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Conserved domains on  [gi|366988491|ref|XP_003674012|]
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hypothetical protein NCAS_0A10730 [Naumovozyma castellii]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
49-227 6.77e-63

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member pfam08660:

Pssm-ID: 471961  Cd Length: 171  Bit Score: 193.59  E-value: 6.77e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491   49 IFVFLGSGGHTGEMLRILQNYkETLLNQDNVLYVGYSDIDSRNKFSKLLQSACK--VEYIEFKKAREVNSGLLASLKSIF 126
Cdd:pfam08660   1 LLVVLGSGGHTGEMLRLLKTL-DKNLNIPRTYVVSSGDNMSLEKAKKFESSRGGrdSDFVRIPRAREVGQSYLSSIFTTL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491  127 LTLMTSLLNVIRIrksiafKPHLILLNGPGTCCILVLWFKLLEWILLfsSSSNIIYIESLARINSLSLTGKIVYWMADEF 206
Cdd:pfam08660  80 RSLLSSIFLVYRI------KPDVILCNGPGTCVPVCFAALLLKLLGL--KRSKIVYVESLARVKTLSLSGKLLYPFADRF 151
                         170       180
                  ....*....|....*....|.
gi 366988491  207 IVQWKELELScAPRAKYFGIL 227
Cdd:pfam08660 152 VVQWPDLADK-YPRAEYYGIL 171
 
Name Accession Description Interval E-value
Alg14 pfam08660
Oligosaccharide biosynthesis protein Alg14 like; Alg14 is involved dolichol-linked ...
49-227 6.77e-63

Oligosaccharide biosynthesis protein Alg14 like; Alg14 is involved dolichol-linked oligosaccharide biosynthesis and anchors the catalytic subunit Alg13 to the ER membrane.


Pssm-ID: 370045  Cd Length: 171  Bit Score: 193.59  E-value: 6.77e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491   49 IFVFLGSGGHTGEMLRILQNYkETLLNQDNVLYVGYSDIDSRNKFSKLLQSACK--VEYIEFKKAREVNSGLLASLKSIF 126
Cdd:pfam08660   1 LLVVLGSGGHTGEMLRLLKTL-DKNLNIPRTYVVSSGDNMSLEKAKKFESSRGGrdSDFVRIPRAREVGQSYLSSIFTTL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491  127 LTLMTSLLNVIRIrksiafKPHLILLNGPGTCCILVLWFKLLEWILLfsSSSNIIYIESLARINSLSLTGKIVYWMADEF 206
Cdd:pfam08660  80 RSLLSSIFLVYRI------KPDVILCNGPGTCVPVCFAALLLKLLGL--KRSKIVYVESLARVKTLSLSGKLLYPFADRF 151
                         170       180
                  ....*....|....*....|.
gi 366988491  207 IVQWKELELScAPRAKYFGIL 227
Cdd:pfam08660 152 VVQWPDLADK-YPRAEYYGIL 171
PssD NF041549
PssD/Cps14F family polysaccharide biosynthesis glycosyltransferase;
49-227 9.95e-26

PssD/Cps14F family polysaccharide biosynthesis glycosyltransferase;


Pssm-ID: 469434 [Multi-domain]  Cd Length: 151  Bit Score: 97.58  E-value: 9.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491  49 IFVFlGSGGHTGEMLRILQNYKetllNQDNVLYVGYSDIDSRNKFSKllqsackVEYIEFKKAREVNSGLlaslkSIFLT 128
Cdd:NF041549   1 LLIY-GSGGHLAQMLRLKPLLD----KYDYFLVTEKSDSTKKLEWSY-------DVHYLLPESRNKNNGL-----KYLFK 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491 129 LMTSLLNVIRIRKSIafKPHLILLNGPGTCCILVLWFKLLewillfssSSNIIYIESLARINSLSLTGKIVYWMADEFIV 208
Cdd:NF041549  64 FLKNIIKSFKILRKY--RPDVVISTGPGIAIPMCLLAKLF--------GKKVIYIETWSRFTSKSLTGKIMYKIADKFYV 133
                        170
                 ....*....|....*....
gi 366988491 209 QWKELeLSCAPRAKYFGIL 227
Cdd:NF041549 134 QWEEL-LKLYPKAIYGGRL 151
 
Name Accession Description Interval E-value
Alg14 pfam08660
Oligosaccharide biosynthesis protein Alg14 like; Alg14 is involved dolichol-linked ...
49-227 6.77e-63

Oligosaccharide biosynthesis protein Alg14 like; Alg14 is involved dolichol-linked oligosaccharide biosynthesis and anchors the catalytic subunit Alg13 to the ER membrane.


Pssm-ID: 370045  Cd Length: 171  Bit Score: 193.59  E-value: 6.77e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491   49 IFVFLGSGGHTGEMLRILQNYkETLLNQDNVLYVGYSDIDSRNKFSKLLQSACK--VEYIEFKKAREVNSGLLASLKSIF 126
Cdd:pfam08660   1 LLVVLGSGGHTGEMLRLLKTL-DKNLNIPRTYVVSSGDNMSLEKAKKFESSRGGrdSDFVRIPRAREVGQSYLSSIFTTL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491  127 LTLMTSLLNVIRIrksiafKPHLILLNGPGTCCILVLWFKLLEWILLfsSSSNIIYIESLARINSLSLTGKIVYWMADEF 206
Cdd:pfam08660  80 RSLLSSIFLVYRI------KPDVILCNGPGTCVPVCFAALLLKLLGL--KRSKIVYVESLARVKTLSLSGKLLYPFADRF 151
                         170       180
                  ....*....|....*....|.
gi 366988491  207 IVQWKELELScAPRAKYFGIL 227
Cdd:pfam08660 152 VVQWPDLADK-YPRAEYYGIL 171
PssD NF041549
PssD/Cps14F family polysaccharide biosynthesis glycosyltransferase;
49-227 9.95e-26

PssD/Cps14F family polysaccharide biosynthesis glycosyltransferase;


Pssm-ID: 469434 [Multi-domain]  Cd Length: 151  Bit Score: 97.58  E-value: 9.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491  49 IFVFlGSGGHTGEMLRILQNYKetllNQDNVLYVGYSDIDSRNKFSKllqsackVEYIEFKKAREVNSGLlaslkSIFLT 128
Cdd:NF041549   1 LLIY-GSGGHLAQMLRLKPLLD----KYDYFLVTEKSDSTKKLEWSY-------DVHYLLPESRNKNNGL-----KYLFK 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 366988491 129 LMTSLLNVIRIRKSIafKPHLILLNGPGTCCILVLWFKLLewillfssSSNIIYIESLARINSLSLTGKIVYWMADEFIV 208
Cdd:NF041549  64 FLKNIIKSFKILRKY--RPDVVISTGPGIAIPMCLLAKLF--------GKKVIYIETWSRFTSKSLTGKIMYKIADKFYV 133
                        170
                 ....*....|....*....
gi 366988491 209 QWKELeLSCAPRAKYFGIL 227
Cdd:NF041549 134 QWEEL-LKLYPKAIYGGRL 151
 
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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