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Conserved domains on  [gi|490217195|ref|WP_004115573|]
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dihydrofolate reductase [Gardnerella vaginalis]

Protein Classification

dihydrofolate reductase family protein( domain architecture ID 106942)

dihydrofolate reductase family protein; similar to Lacticaseibacillus rhamnosus dihydrofolate reductase which reduces dihydrofolic acid to tetrahydrofolic acid, using NADPH as electron donor

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DHFR super family cl17279
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
7-201 2.20e-51

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


The actual alignment was detected with superfamily member pfam00186:

Pssm-ID: 473077 [Multi-domain]  Cd Length: 159  Bit Score: 163.10  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195    7 VRLIWGQAydlegRVGAMGVNGGMPWRLSTDLRYFKAMTISCPVIMGRGTWDSMPekfRPLPGRENIVVSRNPDFNSDGA 86
Cdd:pfam00186   2 ISLIAAMD-----ENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIG---RPLPGRKNIVLTRNPDYKVDGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195   87 KSFTSIEEAICYAKKWIEdnpiehvdssdlpkdgsaVWIIGGGAIFREVIEsqIVDAAYVTQIDTRVEADTFAPNIqklv 166
Cdd:pfam00186  74 EVVHSLEEALALAAEAEE------------------IFIIGGAEIYAQALP--LADRLYITEIDAEFDGDTFFPEI---- 129
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 490217195  167 DDGLWKVArdcdWQESTIKVGANQFNtkYKFMVYE 201
Cdd:pfam00186 130 DPSEWQLV----SREEHEADEKNPYP--YTFVTYE 158
 
Name Accession Description Interval E-value
DHFR_1 pfam00186
Dihydrofolate reductase;
7-201 2.20e-51

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 163.10  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195    7 VRLIWGQAydlegRVGAMGVNGGMPWRLSTDLRYFKAMTISCPVIMGRGTWDSMPekfRPLPGRENIVVSRNPDFNSDGA 86
Cdd:pfam00186   2 ISLIAAMD-----ENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIG---RPLPGRKNIVLTRNPDYKVDGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195   87 KSFTSIEEAICYAKKWIEdnpiehvdssdlpkdgsaVWIIGGGAIFREVIEsqIVDAAYVTQIDTRVEADTFAPNIqklv 166
Cdd:pfam00186  74 EVVHSLEEALALAAEAEE------------------IFIIGGAEIYAQALP--LADRLYITEIDAEFDGDTFFPEI---- 129
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 490217195  167 DDGLWKVArdcdWQESTIKVGANQFNtkYKFMVYE 201
Cdd:pfam00186 130 DPSEWQLV----SREEHEADEKNPYP--YTFVTYE 158
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
7-201 2.28e-47

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


Pssm-ID: 238127 [Multi-domain]  Cd Length: 158  Bit Score: 153.06  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195   7 VRLIWgqAYDLEGrvgAMGVNGGMPWRLSTDLRYFKAMTISCPVIMGRGTWDSMPEkfRPLPGRENIVVSRNPDFNS-DG 85
Cdd:cd00209    1 ISLIV--AVDENG---VIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPR--RPLPGRTNIVLSRQLDYQDaEG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  86 AKSFTSIEEAICYAKKWIEDnpiehvdssdlpkdgsaVWIIGGGAIFREVIESqiVDAAYVTQIDTRVEADTFAPNIqkl 165
Cdd:cd00209   74 VEVVHSLEEALELAENTVEE-----------------IFVIGGAEIYKQALPY--ADRLYLTRIHAEFEGDTFFPEI--- 131
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 490217195 166 vddgLWKvardcDWQESTIKVGANQFNTKYKFMVYE 201
Cdd:cd00209  132 ----DES-----EWELVSEEEVFEEDGYSYTFETYE 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
21-202 1.64e-33

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 125.17  E-value: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  21 VGAMGVNGGMPWRLSTDLRYFKAMTISCP-------------VIMGRGTWDSMPEKFRPLPGRENIVVSRN--PDFNSDG 85
Cdd:PTZ00164  19 KRGIGIGNSLPWHIPEDMKFFSKITTYVReekyekspkkqnaVIMGRKTWESIPKKFRPLKNRINVVLSRTltEEEADPG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  86 AKSFTSIEEAICYAKkwiEDNPIEhvdssdlpkdgsAVWIIGGGAIFREVIESQIVDAAYVTQIDTRVEADTFAPNIqkl 165
Cdd:PTZ00164  99 VLVFGSLEDALRLLA---EDLSIE------------KIFIIGGASVYREALSANLLDKIYLTRVNSEYECDVFFPKI--- 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490217195 166 vDDGLWKVARDCDWQESTikvganqfNTKYKFMVYEP 202
Cdd:PTZ00164 161 -PESFFIVAIVSQTFSTN--------GTSYDFVIYEK 188
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
8-162 1.56e-25

Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440032 [Multi-domain]  Cd Length: 168  Bit Score: 97.23  E-value: 1.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195   8 RLIWGQAYDLEGRVGamGVNGGMPW--RLSTDLRYFKAMTISC-PVIMGRGTWDSMPEKF--RPLPGRENIVVSRNPD-F 81
Cdd:COG0262    2 KLILIVAVSLDGVIG--GPDGDLPWlfPDPEDLAHFKELTAGAdAVLMGRKTYESIAGYWptRPLPGRPKIVLSRTLDeA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  82 NSDGAKSFT-SIEEAICYAKKwiednpiehvdssdlpKDGSAVWIIGGGAIFREVIESQIVDAAYVTQIDTRV-EADTFA 159
Cdd:COG0262   80 DWEGVTVVSgDLEEALAALKA----------------AGGKDIWVIGGGELYRQLLPAGLVDELYLTVVPVVLgEGDRLF 143

                 ...
gi 490217195 160 PNI 162
Cdd:COG0262  144 PEL 146
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
22-184 1.37e-11

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 60.35  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  22 GAMGVNGGMPWR-LSTDLRYFKAMTISCPVIMGRGTWDSMpekFRPLPGRENIVVSRN-PDFNSDGAKSFTSIEEAICYA 99
Cdd:NF041386  13 GVIGRDGELPWPsIPADKRQYRERVADDPVILGRRTFESM---RDDLPGSAQIVLSRSeREFDVETAHHAGGVDEAIEIA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195 100 KKwiednpiehvdssdlpKDGSAVWIIGGGAIFrEVIESQiVDAAYVTQIDTRVEADTFAPNIqklvDDGLWKVARDCDW 179
Cdd:NF041386  90 ES----------------LGAERAYVLGGAAIY-ELFQPH-VDRMVLSRVPGEYEGDAYYPEW----DEDEWELVEETEY 147

                 ....*
gi 490217195 180 QESTI 184
Cdd:NF041386 148 DGFTL 152
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
15-163 1.13e-05

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 44.26  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  15 YDLEGRVGAMGVNGGMPWRLSTDLRYFKAMTISCPVIMGRGTWDSMPekFRPLPGRENIVVSRNPDFNSDGAKSFTSIEE 94
Cdd:NF041668  21 VNAEDDMGHFGNSGDDDVNLMGDKKHEKIPTMDDKNRIGIKLTENIP--VRADGAIICHSKEDNKNYLADGAIECHIHED 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490217195  95 AICYAKKWIEDNPIEhvdssdlpkdgsavwIIGGgaIFREVIESQIVDAAYVTQIDTRVEADTFAPNIQ 163
Cdd:NF041668  99 GGISAFEMFIDEPIH---------------LHGG--IIAEEFEGDEVMIEHDTIIDECFDGADGMPDED 150
 
Name Accession Description Interval E-value
DHFR_1 pfam00186
Dihydrofolate reductase;
7-201 2.20e-51

Dihydrofolate reductase;


Pssm-ID: 425512 [Multi-domain]  Cd Length: 159  Bit Score: 163.10  E-value: 2.20e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195    7 VRLIWGQAydlegRVGAMGVNGGMPWRLSTDLRYFKAMTISCPVIMGRGTWDSMPekfRPLPGRENIVVSRNPDFNSDGA 86
Cdd:pfam00186   2 ISLIAAMD-----ENGVIGKDNDLPWHLPADLKHFKKLTTGKPVIMGRKTFESIG---RPLPGRKNIVLTRNPDYKVDGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195   87 KSFTSIEEAICYAKKWIEdnpiehvdssdlpkdgsaVWIIGGGAIFREVIEsqIVDAAYVTQIDTRVEADTFAPNIqklv 166
Cdd:pfam00186  74 EVVHSLEEALALAAEAEE------------------IFIIGGAEIYAQALP--LADRLYITEIDAEFDGDTFFPEI---- 129
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 490217195  167 DDGLWKVArdcdWQESTIKVGANQFNtkYKFMVYE 201
Cdd:pfam00186 130 DPSEWQLV----SREEHEADEKNPYP--YTFVTYE 158
DHFR cd00209
Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with ...
7-201 2.28e-47

Dihydrofolate reductase (DHFR). Reduces 7,8-dihydrofolate to 5,6,7,8-tetrahydrofolate with NADPH as a cofactor. This is an essential step in the biosynthesis of deoxythymidine phosphate since 5,6,7,8-tetrahydrofolate is required to regenerate 5,10-methylenetetrahydrofolate which is then utilized by thymidylate synthase. Inhibition of DHFR interrupts thymidilate synthesis and DNA replication, inhibitors of DHFR (such as Methotrexate) are used in cancer chemotherapy. 5,6,7,8-tetrahydrofolate also is involved in glycine, serine, and threonine metabolism and aminoacyl-tRNA biosynthesis.


Pssm-ID: 238127 [Multi-domain]  Cd Length: 158  Bit Score: 153.06  E-value: 2.28e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195   7 VRLIWgqAYDLEGrvgAMGVNGGMPWRLSTDLRYFKAMTISCPVIMGRGTWDSMPEkfRPLPGRENIVVSRNPDFNS-DG 85
Cdd:cd00209    1 ISLIV--AVDENG---VIGKDNKLPWHLPEDLKHFKKTTTGNPVIMGRKTFESIPR--RPLPGRTNIVLSRQLDYQDaEG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  86 AKSFTSIEEAICYAKKWIEDnpiehvdssdlpkdgsaVWIIGGGAIFREVIESqiVDAAYVTQIDTRVEADTFAPNIqkl 165
Cdd:cd00209   74 VEVVHSLEEALELAENTVEE-----------------IFVIGGAEIYKQALPY--ADRLYLTRIHAEFEGDTFFPEI--- 131
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 490217195 166 vddgLWKvardcDWQESTIKVGANQFNTKYKFMVYE 201
Cdd:cd00209  132 ----DES-----EWELVSEEEVFEEDGYSYTFETYE 158
PTZ00164 PTZ00164
bifunctional dihydrofolate reductase-thymidylate synthase; Provisional
21-202 1.64e-33

bifunctional dihydrofolate reductase-thymidylate synthase; Provisional


Pssm-ID: 240299 [Multi-domain]  Cd Length: 514  Bit Score: 125.17  E-value: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  21 VGAMGVNGGMPWRLSTDLRYFKAMTISCP-------------VIMGRGTWDSMPEKFRPLPGRENIVVSRN--PDFNSDG 85
Cdd:PTZ00164  19 KRGIGIGNSLPWHIPEDMKFFSKITTYVReekyekspkkqnaVIMGRKTWESIPKKFRPLKNRINVVLSRTltEEEADPG 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  86 AKSFTSIEEAICYAKkwiEDNPIEhvdssdlpkdgsAVWIIGGGAIFREVIESQIVDAAYVTQIDTRVEADTFAPNIqkl 165
Cdd:PTZ00164  99 VLVFGSLEDALRLLA---EDLSIE------------KIFIIGGASVYREALSANLLDKIYLTRVNSEYECDVFFPKI--- 160
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 490217195 166 vDDGLWKVARDCDWQESTikvganqfNTKYKFMVYEP 202
Cdd:PTZ00164 161 -PESFFIVAIVSQTFSTN--------GTSYDFVIYEK 188
FolA COG0262
Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part ...
8-162 1.56e-25

Dihydrofolate reductase [Coenzyme transport and metabolism]; Dihydrofolate reductase is part of the Pathway/BioSystem: Folate biosynthesis


Pssm-ID: 440032 [Multi-domain]  Cd Length: 168  Bit Score: 97.23  E-value: 1.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195   8 RLIWGQAYDLEGRVGamGVNGGMPW--RLSTDLRYFKAMTISC-PVIMGRGTWDSMPEKF--RPLPGRENIVVSRNPD-F 81
Cdd:COG0262    2 KLILIVAVSLDGVIG--GPDGDLPWlfPDPEDLAHFKELTAGAdAVLMGRKTYESIAGYWptRPLPGRPKIVLSRTLDeA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  82 NSDGAKSFT-SIEEAICYAKKwiednpiehvdssdlpKDGSAVWIIGGGAIFREVIESQIVDAAYVTQIDTRV-EADTFA 159
Cdd:COG0262   80 DWEGVTVVSgDLEEALAALKA----------------AGGKDIWVIGGGELYRQLLPAGLVDELYLTVVPVVLgEGDRLF 143

                 ...
gi 490217195 160 PNI 162
Cdd:COG0262  144 PEL 146
folA PRK10769
type 3 dihydrofolate reductase;
24-161 7.61e-24

type 3 dihydrofolate reductase;


Pssm-ID: 182714 [Multi-domain]  Cd Length: 159  Bit Score: 92.49  E-value: 7.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  24 MGVNGGMPWRLSTDLRYFKAMTISCPVIMGRGTWDSMPekfRPLPGRENIVVSRNPDfNSDGAKSFTSIEEAICYAkkwi 103
Cdd:PRK10769  14 IGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESIG---RPLPGRKNIVISSQPG-TDDRVTWVKSVDEALAAA---- 85
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490217195 104 ednpiehvdssdlpKDGSAVWIIGGGAIFREVIESqiVDAAYVTQIDTRVEADTFAPN 161
Cdd:PRK10769  86 --------------GDVPEIMVIGGGRVYEQFLPK--AQRLYLTHIDAEVEGDTHFPD 127
dihyfolred_HdrA_Halo NF041386
dihydrofolate reductase HdrA;
22-184 1.37e-11

dihydrofolate reductase HdrA;


Pssm-ID: 469277 [Multi-domain]  Cd Length: 158  Bit Score: 60.35  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  22 GAMGVNGGMPWR-LSTDLRYFKAMTISCPVIMGRGTWDSMpekFRPLPGRENIVVSRN-PDFNSDGAKSFTSIEEAICYA 99
Cdd:NF041386  13 GVIGRDGELPWPsIPADKRQYRERVADDPVILGRRTFESM---RDDLPGSAQIVLSRSeREFDVETAHHAGGVDEAIEIA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195 100 KKwiednpiehvdssdlpKDGSAVWIIGGGAIFrEVIESQiVDAAYVTQIDTRVEADTFAPNIqklvDDGLWKVARDCDW 179
Cdd:NF041386  90 ES----------------LGAERAYVLGGAAIY-ELFQPH-VDRMVLSRVPGEYEGDAYYPEW----DEDEWELVEETEY 147

                 ....*
gi 490217195 180 QESTI 184
Cdd:NF041386 148 DGFTL 152
trim_DfrL NF041668
trimethoprim-resistant dihydrofolate reductase DfrL;
15-163 1.13e-05

trimethoprim-resistant dihydrofolate reductase DfrL;


Pssm-ID: 469550 [Multi-domain]  Cd Length: 176  Bit Score: 44.26  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195  15 YDLEGRVGAMGVNGGMPWRLSTDLRYFKAMTISCPVIMGRGTWDSMPekFRPLPGRENIVVSRNPDFNSDGAKSFTSIEE 94
Cdd:NF041668  21 VNAEDDMGHFGNSGDDDVNLMGDKKHEKIPTMDDKNRIGIKLTENIP--VRADGAIICHSKEDNKNYLADGAIECHIHED 98
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490217195  95 AICYAKKWIEDNPIEhvdssdlpkdgsavwIIGGgaIFREVIESQIVDAAYVTQIDTRVEADTFAPNIQ 163
Cdd:NF041668  99 GGISAFEMFIDEPIH---------------LHGG--IIAEEFEGDEVMIEHDTIIDECFDGADGMPDED 150
scpA PRK00478
segregation and condensation protein ScpA;
7-137 1.12e-03

segregation and condensation protein ScpA;


Pssm-ID: 234776 [Multi-domain]  Cd Length: 505  Bit Score: 39.14  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490217195   7 VRLIWGQAYDLegrvgAMGVNGGMPWRLSTDLRYFKAMTISCPVIMGRGTWDSMPEKFRPlpgRENIVVSRNPDF---NS 83
Cdd:PRK00478   2 IKLIWCEDLNF-----GIAKNNQIPWKIDEELNHFHQTTTNHTIVMGYNTFQAMNKILAN---QANIVISKKHQRelkNN 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490217195  84 DGAKSFTSIEEAicyakkwiednpIEHVDSSDLpkdgsavWIIGGGAIFREVIE 137
Cdd:PRK00478  74 NELFVFNDLKKL------------LIDFSNVDL-------FIIGGKKTIEQFIK 108
 
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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