NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2590639980|ref|WP_315696365|]
View 

MULTISPECIES: EAL domain-containing protein [Pseudomonas]

Protein Classification

putative bifunctional diguanylate cyclase/phosphodiesterase( domain architecture ID 11472025)

putative bifunctional diguanylate cyclase/phosphodiesterase may only contain one of the two functional domains (GGDEF diguanylate cyclase or EAL family cyclyc-guanylate-specific phosphodiesterase)

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
28-697 0e+00

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 538.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  28 MRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTANEQSDEAVLKGYA 107
Cdd:COG5001     2 LALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 108 SGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQRLTRELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQA 187
Cdd:COG5001    82 LAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 188 PVEQLQGVSVLDLVQLPNVSLWVDSEFYQAYLARRIFRVHDAQLRTQTGQLVPVALSCAP-LPAEQQAMVVTVLDMSVVR 266
Cdd:COG5001   162 LALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLlLLLLLVAVLAIARLITERK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 267 NLHQQLEYQAVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLG 346
Cdd:COG5001   242 RAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 347 NEALLARMGGDEFTALFDGLPYPEQAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAA 426
Cdd:COG5001   322 EGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRA 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 427 KRAGRQQYRFYDQELNGRARSRLMLEDGVRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLE 506
Cdd:COG5001   402 KAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAE 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 507 EARLINRLASWIYRQGVSQRRAWREHFAPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDE 586
Cdd:COG5001   482 ETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEE 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 587 AVKQVNRLRELGVRVALDDFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETP 666
Cdd:COG5001   562 ALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETE 641
                         650       660       670
                  ....*....|....*....|....*....|.
gi 2590639980 667 AQAAWLKANGCAYVQGFIVAHPMTAADAGRF 697
Cdd:COG5001   642 EQLEFLRELGCDYAQGYLFSRPLPAEELEAL 672
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
28-697 0e+00

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 538.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  28 MRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTANEQSDEAVLKGYA 107
Cdd:COG5001     2 LALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 108 SGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQRLTRELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQA 187
Cdd:COG5001    82 LAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 188 PVEQLQGVSVLDLVQLPNVSLWVDSEFYQAYLARRIFRVHDAQLRTQTGQLVPVALSCAP-LPAEQQAMVVTVLDMSVVR 266
Cdd:COG5001   162 LALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLlLLLLLVAVLAIARLITERK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 267 NLHQQLEYQAVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLG 346
Cdd:COG5001   242 RAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 347 NEALLARMGGDEFTALFDGLPYPEQAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAA 426
Cdd:COG5001   322 EGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRA 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 427 KRAGRQQYRFYDQELNGRARSRLMLEDGVRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLE 506
Cdd:COG5001   402 KAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAE 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 507 EARLINRLASWIYRQGVSQRRAWREHFAPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDE 586
Cdd:COG5001   482 ETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEE 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 587 AVKQVNRLRELGVRVALDDFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETP 666
Cdd:COG5001   562 ALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETE 641
                         650       660       670
                  ....*....|....*....|....*....|.
gi 2590639980 667 AQAAWLKANGCAYVQGFIVAHPMTAADAGRF 697
Cdd:COG5001   642 EQLEFLRELGCDYAQGYLFSRPLPAEELEAL 672
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
261-696 2.93e-102

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 327.41  E-value: 2.93e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 261 DMSVVRNLHQQLEYQAVTDPLTGLLNRRGFYQAADAVLmrnEHSDKCQ-ALMYMDLDGFKRINDSLGHDAGDRVLRWVGE 339
Cdd:PRK10060  222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAI---NAADNNQvGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSL 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 340 QLKDCLGNEALLARMGGDEFTALFdglPYPEQAG--RFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLR 417
Cdd:PRK10060  299 AILSCLEEDQTLARLGGDEFLVLA---SHTSQAAleAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIR 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 418 AADVAMYAAKRAGRQQYRFYDQELNGRARSRLMLEDGVRAAIEERAFTLVYQPQVSfADGHLRGFEALLRWQHPSVGDVP 497
Cdd:PRK10060  376 SADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKIT-WRGEVRSLEALVRWQSPERGLIP 454
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 498 PGLFIPLLEEARLINRLASWIYRQGVSQRRAWREHfAPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAE 577
Cdd:PRK10060  455 PLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDK-GINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTE 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 578 TSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAIT 657
Cdd:PRK10060  534 SCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQ 613
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2590639980 658 VIAEGVETPAQAAWLKANGCAYVQGFIVAHPMTAADAGR 696
Cdd:PRK10060  614 VIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFER 652
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
455-693 2.27e-91

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 284.44  E-value: 2.27e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 455 VRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQRRAWREHFa 534
Cdd:cd01948     3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 535 PDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLR 614
Cdd:cd01948    82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2590639980 615 MLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAHPMTAAD 693
Cdd:cd01948   162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
455-693 6.10e-79

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 252.14  E-value: 6.10e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  455 VRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQRRAWREHFA 534
Cdd:smart00052   4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  535 PDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLR 614
Cdd:smart00052  84 PPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLS 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2590639980  615 MLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAHPMTAAD 693
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
455-688 3.14e-70

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 228.74  E-value: 3.14e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 455 VRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQRRAWRehFA 534
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ--LG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 535 PDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLR 614
Cdd:pfam00563  82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2590639980 615 MLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAHP 688
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
275-438 8.36e-37

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 135.54  E-value: 8.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 275 QAVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARM 354
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 355 GGDEFTALFDGLPYpEQAGRFAERLLERMSS--CQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAAKRAGRQ 432
Cdd:TIGR00254  81 GGEEFVVILPGTPL-EDALSKAERLRDAINSkpIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159

                  ....*.
gi 2590639980 433 QYRFYD 438
Cdd:TIGR00254 160 RVVVAD 165
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
28-697 0e+00

Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 538.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  28 MRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTANEQSDEAVLKGYA 107
Cdd:COG5001     2 LALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 108 SGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQRLTRELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQA 187
Cdd:COG5001    82 LAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARAL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 188 PVEQLQGVSVLDLVQLPNVSLWVDSEFYQAYLARRIFRVHDAQLRTQTGQLVPVALSCAP-LPAEQQAMVVTVLDMSVVR 266
Cdd:COG5001   162 LALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLlLLLLLVAVLAIARLITERK 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 267 NLHQQLEYQAVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLG 346
Cdd:COG5001   242 RAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLR 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 347 NEALLARMGGDEFTALFDGLPYPEQAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAA 426
Cdd:COG5001   322 EGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRA 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 427 KRAGRQQYRFYDQELNGRARSRLMLEDGVRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLE 506
Cdd:COG5001   402 KAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAE 481
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 507 EARLINRLASWIYRQGVSQRRAWREHFAPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDE 586
Cdd:COG5001   482 ETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEE 561
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 587 AVKQVNRLRELGVRVALDDFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETP 666
Cdd:COG5001   562 ALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETE 641
                         650       660       670
                  ....*....|....*....|....*....|.
gi 2590639980 667 AQAAWLKANGCAYVQGFIVAHPMTAADAGRF 697
Cdd:COG5001   642 EQLEFLRELGCDYAQGYLFSRPLPAEELEAL 672
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
261-696 2.93e-102

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 327.41  E-value: 2.93e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 261 DMSVVRNLHQQLEYQAVTDPLTGLLNRRGFYQAADAVLmrnEHSDKCQ-ALMYMDLDGFKRINDSLGHDAGDRVLRWVGE 339
Cdd:PRK10060  222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAI---NAADNNQvGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSL 298
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 340 QLKDCLGNEALLARMGGDEFTALFdglPYPEQAG--RFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLR 417
Cdd:PRK10060  299 AILSCLEEDQTLARLGGDEFLVLA---SHTSQAAleAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIR 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 418 AADVAMYAAKRAGRQQYRFYDQELNGRARSRLMLEDGVRAAIEERAFTLVYQPQVSfADGHLRGFEALLRWQHPSVGDVP 497
Cdd:PRK10060  376 SADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKIT-WRGEVRSLEALVRWQSPERGLIP 454
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 498 PGLFIPLLEEARLINRLASWIYRQGVSQRRAWREHfAPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAE 577
Cdd:PRK10060  455 PLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDK-GINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTE 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 578 TSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAIT 657
Cdd:PRK10060  534 SCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQ 613
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2590639980 658 VIAEGVETPAQAAWLKANGCAYVQGFIVAHPMTAADAGR 696
Cdd:PRK10060  614 VIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFER 652
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
129-697 6.39e-102

EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];


Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 323.66  E-value: 6.39e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 129 ALLDQQSNRRMLQRLTRELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQLPNVSL 208
Cdd:COG2200     7 LLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 209 WVDS-EFYQAYLARRIFRVHDAQLRTQTGQLVPVALSCAPLPAEQQAMVVTVLDMSVVRNLHQQLEYQAVTDPLTGLLNR 287
Cdd:COG2200    87 LLLLlLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRR 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 288 RGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARMGGDEFTALFDGLP 367
Cdd:COG2200   167 LLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLA 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 368 YPEQAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAAKRAGRQQYRFYDQElNGRARS 447
Cdd:COG2200   247 AAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAA-EARARR 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 448 RLMLEDGVRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQRR 527
Cdd:COG2200   326 RLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLA 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 528 AWREHfAPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDEAVKQVNRLRELGVRVALDDFG 607
Cdd:COG2200   406 RWPER-GLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFG 484
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 608 AGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAH 687
Cdd:COG2200   485 TGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGR 564
                         570
                  ....*....|
gi 2590639980 688 PMTAADAGRF 697
Cdd:COG2200   565 PLPLEELEAL 574
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
455-693 2.27e-91

EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 284.44  E-value: 2.27e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 455 VRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQRRAWREHFa 534
Cdd:cd01948     3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 535 PDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLR 614
Cdd:cd01948    82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2590639980 615 MLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAHPMTAAD 693
Cdd:cd01948   162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
270-693 1.30e-80

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 273.18  E-value: 1.30e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 270 QQLEYQAVTDPLTGLLNRRGFYQAADAvLMRNEHSdkcQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEA 349
Cdd:PRK11359  370 QHIEQLIQFDPLTGLPNRNNLHNYLDD-LVDKAVS---PVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQ 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 350 LLARMGGDEFTalfdgLPYPE----QAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATypDCGASVEGLLRAADVAMYA 425
Cdd:PRK11359  446 YLCRIEGTQFV-----LVSLEndvsNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDY 518
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 426 AKRAGRQQYRFYDQELNGRARSRLMLEDGVRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLL 505
Cdd:PRK11359  519 IRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLA 598
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 506 EEARLINRLASWIYRQGVSQRRAWREHFAPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNID 585
Cdd:PRK11359  599 EEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDT 678
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 586 EAVKQVNRLRELGVRVALDDFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVET 665
Cdd:PRK11359  679 EIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVET 758
                         410       420
                  ....*....|....*....|....*...
gi 2590639980 666 PAQAAWLKANGCAYVQGFIVAHPMTAAD 693
Cdd:PRK11359  759 KEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
455-693 6.10e-79

Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 252.14  E-value: 6.10e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  455 VRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQRRAWREHFA 534
Cdd:smart00052   4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  535 PDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLR 614
Cdd:smart00052  84 PPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLS 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2590639980  615 MLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAHPMTAAD 693
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
269-692 3.77e-71

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 244.24  E-value: 3.77e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 269 HQQLEYQAVTDPLTGLLNRRGFYQAADAVLMRNEHSdkcqALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNE 348
Cdd:PRK13561  224 YEEQSRNATRFPVSDLPNKALLMALLEQVVARKQTT----ALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPR 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 349 ALLARMGGDEFTALFDGLPYPEQAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATYpDCGASVEGLLRAADVAMYAAKR 428
Cdd:PRK13561  300 MVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFTARR 378
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 429 AGRQQYRFYDQELNGRARSRLMLEDGVRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEA 508
Cdd:PRK13561  379 KGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESC 458
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 509 RLINRLASWIYRQGVSQRRAWREHfAPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDEAV 588
Cdd:PRK13561  459 GLMVTVGHWVLEESCRLLAAWQER-GIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAV 537
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 589 KQVNRLRELGVRVALDDFGAGDCSLRML---RDLPIDTLKIDRHLVARLPDsavDAALVRSVIALCADYAITVIAEGVET 665
Cdd:PRK13561  538 AILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLPE---DDSMVAAIIMLAQSLNLQVIAEGVET 614
                         410       420
                  ....*....|....*....|....*..
gi 2590639980 666 PAQAAWLKANGCAYVQGFIVAHPMTAA 692
Cdd:PRK13561  615 EAQRDWLLKAGVGIAQGFLFARALPIE 641
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
455-688 3.14e-70

EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 228.74  E-value: 3.14e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 455 VRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQRRAWRehFA 534
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ--LG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 535 PDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLR 614
Cdd:pfam00563  82 PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2590639980 615 MLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAHP 688
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
158-689 2.69e-65

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 234.18  E-value: 2.69e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  158 LENAAEGILVVDATGIISFANPAIS----WLLQA----PVEQlqgvsVLDLV------QLPNVslwvdsefYQAYLARRI 223
Cdd:PRK09776   542 LDSIGEAVVCTDMAMKVTFMNPVAEkmtgWTQEEalgvPLLT-----VLHITfgdngpLMENI--------YSCLTSRSA 608
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  224 FRVH-DAQLRTQTGQLVPVALSCAPLPAEQQAMVVTVL---DMSVVRNLHQQLEYQAVTDPLTGLLNRRGFYQ-----AA 294
Cdd:PRK09776   609 AYLEqDVVLHCRSGGSYDVHYSITPLSTLDGENIGSVLviqDVTESRKMLRQLSYSASHDALTHLANRASFEKqlrrlLQ 688
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  295 DAVLMRNEHsdkcqALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARMGGDEFtalfdGLPYP----E 370
Cdd:PRK09776   689 TVNSTHQRH-----ALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEF-----GLLLPdcnvE 758
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  371 QAGRFAERLLERMSSCQHI-DDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAAKRAGRQQYRFY--DQELNGRARS 447
Cdd:PRK09776   759 SARFIATRIISAINDYHFPwEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYepQQAAAHSEHR 838
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  448 RLMLEDGVRAAIEERAFTLVYQ---PQVSFADGHlrgFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQgVS 524
Cdd:PRK09776   839 ALSLAEQWRMIKENQLMMLAHGvasPRIPEARNH---WLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHE-FF 914
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  525 QRRAWREHfAPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMYNIDEAVKQVNRLRELGVRVALD 604
Cdd:PRK09776   915 RQAAKAVA-SKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLS 993
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  605 DFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFI 684
Cdd:PRK09776   994 DFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYA 1073

                   ....*
gi 2590639980  685 VAHPM 689
Cdd:PRK09776  1074 IARPQ 1078
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
247-693 3.28e-62

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 219.81  E-value: 3.28e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 247 PLPAEQQAMVVTVLDMSVVRNlhQQLEYQAVTD--------PLTGLLNRRGFYQAADAVLMRNEHSDKcQALMYMDLDGF 318
Cdd:PRK11829  197 TLPAHHQDDELGVLVRNYNRN--QQLLADAYADmgrishrfPVTELPNRSLFISLLEKEIASSTRTDH-FHLLVIGIETL 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 319 KRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARMGGDEFTALFDGLPYPEQAGRFAERLLERMSSCQHIDDLDLNLGV 398
Cdd:PRK11829  274 QEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSA 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 399 SIGIATYPDCGASVEGLLRAADVAMYAAKRAGRQQYRFYDQELNGRARSRLMLEDGVRAAIEERAFTLVYQPQVSFADGH 478
Cdd:PRK11829  354 SIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQ 433
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 479 LRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQRRAWREHfAPDVVLGISLSRAQFSMPSLVDELQ 558
Cdd:PRK11829  434 VIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKAR-GVSLPLSVNISGLQVQNKQFLPHLK 512
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 559 RVINEQGLSPSQLEVEVAETSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLRMLR---DLPIDTLKIDRHLVARLP 635
Cdd:PRK11829  513 TLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLP 592
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980 636 dsaVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAHPMTAAD 693
Cdd:PRK11829  593 ---EDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAE 647
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
278-435 1.77e-59

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 197.39  E-value: 1.77e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 278 TDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARMGGD 357
Cdd:cd01949     2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980 358 EFTALFDGLPyPEQAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAAKRAGRQQYR 435
Cdd:cd01949    82 EFAILLPGTD-LEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
160-437 2.15e-58

GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants [Signal transduction mechanisms];


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 198.66  E-value: 2.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 160 NAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQLPNVSLWVDSEFYQAYLARRIFRVHDAQLRTQTGQLV 239
Cdd:COG2199     2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 240 PVALSCAPLpaeqQAMVVTVLDMSVVRNLHQQLEYQAVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFK 319
Cdd:COG2199    82 ELLLLLLAL----LLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 320 RINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARMGGDEFTALFDGLPyPEQAGRFAERLLERMSSCQ-HIDDLDLNLGV 398
Cdd:COG2199   158 RINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTD-LEEAEALAERLREALEQLPfELEGKELRVTV 236
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2590639980 399 SIGIATYPDCGASVEGLLRAADVAMYAAKRAGRQQYRFY 437
Cdd:COG2199   237 SIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
pleD PRK09581
response regulator PleD; Reviewed
16-431 5.48e-56

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 197.82  E-value: 5.48e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTAN 95
Cdd:PRK09581    6 LVVDDIPANVKLLEAKLLAEYYTVLTASSGAEAIAICEREQPDIILLDVMMPGMDGFEVCRRLKSDPATTHIPVVMVTAL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  96 EQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALLdqqsnrRMlQRLTREL--EAARAFNASILENAAEG--------- 164
Cdd:PRK09581   86 DDPEDRV-RGLEAGADDFLTKPINDVALFARVKSLT------RL-KMVIDELrlRASTNAEIGVTALMIMAyankdedgr 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 165 ILVVDATgIISFANpaISWLLQA---PVEQLQGVSVLDLVQLPNVSLW-VDSEFyQAYLARRIFrvhdAQLRTQ--TGQL 238
Cdd:PRK09581  158 ILLVDDD-VSQAER--IANILKEefrVVVVSDPSEALFNAAETNYDLViVSANF-ENYDPLRLC----SQLRSKerTRYV 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 239 VPVALScaplPAEQQAMVVTVLDMSV--------------------VR----------NLHQQLEyQAVTDPLTGLLNRR 288
Cdd:PRK09581  230 PILLLV----DEDDDPRLVKALELGVndylmrpidknellarvrtqIRrkryqdalrnNLEQSIE-MAVTDGLTGLHNRR 304
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 289 GFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARMGGDEFTALFDGLPy 368
Cdd:PRK09581  305 YFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTD- 383
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2590639980 369 PEQAGRFAERLLERMSSCQ---HIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAAKRAGR 431
Cdd:PRK09581  384 IEDAIAVAERIRRKIAEEPfiiSDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGR 449
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
446-693 4.67e-55

Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];


Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 197.06  E-value: 4.67e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 446 RSRLMLEDGVRAAIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQ 525
Cdd:COG4943   267 RRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRD 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 526 RRAW-REHfaPDVVLGISLSRAQFSMPSLVDELQRVINEQGLSPSQLEVEVAETSLMyNIDEAVKQVNRLRELGVRVALD 604
Cdd:COG4943   347 LGDLlAAD--PDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAID 423
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 605 DFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFI 684
Cdd:COG4943   424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503

                  ....*....
gi 2590639980 685 VAHPMTAAD 693
Cdd:COG4943   504 FAKPLPAEE 512
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
274-437 5.68e-50

diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 172.05  E-value: 5.68e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  274 YQAVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLAR 353
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  354 MGGDEFTALFDGLPyPEQAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAAKRAGRQQ 433
Cdd:smart00267  81 LGGDEFALLLPETS-LEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159

                   ....
gi 2590639980  434 YRFY 437
Cdd:smart00267 160 VAVY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
276-431 1.32e-47

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 165.12  E-value: 1.32e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 276 AVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARMG 355
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980 356 GDEFTALFDGLPYPE--QAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAAKRAGR 431
Cdd:pfam00990  81 GDEFAILLPETSLEGaqELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGR 158
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
16-150 1.60e-42

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 153.78  E-value: 1.60e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTAn 95
Cdd:COG3437    10 LIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDLILLDVRMPGMDGFELLRLLRADPSTRDIPVIFLTA- 88
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2590639980  96 EQSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQRLTRELEAA 150
Cdd:COG3437    89 LADPEDRERALEAGADDYLTKPFDPEELLARVRNALELRRLQRELDDLVLYLKLA 143
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
16-157 3.27e-37

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 136.96  E-value: 3.27e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTAN 95
Cdd:COG3706     5 LVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDLILLDLEMPDMDGLELCRRLRADPRTADIPIIFLTAL 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2590639980  96 EqSDEAVLKGYASGAVDYMFKPFDPQILKPKVQAL--------------LDQQSNRRMLQRLTRELEAARAFNASI 157
Cdd:COG3706    85 D-DEEDRARALEAGADDYLTKPFDPEELLARVDLVaryggeefaillpgTDLEGALAVAERIREAVAELPSLRVTV 159
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
275-438 8.36e-37

diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 135.54  E-value: 8.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 275 QAVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARM 354
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 355 GGDEFTALFDGLPYpEQAGRFAERLLERMSS--CQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAMYAAKRAGRQ 432
Cdd:TIGR00254  81 GGEEFVVILPGTPL-EDALSKAERLRDAINSkpIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159

                  ....*.
gi 2590639980 433 QYRFYD 438
Cdd:TIGR00254 160 RVVVAD 165
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
458-693 3.69e-36

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 143.21  E-value: 3.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 458 AIEERAFTLVYQPQVSFADGHLRGFEALLRWQHPSVGDVPPGLFIPLLEEARLINRLASWIYRQGVSQRRAWREHFAPDV 537
Cdd:PRK10551  271 GIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVLPVGA 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 538 VLGISLSRAQFSMPSLVDELQRVIneQGLSPSQLEV--EVAETSlMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLRM 615
Cdd:PRK10551  351 KLGINISPAHLHSDSFKADVQRLL--ASLPADHFQIvlEITERD-MVQEEEATKLFAWLHSQGIEIAIDDFGTGHSALIY 427
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980 616 LRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAHPMTAAD 693
Cdd:PRK10551  428 LERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLED 505
CheY COG0784
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ...
9-136 6.29e-35

CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];


Pssm-ID: 440547 [Multi-domain]  Cd Length: 128  Bit Score: 128.81  E-value: 6.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980   9 PDGNSVLLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTP 88
Cdd:COG0784     2 PLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDLILLDINMPGMDGLELLRRIRALPRLPDIP 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2590639980  89 IIFLTANEqSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALLDQQSN 136
Cdd:COG0784    82 IIALTAYA-DEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
OmpR COG0745
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ...
15-138 9.51e-34

DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 440508 [Multi-domain]  Cd Length: 204  Bit Score: 128.15  E-value: 9.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTA 94
Cdd:COG0745     4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDLILLDLMLPGMDGLEVCRRLR--ARPSDIPIIMLTA 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALLDQQSNRR 138
Cdd:COG0745    82 RDDEEDRV-RGLEAGADDYLTKPFDPEELLARIRALLRRRAAEV 124
REC_PA4781-like cd19920
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ...
15-118 4.81e-33

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381147 [Multi-domain]  Cd Length: 103  Bit Score: 122.62  E-value: 4.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTA 94
Cdd:cd19920     1 ILIVDDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDLILLDVMMPGMDGFEVCRRLKADPATRHIPVIFLTA 80
                          90       100
                  ....*....|....*....|....*
gi 2590639980  95 -NEQSDEavLKGYASGAVDYMFKPF 118
Cdd:cd19920    81 lTDTEDK--VKGFELGAVDYITKPF 103
REC_D1_PleD-like cd17538
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ...
15-118 4.86e-33

first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381093 [Multi-domain]  Cd Length: 104  Bit Score: 122.61  E-value: 4.86e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTA 94
Cdd:cd17538     2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDLILLDVMMPGMDGFEVCRRLKEDPETRHIPVIMITA 81
                          90       100
                  ....*....|....*....|....*
gi 2590639980  95 -NEQSDEavLKGYASGAVDYMFKPF 118
Cdd:cd17538    82 lDDREDR--IRGLEAGADDFLSKPI 104
REC_hyHK_CKI1_RcsC-like cd17546
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ...
15-124 6.10e-28

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381099 [Multi-domain]  Cd Length: 113  Bit Score: 108.33  E-value: 6.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRT-RLTPIIFLT 93
Cdd:cd17546     1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDLVLMDLQMPVMDGLEATRRIRELEGGgRRTPIIALT 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2590639980  94 ANEQSDEaVLKGYASGAVDYMFKPFDPQILK 124
Cdd:cd17546    81 ANALEED-REKCLEAGMDDYLSKPVKLDQLK 110
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
15-158 2.64e-27

DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];


Pssm-ID: 441806 [Multi-domain]  Cd Length: 418  Bit Score: 115.06  E-value: 2.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTA 94
Cdd:COG2204     5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDLVLLDLRMPGMDGLELLRELR--ALDPDLPVILLTG 82
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALLDQQSNRR-------------MLQRLTRELEAARAFNASIL 158
Cdd:COG2204    83 YGDVETAV-EAIKAGAFDYLTKPFDLEELLAAVERALERRRLRRenaedsgligrspAMQEVRRLIEKVAPSDATVL 158
REC_OmpR cd17574
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ...
16-117 2.95e-27

phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381116 [Multi-domain]  Cd Length: 99  Bit Score: 105.95  E-value: 2.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLTAN 95
Cdd:cd17574     1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDLIILDVMLPGMDGFEVCRRLREKGSD--IPIIMLTAK 78
                          90       100
                  ....*....|....*....|..
gi 2590639980  96 EQsDEAVLKGYASGAVDYMFKP 117
Cdd:cd17574    79 DE-EEDKVLGLELGADDYITKP 99
REC cd00156
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ...
16-117 4.20e-27

phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381085 [Multi-domain]  Cd Length: 99  Bit Score: 105.39  E-value: 4.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTAN 95
Cdd:cd00156     1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDLVLLDLMMPGMDGLELLRKLR--ELPPDIPVIVLTAK 78
                          90       100
                  ....*....|....*....|..
gi 2590639980  96 EQSDEAVlKGYASGAVDYMFKP 117
Cdd:cd00156    79 ADEEDAV-RALELGADDYLVKP 99
Response_reg pfam00072
Response regulator receiver domain; This domain receives the signal from the sensor partner in ...
16-128 2.46e-26

Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.


Pssm-ID: 395025 [Multi-domain]  Cd Length: 111  Bit Score: 103.77  E-value: 2.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTAN 95
Cdd:pfam00072   2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDLILLDINMPGMDGLELLKRIR--RRDPTTPVIILTAH 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2590639980  96 EQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQ 128
Cdd:pfam00072  80 GDEDDAV-EALEAGADDFLSKPFDPDELLAAIR 111
REC_OmpR_BsPhoP-like cd19937
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ...
16-131 3.21e-25

phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381164 [Multi-domain]  Cd Length: 116  Bit Score: 100.81  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTA- 94
Cdd:cd19937     1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDLIILDLMLPGIDGLEVCRILRSDPKTSSIPIIMLTAk 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVlkGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd19937    81 GEEFDKVL--GLELGADDYITKPFSPRELLARVKAVL 115
LytT COG3279
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ...
16-148 3.66e-25

DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];


Pssm-ID: 442510 [Multi-domain]  Cd Length: 235  Bit Score: 104.51  E-value: 3.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLAR-KDWQVL-TASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLT 93
Cdd:COG3279     5 LIVDDEPLARERLERLLEKyPDLEVVgEASNGEEALELLEEHKPDLVFLDIQMPGLDGFELARQLR--ELDPPPPIIFTT 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2590639980  94 AneqSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQRLTRELE 148
Cdd:COG3279    83 A---YDEYALEAFEVNAVDYLLKPIDEERLAKALEKAKERLEAKAAAEASPEEKD 134
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
265-433 9.08e-25

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 109.33  E-value: 9.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 265 VRN---LHQQLEYQAVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQL 341
Cdd:PRK15426  384 VSNmfvLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLI 463
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 342 KDCLGNEALLARMGGDEFTALFDGLPYpEQAGRFAERLLERMsSCQHID---DLDLNLGVSIGIA-TYPDCGASVEGLLR 417
Cdd:PRK15426  464 SSSLRAQDVAGRVGGEEFCVVLPGASL-AEAAQVAERIRLRI-NEKEILvakSTTIRISASLGVSsAEEDGDYDFEQLQS 541
                         170
                  ....*....|....*.
gi 2590639980 418 AADVAMYAAKRAGRQQ 433
Cdd:PRK15426  542 LADRRLYLAKQAGRNR 557
PRK09894 PRK09894
diguanylate cyclase; Provisional
279-438 1.42e-24

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 104.38  E-value: 1.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 279 DPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMymDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEALLARMGGDE 358
Cdd:PRK09894  132 DVLTGLPGRRVLDESFDHQLRNREPQNLYLALL--DIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 359 FTALfdgLP--YPEQAGRFAERLLERMSScQHI--DDLDLNLGVSIGIaTYPDCGASVEGLLRAADVAMYAAKRAGRQQY 434
Cdd:PRK09894  210 FIIC---LKaaTDEEACRAGERIRQLIAN-HAIthSDGRINITATFGV-SRAFPEETLDVVIGRADRAMYEGKQTGRNRV 284

                  ....
gi 2590639980 435 RFYD 438
Cdd:PRK09894  285 MFID 288
REC_RpfG-like cd17551
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ...
16-120 4.35e-23

phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381103 [Multi-domain]  Cd Length: 118  Bit Score: 94.82  E-value: 4.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLAR-KDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTA 94
Cdd:cd17551     4 LIVDDNPTNLLLLEALLRSaGYLEVVSFTDPREALAWCRENPPDLILLDYMMPGMDGLEFIRRLRALPGLEDVPIVMITA 83
                          90       100
                  ....*....|....*....|....*..
gi 2590639980  95 NEqsDEAV-LKGYASGAVDYMFKPFDP 120
Cdd:cd17551    84 DT--DREVrLRALEAGATDFLTKPFDP 108
YesN COG4753
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ...
15-117 2.22e-22

Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443786 [Multi-domain]  Cd Length: 103  Bit Score: 92.14  E-value: 2.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKD--WQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFL 92
Cdd:COG4753     2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDLVITDINMPGMDGLELLEAIR--ELDPDTKIIIL 79
                          90       100
                  ....*....|....*....|....*
gi 2590639980  93 TANEQsDEAVLKGYASGAVDYMFKP 117
Cdd:COG4753    80 SGYSD-FEYAQEAIKLGADDYLLKP 103
CitB COG4565
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ...
16-142 5.60e-22

DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];


Pssm-ID: 443622 [Multi-domain]  Cd Length: 138  Bit Score: 92.34  E-value: 5.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKD--WQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLT 93
Cdd:COG4565     7 LIVEDDPMVAELLRRYLERLPgfEVVGVASSGEEALALLAEHRPDLILLDIYLPDGDGLELLRELR--ARGPDVDVIVIT 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2590639980  94 AnEQSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQR 142
Cdd:COG4565    85 A-ARDPETVREALRAGVVDYLIKPFTFERLREALERYLEYRRLLREDQE 132
REC_CheY4-like cd17562
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ...
16-131 7.02e-22

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381110 [Multi-domain]  Cd Length: 118  Bit Score: 91.21  E-value: 7.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPenliSMRAL----LARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIF 91
Cdd:cd17562     4 LAVDDSA----SIRQMvsftLRGAGYEVVEAADGRDALSKAQSKKFDLIITDQNMPNMDGIELIKELRKLPAYKFTPILM 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2590639980  92 LTaNEQSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17562    80 LT-TESSDEKKQEGKAAGATGWLVKPFDPEQLLEVVKKVL 118
REC_DivK-like cd17548
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ...
16-127 1.05e-21

phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381100 [Multi-domain]  Cd Length: 115  Bit Score: 90.68  E-value: 1.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTAN 95
Cdd:cd17548     3 LIVEDNPLNMKLARDLLESAGYEVLEAADGEEALEIARKEKPDLILMDIQLPGMDGLEATRLLKEDPATRDIPVIALTAY 82
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2590639980  96 E-QSDEAvlKGYASGAVDYMFKPFDPQILKPKV 127
Cdd:cd17548    83 AmKGDRE--KILEAGCDGYISKPIDTREFLETV 113
REC_typeB_ARR-like cd17584
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ...
16-124 2.51e-21

phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381121 [Multi-domain]  Cd Length: 115  Bit Score: 89.61  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHD--VDLVLLDVQMPEMDGFEVARLMRGSQRtrlTPIIFLT 93
Cdd:cd17584     2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKdeFDLVITDVHMPDMDGFEFLELIRLEMD---LPVIMMS 78
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2590639980  94 ANEqSDEAVLKGYASGAVDYMFKPFDPQILK 124
Cdd:cd17584    79 ADG-STSTVMKGLAHGACDYLLKPVSIEDLK 108
REC_hyHK cd17598
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ...
15-131 2.77e-21

phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381128 [Multi-domain]  Cd Length: 118  Bit Score: 89.69  E-value: 2.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTA 94
Cdd:cd17598     1 ILIVEDSPTQAEQLKHILEEQGYKVQVARNGREALAMLAEHRPTLVISDIVMPEMDGYELCRKIKSDPDLKDIPVILLTT 80
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2590639980  95 neQSD-EAVLKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17598    81 --LSDpRDVIRGLECGADNFITKPYDEKYLLSRIKYIL 116
REC_2_DhkD-like cd17580
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ...
16-123 4.02e-20

second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381118 [Multi-domain]  Cd Length: 112  Bit Score: 85.97  E-value: 4.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTAN 95
Cdd:cd17580     2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDVILSDIGMPGMDGYELARRLRELPWLANTPAIALTGY 81
                          90       100
                  ....*....|....*....|....*...
gi 2590639980  96 EQSdEAVLKGYASGAVDYMFKPFDPQIL 123
Cdd:cd17580    82 GQP-EDRERALEAGFDAHLVKPVDPDEL 108
REC_RR468-like cd17552
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ...
15-132 5.04e-20

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381104 [Multi-domain]  Cd Length: 121  Bit Score: 86.07  E-value: 5.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYP--ENLISMrALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFL 92
Cdd:cd17552     4 ILVIDDEEdiREVVQA-CLEKLAGWEVLTASSGQEGLEKAATEQPDAILLDVMMPDMDGLATLKKLQANPETQSIPVILL 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2590639980  93 TANEQSDEavLKGYAS-GAVDYMFKPFDPQILKPKVQALLD 132
Cdd:cd17552    83 TAKAQPSD--RQRFASlGVAGVIAKPFDPLTLAEQIAKLLG 121
Spo0F COG5803
Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, ...
15-131 8.18e-20

Stage 0 sporulation initiation response regulator Spo0F [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444505 [Multi-domain]  Cd Length: 119  Bit Score: 85.62  E-value: 8.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPenliSMRALL----ARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPII 90
Cdd:COG5803     5 ILIVDDQA----GIRMLLkevlKKEGYEVFQAANGKEALEKVKELKPDLVLLDMKMPGMDGIEILKEIKEIDPD--IPVI 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2590639980  91 FLTANEQSDEAVLKGYaSGAVDYMFKPFDPQILKPKVQALL 131
Cdd:COG5803    79 MMTAYGELDMVEEAKE-LGAKGYFTKPFDIDELREAVNKLL 118
REC_OmpR_PrrA-like cd17627
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ...
15-131 1.03e-19

phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381142 [Multi-domain]  Cd Length: 116  Bit Score: 85.13  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSqrTRLTPIIFLTA 94
Cdd:cd17627     1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPDAVVLDVMMPRLDGLEVCRRLRAA--GNDLPILVLTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17627    79 RDSVSDRV-AGLDAGADDYLVKPFALEELLARVRALL 114
REC_YesN-like cd17536
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ...
15-148 2.05e-19

phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381091 [Multi-domain]  Cd Length: 121  Bit Score: 84.31  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDypENLI--SMRALLarkDWQ------VLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRL 86
Cdd:cd17536     1 VLIVDD--EPLIreGLKKLI---DWEelgfevVGEAENGEEALELIEEHKPDIVITDIRMPGMDGLELIEKIR--ELYPD 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980  87 TPIIFLTA-NEQSdeavlkgYA-----SGAVDYMFKPFDPQILKpkvqalldqqsnrRMLQRLTRELE 148
Cdd:cd17536    74 IKIIILSGyDDFE-------YAqkairLGVVDYLLKPVDEEELE-------------EALEKAKEELD 121
PRK09966 PRK09966
diguanylate cyclase DgcN;
271-431 3.08e-19

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 90.84  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 271 QLEYQAVTDPLTGLLNRRGFYQAADAvLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLGNEAL 350
Cdd:PRK09966  243 QLLRTALHDPLTGLANRAAFRSGINT-LMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 351 LARMGGDEFTALFDGLPYPEQAGRFAERLLERMSScqhidDLDLNLG------VSIGIATYPDcGASVEGLLRAADVAMY 424
Cdd:PRK09966  322 AYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNL-----PFDLHNGhqttmtLSIGYAMTIE-HASAEKLQELADHNMY 395

                  ....*....
gi 2590639980 425 AAK--RAGR 431
Cdd:PRK09966  396 QAKhqRAEK 404
REC_OmpR_PhoB cd17618
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ...
16-131 3.60e-19

phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381133 [Multi-domain]  Cd Length: 118  Bit Score: 83.45  E-value: 3.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPEnLISMRAL-LARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTA 94
Cdd:cd17618     4 LIVEDEPA-IREMIAFnLERAGFDVVEAEDAESAVNLIVEPRPDLILLDWMLPGGSGIQFIRRLKRDEMTRDIPIIMLTA 82
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17618    83 RGEEEDKV-RGLEAGADDYITKPFSPRELVARIKAVL 118
REC_CheY_CheY3 cd19923
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ...
15-131 1.25e-18

phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381150 [Multi-domain]  Cd Length: 119  Bit Score: 82.00  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQ-VLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLT 93
Cdd:cd19923     3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLKAGGFDFVITDWNMPNMDGLELLKTIRADGALSHLPVLMVT 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2590639980  94 AnEQSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd19923    83 A-EAKKENVIAAAQAGVNNYIVKPFTAATLKEKLEKIF 119
REC_OmpR_DrrD-like cd17625
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ...
16-131 2.14e-18

phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381140 [Multi-domain]  Cd Length: 115  Bit Score: 81.11  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLTAN 95
Cdd:cd17625     1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDLIILDIMLPGMDGLEVLKSLREEGIE--TPVLLLTAL 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2590639980  96 EQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17625    79 DAVEDRV-KGLDLGADDYLPKPFSLAELLARIRALL 113
adrA PRK10245
diguanylate cyclase AdrA; Provisional
270-431 2.30e-18

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 87.58  E-value: 2.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 270 QQLEYQAVTDPLTGLLNRRGFyqaadAVLMRNEHsDKCQ------ALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKD 343
Cdd:PRK10245  199 RRLQVMSTRDGMTGVYNRRHW-----ETLLRNEF-DNCRrhhrdaTLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQI 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 344 CLGNEALLARMGGDEFTALFDGLPyPEQAGRFAERLLERMSSCQHIDDLDLNLGVSIGIATYPDCGASVEGLLRAADVAM 423
Cdd:PRK10245  273 TLRGSDVIGRFGGDEFAVIMSGTP-AESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLAL 351

                  ....*...
gi 2590639980 424 YAAKRAGR 431
Cdd:PRK10245  352 YKAKNAGR 359
REC_HupR-like cd17569
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ...
15-130 2.40e-18

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381113 [Multi-domain]  Cd Length: 118  Bit Score: 81.30  E-value: 2.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEV-ARLMRGSQRT-RltpiIFL 92
Cdd:cd17569     3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDVVISDQRMPGMDGAELlKRVRERYPDTvR----ILL 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2590639980  93 TANeqSD-EAVLKGYASGAVD-YMFKPFDPQILKPKV-QAL 130
Cdd:cd17569    79 TGY--ADlDAAIEAINEGEIYrFLTKPWDDEELKETIrQAL 117
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
14-149 2.58e-18

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 88.37  E-value: 2.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  14 VLLVVDDyPENLISM-RALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFL 92
Cdd:PRK11361    6 RILIVDD-EDNVRRMlSTAFALQGFETHCANNGRTALHLFADIHPDVVLMDIRMPEMDGIKALKEMRSHETR--TPVILM 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2590639980  93 TANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQRLTRELEA 149
Cdd:PRK11361   83 TAYAEVETAV-EALRCGAFDYVIKPFDLDELNLIVQRALQLQSMKKEIRHLHQALST 138
REC_TrrA-like cd17554
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ...
15-130 2.89e-18

phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381106 [Multi-domain]  Cd Length: 113  Bit Score: 80.73  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPenliSMRAL----LARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPII 90
Cdd:cd17554     3 ILVVDDEE----NIRELykeeLEDEGYEVVTAGNGEEALEKLESEDPDLVILDIKMPGMDGLETLRKIR--EKKPDLPVI 76
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2590639980  91 FLTA--NEQSDEAVLkgyASGAvdYMFKPFDPQILKPKVQAL 130
Cdd:cd17554    77 ICTAysEYKSDFSSW---AADA--YVVKSSDLTELKETIKRL 113
REC_OmpR_YycF-like cd17614
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ...
15-131 3.02e-18

phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381130 [Multi-domain]  Cd Length: 115  Bit Score: 80.93  E-value: 3.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDypENLIS--MRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsqRTRLTPIIFL 92
Cdd:cd17614     1 ILVVDD--EKPISdiLKFNLTKEGYEVVTAYDGREALEKVEEEQPDLILLDLMLPEKDGLEVCREVR---KTSNVPIIML 75
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2590639980  93 TANEQSDEAVLkGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17614    76 TAKDSEVDKVL-GLELGADDYVTKPFSNRELLARVKANL 113
REC_OmpR_MtPhoP-like cd17615
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ...
15-131 3.61e-18

phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381131 [Multi-domain]  Cd Length: 118  Bit Score: 80.86  E-value: 3.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPE--NLISMRalLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFL 92
Cdd:cd17615     2 VLVVDDEPNitELLSMA--LRYEGWDVETAADGAEALAAAREFRPDAVVLDIMLPDMDGLEVLRRLRADGPD--VPVLFL 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2590639980  93 TANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17615    78 TAKDSVEDRI-AGLTAGGDDYVTKPFSLEEVVARLRALL 115
orf27 CHL00148
Ycf27; Reviewed
15-137 3.77e-18

Ycf27; Reviewed


Pssm-ID: 214376 [Multi-domain]  Cd Length: 240  Bit Score: 84.38  E-value: 3.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDD--YPENLISMRalLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRtrlTPIIFL 92
Cdd:CHL00148    9 ILVVDDeaYIRKILETR--LSIIGYEVITASDGEEALKLFRKEQPDLVILDVMMPKLDGYGVCQEIRKESD---VPIIML 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2590639980  93 TANEQ-SDEavLKGYASGAVDYMFKPFDPQILKPKVQALLDQQSNR 137
Cdd:CHL00148   84 TALGDvSDR--ITGLELGADDYVVKPFSPKELEARIRSVLRRTNKK 127
AmiR COG3707
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ...
16-152 5.70e-18

Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 442921 [Multi-domain]  Cd Length: 194  Bit Score: 82.70  E-value: 5.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLT-ASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsqRTRLTPIIFLTA 94
Cdd:COG3707     7 LVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQIS---EERPAPVILLTA 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  95 NEQSD--EAVLKgyaSGAVDYMFKPFDPQILKPKVQALLdqqSNRRMLQRLTRELEAARA 152
Cdd:COG3707    84 YSDPEliERALE---AGVSAYLVKPLDPEDLLPALELAL---ARFRELRALRRELAKLRE 137
FixJ COG4566
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ...
17-149 6.29e-18

DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443623 [Multi-domain]  Cd Length: 196  Bit Score: 82.46  E-value: 6.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  17 VVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTANE 96
Cdd:COG4566     4 IVDDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGCLLLDVRMPGMSGLELQEELA--ARGSPLPVIFLTGHG 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2590639980  97 QSDEAV--LKgyaSGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQRLTRELEA 149
Cdd:COG4566    82 DVPMAVraMK---AGAVDFLEKPFDDQALLDAVRRALARDRARRAERARRAELRA 133
REC_OmpR_PmrA-like cd17624
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ...
14-131 9.78e-18

phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381139 [Multi-domain]  Cd Length: 115  Bit Score: 79.45  E-value: 9.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  14 VLLVVDDypeNLI--SMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIF 91
Cdd:cd17624     1 ILLVEDD---ALLgdGLKTGLRKAGYAVDWVRTGAEAEAALASGPYDLVILDLGLPDGDGLDLLRRWRRQGQS--LPVLI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2590639980  92 LTANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17624    76 LTARDGVDDRV-AGLDAGADDYLVKPFALEELLARLRALL 114
REC_CheB-like cd17541
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ...
16-117 1.08e-17

phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381096 [Multi-domain]  Cd Length: 125  Bit Score: 79.74  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDypenLISMRALLAR---KDWQ---VLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFE-VARLMrgsqRTRLTP 88
Cdd:cd17541     4 LIVDD----SAVMRKLLSRileSDPDievVGTARDGEEALEKIKELKPDVITLDIEMPVMDGLEaLRRIM----AERPTP 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 2590639980  89 IIFLTAN-EQSDEAVLKGYASGAVDYMFKP 117
Cdd:cd17541    76 VVMVSSLtEEGAEITLEALELGAVDFIAKP 105
REC_LytTR_AlgR-like cd17532
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; ...
16-121 5.23e-17

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AlgR; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AlgR-like group of LytTR/AlgR family response regulators are Streptococcus agalactiae sensory transduction protein LytR, Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR, Bacillus subtilis sensory transduction protein LytT, and Escherichia coli transcriptional regulatory protein BtsR, which are members of two-component regulatory systems. LytR and LytT are components of regulatory systems that regulate genes involved in cell wall metabolism. AlgR positively regulates the algD gene, which codes for a GDP-mannose dehydrogenase, a key enzyme in the alginate biosynthesis pathway. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381087 [Multi-domain]  Cd Length: 118  Bit Score: 77.58  E-value: 5.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYP---ENLISmraLLARkDWQ---VLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMrgSQRTRLTPI 89
Cdd:cd17532     2 LIVDDEPlarEELRY---LLEE-HPDieiVGEAENGEEALEAIEELKPDVVFLDIQMPGLDGLELAKKL--SKLAKPPLI 75
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2590639980  90 IFLTAneqSDEAVLKGYASGAVDYMFKPFDPQ 121
Cdd:cd17532    76 VFVTA---YDEYAVEAFELNAVDYLLKPFSEE 104
REC_NarL-like cd17535
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ...
16-121 9.55e-17

phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381090 [Multi-domain]  Cd Length: 117  Bit Score: 76.78  E-value: 9.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDW--QVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLT 93
Cdd:cd17535     2 LIVDDHPLVREGLRRLLESEPDieVVGEAADGEEALALLRELRPDVVLMDLSMPGMDGIEALRRLRRRYPD--LKVIVLT 79
                          90       100
                  ....*....|....*....|....*...
gi 2590639980  94 ANEqSDEAVLKGYASGAVDYMFKPFDPQ 121
Cdd:cd17535    80 AHD-DPEYVLRALKAGAAGYLLKDSSPE 106
REC_2_GGDEF cd17544
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ...
16-118 1.17e-16

second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381098 [Multi-domain]  Cd Length: 122  Bit Score: 76.40  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEH-DVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTA 94
Cdd:cd17544     4 LVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQHpDIKLVITDYNMPEMDGFELVREIRKKYSRDQLAIIGISA 83
                          90       100
                  ....*....|....*....|....*.
gi 2590639980  95 NEQSDEAV--LKgyaSGAVDYMFKPF 118
Cdd:cd17544    84 SGDNALSArfIK---AGANDFLTKPF 106
REC_OmpR_NsrR-like cd18159
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ...
14-131 4.29e-16

phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381143 [Multi-domain]  Cd Length: 113  Bit Score: 74.63  E-value: 4.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  14 VLLVVDDypenlISMRALLA----RKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLtPI 89
Cdd:cd18159     1 ILIVEDD-----ETIASLLKkhleKWGYEVVLIEDFEDVLEEFLQFKPDLVLLDINLPYFDGFYWCREIR--QISNV-PI 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2590639980  90 IFLTA-NEQSDEavLKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd18159    73 IFISSrDDNMDQ--VMAINMGGDDYITKPFDLDVLLAKIKAIL 113
REC_DC-like cd17534
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ...
16-128 1.65e-15

phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381089 [Multi-domain]  Cd Length: 117  Bit Score: 73.21  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDypENLISM--RALLARKDWQVL-TASSGMEALSALLEHDVDLVLLDVQMP-EMDGFEVARLMRGSQRtrlTPIIF 91
Cdd:cd17534     4 LIVED--EAIIALdlKEILESLGYEVVgIADSGEEAIELAEENKPDLILMDINLKgDMDGIEAAREIREKFD---IPVIF 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2590639980  92 LTANeqSDEAVLKgYA--SGAVDYMFKPFDPQILKPKVQ 128
Cdd:cd17534    79 LTAY--SDEETLE-RAkeTNPYGYLVKPFNERELKAAIE 114
REC_PdtaR-like cd19932
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ...
15-128 1.76e-15

phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381159 [Multi-domain]  Cd Length: 118  Bit Score: 73.22  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDypENLISM--RALLARKDWQVL-TASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSqrtRLTPIIF 91
Cdd:cd19932     3 VLIAED--EALIRMdlREMLEEAGYEVVgEASDGEEAVELAKKHKPDLVIMDVKMPRLDGIEAAKIITSE---NIAPIVL 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  92 LTANEQSDeAVLKGYASGAVDYMFKPFDPQILKPKVQ 128
Cdd:cd19932    78 LTAYSQQD-LVERAKEAGAMAYLVKPFSESDLIPAIE 113
REC_OmpR_kpRstA-like cd17622
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ...
12-131 1.94e-15

phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381137 [Multi-domain]  Cd Length: 116  Bit Score: 72.80  E-value: 1.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  12 NSVLLVVDDYP-ENLISmrALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRtrlTPII 90
Cdd:cd17622     1 TRILLVEDDPKlARLIA--DFLESHGFNVVVEHRGDRALEVIAREKPDAVLLDIMLPGIDGLTLCRDLRPKYQ---GPIL 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2590639980  91 FLTANEqSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17622    76 LLTALD-SDIDHILGLELGADDYVVKPVEPAVLLARLRALL 115
REC_OmpR_CtrA cd17616
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ...
14-131 2.76e-15

phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381132 [Multi-domain]  Cd Length: 114  Bit Score: 72.44  E-value: 2.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  14 VLLVVDDyPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLT 93
Cdd:cd17616     1 VLLIEDD-SATAQSIELMLKSEGFNVYTTDLGEEGLDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLAKVK--TPILILS 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2590639980  94 ANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17616    78 GLADIEDKV-KGLGFGADDYMTKPFHKDELVARIHAIV 114
REC_OmpR_MtrA-like cd17626
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ...
15-131 3.12e-15

phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381141 [Multi-domain]  Cd Length: 115  Bit Score: 72.12  E-value: 3.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDyPENLISMRALLARKD-WQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsqRTRLTPIIFLT 93
Cdd:cd17626     3 ILVVDD-DAALAEMIGIVLRGEgFDPAFCGDGTQALAAFREVRPDLVLLDLMLPGIDGIEVCRQIR---AESGVPIVMLT 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2590639980  94 ANEQSDEAVLkGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17626    79 AKSDTVDVVL-GLESGADDYVAKPFKPKELVARIRARL 115
REC_NtrX-like cd17550
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ...
15-118 3.20e-15

phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381102 [Multi-domain]  Cd Length: 115  Bit Score: 72.14  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTA 94
Cdd:cd17550     1 ILIVDDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPDLVLLDIWLPDMDGLELLKEIK--EKYPDLPVIMISG 78
                          90       100
                  ....*....|....*....|....
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPF 118
Cdd:cd17550    79 HGTIETAV-KATKLGAYDFIEKPL 101
REC_Ycf29 cd19927
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ...
15-117 3.73e-15

phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381154 [Multi-domain]  Cd Length: 102  Bit Score: 71.64  E-value: 3.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTA 94
Cdd:cd19927     1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDLIISDIIMPGVDGYSLLGKLRKNADFDTIPVIFLTA 80
                          90       100
                  ....*....|....*....|...
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKP 117
Cdd:cd19927    81 KGMTSDRI-KGYNAGCDGYLSKP 102
REC_CheC-like cd17593
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ...
28-125 3.87e-15

phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381124 [Multi-domain]  Cd Length: 117  Bit Score: 72.18  E-value: 3.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  28 MRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLTANEQsDEAVLKGYA 107
Cdd:cd17593    17 ARALPADWDVEITFAENGEEALEILREGRIDVLFLDLTMPVMDGYEVLEALPVEQLE--TKVIVVSGDVQ-PEAKERVLE 93
                          90
                  ....*....|....*...
gi 2590639980 108 SGAVDYMFKPFDPQILKP 125
Cdd:cd17593    94 LGALAFLKKPFDPEKLAQ 111
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
16-124 4.06e-15

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 79.51  E-value: 4.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTAN 95
Cdd:PRK11107  671 MAVDDNPANLKLIGALLEEQVEHVVLCDSGHQAVEQAKQRPFDLILMDIQMPGMDGIRACELIRQLPHNQNTPIIAVTAH 750
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2590639980  96 EQSD--EAVLKgyaSGAVDYMFKPFDPQILK 124
Cdd:PRK11107  751 AMAGerERLLS---AGMDDYLAKPIDEAMLK 778
REC_OmpR_CusR-like cd19935
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ...
15-117 4.24e-15

phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381162 [Multi-domain]  Cd Length: 100  Bit Score: 71.32  E-value: 4.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLTA 94
Cdd:cd19935     1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLALTNEYDLIILDVMLPGLDGLEVLRRLRAAGKQ--TPVLMLTA 78
                          90       100
                  ....*....|....*....|...
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKP 117
Cdd:cd19935    79 RDSVEDRV-KGLDLGADDYLVKP 100
REC_PatA-like cd17602
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ...
18-117 5.70e-15

phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.


Pssm-ID: 381129 [Multi-domain]  Cd Length: 102  Bit Score: 71.25  E-value: 5.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  18 VDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTANEQ 97
Cdd:cd17602     4 VDDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDLILIDIDMPDLDGYELCSLLRKSSALKDTPIIMLTGKDG 83
                          90       100
                  ....*....|....*....|
gi 2590639980  98 SDEAVlKGYASGAVDYMFKP 117
Cdd:cd17602    84 LVDRI-RAKMAGASGYLTKP 102
REC_OmpR_CpxR cd17623
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ...
15-131 7.31e-15

phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381138 [Multi-domain]  Cd Length: 115  Bit Score: 71.18  E-value: 7.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRtrlTPIIFLTA 94
Cdd:cd17623     1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPDLVVLDVMLPKMNGLDVLKELRKTSQ---VPVLMLTA 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVLkGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17623    78 RGDDIDRIL-GLELGADDYLPKPFNPRELVARIRAIL 113
REC_OmpR_KdpE-like cd17620
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ...
16-117 9.55e-15

phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381135 [Multi-domain]  Cd Length: 99  Bit Score: 70.27  E-value: 9.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRG-SQrtrlTPIIFLTA 94
Cdd:cd17620     2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDLIILDLGLPDMDGLEVIRRLREwSA----VPVIVLSA 77
                          90       100
                  ....*....|....*....|...
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKP 117
Cdd:cd17620    78 RDEESDKI-AALDAGADDYLTKP 99
REC_Rcp-like cd17557
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ...
15-121 1.27e-14

phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381108 [Multi-domain]  Cd Length: 129  Bit Score: 70.91  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARK--DWQVLTASSGMEALSALLEHD-------VDLVLLDVQMPEMDGFEVARLMRGSQRTR 85
Cdd:cd17557     2 ILLVEDNPGDAELIQEAFKEAgvPNELHVVRDGEEALDFLRGEGeyadaprPDLILLDLNMPRMDGFEVLREIKADPDLR 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2590639980  86 LTPIIFLTANEqSDEAVLKGYASGAVDYMFKPFDPQ 121
Cdd:cd17557    82 RIPVVVLTTSD-AEEDIERAYELGANSYIVKPVDFE 116
REC_OmpR_EcPhoP-like cd19934
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ...
15-131 1.47e-14

phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381161 [Multi-domain]  Cd Length: 117  Bit Score: 70.39  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLTA 94
Cdd:cd19934     1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYDLVVLDLGLPGMDGLSVLRRWRSEGRA--TPVLILTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd19934    79 RDSWQDKV-EGLDAGADDYLTKPFHIEELLARLRALI 114
REC_RssB-like cd17555
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ...
15-117 8.31e-14

phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381107 [Multi-domain]  Cd Length: 116  Bit Score: 68.38  E-value: 8.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTA 94
Cdd:cd17555     3 ILVIDDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDLVLCDLRMPEMDGLEVLKQIT--KESPDTPVIVVSG 80
                          90       100
                  ....*....|....*....|....*
gi 2590639980  95 NEQSDEAV--LKgyaSGAVDYMFKP 117
Cdd:cd17555    81 AGVMSDAVeaLR---LGAWDYLTKP 102
REC_OmpR_ChvI-like cd19936
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ...
17-117 1.38e-13

phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381163 [Multi-domain]  Cd Length: 99  Bit Score: 67.08  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  17 VVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLtPIIFLTA-N 95
Cdd:cd19936     3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDLAILDIKMPRMDGMELLQRLR--QKSTL-PVIFLTSkD 79
                          90       100
                  ....*....|....*....|..
gi 2590639980  96 EQSDEavLKGYASGAVDYMFKP 117
Cdd:cd19936    80 DEIDE--VFGLRMGADDYITKP 99
PRK10955 PRK10955
envelope stress response regulator transcription factor CpxR;
12-136 1.75e-13

envelope stress response regulator transcription factor CpxR;


Pssm-ID: 182864 [Multi-domain]  Cd Length: 232  Bit Score: 70.60  E-value: 1.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  12 NSVLLVVDDypENLISM-RALLARKDWQVLTASSGMEALSaLLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRtrlTPII 90
Cdd:PRK10955    2 NKILLVDDD--RELTSLlKELLEMEGFNVIVAHDGEQALD-LLDDSIDLLLLDVMMPKKNGIDTLKELRQTHQ---TPVI 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2590639980  91 FLTANEQSDEAVLkGYASGAVDYMFKPFDPQILKPKVQALL------DQQSN 136
Cdd:PRK10955   76 MLTARGSELDRVL-GLELGADDYLPKPFNDRELVARIRAILrrshwsEQQQN 126
REC_OmpR_BaeR-like cd19938
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ...
15-131 2.24e-13

phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381165 [Multi-domain]  Cd Length: 114  Bit Score: 67.02  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRtrlTPIIFLTA 94
Cdd:cd19938     2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDLILLDLMLPGTDGLTLCREIRRFSD---VPIIMVTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2590639980  95 N-EQSDEavLKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd19938    79 RvEEIDR--LLGLELGADDYICKPYSPREVVARVKAIL 114
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
146-272 2.27e-13

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 72.19  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 146 ELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQLPNVslwVDSEFYQAYLARRIFR 225
Cdd:COG3852     1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP---LRELLERALAEGQPVT 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2590639980 226 VHDAQLRTQTGQLVPVALSCAPL--PAEQQAMVVTVLDMSVVRNLHQQL 272
Cdd:COG3852    78 EREVTLRRKDGEERPVDVSVSPLrdAEGEGGVLLVLRDITERKRLEREL 126
REC_OmpR_ArcA_TorR-like cd17619
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ...
15-128 2.65e-13

phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381134 [Multi-domain]  Cd Length: 113  Bit Score: 66.64  E-value: 2.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLtPIIFLTA 94
Cdd:cd17619     3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILARQDIDLVLLDINLPGKDGLSLTRELR--EQSEV-GIILVTG 79
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2590639980  95 NEQSDEAVLkGYASGAVDYMFKPFDPQILKPKVQ 128
Cdd:cd17619    80 RDDEVDRIV-GLEIGADDYVTKPFNPRELLVRAK 112
REC_NtrC cd19919
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ...
12-119 3.08e-13

phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381146 [Multi-domain]  Cd Length: 116  Bit Score: 66.53  E-value: 3.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  12 NSVLLVVDDYpenliSMRALLAR----KDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVarLMRGSQRTRLT 87
Cdd:cd19919     1 KTVWIVDDDS-----SIRWVLERalagAGLTVTSFENAQEALAALASSQPDVLISDIRMPGMDGLAL--LAQIKQRHPDL 73
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2590639980  88 PIIFLTANEQSDEAVlKGYASGAVDYMFKPFD 119
Cdd:cd19919    74 PVIIMTAHSDLDSAV-SAYQGGAFEYLPKPFD 104
PRK15479 PRK15479
transcriptional regulator TctD;
15-131 3.52e-13

transcriptional regulator TctD;


Pssm-ID: 185376 [Multi-domain]  Cd Length: 221  Bit Score: 69.36  E-value: 3.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVarLMRGSQRTRLTPIIFLTA 94
Cdd:PRK15479    3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLLQSEMYALAVLDINMPGMDGLEV--LQRLRKRGQTLPVLLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:PRK15479   81 RSAVADRV-KGLNVGADDYLPKPFELEELDARLRALL 116
PRK11083 PRK11083
DNA-binding response regulator CreB; Provisional
15-144 3.74e-13

DNA-binding response regulator CreB; Provisional


Pssm-ID: 236838 [Multi-domain]  Cd Length: 228  Bit Score: 69.22  E-value: 3.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYP---ENLISMralLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgSQRTRLtPIIF 91
Cdd:PRK11083    6 ILLVEDEQaiaDTLVYA---LQSEGFTVEWFERGLPALDKLRQQPPDLVILDVGLPDISGFELCRQLL-AFHPAL-PVIF 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2590639980  92 LTA-NEQSDEAVlkGYASGAVDYMFKPFDPQILKPKVQALLdqqsnRRMLQRLT 144
Cdd:PRK11083   81 LTArSDEVDRLV--GLEIGADDYVAKPFSPREVAARVRTIL-----RRVKKFAA 127
REC_CheV-like cd19924
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ...
15-117 5.90e-13

phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381151 [Multi-domain]  Cd Length: 111  Bit Score: 65.48  E-value: 5.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSAL---------LEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTR 85
Cdd:cd19924     1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLenlakegndLSKELDLIITDIEMPKMDGYELTFELRDDPRLA 80
                          90       100       110
                  ....*....|....*....|....*....|..
gi 2590639980  86 LTPIIFLTAnEQSDEAVLKGYASGAVDYMFKP 117
Cdd:cd19924    81 NIPVILNSS-LSGEFSRARGKKVGADAYLAKF 111
REC_NtrC1-like cd17572
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ...
15-135 6.42e-13

phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381114 [Multi-domain]  Cd Length: 121  Bit Score: 65.68  E-value: 6.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPenliSMRAL----LARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPII 90
Cdd:cd17572     1 VLLVEDSP----SLAALyqeyLSDEGYKVTHVETGKEALAFLSDQPPDVVLLDLKLPDMSGMEILKWIQ--ERSLPTSVI 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2590639980  91 FLTANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALLDQQS 135
Cdd:cd17572    75 VITAHGSVDIAV-EAMRLGAYDFLEKPFDADRLRVTVRNALKHRK 118
ompR PRK09468
osmolarity response regulator; Provisional
15-136 6.48e-13

osmolarity response regulator; Provisional


Pssm-ID: 181883 [Multi-domain]  Cd Length: 239  Bit Score: 68.85  E-value: 6.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPEnlisMRALLAR----KDWQVLTASSGmEALSALLEHD-VDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPI 89
Cdd:PRK09468    8 ILVVDDDMR----LRALLERylteQGFQVRSAANA-EQMDRLLTREsFHLMVLDLMLPGEDGLSICRRLRSQNNP--TPI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2590639980  90 IFLTAN-EQSDEAVlkGYASGAVDYMFKPFDPQILKPKVQALLDQQSN 136
Cdd:PRK09468   81 IMLTAKgEEVDRIV--GLEIGADDYLPKPFNPRELLARIRAVLRRQAP 126
PRK15347 PRK15347
two component system sensor kinase;
16-117 8.39e-13

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 71.98  E-value: 8.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPEN--LISMraLLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQ--RTRLTPIIF 91
Cdd:PRK15347  694 LLVDDVETNrdIIGM--MLVELGQQVTTAASGTEALELGRQHRFDLVLMDIRMPGLDGLETTQLWRDDPnnLDPDCMIVA 771
                          90       100
                  ....*....|....*....|....*.
gi 2590639980  92 LTANEQSDEAVlKGYASGAVDYMFKP 117
Cdd:PRK15347  772 LTANAAPEEIH-RCKKAGMNHYLTKP 796
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
4-100 8.95e-13

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 71.93  E-value: 8.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980   4 AHTQLPDGNSVLLVVDDYPENlismRALLARK----DWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMR 79
Cdd:PRK10841  793 DKAVSDNDDMMILVVDDHPIN----RRLLADQlgslGYQCKTANDGVDALNVLSKNHIDIVLTDVNMPNMDGYRLTQRLR 868
                          90       100
                  ....*....|....*....|.
gi 2590639980  80 gsQRTRLTPIIFLTANEQSDE 100
Cdd:PRK10841  869 --QLGLTLPVIGVTANALAEE 887
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
16-141 9.85e-13

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 71.51  E-value: 9.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVAR-LMRGSQRTRLTPIIFLTA 94
Cdd:PRK11091  529 LLVEDIELNVIVARSVLEKLGNSVDVAMTGKEALEMFDPDEYDLVLLDIQLPDMTGLDIAReLRERYPREDLPPLVALTA 608
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980  95 N---------EQS-DEAVLKGYASGAVDYMFKPF------DPQILKPKV-----QALLDQQsnrrMLQ 141
Cdd:PRK11091  609 NvlkdkkeylDAGmDDVLSKPLSVPALTAMIKKFwdtqddEESTVTTEEsskanEALLDIP----MLE 672
COG4567 COG4567
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ...
9-120 2.41e-12

DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 443624 [Multi-domain]  Cd Length: 177  Bit Score: 65.71  E-value: 2.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980   9 PDGNSVLLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTP 88
Cdd:COG4567     1 SAEDRSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDYAVLDLRLGDGSGLDLIEALRERDPD--AR 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2590639980  89 IIFLTaneqsdeavlkGYAS----------GAVDYMFKPFDP 120
Cdd:COG4567    79 IVVLT-----------GYASiataveaiklGADDYLAKPADA 109
REC_OmpR_BfmR-like cd19939
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ...
15-131 2.43e-12

phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381166 [Multi-domain]  Cd Length: 116  Bit Score: 63.93  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLtPIIFLTA 94
Cdd:cd19939     2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSLVVLDIMLPGMDGLTVCREVR--EHSHV-PILMLTA 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVLkGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd19939    79 RTEEMDRVL-GLEMGADDYLCKPFSPRELLARVRALL 114
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
15-119 2.60e-12

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 69.29  E-value: 2.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLTA 94
Cdd:PRK10365    8 ILVVDDDISHCTILQALLRGWGYNVALANSGRQALEQVREQVFDLVLCDVRMAEMDGIATLKEIKALNPA--IPVLIMTA 85
                          90       100
                  ....*....|....*....|....*
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPFD 119
Cdd:PRK10365   86 YSSVETAV-EALKTGALDYLIKPLD 109
PRK11517 PRK11517
DNA-binding response regulator HprR;
15-135 3.35e-12

DNA-binding response regulator HprR;


Pssm-ID: 183172 [Multi-domain]  Cd Length: 223  Bit Score: 66.46  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRtrlTPIIFLTA 94
Cdd:PRK11517    3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKDDYALIILDIMLPGMDGWQILQTLRTAKQ---TPVICLTA 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALLDQQS 135
Cdd:PRK11517   80 RDSVDDRV-RGLDSGANDYLVKPFSFSELLARVRAQLRQHH 119
REC_DctD-like cd17549
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ...
16-143 4.55e-12

phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381101 [Multi-domain]  Cd Length: 130  Bit Score: 63.66  E-value: 4.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTAN 95
Cdd:cd17549     2 LLVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGVVISDIRMPGMDGLELLAQIR--ELDPDLPVILITGH 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2590639980  96 EQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALLDQQS----NRRMLQRL 143
Cdd:cd17549    80 GDVPMAV-EAMRAGAYDFLEKPFDPERLLDVVRRALEKRRlvleNRRLRQQL 130
REC_ETR-like cd19933
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ...
15-95 7.41e-12

phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381160 [Multi-domain]  Cd Length: 117  Bit Score: 62.80  E-value: 7.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSAL--LEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTP-IIF 91
Cdd:cd19933     3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLasAEHSFQLVLLDLCMPEMDGFEVALRIRKLFGRRERPlIVA 82

                  ....
gi 2590639980  92 LTAN 95
Cdd:cd19933    83 LTAN 86
REC smart00448
cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar ...
15-67 8.59e-12

cheY-homologous receiver domain; CheY regulates the clockwise rotation of E. coli flagellar motors. This domain contains a phosphoacceptor site that is phosphorylated by histidine kinase homologues.


Pssm-ID: 214668 [Multi-domain]  Cd Length: 55  Bit Score: 60.27  E-value: 8.59e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2590639980   15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMP 67
Cdd:smart00448   3 ILVVDDDPLLRELLKALLEKEGYEVDEATDGEEALELLKEEKPDLILLDIMMP 55
PRK11059 PRK11059
regulatory protein CsrD; Provisional
275-682 9.17e-12

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 68.35  E-value: 9.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 275 QAVTDPLTGLLNRRGFYQAADAVLMRNEHSDKCQALMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKDCLG--NEALLA 352
Cdd:PRK11059  227 NAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMryPGALLA 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 353 RMGGDEFTALfdgLPYPEQ--AGRFAERLL---ERMSSCQHIDDLDLnlgVSIGIATYPDcGASVEGLLRAADVAMYAAK 427
Cdd:PRK11059  307 RYSRSDFAVL---LPHRSLkeADSLASQLLkavDALPPPKMLDRDDF---LHIGICAYRS-GQSTEQVMEEAEMALRSAQ 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 428 RAGRQQYRFYD----QELN-GRARSRLMLEdgvrAAIEERAFTLVYQPQVSFaDGHLRGFEALLRWQHPSVGDVPPGLFI 502
Cdd:PRK11059  380 LQGGNGWFVYDkaqlPEKGrGSVRWRTLLE----QTLVRGGPRLYQQPAVTR-DGKVHHRELFCRIRDGQGELLSAELFM 454
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 503 PLLEEARLINRlaswIYRQGVSQ----RRAWrehfaPDVVLGISLSRAQFSMPS----LVDELQRVINEQGlspSQLEVE 574
Cdd:PRK11059  455 PMVQQLGLSEQ----YDRQVIERvlplLRYW-----PEENLSINLSVDSLLSRAfqrwLRDTLLQCPRSQR---KRLIFE 522
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 575 VAETSLMYNIDEAVKQVNRLRELGVRVALDDFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADY 654
Cdd:PRK11059  523 LAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGT 602
                         410       420
                  ....*....|....*....|....*...
gi 2590639980 655 AITVIAEGVETPAQAAWLKANGCAYVQG 682
Cdd:PRK11059  603 ETQVFATGVESREEWQTLQELGVSGGQG 630
REC_CheY cd17542
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ...
16-121 1.33e-11

phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381097 [Multi-domain]  Cd Length: 117  Bit Score: 61.91  E-value: 1.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYpenlISMRALLAR---KDWQ--VLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsqrtRLTP-- 88
Cdd:cd17542     4 LIVDDA----AFMRMMLKDiltKAGYevVGEAANGEEAVEKYKELKPDLVTMDITMPEMDGIEALKEIK-----KIDPna 74
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2590639980  89 -IIFLTANEQsDEAVLKGYASGAVDYMFKPFDPQ 121
Cdd:cd17542    75 kVIMCSAMGQ-EEMVKEAIKAGAKDFIVKPFQPE 107
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
8-130 1.60e-11

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 67.84  E-value: 1.60e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980    8 LPDGNSVLlVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgSQRTRLt 87
Cdd:PRK09959   955 LPEKLSIL-IADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDLLITDVNMPNMDGFELTRKLR-EQNSSL- 1031
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 2590639980   88 PIIFLTANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQAL 130
Cdd:PRK09959  1032 PIWGLTANAQANERE-KGLSCGMNLCLFKPLTLDVLKTHLSQL 1073
REC_citrate_TCS cd19925
phosphoacceptor receiver (REC) domain of citrate family two-component system response ...
38-129 2.28e-11

phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381152 [Multi-domain]  Cd Length: 118  Bit Score: 61.49  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  38 QVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTAnEQSDEAVLKGYASGAVDYMFKP 117
Cdd:cd19925    28 VIGTAGTGEEALKLLKERQPDLILLDIYLPDGNGLDLLRELR--AAGHDVDVIVVTA-ANDVETVREALRLGVVDYLIKP 104
                          90
                  ....*....|..
gi 2590639980 118 FDPQILKPKVQA 129
Cdd:cd19925   105 FTFERLRQRLER 116
PRK10610 PRK10610
chemotaxis protein CheY;
8-133 2.51e-11

chemotaxis protein CheY;


Pssm-ID: 170568 [Multi-domain]  Cd Length: 129  Bit Score: 61.53  E-value: 2.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980   8 LPDGNSVLLVVDDYPENLISMRALLARKDWQ-VLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRL 86
Cdd:PRK10610    1 MADKELKFLVVDDFSTMRRIVRNLLKELGFNnVEEAEDGVDALNKLQAGGFGFVISDWNMPNMDGLELLKTIRADGAMSA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2590639980  87 TPIIFLTAnEQSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALLDQ 133
Cdd:PRK10610   81 LPVLMVTA-EAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEK 126
PRK00742 PRK00742
chemotaxis-specific protein-glutamate methyltransferase CheB;
16-152 4.67e-11

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 234828 [Multi-domain]  Cd Length: 354  Bit Score: 64.79  E-value: 4.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDypenliS--MRALLAR-----KDWQVL-TASSGMEALSALLEHDVDLVLLDVQMPEMDGFE-VARLMrgsqRTRL 86
Cdd:PRK00742    7 LVVDD------SafMRRLISEilnsdPDIEVVgTAPDGLEAREKIKKLNPDVITLDVEMPVMDGLDaLEKIM----RLRP 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2590639980  87 TPII-FLTANEQSDEAVLKGYASGAVDYMFKPF-----DPQILKP----KVQALldqqSNRRMLQRLTRELEAARA 152
Cdd:PRK00742   77 TPVVmVSSLTERGAEITLRALELGAVDFVTKPFlgislGMDEYKEelaeKVRAA----ARARVRALPPRAAAAARA 148
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
566-690 5.85e-11

c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 64.82  E-value: 5.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 566 LSPSQLEVEVAETSLmynIDEAV-KQVNRLRELGVRVALDDFGAGDCSLRMLRDlpIDTLKIDrhlVarlpdSAVDAALV 644
Cdd:COG3434    81 LPPERVVLEILEDVE---PDEELlEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID---V-----LALDLEEL 147
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2590639980 645 RSVIALCADYAITVIAEGVETPAQAAWLKANGCAYVQGFIVAHPMT 690
Cdd:COG3434   148 AELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
REC_Spo0A cd17561
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ...
39-118 6.09e-11

phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381109 [Multi-domain]  Cd Length: 108  Bit Score: 59.93  E-value: 6.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  39 VLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFLTANEQSDEAvLKGYASGAVDYMFKPF 118
Cdd:cd17561    30 VGVAHNGQEALELIEEKEPDVLLLDIIMPHLDGIGVLEKLRRMRLEKRPKIIMLTAFGQEDIT-QRAVELGASYYILKPF 108
psREC_PRR cd17582
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ...
14-117 7.46e-11

pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.


Pssm-ID: 381120 [Multi-domain]  Cd Length: 104  Bit Score: 59.34  E-value: 7.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  14 VLLVVDDyPENLISMRALLARKDWQVLTASSGMEALSAL--LEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIF 91
Cdd:cd17582     1 VLLVEND-DSTRQIVTALLRKCSYEVTAASDGLQAWDVLedEQNEIDLILTEVDLPVSSGFKLLSYIMRHKICKNIPVIM 79
                          90       100
                  ....*....|....*....|....*.
gi 2590639980  92 LTANEqSDEAVLKGYASGAVDYMFKP 117
Cdd:cd17582    80 MSSQD-SVGVVFKCLSKGAADYLVKP 104
PRK11697 PRK11697
two-component system response regulator BtsR;
16-148 7.77e-11

two-component system response regulator BtsR;


Pssm-ID: 236956 [Multi-domain]  Cd Length: 238  Bit Score: 62.94  E-value: 7.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYP---ENLismRALLAR-KDWQVL-TASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRltpII 90
Cdd:PRK11697    5 LIVDDEPlarEEL---RELLQEeGDIEIVgECSNAIEAIGAIHRLKPDVVFLDIQMPRISGLELVGMLDPEHMPY---IV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980  91 FLTANeqsDEAVLKGYASGAVDYMFKPFDPQILkpkvqalldqqsnRRMLQRLTRELE 148
Cdd:PRK11697   79 FVTAF---DEYAIKAFEEHAFDYLLKPIDPARL-------------AKTLARLRQERS 120
CitB COG2197
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ...
15-78 1.68e-10

DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];


Pssm-ID: 441799 [Multi-domain]  Cd Length: 131  Bit Score: 59.14  E-value: 1.68e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2590639980  15 LLVVDDYPENLISMRALLARKD--WQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLM 78
Cdd:COG2197     4 VLIVDDHPLVREGLRALLEAEPdiEVVGEAADGEEALELLEELRPDVVLLDIRMPGMDGLEALRRL 69
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
310-434 4.66e-10

Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.


Pssm-ID: 143637 [Multi-domain]  Cd Length: 133  Bit Score: 58.14  E-value: 4.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 310 LMYMDLDGFKRINDSLGHDAGDRVLRWVGEQLKD-CLGNEALLARMGGDEFTALFdGLPYPEQAGRFAERLLERMSSCQh 388
Cdd:cd07556     4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSlIRRSGDLKIKTIGDEFMVVS-GLDHPAAAVAFAEDMREAVSALN- 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2590639980 389 iDDLDLNLGVSIGIATYPdCGASVEGLLRAADVAMYAAKRAGRQQY 434
Cdd:cd07556    82 -QSEGNPVRVRIGIHTGP-VVVGVIGSRPQYDVWGALVNLASRMES 125
PRK15115 PRK15115
response regulator GlrR; Provisional
15-164 6.71e-10

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 61.78  E-value: 6.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPE--NLISMRalLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGF----EVARLMRGsqrtrlTP 88
Cdd:PRK15115    8 LLLVDDDPGllKLLGMR--LTSEGYSVVTAESGQEALRVLNREKVDLVISDLRMDEMDGMqlfaEIQKVQPG------MP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  89 IIFLTANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL-------DQQSNRRMLQR---LTRELEAAR---AFNA 155
Cdd:PRK15115   80 VIILTAHGSIPDAV-AATQQGVFSFLTKPVDRDALYKAIDDALeqsapatDERWREAIVTRsplMLRLLEQARmvaQSDV 158

                  ....*....
gi 2590639980 156 SILENAAEG 164
Cdd:PRK15115  159 SVLINGQSG 167
REC_HupR cd17596
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ...
15-147 6.81e-10

phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381127 [Multi-domain]  Cd Length: 133  Bit Score: 57.38  E-value: 6.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLaRKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIflTA 94
Cdd:cd17596     3 ILVVDDEVRSLEALRRTL-EEDFDVLTAASAEEALAILEEEWVQVILCDQRMPGTTGVEFLKEVRERWPEVVRIII--SG 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2590639980  95 NEQSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQRLTREL 147
Cdd:cd17596    80 YTDSEDIIAGINEAGIYQYLTKPWHPDQLLLTVRNAARLFELQRENERLSLEL 132
REC_FixJ cd17537
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ...
17-129 7.10e-10

phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381092 [Multi-domain]  Cd Length: 116  Bit Score: 56.83  E-value: 7.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  17 VVDDYPENLISMRALLARKDWQVLTASSGmealSALLEHDVDL----VLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFL 92
Cdd:cd17537     5 VVDDDEAVRDSLAFLLRSVGLAVKTFTSA----SAFLAAAPPDqpgcLVLDVRMPGMSGLELQDELLARGSN--IPIIFI 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  93 TANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQA 129
Cdd:cd17537    79 TGHGDVPMAV-EAMKAGAVDFLEKPFRDQVLLDAIEQ 114
REC_typeA_ARR cd17581
phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and ...
16-117 8.20e-10

phosphoacceptor receiver (REC) domain of type A Arabidopsis response regulators (ARRs) and similar proteins; Type-A response regulators of Arabidopsis (ARRs) are involved in cytokinin signaling, which involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Type-A ARRs function downstream of and are regulated by type-B ARRs, which are a class of MYB-type transcription factors. As primary cytokinin response genes, type-A ARRs act as redundant negative feedback regulators of cytokinin signaling by inactivating the phosphorelay. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-A ARRs are similar in domain structure to CheY, in that they lack a typical output domain and only contain a stand-alone receiver (REC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381119 [Multi-domain]  Cd Length: 122  Bit Score: 56.99  E-value: 8.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEAL-----------SALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRT 84
Cdd:cd17581     2 LAVDDSLVDRKVIERLLRISSCRVTAVDSGKRALeflgledeedsSNFNEPKVNMIITDYCMPGMTGYDLLKKVKESSAL 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2590639980  85 RLTPIIFLTAnEQSDEAVLKGYASGAVDYMFKP 117
Cdd:cd17581    82 KEIPVVIMSS-ENIPTRISRCLEEGAEDFLLKP 113
REC_OmpR_RegX3-like cd17621
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ...
15-117 8.56e-10

phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381136 [Multi-domain]  Cd Length: 99  Bit Score: 56.44  E-value: 8.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRtrlTPIIFLTA 94
Cdd:cd17621     1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADIVLLDLMLPGLSGTEVCRQLRARSN---VPVIMVTA 77
                          90       100
                  ....*....|....*....|...
gi 2590639980  95 NEQSDEAVLkGYASGAVDYMFKP 117
Cdd:cd17621    78 KDSEIDKVV-GLELGADDYVTKP 99
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
138-263 1.63e-09

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: 60.36  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 138 RMLQRLTRELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQLpnvslwvdsEFYQA 217
Cdd:COG5000    76 DQLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPE---------LDLAE 146
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2590639980 218 YLARRIFRVHDAQLRTQTGQLVPVALSCAPLPAEQQamVVTVLDMS 263
Cdd:COG5000   147 LLREALERGWQEEIELTRDGRRTLLVRASPLRDDGY--VIVFDDIT 190
REC_RegA-like cd17563
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ...
12-124 1.65e-09

phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381111 [Multi-domain]  Cd Length: 112  Bit Score: 55.91  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  12 NSVLLVVDDYPENLISMRALlARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIF 91
Cdd:cd17563     1 KSLLLVDDDEVFAERLARAL-ERRGFEVETAHSVEEALALAREEKPDYAVLDLRLGGDSGLDLIPPLR--ALQPDARIVV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2590639980  92 LTaneqsdeavlkGYAS----------GAVDYMFKPFD-PQILK 124
Cdd:cd17563    78 LT-----------GYASiataveaiklGADDYLAKPADaDEILA 110
PRK10651 PRK10651
transcriptional regulator NarL; Provisional
15-129 1.76e-09

transcriptional regulator NarL; Provisional


Pssm-ID: 182619 [Multi-domain]  Cd Length: 216  Bit Score: 58.50  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYP------ENLISMRAllarkDWQVLT-ASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlT 87
Cdd:PRK10651    9 ILLIDDHPmlrtgvKQLISMAP-----DITVVGeASNGEQGIELAESLDPDLILLDLNMPGMNGLETLDKLREKSLS--G 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2590639980  88 PIIFLTANEQSDEaVLKGYASGAVDYMFKPFDPQILKPKVQA 129
Cdd:PRK10651   82 RIVVFSVSNHEED-VVTALKRGADGYLLKDMEPEDLLKALQQ 122
REC_Spo0F-like cd17553
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ...
15-131 4.27e-09

phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381105 [Multi-domain]  Cd Length: 117  Bit Score: 54.87  E-value: 4.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTA 94
Cdd:cd17553     3 ILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDLVLLDMKIPGMDGIEILKRMK--VIDENIRVIIMTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDeAVLKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:cd17553    81 YGELD-MIQESKELGALTHFAKPFDIDEIRDAVKKYL 116
PRK10766 PRK10766
two-component system response regulator TorR;
15-131 6.06e-09

two-component system response regulator TorR;


Pssm-ID: 182711 [Multi-domain]  Cd Length: 221  Bit Score: 56.97  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgSQRTrlTPIIFLTA 94
Cdd:PRK10766    5 ILVVEDEPVTRARLQGYFEQEGYTVSEAASGAGMREIMQNQHVDLILLDINLPGEDGLMLTRELR-SRST--VGIILVTG 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVLkGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:PRK10766   82 RTDSIDRIV-GLEMGADDYVTKPLELRELLVRVKNLL 117
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
14-119 7.60e-09

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 58.73  E-value: 7.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  14 VLLVVDDYPENLISMRALlARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGfeVARLMRGSQRTRLTPIIFLT 93
Cdd:PRK10923    6 VWVVDDDSSIRWVLERAL-AGAGLTCTTFENGNEVLEALASKTPDVLLSDIRMPGMDG--LALLKQIKQRHPMLPVIIMT 82
                          90       100
                  ....*....|....*....|....*.
gi 2590639980  94 ANEQSDEAVlKGYASGAVDYMFKPFD 119
Cdd:PRK10923   83 AHSDLDAAV-SAYQQGAFDYLPKPFD 107
REC_OmpR_VirG cd17594
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ...
16-129 1.11e-08

phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381125 [Multi-domain]  Cd Length: 113  Bit Score: 53.60  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYpenlISMRALLAR----KDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrltPIIF 91
Cdd:cd17594     3 LVVDDD----AAMRHLLILylreRGFDVTAAADGAEEARLMLHRRVDLVLLDLRLGQESGLDLLRTIRARSDV---PIII 75
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2590639980  92 LTANEQSDEAVLKGYASGAVDYMFKPFDPQILKPKVQA 129
Cdd:cd17594    76 ISGDRRDEIDRVVGLELGADDYLAKPFGLRELLARVRA 113
REC_TrxB cd17595
phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase ...
14-132 1.23e-08

phosphoacceptor receiver (REC) domain a fused response regulator with a thioredoxin reductase output domain; This family is composed of uncharacterized fusion proteins containing a REC domain and a thioredoxin reductase domain. Thioredoxin reductase catalyzes the reduction of thioredoxin and is thus a central component in the thioredoxin system. Fusion proteins containing REC and thioredoxin reductase domains could play an important role in the environmental regulation of the cellular dithiol-disulfide ratio. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381126 [Multi-domain]  Cd Length: 135  Bit Score: 53.88  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  14 VLLVVDDYPENLISM-RALLAR--KDWQVLTASSGMEALSALLE-----HDVDLVLLDVQMPEMDGFE----VARLMRGS 81
Cdd:cd17595     2 IILTVDDDPQVLRAVaRDLRRQygKDYRVLRADSGAEALDALKElklrgEAVALFLVDQRMPEMDGVEflekAMELFPEA 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2590639980  82 QRtrltpiIFLTANEQSDEAVlKGYASGAVD-YMFKPFDP--QILKPKVQALLD 132
Cdd:cd17595    82 KR------VLLTAYADTDAAI-RAINDVQLDyYLLKPWDPpeEKLYPVLDDLLD 128
PRK11173 PRK11173
two-component response regulator; Provisional
15-159 1.32e-08

two-component response regulator; Provisional


Pssm-ID: 183013 [Multi-domain]  Cd Length: 237  Bit Score: 56.18  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLtpiIFLTA 94
Cdd:PRK11173    6 ILIVEDELVTRNTLKSIFEAEGYDVFEATDGAEMHQILSENDINLVIMDINLPGKNGLLLARELREQANVAL---MFLTG 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2590639980  95 NEQSDEAVLkGYASGAVDYMFKPFDPQILKPKVQALLDQQSNRRMLQRLTRELEAARaFNASILE 159
Cdd:PRK11173   83 RDNEVDKIL-GLEIGADDYITKPFNPRELTIRARNLLSRTMNLGTVSEERRSVESYK-FNGWELD 145
PRK10710 PRK10710
DNA-binding transcriptional regulator BaeR; Provisional
6-131 1.81e-08

DNA-binding transcriptional regulator BaeR; Provisional


Pssm-ID: 182665 [Multi-domain]  Cd Length: 240  Bit Score: 55.85  E-value: 1.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980   6 TQLPDGNSV--LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsqR 83
Cdd:PRK10710    2 TELPIDENTprILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDLILLDLMLPGTDGLTLCREIR---R 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2590639980  84 TRLTPIIFLTAN-EQSDEavLKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:PRK10710   79 FSDIPIVMVTAKiEEIDR--LLGLEIGADDYICKPYSPREVVARVKTIL 125
PRK10161 PRK10161
phosphate response regulator transcription factor PhoB;
14-135 1.94e-08

phosphate response regulator transcription factor PhoB;


Pssm-ID: 182277 [Multi-domain]  Cd Length: 229  Bit Score: 55.49  E-value: 1.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  14 VLLVVDDYP-ENLISMraLLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFL 92
Cdd:PRK10161    5 ILVVEDEAPiREMVCF--VLEQNGFQPVEAEDYDSAVNQLNEPWPDLILLDWMLPGGSGIQFIKHLKRESMTRDIPVVML 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2590639980  93 TANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALLDQQS 135
Cdd:PRK10161   83 TARGEEEDRV-RGLETGADDYITKPFSPKELVARIKAVMRRIS 124
REC_CpdR_CckA-like cd18160
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ...
15-118 2.52e-08

phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381144 [Multi-domain]  Cd Length: 103  Bit Score: 52.12  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSAL-LEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLT 93
Cdd:cd18160     2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLqQGKDIDIVVTDIVMPEMDGIELAREARKIDPD--VKILFIS 79
                          90       100
                  ....*....|....*....|....*
gi 2590639980  94 ANEQsDEAVLKGYASGAVDYMFKPF 118
Cdd:cd18160    80 GGAA-AAPELLSDAVGDNATLKKPF 103
psREC-like_D2_PleD cd17539
REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with ...
16-143 3.31e-08

REC-like adaptor domain (D2) of response regulator PleD; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a pseudo receiver (psREC)-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes the REC-like adaptor domain D2 of PleD, which is an inactive domain.


Pssm-ID: 381094 [Multi-domain]  Cd Length: 124  Bit Score: 52.32  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLaRKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIfLTAN 95
Cdd:cd17539     2 LLVDDRPSSAERIAAML-SSEHEVVVEADPDEALFRAAEGPFDLVIVSLALEDFDGLRLCSQLRSLERTRQLPIL-AVAD 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2590639980  96 EQSDEAVLKGYASGAVDYMFKPFDPQILKPKVQAlldQQSNRRMLQRL 143
Cdd:cd17539    80 PGDRGRLIRALEIGVNDYLVRPIDPNELLARVRT---QIRRKRYTDYL 124
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
127-323 5.13e-08

Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 56.14  E-value: 5.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 127 VQALLDQQSNRRMLQRLTRELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQlpnv 206
Cdd:COG5809   116 IEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIH---- 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 207 slWVDSEFYQAYLARRIFRVHDAQL----RTQTGQLVPVALSCAPL-PAEQQAMVVTVL-DMSVVRNLHQQLEYQ----- 275
Cdd:COG5809   192 --SDDQENVAAFISQLLKDGGIAQGevrfWTKDGRWRLLEASGAPIkKNGEVDGIVIIFrDITERKKLEELLRKSeklsv 269
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2590639980 276 -----AVT-----DPLTGLlnrRGFYQaadavLMR-NEHSDKcqaLMYMD--LDGFKRIND 323
Cdd:COG5809   270 vgelaAGIaheirNPLTSL---KGFIQ-----LLKdTIDEEQ---KTYLDimLSELDRIES 319
PRK15369 PRK15369
two component system response regulator;
15-144 7.17e-08

two component system response regulator;


Pssm-ID: 185267 [Multi-domain]  Cd Length: 211  Bit Score: 53.54  E-value: 7.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYpeNLIS---MRALLARKDWQVL-TASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPII 90
Cdd:PRK15369    6 ILLVDDH--ELIIngiKNMLAPYPRYKIVgQVDNGLEVYNACRQLEPDIVILDLGLPGMNGLDVIPQLH--QRWPAMNIL 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  91 FLTANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQAL------LDQQSNRRMLQRLT 144
Cdd:PRK15369   82 VLTARQEEHMAS-RTLAAGALGYVLKKSPQQILLAAIQTVavgkryIDPALNREAILALL 140
REC_LytTR_AgrA-like cd17533
phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; ...
38-136 7.72e-08

phosphoacceptor receiver (REC) domain of LytTR/AlgR family response regulators similar to AgrA; Members of the LytTR/AlgR family of response regulators contain a REC domain and a unique LytTR DNA-binding output domain that lacks the helix-turn-helix motif and consists mostly of beta-strands. Transcriptional regulators with the LytTR-type output domains are involved in biosynthesis of extracellular polysaccharides, fimbriation, expression of exoproteins, including toxins, and quorum sensing. Included in this AgrA-like group of LytTR/AlgR family response regulators are Staphylococcus aureus accessory gene regulator protein A (AgrA) and Streptococcus pneumoniae response regulator ComE, which are members of two-component regulatory systems. AgrA is a global regulator that controls the synthesis of virulence factors and other exoproteins. ComE is part of the ComD-ComE system that is part of a quorum-sensing signaling pathway that controls the development of competence, a physiological state required for genetic transformation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381088 [Multi-domain]  Cd Length: 131  Bit Score: 51.47  E-value: 7.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  38 QVLTASSGMEALSALLE---HDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIFLTAneqSDEAVLKG--YASGAVD 112
Cdd:cd17533    32 VIELTGKTEELLEKIKErgkNGIYFLDIDIKMEEKNGLEVAQKIR--KYDPYAIIIFVTT---HSEFAPLTfeYKVAALD 106
                          90       100
                  ....*....|....*....|....*
gi 2590639980 113 YMFKPFDPQILKPKV-QALLDQQSN 136
Cdd:cd17533   107 FILKPLKLEEFKKRIeECIKYAQKN 131
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
152-248 8.99e-08

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 50.88  E-value: 8.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 152 AFNASILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQlPNVSLWVDSEFYQAYLARRIFRVHDAQL 231
Cdd:pfam00989   1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIP-EEDDAEVAELLRQALLQGEESRGFEVSF 79
                          90
                  ....*....|....*..
gi 2590639980 232 RTQTGQLVPVALSCAPL 248
Cdd:pfam00989  80 RVPDGRPRHVEVRASPV 96
PRK12555 PRK12555
chemotaxis-specific protein-glutamate methyltransferase CheB;
16-117 1.14e-07

chemotaxis-specific protein-glutamate methyltransferase CheB;


Pssm-ID: 237135 [Multi-domain]  Cd Length: 337  Bit Score: 54.12  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYP---ENLisMRALLARKDWQVL-TASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVAR-LMrgsqRTRLTPII 90
Cdd:PRK12555    4 GIVNDSPlavEAL--RRALARDPDHEVVwVATDGAQAVERCAAQPPDVILMDLEMPRMDGVEATRrIM----AERPCPIL 77
                          90       100
                  ....*....|....*....|....*...
gi 2590639980  91 FLTAN-EQSDEAVLKGYASGAVDYMFKP 117
Cdd:PRK12555   78 IVTSLtERNASRVFEAMGAGALDAVDTP 105
PRK10701 PRK10701
DNA-binding transcriptional regulator RstA; Provisional
12-134 1.52e-07

DNA-binding transcriptional regulator RstA; Provisional


Pssm-ID: 236738 [Multi-domain]  Cd Length: 240  Bit Score: 53.10  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  12 NSVLLVVDDyPE--NLISmrALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRtrlTPI 89
Cdd:PRK10701    2 NKIVFVEDD-AEvgSLIA--AYLAKHDIDVTVEPRGDRAEATILREQPDLVLLDIMLPGKDGMTICRDLRPKWQ---GPI 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2590639980  90 IFLTANEqSDEAVLKGYASGAVDYMFKPFDPQILKPKVQALLDQQ 134
Cdd:PRK10701   76 VLLTSLD-SDMNHILALEMGACDYILKTTPPAVLLARLRLHLRQN 119
PRK10643 PRK10643
two-component system response regulator PmrA;
42-139 1.59e-07

two-component system response regulator PmrA;


Pssm-ID: 182612 [Multi-domain]  Cd Length: 222  Bit Score: 52.73  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  42 ASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLTANEQSDEAVlKGYASGAVDYMFKPFDPQ 121
Cdd:PRK10643   30 ASTAREAEALLESGHYSLVVLDLGLPDEDGLHLLRRWRQKKYT--LPVLILTARDTLEDRV-AGLDVGADDYLVKPFALE 106
                          90
                  ....*....|....*...
gi 2590639980 122 ILKPKVQALLdqqsnRRM 139
Cdd:PRK10643  107 ELHARIRALI-----RRH 119
REC_hyHK_blue-like cd18161
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ...
16-118 1.59e-07

phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381145 [Multi-domain]  Cd Length: 102  Bit Score: 50.04  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEH-DVDLVLLDVQMP-EMDGFEVARLMRgSQRTRLtPIIFLT 93
Cdd:cd18161     2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGpDIDLLVTDVIMPgGMNGSQLAEEAR-RRRPDL-KVLLTS 79
                          90       100
                  ....*....|....*....|....*
gi 2590639980  94 AneQSDEAVLKGYASGAVDYMFKPF 118
Cdd:cd18161    80 G--YAENAIEGGDLAPGVDVLSKPF 102
REC_PilR cd19926
phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR ...
16-117 1.87e-07

phosphoacceptor receiver (REC) domain of type 4 fimbriae expression regulatory protein PilR and similar proteins; Pseudomonas aeruginosa PilR is the response regulator of the PilS/PilR two-component regulatory system (PilSR TCS) that acts in conjunction with sigma-54 to regulate the expression of type 4 pilus (T4P) major subunit PilA. In addition, the PilSR TCS regulates flagellum-dependent swimming motility and pilus-dependent twitching motility. PilR contains an N-terminal REC domain, a central sigma-54 interaction domain, and a C-terminal Fis-type helix-turn-helix DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381153 [Multi-domain]  Cd Length: 100  Bit Score: 49.46  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMrgSQRTRLTPIIFLTAN 95
Cdd:cd19926     2 LVVDDEPDIRELLEITLGRMGLDVRSARNVKEARELLASEPYDLCLTDMRLPDGSGLELVQHI--QQRLPQTPVAVITAY 79
                          90       100
                  ....*....|....*....|..
gi 2590639980  96 EQSDEAVlKGYASGAVDYMFKP 117
Cdd:cd19926    80 GSLDTAI-EALKAGAFDFLTKP 100
PRK09836 PRK09836
DNA-binding transcriptional activator CusR; Provisional
15-131 2.10e-07

DNA-binding transcriptional activator CusR; Provisional


Pssm-ID: 182102 [Multi-domain]  Cd Length: 227  Bit Score: 52.23  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLTA 94
Cdd:PRK09836    3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHLAMTGDYDLIILDIMLPDVNGWDIVRMLRSANKG--MPILLLTA 80
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:PRK09836   81 LGTIEHRV-KGLELGADDYLVKPFAFAELLARVRTLL 116
PRK10336 PRK10336
two-component system response regulator QseB;
14-131 3.22e-07

two-component system response regulator QseB;


Pssm-ID: 182387 [Multi-domain]  Cd Length: 219  Bit Score: 51.82  E-value: 3.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  14 VLLVVDDypeNLIS--MRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLTPIIF 91
Cdd:PRK10336    3 ILLIEDD---MLIGdgIKTGLSKMGFSVDWFTQGRQGKEALYSAPYDAVILDLTLPGMDGRDILREWR--EKGQREPVLI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2590639980  92 LTANEQSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALL 131
Cdd:PRK10336   78 LTARDALAERV-EGLRLGADDYLCKPFALIEVAARLEALM 116
REC_NarL cd19931
phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate ...
15-123 4.79e-07

phosphoacceptor receiver (REC) domain of Nitrate/Nitrite response regulator L (NarL); Nitrate/nitrite response regulator protein NarL contains an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. Escherichia coli NarL activates the expression of the nitrate reductase (narGHJI) and formate dehydrogenase-N (fdnGHI) operons, and represses the transcription of the fumarate reductase (frdABCD) operon in response to a nitrate/nitrite induction signal. Phosphorylation of the NarL REC domain releases the C-terminal HTH output domain that subsequently binds specific DNA promoter sites to repress or activate gene expression. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381158 [Multi-domain]  Cd Length: 117  Bit Score: 48.88  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYP------ENLISMRALLArkdwQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRG-SQRTRLt 87
Cdd:cd19931     1 VLLIDDHPllrkgiKQLIELDPDFT----VVGEASSGEEGIELAERLDPDLILLDLNMKGMSGLDTLKALREeGVSARI- 75
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2590639980  88 pIIFLTANEQSDeaVLKGYASGAVDYMFKPFDPQIL 123
Cdd:cd19931    76 -VILTVSDAEDD--VVTALRAGADGYLLKDMEPEDL 108
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
145-273 6.52e-07

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 52.47  E-value: 6.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 145 RELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQlpnvslwvDSEFYQAYLARRif 224
Cdd:COG3829     4 LELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIP--------NSPLLEVLKTGK-- 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2590639980 225 RVHDAQLRTQtGQLVPVALSCAPLPAEQQ--AMVVTVLDMSVVRNLHQQLE 273
Cdd:COG3829    74 PVTGVIQKTG-GKGKTVIVTAIPIFEDGEviGAVETFRDITELKRLERKLR 123
PRK10693 PRK10693
two-component system response regulator RssB;
42-117 9.31e-07

two-component system response regulator RssB;


Pssm-ID: 182652 [Multi-domain]  Cd Length: 303  Bit Score: 51.14  E-value: 9.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  42 ASSGMEALSALLEHDVDLVLLDVQMPEMDGFE-VARL-MRGSQrtrlTPIIFLTANEQ-SDEA-VLKgyaSGAVDYMFKP 117
Cdd:PRK10693    3 AANGVDALELLGGFTPDLIICDLAMPRMNGIEfVEHLrNRGDQ----TPVLVISATENmADIAkALR---LGVQDVLLKP 75
REC_DesR-like cd19930
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ...
15-79 1.23e-06

phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381157 [Multi-domain]  Cd Length: 117  Bit Score: 47.65  E-value: 1.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2590639980  15 LLVVDDYPENLISMRALLARKD--WQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMR 79
Cdd:cd19930     1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDVAILDIEMPGRTGLEVAAELR 67
PRK13557 PRK13557
histidine kinase; Provisional
11-132 1.29e-06

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 51.60  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  11 GNSVLLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEH-DVDLVLLDVQMP-EMDGFEVARLMRgsqrtRLTP 88
Cdd:PRK13557  414 GTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHpEVDLLFTDLIMPgGMNGVMLAREAR-----RRQP 488
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2590639980  89 II--FLTAneqsdeavlkGYASGAV----------DYMFKPFDPQILKPKVQALLD 132
Cdd:PRK13557  489 KIkvLLTT----------GYAEASIertdaggsefDILNKPYRRAELARRVRMVLD 534
PAS COG2202
PAS domain [Signal transduction mechanisms];
142-273 1.47e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 50.41  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 142 RLTRELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLvqlpnVSLWVDSEFYQAY--- 218
Cdd:COG2202     1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL-----LPPEDDDEFLELLraa 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980 219 LARRIFRVHDAQLRTQTGQLVPVALSCAPLPAEQ---QAMVVTVLDMSVVRNLHQQLE 273
Cdd:COG2202    76 LAGGGVWRGELRNRRKDGSLFWVELSISPVRDEDgeiTGFVGIARDITERKRAEEALR 133
PAS COG2202
PAS domain [Signal transduction mechanisms];
142-272 2.01e-06

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 50.02  E-value: 2.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 142 RLTRELEAARAFNASILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQLPnvslwvDSEFYQAYLAR 221
Cdd:COG2202   127 RAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPE------DRERLLELLRR 200
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980 222 RI---FRVHDAQLRTQTGQLVPVALSCAPLP----AEQQAMVVTVLDMSVVRNLHQQL 272
Cdd:COG2202   201 LLeggRESYELELRLKDGDGRWVWVEASAVPlrdgGEVIGVLGIVRDITERKRAEEAL 258
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
152-201 2.52e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.


Pssm-ID: 214512  Cd Length: 67  Bit Score: 45.47  E-value: 2.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2590639980  152 AFNASILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLV 201
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI 50
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
350-427 3.06e-06

Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];


Pssm-ID: 442920 [Multi-domain]  Cd Length: 179  Bit Score: 47.98  E-value: 3.06e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2590639980 350 LLARMGGDEFTALFDGLPyPEQAGRFAERLLERMSSCQHIddldlNLGVSIGIATypdcgasvEGLLRAADvAMYAAK 427
Cdd:COG3706   117 LVARYGGEEFAILLPGTD-LEGALAVAERIREAVAELPSL-----RVTVSIGVAG--------DSLLKRAD-ALYQAR 179
REC_GlnL-like cd17565
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ...
17-117 3.25e-06

phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381112 [Multi-domain]  Cd Length: 103  Bit Score: 46.11  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  17 VVDDYPeNLISMRALLARKDWQ---VLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEvarLMRGSQRTRLTPIIFLT 93
Cdd:cd17565     3 IVDDDK-NIIKILSDIIEDDDLgevVGEADNGAQAYDEILFLQPDIVLIDLLMPGMDGIQ---LVRKLKDTGSNGKFIMI 78
                          90       100
                  ....*....|....*....|....
gi 2590639980  94 ANEQSDEAVLKGYASGAVDYMFKP 117
Cdd:cd17565    79 SQVSDKEMIGKAYQAGIEFFINKP 102
fixJ PRK09390
response regulator FixJ; Provisional
17-133 3.33e-06

response regulator FixJ; Provisional


Pssm-ID: 181815 [Multi-domain]  Cd Length: 202  Bit Score: 48.46  E-value: 3.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  17 VVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgSQRTRLtPIIFLTANE 96
Cdd:PRK09390    8 VVDDDEAMRDSLAFLLDSAGFEVRLFESAQAFLDALPGLRFGCVVTDVRMPGIDGIELLRRLK-ARGSPL-PVIVMTGHG 85
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2590639980  97 QSDEAVlKGYASGAVDYMFKPFDPQILKPKVQALLDQ 133
Cdd:PRK09390   86 DVPLAV-EAMKLGAVDFIEKPFEDERLIGAIERALAQ 121
PRK10816 PRK10816
two-component system response regulator PhoP;
38-135 4.28e-06

two-component system response regulator PhoP;


Pssm-ID: 182755 [Multi-domain]  Cd Length: 223  Bit Score: 48.58  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  38 QVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFLTANE--QSDEAVLKgyaSGAVDYMF 115
Cdd:PRK10816   26 QVDAAEDAKEADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSNDVS--LPILVLTAREswQDKVEVLS---AGADDYVT 100
                          90       100
                  ....*....|....*....|
gi 2590639980 116 KPFDPQILKPKVQALLDQQS 135
Cdd:PRK10816  101 KPFHIEEVMARMQALMRRNS 120
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
161-262 4.86e-06

PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 45.70  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 161 AAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQLPNVSLWVdsEFYQAYLARRIFRVHDAQLRTQTGQLVP 240
Cdd:cd00130     1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELR--ERLENLLSGGEPVTLEVRLRRKDGSVIW 78
                          90       100
                  ....*....|....*....|....*
gi 2590639980 241 VALSCAPL---PAEQQAMVVTVLDM 262
Cdd:cd00130    79 VLVSLTPIrdeGGEVIGLLGVVRDI 103
REC_RocR cd17530
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ...
15-76 7.78e-06

phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381086 [Multi-domain]  Cd Length: 123  Bit Score: 45.51  E-value: 7.78e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2590639980  15 LLVVDDypENLISMRALLARKDW---QVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVAR 76
Cdd:cd17530     3 VLVLDD--DPFQCMMAATILEDLgpgNVDEADDGREALVILLCNAPDIIICDLKMPDMDGIEFLR 65
PRK09958 PRK09958
acid-sensing system DNA-binding response regulator EvgA;
16-90 8.85e-06

acid-sensing system DNA-binding response regulator EvgA;


Pssm-ID: 182168 [Multi-domain]  Cd Length: 204  Bit Score: 47.20  E-value: 8.85e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2590639980  16 LVVDDYPENLISMRALLARKDWQVLTA-SSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPII 90
Cdd:PRK09958    4 IIIDDHPLAIAAIRNLLIKNDIEILAElTEGGSAVQRVETLKPDIVIIDVDIPGVNGIQVLETLRKRQYSGIIIIV 79
REC_TPR cd17589
phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR) ...
16-124 1.29e-05

phosphoacceptor receiver (REC) domain of uncharacterized tetratricopeptide repeat (TPR)-containing response regulators; Response regulators share the common phosphoacceptor REC domain and different output domains. This subfamily contains uncharacterized response regulators with TPR repeats as the effector or output domain, which might contain between 3 to 16 TPR repeats (each about 34 amino acids). TPR-containing proteins occur in all domains of life and the abundance of TPR-containing proteins in a bacterial proteome is not indicative of virulence. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members in this subfamily may contain inactive REC domains lacking canonical metal-binding and active site residues.


Pssm-ID: 381123 [Multi-domain]  Cd Length: 115  Bit Score: 44.95  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPENLISMRALL----ARkdwQVLTASSGMEALSALLEHDVDLVLLDVQMPE-MDGFEVARLMRGSQRTRLTPII 90
Cdd:cd17589     2 LIVDDQPTFRSMLKSMLrslgVT---RIDTASSGEEALRMCENKTYDIVLCDYNLGKgKNGQQLLEELRHKKLISPSTVF 78
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2590639980  91 FLTANEQSDEAVLKGYASGAVDYMFKPFDPQILK 124
Cdd:cd17589    79 IMVTGESSRAMVLSALELEPDDYLLKPFTVSELR 112
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
141-228 1.34e-05

Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 48.26  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 141 QRLTRELEAarafnasILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQLPNVSLWVDSEFYQAYLA 220
Cdd:COG3283    76 EREHLELDA-------LLEALPDPVFSIDLKGKIELANPAALSLLGLSEEELIGQPLSELLKGFNFSRWLESNEPRPQSE 148

                  ....*...
gi 2590639980 221 RRIFRVHD 228
Cdd:COG3283   149 RVVINGQD 156
REC_WspR-like cd17575
phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The ...
13-120 2.13e-05

phosphoacceptor receiver (REC) domain of WspR response regulator and similar proteins; The GGDEF response regulator WspR is part of the Wsp system that is homologous to chemotaxis systems and also includes the membrane-bound receptor protein WspA. In response to growth on surfaces, WspR is phosphorylated by the Wsp signal transduction complex and is activated, functioning as a diguanylate cyclase (DGC) that catalyzes c-di-GMP synthesis. WspR is a hybrid response regulator-diguanylate cyclase, containing an N-terminal REC domain and a C-terminal GGDEF domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381117 [Multi-domain]  Cd Length: 128  Bit Score: 44.71  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  13 SVLLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTRLTPIIFL 92
Cdd:cd17575     2 MVLLVDDQAIIGEAVRRALADEEDIDFHYCSDPTEAIEVASQIKPTVILQDLVMPGVDGLTLVRFFRANPATRDIPIIVL 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 2590639980  93 TANEqsdEAVLKG--YASGAVDYMFKPFDP 120
Cdd:cd17575    82 STKE---EPEVKSeaFALGANDYLVKLPDK 108
PRK14084 PRK14084
DNA-binding response regulator;
16-136 2.18e-05

DNA-binding response regulator;


Pssm-ID: 184495 [Multi-domain]  Cd Length: 246  Bit Score: 46.67  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  16 LVVDDYPenlismralLARKDWQVL-----------TASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMrgsQRT 84
Cdd:PRK14084    4 LIVDDEP---------LARNELTYLlneiggfeeinEAENVKETLEALLINQYDIIFLDINLMDESGIELAAKI---QKM 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2590639980  85 RLTP-IIFLTANEQSdeAVlKGYASGAVDYMFKPFDPQILKP---KVQALLDQQSN 136
Cdd:PRK14084   72 KEPPaIIFATAHDQF--AV-KAFELNATDYILKPFEQKRIEQavnKVRATKAKDDN 124
PLN03029 PLN03029
type-a response regulator protein; Provisional
15-146 6.04e-05

type-a response regulator protein; Provisional


Pssm-ID: 215544 [Multi-domain]  Cd Length: 222  Bit Score: 45.02  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHD--------------------VDLVLLDVQMPEMDGFEV 74
Cdd:PLN03029   11 VLAVDDSLIDRKLIEKLLKTSSYQVTTVDSGSKALKFLGLHEddrsnpdtpsvspnshqeveVNLIITDYCMPGMTGYDL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  75 ARLMRGSQRTRLTPIIFLTAnEQSDEAVLKGYASGAVDYMFKP--------FDPQILKPKVQAllDQQSNRRMLQRLTRE 146
Cdd:PLN03029   91 LKKIKESSSLRNIPVVIMSS-ENVPSRITRCLEEGAEEFFLKPvqlsdlnrLKPHMMKTKSKN--QKQENQEKQEKLEES 167
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
593-689 8.23e-05

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 44.99  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 593 RLRELGvRVALDDFGAGDCSLRMLRDLPIDTLKIDRHLVARLPDSAVDAALVRSVIALCADYAITVIAEGVETPAQAAWL 672
Cdd:PRK11596  148 SMCEFG-PLWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDV 226
                          90
                  ....*....|....*..
gi 2590639980 673 KANGCAYVQGFIVAHPM 689
Cdd:PRK11596  227 QRSPAFAAQGYFLSRPA 243
PRK10529 PRK10529
DNA-binding transcriptional activator KdpE; Provisional
12-136 1.53e-04

DNA-binding transcriptional activator KdpE; Provisional


Pssm-ID: 182522 [Multi-domain]  Cd Length: 225  Bit Score: 43.64  E-value: 1.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  12 NSVLLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRgsQRTRLtPIIF 91
Cdd:PRK10529    1 MTNVLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDLIILDLGLPDGDGIEFIRDLR--QWSAI-PVIV 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2590639980  92 LTA-NEQSDEavLKGYASGAVDYMFKPFDPQILKPKVQALLDQQSN 136
Cdd:PRK10529   78 LSArSEESDK--IAALDAGADDYLSKPFGIGELQARLRVALRRHSA 121
PRK09935 PRK09935
fimbriae biosynthesis transcriptional regulator FimZ;
15-98 3.30e-04

fimbriae biosynthesis transcriptional regulator FimZ;


Pssm-ID: 182154 [Multi-domain]  Cd Length: 210  Bit Score: 42.56  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLAR-KDWQV-LTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIFL 92
Cdd:PRK09935    6 VIIMDTHPIIRMSIEVLLQKnSELQIvLKTDDYRITIDYLRTRPVDLIIMDIDLPGTDGFTFLKRIKQIQST--VKVLFL 83

                  ....*.
gi 2590639980  93 TANEQS 98
Cdd:PRK09935   84 SSKSEC 89
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
156-276 4.15e-04

PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 40.74  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 156 SILENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVQLPnvslwvDSEFYQAYLARRIFRVHDA-----Q 230
Cdd:TIGR00229   7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEE------DREEVRERIERRLEGEPEPvseerR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2590639980 231 LRTQTGQLVPVALSCAPLPAEQQAMVVtvldMSVVRNLHQQLEYQA 276
Cdd:TIGR00229  81 VRRKDGSEIWVEVSVSPIRTNGGELGV----VGIVRDITERKEAEE 122
REC_RitR-like cd19922
receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus ...
32-118 4.17e-04

receiver (REC) domain of orphan response regulator RitR and similar domains; Streptococcus pneumoniae RitR (Repressor of iron transport Regulator, formerly RR489) is an orphan two-component signal transduction response regulator that is required for lung pathogenicity. It acts to repress iron uptake via binding the pneumococcal iron uptake (Piu) transporter promoter. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. However, members of this family do not contain the phosphorylatable aspartic acid residue and are phosphorylation-independent.


Pssm-ID: 381149 [Multi-domain]  Cd Length: 110  Bit Score: 40.54  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  32 LARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMrgsQRTRLTPIIFLTANEQSDEAVLKGYASGAV 111
Cdd:cd19922    18 LQKEGYRVDLVETGQEALSLALETDYDLILLNVNLSDMSAQDFAEKL---SRIKPASVIIVLDHWEDLQEELEEVQRFAV 94

                  ....*..
gi 2590639980 112 DYMFKPF 118
Cdd:cd19922    95 SYVVKPV 101
PRK10403 PRK10403
nitrate/nitrite response regulator protein NarP;
15-129 4.83e-04

nitrate/nitrite response regulator protein NarP;


Pssm-ID: 182431 [Multi-domain]  Cd Length: 215  Bit Score: 42.15  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALL---ARKDwQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVARLMRGSQRTrlTPIIF 91
Cdd:PRK10403    9 VLIVDDHPLMRRGVRQLLeldPGFE-VVAEAGDGASAIDLANRLDPDVILLDLNMKGMSGLDTLNALRRDGVT--AQIII 85
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2590639980  92 LTANEQSDEaVLKGYASGAVDYMFKPFDPQILKPKVQA 129
Cdd:PRK10403   86 LTVSDASSD-VFALIDAGADGYLLKDSDPEVLLEAIRA 122
REC_PhyR cd17540
phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is ...
13-131 1.25e-03

phosphoacceptor receiver (REC) domain of response regulator PhyR and similar proteins; PhyR is a hybrid stress regulator that contains an N-terminal sigma-like (SL) domain and a C-terminal REC domain. Phosphorylation of the REC domain is known to promote binding of the SL domain to an anti-sigma factor. PhyR thus functions as an anti-anti-sigma factor in its phosphorylated state. It is involved in the general stress response. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381095 [Multi-domain]  Cd Length: 117  Bit Score: 39.15  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  13 SVLLVVDDYPenLISM--RALLARKDWQVL-TASSGMEALSALLEHDVDLVLLDVQMPE-MDGFEVARLMrgsQRTRLTP 88
Cdd:cd17540     1 TRVLIIEDEP--LIAMdlEQIVEDLGHQVVgIARTRDEAVALARRERPDLILADIQLADgSSGIDAVNEI---LTTHDVP 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2590639980  89 IIFLTAneqSDEAVLKGYASGAVDYMFKPFDPQILKPKV-QALL 131
Cdd:cd17540    76 VIFVTA---YPERLLTGERPEPTFLITKPFDPEMVKAAIsQALF 116
REC_RcNtrC-like cd19928
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ...
15-117 2.22e-03

phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381155 [Multi-domain]  Cd Length: 100  Bit Score: 37.87  E-value: 2.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980  15 LLVVDDYPENLISMRALLARKDWQVLTASSGMEALSALLEHDVDLVLLDVQMPEMDGFEVarLMRGSQRTRLTPIIFLTA 94
Cdd:cd19928     1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDLVITDVVMPDENGLDL--IPRIKKARPDLPIIVMSA 78
                          90       100
                  ....*....|....*....|...
gi 2590639980  95 NEQSDEAVlKGYASGAVDYMFKP 117
Cdd:cd19928    79 QNTLMTAV-KAAERGAFEYLPKP 100
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
158-266 6.20e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 37.01  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2590639980 158 LENAAEGILVVDATGIISFANPAISWLLQAPVEQLQGVSVLDLVqlpnvsLWVDSEFYQAYLARRI---FRVHDAQLRTQ 234
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELL------PPEDAARLERALRRALegeEPIDFLEELLL 74
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2590639980 235 TGQLVPVALSCAPLPAEQ---QAMVVTVLDMSVVR 266
Cdd:pfam08448  75 NGEERHYELRLTPLRDPDgevIGVLVISRDITERR 109
REC_HP-RR-like cd17573
phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; ...
58-123 6.25e-03

phosphoacceptor receiver (REC) domain of orphan response regulator HP-RR and similar proteins; Helicobacter pylori response regulator hp1043 (HP-RR) is an orphan response regulator which is phosphorylation-independent and is essential for growth. HP-RR functions as a cell growth-associated regulator in the absence of post-translational modification. Members of this subfamily contain REC and DNA-binding output domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.


Pssm-ID: 381115 [Multi-domain]  Cd Length: 110  Bit Score: 37.02  E-value: 6.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2590639980  58 DLVLLDVQMPEMDGFEVarLMRGSQRTRLTPIIFLTANEQSDEAVLkGYASGAVDYMFKPFDPQIL 123
Cdd:cd17573    44 DLVLVSDKLPDGNGLSI--VSRIKEKHPSIVVIVLSDNPKTEQEIE-AFKEGADDYIAKPFDFKVL 106
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH