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Conserved domains on  [gi|83578103|ref|NP_012984|]
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glycogenin glucosyltransferase GLG1 [Saccharomyces cerevisiae S288C]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
6-279 1.23e-78

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


:

Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 249.10  E-value: 1.23e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103   6 AIATLLYSADYLPGVFALGHQVNKLleeagkKGDIETCLIVTTSLfngtlSELAKNILQSIYTKIVLVEPLNCQEESIqk 85
Cdd:cd02537   2 AYVTLLTNDDYLPGALVLGYSLRKV------GSSYDLVVLVTPGV-----SEESREALEEVGWIVREVEPIDPPDSAN-- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  86 nsenlaLLERPELSFALIKARLWELTQFEQVLYLDSDTLPLnKEFLKLFDImskqtTSQVGAIADIGWPDMFNSGVMMLI 165
Cdd:cd02537  69 ------LLKRPRFKDTYTKLRLWNLTEYDKVVFLDADTLVL-RNIDELFDL-----PGEFAAAPDCGWPDLFNSGVFVLK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 166 PDADTASVLQNYIFENTSIDGSDQGILNQFFNQNCctdelvkdsfsrEWVQLSFTYNVTIPNLGYQSSPamNYFKPSIKL 245
Cdd:cd02537 137 PSEETFNDLLDALQDTPSFDGGDQGLLNSYFSDRG------------IWKRLPFTYNALKPLRYLHPEA--LWFGDEIKV 202
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 83578103 246 IHFIGKHKPWSLWSQKN----FIKNEYHDQWNEVYEEF 279
Cdd:cd02537 203 VHFIGGDKPWSWWRDPEtkekDDYNELHQWWWDIYDEL 240
PRK13914 super family cl36314
invasion associated endopeptidase;
291-424 5.97e-04

invasion associated endopeptidase;


The actual alignment was detected with superfamily member PRK13914:

Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 42.87  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  291 KPKISDSDKTETPETITPVDAP-------PSNEPTTNQEIDTISTVEENVDNQNAEPVPNSDHSPAPNPVPldftkwlTT 363
Cdd:PRK13914 240 KLAIKQTANTATPKAEVKTEAPaaekqaaPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPST-------NT 312
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83578103  364 FINKDHLTNQPVNESREYSKENDNNIINSSSNRDQESPPNSTQ---ELNSSYSVVSTQADSDEH 424
Cdd:PRK13914 313 NANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQgssNNNSNSSASAIIAEAQKH 376
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
6-279 1.23e-78

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 249.10  E-value: 1.23e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103   6 AIATLLYSADYLPGVFALGHQVNKLleeagkKGDIETCLIVTTSLfngtlSELAKNILQSIYTKIVLVEPLNCQEESIqk 85
Cdd:cd02537   2 AYVTLLTNDDYLPGALVLGYSLRKV------GSSYDLVVLVTPGV-----SEESREALEEVGWIVREVEPIDPPDSAN-- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  86 nsenlaLLERPELSFALIKARLWELTQFEQVLYLDSDTLPLnKEFLKLFDImskqtTSQVGAIADIGWPDMFNSGVMMLI 165
Cdd:cd02537  69 ------LLKRPRFKDTYTKLRLWNLTEYDKVVFLDADTLVL-RNIDELFDL-----PGEFAAAPDCGWPDLFNSGVFVLK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 166 PDADTASVLQNYIFENTSIDGSDQGILNQFFNQNCctdelvkdsfsrEWVQLSFTYNVTIPNLGYQSSPamNYFKPSIKL 245
Cdd:cd02537 137 PSEETFNDLLDALQDTPSFDGGDQGLLNSYFSDRG------------IWKRLPFTYNALKPLRYLHPEA--LWFGDEIKV 202
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 83578103 246 IHFIGKHKPWSLWSQKN----FIKNEYHDQWNEVYEEF 279
Cdd:cd02537 203 VHFIGGDKPWSWWRDPEtkekDDYNELHQWWWDIYDEL 240
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
9-258 1.13e-19

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.


Pssm-ID: 279798 [Multi-domain]  Cd Length: 252  Bit Score: 88.92  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103     9 TLLYSADYLPGVFALGHQVNKLLEEAGkkgdietcliVTTSLFNGTLSELAKNILQSIYTKIVLVEPLNCQEESIQKNSE 88
Cdd:pfam01501   3 ALALDKNYLLGASVSIKSLLKNNSDFA----------LNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFEYFS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103    89 NLALLERPELSFA-LIKARLWELT-QFEQVLYLDSDTLPlNKEFLKLFDI----------------MSKQTTSQVGAIAD 150
Cdd:pfam01501  73 KLKLRSPKYWSLLnYLRLYLPDLFpKLDKILYLDADIVV-QGDLSPLWDIdlggkvlaavednyfqRYPNFSEPIILENF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103   151 IGWPDMFNSGVMMLIPDADTA-SVLQNYI-FENTSIDGS-----DQGILNQFFNQNCCTdelvkdsfsrewvqLSFTYNV 223
Cdd:pfam01501 152 GPPACYFNAGMLLFDLDAWRKeNITERYIkWLNLNENRTlwklgDQDPLNIVFYGKVKP--------------LDPRWNV 217
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 83578103   224 tIPNLGYQSSPAMNYFKPSIKLIHFIGKHKPWSLW 258
Cdd:pfam01501 218 -LGLGYYNKKKSLNEITENAAVIHYNGPTKPWLDI 251
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
112-277 1.41e-12

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 68.85  E-value: 1.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 112 QFEQVLYLDSDTLPLNKeFLKLFDI-MSKQTtsqVGAIADIGWPDM----------------FNSGVMMLIPDADTASVL 174
Cdd:COG1442 100 DYDKVLYLDADTLVLGD-LSELWDIdLGGNL---LAAVRDGTVTGSqkkrakrlglpdddgyFNSGVLLINLKKWREENI 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 175 QNYIFE-----NTSIDGSDQGILNQFFNQNcctdelvkdsfsreWVQLSFTYNvTIPNLGYQSSPA-----MNYFKPSIK 244
Cdd:COG1442 176 TEKALEflkenPDKLKYPDQDILNIVLGGK--------------VKFLPPRYN-YQYSLYYELKDKsnkkeLLEARKNPV 240
                       170       180       190
                ....*....|....*....|....*....|...
gi 83578103 245 LIHFIGKHKPWSLWSQknfikNEYHDQWNEVYE 277
Cdd:COG1442 241 IIHYTGPTKPWHKWCT-----HPYADLYWEYLK 268
PRK13914 PRK13914
invasion associated endopeptidase;
291-424 5.97e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 42.87  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  291 KPKISDSDKTETPETITPVDAP-------PSNEPTTNQEIDTISTVEENVDNQNAEPVPNSDHSPAPNPVPldftkwlTT 363
Cdd:PRK13914 240 KLAIKQTANTATPKAEVKTEAPaaekqaaPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPST-------NT 312
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83578103  364 FINKDHLTNQPVNESREYSKENDNNIINSSSNRDQESPPNSTQ---ELNSSYSVVSTQADSDEH 424
Cdd:PRK13914 313 NANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQgssNNNSNSSASAIIAEAQKH 376
 
Name Accession Description Interval E-value
GT8_Glycogenin cd02537
Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin ...
6-279 1.23e-78

Glycogenin belongs the GT 8 family and initiates the biosynthesis of glycogen; Glycogenin initiates the biosynthesis of glycogen by incorporating glucose residues through a self-glucosylation reaction at a Tyr residue, and then acts as substrate for chain elongation by glycogen synthase and branching enzyme. It contains a conserved DxD motif and an N-terminal beta-alpha-beta Rossmann-like fold that are common to the nucleotide-binding domains of most glycosyltransferases. The DxD motif is essential for coordination of the catalytic divalent cation, most commonly Mn2+. Glycogenin can be classified as a retaining glycosyltransferase, based on the relative anomeric stereochemistry of the substrate and product in the reaction catalyzed. It is placed in glycosyltransferase family 8 which includes lipopolysaccharide glucose and galactose transferases and galactinol synthases.


Pssm-ID: 133018 [Multi-domain]  Cd Length: 240  Bit Score: 249.10  E-value: 1.23e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103   6 AIATLLYSADYLPGVFALGHQVNKLleeagkKGDIETCLIVTTSLfngtlSELAKNILQSIYTKIVLVEPLNCQEESIqk 85
Cdd:cd02537   2 AYVTLLTNDDYLPGALVLGYSLRKV------GSSYDLVVLVTPGV-----SEESREALEEVGWIVREVEPIDPPDSAN-- 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  86 nsenlaLLERPELSFALIKARLWELTQFEQVLYLDSDTLPLnKEFLKLFDImskqtTSQVGAIADIGWPDMFNSGVMMLI 165
Cdd:cd02537  69 ------LLKRPRFKDTYTKLRLWNLTEYDKVVFLDADTLVL-RNIDELFDL-----PGEFAAAPDCGWPDLFNSGVFVLK 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 166 PDADTASVLQNYIFENTSIDGSDQGILNQFFNQNCctdelvkdsfsrEWVQLSFTYNVTIPNLGYQSSPamNYFKPSIKL 245
Cdd:cd02537 137 PSEETFNDLLDALQDTPSFDGGDQGLLNSYFSDRG------------IWKRLPFTYNALKPLRYLHPEA--LWFGDEIKV 202
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 83578103 246 IHFIGKHKPWSLWSQKN----FIKNEYHDQWNEVYEEF 279
Cdd:cd02537 203 VHFIGGDKPWSWWRDPEtkekDDYNELHQWWWDIYDEL 240
Glyco_transf_8 pfam01501
Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to ...
9-258 1.13e-19

Glycosyl transferase family 8; This family includes enzymes that transfer sugar residues to donor molecules. Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. This family includes Lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, and glycogenin glucosyltransferase.


Pssm-ID: 279798 [Multi-domain]  Cd Length: 252  Bit Score: 88.92  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103     9 TLLYSADYLPGVFALGHQVNKLLEEAGkkgdietcliVTTSLFNGTLSELAKNILQSIYTKIVLVEPLNCQEESIQKNSE 88
Cdd:pfam01501   3 ALALDKNYLLGASVSIKSLLKNNSDFA----------LNFHIFTDDIPVENLDILNWLASSYKPVLPLLESDIKIFEYFS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103    89 NLALLERPELSFA-LIKARLWELT-QFEQVLYLDSDTLPlNKEFLKLFDI----------------MSKQTTSQVGAIAD 150
Cdd:pfam01501  73 KLKLRSPKYWSLLnYLRLYLPDLFpKLDKILYLDADIVV-QGDLSPLWDIdlggkvlaavednyfqRYPNFSEPIILENF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103   151 IGWPDMFNSGVMMLIPDADTA-SVLQNYI-FENTSIDGS-----DQGILNQFFNQNCCTdelvkdsfsrewvqLSFTYNV 223
Cdd:pfam01501 152 GPPACYFNAGMLLFDLDAWRKeNITERYIkWLNLNENRTlwklgDQDPLNIVFYGKVKP--------------LDPRWNV 217
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 83578103   224 tIPNLGYQSSPAMNYFKPSIKLIHFIGKHKPWSLW 258
Cdd:pfam01501 218 -LGLGYYNKKKSLNEITENAAVIHYNGPTKPWLDI 251
RfaJ COG1442
Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope ...
112-277 1.41e-12

Lipopolysaccharide biosynthesis protein, LPS:glycosyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441051 [Multi-domain]  Cd Length: 301  Bit Score: 68.85  E-value: 1.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 112 QFEQVLYLDSDTLPLNKeFLKLFDI-MSKQTtsqVGAIADIGWPDM----------------FNSGVMMLIPDADTASVL 174
Cdd:COG1442 100 DYDKVLYLDADTLVLGD-LSELWDIdLGGNL---LAAVRDGTVTGSqkkrakrlglpdddgyFNSGVLLINLKKWREENI 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 175 QNYIFE-----NTSIDGSDQGILNQFFNQNcctdelvkdsfsreWVQLSFTYNvTIPNLGYQSSPA-----MNYFKPSIK 244
Cdd:COG1442 176 TEKALEflkenPDKLKYPDQDILNIVLGGK--------------VKFLPPRYN-YQYSLYYELKDKsnkkeLLEARKNPV 240
                       170       180       190
                ....*....|....*....|....*....|...
gi 83578103 245 LIHFIGKHKPWSLWSQknfikNEYHDQWNEVYE 277
Cdd:COG1442 241 IIHYTGPTKPWHKWCT-----HPYADLYWEYLK 268
Glyco_transf_8 cd00505
Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis ...
87-255 7.22e-12

Members of glycosyltransferase family 8 (GT-8) are involved in lipopolysaccharide biosynthesis and glycogen synthesis; Members of this family are involved in lipopolysaccharide biosynthesis and glycogen synthesis. GT-8 comprises enzymes with a number of known activities: lipopolysaccharide galactosyltransferase, lipopolysaccharide glucosyltransferase 1, glycogenin glucosyltransferase, and N-acetylglucosaminyltransferase. GT-8 enzymes contains a conserved DXD motif which is essential in the coordination of a catalytic divalent cation, most commonly Mn2+.


Pssm-ID: 132996 [Multi-domain]  Cd Length: 246  Bit Score: 65.93  E-value: 7.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  87 SENLALLERPELSFALIKARLWELTQ-FEQVLYLDSDTLPLNkEFLKLFDIMSKQttSQVGAIADIGWP----------- 154
Cdd:cd00505  69 SVDSEHLKRPIKIVTLTKLHLPNLVPdYDKILYVDADILVLT-DIDELWDTPLGG--QELAAAPDPGDRregkyyrqkrs 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 155 -----DMFNSGVMMLIPDADT-----ASVLQNYIFENTSIDGSDQGILNQFFNQNcctDELVKdsfsrewvQLSFTYNVT 224
Cdd:cd00505 146 hlagpDYFNSGVFVVNLSKERrnqllKVALEKWLQSLSSLSGGDQDLLNTFFKQV---PFIVK--------SLPCIWNVR 214
                       170       180       190
                ....*....|....*....|....*....|.
gi 83578103 225 IPNLgYQSSPAMNYFKPSIKLIHFIGKHKPW 255
Cdd:cd00505 215 LTGC-YRSLNCFKAFVKNAKVIHFNGPTKPW 244
GT8_A4GalT_like cd04194
A4GalT_like proteins catalyze the addition of galactose or glucose residues to the ...
110-255 9.99e-11

A4GalT_like proteins catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface; The members of this family of glycosyltransferases catalyze the addition of galactose or glucose residues to the lipooligosaccharide (LOS) or lipopolysaccharide (LPS) of the bacterial cell surface. The enzymes exhibit broad substrate specificities. The known functions found in this family include: Alpha-1,4-galactosyltransferase, LOS-alpha-1,3-D-galactosyltransferase, UDP-glucose:(galactosyl) LPS alpha1,2-glucosyltransferase, UDP-galactose: (glucosyl) LPS alpha1,2-galactosyltransferase, and UDP-glucose:(glucosyl) LPS alpha1,2-glucosyltransferase. Alpha-1,4-galactosyltransferase from N. meningitidis adds an alpha-galactose from UDP-Gal (the donor) to a terminal lactose (the acceptor) of the LOS structure of outer membrane. LOSs are virulence factors that enable the organism to evade the immune system of host cells. In E. coli, the three alpha-1,2-glycosyltransferases, that are involved in the synthesis of the outer core region of the LPS, are all members of this family. The three enzymes share 40 % of sequence identity, but have different sugar donor or acceptor specificities, representing the structural diversity of LPS.


Pssm-ID: 133037 [Multi-domain]  Cd Length: 248  Bit Score: 62.23  E-value: 9.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 110 LTQFEQVLYLDSDTLpLNKEFLKLFDIMSKqtTSQVGAIADIG---------------WPDMFNSGVMMLipdaDTAS-- 172
Cdd:cd04194  93 LPDYDKVLYLDADII-VLGDLSELFDIDLG--DNLLAAVRDPFieqekkrkrrlggydDGSYFNSGVLLI----NLKKwr 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103 173 --VLQNYIFENTSIDGS-----DQGILNQFFNQNcctdelvkdsfsreWVQLSFTYN--VTIPNLGYQSSPAMNYFKP-- 241
Cdd:cd04194 166 eeNITEKLLELIKEYGGrliypDQDILNAVLKDK--------------ILYLPPRYNfqTGFYYLLKKKSKEEQELEEar 231
                       170
                ....*....|....*
gi 83578103 242 -SIKLIHFIGKHKPW 255
Cdd:cd04194 232 kNPVIIHYTGSDKPW 246
PRK13914 PRK13914
invasion associated endopeptidase;
291-424 5.97e-04

invasion associated endopeptidase;


Pssm-ID: 237555 [Multi-domain]  Cd Length: 481  Bit Score: 42.87  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  291 KPKISDSDKTETPETITPVDAP-------PSNEPTTNQEIDTISTVEENVDNQNAEPVPNSDHSPAPNPVPldftkwlTT 363
Cdd:PRK13914 240 KLAIKQTANTATPKAEVKTEAPaaekqaaPVVKENTNTNTATTEKKETTTQQQTAPKAPTEAAKPAPAPST-------NT 312
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 83578103  364 FINKDHLTNQPVNESREYSKENDNNIINSSSNRDQESPPNSTQ---ELNSSYSVVSTQADSDEH 424
Cdd:PRK13914 313 NANKTNTNTNTNTNNTNTSTPSKNTNTNTNSNTNTNSNTNANQgssNNNSNSSASAIIAEAQKH 376
PRK08581 PRK08581
amidase domain-containing protein;
277-505 6.84e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 42.85  E-value: 6.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  277 EEFKEEHQLNNEVSKPKISDSDKTETPETITPVDAPPSNEPTTNQEIDTISTVEENVDNQNaepVPNSDHSPAPNPVPLD 356
Cdd:PRK08581  43 SKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSNNIIDFIYKNLPQTN---INQLLTKNKYDDNYSL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  357 FTKWLTTFINKDHLTNQPVNESREYSKENDNNIINSSSNRDQES-------------PPNSTQELNSSYSVVSTQADSDE 423
Cdd:PRK08581 120 TTLIQNLFNLNSDISDYEQPRNSEKSTNDSNKNSDSSIKNDTDTqsskqdkadnqkaPSSNNTKPSTSNKQPNSPKPTQP 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83578103  424 HQN---AEEEDSTTDNASNSGEESHLDDISTAASSNNNVSNQPDGKNFSNSKENN---ISVESSPSNPEQKRSTDNIQKP 497
Cdd:PRK08581 200 NQSnsqPASDDTANQKSSSKDNQSMSDSALDSILDQYSEDAKKTQKDYASQSKKDkteTSNTKNPQLPTQDELKHKSKPA 279

                 ....*...
gi 83578103  498 SVSTNDLP 505
Cdd:PRK08581 280 QSFENDVN 287
 
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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