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Conserved domains on  [gi|582519897|gb|EVY12007|]
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N-(5'-phosphoribosyl)anthranilate isomerase [Staphylococcus aureus F83251]

Protein Classification

triose-phosphate isomerase; tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like( domain architecture ID 10793929)

triose-phosphate isomerase (TIM) is a glycolytic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate| tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like (DUS1L) catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13958 PRK13958
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional
 2-208 8.58e-127

N-(5'-phosphoribosyl)anthranilate isomerase; Provisional


:

Pssm-ID: 184418  Cd Length: 207  Bit Score: 355.96  E-value: 8.58e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   2 MKLKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVMVNPDLTTIEHVLSNTSINTIQ 81
Cdd:PRK13958   1 MKLKFCGFTTIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVVVNPDLTTIEHILSNTSINTIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  82 LHGTESIDFIQEIKKKYSSIKITKALAADENIIQNINKYKGFVDLFIIDTPSVSYGGTGQTYDWTILKHIKDIPYLIAGG 161
Cdd:PRK13958  81 LHGTESIDFIQEIKKKYSSIKIIKALPADENIIQNINKYKGFVDLFIIDTPSVSYGGTGQTYDWTILKHIKDIPYLIAGG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 582519897 162 INSENIQTVNQLKLSHQGYDLASGIEVNGRKDIEKMTAIVNIVKGDR 208
Cdd:PRK13958 161 INSENIQTVEQLKLSHQGYDIASGIETNGRKDINKMTAIVNIVKGDR 207
 
Name Accession Description Interval E-value
PRK13958 PRK13958
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional
 2-208 8.58e-127

N-(5'-phosphoribosyl)anthranilate isomerase; Provisional


Pssm-ID: 184418  Cd Length: 207  Bit Score: 355.96  E-value: 8.58e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   2 MKLKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVMVNPDLTTIEHVLSNTSINTIQ 81
Cdd:PRK13958   1 MKLKFCGFTTIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVVVNPDLTTIEHILSNTSINTIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  82 LHGTESIDFIQEIKKKYSSIKITKALAADENIIQNINKYKGFVDLFIIDTPSVSYGGTGQTYDWTILKHIKDIPYLIAGG 161
Cdd:PRK13958  81 LHGTESIDFIQEIKKKYSSIKIIKALPADENIIQNINKYKGFVDLFIIDTPSVSYGGTGQTYDWTILKHIKDIPYLIAGG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 582519897 162 INSENIQTVNQLKLSHQGYDLASGIEVNGRKDIEKMTAIVNIVKGDR 208
Cdd:PRK13958 161 INSENIQTVEQLKLSHQGYDIASGIETNGRKDINKMTAIVNIVKGDR 207
TrpF COG0135
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ...
 1-206 8.77e-74

Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; Phosphoribosylanthranilate isomerase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439905  Cd Length: 208  Bit Score: 221.94  E-value: 8.77e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   1 MMKLKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVMVNPDLTTIEHVLSNTSINTI 80
Cdd:COG0135    1 MTRVKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPPFVKKVGVFVNADPEEILEIVEAVGLDAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  81 QLHGTESIDFIQEIKKKYsSIKITKALAADENI-IQNINKYKGFVDLFIIDTPS-VSYGGTGQTYDWTILKHIK-DIPYL 157
Cdd:COG0135   81 QLHGDESPEYCAALRERL-GLPVIKAIRVGDGAdLEEAAAYAPVADALLLDAKVpGLYGGTGKTFDWSLLAGLAlPKPVI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 582519897 158 IAGGINSENIQTVnqLKLSH-QGYDLASGIEV-NGRKDIEKMTAIVNIVKG 206
Cdd:COG0135  160 LAGGLTPENVAEA--IRLVRpYGVDVSSGVESaPGVKDPDKIRAFVEAVRA 208
PRAI cd00405
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ...
 4-204 3.94e-69

Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan biosynthesis, the conversion of N-(5'- phosphoribosyl)-anthranilate (PRA) to 1-(o-carboxyphenylamino)- 1-deoxyribulose 5-phosphate (CdRP). Most PRAIs are monomeric, monofunctional and thermolabile, but in some thermophile organisms PRAI is dimeric for reasons of stability and in others it is fused to other components of the tryptophan biosynthesis pathway to form multifunctional enzymes.


Pssm-ID: 238237  Cd Length: 203  Bit Score: 209.74  E-value: 3.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   4 LKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVMVNPDLTTIEHVLSNTSINTIQLH 83
Cdd:cd00405    1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVKRVGVFVNEDLEEILEIAEELGLDVVQLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  84 GTESIDFIQEIKKKYsSIKITKAL-AADENIIQNINKYKGFVDLFIIDTPSVS-YGGTGQTYDWTILKHIK-DIPYLIAG 160
Cdd:cd00405   81 GDESPEYCAQLRARL-GLPVIKAIrVKDEEDLEKAAAYAGEVDAILLDSKSGGgGGGTGKTFDWSLLRGLAsRKPVILAG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 582519897 161 GINSENIQTVNQLkLSHQGYDLASGIEVN-GRKDIEKMTAIVNIV 204
Cdd:cd00405  160 GLTPDNVAEAIRL-VRPYGVDVSSGVETSpGIKDPEKIRAFIEAA 203
PRAI pfam00697
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
4-202 4.10e-33

N-(5'phosphoribosyl)anthranilate (PRA) isomerase;


Pssm-ID: 395566  Cd Length: 193  Bit Score: 117.45  E-value: 4.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897    4 LKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIdkVCVMVNPDLTTIEHVLSNTSINTIQLH 83
Cdd:pfam00697   1 AKICGLTRLSDVKAAVKAGADYLGLIFSESSKRQVSPEQAQELRSPVPLLL--VGVFVNQPIDDVLRIAQVLGLDVVQLH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   84 GTESIDFIQEIKKKYSSIKITKaLAADENIIQNINKYKGfVDLFIIDTPSvsyGGTGQTYDWTILKHI--KDIPYLIAGG 161
Cdd:pfam00697  79 GDEDQEYENLLPTGVPVIKAIW-VPDSVDTVDIARRADH-VDLPLLDSGA---GGTGELFDWSLVSKWlkSGLKVILAGG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 582519897  162 INSENI-QTVNQLKLShqGYDLASGIEVNGRKDIEKMTAIVN 202
Cdd:pfam00697 154 LNPDNVvEAIKTPGVI--GVDVSSGVETNGIKDLNKIRKFVQ 193
 
Name Accession Description Interval E-value
PRK13958 PRK13958
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional
 2-208 8.58e-127

N-(5'-phosphoribosyl)anthranilate isomerase; Provisional


Pssm-ID: 184418  Cd Length: 207  Bit Score: 355.96  E-value: 8.58e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   2 MKLKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVMVNPDLTTIEHVLSNTSINTIQ 81
Cdd:PRK13958   1 MKLKFCGFTTIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVVVNPDLTTIEHILSNTSINTIQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  82 LHGTESIDFIQEIKKKYSSIKITKALAADENIIQNINKYKGFVDLFIIDTPSVSYGGTGQTYDWTILKHIKDIPYLIAGG 161
Cdd:PRK13958  81 LHGTESIDFIQEIKKKYSSIKIIKALPADENIIQNINKYKGFVDLFIIDTPSVSYGGTGQTYDWTILKHIKDIPYLIAGG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 582519897 162 INSENIQTVNQLKLSHQGYDLASGIEVNGRKDIEKMTAIVNIVKGDR 208
Cdd:PRK13958 161 INSENIQTVEQLKLSHQGYDIASGIETNGRKDINKMTAIVNIVKGDR 207
TrpF COG0135
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ...
 1-206 8.77e-74

Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; Phosphoribosylanthranilate isomerase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 439905  Cd Length: 208  Bit Score: 221.94  E-value: 8.77e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   1 MMKLKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVMVNPDLTTIEHVLSNTSINTI 80
Cdd:COG0135    1 MTRVKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPPFVKKVGVFVNADPEEILEIVEAVGLDAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  81 QLHGTESIDFIQEIKKKYsSIKITKALAADENI-IQNINKYKGFVDLFIIDTPS-VSYGGTGQTYDWTILKHIK-DIPYL 157
Cdd:COG0135   81 QLHGDESPEYCAALRERL-GLPVIKAIRVGDGAdLEEAAAYAPVADALLLDAKVpGLYGGTGKTFDWSLLAGLAlPKPVI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 582519897 158 IAGGINSENIQTVnqLKLSH-QGYDLASGIEV-NGRKDIEKMTAIVNIVKG 206
Cdd:COG0135  160 LAGGLTPENVAEA--IRLVRpYGVDVSSGVESaPGVKDPDKIRAFVEAVRA 208
PRAI cd00405
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ...
 4-204 3.94e-69

Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan biosynthesis, the conversion of N-(5'- phosphoribosyl)-anthranilate (PRA) to 1-(o-carboxyphenylamino)- 1-deoxyribulose 5-phosphate (CdRP). Most PRAIs are monomeric, monofunctional and thermolabile, but in some thermophile organisms PRAI is dimeric for reasons of stability and in others it is fused to other components of the tryptophan biosynthesis pathway to form multifunctional enzymes.


Pssm-ID: 238237  Cd Length: 203  Bit Score: 209.74  E-value: 3.94e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   4 LKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVMVNPDLTTIEHVLSNTSINTIQLH 83
Cdd:cd00405    1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVKRVGVFVNEDLEEILEIAEELGLDVVQLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  84 GTESIDFIQEIKKKYsSIKITKAL-AADENIIQNINKYKGFVDLFIIDTPSVS-YGGTGQTYDWTILKHIK-DIPYLIAG 160
Cdd:cd00405   81 GDESPEYCAQLRARL-GLPVIKAIrVKDEEDLEKAAAYAGEVDAILLDSKSGGgGGGTGKTFDWSLLRGLAsRKPVILAG 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 582519897 161 GINSENIQTVNQLkLSHQGYDLASGIEVN-GRKDIEKMTAIVNIV 204
Cdd:cd00405  160 GLTPDNVAEAIRL-VRPYGVDVSSGVETSpGIKDPEKIRAFIEAA 203
PRK01222 PRK01222
phosphoribosylanthranilate isomerase;
1-206 3.00e-65

phosphoribosylanthranilate isomerase;


Pssm-ID: 234923  Cd Length: 210  Bit Score: 200.03  E-value: 3.00e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   1 MMKLKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDKVCVMVNPDLTTIEHVLSNTSINTI 80
Cdd:PRK01222   2 RMRVKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAALPPFVKVVGVFVNASDEEIDEIVETVPLDLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  81 QLHGTESIDFIQEIKKKYsSIKITKALAADENI-IQNINKYKGFVDLFIIDTPSVSYGGTGQTYDWTILKHIKDIPYLIA 159
Cdd:PRK01222  82 QLHGDETPEFCRQLKRRY-GLPVIKALRVRSAGdLEAAAAYYGDADGLLLDAYVGLPGGTGKTFDWSLLPAGLAKPWILA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 582519897 160 GGINSENI-QTVNQLKLShqGYDLASGIEV-NGRKDIEKMTAIVNIVKG 206
Cdd:PRK01222 161 GGLNPDNVaEAIRQVRPY--GVDVSSGVESaPGIKDPEKIRAFIEAVKS 207
PRK09427 PRK09427
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ...
 5-206 4.14e-36

bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase TrpF;


Pssm-ID: 236509 [Multi-domain]  Cd Length: 454  Bit Score: 131.48  E-value: 4.14e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   5 KFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPnhIDKVCVMVNPDLTTIEHVLSNTSINTIQLHG 84
Cdd:PRK09427 260 KVCGLTRPQDAKAAYDAGAVYGGLIFVEKSPRYVSLEQAQEIIAAAP--LRYVGVFRNADIEDIVDIAKQLSLAAVQLHG 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  85 TESIDFIQEIKKKY-SSIKITKALAADENIiqNINKYKGfVDLFIIDTPSvsyGGTGQTYDWTILKHIKDIPYLIAGGIN 163
Cdd:PRK09427 338 DEDQAYIDALREALpKTCQIWKAISVGDTL--PARDLQH-VDRYLLDNGQ---GGTGQTFDWSLLPGQSLDNVLLAGGLN 411

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 582519897 164 SENIQTVNQLKLShqGYDLASGIEVN-GRKDIEKMTAIVNIVKG 206
Cdd:PRK09427 412 PDNCQQAAQLGCA--GLDFNSGVESApGIKDAQKLASVFQTLRA 453
PRAI pfam00697
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
4-202 4.10e-33

N-(5'phosphoribosyl)anthranilate (PRA) isomerase;


Pssm-ID: 395566  Cd Length: 193  Bit Score: 117.45  E-value: 4.10e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897    4 LKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIdkVCVMVNPDLTTIEHVLSNTSINTIQLH 83
Cdd:pfam00697   1 AKICGLTRLSDVKAAVKAGADYLGLIFSESSKRQVSPEQAQELRSPVPLLL--VGVFVNQPIDDVLRIAQVLGLDVVQLH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   84 GTESIDFIQEIKKKYSSIKITKaLAADENIIQNINKYKGfVDLFIIDTPSvsyGGTGQTYDWTILKHI--KDIPYLIAGG 161
Cdd:pfam00697  79 GDEDQEYENLLPTGVPVIKAIW-VPDSVDTVDIARRADH-VDLPLLDSGA---GGTGELFDWSLVSKWlkSGLKVILAGG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 582519897  162 INSENI-QTVNQLKLShqGYDLASGIEVNGRKDIEKMTAIVN 202
Cdd:pfam00697 154 LNPDNVvEAIKTPGVI--GVDVSSGVETNGIKDLNKIRKFVQ 193
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 2-205 1.26e-29

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 114.91  E-value: 1.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   2 MKLKFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTI-TQIKKLASAVPN-HIDKVCVMVNPDLTTIEHVLSNTSINT 79
Cdd:PRK13803   3 PKIKICGIKDSALISKAVDMLPDFIGFIFYEKSPRFVGNkFLAPNLEKAIRKaGGRPVGVFVNESAKAMLKFSKKNGIDF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  80 IQLHGTESI---DFIQEIKKKysSIKITKALAADEN-IIQNINKYKGFVDLFIIDTPSVSYGGTGQTYDW-TILKHIKDI 154
Cdd:PRK13803  83 VQLHGAESKaepAYCQRIYKK--SIKKIGSFLIDDAfGFEVLDEYRDHVKYFLFDNKTKIYGGSGKSFDWeKFYNYNFKF 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 582519897 155 PYLIAGGINSENIQTVNQLKLSHQ-GYDLASGIEV-NGRKDIEKMTAIVNIVK 205
Cdd:PRK13803 161 PFFLSGGLSPTNFDRIINLTHPQIlGIDVSSGFEDsPGNKKLTLLKSFITNVK 213
PLN02363 PLN02363
phosphoribosylanthranilate isomerase
 5-205 8.84e-24

phosphoribosylanthranilate isomerase


Pssm-ID: 215207  Cd Length: 256  Bit Score: 94.93  E-value: 8.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897   5 KFCGFTSIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHIDK-VCVMVNPDLTTIEHVLSNTSINTIQLH 83
Cdd:PLN02363  50 KMCGITSARDAAMAVEAGADFIGMILWPKSKRSISLSVAKEISQVAREGGAKpVGVFVDDDANTILRAADSSDLELVQLH 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 582519897  84 GTESIDFIQEIKKKyssIKITKALAADEN---IIQNINKYKGFVDLFIIDTpsvSYGGTGQTYDWTILK--HIKDIP-YL 157
Cdd:PLN02363 130 GNGSRAAFSRLVRE---RKVIYVLNANEDgklLNVVPEEDCHLADWILVDS---ATGGSGKGFNWQNFKlpSVRSRNgWL 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 582519897 158 IAGGINSENI-QTVNQLKLShqGYDLASGIEVNG--RKDIEKMTAIVNIVK 205
Cdd:PLN02363 204 LAGGLTPENVhEAVSLLKPT--GVDVSSGICGPDgiRKDPSKISSFISAVK 252
 
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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