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Conserved domains on  [gi|489016034|ref|WP_002926554|]
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MULTISPECIES: HigA family addiction module antitoxin [Streptococcus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VapI COG3093
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ...
 15-93 1.31e-23

Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];


:

Pssm-ID: 442327 [Multi-domain]  Cd Length: 87  Bit Score: 92.95  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489016034  15 HPGQYV-EEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQTWLNLQNAYDVKVAEIAEQRE 93
Cdd:COG3093    8 HPGEILrEEFLEPLGLSQTELAKALGVSRQRISEILNGKRAITADTALRLARAFGTSAEFWLNLQAAYDLWLARQKAGEE 87
ImmA COG2856
Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, ...
 252-346 4.18e-10

Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 442104  Cd Length: 105  Bit Score: 56.21  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489016034 252 DRNKASDIFWFSLFHEIGHILENDFSSDDGNSESYLRSEEQADQFAKDLLIRPEDYQAFVEKGNFDksDVIRFAEEIDIH 331
Cdd:COG2856    4 NSNLSPERQRFTLAHELGHLLLHRGGETDLFLSSDDKIEREANAFAAELLMPEEALRELLKEKLSE--DLEELAKRFGVS 81

                         90
                 ....*....|....*
gi 489016034 332 PSVVLGRLQNEGILS 346
Cdd:COG2856   82 EEALLYRLKELGLID 96
 
Name Accession Description Interval E-value
VapI COG3093
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ...
 15-93 1.31e-23

Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];


Pssm-ID: 442327 [Multi-domain]  Cd Length: 87  Bit Score: 92.95  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489016034  15 HPGQYV-EEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQTWLNLQNAYDVKVAEIAEQRE 93
Cdd:COG3093    8 HPGEILrEEFLEPLGLSQTELAKALGVSRQRISEILNGKRAITADTALRLARAFGTSAEFWLNLQAAYDLWLARQKAGEE 87
antidote_HigA TIGR02607
addiction module antidote protein, HigA family; Members of this family form a distinct clade ...
 15-87 4.20e-20

addiction module antidote protein, HigA family; Members of this family form a distinct clade within the larger family HTH_3 of helix-turn-helix proteins, described by pfam01381. Members of this clade are strictly bacterial and nearly always shorter than 110 amino acids. This family includes the characterized member HigA, without which the killer protein HigB cannot be cloned. The hig (host inhibition of growth) system is noted to be unusual in that killer protein is uncoded by the upstream member of the gene pair. [Regulatory functions, DNA interactions, Regulatory functions, Protein interactions, Mobile and extrachromosomal element functions, Other]


Pssm-ID: 274228 [Multi-domain]  Cd Length: 78  Bit Score: 83.44  E-value: 4.20e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489016034   15 HPGQ-YVEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQTWLNLQNAYDVKVAE 87
Cdd:TIGR02607   4 HPGEiLLEEFLEPLGLSVRALAKALGVSRSTLSRIVNGRAAITADMALRLAKALGTSPEFWLNLQNAYDLWIAE 77
ImmA COG2856
Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, ...
 252-346 4.18e-10

Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442104  Cd Length: 105  Bit Score: 56.21  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489016034 252 DRNKASDIFWFSLFHEIGHILENDFSSDDGNSESYLRSEEQADQFAKDLLIRPEDYQAFVEKGNFDksDVIRFAEEIDIH 331
Cdd:COG2856    4 NSNLSPERQRFTLAHELGHLLLHRGGETDLFLSSDDKIEREANAFAAELLMPEEALRELLKEKLSE--DLEELAKRFGVS 81

                         90
                 ....*....|....*
gi 489016034 332 PSVVLGRLQNEGILS 346
Cdd:COG2856   82 EEALLYRLKELGLID 96
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 17-74 6.67e-08

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 48.70  E-value: 6.67e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489016034  17 GQYVEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQTW 74
Cdd:cd00093    1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL 58
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 20-74 9.95e-07

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 45.22  E-value: 9.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489016034   20 VEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQTW 74
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLDEL 55
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
20-72 2.71e-06

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 44.05  E-value: 2.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 489016034    20 VEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQ 72
Cdd:smart00530   2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLD 54
Peptidase_M78 pfam06114
IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, ...
 261-306 1.57e-04

IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.


Pssm-ID: 399250  Cd Length: 122  Bit Score: 40.87  E-value: 1.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 489016034  261 WFSLFHEIGHIL---ENDFSSDDGNSESYLRSEEQADQFAKDLLIrPED 306
Cdd:pfam06114  42 RFTLAHELGHLLlheGGDTLSDQFDFKTAEAREREANIFAAALLM-PYE 89
 
Name Accession Description Interval E-value
VapI COG3093
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ...
 15-93 1.31e-23

Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];


Pssm-ID: 442327 [Multi-domain]  Cd Length: 87  Bit Score: 92.95  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489016034  15 HPGQYV-EEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQTWLNLQNAYDVKVAEIAEQRE 93
Cdd:COG3093    8 HPGEILrEEFLEPLGLSQTELAKALGVSRQRISEILNGKRAITADTALRLARAFGTSAEFWLNLQAAYDLWLARQKAGEE 87
antidote_HigA TIGR02607
addiction module antidote protein, HigA family; Members of this family form a distinct clade ...
 15-87 4.20e-20

addiction module antidote protein, HigA family; Members of this family form a distinct clade within the larger family HTH_3 of helix-turn-helix proteins, described by pfam01381. Members of this clade are strictly bacterial and nearly always shorter than 110 amino acids. This family includes the characterized member HigA, without which the killer protein HigB cannot be cloned. The hig (host inhibition of growth) system is noted to be unusual in that killer protein is uncoded by the upstream member of the gene pair. [Regulatory functions, DNA interactions, Regulatory functions, Protein interactions, Mobile and extrachromosomal element functions, Other]


Pssm-ID: 274228 [Multi-domain]  Cd Length: 78  Bit Score: 83.44  E-value: 4.20e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489016034   15 HPGQ-YVEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQTWLNLQNAYDVKVAE 87
Cdd:TIGR02607   4 HPGEiLLEEFLEPLGLSVRALAKALGVSRSTLSRIVNGRAAITADMALRLAKALGTSPEFWLNLQNAYDLWIAE 77
ImmA COG2856
Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, ...
 252-346 4.18e-10

Zn-dependent peptidase ImmA, M78 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442104  Cd Length: 105  Bit Score: 56.21  E-value: 4.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489016034 252 DRNKASDIFWFSLFHEIGHILENDFSSDDGNSESYLRSEEQADQFAKDLLIRPEDYQAFVEKGNFDksDVIRFAEEIDIH 331
Cdd:COG2856    4 NSNLSPERQRFTLAHELGHLLLHRGGETDLFLSSDDKIEREANAFAAELLMPEEALRELLKEKLSE--DLEELAKRFGVS 81

                         90
                 ....*....|....*
gi 489016034 332 PSVVLGRLQNEGILS 346
Cdd:COG2856   82 EEALLYRLKELGLID 96
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 17-74 6.67e-08

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 48.70  E-value: 6.67e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 489016034  17 GQYVEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQTW 74
Cdd:cd00093    1 GERLKELRKEKGLTQEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALGVSLDEL 58
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
17-71 2.55e-07

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 47.68  E-value: 2.55e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489016034  17 GQYVEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSM 71
Cdd:COG1396    9 GERLRELRKARGLTQEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALGVSL 63
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
17-72 7.73e-07

DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 45.99  E-value: 7.73e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489016034  17 GQYVEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQ 72
Cdd:COG1476    6 GNRLKELRKERGLTQEELAELLGVSRQTISAIENGKYNPSLELALKIARALGVSLE 61
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
 20-74 9.95e-07

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 45.22  E-value: 9.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 489016034   20 VEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQTW 74
Cdd:pfam01381   1 LKELREELGLSQEELAEKLGVSRSTISKIENGKREPSLETLKKLAEALGVSLDEL 55
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
20-72 2.71e-06

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 44.05  E-value: 2.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 489016034    20 VEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSMQ 72
Cdd:smart00530   2 LKELREEKGLTQEELAEKLGVSRSTLSRIENGKRKPSLETLKKLAKALGVSLD 54
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 12-71 8.43e-06

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 43.00  E-value: 8.43e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489016034  12 IAFHPGQYVEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSM 71
Cdd:COG1813    9 LVEDYGERIREAREARGLSQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALGISL 68
HTH_19 pfam12844
Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. ...
 17-75 3.98e-05

Helix-turn-helix domain; Members of this family contains a DNA-binding helix-turn-helix domain. This family contains many example antitoxins from bacterial toxin-antitoxin systems. These antitoxins are likely to be DNA-binding domains.


Pssm-ID: 463728 [Multi-domain]  Cd Length: 64  Bit Score: 41.12  E-value: 3.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489016034   17 GQYVEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKLSGVSmQTWL 75
Cdd:pfam12844   1 GERLRKAREERGLTQEELAERLGISRSQLSAIENGKSVPPAETLYKIAELLGVP-ANWL 58
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
 9-66 1.28e-04

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 40.39  E-value: 1.28e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489016034   9 KDLIAFHP----GQYVEEMIEDYNVTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAKL 66
Cdd:COG3620    7 RDVVTVSPddtlGEALRLMRKELGLSQLPVAELVGVSQSDILRIESGKRDPTVSTLEKIAEA 68
Peptidase_M78 pfam06114
IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, ...
 261-306 1.57e-04

IrrE N-terminal-like domain; This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.


Pssm-ID: 399250  Cd Length: 122  Bit Score: 40.87  E-value: 1.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 489016034  261 WFSLFHEIGHIL---ENDFSSDDGNSESYLRSEEQADQFAKDLLIrPED 306
Cdd:pfam06114  42 RFTLAHELGHLLlheGGDTLSDQFDFKTAEAREREANIFAAALLM-PYE 89
YiaG COG2944
DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription];
16-47 3.14e-04

DNA-binding transcriptional regulator YiaG, XRE-type HTH domain [Transcription];


Pssm-ID: 442187 [Multi-domain]  Cd Length: 64  Bit Score: 38.38  E-value: 3.14e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 489016034  16 PGQYVEEMIEDYNVTQKEFAERLGVSAKTVSK 47
Cdd:COG2944    7 TPEEIRALRERLGLSQAEFAALLGVSVSTVRR 38
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
29-65 3.22e-04

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 38.72  E-value: 3.22e-04
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 489016034    29 VTQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAK 65
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLA 37
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
29-62 3.56e-04

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 42.11  E-value: 3.56e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 489016034  29 VTQKEFAERLGVSAKTVSKLVNAEESISKETAHK 62
Cdd:COG1609    4 VTIKDVARLAGVSVATVSRVLNGPPRVSEETRER 37
LacI pfam00356
Bacterial regulatory proteins, lacI family;
30-65 4.35e-04

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 37.62  E-value: 4.35e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 489016034   30 TQKEFAERLGVSAKTVSKLVNAEESISKETAHKLAK 65
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEA 36
YozG COG3655
DNA-binding transcriptional regulator, XRE family [Transcription];
22-90 9.41e-04

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


Pssm-ID: 442872 [Multi-domain]  Cd Length: 69  Bit Score: 37.43  E-value: 9.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489016034  22 EMIEDYNVTQKEFAERLGVSAKTVSKLVNaeesisketahklAKLSGVSMQTWLNLQNAYDVKVAEIAE 90
Cdd:COG3655    8 ELLAERGMTKKELAEATGISRATLSRLKN-------------GKAKAVRLDTLEKICKALDCQPGDLLE 63
HTH_26 pfam13443
Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to ...
 22-65 1.70e-03

Cro/C1-type HTH DNA-binding domain; This is a helix-turn-helix domain that probably binds to DNA.


Pssm-ID: 433211 [Multi-domain]  Cd Length: 63  Bit Score: 36.36  E-value: 1.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 489016034   22 EMIEDYNVTQKEFAERLGVSAKTVSKLVNAE-ESISKETAHKLAK 65
Cdd:pfam13443   4 KLMADRGISKSDLARATGISRATLSRLRKGKpKRVSLDTLDKICD 48
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 32-62 2.72e-03

Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.


Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 35.46  E-value: 2.72e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 489016034  32 KEFAERLGVSAKTVSKLVNAEESISKETAHK 62
Cdd:cd01392    1 KDIARAAGVSVATVSRVLNGKPRVSEETRER 31
Spo0J COG1475
Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, ...
 21-96 2.76e-03

Chromosome segregation protein Spo0J, contains ParB-like nuclease domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441084 [Multi-domain]  Cd Length: 241  Bit Score: 38.82  E-value: 2.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489016034  21 EEMIEDYNVTQKEFAERLGVSAKTVSKLVN------------AEESISKETAHKLAKLSGVSMQtwlnlQNAYDVKVAEI 88
Cdd:COG1475  113 QRLLEEFGLTQEEIAERLGKSRSEVSNLLRllklppevqealREGKLSLGHARALAALSDPERQ-----EELAEKIIEEG 187


                 ....*...
gi 489016034  89 AEQRELEE 96
Cdd:COG1475  188 LSVRETEE 195
HigA COG5499
Antitoxin component HigA of the HigAB toxin-antitoxin module, contains an N-terminal HTH ...
 24-70 4.94e-03

Antitoxin component HigA of the HigAB toxin-antitoxin module, contains an N-terminal HTH domain [Defense mechanisms];


Pssm-ID: 444250  Cd Length: 127  Bit Score: 36.73  E-value: 4.94e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489016034  24 IEDYNVTQKEFAERLGvSAKTVSKLVNAEESISKETAHKLAKLSGVS 70
Cdd:COG5499   74 MEQHGLTQKDLAPEIG-SKSRVSEILNGKRSLTLEMIRKLAERFGIP 119
 
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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