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Conserved domains on  [gi|568064775|ref|WP_024052451|]
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MULTISPECIES: AraC family transcriptional regulator [Streptococcus]

Protein Classification

AraC family transcriptional regulator( domain architecture ID 15746445)

AraC family transcriptional regulator containing a cupin domain as its effector domain and an AraC family helix-turn-helix (HTH) DNA binding domain, controls the expression of genes with diverse biological functions including metabolism, stress response, and virulence

CATH:  2.60.120.10
Gene Ontology:  GO:0003700|GO:0006355|GO:0043565
PubMed:  11282467|33837749|9409145|12270809|19478949|14697267|9573603
SCOP:  3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
204-287 2.13e-28

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 104.17  E-value: 2.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775   204 ELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITP 283
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 568064775   284 SQYR 287
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
53-289 1.61e-27

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


:

Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 107.17  E-value: 1.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775  53 FHIDYDYFNSEAGDIILIRPNALHSIHPIENRRHYMDAINFHLDLMGYSAMDQASIEYLQPLYNGQLDFVRVIKPNQPAY 132
Cdd:COG2207   10 LLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 133 ADIRQCLLDAMKTGYYRTEYFEFQLKAQLNQLFFLLFENGYVISKEQSLEGYRKEEKIRTIIDYIGSHY-------QEEL 205
Cdd:COG2207   90 LLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLlllllllLLLL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 206 TIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQ 285
Cdd:COG2207  170 TLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSE 249


                 ....
gi 568064775 286 YRKK 289
Cdd:COG2207  250 YRKR 253
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
16-79 2.46e-05

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


:

Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 42.82  E-value: 2.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568064775  16 GTPYSLTRTITKNGQpDILFHWHTDV-ELVYVHEGTAQFHIDYDYFNSEAGDIILIRPNALHSIH 79
Cdd:COG0662   24 GERLSVKRITVPPGA-ELSLHVHPHRdEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLR 87
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
204-287 2.13e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 104.17  E-value: 2.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775   204 ELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITP 283
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 568064775   284 SQYR 287
Cdd:smart00342  81 SEYR 84
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 188-289 4.80e-28

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: 109.86  E-value: 4.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 188 EKIRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNN 267
Cdd:COG4977  210 PRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGS 289

                         90       100
                 ....*....|....*....|..
gi 568064775 268 LSNFNRQFKKYYQITPSQYRKK 289
Cdd:COG4977  290 ASHFRRAFRRRFGVSPSAYRRR 311
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
53-289 1.61e-27

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 107.17  E-value: 1.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775  53 FHIDYDYFNSEAGDIILIRPNALHSIHPIENRRHYMDAINFHLDLMGYSAMDQASIEYLQPLYNGQLDFVRVIKPNQPAY 132
Cdd:COG2207   10 LLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 133 ADIRQCLLDAMKTGYYRTEYFEFQLKAQLNQLFFLLFENGYVISKEQSLEGYRKEEKIRTIIDYIGSHY-------QEEL 205
Cdd:COG2207   90 LLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLlllllllLLLL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 206 TIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQ 285
Cdd:COG2207  170 TLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSE 249


                 ....
gi 568064775 286 YRKK 289
Cdd:COG2207  250 YRKR 253
HTH_18 pfam12833
Helix-turn-helix domain;
210-289 6.07e-22

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 87.26  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775  210 LAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELL-QHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQYRK 288
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 568064775  289 K 289
Cdd:pfam12833  81 R 81
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
187-287 1.10e-14

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 68.80  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 187 EEKIRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFN 266
Cdd:PRK10219   4 QKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYV 83

                         90       100
                 ....*....|....*....|.
gi 568064775 267 NLSNFNRQFKKYYQITPSQYR 287
Cdd:PRK10219  84 SQQTFSRVFRRQFDRTPSDYR 104
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 190-287 5.22e-12

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: 65.47  E-value: 5.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775  190 IRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQhSTLPVLEIATQSGFNNLS 269
Cdd:TIGR04094 287 IRAVIQYINLNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLR-SQIPVSEVSNELGFYDLS 365

                          90
                  ....*....|....*...
gi 568064775  270 NFNRQFKKYYQITPSQYR 287
Cdd:TIGR04094 366 HFSRTFKKHTGVSPKQYQ 383
viru_reg_Rsp NF033869
AraC family transcriptional regulator Rsp; Rsp (repressor of surface proteins), as described ...
 193-287 9.03e-11

AraC family transcriptional regulator Rsp; Rsp (repressor of surface proteins), as described in Staphylococcus aureus, is a large protein with an AraC-like helix-turn-helix DNA-binding domain. Regulatory targets include the accessory gene regulator (agr) operon, which in turn regulates a large number of virulence factors.


Pssm-ID: 411433 [Multi-domain]  Cd Length: 701  Bit Score: 62.04  E-value: 9.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 193 IIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFN 272
Cdd:NF033869 152 CLTFIHDHISSNLSLRDVAQHCNISESYCSNLFVRYLNMNFKDYFTSLKLCHAIQLLLSTNHSINAISELSGFSSHTNFT 231

                         90
                 ....*....|....*
gi 568064775 273 RQFKKYYQITPSQYR 287
Cdd:NF033869 232 NQFKNYLNFSPKQFR 246
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 36-115 2.19e-09

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: 54.75  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775   36 HWHTDVELVYVHEGTAQFHIDYDYFNSEAGDIILIRPNALHSIHPIENRRHYMDAINFHLDLMGYSAMDQASIEYLQPLY 115
Cdd:pfam02311  19 HVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEPELLERILADISILAGGPLPL 98
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 31-83 2.64e-09

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: 52.87  E-value: 2.64e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568064775  31 PDILFHWHTDV-ELVYVHEGTAQFHIDYDY-FNSEAGDIILIRPNALHSIHPIEN 83
Cdd:cd02208   10 TSSPPHWHPEQdEIFYVLSGEGELTLDDGEtVELKAGDIVLIPPGVPHSFVNTSD 64
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
16-79 2.46e-05

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 42.82  E-value: 2.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568064775  16 GTPYSLTRTITKNGQpDILFHWHTDV-ELVYVHEGTAQFHIDYDYFNSEAGDIILIRPNALHSIH 79
Cdd:COG0662   24 GERLSVKRITVPPGA-ELSLHVHPHRdEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLR 87
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
30-289 3.34e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 44.51  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775  30 QPDILFHWHTDVELVYVHEGTAqFHIDYDY-FNSEAGDIILIRPNALHSihpienrrhyMDAINfhlDLmgysAMDqaSI 108
Cdd:PRK13501  28 QETFVEHTHQFCEIVIVWRGNG-LHVLNDHpYRITCGDVFYIQAADHHS----------YESVH---DL----VLD--NI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 109 EYLQPLYNGQLDFVRVIKPNQP----------------AYADIRQCLLDAMKTGyyrteyfefQLKAQLNQLFFL----- 167
Cdd:PRK13501  88 IYCPERLHLNAQWHKLLPPLGPeqnqgywrlttqgmaqARPIIQQLAQESRKTD---------SWSIQLTEVLLLqlaiv 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 168 LFENGYVISKEQSL-EGYRKEEKIRTIIDYIGSHYQeeltidqLAQIC---GYSDTHFMNFFKKHLGVSCMEYVIQFRLR 243
Cdd:PRK13501 159 LKRHRYRAEQAHLLpDGEQLDLIMSALQQSLGAYFD-------MADFChknQLVERSLKQLFRQQTGMSISHYLRQIRLC 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568064775 244 KAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQYRKK 289
Cdd:PRK13501 232 HAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQR 277
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 13-78 1.61e-04

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 39.81  E-value: 1.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568064775  13 KTQGTPYSLTRTITKNGQPDILfHWHTDVELVY-VHEGTAQFHIDYDYFNSEAGDIILIRPNALHSI 78
Cdd:cd02214   13 NDGDPRYSLAHARVPPGESTLP-HRLKGSEEVYyILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRI 78
 
Name Accession Description Interval E-value
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
204-287 2.13e-28

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 104.17  E-value: 2.13e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775   204 ELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITP 283
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 568064775   284 SQYR 287
Cdd:smart00342  81 SEYR 84
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 188-289 4.80e-28

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: 109.86  E-value: 4.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 188 EKIRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNN 267
Cdd:COG4977  210 PRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGS 289

                         90       100
                 ....*....|....*....|..
gi 568064775 268 LSNFNRQFKKYYQITPSQYRKK 289
Cdd:COG4977  290 ASHFRRAFRRRFGVSPSAYRRR 311
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
53-289 1.61e-27

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 107.17  E-value: 1.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775  53 FHIDYDYFNSEAGDIILIRPNALHSIHPIENRRHYMDAINFHLDLMGYSAMDQASIEYLQPLYNGQLDFVRVIKPNQPAY 132
Cdd:COG2207   10 LLLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 133 ADIRQCLLDAMKTGYYRTEYFEFQLKAQLNQLFFLLFENGYVISKEQSLEGYRKEEKIRTIIDYIGSHY-------QEEL 205
Cdd:COG2207   90 LLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLlllllllLLLL 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 206 TIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQ 285
Cdd:COG2207  170 TLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSE 249


                 ....
gi 568064775 286 YRKK 289
Cdd:COG2207  250 YRKR 253
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 185-288 1.67e-27

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: 108.99  E-value: 1.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 185 RKEEKIRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQhSTLPVLEIATQSG 264
Cdd:COG2169   81 PRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQ-TGLSVTDAAYAAG 159

                         90       100
                 ....*....|....*....|....
gi 568064775 265 FNNLSNFNRQFKKYYQITPSQYRK 288
Cdd:COG2169  160 FGSLSRFYEAFKKLLGMTPSAYRR 183
HTH_18 pfam12833
Helix-turn-helix domain;
210-289 6.07e-22

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 87.26  E-value: 6.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775  210 LAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELL-QHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQYRK 288
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 568064775  289 K 289
Cdd:pfam12833  81 R 81
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
187-287 1.10e-14

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 68.80  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 187 EEKIRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFN 266
Cdd:PRK10219   4 QKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYV 83

                         90       100
                 ....*....|....*....|.
gi 568064775 267 NLSNFNRQFKKYYQITPSQYR 287
Cdd:PRK10219  84 SQQTFSRVFRRQFDRTPSDYR 104
PRK10371 PRK10371
transcriptional regulator MelR;
190-288 1.65e-14

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 72.16  E-value: 1.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 190 IRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLS 269
Cdd:PRK10371 193 VSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSS 272

                         90
                 ....*....|....*....
gi 568064775 270 NFNRQFKKYYQITPSQYRK 288
Cdd:PRK10371 273 RFYSTFGKYVGMSPQQYRK 291
ftrA PRK09393
transcriptional activator FtrA; Provisional
 193-289 2.06e-14

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 71.92  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 193 IIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFN 272
Cdd:PRK09393 223 LIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLR 302

                         90
                 ....*....|....*..
gi 568064775 273 RQFKKYYQITPSQYRKK 289
Cdd:PRK09393 303 HHFRRRAATSPAAYRKR 319
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
190-287 1.98e-13

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 65.89  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 190 IRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLS 269
Cdd:PRK11511  11 IHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQ 90

                         90
                 ....*....|....*...
gi 568064775 270 NFNRQFKKYYQITPSQYR 287
Cdd:PRK11511  91 TLTRTFKNYFDVPPHKYR 108
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 190-287 5.22e-12

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: 65.47  E-value: 5.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775  190 IRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQhSTLPVLEIATQSGFNNLS 269
Cdd:TIGR04094 287 IRAVIQYINLNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLR-SQIPVSEVSNELGFYDLS 365

                          90
                  ....*....|....*...
gi 568064775  270 NFNRQFKKYYQITPSQYR 287
Cdd:TIGR04094 366 HFSRTFKKHTGVSPKQYQ 383
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
190-288 4.56e-11

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 61.95  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 190 IRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLS 269
Cdd:PRK15121   7 IRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQYRFDSQQ 86

                         90
                 ....*....|....*....
gi 568064775 270 NFNRQFKKYYQITPSQYRK 288
Cdd:PRK15121  87 TFTRAFKKQFAQTPALYRR 105
viru_reg_Rsp NF033869
AraC family transcriptional regulator Rsp; Rsp (repressor of surface proteins), as described ...
 193-287 9.03e-11

AraC family transcriptional regulator Rsp; Rsp (repressor of surface proteins), as described in Staphylococcus aureus, is a large protein with an AraC-like helix-turn-helix DNA-binding domain. Regulatory targets include the accessory gene regulator (agr) operon, which in turn regulates a large number of virulence factors.


Pssm-ID: 411433 [Multi-domain]  Cd Length: 701  Bit Score: 62.04  E-value: 9.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 193 IIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFN 272
Cdd:NF033869 152 CLTFIHDHISSNLSLRDVAQHCNISESYCSNLFVRYLNMNFKDYFTSLKLCHAIQLLLSTNHSINAISELSGFSSHTNFT 231

                         90
                 ....*....|....*
gi 568064775 273 RQFKKYYQITPSQYR 287
Cdd:NF033869 232 NQFKNYLNFSPKQFR 246
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
182-287 1.84e-10

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 60.08  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 182 EGYRKEEKIRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIAT 261
Cdd:PRK13503 165 NGENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAY 244

                         90       100
                 ....*....|....*....|....*.
gi 568064775 262 QSGFNNLSNFNRQFKKYYQITPSQYR 287
Cdd:PRK13503 245 RCGFGDSNHFSTLFRREFSWSPRDIR 270
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
189-289 6.37e-10

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 58.83  E-value: 6.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 189 KIRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNL 268
Cdd:PRK10572 184 RVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQ 263

                         90       100
                 ....*....|....*....|.
gi 568064775 269 SNFNRQFKKYYQITPSQYRKK 289
Cdd:PRK10572 264 LYFSRVFKKCTGASPSEFRAR 284
AraC_binding pfam02311
AraC-like ligand binding domain; This family represents the arabinose-binding and dimerization ...
 36-115 2.19e-09

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: 54.75  E-value: 2.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775   36 HWHTDVELVYVHEGTAQFHIDYDYFNSEAGDIILIRPNALHSIHPIENRRHYMDAINFHLDLMGYSAMDQASIEYLQPLY 115
Cdd:pfam02311  19 HVHDFYVIGYIERGVGRFRLNGRTYHLGPGDLFLLPPGEPHDYEPESEDGWRYRWLYFEPELLERILADISILAGGPLPL 98
cupin_RmlC-like cd02208
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 31-83 2.64e-09

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: 52.87  E-value: 2.64e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568064775  31 PDILFHWHTDV-ELVYVHEGTAQFHIDYDY-FNSEAGDIILIRPNALHSIHPIEN 83
Cdd:cd02208   10 TSSPPHWHPEQdEIFYVLSGEGELTLDDGEtVELKAGDIVLIPPGVPHSFVNTSD 64
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
163-287 3.72e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 50.49  E-value: 3.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 163 QLFFLLFENGYViskEQSLEGYRKEEKIRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRL 242
Cdd:PRK13500 184 QLVMLLNRHRYT---SDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRV 260

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568064775 243 RKAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQYR 287
Cdd:PRK13500 261 CHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQWR 305
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 185-289 4.37e-07

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 50.41  E-value: 4.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 185 RKEEKIRTIIDYIGSHYQEE-LTIDQLAQICGYSDTHFMNFFKKHlGVSCMEYVIQFRLRKAAELLQHSTL--PVLEIAT 261
Cdd:PRK09685 194 RRERQFQKVVALIDQSIQEEiLRPEWIAGELGISVRSLYRLFAEQ-GLVVAQYIRNRRLDRCADDLRPAADdeKITSIAY 272

                         90       100
                 ....*....|....*....|....*...
gi 568064775 262 QSGFNNLSNFNRQFKKYYQITPSQYRKK 289
Cdd:PRK09685 273 KWGFSDSSHFSTAFKQRFGVSPGEYRRK 300
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
186-287 5.20e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 50.05  E-value: 5.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 186 KEEKIRTIIDYIGSHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGF 265
Cdd:PRK13502 174 RETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGF 253

                         90       100
                 ....*....|....*....|..
gi 568064775 266 NNLSNFNRQFKKYYQITPSQYR 287
Cdd:PRK13502 254 EDSNYFSVVFTRETGMTPSQWR 275
QdoI COG1917
Cupin domain protein related to quercetin dioxygenase [General function prediction only];
36-79 5.75e-07

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


Pssm-ID: 441521 [Multi-domain]  Cd Length: 99  Bit Score: 47.15  E-value: 5.75e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 568064775  36 HWHTDVELVYVHEGTAQFHIDYDYFNSEAGDIILIRPNALHSIH 79
Cdd:COG1917   39 HSHPGEELIYVLEGEGEVEVGGEEYELKPGDVVFIPPGVPHAFR 82
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 251-288 1.44e-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: 41.37  E-value: 1.44e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568064775  251 HSTLPVLEIATQSGFNnLSNFNRQFKKYYQITPSQYRK 288
Cdd:pfam00165   6 STNLTIADIADELGFS-RSYFSRLFKKYTGVTPSQYRH 42
ManC COG0662
Mannose-6-phosphate isomerase, cupin superfamily [Carbohydrate transport and metabolism];
16-79 2.46e-05

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


Pssm-ID: 440426 [Multi-domain]  Cd Length: 114  Bit Score: 42.82  E-value: 2.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568064775  16 GTPYSLTRTITKNGQpDILFHWHTDV-ELVYVHEGTAQFHIDYDYFNSEAGDIILIRPNALHSIH 79
Cdd:COG0662   24 GERLSVKRITVPPGA-ELSLHVHPHRdEFFYVLEGTGEVTIGDEEVELKAGDSVYIPAGVPHRLR 87
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 199-236 3.08e-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: 40.60  E-value: 3.08e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 568064775  199 SHYQEELTIDQLAQICGYSDTHFMNFFKKHLGVSCMEY 236
Cdd:pfam00165   3 ENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQY 40
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
30-289 3.34e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 44.51  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775  30 QPDILFHWHTDVELVYVHEGTAqFHIDYDY-FNSEAGDIILIRPNALHSihpienrrhyMDAINfhlDLmgysAMDqaSI 108
Cdd:PRK13501  28 QETFVEHTHQFCEIVIVWRGNG-LHVLNDHpYRITCGDVFYIQAADHHS----------YESVH---DL----VLD--NI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 109 EYLQPLYNGQLDFVRVIKPNQP----------------AYADIRQCLLDAMKTGyyrteyfefQLKAQLNQLFFL----- 167
Cdd:PRK13501  88 IYCPERLHLNAQWHKLLPPLGPeqnqgywrlttqgmaqARPIIQQLAQESRKTD---------SWSIQLTEVLLLqlaiv 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 168 LFENGYVISKEQSL-EGYRKEEKIRTIIDYIGSHYQeeltidqLAQIC---GYSDTHFMNFFKKHLGVSCMEYVIQFRLR 243
Cdd:PRK13501 159 LKRHRYRAEQAHLLpDGEQLDLIMSALQQSLGAYFD-------MADFChknQLVERSLKQLFRQQTGMSISHYLRQIRLC 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 568064775 244 KAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQYRKK 289
Cdd:PRK13501 232 HAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQR 277
COG3837 COG3837
Uncharacterized conserved protein, cupin superfamily [Function unknown];
29-79 7.08e-05

Uncharacterized conserved protein, cupin superfamily [Function unknown];


Pssm-ID: 443048 [Multi-domain]  Cd Length: 115  Bit Score: 41.54  E-value: 7.08e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568064775  29 GQPDILFHWHTDV-ELVYVHEGTAQFHIDYDYFNSEAGDIILIRPNALHSIH 79
Cdd:COG3837   38 GASSSPYHAHSAEeEFVYVLEGELTLRIGGEEYVLEPGDSVGFPAGVPHRLR 89
cupin_MJ1618 cd02214
Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes ...
 13-78 1.61e-04

Methanocaldococcus jannaschii MJ1618 and related proteins, cupin domain; This family includes bacterial and archaeal proteins homologous to MJ1618, a Methanocaldococcus jannaschii protein of unknown function with a cupin beta barrel domain. The active site of members of the cupin superfamily is generally located at the center of a conserved barrel and usually includes a metal ion.


Pssm-ID: 380344 [Multi-domain]  Cd Length: 100  Bit Score: 39.81  E-value: 1.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568064775  13 KTQGTPYSLTRTITKNGQPDILfHWHTDVELVY-VHEGTAQFHIDYDYFNSEAGDIILIRPNALHSI 78
Cdd:cd02214   13 NDGDPRYSLAHARVPPGESTLP-HRLKGSEEVYyILEGEGTMEIDGEPREVGPGDAVLIPPGAVQRI 78
cupin_OxDC-like cd20306
Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and ...
 36-78 2.45e-04

Oxalate decarboxylase (OxDC)-like cupin domain; This subfamily contains bacterial and eukaryotic cupin domains of proteins homologous to oxalate decarboxylase (OxDC; EC 4.1.1.2) such as MSMEG_2254, a putative OxDC from Mycobacterium smegmatis. OxDC is a manganese-dependent bicupin that catalyzes the conversion of oxalate to formate and carbon dioxide, utilizing dioxygen as a cofactor. It is evolutionarily related to oxalate oxidase (OxOx or germin; EC 1.2.3.4) which, in contrast, converts oxalate and dioxygen to carbon dioxide and hydrogen peroxide. OxDC is classified as a bicupin because it contains two cupin folds with each domain containing one manganese binding site, with four manganese binding residues (three histidines and one glutamate) conserved as well as a number of hydrophobic residues.


Pssm-ID: 380440 [Multi-domain]  Cd Length: 151  Bit Score: 40.65  E-value: 2.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 568064775  36 HWHTDV-ELVYVHEGTAQFHI-----DYDYFNSEAGDIILIRPNALHSI 78
Cdd:cd20306   50 HWHPNAnELGYVISGEARVSIldptgSLDTFTVKPGQVVFIPQGWLHWI 98
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 230-288 8.48e-04

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 40.36  E-value: 8.48e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 568064775 230 GVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQYRK 288
Cdd:PRK15185 247 GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPSTFIK 305
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 227-286 1.39e-03

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 39.66  E-value: 1.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568064775 227 KHLGVSCMEYVIQFRLRKAAELLQHSTLPVLEIATQSGFNNLSNFNRQFKKYYQITPSQY 286
Cdd:PRK15186 219 KQENTSFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278
cupin_YbfI-like_N cd07001
AraC/XylS family transcriptional regulators similar to Bacillus subtilis YbfI, N-terminal ...
 30-94 1.81e-03

AraC/XylS family transcriptional regulators similar to Bacillus subtilis YbfI, N-terminal cupin domain; This family contains 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, including YbfI, an uncharacterized Bacillus subtilis. In Pseudomonas putida, this protein is thought to regulate the expression of phenylserine aldolase. Proteins in this family belong to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.


Pssm-ID: 380405 [Multi-domain]  Cd Length: 76  Bit Score: 36.60  E-value: 1.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568064775  30 QPDILFHWHTDVELVYVHEGTAQFHIDYDYFNSEAGDIILIRPNALHSIHPIENRRHYMDAINFH 94
Cdd:cd07001   12 QKSFPNHFHDFYVIGFIESGQRTLFCEGKEYTVEPGDLLLINPRDVHSCIQISGRRLDYERINIW 76
cupin_HP0902-like cd02230
Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes ...
 43-83 2.17e-03

Helicobacter pylori HP0902 and related proteins, cupin domain; This family includes prokaryotic and archaeal proteins homologous to HP0902, a functionally uncharacterized protein from Helicobacter pylori and Spy1581, a protein of unknown function from Streptococcus pyogenes. These proteins demonstrate all-beta cupin folds that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins, and thus may have a putative role in H. pylori pathogenicity.


Pssm-ID: 380358 [Multi-domain]  Cd Length: 83  Bit Score: 36.33  E-value: 2.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 568064775  43 LVYVHEGTAQFHIDYDYFNSEAGDIILIRPNALHSIHPIEN 83
Cdd:cd02230   34 TVQVLEGEAEFTIGGETVTLKAGELIVMPANVPHALKAEED 74
Cupin_2 pfam07883
Cupin domain; This family represents the conserved barrel domain of the 'cupin' superfamily ( ...
 32-79 2.21e-03

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: 36.08  E-value: 2.21e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568064775   32 DILFHWHTD-VELVYVHEGTAQFHID---YDYfnsEAGDIILIRPNALHSIH 79
Cdd:pfam07883  10 SSPPHRHPGeDEFFYVLEGEGELTVDgeeVVL---KAGDSVYFPAGVPHRFR 58
 
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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