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Conserved domains on  [gi|2770131014|ref|NP_001418281|]
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exostosin-like 3 [Rattus norvegicus]

Protein Classification

exostosin( domain architecture ID 10503393)

exostosin is a family 47 glycosyltransferase that is required for the biosynthesis of heparan-sulfate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_transf_64 pfam09258
Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction ...
 663-900 5.15e-138

Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. They are also required for the biosynthesis of heparan-sulphate.


:

Pssm-ID: 430488  Cd Length: 241  Bit Score: 411.30  E-value: 5.15e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 663 FTVVMLT-YEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRTEKNSLNNRFLPWNEIETEAIL 741
Cdd:pfam09258   1 FTAVINTyYSRIDLLLKLLQRYAGSPHLAKIIVLWNNPKPPPELSRWPGTGVPVTVIRQKRNSLNNRFLPYPEIETDAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 742 SIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDIPHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAI 821
Cdd:pfam09258  81 SLDDDILLSTDEIDFAFRVWRSFPDRIVGFPPRSHFWDLSSGRWGYTSEWTNEYSMVLTGAAFYHRYYLYLYTHSLPKSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 822 RDMVDEYINCEDIAMNFLVSHITRKPPIKVTSRWTFRCPGCPQ--ALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRV 899
Cdd:pfam09258 161 RTLVDETQNCEDILMNFLVANVTRKPPVKVTQRKQFKEGKNSGkvGLSSRPGHFLQRSKCINKFAAVFGYMPLVYSQIRL 240


                  .
gi 2770131014 900 D 900
Cdd:pfam09258 241 D 241
Exostosin pfam03016
Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on ...
 190-500 1.74e-45

Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear.


:

Pssm-ID: 397245  Cd Length: 290  Bit Score: 165.29  E-value: 1.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 190 LTSGFPVFVYD-----------------SDQFAFGSYLDPLVKQAFQatvranVYVTENAAIACLYVVLVGEIQEP---- 248
Cdd:pfam03016   1 SCKGLKVYVYDlpprfnedllqpcrsltGWYSAEQFLLESILHSRIE------CRTSDPDEADCFFVPFYASLDASrhll 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 249 ----AVLQPADLEKQLHSLPHW-RTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVA--QSTFYAAQYRAGFDLVVsPLVH 321
Cdd:pfam03016  75 nsalTDLFRELLDWLKSQYPYWnRSGGRDHFIVSGHPAWSFRRTAPDVDWGRAMLLnlTVLFSEDQFRPGKDVAL-PYPT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 322 AMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEarSFEEEMEGDPPADYDDRIIATlkavqdskldqvlveftck 401
Cdd:pfam03016 154 PFHPDIGQWQDISPSNRRKTLLFFAGNRRRGYSGKIRP--LLLEECKGNPDADICGGLQCT------------------- 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 402 nqpkpslptewalcGEREDRLELLKLSTFALiITPGDPSLlissgcATRLFEALEVGAVPVVLGEQVQLPYHDMLQWNEA 481
Cdd:pfam03016 213 --------------PGRDKYMELLRSSRFCL-QPPGDTPT------SPRLFDALLAGCIPVIISDGWELPFADVIDWRKF 271

                         330
                  ....*....|....*....
gi 2770131014 482 ALVVPKPRVTEVHFLLRSL 500
Cdd:pfam03016 272 SVFVPENDIPELKSILRSL 290
TPR_MLP1_2 super family cl25510
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 71-150 5.90e-06

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


The actual alignment was detected with superfamily member pfam07926:

Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 46.48  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014  71 NELceVKHVLDLCRIREsVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQdllQLKNVISQTEHSYKELMAQNQ 150
Cdd:pfam07926  47 REL--VLHAEDIKALQA-LREELNELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQNK 120
 
Name Accession Description Interval E-value
Glyco_transf_64 pfam09258
Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction ...
 663-900 5.15e-138

Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. They are also required for the biosynthesis of heparan-sulphate.


Pssm-ID: 430488  Cd Length: 241  Bit Score: 411.30  E-value: 5.15e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 663 FTVVMLT-YEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRTEKNSLNNRFLPWNEIETEAIL 741
Cdd:pfam09258   1 FTAVINTyYSRIDLLLKLLQRYAGSPHLAKIIVLWNNPKPPPELSRWPGTGVPVTVIRQKRNSLNNRFLPYPEIETDAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 742 SIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDIPHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAI 821
Cdd:pfam09258  81 SLDDDILLSTDEIDFAFRVWRSFPDRIVGFPPRSHFWDLSSGRWGYTSEWTNEYSMVLTGAAFYHRYYLYLYTHSLPKSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 822 RDMVDEYINCEDIAMNFLVSHITRKPPIKVTSRWTFRCPGCPQ--ALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRV 899
Cdd:pfam09258 161 RTLVDETQNCEDILMNFLVANVTRKPPVKVTQRKQFKEGKNSGkvGLSSRPGHFLQRSKCINKFAAVFGYMPLVYSQIRL 240


                  .
gi 2770131014 900 D 900
Cdd:pfam09258 241 D 241
Exostosin pfam03016
Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on ...
 190-500 1.74e-45

Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear.


Pssm-ID: 397245  Cd Length: 290  Bit Score: 165.29  E-value: 1.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 190 LTSGFPVFVYD-----------------SDQFAFGSYLDPLVKQAFQatvranVYVTENAAIACLYVVLVGEIQEP---- 248
Cdd:pfam03016   1 SCKGLKVYVYDlpprfnedllqpcrsltGWYSAEQFLLESILHSRIE------CRTSDPDEADCFFVPFYASLDASrhll 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 249 ----AVLQPADLEKQLHSLPHW-RTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVA--QSTFYAAQYRAGFDLVVsPLVH 321
Cdd:pfam03016  75 nsalTDLFRELLDWLKSQYPYWnRSGGRDHFIVSGHPAWSFRRTAPDVDWGRAMLLnlTVLFSEDQFRPGKDVAL-PYPT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 322 AMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEarSFEEEMEGDPPADYDDRIIATlkavqdskldqvlveftck 401
Cdd:pfam03016 154 PFHPDIGQWQDISPSNRRKTLLFFAGNRRRGYSGKIRP--LLLEECKGNPDADICGGLQCT------------------- 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 402 nqpkpslptewalcGEREDRLELLKLSTFALiITPGDPSLlissgcATRLFEALEVGAVPVVLGEQVQLPYHDMLQWNEA 481
Cdd:pfam03016 213 --------------PGRDKYMELLRSSRFCL-QPPGDTPT------SPRLFDALLAGCIPVIISDGWELPFADVIDWRKF 271

                         330
                  ....*....|....*....
gi 2770131014 482 ALVVPKPRVTEVHFLLRSL 500
Cdd:pfam03016 272 SVFVPENDIPELKSILRSL 290
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 71-150 5.90e-06

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 46.48  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014  71 NELceVKHVLDLCRIREsVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQdllQLKNVISQTEHSYKELMAQNQ 150
Cdd:pfam07926  47 REL--VLHAEDIKALQA-LREELNELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQNK 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
87-150 7.85e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 7.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2770131014  87 ESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQ 150
Cdd:COG4372    69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
663-778 1.29e-03

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 41.13  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 663 FTVVMLTYEREEVLMNSLERLNGLPYLN-KVVVVWNSPKLPSEDLL----WPDigvpIMVVRTEKN----SLNNRFLpwN 733
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQTYPPfEVIVVDNGSTDGTAELLaalaFPR----VRVIRNPENlgfaAARNLGL--R 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2770131014 734 EIETEAILSIDDDAHLRHDEI-------MFGFRvwREARDRIVGFPGRYHAW 778
Cdd:COG1216    79 AAGGDYLLFLDDDTVVEPDWLerllaaaCLLIR--REVFEEVGGFDERFFLY 128
 
Name Accession Description Interval E-value
Glyco_transf_64 pfam09258
Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction ...
 663-900 5.15e-138

Glycosyl transferase family 64 domain; Members of this family catalyze the transfer reaction of N-acetylglucosamine and N-acetylgalactosamine from the respective UDP-sugars to the non-reducing end of [glucuronic acid]beta 1-3[galactose]beta 1-O-naphthalenemethanol, an acceptor substrate analog of the natural common linker of various glycosylaminoglycans. They are also required for the biosynthesis of heparan-sulphate.


Pssm-ID: 430488  Cd Length: 241  Bit Score: 411.30  E-value: 5.15e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 663 FTVVMLT-YEREEVLMNSLERLNGLPYLNKVVVVWNSPKLPSEDLLWPDIGVPIMVVRTEKNSLNNRFLPWNEIETEAIL 741
Cdd:pfam09258   1 FTAVINTyYSRIDLLLKLLQRYAGSPHLAKIIVLWNNPKPPPELSRWPGTGVPVTVIRQKRNSLNNRFLPYPEIETDAVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 742 SIDDDAHLRHDEIMFGFRVWREARDRIVGFPGRYHAWDIPHQSWLYNSNYSCELSMVLTGAAFFHKYYAYLYSYVMPQAI 821
Cdd:pfam09258  81 SLDDDILLSTDEIDFAFRVWRSFPDRIVGFPPRSHFWDLSSGRWGYTSEWTNEYSMVLTGAAFYHRYYLYLYTHSLPKSL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 822 RDMVDEYINCEDIAMNFLVSHITRKPPIKVTSRWTFRCPGCPQ--ALSHDDSHFHERHKCINFFVKVYGYMPLLYTQFRV 899
Cdd:pfam09258 161 RTLVDETQNCEDILMNFLVANVTRKPPVKVTQRKQFKEGKNSGkvGLSSRPGHFLQRSKCINKFAAVFGYMPLVYSQIRL 240


                  .
gi 2770131014 900 D 900
Cdd:pfam09258 241 D 241
Exostosin pfam03016
Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on ...
 190-500 1.74e-45

Exostosin family; The EXT family is a family of tumour suppressor genes. Mutations of EXT1 on 8q24.1, EXT2 on 11p11-13, and EXT3 on 19p have been associated with the autosomal dominant disorder known as hereditary multiple exostoses (HME). This is the most common known skeletal dysplasia. The chromosomal locations of other EXT genes suggest association with other forms of neoplasia. EXT1 and EXT2 have both been shown to encode a heparan sulphate polymerase with both D-glucuronyl (GlcA) and N-acetyl-D-glucosaminoglycan (GlcNAC) transferase activities. The nature of the defect in heparan sulphate biosynthesis in HME is unclear.


Pssm-ID: 397245  Cd Length: 290  Bit Score: 165.29  E-value: 1.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 190 LTSGFPVFVYD-----------------SDQFAFGSYLDPLVKQAFQatvranVYVTENAAIACLYVVLVGEIQEP---- 248
Cdd:pfam03016   1 SCKGLKVYVYDlpprfnedllqpcrsltGWYSAEQFLLESILHSRIE------CRTSDPDEADCFFVPFYASLDASrhll 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 249 ----AVLQPADLEKQLHSLPHW-RTDGHNHVIINLSRKSDTQNLLYNVSTGRAMVA--QSTFYAAQYRAGFDLVVsPLVH 321
Cdd:pfam03016  75 nsalTDLFRELLDWLKSQYPYWnRSGGRDHFIVSGHPAWSFRRTAPDVDWGRAMLLnlTVLFSEDQFRPGKDVAL-PYPT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 322 AMSEPNFMEIPPQVPVKRKYLFTFQGEKIESLRSSLQEarSFEEEMEGDPPADYDDRIIATlkavqdskldqvlveftck 401
Cdd:pfam03016 154 PFHPDIGQWQDISPSNRRKTLLFFAGNRRRGYSGKIRP--LLLEECKGNPDADICGGLQCT------------------- 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 402 nqpkpslptewalcGEREDRLELLKLSTFALiITPGDPSLlissgcATRLFEALEVGAVPVVLGEQVQLPYHDMLQWNEA 481
Cdd:pfam03016 213 --------------PGRDKYMELLRSSRFCL-QPPGDTPT------SPRLFDALLAGCIPVIISDGWELPFADVIDWRKF 271

                         330
                  ....*....|....*....
gi 2770131014 482 ALVVPKPRVTEVHFLLRSL 500
Cdd:pfam03016 272 SVFVPENDIPELKSILRSL 290
TPR_MLP1_2 pfam07926
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ...
 71-150 5.90e-06

TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.


Pssm-ID: 462316 [Multi-domain]  Cd Length: 129  Bit Score: 46.48  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014  71 NELceVKHVLDLCRIREsVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQdllQLKNVISQTEHSYKELMAQNQ 150
Cdd:pfam07926  47 REL--VLHAEDIKALQA-LREELNELKAEIAELKAEAESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNEQNK 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
87-150 7.85e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.97  E-value: 7.85e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2770131014  87 ESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQ 150
Cdd:COG4372    69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
87-149 1.22e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 1.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2770131014  87 ESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQN 149
Cdd:COG4372   118 EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE 180
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
663-778 1.29e-03

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 41.13  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770131014 663 FTVVMLTYEREEVLMNSLERLNGLPYLN-KVVVVWNSPKLPSEDLL----WPDigvpIMVVRTEKN----SLNNRFLpwN 733
Cdd:COG1216     5 VSVVIPTYNRPELLRRCLESLLAQTYPPfEVIVVDNGSTDGTAELLaalaFPR----VRVIRNPENlgfaAARNLGL--R 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2770131014 734 EIETEAILSIDDDAHLRHDEI-------MFGFRvwREARDRIVGFPGRYHAW 778
Cdd:COG1216    79 AAGGDYLLFLDDDTVVEPDWLerllaaaCLLIR--REVFEEVGGFDERFFLY 128
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 92-148 3.26e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2770131014  92 ELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQ 148
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 87-150 3.34e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 3.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2770131014  87 ESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQ 150
Cdd:COG3883    33 EAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 86-150 7.94e-03

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 38.07  E-value: 7.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2770131014  86 RESVSEELLQLEAKRQELNSEIAKLNLKIEACKKSIENAKQDLLQLKNVISQTEHSYKELMAQNQ 150
Cdd:pfam11559  54 RESLNETIRTLEAEIERLQSKIERLKTQLEDLERELALLQAKERQLEKKLKTLEQKLKNEKEELQ 118
 
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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