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Conserved domains on  [gi|291333320|gb|ADD93027|]
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hypothetical protein [uncultured archaeon MedDCM-OCT-S04-C246]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG1389 super family cl34248
DNA topoisomerase VI, subunit B [Replication, recombination and repair];
1-153 5.46e-77

DNA topoisomerase VI, subunit B [Replication, recombination and repair];


The actual alignment was detected with superfamily member COG1389:

Pssm-ID: 440999 [Multi-domain]  Cd Length: 530  Bit Score: 238.57  E-value: 5.46e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   1 MNKAEEISSKQKQIAVSEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNKQRG-DKIEFITQDN 79
Cdd:COG1389    1 AAIAEELAEKQKEISVAEFFEKNKQLLGFDSPARALYTTVKEAVDNSLDACEEAGILPDIKVSIERVDGkDIYRVTVEDN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291333320  80 GPGIPRNAIEDVFGKFLLGSRFHAIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDTRK 153
Cdd:COG1389   81 GPGIPPEQIPKVFGKLLYGSKFHVLRQSRGQQGIGISAAVLYAQMTTGKPVEVISKTGGSEPAYYFELKIDTKK 154
 
Name Accession Description Interval E-value
COG1389 COG1389
DNA topoisomerase VI, subunit B [Replication, recombination and repair];
1-153 5.46e-77

DNA topoisomerase VI, subunit B [Replication, recombination and repair];


Pssm-ID: 440999 [Multi-domain]  Cd Length: 530  Bit Score: 238.57  E-value: 5.46e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   1 MNKAEEISSKQKQIAVSEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNKQRG-DKIEFITQDN 79
Cdd:COG1389    1 AAIAEELAEKQKEISVAEFFEKNKQLLGFDSPARALYTTVKEAVDNSLDACEEAGILPDIKVSIERVDGkDIYRVTVEDN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291333320  80 GPGIPRNAIEDVFGKFLLGSRFHAIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDTRK 153
Cdd:COG1389   81 GPGIPPEQIPKVFGKLLYGSKFHVLRQSRGQQGIGISAAVLYAQMTTGKPVEVISKTGGSEPAYYFELKIDTKK 154
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
 1-153 9.18e-67

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 212.06  E-value: 9.18e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   1 MNKAEEISSKQKQIAVSEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNK--QRGDKIEFITQD 78
Cdd:PRK04184   2 AIAEELAKEKFREISVAEFFEKNKELLGFDNPARALYTTVKELVDNSLDACEEAGILPDIKIEIKRvdEGKDHYRVTVED 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291333320  79 NGPGIPRNAIEDVFGKFLLGSRFHAIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDTRK 153
Cdd:PRK04184  82 NGPGIPPEEIPKVFGKLLYGSKFHNLRQSRGQQGIGISAAVLYAQMTTGKPVRVISSTGGSKKAYYFELKIDTKK 156
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
 17-153 2.83e-59

Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends.


Pssm-ID: 340410 [Multi-domain]  Cd Length: 203  Bit Score: 183.32  E-value: 2.83e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320  17 SEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNKQRGDKIEFITQDNGPGIPRNAIEDVFGKFL 96
Cdd:cd16933    1 AEFFRKNKEMLGFDNPIRSLYTTVRELVENSLDATEEAGILPDIKVEIEEIGKDHYKVIVEDNGPGIPEEQIPKVFGKVL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 291333320  97 LGSRFHaIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDTRK 153
Cdd:cd16933   81 YGSKYH-NKQSRGQQGLGISAAVLYSQMTTGKPVEIISSTKDSNYAYVVKLMIDTDK 136
top6b TIGR01052
DNA topoisomerase VI, B subunit; This model describes DNA topoisomerase VI, an archaeal type ...
 8-153 3.90e-56

DNA topoisomerase VI, B subunit; This model describes DNA topoisomerase VI, an archaeal type II DNA topoisomerase (DNA gyrase). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273417 [Multi-domain]  Cd Length: 488  Bit Score: 183.48  E-value: 3.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320    8 SSKQKQIAVSEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNKQRGDKIEFITQDNGPGIPRNA 87
Cdd:TIGR01052   1 KEKFREMSVAEFFRKNKHMLGYSGKIRSLTTVIHELVTNSLDACEEAGILPDIKVEIEKIGKDHYKVTVEDNGPGIPEEY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291333320   88 IEDVFGKFLLGSRFHAIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDTRK 153
Cdd:TIGR01052  81 IPKVFGKMLAGSKFHRIIQSRGQQGIGISGAVLYSQMTTGKPVKVISSTGGEIYVYKMKLKIDVQK 146
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 36-135 2.74e-10

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 54.96  E-value: 2.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320    36 IITAVKESVDNSLDACEEArilPNIHVELnKQRGDKIEFITQDNGPGIPRNAIEDVFGKFllgSRFHAIRQTRGQQGIGI 115
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPEG---GRITVTL-ERDGDHVEITVEDNGPGIPPEDLEKIFEPF---FRTDKRSRKIGGTGLGL 78

                           90       100
                   ....*....|....*....|
gi 291333320   116 TGVVMYSQLTTGsKTHVISK 135
Cdd:smart00387  79 SIVKKLVELHGG-EISVESE 97
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 39-145 2.55e-08

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 50.02  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   39 AVKESVDNSLDACEEarilpNIHVELNKQRGDKIEFITQDNGPGIPRNAIEDVFGKFLLGSRFHAIRQTRGQQGIGI--T 116
Cdd:pfam13589   4 ALAELIDNSIDADAT-----NIKIEVNKNRGGGTEIVIEDDGHGMSPEELINALRLATSAKEAKRGSTDLGRYGIGLklA 78

                          90       100
                  ....*....|....*....|....*....
gi 291333320  117 GVVMYSQLTtgskthVISKIKDDASAVFV 145
Cdd:pfam13589  79 SLSLGAKLT------VTSKKEGKSSTLTL 101
 
Name Accession Description Interval E-value
COG1389 COG1389
DNA topoisomerase VI, subunit B [Replication, recombination and repair];
1-153 5.46e-77

DNA topoisomerase VI, subunit B [Replication, recombination and repair];


Pssm-ID: 440999 [Multi-domain]  Cd Length: 530  Bit Score: 238.57  E-value: 5.46e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   1 MNKAEEISSKQKQIAVSEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNKQRG-DKIEFITQDN 79
Cdd:COG1389    1 AAIAEELAEKQKEISVAEFFEKNKQLLGFDSPARALYTTVKEAVDNSLDACEEAGILPDIKVSIERVDGkDIYRVTVEDN 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 291333320  80 GPGIPRNAIEDVFGKFLLGSRFHAIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDTRK 153
Cdd:COG1389   81 GPGIPPEQIPKVFGKLLYGSKFHVLRQSRGQQGIGISAAVLYAQMTTGKPVEVISKTGGSEPAYYFELKIDTKK 154
PRK04184 PRK04184
DNA topoisomerase VI subunit B; Validated
 1-153 9.18e-67

DNA topoisomerase VI subunit B; Validated


Pssm-ID: 235246 [Multi-domain]  Cd Length: 535  Bit Score: 212.06  E-value: 9.18e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   1 MNKAEEISSKQKQIAVSEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNK--QRGDKIEFITQD 78
Cdd:PRK04184   2 AIAEELAKEKFREISVAEFFEKNKELLGFDNPARALYTTVKELVDNSLDACEEAGILPDIKIEIKRvdEGKDHYRVTVED 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 291333320  79 NGPGIPRNAIEDVFGKFLLGSRFHAIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDTRK 153
Cdd:PRK04184  82 NGPGIPPEEIPKVFGKLLYGSKFHNLRQSRGQQGIGISAAVLYAQMTTGKPVRVISSTGGSKKAYYFELKIDTKK 156
PRK14868 PRK14868
DNA topoisomerase VI subunit B; Provisional
 4-151 2.32e-60

DNA topoisomerase VI subunit B; Provisional


Pssm-ID: 237842 [Multi-domain]  Cd Length: 795  Bit Score: 200.03  E-value: 2.32e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   4 AEEISSKQKQIAVSEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELnKQRGDKIEFITQDNGPGI 83
Cdd:PRK14868  15 AEELAESQREISIAEFFEKNKHMLGFDSGARGLVTAVKEAVDNALDATEEAGILPDIYVEI-EEVGDYYRLVVEDNGPGI 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 291333320  84 PRNAIEDVFGKFLLGSRFHAIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDT 151
Cdd:PRK14868  94 TKEQIPKVFGKLLYGSRFHAREQSRGQQGIGISAAVLYSQLTSGKPAKITSRTQGSEEAQYFELIIDT 161
HATPase_TopVIB-like cd16933
Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family ...
 17-153 2.83e-59

Histidine kinase-like ATPase domain of type IIB topoisomerase, Topo VI, subunit B; This family includes the histidine kinase-like ATPase (HATPase) domain of the B subunit of topoisomerase VI (Topo VIB). Topo VI is a heterotetrameric complex composed of two TopVIA and two TopVIB subunits and is categorized as a type II B DNA topoisomerase. It is found in archaea and also in plants. Type II enzymes cleave both strands of a DNA duplex and pass a second duplex through the resulting break in an ATP-dependent mechanism. DNA cleavage by Topo VI generates two-nucleotide 5'-protruding ends.


Pssm-ID: 340410 [Multi-domain]  Cd Length: 203  Bit Score: 183.32  E-value: 2.83e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320  17 SEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNKQRGDKIEFITQDNGPGIPRNAIEDVFGKFL 96
Cdd:cd16933    1 AEFFRKNKEMLGFDNPIRSLYTTVRELVENSLDATEEAGILPDIKVEIEEIGKDHYKVIVEDNGPGIPEEQIPKVFGKVL 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 291333320  97 LGSRFHaIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDTRK 153
Cdd:cd16933   81 YGSKYH-NKQSRGQQGLGISAAVLYSQMTTGKPVEIISSTKDSNYAYVVKLMIDTDK 136
top6b TIGR01052
DNA topoisomerase VI, B subunit; This model describes DNA topoisomerase VI, an archaeal type ...
 8-153 3.90e-56

DNA topoisomerase VI, B subunit; This model describes DNA topoisomerase VI, an archaeal type II DNA topoisomerase (DNA gyrase). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273417 [Multi-domain]  Cd Length: 488  Bit Score: 183.48  E-value: 3.90e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320    8 SSKQKQIAVSEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNKQRGDKIEFITQDNGPGIPRNA 87
Cdd:TIGR01052   1 KEKFREMSVAEFFRKNKHMLGYSGKIRSLTTVIHELVTNSLDACEEAGILPDIKVEIEKIGKDHYKVTVEDNGPGIPEEY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 291333320   88 IEDVFGKFLLGSRFHAIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKDDASAVFVELGLDTRK 153
Cdd:TIGR01052  81 IPKVFGKMLAGSKFHRIIQSRGQQGIGISGAVLYSQMTTGKPVKVISSTGGEIYVYKMKLKIDVQK 146
PRK14867 PRK14867
DNA topoisomerase VI subunit B; Provisional
 5-138 5.00e-40

DNA topoisomerase VI subunit B; Provisional


Pssm-ID: 237841 [Multi-domain]  Cd Length: 659  Bit Score: 143.03  E-value: 5.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   5 EEISSKQKQIAVSEFFEKNKHFLGFDSLQRSIITAVKESVDNSLDACEEARILPNIHVELNKQRGDKIEFITQDNGPGIP 84
Cdd:PRK14867   6 ESLFDEFKEHSISEFFRKNKHMLGYSGKLRSMTTIIHELVTNSLDACEEAEILPDIKVEIEKLGSDHYKVAVEDNGPGIP 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 291333320  85 RNAIEDVFGKFLLGSRFHAIRQTRGQQGIGITGVVMYSQLTTGSKTHVISKIKD 138
Cdd:PRK14867  86 PEFVPKVFGKMLAGSKMHRLIQSRGQQGIGAAGVLLFSQITTGKPLKITTSTGD 139
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
 36-135 2.74e-10

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 54.96  E-value: 2.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320    36 IITAVKESVDNSLDACEEArilPNIHVELnKQRGDKIEFITQDNGPGIPRNAIEDVFGKFllgSRFHAIRQTRGQQGIGI 115
Cdd:smart00387   6 LRQVLSNLLDNAIKYTPEG---GRITVTL-ERDGDHVEITVEDNGPGIPPEDLEKIFEPF---FRTDKRSRKIGGTGLGL 78

                           90       100
                   ....*....|....*....|
gi 291333320   116 TGVVMYSQLTTGsKTHVISK 135
Cdd:smart00387  79 SIVKKLVELHGG-EISVESE 97
HATPase_c_3 pfam13589
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, ...
 39-145 2.55e-08

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 433332 [Multi-domain]  Cd Length: 135  Bit Score: 50.02  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   39 AVKESVDNSLDACEEarilpNIHVELNKQRGDKIEFITQDNGPGIPRNAIEDVFGKFLLGSRFHAIRQTRGQQGIGI--T 116
Cdd:pfam13589   4 ALAELIDNSIDADAT-----NIKIEVNKNRGGGTEIVIEDDGHGMSPEELINALRLATSAKEAKRGSTDLGRYGIGLklA 78

                          90       100
                  ....*....|....*....|....*....
gi 291333320  117 GVVMYSQLTtgskthVISKIKDDASAVFV 145
Cdd:pfam13589  79 SLSLGAKLT------VTSKKEGKSSTLTL 101
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
 33-128 1.67e-07

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 47.36  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320   33 QRSIITAVKESVDNSLDACEEArilPNIHVELnkQRGDKIEFITQDNGPGIPRNAIEDVFGKFllgsrFHAIRQTRGQQG 112
Cdd:pfam02518   3 ELRLRQVLSNLLDNALKHAAKA---GEITVTL--SEGGELTLTVEDNGIGIPPEDLPRIFEPF-----STADKRGGGGTG 72

                          90
                  ....*....|....*.
gi 291333320  113 IGITGVVMYSQLTTGS 128
Cdd:pfam02518  73 LGLSIVRKLVELLGGT 88
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
 36-115 1.30e-05

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 42.20  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320  36 IITAVKESVDNSLDACEEARilpNIHVELnKQRGDKIEFITQDNGPGIPRNAIEDVFGkfllgsRFHAIRQTRGQQGIGI 115
Cdd:cd00075    1 LEQVLSNLLDNALKYSPPGG---TIEISL-RQEGDGVVLEVEDNGPGIPEEDLERIFE------RFYRGDKSREGGGTGL 70
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
 60-130 7.87e-05

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 40.17  E-value: 7.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 291333320  60 IHVELNKQRGDKIEFITQDNGPGIPRNAIEDVFGKFLLGSRFHAirQTRGQQGIGITGVVMYSQLTTGSKT 130
Cdd:cd16925   26 IRCILEKFRLNRFLLTVSDSGPGIPPNLREEIFERFRQGDGSST--RAHGGTGLGLSIVKEFVELHGGTVT 94
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
 44-94 1.58e-04

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 40.99  E-value: 1.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 291333320  44 VDNSLDACEEARIL-PNIHVELnKQRGDKIEFITQDNGPGIPRNAIEDVFGK 94
Cdd:COG3290  290 LDNAIEAVEKLPEEeRRVELSI-RDDGDELVIEVEDSGPGIPEELLEKIFER 340
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
60-115 1.94e-04

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 40.28  E-value: 1.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 291333320  60 IHVELnKQRGDKIEFITQDNGPGIPRNAIEDVFgkfllgSRFHAIRQTRGQQGIGI 115
Cdd:COG2205  154 ITISA-RREGDGVRISVSDNGPGIPEEELERIF------ERFYRGDNSRGEGGTGL 202
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 44-92 3.47e-04

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 39.95  E-value: 3.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 291333320  44 VDNSLDACEEArilPNIHVELnKQRGDKIEFITQDNGPGIPRNAIEDVF 92
Cdd:COG5000  326 LKNAIEAIEEG---GEIEVST-RREDGRVRIEVSDNGPGIPEEVLERIF 370
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 39-127 5.55e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 37.83  E-value: 5.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291333320  39 AVKESVDNSLDACEEARILpNIHVELNkqrGDKIEFITQDNGPGIPRNAIEDVFGKFLLGSRFHAIRQTrgqQGIGITGV 118
Cdd:cd16945    8 AINNLLDNAIDFSPEGGLI-ALQLEAD---TEGIELLVFDEGSGIPDYALNRVFERFYSLPRPHSGQKS---TGLGLAFV 80


                 ....*....
gi 291333320 119 VMYSQLTTG 127
Cdd:cd16945   81 QEVAQLHGG 89
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 37-92 6.43e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 37.27  E-value: 6.43e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 291333320  37 ITAVKESVDNSLDACEEARILPN-IHVELNkQRGDKIEFITQDNGPGIPRNAIEDVF 92
Cdd:cd16915    2 ITIVGNLIDNALDALAATGAPNKqVEVFLR-DEGDDLVIEVRDTGPGIAPELRDKVF 57
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
44-115 6.84e-04

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 39.12  E-value: 6.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 291333320  44 VDNSLDACEEARilpNIHVELnKQRGDKIEFITQDNGPGIPRNAIEDVFgkfllgSRFHAIRQTRGQQGIGI 115
Cdd:COG0642  232 LSNAIKYTPEGG---TVTVSV-RREGDRVRISVEDTGPGIPPEDLERIF------EPFFRTDPSRRGGGTGL 293
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
 44-95 7.17e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 37.44  E-value: 7.17e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 291333320  44 VDNSLDACEEaRILPNIHVELNKQrGDKIEFITQDNGPGIPRNAIEDVFGKF 95
Cdd:cd16976    9 LQNALDAMGK-VENPRIRIAARRL-GGRLVLVVRDNGPGIAEEHLSRVFDPF 58
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
 44-92 9.13e-04

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 38.63  E-value: 9.13e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 291333320  44 VDNSLDACEEARiLPNIHVELnKQRGDKIEFITQDNGPGIPRNAIEDVF 92
Cdd:COG4191  265 LINAIDAMEEGE-GGRITIST-RREGDYVVISVRDNGPGIPPEVLERIF 311
HATPase_MutL-MLH-PMS-like cd16926
Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, ...
 39-92 6.35e-03

Histidine kinase-like ATPase domain of DNA mismatch repair proteins Escherichia coli MutL, human MutL homologs (MLH/ PMS), and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of Escherichia coli MutL, human MLH1 (mutL homolog 1), human PMS1 (PMS1 homolog 1, mismatch repair system component), human MLH3 (mutL homolog 3), and human PMS2 (PMS1 homolog 2, mismatch repair system component). MutL homologs (MLH/PMS) participate in MMR (DNA mismatch repair), and in addition have role(s) in DNA damage signaling and suppression of homologous recombination (recombination between partially homologous parental DNAs). The primary role of MutL in MMR is to mediate protein-protein interactions during mismatch recognition and strand removal; a ternary complex is formed between MutS, MutL, and the mismatched DNA, which activates the MutH endonuclease.


Pssm-ID: 340403 [Multi-domain]  Cd Length: 188  Bit Score: 35.88  E-value: 6.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 291333320  39 AVKESVDNSLDAceEARilpNIHVELNKQRGDKIEFItqDNGPGIPRNAIEDVF 92
Cdd:cd16926   17 VVKELVENSIDA--GAT---RIDVEIEEGGLKLIRVT--DNGSGISREDLELAF 63
 
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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