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Conserved domains on  [gi|491099184|ref|WP_004960785|]
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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 4.73e-38

Predicted transcriptional regulator, contains HTH domain [Transcription];


:

Pssm-ID: 442112  Cd Length: 123  Bit Score: 135.02  E-value: 4.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491099184  11 IQKGESKTLEFKQQLPKGQQIAKTLIAFANSSGGKLIIGVTDDRQLVGIqEDIFDLQDKITSMIYELCVPQLAVQIYVEN 90
Cdd:COG2865    7 LAGGESETLEFKESLNEPDEILKTVCAFANTEGGTLLIGVDDDGEIVGL-DDPDKLLERLENLIADNISPPIRPDVEEVE 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491099184  91 IDGIELLVVEVARGSLFPYYLKpmgREQGTYIRIGASNRVA 131
Cdd:COG2865   86 IDGKRVLVIEVPPGPSKPYYLK---GKGGAYIRVGSSSRPL 123
HATPase_c_4 pfam13749
Putative ATP-dependent DNA helicase recG C-terminal; This domain may well interact selectively ...
 290-376 2.71e-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: 2.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491099184  290 GRNIKVAVYDDLVNIVSPGGLPNGLTEDDL-LYGRSEIRNRVLARVFRELGYIEHWGSGLQRIIQMCEVEGLTTPEFSET 368
Cdd:pfam13749   1 GAPIQIEIFDDRLEITSPGGLPGGVTVEDLgLDGVSKSRNPLLASLFRRLGLIEERGSGIRRILEAMEEAGLPEPEFIED 80


                  ....*...
gi 491099184  369 GDFFDVKL 376
Cdd:pfam13749  81 GDSFRVTL 88
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 419-468 2.06e-06

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: 44.89  E-value: 2.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 491099184  419 LTERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWLERV 468
Cdd:pfam12802   3 LTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVERE 52
 
Name Accession Description Interval E-value
COG2865 COG2865
Predicted transcriptional regulator, contains HTH domain [Transcription];
11-131 4.73e-38

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 442112  Cd Length: 123  Bit Score: 135.02  E-value: 4.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491099184  11 IQKGESKTLEFKQQLPKGQQIAKTLIAFANSSGGKLIIGVTDDRQLVGIqEDIFDLQDKITSMIYELCVPQLAVQIYVEN 90
Cdd:COG2865    7 LAGGESETLEFKESLNEPDEILKTVCAFANTEGGTLLIGVDDDGEIVGL-DDPDKLLERLENLIADNISPPIRPDVEEVE 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491099184  91 IDGIELLVVEVARGSLFPYYLKpmgREQGTYIRIGASNRVA 131
Cdd:COG2865   86 IDGKRVLVIEVPPGPSKPYYLK---GKGGAYIRVGSSSRPL 123
AlbA_2 pfam04326
Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.
 15-132 1.46e-30

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


Pssm-ID: 461263  Cd Length: 116  Bit Score: 114.70  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491099184   15 ESKTLEFKQQL--PKGQQIAKTLIAFANSSGGKLIIGVTDDRQLVGIQEDIFDLQDKITSMIYELCVPQLAVQIYVENID 92
Cdd:pfam04326   1 ESETLEFKESLgkSSKKKIAKTISAFANTEGGTIVIGVDDTGKIVGVSDDEKDTEDLLKNQILDLIKPPIEVDIEEIEID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 491099184   93 GIELLVVEVARGSLFPYYlkpmGREQGTYIRIGASNRVAS 132
Cdd:pfam04326  81 GKYVLVVEIPEGKLKPYY----TNKGEVYIRVGSSSRPAS 116
HATPase_c_4 pfam13749
Putative ATP-dependent DNA helicase recG C-terminal; This domain may well interact selectively ...
 290-376 2.71e-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: 2.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491099184  290 GRNIKVAVYDDLVNIVSPGGLPNGLTEDDL-LYGRSEIRNRVLARVFRELGYIEHWGSGLQRIIQMCEVEGLTTPEFSET 368
Cdd:pfam13749   1 GAPIQIEIFDDRLEITSPGGLPGGVTVEDLgLDGVSKSRNPLLASLFRRLGLIEERGSGIRRILEAMEEAGLPEPEFIED 80


                  ....*...
gi 491099184  369 GDFFDVKL 376
Cdd:pfam13749  81 GDSFRVTL 88
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 419-468 2.06e-06

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: 44.89  E-value: 2.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 491099184  419 LTERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWLERV 468
Cdd:pfam12802   3 LTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVERE 52
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 419-470 1.10e-05

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 46.06  E-value: 1.10e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491099184 419 LTERQIQILGLIQQQPK-----ISYRQMTEQLGIHKSAIQKHLESLKDAGWLERVGG 470
Cdd:COG1974    4 LTKRQREILDFIKEYIRergypPSQREIAEALGLSSSAVHRHLKALEKKGYLRRDPG 60
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 421-478 2.28e-04

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: 39.59  E-value: 2.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491099184 421 ERQIQILGLIQQQPkISYRQMTEQLGIHKSAIQKHLESLKDAGWLE-RVGGTRGYWAIK 478
Cdd:cd00090    7 PTRLRILRLLLEGP-LTVSELAERLGLSQSTVSRHLKKLEEAGLVEsRREGRRVYYSLT 64
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
419-467 3.98e-04

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 39.50  E-value: 3.98e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 491099184   419 LTERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWLER 467
Cdd:smart00347   8 LTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRR 56
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
421-474 4.79e-03

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 39.00  E-value: 4.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491099184 421 ERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGW-LERVGGtRGY 474
Cdd:PRK11886   4 TVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLdIFSVKG-KGY 57
 
Name Accession Description Interval E-value
COG2865 COG2865
Predicted transcriptional regulator, contains HTH domain [Transcription];
11-131 4.73e-38

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 442112  Cd Length: 123  Bit Score: 135.02  E-value: 4.73e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491099184  11 IQKGESKTLEFKQQLPKGQQIAKTLIAFANSSGGKLIIGVTDDRQLVGIqEDIFDLQDKITSMIYELCVPQLAVQIYVEN 90
Cdd:COG2865    7 LAGGESETLEFKESLNEPDEILKTVCAFANTEGGTLLIGVDDDGEIVGL-DDPDKLLERLENLIADNISPPIRPDVEEVE 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 491099184  91 IDGIELLVVEVARGSLFPYYLKpmgREQGTYIRIGASNRVA 131
Cdd:COG2865   86 IDGKRVLVIEVPPGPSKPYYLK---GKGGAYIRVGSSSRPL 123
AlbA_2 pfam04326
Putative DNA-binding domain; This family belongs to the AlbA clan of DNA-binding domains.
 15-132 1.46e-30

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


Pssm-ID: 461263  Cd Length: 116  Bit Score: 114.70  E-value: 1.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491099184   15 ESKTLEFKQQL--PKGQQIAKTLIAFANSSGGKLIIGVTDDRQLVGIQEDIFDLQDKITSMIYELCVPQLAVQIYVENID 92
Cdd:pfam04326   1 ESETLEFKESLgkSSKKKIAKTISAFANTEGGTIVIGVDDTGKIVGVSDDEKDTEDLLKNQILDLIKPPIEVDIEEIEID 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 491099184   93 GIELLVVEVARGSLFPYYlkpmGREQGTYIRIGASNRVAS 132
Cdd:pfam04326  81 GKYVLVVEIPEGKLKPYY----TNKGEVYIRVGSSSRPAS 116
HATPase_c_4 pfam13749
Putative ATP-dependent DNA helicase recG C-terminal; This domain may well interact selectively ...
 290-376 2.71e-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: 2.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491099184  290 GRNIKVAVYDDLVNIVSPGGLPNGLTEDDL-LYGRSEIRNRVLARVFRELGYIEHWGSGLQRIIQMCEVEGLTTPEFSET 368
Cdd:pfam13749   1 GAPIQIEIFDDRLEITSPGGLPGGVTVEDLgLDGVSKSRNPLLASLFRRLGLIEERGSGIRRILEAMEEAGLPEPEFIED 80


                  ....*...
gi 491099184  369 GDFFDVKL 376
Cdd:pfam13749  81 GDSFRVTL 88
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 419-468 2.06e-06

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: 44.89  E-value: 2.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 491099184  419 LTERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWLERV 468
Cdd:pfam12802   3 LTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVERE 52
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 419-470 1.10e-05

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


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 46.06  E-value: 1.10e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491099184 419 LTERQIQILGLIQQQPK-----ISYRQMTEQLGIHKSAIQKHLESLKDAGWLERVGG 470
Cdd:COG1974    4 LTKRQREILDFIKEYIRergypPSQREIAEALGLSSSAVHRHLKALEKKGYLRRDPG 60
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
425-473 2.58e-05

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 45.30  E-value: 2.58e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 491099184 425 QILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWLERVGGTRG 473
Cdd:COG2345   17 RILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLVERETERRG 65
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
421-465 9.78e-05

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 39.72  E-value: 9.78e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 491099184  421 ERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWL 465
Cdd:pfam13412   1 ETDRKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
IclR COG1414
DNA-binding transcriptional regulator, IclR family [Transcription];
421-475 1.07e-04

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


Pssm-ID: 441024 [Multi-domain]  Cd Length: 253  Bit Score: 43.65  E-value: 1.07e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491099184 421 ERQIQILGLIQQQPK-ISYRQMTEQLGIHKSAIQKHLESLKDAGWLERVGGTRGYW 475
Cdd:COG1414    9 ERALAILEALAEAGGgLSLSELARRLGLPKSTVHRLLATLEEEGYVERDPEGGRYR 64
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 421-478 2.28e-04

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: 39.59  E-value: 2.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491099184 421 ERQIQILGLIQQQPkISYRQMTEQLGIHKSAIQKHLESLKDAGWLE-RVGGTRGYWAIK 478
Cdd:cd00090    7 PTRLRILRLLLEGP-LTVSELAERLGLSQSTVSRHLKKLEEAGLVEsRREGRRVYYSLT 64
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
419-467 3.98e-04

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 39.50  E-value: 3.98e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 491099184   419 LTERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWLER 467
Cdd:smart00347   8 LTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRR 56
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
419-468 7.19e-04

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 39.95  E-value: 7.19e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 491099184 419 LTERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWLERV 468
Cdd:COG1846   36 LTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVERE 85
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 419-467 2.33e-03

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: 36.37  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 491099184  419 LTERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWLER 467
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIER 49
HTH_ICLR smart00346
helix_turn_helix isocitrate lyase regulation;
421-475 3.91e-03

helix_turn_helix isocitrate lyase regulation;


Pssm-ID: 214629 [Multi-domain]  Cd Length: 91  Bit Score: 36.41  E-value: 3.91e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 491099184   421 ERQIQILGLIQQQPK-ISYRQMTEQLGIHKSAIQKHLESLKDAGWLERVGGTRGYW 475
Cdd:smart00346   5 ERGLAVLRALAEEPGgLTLAELAERLGLSKSTAHRLLNTLQELGYVEQDGQNGRYR 60
PRK11886 PRK11886
bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;
421-474 4.79e-03

bifunctional biotin--[acetyl-CoA-carboxylase] ligase/biotin operon repressor BirA;


Pssm-ID: 237010 [Multi-domain]  Cd Length: 319  Bit Score: 39.00  E-value: 4.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491099184 421 ERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGW-LERVGGtRGY 474
Cdd:PRK11886   4 TVMLQLLSLLADGDFHSGEQLGEELGISRAAIWKHIQTLEEWGLdIFSVKG-KGY 57
Lrp COG1522
DNA-binding transcriptional regulator, Lrp family [Transcription];
419-469 5.46e-03

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


Pssm-ID: 441131 [Multi-domain]  Cd Length: 138  Bit Score: 37.07  E-value: 5.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491099184 419 LTERQIQILGLIQQQPKISYRQMTEQLGIHKSAIQKHLESLKDAGWLERVG 469
Cdd:COG1522    3 LDEIDRRILRLLQEDGRLSFAELAERVGLSESTVLRRVRRLEEAGVIRGYG 53
 
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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