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Conserved domains on  [gi|398364971|ref|NP_010290|]
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phosphoribosylanthranilate isomerase TRP1 [Saccharomyces cerevisiae S288C]

Protein Classification

triose-phosphate isomerase; tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)]-like( domain architecture ID 11107491)

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
PRAI pfam00697
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
24-220 5.77e-82

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


:

Pssm-ID: 395566  Cd Length: 193  Bit Score: 242.64  E-value: 5.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971   24 AAECALDSDADLLGIICVPN-RKRTIDPVIARKISSLVKAYKNSSGTPKYLVGVFRNQPKEDVLALVNDYGIDIVQLHGD 102
Cdd:pfam00697   1 AKICGLTRLSDVKAAVKAGAdYLGLIFSESSKRQVSPEQAQELRSPVPLLLVGVFVNQPIDDVLRIAQVLGLDVVQLHGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  103 EsWQEYQEFL--GLPVIKRLVFPKDCNILLSAaSQKPHSFIPLFDSEAGGTGELLDWNSISDWVGRQespesLHFMLAGG 180
Cdd:pfam00697  81 E-DQEYENLLptGVPVIKAIWVPDSVDTVDIA-RRADHVDLPLLDSGAGGTGELFDWSLVSKWLKSG-----LKVILAGG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 398364971  181 LTPENVGDALRLNGVIGVDVSGGVETNGVKDSNKIANFVK 220
Cdd:pfam00697 154 LNPDNVVEAIKTPGVIGVDVSSGVETNGIKDLNKIRKFVQ 193
 
Name Accession Description Interval E-value
PRAI pfam00697
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
24-220 5.77e-82

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


Pssm-ID: 395566  Cd Length: 193  Bit Score: 242.64  E-value: 5.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971   24 AAECALDSDADLLGIICVPN-RKRTIDPVIARKISSLVKAYKNSSGTPKYLVGVFRNQPKEDVLALVNDYGIDIVQLHGD 102
Cdd:pfam00697   1 AKICGLTRLSDVKAAVKAGAdYLGLIFSESSKRQVSPEQAQELRSPVPLLLVGVFVNQPIDDVLRIAQVLGLDVVQLHGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  103 EsWQEYQEFL--GLPVIKRLVFPKDCNILLSAaSQKPHSFIPLFDSEAGGTGELLDWNSISDWVGRQespesLHFMLAGG 180
Cdd:pfam00697  81 E-DQEYENLLptGVPVIKAIWVPDSVDTVDIA-RRADHVDLPLLDSGAGGTGELFDWSLVSKWLKSG-----LKVILAGG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 398364971  181 LTPENVGDALRLNGVIGVDVSGGVETNGVKDSNKIANFVK 220
Cdd:pfam00697 154 LNPDNVVEAIKTPGVIGVDVSSGVETNGIKDLNKIRKFVQ 193
PRAI cd00405
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ...
 14-222 7.70e-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: 7.70e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  14 VKVCGLQSTEAAECALDSDADLLGIICVPNRKRTIDPVIARKISSLVKAYKNssgtpkyLVGVFRNQPKEDVLALVNDYG 93
Cdd:cd00405    1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVK-------RVGVFVNEDLEEILEIAEELG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  94 IDIVQLHGDESWQEYQEF---LGLPVIKRLVFPKDCNILLSAASQKPHSFIpLFDSE----AGGTGELLDWNSISDWVGR 166
Cdd:cd00405   74 LDVVQLHGDESPEYCAQLrarLGLPVIKAIRVKDEEDLEKAAAYAGEVDAI-LLDSKsgggGGGTGKTFDWSLLRGLASR 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398364971 167 qespesLHFMLAGGLTPENVGDALRLNGVIGVDVSGGVETN-GVKDSNKIANFVKNA 222
Cdd:cd00405  153 ------KPVILAGGLTPDNVAEAIRLVRPYGVDVSSGVETSpGIKDPEKIRAFIEAA 203
TrpF COG0135
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ...
 12-224 4.37e-62

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: 192.66  E-value: 4.37e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  12 PLVKVCGLQSTEAAECALDSDADLLGIICVPNRKRTIDPVIARKISSLVKAYKNSsgtpkylVGVFRNQPKEDVLALVND 91
Cdd:COG0135    2 TRVKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPPFVKK-------VGVFVNADPEEILEIVEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  92 YGIDIVQLHGDESWQEYQEF---LGLPVIKRLVFPKDCNILLSAASQKPHSFIpLFDS----EAGGTGELLDWNSISDWV 164
Cdd:COG0135   75 VGLDAVQLHGDESPEYCAALrerLGLPVIKAIRVGDGADLEEAAAYAPVADAL-LLDAkvpgLYGGTGKTFDWSLLAGLA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364971 165 GRqespesLHFMLAGGLTPENVGDALRLNGVIGVDVSGGVET-NGVKDSNKIANFVKNAKK 224
Cdd:COG0135  154 LP------KPVILAGGLTPENVAEAIRLVRPYGVDVSSGVESaPGVKDPDKIRAFVEAVRA 208
PRK01222 PRK01222
phosphoribosylanthranilate isomerase;
14-224 3.98e-51

phosphoribosylanthranilate isomerase;


Pssm-ID: 234923  Cd Length: 210  Bit Score: 164.59  E-value: 3.98e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  14 VKVCGLQSTEAAECALDSDADLLGIICVPNRKRTIDPVIARKISSLVKAYKNssgtpkyLVGVFRNQPKEDVLALVNDYG 93
Cdd:PRK01222   5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAALPPFVK-------VVGVFVNASDEEIDEIVETVP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  94 IDIVQLHGDESwQEYQEFL----GLPVIKrlVFP-KDCNILLSAASQKPHSFIPLFDS---EAGGTGELLDWNSISDWVG 165
Cdd:PRK01222  78 LDLLQLHGDET-PEFCRQLkrryGLPVIK--ALRvRSAGDLEAAAAYYGDADGLLLDAyvgLPGGTGKTFDWSLLPAGLA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971 166 RQespeslhFMLAGGLTPENVGDALRLNGVIGVDVSGGVET-NGVKDSNKIANFVKNAKK 224
Cdd:PRK01222 155 KP-------WILAGGLNPDNVAEAIRQVRPYGVDVSSGVESaPGIKDPEKIRAFIEAVKS 207
 
Name Accession Description Interval E-value
PRAI pfam00697
N-(5'phosphoribosyl)anthranilate (PRA) isomerase;
24-220 5.77e-82

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


Pssm-ID: 395566  Cd Length: 193  Bit Score: 242.64  E-value: 5.77e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971   24 AAECALDSDADLLGIICVPN-RKRTIDPVIARKISSLVKAYKNSSGTPKYLVGVFRNQPKEDVLALVNDYGIDIVQLHGD 102
Cdd:pfam00697   1 AKICGLTRLSDVKAAVKAGAdYLGLIFSESSKRQVSPEQAQELRSPVPLLLVGVFVNQPIDDVLRIAQVLGLDVVQLHGD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  103 EsWQEYQEFL--GLPVIKRLVFPKDCNILLSAaSQKPHSFIPLFDSEAGGTGELLDWNSISDWVGRQespesLHFMLAGG 180
Cdd:pfam00697  81 E-DQEYENLLptGVPVIKAIWVPDSVDTVDIA-RRADHVDLPLLDSGAGGTGELFDWSLVSKWLKSG-----LKVILAGG 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 398364971  181 LTPENVGDALRLNGVIGVDVSGGVETNGVKDSNKIANFVK 220
Cdd:pfam00697 154 LNPDNVVEAIKTPGVIGVDVSSGVETNGIKDLNKIRKFVQ 193
PRAI cd00405
Phosphoribosylanthranilate isomerase (PRAI) catalyzes the fourth step of the tryptophan ...
 14-222 7.70e-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: 7.70e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  14 VKVCGLQSTEAAECALDSDADLLGIICVPNRKRTIDPVIARKISSLVKAYKNssgtpkyLVGVFRNQPKEDVLALVNDYG 93
Cdd:cd00405    1 VKICGITTLEDALAAAEAGADAIGFIFAPKSPRYVSPEQAREIVAALPPFVK-------RVGVFVNEDLEEILEIAEELG 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  94 IDIVQLHGDESWQEYQEF---LGLPVIKRLVFPKDCNILLSAASQKPHSFIpLFDSE----AGGTGELLDWNSISDWVGR 166
Cdd:cd00405   74 LDVVQLHGDESPEYCAQLrarLGLPVIKAIRVKDEEDLEKAAAYAGEVDAI-LLDSKsgggGGGTGKTFDWSLLRGLASR 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 398364971 167 qespesLHFMLAGGLTPENVGDALRLNGVIGVDVSGGVETN-GVKDSNKIANFVKNA 222
Cdd:cd00405  153 ------KPVILAGGLTPDNVAEAIRLVRPYGVDVSSGVETSpGIKDPEKIRAFIEAA 203
TrpF COG0135
Phosphoribosylanthranilate isomerase [Amino acid transport and metabolism]; ...
 12-224 4.37e-62

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: 192.66  E-value: 4.37e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  12 PLVKVCGLQSTEAAECALDSDADLLGIICVPNRKRTIDPVIARKISSLVKAYKNSsgtpkylVGVFRNQPKEDVLALVND 91
Cdd:COG0135    2 TRVKICGLTRPEDARAAVEAGADALGFVFYPKSPRYVSPEQAAELAAALPPFVKK-------VGVFVNADPEEILEIVEA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  92 YGIDIVQLHGDESWQEYQEF---LGLPVIKRLVFPKDCNILLSAASQKPHSFIpLFDS----EAGGTGELLDWNSISDWV 164
Cdd:COG0135   75 VGLDAVQLHGDESPEYCAALrerLGLPVIKAIRVGDGADLEEAAAYAPVADAL-LLDAkvpgLYGGTGKTFDWSLLAGLA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364971 165 GRqespesLHFMLAGGLTPENVGDALRLNGVIGVDVSGGVET-NGVKDSNKIANFVKNAKK 224
Cdd:COG0135  154 LP------KPVILAGGLTPENVAEAIRLVRPYGVDVSSGVESaPGVKDPDKIRAFVEAVRA 208
PRK01222 PRK01222
phosphoribosylanthranilate isomerase;
14-224 3.98e-51

phosphoribosylanthranilate isomerase;


Pssm-ID: 234923  Cd Length: 210  Bit Score: 164.59  E-value: 3.98e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  14 VKVCGLQSTEAAECALDSDADLLGIICVPNRKRTIDPVIARKISSLVKAYKNssgtpkyLVGVFRNQPKEDVLALVNDYG 93
Cdd:PRK01222   5 VKICGITTPEDAEAAAELGADAIGFVFYPKSPRYVSPEQAAELAAALPPFVK-------VVGVFVNASDEEIDEIVETVP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  94 IDIVQLHGDESwQEYQEFL----GLPVIKrlVFP-KDCNILLSAASQKPHSFIPLFDS---EAGGTGELLDWNSISDWVG 165
Cdd:PRK01222  78 LDLLQLHGDET-PEFCRQLkrryGLPVIK--ALRvRSAGDLEAAAAYYGDADGLLLDAyvgLPGGTGKTFDWSLLPAGLA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971 166 RQespeslhFMLAGGLTPENVGDALRLNGVIGVDVSGGVET-NGVKDSNKIANFVKNAKK 224
Cdd:PRK01222 155 KP-------WILAGGLNPDNVAEAIRQVRPYGVDVSSGVESaPGIKDPEKIRAFIEAVKS 207
PLN02363 PLN02363
phosphoribosylanthranilate isomerase
 8-223 1.52e-42

phosphoribosylanthranilate isomerase


Pssm-ID: 215207  Cd Length: 256  Bit Score: 144.23  E-value: 1.52e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971   8 GSSGPLVKVCGLQSTEAAECALDSDADLLGIICVPNRKRTIDPVIARKISSLVKAYKNSSgtpkylVGVFRNQPKEDVLA 87
Cdd:PLN02363  43 GKDRPLVKMCGITSARDAAMAVEAGADFIGMILWPKSKRSISLSVAKEISQVAREGGAKP------VGVFVDDDANTILR 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  88 LVNDYGIDIVQLHGDESwqeYQEFLGLPVIKRLVFPKDCN---ILLSAASQKPHSFIP--LFDSEAGGTGELLDWNSISD 162
Cdd:PLN02363 117 AADSSDLELVQLHGNGS---RAAFSRLVRERKVIYVLNANedgKLLNVVPEEDCHLADwiLVDSATGGSGKGFNWQNFKL 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398364971 163 WVGRQESPeslhFMLAGGLTPENVGDALRLNGVIGVDVSGGVE-TNGV-KDSNKIANFVKNAK 223
Cdd:PLN02363 194 PSVRSRNG----WLLAGGLTPENVHEAVSLLKPTGVDVSSGICgPDGIrKDPSKISSFISAVK 252
PRK09427 PRK09427
bifunctional indole-3-glycerol-phosphate synthase TrpC/phosphoribosylanthranilate isomerase ...
 15-218 2.28e-42

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


Pssm-ID: 236509 [Multi-domain]  Cd Length: 454  Bit Score: 148.42  E-value: 2.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  15 KVCGLQSTEAAECALDSDADLLGIICVPNRKRTIDPVIARKISSlvkayknssGTPKYLVGVFRNQPKEDVLALVNDYGI 94
Cdd:PRK09427 260 KVCGLTRPQDAKAAYDAGAVYGGLIFVEKSPRYVSLEQAQEIIA---------AAPLRYVGVFRNADIEDIVDIAKQLSL 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  95 DIVQLHGDESwQEYQEFLglpvikRLVFPKDCNI--LLSAASQKPHSFIP-----LFDSEAGGTGELLDWNSIsdwvgrq 167
Cdd:PRK09427 331 AAVQLHGDED-QAYIDAL------REALPKTCQIwkAISVGDTLPARDLQhvdryLLDNGQGGTGQTFDWSLL------- 396

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 398364971 168 eSPESLH-FMLAGGLTPENVGDALRLnGVIGVDVSGGVETN-GVKDSNKIANF 218
Cdd:PRK09427 397 -PGQSLDnVLLAGGLNPDNCQQAAQL-GCAGLDFNSGVESApGIKDAQKLASV 447
PRK13803 PRK13803
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
 12-224 5.61e-25

bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional


Pssm-ID: 237513 [Multi-domain]  Cd Length: 610  Bit Score: 102.20  E-value: 5.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  12 PLVKVCGLQSTEAAECALDSDADLLGIICVPNRKRTI-DPVIARKissLVKAYKNSSGTPkylVGVFRNQPKEDVLALVN 90
Cdd:PRK13803   3 PKIKICGIKDSALISKAVDMLPDFIGFIFYEKSPRFVgNKFLAPN---LEKAIRKAGGRP---VGVFVNESAKAMLKFSK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  91 DYGIDIVQLHGDESWQE--YQEFLGLPVIKRL-VFPKDCNILLSAAS-QKPHSFIPLFDSEA---GGTGELLDWNSISDW 163
Cdd:PRK13803  77 KNGIDFVQLHGAESKAEpaYCQRIYKKSIKKIgSFLIDDAFGFEVLDeYRDHVKYFLFDNKTkiyGGSGKSFDWEKFYNY 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364971 164 VGRqespesLHFMLAGGLTPENVGDALRLN--GVIGVDVSGGVE-TNGVKDSNKIANFVKNAKK 224
Cdd:PRK13803 157 NFK------FPFFLSGGLSPTNFDRIINLThpQILGIDVSSGFEdSPGNKKLTLLKSFITNVKK 214
PRK13958 PRK13958
N-(5'-phosphoribosyl)anthranilate isomerase; Provisional
 14-223 9.57e-22

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


Pssm-ID: 184418  Cd Length: 207  Bit Score: 88.63  E-value: 9.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  14 VKVCGLQSTEAAECALDSDADLLGIICVPNRKRTIDPVIARKISSLVKAYKnssgtpkYLVGVFRNQPKEDVLALVNDYG 93
Cdd:PRK13958   3 LKFCGFTTIKDVTAASQLPIDAIGFIHYEKSKRHQTITQIKKLASAVPNHI-------DKVCVVVNPDLTTIEHILSNTS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364971  94 IDIVQLHGDESWQEYQE----FLGLPVIKRLvfPKDCNILLSAASQKPH--SFIPLFDSEA-GGTGELLDWNSIsdwvgr 166
Cdd:PRK13958  76 INTIQLHGTESIDFIQEikkkYSSIKIIKAL--PADENIIQNINKYKGFvdLFIIDTPSVSyGGTGQTYDWTIL------ 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 398364971 167 qESPESLHFMLAGGLTPENVG--DALRLNGViGVDVSGGVETNGVKDSNK---IANFVKNAK 223
Cdd:PRK13958 148 -KHIKDIPYLIAGGINSENIQtvEQLKLSHQ-GYDIASGIETNGRKDINKmtaIVNIVKGDR 207
 
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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