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Conserved domains on  [gi|496228152|ref|WP_008942187|]
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MULTISPECIES: helix-turn-helix domain-containing protein [Acinetobacter]

Protein Classification

helix-turn-helix domain-containing protein( domain architecture ID 11458298)

helix-turn-helix domain-containing protein with a putative ATP-dependent DNA helicase RecG C-terminal domain, may bind DNA and function as a transcriptional regulator

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2865 COG2865
Predicted transcriptional regulator, contains HTH domain [Transcription];
11-131 3.84e-36

Predicted transcriptional regulator, contains HTH domain [Transcription];


:

Pssm-ID: 442112  Cd Length: 123  Bit Score: 129.62  E-value: 3.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228152  11 IQKGESKTLEFKQQLPKGQQIAKTLIAFANGSGGKLIVGVTDDRQLVGIqDDIFELQDKITSMIYELCAPQLAAQIYIEN 90
Cdd:COG2865    7 LAGGESETLEFKESLNEPDEILKTVCAFANTEGGTLLIGVDDDGEIVGL-DDPDKLLERLENLIADNISPPIRPDVEEVE 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496228152  91 IAGVELLVVEVARGSLFPYYLKSvgrEQGTYIRLGASNRVA 131
Cdd:COG2865   86 IDGKRVLVIEVPPGPSKPYYLKG---KGGAYIRVGSSSRPL 123
HATPase_c_4 pfam13749
Putative ATP-dependent DNA helicase recG C-terminal; This domain may well interact selectively ...
 290-376 2.04e-30

Putative ATP-dependent DNA helicase recG C-terminal; This domain may well interact selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.


:

Pssm-ID: 463975  Cd Length: 88  Bit Score: 113.01  E-value: 2.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228152  290 GRNIKVAVYDDLVNIVSPGGLPNGLTEADL-LQGRSEIRNRVLARVFRELGYIEHWGSGLQRIQQMCEAENLPTPEFVET 368
Cdd:pfam13749   1 GAPIQIEIFDDRLEITSPGGLPGGVTVEDLgLDGVSKSRNPLLASLFRRLGLIEERGSGIRRILEAMEEAGLPEPEFIED 80


                  ....*...
gi 496228152  369 GDFFDVKL 376
Cdd:pfam13749  81 GDSFRVTL 88
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 411-462 2.18e-07

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


:

Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 51.07  E-value: 2.18e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496228152 411 LTERQQEILVLIQ-----HNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLERVGG 462
Cdd:COG1974    4 LTKRQREILDFIKeyireRGYPPSQREIAEALGLSSSAVHRHLKALEKKGYLRRDPG 60
 
Name Accession Description Interval E-value
COG2865 COG2865
Predicted transcriptional regulator, contains HTH domain [Transcription];
11-131 3.84e-36

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 442112  Cd Length: 123  Bit Score: 129.62  E-value: 3.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228152  11 IQKGESKTLEFKQQLPKGQQIAKTLIAFANGSGGKLIVGVTDDRQLVGIqDDIFELQDKITSMIYELCAPQLAAQIYIEN 90
Cdd:COG2865    7 LAGGESETLEFKESLNEPDEILKTVCAFANTEGGTLLIGVDDDGEIVGL-DDPDKLLERLENLIADNISPPIRPDVEEVE 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496228152  91 IAGVELLVVEVARGSLFPYYLKSvgrEQGTYIRLGASNRVA 131
Cdd:COG2865   86 IDGKRVLVIEVPPGPSKPYYLKG---KGGAYIRVGSSSRPL 123
HATPase_c_4 pfam13749
Putative ATP-dependent DNA helicase recG C-terminal; This domain may well interact selectively ...
 290-376 2.04e-30

Putative ATP-dependent DNA helicase recG C-terminal; This domain may well interact selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.


Pssm-ID: 463975  Cd Length: 88  Bit Score: 113.01  E-value: 2.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228152  290 GRNIKVAVYDDLVNIVSPGGLPNGLTEADL-LQGRSEIRNRVLARVFRELGYIEHWGSGLQRIQQMCEAENLPTPEFVET 368
Cdd:pfam13749   1 GAPIQIEIFDDRLEITSPGGLPGGVTVEDLgLDGVSKSRNPLLASLFRRLGLIEERGSGIRRILEAMEEAGLPEPEFIED 80


                  ....*...
gi 496228152  369 GDFFDVKL 376
Cdd:pfam13749  81 GDSFRVTL 88
AlbA_2 pfam04326
Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.
 15-132 7.77e-28

Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.


Pssm-ID: 461263  Cd Length: 116  Bit Score: 107.00  E-value: 7.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228152   15 ESKTLEFKQQL--PKGQQIAKTLIAFANGSGGKLIVGVTDDRQLVGIQDDIFELQDKITSMIYELCAPQLAAQIYIENIA 92
Cdd:pfam04326   1 ESETLEFKESLgkSSKKKIAKTISAFANTEGGTIVIGVDDTGKIVGVSDDEKDTEDLLKNQILDLIKPPIEVDIEEIEID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 496228152   93 GVELLVVEVARGSLFPYYlksvGREQGTYIRLGASNRVAS 132
Cdd:pfam04326  81 GKYVLVVEIPEGKLKPYY----TNKGEVYIRVGSSSRPAS 116
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 411-462 2.18e-07

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 51.07  E-value: 2.18e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496228152 411 LTERQQEILVLIQ-----HNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLERVGG 462
Cdd:COG1974    4 LTKRQREILDFIKeyireRGYPPSQREIAEALGLSSSAVHRHLKALEKKGYLRRDPG 60
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
413-457 4.76e-06

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 43.58  E-value: 4.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 496228152  413 ERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWL 457
Cdd:pfam13412   1 ETDRKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 417-470 4.62e-05

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 41.52  E-value: 4.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496228152 417 EILVLIQHNPKvSYRSLAEQLGINQSALQKHLNHLKDAGWLE-RVGGTRGYWAIK 470
Cdd:cd00090   11 RILRLLLEGPL-TVSELAERLGLSQSTVSRHLKKLEEAGLVEsRREGRRVYYSLT 64
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
411-459 3.68e-04

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 39.88  E-value: 3.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 496228152   411 LTERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLER 459
Cdd:smart00347   8 LTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRR 56
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 409-462 9.92e-03

SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA. [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 273106 [Multi-domain]  Cd Length: 199  Bit Score: 37.39  E-value: 9.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496228152  409 SQLTERQQEILVLI-------QHNPkvSYRSLAEQLGI-NQSALQKHLNHLKDAGWLERVGG 462
Cdd:TIGR00498   2 KPLTARQQEVLDLIrahiestGYPP--SIREIARAVGLrSPSAAEEHLKALERKGYIERDPG 61
 
Name Accession Description Interval E-value
COG2865 COG2865
Predicted transcriptional regulator, contains HTH domain [Transcription];
11-131 3.84e-36

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 442112  Cd Length: 123  Bit Score: 129.62  E-value: 3.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228152  11 IQKGESKTLEFKQQLPKGQQIAKTLIAFANGSGGKLIVGVTDDRQLVGIqDDIFELQDKITSMIYELCAPQLAAQIYIEN 90
Cdd:COG2865    7 LAGGESETLEFKESLNEPDEILKTVCAFANTEGGTLLIGVDDDGEIVGL-DDPDKLLERLENLIADNISPPIRPDVEEVE 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 496228152  91 IAGVELLVVEVARGSLFPYYLKSvgrEQGTYIRLGASNRVA 131
Cdd:COG2865   86 IDGKRVLVIEVPPGPSKPYYLKG---KGGAYIRVGSSSRPL 123
HATPase_c_4 pfam13749
Putative ATP-dependent DNA helicase recG C-terminal; This domain may well interact selectively ...
 290-376 2.04e-30

Putative ATP-dependent DNA helicase recG C-terminal; This domain may well interact selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.


Pssm-ID: 463975  Cd Length: 88  Bit Score: 113.01  E-value: 2.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228152  290 GRNIKVAVYDDLVNIVSPGGLPNGLTEADL-LQGRSEIRNRVLARVFRELGYIEHWGSGLQRIQQMCEAENLPTPEFVET 368
Cdd:pfam13749   1 GAPIQIEIFDDRLEITSPGGLPGGVTVEDLgLDGVSKSRNPLLASLFRRLGLIEERGSGIRRILEAMEEAGLPEPEFIED 80


                  ....*...
gi 496228152  369 GDFFDVKL 376
Cdd:pfam13749  81 GDSFRVTL 88
AlbA_2 pfam04326
Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.
 15-132 7.77e-28

Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.


Pssm-ID: 461263  Cd Length: 116  Bit Score: 107.00  E-value: 7.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228152   15 ESKTLEFKQQL--PKGQQIAKTLIAFANGSGGKLIVGVTDDRQLVGIQDDIFELQDKITSMIYELCAPQLAAQIYIENIA 92
Cdd:pfam04326   1 ESETLEFKESLgkSSKKKIAKTISAFANTEGGTIVIGVDDTGKIVGVSDDEKDTEDLLKNQILDLIKPPIEVDIEEIEID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 496228152   93 GVELLVVEVARGSLFPYYlksvGREQGTYIRLGASNRVAS 132
Cdd:pfam04326  81 GKYVLVVEIPEGKLKPYY----TNKGEVYIRVGSSSRPAS 116
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 411-462 2.18e-07

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 51.07  E-value: 2.18e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 496228152 411 LTERQQEILVLIQ-----HNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLERVGG 462
Cdd:COG1974    4 LTKRQREILDFIKeyireRGYPPSQREIAEALGLSSSAVHRHLKALEKKGYLRRDPG 60
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
413-457 4.76e-06

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 43.58  E-value: 4.76e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 496228152  413 ERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWL 457
Cdd:pfam13412   1 ETDRKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 409-460 2.84e-05

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 41.81  E-value: 2.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 496228152  409 SQLTERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLERV 460
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVERE 52
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 417-470 4.62e-05

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 41.52  E-value: 4.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 496228152 417 EILVLIQHNPKvSYRSLAEQLGINQSALQKHLNHLKDAGWLE-RVGGTRGYWAIK 470
Cdd:cd00090   11 RILRLLLEGPL-TVSELAERLGLSQSTVSRHLKKLEEAGLVEsRREGRRVYYSLT 64
Lrp COG1522
DNA-binding transcriptional regulator, Lrp family [Transcription];
410-461 6.20e-05

DNA-binding transcriptional regulator, Lrp family [Transcription];


Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 42.84  E-value: 6.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496228152 410 QLTERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLERVG 461
Cdd:COG1522    2 ELDEIDRRILRLLQEDGRLSFAELAERVGLSESTVLRRVRRLEEAGVIRGYG 53
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
405-460 1.04e-04

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 42.26  E-value: 1.04e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496228152 405 AIEASQLTERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLERV 460
Cdd:COG1846   30 ALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVERE 85
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
408-465 2.82e-04

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 42.22  E-value: 2.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 496228152 408 ASQLTERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLERVGGTRG 465
Cdd:COG2345    8 AALADPTRRRILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLVERETERRG 65
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
411-459 3.68e-04

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 39.88  E-value: 3.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 496228152   411 LTERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLER 459
Cdd:smart00347   8 LTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRR 56
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 411-459 4.47e-04

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 426012 [Multi-domain]  Cd Length: 59  Bit Score: 38.30  E-value: 4.47e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 496228152  411 LTERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLER 459
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIER 49
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
413-466 4.65e-04

Predicted transcriptional regulator, contains two HTH domains [Transcription];


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 40.63  E-value: 4.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496228152 413 ERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWL--ERVGGTRGY 466
Cdd:COG3398   21 DTRRRIYEYIRENPGIHFREIVRDLGLNRGTLRYHLRRLEREGKItsEKDGGRTRY 76
DmsR COG3413
Predicted transcriptional regulator, contains HTH domain [General function prediction only];
399-448 4.73e-04

Predicted transcriptional regulator, contains HTH domain [General function prediction only];


Pssm-ID: 442639 [Multi-domain]  Cd Length: 143  Bit Score: 40.31  E-value: 4.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 496228152 399 IEGLGGAIEASQLTERQQEILVLIQHN-----P-KVSYRSLAEQLGINQSALQKHL 448
Cdd:COG3413   74 LDRPTRSSLLDGLTDRQREALETAYEMgyfevPrEATLEELAEELGISKSTLSEHL 129
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
415-459 5.21e-04

Predicted transcriptional regulator, contains two HTH domains [Transcription];


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 40.63  E-value: 5.21e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 496228152 415 QQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLER 459
Cdd:COG3398   99 PRRILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGLVER 143
ArsR COG0640
DNA-binding transcriptional regulator, ArsR family [Transcription];
433-459 1.48e-03

DNA-binding transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 440405 [Multi-domain]  Cd Length: 92  Bit Score: 37.95  E-value: 1.48e-03
                         10        20
                 ....*....|....*....|....*..
gi 496228152 433 LAEQLGINQSALQKHLNHLKDAGWLER 459
Cdd:COG0640   39 LAEALGLSQSTVSHHLKVLREAGLVTS 65
HTH_ARSR smart00418
helix_turn_helix, Arsenical Resistance Operon Repressor;
417-472 1.48e-03

helix_turn_helix, Arsenical Resistance Operon Repressor;


Pssm-ID: 197713 [Multi-domain]  Cd Length: 66  Bit Score: 37.19  E-value: 1.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 496228152   417 EILVLIQHNPKvSYRSLAEQLGINQSALQKHLNHLKDAGWLE-RVGGTRGYWAIKKE 472
Cdd:smart00418   1 KILKLLAEGEL-CVCELAEILGLSQSTVSHHLKKLREAGLVEsRREGKRVYYSLTDE 56
HTH_10 pfam04967
HTH DNA binding domain;
411-449 1.60e-03

HTH DNA binding domain;


Pssm-ID: 282780 [Multi-domain]  Cd Length: 53  Bit Score: 36.43  E-value: 1.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 496228152  411 LTERQQEILVLIQHN-----PK-VSYRSLAEQLGINQSALQKHLN 449
Cdd:pfam04967   1 LTDRQLEVLRLAYEMgyfdyPRrVTLKELAKELGISKSTLSEHLR 45
LexA_DNA_bind pfam01726
LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor ...
 411-463 1.87e-03

LexA DNA binding domain; This is the DNA binding domain of the LexA SOS regulon repressor which prevents expression of DNA repair proteins. The aligned region contains a variant form of the helix-turn-helix DNA binding motif. This domain is found associated with pfam00717 the auto-proteolytic domain of LexA EC:3.4.21.88.


Pssm-ID: 396335 [Multi-domain]  Cd Length: 63  Bit Score: 36.59  E-value: 1.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496228152  411 LTERQQEILVLI-------QHNPkvSYRSLAEQLGINQ-SALQKHLNHLKDAGWLERVGGT 463
Cdd:pfam01726   2 LTERQREVLDFIkasieetGYPP--SRREIARALGLRSpNAAEEHLKALERKGYIERDPGK 60
HI1514 COG3941
Phage tail tape-measure protein, controls tail length [Mobilome: prophages, transposons];
387-475 3.67e-03

Phage tail tape-measure protein, controls tail length [Mobilome: prophages, transposons];


Pssm-ID: 443141 [Multi-domain]  Cd Length: 833  Bit Score: 39.95  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228152 387 AIGGAIDHLSGAIEGLGGAIEASQLTerQQEILVLIQHNPKVsYRSLAEQLGINQSALQKhlnhLKDAGWLERVGGTRGY 466
Cdd:COG3941  126 ALGGSQEQLEGATLALGQMWAKGKLQ--GEELNQLAERGVPA-WKLLAKAMGVTVAELQK----MVEKGKLGAEDAIPAL 198

                         90
                 ....*....|
gi 496228152 467 W-AIKKEFGG 475
Cdd:COG3941  199 LdAMGKRFGG 208
GlpR COG1349
DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, ...
 412-462 4.08e-03

DNA-binding transcriptional regulator of sugar metabolism, DeoR/GlpR family [Transcription, Carbohydrate transport and metabolism];


Pssm-ID: 440960 [Multi-domain]  Cd Length: 254  Bit Score: 38.96  E-value: 4.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496228152 412 TERQQEILVLIQHNPKVSYRSLAEQLGINQSALQKHLNHLKDAGWLERV-GG 462
Cdd:COG1349    4 EERRQKILELLRERGRVSVEELAERLGVSEETIRRDLAELEEQGLLRRVhGG 55
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 409-462 9.92e-03

SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA. [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 273106 [Multi-domain]  Cd Length: 199  Bit Score: 37.39  E-value: 9.92e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496228152  409 SQLTERQQEILVLI-------QHNPkvSYRSLAEQLGI-NQSALQKHLNHLKDAGWLERVGG 462
Cdd:TIGR00498   2 KPLTARQQEVLDLIrahiestGYPP--SIREIARAVGLrSPSAAEEHLKALERKGYIERDPG 61
 
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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