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Conserved domains on  [gi|2184264921|ref|WP_236163245|]
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MULTISPECIES: GlxA family transcriptional regulator [Acinetobacter]

Protein Classification

GlxA family transcriptional regulator( domain architecture ID 11471967)

GlxA family transcriptional regulator contains an amidase domain and an AraC-type DNA-binding helix-turn-helix (HTH) domain

Gene Ontology:  GO:0003677|GO:0003700|GO:0006355
PubMed:  15808743|33837749|15070401|11282467

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 2-324 1.16e-120

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: 349.46  E-value: 1.16e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   2 KQVVILAFDGALASAITGIVDLFSMAgaswNRIQNQQierLFEVKIASPKGQSIQCINGIKMHAELSYQEIQYADLVVVP 81
Cdd:COG4977     1 LRVAFLLLPGFSLLDLAGPLEVFRLA----NRLAGRP---LYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  82 tigAALLSVLQRTPELIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVELKVERMITHAD 161
Cdd:COG4977    74 ---GGLDPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 162 HIYCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSFVIDYRRDSQLS-YSLMKIAKPHQDALVQEVQNWMEQHYSQNFNLD 240
Cdd:COG4977   151 DILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAqFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 241 EIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYRR 320
Cdd:COG4977   231 ELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRR 310


                  ....
gi 2184264921 321 RFSR 324
Cdd:COG4977   311 RFRA 314
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 2-324 1.16e-120

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: 349.46  E-value: 1.16e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   2 KQVVILAFDGALASAITGIVDLFSMAgaswNRIQNQQierLFEVKIASPKGQSIQCINGIKMHAELSYQEIQYADLVVVP 81
Cdd:COG4977     1 LRVAFLLLPGFSLLDLAGPLEVFRLA----NRLAGRP---LYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  82 tigAALLSVLQRTPELIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVELKVERMITHAD 161
Cdd:COG4977    74 ---GGLDPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 162 HIYCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSFVIDYRRDSQLS-YSLMKIAKPHQDALVQEVQNWMEQHYSQNFNLD 240
Cdd:COG4977   151 DILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAqFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 241 EIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYRR 320
Cdd:COG4977   231 ELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRR 310


                  ....
gi 2184264921 321 RFSR 324
Cdd:COG4977   311 RFRA 314
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 4-199 1.88e-68

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153232 [Multi-domain]  Cd Length: 195  Bit Score: 212.12  E-value: 1.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   4 VVILAFDGALASAITGIVDLFSMAGASWNRIQNQQieRLFEVKIASPKGQSIQCINGIKMHAELSYQEIQYADLVVVPTI 83
Cdd:cd03138     1 VTLLAYPGALASSLAGLLDLLRAANRLARRQQGGA--PPFEVRLVSLDGGPVLLAGGILILPDATLADVPAPDLVIVPGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  84 GAAL-LSVLQRTPELIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVELKVERMITHADH 162
Cdd:cd03138    79 GGDPdELLLADNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGN 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2184264921 163 IYCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSFVID 199
Cdd:cd03138   159 LITAGGAMAWADLALHLIERLAGPELAQLVARFLLID 195
ftrA PRK09393
transcriptional activator FtrA; Provisional
 4-324 6.47e-47

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 160.90  E-value: 6.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   4 VVILAFDGaLASAITGI-VDLFSMA----GASWNRiqnqqierlFEVkIASPKGqSIQCINGIKMHAELSYQEIQYADLV 78
Cdd:PRK09393   12 VVALAYDG-LCTFEFGCaVEIFGLPrpelGVDWYR---------FAV-AAVEPG-PLRAAGGITVVADGGLELLDRADTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  79 VVPtigaALLSVLQRTPE-LIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVELKVERMI 157
Cdd:PRK09393   80 VIP----GWRGPDAPVPEpLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 158 THADHIYCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSFVIDYRRD-SQLSYslmkIAKP---HQDALVQEVQNWMEQHY 233
Cdd:PRK09393  156 VDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRDgGQAQF----VPRPvasRESDRLGPLIDWMRAHL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 234 SQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGL 313
Cdd:PRK09393  232 AEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAAT 311

                         330
                  ....*....|.
gi 2184264921 314 TPLDYRRRFSR 324
Cdd:PRK09393  312 SPAAYRKRFGR 322
HTH_18 pfam12833
Helix-turn-helix domain;
242-321 3.64e-24

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 93.81  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 242 IAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQL-EQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYRR 320
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 2184264921 321 R 321
Cdd:pfam12833  81 R 81
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
236-319 1.00e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 92.62  E-value: 1.00e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  236 NFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTP 315
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 2184264921  316 LDYR 319
Cdd:smart00342  81 SEYR 84
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 202-319 8.95e-15

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: 74.33  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 202 RDSQLSYSLMKIAKP---HQDALVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAAr 278
Cdd:TIGR04094 264 RDSAIIYFTELLHEIsinHHSPLIRAVIQYINLNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEA- 342

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2184264921 279 KQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYR 319
Cdd:TIGR04094 343 KYLLRSQIPVSEVSNELGFYDLSHFSRTFKKHTGVSPKQYQ 383
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 2-324 1.16e-120

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: 349.46  E-value: 1.16e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   2 KQVVILAFDGALASAITGIVDLFSMAgaswNRIQNQQierLFEVKIASPKGQSIQCINGIKMHAELSYQEIQYADLVVVP 81
Cdd:COG4977     1 LRVAFLLLPGFSLLDLAGPLEVFRLA----NRLAGRP---LYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  82 tigAALLSVLQRTPELIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVELKVERMITHAD 161
Cdd:COG4977    74 ---GGLDPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 162 HIYCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSFVIDYRRDSQLS-YSLMKIAKPHQDALVQEVQNWMEQHYSQNFNLD 240
Cdd:COG4977   151 DILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAqFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVD 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 241 EIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYRR 320
Cdd:COG4977   231 ELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRR 310


                  ....
gi 2184264921 321 RFSR 324
Cdd:COG4977   311 RFRA 314
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 4-199 1.88e-68

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153232 [Multi-domain]  Cd Length: 195  Bit Score: 212.12  E-value: 1.88e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   4 VVILAFDGALASAITGIVDLFSMAGASWNRIQNQQieRLFEVKIASPKGQSIQCINGIKMHAELSYQEIQYADLVVVPTI 83
Cdd:cd03138     1 VTLLAYPGALASSLAGLLDLLRAANRLARRQQGGA--PPFEVRLVSLDGGPVLLAGGILILPDATLADVPAPDLVIVPGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  84 GAAL-LSVLQRTPELIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVELKVERMITHADH 162
Cdd:cd03138    79 GGDPdELLLADNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGN 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2184264921 163 IYCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSFVID 199
Cdd:cd03138   159 LITAGGAMAWADLALHLIERLAGPELAQLVARFLLID 195
ftrA PRK09393
transcriptional activator FtrA; Provisional
 4-324 6.47e-47

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 160.90  E-value: 6.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   4 VVILAFDGaLASAITGI-VDLFSMA----GASWNRiqnqqierlFEVkIASPKGqSIQCINGIKMHAELSYQEIQYADLV 78
Cdd:PRK09393   12 VVALAYDG-LCTFEFGCaVEIFGLPrpelGVDWYR---------FAV-AAVEPG-PLRAAGGITVVADGGLELLDRADTI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  79 VVPtigaALLSVLQRTPE-LIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVELKVERMI 157
Cdd:PRK09393   80 VIP----GWRGPDAPVPEpLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLY 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 158 THADHIYCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSFVIDYRRD-SQLSYslmkIAKP---HQDALVQEVQNWMEQHY 233
Cdd:PRK09393  156 VDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRDgGQAQF----VPRPvasRESDRLGPLIDWMRAHL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 234 SQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGL 313
Cdd:PRK09393  232 AEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAAT 311

                         330
                  ....*....|.
gi 2184264921 314 TPLDYRRRFSR 324
Cdd:PRK09393  312 SPAAYRKRFGR 322
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 4-198 2.25e-37

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 131.85  E-value: 2.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   4 VVILAFDGALASAITGIVDLFSMAgaswNRIQNqqiERLFEVKIASPKGQSIQCINGIKMHAELSYQEIQYADLVVVPti 83
Cdd:cd03137     1 VAVLVFPGVSLLDLSGPAEVFGEA----NRALG---PPAYELRVCSPEGGPVRSSSGLSLVADAGLDALAAADTVIVP-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  84 GAALLSVLQRTPELIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVELKVERMITHADHI 163
Cdd:cd03137    72 GGPDVDGRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNV 151

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2184264921 164 YCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSFVI 198
Cdd:cd03137   152 WTSAGVTAGIDLCLHLVREDLGAAVANRVARRLVV 186
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 4-199 5.48e-34

AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153230 [Multi-domain]  Cd Length: 185  Bit Score: 123.08  E-value: 5.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   4 VVILAFDGALASAITGIVDLFSMAgaswNRIQNQqieRLFEVKIASPKGQSIQCINGIKMHAELSYQEIQYADLVVVPti 83
Cdd:cd03136     1 FGFLLLPGFSLLALASAIEPLRAA----NRLAGR---ELYRWRVLSLDGAPVTSSNGLRVAPDAALEDAPPLDYLFVV-- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  84 gAALLSVLQRTPELIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVELKVERMITHADHI 163
Cdd:cd03136    72 -GGLGARRAVTPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQVTRDLFEIDGDRL 150

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2184264921 164 YCAgGGLAWFDLGLHLIERFYGFEVAIQTAKSFVID 199
Cdd:cd03136   151 TCA-GGTAALDLMLELIARDHGAALAARVAEQFLHD 185
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 4-200 1.44e-26

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153233 [Multi-domain]  Cd Length: 183  Bit Score: 103.39  E-value: 1.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   4 VVILAFDGALASAITGIVDLFSMAGaswnriqnqQIERLFEVKIASPKGQSIQCINGIKMHAELSYQEIQYADLVVVPti 83
Cdd:cd03139     1 VGILLFPGVEVLDVIGPYEVFGRAP---------RLAAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDLDVLLVP-- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  84 GAALLSVLQRTPELIIFL--QYAQQQHfmIAANCTGNFFLAEAGILNGKQATTHWGFEAIFKQRYPQVElkVERMITHAD 161
Cdd:cd03139    70 GGGGTRALVNDPALLDFIrrQAARAKY--VTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVV--VDARWVVDG 145

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2184264921 162 HIYCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSfvIDY 200
Cdd:cd03139   146 NIWTSGGVSAGIDMALALVARLFGEELAQAVALL--IEY 182
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
135-324 1.06e-24

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 100.62  E-value: 1.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 135 HWGFEAIFKQRYPQVELKVERMITHADHIYCAGGGLAWFDLGLHLIERFYGFEVAIQTAKSFVIDYRRDSQLSYSLMKIA 214
Cdd:COG2207    67 LGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLL 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 215 KPHQDALVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLA 294
Cdd:COG2207   147 LLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYE 226

                         170       180       190
                  ....*....|....*....|....*....|
gi 2184264921 295 VGYNDSSSFRRLFLKKTGLTPLDYRRRFSR 324
Cdd:COG2207   227 LGFSSQSHFSRAFKKRFGVTPSEYRKRLRA 256
HTH_18 pfam12833
Helix-turn-helix domain;
242-321 3.64e-24

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 93.81  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 242 IAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQL-EQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYRR 320
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 2184264921 321 R 321
Cdd:pfam12833  81 R 81
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
236-319 1.00e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 92.62  E-value: 1.00e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  236 NFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTP 315
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 2184264921  316 LDYR 319
Cdd:smart00342  81 SEYR 84
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 216-321 1.73e-21

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: 93.58  E-value: 1.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 216 PHQDALVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDyTVEQIMLAV 295
Cdd:COG2169    80 PPRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGL-SVTDAAYAA 158

                          90       100
                  ....*....|....*....|....*.
gi 2184264921 296 GYNDSSSFRRLFLKKTGLTPLDYRRR 321
Cdd:COG2169   159 GFGSLSRFYEAFKKLLGMTPSAYRRG 184
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
217-319 3.27e-16

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 77.41  E-value: 3.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 217 HQDALVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVG 296
Cdd:PRK13503  168 NSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCG 247

                          90       100
                  ....*....|....*....|...
gi 2184264921 297 YNDSSSFRRLFLKKTGLTPLDYR 319
Cdd:PRK13503  248 FGDSNHFSTLFRREFSWSPRDIR 270
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 202-319 8.95e-15

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: 74.33  E-value: 8.95e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 202 RDSQLSYSLMKIAKP---HQDALVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAAr 278
Cdd:TIGR04094 264 RDSAIIYFTELLHEIsinHHSPLIRAVIQYINLNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEA- 342

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2184264921 279 KQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYR 319
Cdd:TIGR04094 343 KYLLRSQIPVSEVSNELGFYDLSHFSRTFKKHTGVSPKQYQ 383
PRK10371 PRK10371
transcriptional regulator MelR;
212-320 1.85e-13

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 69.85  E-value: 1.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 212 KIAKPHQDALVQEVQNWMEQ-------HYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQT 284
Cdd:PRK10371  176 KTSRTHKNSVSRHAQFYVSQmlgfiaeNYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDT 255

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2184264921 285 DYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYRR 320
Cdd:PRK10371  256 DKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYRK 291
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 2-139 5.91e-13

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 65.74  E-value: 5.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   2 KQVVILAFDGALASAITGIVDLFSMAGaswnriqnqqierlFEVKIASPKGQSIQCINGIKMHAELSYQEIQYA--DLVV 79
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAG--------------IKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDdyDALV 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  80 VPTiGAALLSVLQRTPELIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFE 139
Cdd:pfam01965  67 LPG-GRAGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVK 125
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
219-324 2.18e-12

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 66.54  E-value: 2.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 219 DALVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYN 298
Cdd:PRK10572  182 DPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYD 261

                          90       100
                  ....*....|....*....|....*.
gi 2184264921 299 DSSSFRRLFLKKTGLTPLDYRRRFSR 324
Cdd:PRK10572  262 DQLYFSRVFKKCTGASPSEFRARCEE 287
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-139 1.45e-11

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 62.04  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   1 MKQVVILAFDGALASAITGIVDLFSMAGaswnriqnqqierlFEVKIASP-KGQSIQCINGIKMHAELSYQEI---QYaD 76
Cdd:COG0693     2 MKKVLILLTDGFEDEELTVPYDALREAG--------------AEVDVASPeGGPPVTSKHGITVTADKTLDDVdpdDY-D 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2184264921  77 LVVVP--TIGAALLsvlqRT-PELIIFLQYAQQQHFMIAANCTGNFFLAEAGILNGKQATTHWGFE 139
Cdd:COG0693    67 ALVLPggHGAPDDL----REdPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIE 128
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
217-321 5.99e-11

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 58.78  E-value: 5.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 217 HQDaLVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVG 296
Cdd:PRK10219    3 HQK-IIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLG 81

                          90       100
                  ....*....|....*....|....*
gi 2184264921 297 YNDSSSFRRLFLKKTGLTPLDYRRR 321
Cdd:PRK10219   82 YVSQQTFSRVFRRQFDRTPSDYRHR 106
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
229-324 1.08e-10

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 61.46  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 229 MEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFL 308
Cdd:PRK13501  185 LQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFT 264

                          90
                  ....*....|....*.
gi 2184264921 309 KKTGLTPLDYRRRFSR 324
Cdd:PRK13501  265 REAGMTPRDYRQRFIR 280
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
219-319 1.31e-08

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 55.06  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 219 DALVQEVQNWMEQhysqNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYN 298
Cdd:PRK13502  179 DKLITALANSLEC----PFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFE 254

                          90       100
                  ....*....|....*....|.
gi 2184264921 299 DSSSFRRLFLKKTGLTPLDYR 319
Cdd:PRK13502  255 DSNYFSVVFTRETGMTPSQWR 275
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 265-323 5.39e-08

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 53.22  E-value: 5.39e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2184264921 265 PNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYRRRFS 323
Cdd:PRK10296  217 PMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRKKLT 275
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 229-270 6.07e-08

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: 48.30  E-value: 6.07e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2184264921 229 MEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQ 270
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
237-319 1.19e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 49.33  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 237 FNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPL 316
Cdd:PRK13500  223 FALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPS 302


                  ...
gi 2184264921 317 DYR 319
Cdd:PRK13500  303 QWR 305
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 43-134 1.49e-06

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 47.60  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  43 FEVKIASPKGQSIQCINGIKMHAELSYQEIQYADLVVVPTIGAALLSVLQrTPELIIFLQYAQQQHFMIAANCTGNFFLA 122
Cdd:cd03140    27 FEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWDNPE-APDLAGLVRQALKQGKPVAAICGATLALA 105

                          90
                  ....*....|..
gi 2184264921 123 EAGILNGKQATT 134
Cdd:cd03140   106 RAGLLNNRKHTS 117
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 43-183 4.29e-06

Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 46.01  E-value: 4.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  43 FEVKIAS-PKGQSIQCINGIKMHAELSYQEIQY--ADLVVVP--TIGAALLSvlqRTPELIIFLQYAQQQHFMIAANCTG 117
Cdd:cd03135    26 IEVTTASlEKKLAVGSSHGIKVKADKTLSDVNLddYDAIVIPggLPGAQNLA---DNEKLIKLLKEFNAKGKLIAAICAA 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2184264921 118 NFFLAEAGILNGKQATTHWGFEA-IFKQRYPQVELKV-ERMIThadhiyCAGGGLAwFDLGLHLIERF 183
Cdd:cd03135   103 PAVLAKAGLLKGKKATCYPGFEDkLGGANYVDEPVVVdGNIIT------SRGPGTA-FEFALKIVEAL 163
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 242-323 1.12e-05

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 46.18  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 242 IAQHFNLSTRSLIRRFkAALDLAPNQYLQAMRIE--AARKQLEQTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYR 319
Cdd:PRK09685  220 IAGELGISVRSLYRLF-AEQGLVVAQYIRNRRLDrcADDLRPAADDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGEYR 298


                  ....
gi 2184264921 320 RRFS 323
Cdd:PRK09685  299 RKFR 302
PRK15121 PRK15121
MDR efflux pump AcrAB transcriptional activator RobA;
218-320 1.55e-04

MDR efflux pump AcrAB transcriptional activator RobA;


Pssm-ID: 185076 [Multi-domain]  Cd Length: 289  Bit Score: 42.69  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 218 QDALVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLEQTDYTVEQIMLAVGY 297
Cdd:PRK15121    3 QAGIIRDLLIWLEGHLDQPLSLDNVAAKAGYSKWHLQRMFKDVTGHAIGAYIRARRLSKAAVALRLTSRPILDIALQYRF 82

                          90       100
                  ....*....|....*....|...
gi 2184264921 298 NDSSSFRRLFLKKTGLTPLDYRR 320
Cdd:PRK15121   83 DSQQTFTRAFKKQFAQTPALYRR 105
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 218-318 3.63e-04

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 41.59  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 218 QDALVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAmRIEAARKQLEQTDYTVEQIMLAVGY 297
Cdd:PRK15186  179 QNTLAENIYNIIISDISRKWALKDISDSLYMSCSTLKRKLKQENTSFSEVYLNA-RMNKATKLLRNSEYNITRVAYMCGY 257

                          90       100
                  ....*....|....*....|.
gi 2184264921 298 NDSSSFRRLFLKKTGLTPLDY 318
Cdd:PRK15186  258 DSASYFTCVFKKHFKTTPSEF 278
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 213-315 5.16e-04

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 41.13  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 213 IAKPHQDALVQEVQNWMEQHYSQNFNLDEIAQHFNLSTRSLIRRFKAALDLAPNQYLQAmRIEAARKQLEQTDYTVEQIM 292
Cdd:PRK15185  199 ILSSAQITLKERVYNIISSSPSRQWKLTDVADHIFMSTSTLKRKLAEEGTSFSDIYLSA-RMNQAAKLLRIGNHNVNAVA 277

                          90       100
                  ....*....|....*....|...
gi 2184264921 293 LAVGYNDSSSFRRLFLKKTGLTP 315
Cdd:PRK15185  278 LKCGYDSTSYFIQCFKKYFKTTP 300
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 203-325 7.71e-04

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 40.68  E-value: 7.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921 203 DSQLSYSLMKIAKPHQDALVQEVQNwmeQHYSQNFNLDEIAQHFnLSTRSLIRRFKAALDLAPNQYLQAMRIEAARKQLE 282
Cdd:PRK09978  128 DEHFIPLLLNVLQPNMRTRVCTVIN---NNIAHEWTLARIASEL-LMSPSLLKKKLREEETSYSQLLTECRMQRALQLIV 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2184264921 283 QTDYTVEQIMLAVGYNDSSSFRRLFLKKTGLTPLDYRRRFSRH 325
Cdd:PRK09978  204 IHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQERSAQG 246
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 279-320 9.32e-04

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: 36.36  E-value: 9.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2184264921 279 KQLEQTDYTVEQIMLAVGYnDSSSFRRLFLKKTGLTPLDYRR 320
Cdd:pfam00165   2 RENLSTNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 43-133 1.04e-03

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 39.06  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921  43 FEVKIASPK-GQSIQCING-IKMHAELSYQEIQYA--DLVVVPtiGAALLSVLQRTPELIIFLQYAQQQHFMIAANCTGN 118
Cdd:cd03134    27 AEVVVAGPEaGGEIQGKHGyDTVTVDLTIADVDADdyDALVIP--GGTNPDKLRRDPDAVAFVRAFAEAGKPVAAICHGP 104

                          90
                  ....*....|....*
gi 2184264921 119 FFLAEAGILNGKQAT 133
Cdd:cd03134   105 WVLISAGVVRGRKLT 119
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 4-121 9.85e-03

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 35.65  E-value: 9.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2184264921   4 VVILAFDGALASAITGIVDLFSMAGaswnriqnqqierlFEVKIASPKGQSIQCIngikmhaelsyQEIQYADLVVVPTi 83
Cdd:cd01653     1 VAVLLFPGFEELELASPLDALREAG--------------AEVDVVSPDGGPVESD-----------VDLDDYDGLILPG- 54

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2184264921  84 GAALLSVLQRTPELIIFLQYAQQQHFMIAANCTGNFFL 121
Cdd:cd01653    55 GPGTPDDLARDEALLALLREAAAAGKPILGICLGAQLL 92
 
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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