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Conserved domains on  [gi|16078965|ref|NP_389786|]
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putative transcriptional regulator (AraC/XylS family) [Bacillus subtilis subsp. subtilis str. 168]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_YobQ-like_N cd07003
Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes ...
 12-79 3.24e-32

Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes bacterial proteins homologous to Bacillus subtilis YobQ and Photobacterium leiognathi LumQ, both uncharacterized proteins thought to be DNA-binding proteins that may function as AraC/XylS family transcriptional regulators. YobQ has an N-terminal cupin beta barrel domain (represented by this alignment model) and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


:

Pssm-ID: 380407 [Multi-domain]  Cd Length: 66  Bit Score: 112.10  E-value: 3.24e-32
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16078965  12 EKRTYTRLYHSHKHAysQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDVP 79
Cdd:cd07003   1 RTYSHDQSSHSHEHA--QLVLPLSGSLELEVEGRGSRVKPDIGLYIPPNAEHRFAGSSDNRCLVLDLP 66
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
4-236 1.12e-24

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 98.31  E-value: 1.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965   4 DSLQEIICEKRTYTRLYHSHKHAYSQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDVPLHAM 83
Cdd:COG2207  22 LLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  84 KIDEYRAGSGIEAALDPFWSSIRYLLTEEAKAGTANSLHMLVQYIKEKLQSHSYASIAYIHSHLFERLTIKKLAEIEHYH 163
Cdd:COG2207 102 LLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLS 181

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078965 164 PAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWFTKSTGMPPRLYRNTL 236
Cdd:COG2207 182 PRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRL 254
 
Name Accession Description Interval E-value
cupin_YobQ-like_N cd07003
Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes ...
 12-79 3.24e-32

Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes bacterial proteins homologous to Bacillus subtilis YobQ and Photobacterium leiognathi LumQ, both uncharacterized proteins thought to be DNA-binding proteins that may function as AraC/XylS family transcriptional regulators. YobQ has an N-terminal cupin beta barrel domain (represented by this alignment model) and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380407 [Multi-domain]  Cd Length: 66  Bit Score: 112.10  E-value: 3.24e-32
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16078965  12 EKRTYTRLYHSHKHAysQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDVP 79
Cdd:cd07003   1 RTYSHDQSSHSHEHA--QLVLPLSGSLELEVEGRGSRVKPDIGLYIPPNAEHRFAGSSDNRCLVLDLP 66
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
4-236 1.12e-24

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 98.31  E-value: 1.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965   4 DSLQEIICEKRTYTRLYHSHKHAYSQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDVPLHAM 83
Cdd:COG2207  22 LLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  84 KIDEYRAGSGIEAALDPFWSSIRYLLTEEAKAGTANSLHMLVQYIKEKLQSHSYASIAYIHSHLFERLTIKKLAEIEHYH 163
Cdd:COG2207 102 LLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLS 181

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078965 164 PAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWFTKSTGMPPRLYRNTL 236
Cdd:COG2207 182 PRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRL 254
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
150-233 1.73e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 92.62  E-value: 1.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965    150 RLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWFTKSTGMPP 229
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 16078965    230 RLYR 233
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
156-234 1.52e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 79.94  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965   156 LAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMER-NETLTVVSEALGFQNLSSFTRWFTKSTGMPPRLYRN 234
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 129-233 3.06e-14

YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only one protein with the YSIRK variant form of signal peptide (TIGR01168) were examined for conserved genes near that one tagged protein. This protein is found adjacent to at various classes of repetitive or low-complexity YSIRK proteins (whether unique in genome or not), in a range of species (Enterococcus faecalis X98, Ruminococcus torques, Coprobacillus sp. D7, Lysinibacillus fusiformis ZC1, Streptococcus equi subsp. equi 4047, etc). The affliated YSIRK proteins include Streptococcal protective antigen (see ) and proteins with the Rib/alpha/Esp surface antigen repeat (see TIGR02331). The last quarter of this protein has an AraC family helix-turn-helix (HTH)transcriptional regulator domain.


Pssm-ID: 274977 [Multi-domain]  Cd Length: 383  Bit Score: 71.25  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965   129 KEKLQSHSY---ASIAYIHSHLFERLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMErNETLTVV 205
Cdd:TIGR04094 277 EISINHHSPlirAVIQYINLNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRS-QIPVSEV 355

                          90       100
                  ....*....|....*....|....*...
gi 16078965   206 SEALGFQNLSSFTRWFTKSTGMPPRLYR 233
Cdd:TIGR04094 356 SNELGFYDLSHFSRTFKKHTGVSPKQYQ 383
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
20-78 2.21e-09

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 53.31  E-value: 2.21e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16078965  20 YHSHKHAYSQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDV 78
Cdd:COG1917  36 TPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVV 94
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
137-235 5.97e-09

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 52.80  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  137 YASIAYIHSHLFERLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSS 216
Cdd:PRK11511  12 HSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQT 91

                         90
                 ....*....|....*....
gi 16078965  217 FTRWFTKSTGMPPRLYRNT 235
Cdd:PRK11511  92 LTRTFKNYFDVPPHKYRMT 110
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 22-78 7.86e-08

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 48.02  E-value: 7.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 16078965    22 SHKHAYS-QFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDV 78
Cdd:pfam07883  13 PHRHPGEdEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
30-66 2.75e-05

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 44.12  E-value: 2.75e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 16078965   30 FLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFR 66
Cdd:PRK11171  86 FLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLR 122
 
Name Accession Description Interval E-value
cupin_YobQ-like_N cd07003
Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes ...
 12-79 3.24e-32

Bacillus subtilis YobQ and related proteins, N-terminal cupin domain; This family includes bacterial proteins homologous to Bacillus subtilis YobQ and Photobacterium leiognathi LumQ, both uncharacterized proteins thought to be DNA-binding proteins that may function as AraC/XylS family transcriptional regulators. YobQ has an N-terminal cupin beta barrel domain (represented by this alignment model) and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380407 [Multi-domain]  Cd Length: 66  Bit Score: 112.10  E-value: 3.24e-32
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16078965  12 EKRTYTRLYHSHKHAysQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDVP 79
Cdd:cd07003   1 RTYSHDQSSHSHEHA--QLVLPLSGSLELEVEGRGSRVKPDIGLYIPPNAEHRFAGSSDNRCLVLDLP 66
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
4-236 1.12e-24

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 98.31  E-value: 1.12e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965   4 DSLQEIICEKRTYTRLYHSHKHAYSQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDVPLHAM 83
Cdd:COG2207  22 LLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLL 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  84 KIDEYRAGSGIEAALDPFWSSIRYLLTEEAKAGTANSLHMLVQYIKEKLQSHSYASIAYIHSHLFERLTIKKLAEIEHYH 163
Cdd:COG2207 102 LLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLS 181

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078965 164 PAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWFTKSTGMPPRLYRNTL 236
Cdd:COG2207 182 PRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRL 254
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
150-233 1.73e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 92.62  E-value: 1.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965    150 RLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWFTKSTGMPP 229
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 16078965    230 RLYR 233
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
156-234 1.52e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 79.94  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965   156 LAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMER-NETLTVVSEALGFQNLSSFTRWFTKSTGMPPRLYRN 234
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDtGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 140-235 3.54e-17

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 79.05  E-value: 3.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965 140 IAYIHSHLFERLTIKKLAE---------IEHyhpayysswFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALG 210
Cdd:COG4977 216 QAWMEANLEEPLSVDELARragmsprtlERR---------FRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACG 286

                        90       100
                ....*....|....*....|....*
gi 16078965 211 FQNLSSFTRWFTKSTGMPPRLYRNT 235
Cdd:COG4977 287 FGSASHFRRAFRRRFGVSPSAYRRR 311
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 129-233 3.06e-14

YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only one protein with the YSIRK variant form of signal peptide (TIGR01168) were examined for conserved genes near that one tagged protein. This protein is found adjacent to at various classes of repetitive or low-complexity YSIRK proteins (whether unique in genome or not), in a range of species (Enterococcus faecalis X98, Ruminococcus torques, Coprobacillus sp. D7, Lysinibacillus fusiformis ZC1, Streptococcus equi subsp. equi 4047, etc). The affliated YSIRK proteins include Streptococcal protective antigen (see ) and proteins with the Rib/alpha/Esp surface antigen repeat (see TIGR02331). The last quarter of this protein has an AraC family helix-turn-helix (HTH)transcriptional regulator domain.


Pssm-ID: 274977 [Multi-domain]  Cd Length: 383  Bit Score: 71.25  E-value: 3.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965   129 KEKLQSHSY---ASIAYIHSHLFERLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMErNETLTVV 205
Cdd:TIGR04094 277 EISINHHSPlirAVIQYINLNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRS-QIPVSEV 355

                          90       100
                  ....*....|....*....|....*...
gi 16078965   206 SEALGFQNLSSFTRWFTKSTGMPPRLYR 233
Cdd:TIGR04094 356 SNELGFYDLSHFSRTFKKHTGVSPKQYQ 383
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 140-234 4.17e-12

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 64.69  E-value: 4.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965 140 IAYIHSHLFERLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLmERNETLTVVSEALGFQNLSSFTR 219
Cdd:COG2169  90 CRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFGSLSRFYE 168

                        90
                ....*....|....*
gi 16078965 220 WFTKSTGMPPRLYRN 234
Cdd:COG2169 169 AFKKLLGMTPSAYRR 183
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
20-78 2.21e-09

Cupin domain protein related to quercetin dioxygenase [General function prediction only];


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 53.31  E-value: 2.21e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16078965  20 YHSHKHAYSQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDV 78
Cdd:COG1917  36 TPWHSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFRNLGDEPAVLLVV 94
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
20-78 5.67e-09

Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 52.45  E-value: 5.67e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16078965  20 YHSHKHAySQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDV 78
Cdd:COG0662  42 LHVHPHR-DEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLRNPGDEPLELLEV 99
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
137-235 5.97e-09

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 52.80  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  137 YASIAYIHSHLFERLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSS 216
Cdd:PRK11511  12 HSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQT 91

                         90
                 ....*....|....*....
gi 16078965  217 FTRWFTKSTGMPPRLYRNT 235
Cdd:PRK11511  92 LTRTFKNYFDVPPHKYRMT 110
PRK10371 PRK10371
transcriptional regulator MelR;
142-233 9.30e-09

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 54.83  E-value: 9.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  142 YIHSHLFERLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWF 221
Cdd:PRK10371 199 FIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTF 278

                         90
                 ....*....|..
gi 16078965  222 TKSTGMPPRLYR 233
Cdd:PRK10371 279 GKYVGMSPQQYR 290
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
19-78 7.80e-08

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 49.25  E-value: 7.80e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  19 LYHSHKHAYsQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDV 78
Cdd:COG3837  43 PYHAHSAEE-EFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLRNRGDEPARYLVV 101
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 22-78 7.86e-08

Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ('cupa' is the Latin term for a small barrel).


Pssm-ID: 462300 [Multi-domain]  Cd Length: 71  Bit Score: 48.02  E-value: 7.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 16078965    22 SHKHAYS-QFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDV 78
Cdd:pfam07883  13 PHRHPGEdEFFYVLEGEGELTVDGEEVVLKAGDSVYFPAGVPHRFRNTGDEPARLLDV 70
ftrA PRK09393
transcriptional activator FtrA; Provisional
 126-233 1.74e-07

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 51.12  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  126 QYIKEKLQSHSYASIA----YIHSHLFERLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNET 201
Cdd:PRK09393 206 QFVPRPVASRESDRLGplidWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALS 285

                         90       100       110
                 ....*....|....*....|....*....|..
gi 16078965  202 LTVVSEALGFQNLSSFTRWFTKSTGMPPRLYR 233
Cdd:PRK09393 286 IDQIAERAGFGSEESLRHHFRRRAATSPAAYR 317
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 17-78 2.28e-07

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


Pssm-ID: 380338 [Multi-domain]  Cd Length: 73  Bit Score: 47.09  E-value: 2.28e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078965  17 TRLYHSHKHAYsQFLFPLEGSIDLETE-GRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDV 78
Cdd:cd02208  11 SSPPHWHPEQD-EIFYVLSGEGELTLDdGETVELKAGDIVLIPPGVPHSFVNTSDEPAVFLVV 72
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
142-234 2.97e-07

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 49.97  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  142 YIHSHLFERLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWF 221
Cdd:PRK10572 191 YISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVF 270

                         90
                 ....*....|...
gi 16078965  222 TKSTGMPPRLYRN 234
Cdd:PRK10572 271 KKCTGASPSEFRA 283
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
171-233 4.61e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 49.52  E-value: 4.61e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16078965  171 FKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWFTKSTGMPPRLYR 233
Cdd:PRK13501 213 FRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYR 275
cupin_TM1459-like cd02222
Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial ...
 20-75 2.89e-06

Thermotoga maritima TM1459 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to Thermotoga maritima TM1459, a manganese-containing cupin that has been shown to cleave C=C bonds in the presence of alkylperoxide as oxidant in vitro. Its biological function is still unknown. This family also includes Halorhodospira halophila Hhal_0468. Structures of these proteins show a cupin fold with a conserved "jelly roll-like" beta-barrel fold that form a homodimer.


Pssm-ID: 380351 [Multi-domain]  Cd Length: 91  Bit Score: 44.36  E-value: 2.89e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  20 YHSHKHAYSQFlfPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNE----CLV 75
Cdd:cd02222  32 LHTHPWEHEVY--VLRGKGVVVIGGEEYPVKPGDVVYIPPNEPHQFRNTGDEPlgflCIV 89
cupin_UGlyAH_N cd02211
(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family ...
 30-69 4.47e-06

(S)-ureidoglycine aminohydrolase and related proteins, N-terminal cupin domain; This family includes the N-terminal cupin domain of (S)-ureidoglycine aminohydrolase (UGlyAH), an enzyme that converts (S)-ureidoglycine into (S)-ureidoglycolate and ammonia, providing the final substrate to the ureide pathway. The ureide pathway has recently been identified as the metabolic route of purine catabolism in plants and some bacteria where, uric acid, which is a major product of the early stage of purine catabolism, is degraded into glyoxylate and ammonia via stepwise reactions by seven different enzymes. Thus, this pathway has a possible physiological role in mobilization of purine ring nitrogen for further assimilation. This enzyme from Arabidopsis thaliana(AtUGlyAH) has been shown to bind a Mn2+ ion, via the C-terminal cupin domain, which acts as a molecular anchor to bind (S)-ureidoglycine, and its binding mode dictates the enantioselectivity of the reaction. The structure of AtUGlyAH shows a bi-cupin fold with a conserved "jelly roll-like" beta-barrel fold and an octameric functional unit. Several structural homologs of UGlyAH, including the Escherichia coli ortholog YlbA (also known as GlxB6), also exhibit similar features.


Pssm-ID: 380341 [Multi-domain]  Cd Length: 117  Bit Score: 44.43  E-value: 4.47e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 16078965  30 FLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIG 69
Cdd:cd02211  50 FLYVLEGEVELTVGGETHTLTAGGYAYLPPGTKHSLRNAG 89
cupin_NimR-like_N cd06124
AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This ...
 22-69 1.14e-05

AraC/XylS family transcriptional regulators similar to NimR, N-terminal cupin domain; This family contains mostly bacterial proteins containing an AraC/XylS family helix-turn-helix (HTH) DNA-binding domain C-terminal to a cupin domain, and may be possible transcriptional regulators. Included in this family is Escherichia coli HTH-type transcriptional regulator NimR (also called YeaM) that negatively regulates expression of the nimT operon and its own expression. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380379 [Multi-domain]  Cd Length: 95  Bit Score: 42.94  E-value: 1.14e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 16078965  22 SHKHAYSQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIG 69
Cdd:cd06124  16 WHSHPWGQLLYASSGVMTVETEDGRWLVPPQRAVWIPAGVEHSVRMLG 63
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
172-233 2.49e-05

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 44.28  E-value: 2.49e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16078965  172 KKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWFTKSTGMPPRLYR 233
Cdd:PRK13503 209 KQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
PRK11171 PRK11171
(S)-ureidoglycine aminohydrolase;
30-66 2.75e-05

(S)-ureidoglycine aminohydrolase;


Pssm-ID: 183011 [Multi-domain]  Cd Length: 266  Bit Score: 44.12  E-value: 2.75e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 16078965   30 FLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFR 66
Cdd:PRK11171  86 FLFVVEGEITLTLEGKTHALSEGGYAYLPPGSDWTLR 122
AraC_binding_2 pfam14525
AraC-binding-like domain; This domain is related to the AraC ligand binding domain pfam02311.
 30-126 2.92e-05

AraC-binding-like domain; This domain is related to the AraC ligand binding domain pfam02311.


Pssm-ID: 434015  Cd Length: 173  Bit Score: 43.06  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965    30 FLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDVPLHAMKIDEYRAGSGIEAALD-------PFW 102
Cdd:pfam14525  58 LQLPLSGSAEIEQGGREVVLGPGDAVLLDPGRPYRLRWSEDCEQLVLRIPLRALLGRPLRRPLRFAPRLDldsglgaLWL 137

                          90       100
                  ....*....|....*....|....
gi 16078965   103 SSIRYLLTEEAKAGTANSLHMLVQ 126
Cdd:pfam14525 138 RLLRLLAAELAALGPALASSPLVA 161
cupin_TcmJ-like cd06991
TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of ...
 23-75 3.24e-05

TcmJ monooxygenase and related proteins, cupin domain; This family includes TcmJ, a subunit of the tetracenomycin (TCM) polyketide synthase (PKS) type II complex in Streptomyces glaucescens. TcmJ is a quinone-forming monooxygenase involved in the modification of aromatic polyketides synthesized by polyketide synthases of types II and III. Orthologs of TcmJ include the Streptomyces BenD (benastatin biosynthetic pathway), the Streptomyces olivaceus ElmJ (polyketide antibiotic elloramycin biosynthetic pathway), the Actinomadura hibisca PdmL (pradimicin biosynthetic pathway), the Streptomyces cyaneus CurC (curamycin biosynthetic pathway), the Streptomyces rishiriensis Lct30 (lactonamycin biosynthetic pathway), and the Streptomyces WhiE II (spore pigment polyketide biosynthetic pathway). Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380396 [Multi-domain]  Cd Length: 105  Bit Score: 41.90  E-value: 3.24e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 16078965  23 HKHAYS-QFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLV 75
Cdd:cd06991  35 HYHPYSeEFLYVVRGRLVVRVDGEPVVLEAGEALLVPRGVRHRLENAGDEPARL 88
cupin_XRE_C cd02209
XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; ...
 25-76 4.40e-05

XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain; This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380339 [Multi-domain]  Cd Length: 90  Bit Score: 40.95  E-value: 4.40e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 16078965  25 HAYSQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVL 76
Cdd:cd02209  35 HEGEEFGYVLEGELELTVGGETYVLEAGDSIYFDSDVPHRYRNPGDEPARVL 86
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 143-183 5.85e-05

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 39.44  E-value: 5.85e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 16078965   143 IHSHLFERLTIKKLAEIEHYHPAYYSSWFKKQTGKSPQNYI 183
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYR 41
cupin_KdgF cd02238
pectin degradation protein KdgF and related proteins, cupin domain; This family includes ...
 21-78 1.95e-04

pectin degradation protein KdgF and related proteins, cupin domain; This family includes bacterial and archaeal pectin degradation protein KdgF that catalyzes the linearization of unsaturated uronates from both pectin and alginate, which are polysaccharides found in the cell walls of plants and brown algae, respectively, and represent an important source of carbon. These polysaccharides, mostly consisting of chains of uronates, can be metabolized by bacteria through a pathway of enzymatic steps to the key metabolite 2-keto-3-deoxygluconate (KDG). Pectin degradation is used by many plant-pathogenic bacteria during infection, and also, pectin and alginate can both represent abundant sources of carbohydrate for the production of biofuels. These proteins belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold.


Pssm-ID: 380366 [Multi-domain]  Cd Length: 104  Bit Score: 39.37  E-value: 1.95e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16078965  21 HSHKHaySQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGrnECLVLDV 78
Cdd:cd02238  43 HSHPH--EQIGYVLSGRFEFTIGGETRILKPGDSYYIPPNVPHGAEALE--DSVLLDV 96
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
171-234 3.08e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 41.24  E-value: 3.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16078965  171 FKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWFTKSTGMPPRLYRN 234
Cdd:PRK13500 243 FRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQWRH 306
cupin_QDO_N_C cd02215
quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known ...
 21-66 4.10e-04

quercetinase, N- and C-terminal cupin domains; This family contains quercetinase (also known as quercetin 2,3-dioxygenase, 2,3QD, QDO and YxaG; EC 1.13.11.24), a mononuclear copper-dependent dioxygenase that catalyzes the cleavage of the flavonol quercetin (5,7,3',4'-tetrahydroxyflavonol) heterocyclic ring to produce 2-protocatechuoyl-phloroglucinol carboxylic acid and carbon monoxide. Bacillus subtilis quercetin 2,3-dioxygenase (QDO) is a homodimer that shows oxygenase activity with several divalent metals such as Mn2+, Co2+, Fe2+, and Cu2+, although the preferred one appears to be Mn2+. The dioxygen binds to the metal ion of the Cu-QDO-quercetin complex, yielding a Cu2+-superoxo quercetin radical intermediate, which then forms a Cu2+-alkylperoxo complex which then evolves into endoperoxide intermediate that decomposes to the product. Quercetinase is a bicupin with two tandem cupin beta-barrel domains, both of which are included in this alignment model. The pirins, which also belong to the cupin domain family, have been shown to catalyze a reaction involving quercetin and may have a function similar to that of quercetinase.


Pssm-ID: 380345 [Multi-domain]  Cd Length: 122  Bit Score: 39.06  E-value: 4.10e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 16078965  21 HSHKHAYSQFlFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFR 66
Cdd:cd02215  48 HYHKRHHETF-YVLEGRLQLWLDGESRLLTPGDFASVPPGTIHAYR 92
cupin_YdbB-like cd02226
Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial ...
 20-76 5.58e-04

Bacillus subtilis YdbB and related proteins, cupin domain; This family includes bacterial proteins homologous to YdbB, a Bacillus subtilis protein of unknown function. It also includes protein Nmb1881 From Neisseria meningitidis, also of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380355 [Multi-domain]  Cd Length: 94  Bit Score: 38.19  E-value: 5.58e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16078965  20 YHSHKHAYS-QFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIgrNECLVL 76
Cdd:cd02226  35 FVWHKHDDEdELFLVLEGELTIDFRDRDVTLGPGEFFVVPKGVEHRPVAE--EETVVL 90
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
171-234 7.33e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 40.04  E-value: 7.33e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16078965  171 FKKQTGKSPQNYIADLRLEEAKRMLMERNETLTVVSEALGFQNLSSFTRWFTKSTGMPPRLYRN 234
Cdd:PRK13502 213 FRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRH 276
AllE COG3257
Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];
30-106 7.50e-04

Ureidoglycine aminohydrolase [Nucleotide transport and metabolism];


Pssm-ID: 442488 [Multi-domain]  Cd Length: 262  Bit Score: 39.81  E-value: 7.50e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16078965  30 FLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGrneclvlDVPLHAMKIDE-YRAGSGIEAAlDPFWSSIR 106
Cdd:COG3257  84 FLFVLEGEVTLTLGGETHELTPGGYAYLPPGTPWTLRNAG-------DEPARFHWIRKrYEPVEGLEAP-EAFVGNEA 153
cupin_HpaA-like_N cd06999
AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain; Members ...
 23-66 1.15e-03

AraC/XylS family transcriptional regulators similar to HpaA, N-terminal cupin domain; Members of this family contain an N-terminal cupin domain and a C-terminal AraC/XylS family helix-turn-helix (HTH) DNA-binding domain, similar to Escherichia coli 4-hydroxyphenylacetate catabolism regulatory protein HpaA (also known as 4HPA). HpaA is encoded by the hpaA gene which is located upstream of hpaBC. It is activated by 4-HPA, 3-HPA and phenylacetate, and represents a member of the AraC/XylS family of regulators that recognizes aromatic effectors. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380403 [Multi-domain]  Cd Length: 98  Bit Score: 37.09  E-value: 1.15e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 16078965  23 HKHA-YSQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFR 66
Cdd:cd06999  38 HRHAdLFQVLYIESGGGEVRLDGRTHPLSAPALVVVPPGVVHGFR 82
cupin_QdtA-like cd20292
sugar 3,4-ketoisomerase QdtA and related proteins, cupin domain; This family includes cupin ...
 21-76 1.79e-03

sugar 3,4-ketoisomerase QdtA and related proteins, cupin domain; This family includes cupin domains of several bacterial proteins homologous to sugar 3,4-ketoisomerases. Thermoanaerobacterium thermosaccharolyticum QdtA catalyzes a key step in the biosynthesis of these sugars, the conversion of thymidine diphosphate (dTDP)-4-keto-6-deoxyglucose to dTDP-3-keto-6-deoxyglucose. In Aneurinibacillus thermoaerophilus, TDP-4-oxo-6-deoxy-alpha-D-glucose-3,4-oxoisomerase (also known as FdtA) is involved in the biosynthesis of dTDP-Fucp3NAc (3-acetamido-3,6-dideoxy-alpha-d-galactose), which is part of the repeating units of the glycan chain in the S-layer. Shewanella denitrificans bifunctional ketoisomerase/N-acetyltransferase (also known as FdtD) is involved in the third and fifth steps in the production of 3-acetamido-3,6-dideoxy-alpha-d-galactose or Fuc3NAc; the C-terminal cupin domain harbors the active site responsible for the isomerization reaction. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380426  Cd Length: 117  Bit Score: 37.07  E-value: 1.79e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16078965  21 HSHKHAySQFLFPLEGSIDLETE-GRQ---VKLN-PDHFLYIPPQCEHRFRSIGRNE-CLVL 76
Cdd:cd20292  45 HAHKKL-EQLLICLSGSCEVILDdGKEkeeFVLDsPNKGLYIPPGVWHEMYDFSPDAvLLVL 105
cupin_MAE_RS03005 cd06987
Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes ...
 21-100 2.32e-03

Microcystis aeruginosa MAE_RS03005 and related proteins, cupin domain; This family includes bacterial and some eukaryotic proteins homologous to MAE_RS03005, a Microcystis aeruginosa protein of unknown function. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380392 [Multi-domain]  Cd Length: 122  Bit Score: 36.86  E-value: 2.32e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965  21 HSHKHAYSQFlFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIG--RNECLVLDVPlhamkiDEYRAG---SGIE 95
Cdd:cd06987  44 NTHPAAHEMF-FVLAGEGRAYCDGQRVPLRPGDALVVPPGSEHVIENTGsgRLYCLTLMVP------NEGFAElirSGIP 116


                ....*
gi 16078965  96 AALDP 100
Cdd:cd06987 117 AELDD 121
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 23-102 2.65e-03

AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization domain of the bacterial gene regulatory protein AraC. The domain is found in conjunction with the helix-turn-helix (HTH) DNA-binding motif pfam00165. This domain is distantly related to the Cupin domain pfam00190.


Pssm-ID: 396749 [Multi-domain]  Cd Length: 134  Bit Score: 37.03  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16078965    23 HKHAYSQFLFPLEGSIDLETEGRQVKLNPDHFLYIPPQCEHRFRSIGRNECLVLDVPLHAMKIDEYRAGSGIEAALDPFW 102
Cdd:pfam02311  19 HVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEPELLERILADISILAGGPLPL 98
 
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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