKGGFFYERWGDAPVHSIAVSLFLPKDDIHFFRDIGyYHDP 313
 
Name Accession Description Interval E-value
KTR1 COG5020
Mannosyltransferase [Carbohydrate transport and metabolism];
1-404 0e+00

Mannosyltransferase [Carbohydrate transport and metabolism];


Pssm-ID: 227353  Cd Length: 399  Bit Score: 572.40  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497   1 MSVHHKKKLMPKSALLIRkyqkgirssfiGLIIVLSFLFFMSGSRSP--------EVPIAQGTSVSRVASKDYLMPFTDK 72
Cdd:COG5020    1 KKIRRFLLLIPRSVLYVL-----------FLVSLFAIYVFYVGEPSSiqsqdepnELPSSEGDAIRNRDSKFSINCYNDE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497  73 SQGVIHPVDDgkKEKGVMVTLARNSDLWNLVKSIRHVEDRFNNRYHYDWVFLNDQPFSDEFKRVTSALVSGKAKYGTIPK 152
Cdd:COG5020   70 LLYLEAPSYP--RENATFVMLARNSDLEDVLSSIRSVEDRFNKNFHYPWVFLNDEPFTEEFKEATSDITSGLTEFGLIPK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497 153 DHWSIPSWIDTEKFDEKRLAMGKLDIPYGSSVPYRHMCRFQSGFIWRHPLLEEYEWFWRVDTDITLFCDIQYDIFKFLKV 232
Cdd:COG5020  148 DEWNFPEWIDEDKAAESLDDMADEGILYGGSESYRHMCRFFSGFFYRHPLLDEYDYYWRVEPDVKLYCDIDYDPFRYMKD 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497 233 NNKKYGFILSVSEYERTIPTLWETTKKFIKKNPKFLHKNNLMKFISNDDGDTYNMCHFWTNFEIGSLDFFRSDAYREYFD 312
Cdd:COG5020  228 NNKVYGFVISLYEYEETIPTLWRTTKKFIKKNPGYLSENNLWKFISNDDGIDYNLCHFWSNFEIANLDFFRSEAYRKYFD 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497 313 YLDSSGGFFYERWGDAPVHSIAASLFLDKSEIHFFDGLGFHHPDFTSCPIEQKIRLQNKCICEPSKDVTWTPdYFCTRKY 392
Cdd:COG5020  308 YLDKSGGFFYERWGDAPVHSIAASLFLDKDQIHYFRDIGYHHSPFHHCPLNAGTRLGCRCNCDPGKDITDSS-GSCLGKW 386
                        410
                 ....*....|..
gi 398365497 393 FSAGNYKLPPGI 404
Cdd:COG5020  387 FNLLNGDKPEGW 398
Glyco_transf_15 pfam01793
Glycolipid 2-alpha-mannosyltransferase; This is a family of alpha-1,2 mannosyl-transferases ...
68-355 8.27e-142

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: 406.45  E-value: 8.27e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497   68 PFTDKSQGVIHPVD-DGKKEKGVMVTLARNSDLWNLVKSIRHVEDRFNNRYHYDWVFLNDQPFSDEFKRVTSALVSGKAK 146
Cdd:pfam01793  24 ANLPKSASGRKPMPnDENEYNATILTLVRNSELRKILRSIKQVEKRFNKKFNYPYVFINDEPFTEKFKAKITKLVSADVE 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497  147 YGTIPKDHWSIPSWIDTEKFDEKRLAMGKLDIPYGSSVPYRHMCRFQSGFIWRHPLLEEYEWFWRVDTDITLFCDIQYDI 226
Cdd:pfam01793 104 FGTIPPEHWSYPDFIDSTKAAKARIDLADANIPYGDSESYRHMCRFYSGFFYKHPELQKYDYYWRIEPGIKFNCDINYDI 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398365497  227 FKFLKVNNKKYGFILSVSEYERTIPTLWETTKKFIKKNPKFLHKNNLMKFISNDDGDTYNMCHFWTNFEIGSLDFFRSDA 306
Cdd:pfam01793 184 FKYMQDNNKIYGFTLSLYEIEETIPTLWDSTLNFMKQNPEFIAKNNNRSWLSDDGGNTYNTCHFWSNFEIGDLDFFRSEA 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 398365497  307 YREYFDYLDSSGGFFYERWGDAPVHSIAASLFLDKSEIHFFDGLG-FHHP 355
Cdd:pfam01793 264 YEKYFEYLDSKGGFFYERWGDAPVHSIAVSLFLPKDDIHFFRDIGyYHDP 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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