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Conserved domains on  [gi|62955097|ref|NP_001017560|]
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tRNA-queuosine alpha-mannosyltransferase [Danio rerio]

Protein Classification

DUF3524 and Glycosyltransferase_GTB_type domain-containing protein( domain architecture ID 10572306)

DUF3524 and Glycosyltransferase_GTB_type domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 7.77e-93

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


:

Pssm-ID: 432280  Cd Length: 165  Bit Score: 277.13  E-value: 7.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097     2 SVLLLEAFYGGSHKQLLDLLKESV-EDCVSFTLPAKKWHWRARTSALYFMQAVLANSSY-RVLFTSSVLNLAELVALRPD 79
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSpHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097    80 LGHLKKVLYFHENQLVYPVRKSQERDFQYGYNQILSCLVADVVVFNSSFNMESFLSSISTFMKTMPDHRPKDLERLIRPK 159
Cdd:pfam12038  81 LANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRAK 160


                  ....*
gi 62955097   160 CHVLH 164
Cdd:pfam12038 161 SRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 167-368 4.38e-16

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.


:

Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 77.44  E-value: 4.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 167 IRFPDVTRFLPAHKRLRH---PVRCDDIHAPAAKSHIqtsspssypdveppekMLNVAGTNQSHEPTSVTPHQETASPLC 243
Cdd:cd01635  31 HEVTVLALLLLALRRILKkllELKPDVVHAHSPHAAA----------------LAALLAARLLGIPIVVTVHGPDSLEST 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 244 GHEGEKLRPLHI-------VWPHRWEHDKDPQLFFQTLLKLKDRQLSFEVSVLGETFTDVPDIFSEAKEQLVDHIQHWGF 316
Cdd:cd01635  95 RSELLALARLLVslpladkVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGG 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 62955097 317 MPSKEDYLKVLCQADVVVSTAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIF 368
Cdd:cd01635 175 LVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 327-420 7.07e-07

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 48.06  E-value: 7.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 327 LCQADVVVSTAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIFP--ATYLY---STPEQLCKRLQEFCKRPQLAR---QHV 398
Cdd:COG0438  18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEdgETGLLvppGDPEALAEAILRLLEDPELRRrlgEAA 97

                        90       100
                ....*....|....*....|..
gi 62955097 399 VQVSLSSFSWDSLGDNFRSLLK 420
Cdd:COG0438  98 RERAEERFSWEAIAERLLALYE 119
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 7.77e-93

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 277.13  E-value: 7.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097     2 SVLLLEAFYGGSHKQLLDLLKESV-EDCVSFTLPAKKWHWRARTSALYFMQAVLANSSY-RVLFTSSVLNLAELVALRPD 79
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSpHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097    80 LGHLKKVLYFHENQLVYPVRKSQERDFQYGYNQILSCLVADVVVFNSSFNMESFLSSISTFMKTMPDHRPKDLERLIRPK 159
Cdd:pfam12038  81 LANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRAK 160


                  ....*
gi 62955097   160 CHVLH 164
Cdd:pfam12038 161 SRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 167-368 4.38e-16

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.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 77.44  E-value: 4.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 167 IRFPDVTRFLPAHKRLRH---PVRCDDIHAPAAKSHIqtsspssypdveppekMLNVAGTNQSHEPTSVTPHQETASPLC 243
Cdd:cd01635  31 HEVTVLALLLLALRRILKkllELKPDVVHAHSPHAAA----------------LAALLAARLLGIPIVVTVHGPDSLEST 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 244 GHEGEKLRPLHI-------VWPHRWEHDKDPQLFFQTLLKLKDRQLSFEVSVLGETFTDVPDIFSEAKEQLVDHIQHWGF 316
Cdd:cd01635  95 RSELLALARLLVslpladkVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGG 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 62955097 317 MPSKEDYLKVLCQADVVVSTAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIF 368
Cdd:cd01635 175 LVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 327-420 7.07e-07

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 48.06  E-value: 7.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 327 LCQADVVVSTAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIFP--ATYLY---STPEQLCKRLQEFCKRPQLAR---QHV 398
Cdd:COG0438  18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEdgETGLLvppGDPEALAEAILRLLEDPELRRrlgEAA 97

                        90       100
                ....*....|....*....|..
gi 62955097 399 VQVSLSSFSWDSLGDNFRSLLK 420
Cdd:COG0438  98 RERAEERFSWEAIAERLLALYE 119
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
261-354 1.72e-03

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 38.65  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097   261 WEHDKDPQLFFQTLLKLKDRQLSFEVSVLGEtftDVPDIFSEAKEQLVDHIQHWGFMPSKEDYLKvlcQADVVVSTAKHE 340
Cdd:pfam13692  11 HPNVKGVDYLLEAVPLLRKRDNDVRLVIVGD---GPEEELEELAAGLEDRVIFTGFVEDLAELLA---AADVFVLPSLYE 84

                          90
                  ....*....|....
gi 62955097   341 FFGVAMLEAVHCGC 354
Cdd:pfam13692  85 GFGLKLLEAMAAGL 98
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 7.77e-93

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 277.13  E-value: 7.77e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097     2 SVLLLEAFYGGSHKQLLDLLKESV-EDCVSFTLPAKKWHWRARTSALYFMQAVLANSSY-RVLFTSSVLNLAELVALRPD 79
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSpHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097    80 LGHLKKVLYFHENQLVYPVRKSQERDFQYGYNQILSCLVADVVVFNSSFNMESFLSSISTFMKTMPDHRPKDLERLIRPK 159
Cdd:pfam12038  81 LANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRAK 160


                  ....*
gi 62955097   160 CHVLH 164
Cdd:pfam12038 161 SRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 167-368 4.38e-16

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.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 77.44  E-value: 4.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 167 IRFPDVTRFLPAHKRLRH---PVRCDDIHAPAAKSHIqtsspssypdveppekMLNVAGTNQSHEPTSVTPHQETASPLC 243
Cdd:cd01635  31 HEVTVLALLLLALRRILKkllELKPDVVHAHSPHAAA----------------LAALLAARLLGIPIVVTVHGPDSLEST 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 244 GHEGEKLRPLHI-------VWPHRWEHDKDPQLFFQTLLKLKDRQLSFEVSVLGETFTDVPDIFSEAKEQLVDHIQHWGF 316
Cdd:cd01635  95 RSELLALARLLVslpladkVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGG 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 62955097 317 MPSKEDYLKVLCQADVVVSTAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIF 368
Cdd:cd01635 175 LVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 255-420 1.29e-08

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). 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. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the 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 members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 56.39  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 255 IVWPHRWEHDKDPQLFFQTLLKLKDRQLSFEVSVLGETftdvPDIFSEAKEQ---LVDHIQHWGFMPsKEDYLKVLCQAD 331
Cdd:cd03801 195 LLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGD----GPLRAELEELelgLGDRVRFLGFVP-DEELPALYAAAD 269

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 332 VVVSTAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIFPATYLY-----STPEQLCKRLQEFCKRPQL-------ARQHVV 399
Cdd:cd03801 270 VFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGlvvppDDVEALADALLRLLADPELrarlgraARERVA 349

                       170       180
                ....*....|....*....|.
gi 62955097 400 QvslsSFSWDSLGDNFRSLLK 420
Cdd:cd03801 350 E----RFSWERVAERLLDLYR 366
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 263-354 2.57e-07

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 52.21  E-value: 2.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 263 HDKDPQLFFQTLLKLKDRQLSFEVSVLGETFTDVPDIFSEAKEQLVDHIQHWGFMpskEDYLKVLCQADVVVSTAKHEFF 342
Cdd:cd03808 200 KDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFR---SDVPELLAESDVFVLPSYREGL 276

                        90
                ....*....|..
gi 62955097 343 GVAMLEAVHCGC 354
Cdd:cd03808 277 PRSLLEAMAAGR 288
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 327-420 7.07e-07

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 48.06  E-value: 7.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 327 LCQADVVVSTAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIFP--ATYLY---STPEQLCKRLQEFCKRPQLAR---QHV 398
Cdd:COG0438  18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEdgETGLLvppGDPEALAEAILRLLEDPELRRrlgEAA 97

                        90       100
                ....*....|....*....|..
gi 62955097 399 VQVSLSSFSWDSLGDNFRSLLK 420
Cdd:COG0438  98 RERAEERFSWEAIAERLLALYE 119
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 257-409 3.79e-04

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 42.35  E-value: 3.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 257 WPHrwehdKDPQLFFQTLLKLKDRQLSFEVSVLGETFTDVPDIFSEAKE-QLVDHIQHWGFMPsKEDYLKVLCQADVVVS 335
Cdd:cd03809 202 EPR-----KNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKlGLGGRVRFLGYVS-DEDLPALYRGARAFVF 275

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62955097 336 TAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIFPATYLY---STPEQLCKRLQEFCKRPQLARQHVV--QVSLSSFSWD 409
Cdd:cd03809 276 PSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYfdpLDPESIADAILRLLEDPSLREELIRkgLERAKKFSWE 354
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 251-354 4.20e-04

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 42.34  E-value: 4.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097 251 RPLHIVWPHRWEHDKDPQLFFQTLLKLKDrQLSFEVSVLGetftDVP--DIFSEAKEQ--LVDHIQHWGFmpsKEDYLKV 326
Cdd:cd03819 181 GKPVVGYVGRLSPEKGWLLLVDAAAELKD-EPDFRLLVAG----DGPerDEIRRLVERlgLRDRVTFTGF---REDVPAA 252

                        90       100
                ....*....|....*....|....*...
gi 62955097 327 LCQADVVVSTAKHEFFGVAMLEAVHCGC 354
Cdd:cd03819 253 LAASDVVVLPSLHEEFGRVALEAMACGT 280
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
261-354 1.72e-03

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 38.65  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097   261 WEHDKDPQLFFQTLLKLKDRQLSFEVSVLGEtftDVPDIFSEAKEQLVDHIQHWGFMPSKEDYLKvlcQADVVVSTAKHE 340
Cdd:pfam13692  11 HPNVKGVDYLLEAVPLLRKRDNDVRLVIVGD---GPEEELEELAAGLEDRVIFTGFVEDLAELLA---AADVFVLPSLYE 84

                          90
                  ....*....|....
gi 62955097   341 FFGVAMLEAVHCGC 354
Cdd:pfam13692  85 GFGLKLLEAMAAGL 98
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 255-368 2.25e-03

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 38.41  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62955097   255 IVWPHRWEHDKDPQLFFQTLLKLKDRQLSFEVSVLGETFTDVPDIFSEAKEQLVDHIQHWGFMPSKE--DYLKvlcQADV 332
Cdd:pfam00534   5 ILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDlpELLK---IADV 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 62955097   333 VVSTAKHEFFGVAMLEAVHCGCYPLCPKALVYPEIF 368
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV 117
 
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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