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Conserved domains on  [gi|780222879|ref|WP_045525402|]
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GGDEF and EAL domain-containing protein [Aeromonas caviae]

Protein Classification

GGDEF and EAL domain-containing protein( domain architecture ID 13663151)

GGDEF and EAL domain-containing protein with GAF and PAS sensor domains may function as a diguanylate cyclase and/or diguanylate phosphodiesterase

Graphical summary

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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 ...
302-978 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: 567.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 302 EFQPRGQDLWLIPRCVVEGDAFAVVKPMPMDIGPGREIFQHGQSLYVEDLALRYPQSSQLLALDAKAYVGIPFPGPNGLP 381
Cdd:COG5001    5 AALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 382 LGQLTLLLATPLADPAPLLDVLYEQRERAASELQRLANDDALRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASE 461
Cdd:COG5001   85 LLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLAL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 462 EMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKETA 541
Cdd:COG5001  165 LLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAE 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 542 RHIERLAYYDDLCDLYNRRSLTDIMQRTLQAP--SGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENL 619
Cdd:COG5001  245 ERLRHLAYHDPLTGLPNRRLFLDRLEQALARArrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGD 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 620 VLARTSGDEFALLFTALGQgyiTAKilAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVH 699
Cdd:COG5001  325 TVARLGGDEFAVLLPDLDD---PED--AEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMY 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 700 MAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPI 779
Cdd:COG5001  400 RAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPL 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 780 AEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENR 859
Cdd:COG5001  480 AEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDP 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 860 LESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVE 939
Cdd:COG5001  560 EEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVE 639
                        650       660       670
                 ....*....|....*....|....*....|....*....
gi 780222879 940 EEEQLAVLKALGCQHYQGFLTSRPLPVKALESLLGATPA 978
Cdd:COG5001  640 TEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
122-253 5.89e-03

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 38.23  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  122 QQQYDAMLESLKECLGADRLILWHYQAHgalgGEQLTPVFTLGVDALGAIRGDSRYIRALRARGALSFSEAAHQPMLSQH 201
Cdd:pfam01590   3 EEILQTILEELRELLGADRCALYLPDAD----GLEYLPPGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPRFLDP 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 780222879  202 Y-YLADANVCSRLDGALLEQEKLIGVLSLeYAESTLISDDTLQLVRHCARLLG 253
Cdd:pfam01590  79 LlLLRNFGIRSLLAVPIIDDGELLGVLVL-HHPRPPFTEEELELLEVLADQVA 130
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
302-978 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: 567.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 302 EFQPRGQDLWLIPRCVVEGDAFAVVKPMPMDIGPGREIFQHGQSLYVEDLALRYPQSSQLLALDAKAYVGIPFPGPNGLP 381
Cdd:COG5001    5 AALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 382 LGQLTLLLATPLADPAPLLDVLYEQRERAASELQRLANDDALRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASE 461
Cdd:COG5001   85 LLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLAL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 462 EMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKETA 541
Cdd:COG5001  165 LLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAE 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 542 RHIERLAYYDDLCDLYNRRSLTDIMQRTLQAP--SGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENL 619
Cdd:COG5001  245 ERLRHLAYHDPLTGLPNRRLFLDRLEQALARArrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGD 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 620 VLARTSGDEFALLFTALGQgyiTAKilAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVH 699
Cdd:COG5001  325 TVARLGGDEFAVLLPDLDD---PED--AEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMY 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 700 MAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPI 779
Cdd:COG5001  400 RAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPL 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 780 AEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENR 859
Cdd:COG5001  480 AEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDP 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 860 LESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVE 939
Cdd:COG5001  560 EEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVE 639
                        650       660       670
                 ....*....|....*....|....*....|....*....
gi 780222879 940 EEEQLAVLKALGCQHYQGFLTSRPLPVKALESLLGATPA 978
Cdd:COG5001  640 TEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
528-978 6.18e-104

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 338.58  E-value: 6.18e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 528 VCSFHDITQEKETARHIERLAYYDDLCDLYNRRSLTDIMQRTLQAPSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAV 607
Cdd:PRK10060 217 ICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 608 VVRLKSLPQENLVLARTSGDEFALLFTALGQGyitakiLAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDH 687
Cdd:PRK10060 297 SLAILSCLEEDQTLARLGGDEFLVLASHTSQA------ALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDS 370
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 688 LVLMQQADTAVHMAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPqyRVD-NGTLSGIEALLRWQKA 766
Cdd:PRK10060 371 ESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQP--KITwRGEVRSLEALVRWQSP 448
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 767 DGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNNGLAIpHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRL 846
Cdd:PRK10060 449 ERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINL-RVAVNVSARQLADQTIFTALKQALQELNFEYCPI 527
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 847 LLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLA 926
Cdd:PRK10060 528 DVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVA 607
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 780222879 927 RVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKALESLLGATPA 978
Cdd:PRK10060 608 QALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYLK 659
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
728-966 1.23e-103

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: 322.96  E-value: 1.23e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 728 NQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNN 807
Cdd:cd01948    1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 808 GLAIpHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSS 887
Cdd:cd01948   81 GPDL-RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879 888 LAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPV 966
Cdd:cd01948  160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
728-966 1.97e-90

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 287.96  E-value: 1.97e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879   728 NQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNN 807
Cdd:smart00052   2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879   808 GLAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSS 887
Cdd:smart00052  82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879   888 LAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPV 966
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
728-963 1.05e-79

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: 258.79  E-value: 1.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  728 NQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNN 807
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  808 glAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSS 887
Cdd:pfam00563  82 --PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780222879  888 LAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRP 963
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
547-707 4.94e-25

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: 102.42  E-value: 4.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  547 LAYYDDLCDLYNRRSLTDIMQRTLQ--APSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLART 624
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKraRRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  625 SGDEFALLF--TALGQgyitAKILAEhfaRELMGIFRAPFDI-GDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMA 701
Cdd:TIGR00254  81 GGEEFVVILpgTPLED----ALSKAE---RLRDAINSKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQA 153

                  ....*.
gi 780222879  702 KRAGQG 707
Cdd:TIGR00254 154 KKAGRN 159
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
122-253 5.89e-03

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 38.23  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  122 QQQYDAMLESLKECLGADRLILWHYQAHgalgGEQLTPVFTLGVDALGAIRGDSRYIRALRARGALSFSEAAHQPMLSQH 201
Cdd:pfam01590   3 EEILQTILEELRELLGADRCALYLPDAD----GLEYLPPGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPRFLDP 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 780222879  202 Y-YLADANVCSRLDGALLEQEKLIGVLSLeYAESTLISDDTLQLVRHCARLLG 253
Cdd:pfam01590  79 LlLLRNFGIRSLLAVPIIDDGELLGVLVL-HHPRPPFTEEELELLEVLADQVA 130
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
302-978 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: 567.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 302 EFQPRGQDLWLIPRCVVEGDAFAVVKPMPMDIGPGREIFQHGQSLYVEDLALRYPQSSQLLALDAKAYVGIPFPGPNGLP 381
Cdd:COG5001    5 AALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 382 LGQLTLLLATPLADPAPLLDVLYEQRERAASELQRLANDDALRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASE 461
Cdd:COG5001   85 LLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLAL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 462 EMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKETA 541
Cdd:COG5001  165 LLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAE 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 542 RHIERLAYYDDLCDLYNRRSLTDIMQRTLQAP--SGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENL 619
Cdd:COG5001  245 ERLRHLAYHDPLTGLPNRRLFLDRLEQALARArrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGD 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 620 VLARTSGDEFALLFTALGQgyiTAKilAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVH 699
Cdd:COG5001  325 TVARLGGDEFAVLLPDLDD---PED--AEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMY 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 700 MAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPI 779
Cdd:COG5001  400 RAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPL 479
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 780 AEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENR 859
Cdd:COG5001  480 AEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDP 559
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 860 LESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVE 939
Cdd:COG5001  560 EEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVE 639
                        650       660       670
                 ....*....|....*....|....*....|....*....
gi 780222879 940 EEEQLAVLKALGCQHYQGFLTSRPLPVKALESLLGATPA 978
Cdd:COG5001  640 TEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
399-973 7.46e-111

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: 354.48  E-value: 7.46e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 399 LLDVLYEQRERAASELQRLANDDALRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGD 478
Cdd:COG2200    6 ALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLAL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 479 TLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKETARHIERLAYYDDLCDLYN 558
Cdd:COG2200   86 LLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 559 R--RSLTDIMQRTLQAPSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLFTAL 636
Cdd:COG2200  166 RllLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 637 GqgyitAKILAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMAKRAGQGNHIFFSEAM 716
Cdd:COG2200  246 A-----AAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 717 AEKEKsKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKT 796
Cdd:COG2200  321 ARARR-RLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLER 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 797 ACAQYSFWLNNGLAIPhLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLI 876
Cdd:COG2200  400 ALRQLARWPERGLDLR-LSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 877 SIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQ 956
Cdd:COG2200  479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558
                        570
                 ....*....|....*..
gi 780222879 957 GFLTSRPLPVKALESLL 973
Cdd:COG2200  559 GYLFGRPLPLEELEALL 575
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
528-978 6.18e-104

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 338.58  E-value: 6.18e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 528 VCSFHDITQEKETARHIERLAYYDDLCDLYNRRSLTDIMQRTLQAPSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAV 607
Cdd:PRK10060 217 ICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 608 VVRLKSLPQENLVLARTSGDEFALLFTALGQGyitakiLAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDH 687
Cdd:PRK10060 297 SLAILSCLEEDQTLARLGGDEFLVLASHTSQA------ALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDS 370
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 688 LVLMQQADTAVHMAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPqyRVD-NGTLSGIEALLRWQKA 766
Cdd:PRK10060 371 ESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQP--KITwRGEVRSLEALVRWQSP 448
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 767 DGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNNGLAIpHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRL 846
Cdd:PRK10060 449 ERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINL-RVAVNVSARQLADQTIFTALKQALQELNFEYCPI 527
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 847 LLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLA 926
Cdd:PRK10060 528 DVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVA 607
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 780222879 927 RVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKALESLLGATPA 978
Cdd:PRK10060 608 QALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYLK 659
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
728-966 1.23e-103

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: 322.96  E-value: 1.23e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 728 NQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNN 807
Cdd:cd01948    1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 808 GLAIpHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSS 887
Cdd:cd01948   81 GPDL-RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879 888 LAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPV 966
Cdd:cd01948  160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
523-965 2.47e-99

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 330.19  E-value: 2.47e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 523 EISHFVCSFHdITQEkETARHIERLAYYDDLCDLYNR----RSLTDIMQRTLQApsgqwgALLLLDLDNFKSINDSLGHA 598
Cdd:PRK11359 353 DISQHLAALA-LEQE-KSRQHIEQLIQFDPLTGLPNRnnlhNYLDDLVDKAVSP------VVYLIGVDHFQDVIDSLGYA 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 599 CGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLFTALGQGYITakilaeHFARELMGIFRAPFDIGDHKLHCSASVGIS 678
Cdd:PRK11359 425 WADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNIT------QIADELRNVVSKPIMIDDKPFPLTLSIGIS 498
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 679 LFSDDDKDHLvlMQQADTAVHMAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIE 758
Cdd:PRK11359 499 YDVGKNRDYL--LSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIE 576
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 759 ALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPHLSVNVSARQFHTAGFVQQVEYILRD 838
Cdd:PRK11359 577 ALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQA 656
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 839 TGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAI 918
Cdd:PRK11359 657 WGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILAL 736
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 780222879 919 VKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLP 965
Cdd:PRK11359 737 LEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLP 783
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
728-966 1.97e-90

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 287.96  E-value: 1.97e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879   728 NQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNN 807
Cdd:smart00052   2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879   808 GLAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSS 887
Cdd:smart00052  82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879   888 LAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPV 966
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
728-963 1.05e-79

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: 258.79  E-value: 1.05e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  728 NQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNN 807
Cdd:pfam00563   2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  808 glAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSS 887
Cdd:pfam00563  82 --PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780222879  888 LAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRP 963
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
724-978 5.01e-73

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: 250.99  E-value: 5.01e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 724 LSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSF 803
Cdd:COG4943  270 LSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGD 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 804 WL--NNGLaipHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVvLENRLESIARIRQLKALGLLISIDDF 881
Cdd:COG4943  350 LLaaDPDF---HISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERG-FIDPAKARAVIAALREAGHRIAIDDF 425
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 882 GTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTS 961
Cdd:COG4943  426 GTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFA 505
                        250
                 ....*....|....*..
gi 780222879 962 RPLPVKALESLLGATPA 978
Cdd:COG4943  506 KPLPAEEFIAWLAAQRA 522
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
521-970 3.11e-72

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 251.94  E-value: 3.11e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 521 EEEISHFVCSFhDITQEKETARHIE--RLAYYDDLCDLYNRRSLTDIMQRTLQapSGQWGALLLLDLDNFKSINDSLGHA 598
Cdd:PRK13561 203 DDEIGMLVRSY-NLNQQLLQRQYEEqsRNATRFPVSDLPNKALLMALLEQVVA--RKQTTALMIITCETLRDTAGVLKEA 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 599 CGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLftalgqgyitAKILAEHF-----ARELMGIFRAPFDIGDHKLHCSA 673
Cdd:PRK13561 280 QREILLLTLVEKLKSVLSPRMVLAQISGYDFAII----------ANGVKEPWhaitlGQQVLTIINERLPIQRIQLRPSC 349
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 674 SVGISLFsDDDKDHLVLMQQADTAVHMAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGT 753
Cdd:PRK13561 350 SIGIAMF-YGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGK 428
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 754 LSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPhLSVNVSARQFHTAGFVQQVE 833
Cdd:PRK13561 429 LVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLP-LSVNLSALQLMHPNMVADML 507
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 834 YILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSSLAYL---RDLPADEVKLDRSFIQTLv 910
Cdd:PRK13561 508 ELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGL- 586
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 911 hsEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKALE 970
Cdd:PRK13561 587 --PEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFE 644
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
550-971 1.63e-69

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 244.85  E-value: 1.63e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 550 YDDLCDLYNRRSLTDIMQRTL------QAPSGQWGA----LLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENL 619
Cdd:PRK11829 225 YADMGRISHRFPVTELPNRSLfislleKEIASSTRTdhfhLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSD 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 620 VLARTSGDEFALLftalgQGYITAKILAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVH 699
Cdd:PRK11829 305 LLAQLSKTEFAVL-----ARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMM 379
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 700 MAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPI 779
Cdd:PRK11829 380 AAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHF 459
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 780 AEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPhLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENR 859
Cdd:PRK11829 460 AEEEGMMVPLGNWVLEEACRILADWKARGVSLP-LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDL 538
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 860 LESIARIRQLKALGLLISIDDFGTGYSSLAYLR---DLPADEVKLDRSFIQTLvhsEQDKAIVKAILDLARVFRFTVTAE 936
Cdd:PRK11829 539 DEALRLLRELQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAE 615
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 780222879 937 GVEEEEQLAVLKALGCQHYQGFLTSRPLPVKALES 971
Cdd:PRK11829 616 GVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEFEA 650
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
434-975 5.63e-58

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 217.23  E-value: 5.63e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  434 DGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDT--LKEEVIAA-VNRQGYWLGEEQCLH-REGHLFP 509
Cdd:PRK09776  547 EAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVLHITFGDNgpLMENIYSClTSRSAAYLEQDVVLHcRSGGSYD 626
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  510 VRLMVSGVKDEEEEISHFVCSFHDITQEKETARHIERLAYYDDLCDLYNRRSLTDIMQRTLQAPS--GQWGALLLLDLDN 587
Cdd:PRK09776  627 VHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNstHQRHALVFIDLDR 706
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  588 FKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLF--------TALGQGYITAkILAEHFARElmgiFR 659
Cdd:PRK09776  707 FKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLpdcnvesaRFIATRIISA-INDYHFPWE----GR 781
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  660 ApFDIGdhklhcsASVGISLFSDDDKDHLVLMQQADTAVHMAKRAGQGNHIF--FSEAMAEKEKSKLSLNNQLRDALRNN 737
Cdd:PRK09776  782 V-YRVG-------ASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVyePQQAAAHSEHRALSLAEQWRMIKENQ 853
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  738 ELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWL-NNGLAIphlSV 816
Cdd:PRK09776  854 LMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVaSKGLSI---AL 930
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  817 NVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPA 896
Cdd:PRK09776  931 PLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMA 1010
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  897 DEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKA-LESLLGA 975
Cdd:PRK09776 1011 DYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLlLNSSYFA 1090
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
549-705 8.71e-42

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: 150.01  E-value: 8.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 549 YYDDLCDLYNRRSLTDIMQRTLQAP--SGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSG 626
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARArrSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879 627 DEFALLFTAlgqgyiTAKILAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMAKRAG 705
Cdd:cd01949   81 DEFAILLPG------TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSG 153
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
436-712 8.92e-41

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: 151.67  E-value: 8.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 436 LLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVS 515
Cdd:COG2199    2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 516 GVKDEEEEISHFVCSFHDITQEKETARHIERLAYYDDLCDLYNRRSLTDIMQRTLQ--APSGQWGALLLLDLDNFKSIND 593
Cdd:COG2199   82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELAraRREGRPLALLLIDLDHFKRIND 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 594 SLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLFTALGQGyiTAKILAEHFARElmgIFRAPFDIGDHKLHCSA 673
Cdd:COG2199  162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLE--EAEALAERLREA---LEQLPFELEGKELRVTV 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 780222879 674 SVGISLFSDDDKDHLVLMQQADTAVHMAKRAGQGNHIFF 712
Cdd:COG2199  237 SIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
546-712 2.13e-37

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 137.76  E-value: 2.13e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879   546 RLAYYDDLCDLYNRRSLTDIMQRTLQA--PSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLAR 623
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRaqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879   624 TSGDEFALLFTAlgqgyITAKIlAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMAKR 703
Cdd:smart00267  81 LGGDEFALLLPE-----TSLEE-AIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154

                   ....*....
gi 780222879   704 AGQGNHIFF 712
Cdd:smart00267 155 AGRNQVAVY 163
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
548-708 9.05e-37

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: 135.84  E-value: 9.05e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  548 AYYDDLCDLYNRRSLTDIMQRTLQ--APSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTS 625
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQraLREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  626 GDEFALLFTALGQGyiTAKILAEhFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMAKRAG 705
Cdd:pfam00990  81 GDEFAILLPETSLE--GAQELAE-RIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAG 157

                  ...
gi 780222879  706 QGN 708
Cdd:pfam00990 158 RNR 160
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
733-969 2.67e-33

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 135.50  E-value: 2.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 733 ALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTAcAQYSFWLNNGL-AI 811
Cdd:PRK10551 271 GIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELI-ARDAAELQKVLpVG 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 812 PHLSVNVSARQFHTAGFVQQVEYILrdTGVPPS--RLLLEITESVVLENRlESIARIRQLKALGLLISIDDFGTGYSSLA 889
Cdd:PRK10551 350 AKLGINISPAHLHSDSFKADVQRLL--ASLPADhfQIVLEITERDMVQEE-EATKLFAWLHSQGIEIAIDDFGTGHSALI 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 890 YLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKAL 969
Cdd:PRK10551 427 YLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDF 506
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
547-707 4.94e-25

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: 102.42  E-value: 4.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  547 LAYYDDLCDLYNRRSLTDIMQRTLQ--APSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLART 624
Cdd:TIGR00254   1 QAVRDPLTGLYNRRYLEEMLDSELKraRRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  625 SGDEFALLF--TALGQgyitAKILAEhfaRELMGIFRAPFDI-GDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMA 701
Cdd:TIGR00254  81 GGEEFVVILpgTPLED----ALSKAE---RLRDAINSKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQA 153

                  ....*.
gi 780222879  702 KRAGQG 707
Cdd:TIGR00254 154 KKAGRN 159
PAS COG2202
PAS domain [Signal transduction mechanisms];
413-546 9.10e-22

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 95.86  E-value: 9.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 413 ELQRLANDDALRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQG 492
Cdd:COG2202    1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 780222879 493 YWLGEEQCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKETARHIER 546
Cdd:COG2202   81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRE 134
PRK09894 PRK09894
diguanylate cyclase; Provisional
550-714 1.88e-17

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 83.96  E-value: 1.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 550 YDDLCDLYNRRSLTDIMQRTLQAPSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEF 629
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEF 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 630 ALLF--TALGQGYITAKILaehfaRELmgIFRAPFDIGDHKLHCSASVGIS-LFSDDDKDhlVLMQQADTAVHMAKRAGQ 706
Cdd:PRK09894 211 IICLkaATDEEACRAGERI-----RQL--IANHAITHSDGRINITATFGVSrAFPEETLD--VVIGRADRAMYEGKQTGR 281

                 ....*...
gi 780222879 707 GNHIFFSE 714
Cdd:PRK09894 282 NRVMFIDE 289
pleD PRK09581
response regulator PleD; Reviewed
547-705 2.36e-17

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 86.11  E-value: 2.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 547 LAYYDDLCDLYNRRSLtDIMQRTLQAPSGQWG---ALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLAR 623
Cdd:PRK09581 291 MAVTDGLTGLHNRRYF-DMHLKNLIERANERGkplSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 624 TSGDEFALLF--TALGQGYITAKILAEHFARElmgifraPFDI--GDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVH 699
Cdd:PRK09581 370 YGGEEFVVVMpdTDIEDAIAVAERIRRKIAEE-------PFIIsdGKERLNVTVSIGVAELRPSGDTIEALIKRADKALY 442

                 ....*.
gi 780222879 700 MAKRAG 705
Cdd:PRK09581 443 EAKNTG 448
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
547-721 3.68e-13

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 73.51  E-value: 3.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 547 LAYYDDLCDLYNRRSLTDIMQR--TLQAPSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLART 624
Cdd:PRK15426 397 QAWHDPLTRLYNRGALFEKARAlaKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 625 SGDEFALLF--TALGQgyitAKILAEHFARELMG--IFRAPfdigDHKLHCSASVGIS-LFSDDDKDHLVLMQQADTAVH 699
Cdd:PRK15426 477 GGEEFCVVLpgASLAE----AAQVAERIRLRINEkeILVAK----STTIRISASLGVSsAEEDGDYDFEQLQSLADRRLY 548
                        170       180
                 ....*....|....*....|..
gi 780222879 700 MAKRAGQgNHIFFSEAMAEKEK 721
Cdd:PRK15426 549 LAKQAGR-NRVCASDNAHEREV 569
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
443-536 8.62e-13

PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 65.18  E-value: 8.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  443 GIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQgyWLGEEQCLHREGHLFPVRLMVSGVKDEEE 522
Cdd:pfam13426   2 GRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
                          90
                  ....*....|....
gi 780222879  523 EISHFVCSFHDITQ 536
Cdd:pfam13426  80 ELVGIIAILRDITE 93
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
424-548 1.81e-12

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 69.88  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 424 RLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPtyYGDTLKEEVIAAV-NRQGYWLGEEQCLH 502
Cdd:COG3852    8 LLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFP--EDSPLRELLERALaEGQPVTEREVTLRR 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 780222879 503 REGHLFPVRLMVSGVKDEEEEIsHFVCSFHDITQEKETARHIERLA 548
Cdd:COG3852   86 KDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERELRRAE 130
PAS COG2202
PAS domain [Signal transduction mechanisms];
406-544 2.51e-12

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 68.13  E-value: 2.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 406 QRERAASELQRLANddalRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEvI 485
Cdd:COG2202  124 ERKRAEEALRESEE----RLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLEL-L 198
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 486 AAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDE-EEEISHFVCSFHDITQEKETARHI 544
Cdd:COG2202  199 RRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRdGGEVIGVLGIVRDITERKRAEEAL 258
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
842-968 2.60e-12

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 69.83  E-value: 2.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 842 PPSRLLLEITESVVLENRLesIARIRQLKALGLLISIDDFGTGYSSLAYLRDlpADEVKLDrsfiqtlvHSEQDKAIVKA 921
Cdd:COG3434   82 PPERVVLEILEDVEPDEEL--LEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID--------VLALDLEELAE 149
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 780222879 922 ILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKA 968
Cdd:COG3434  150 LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
PRK09966 PRK09966
diguanylate cyclase DgcN;
517-679 2.69e-12

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 70.04  E-value: 2.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 517 VKDEE-EEISHFVCSFHDITQEKE------TARHIE--RLAYYDDLCDLYNR---RSLTDIMQRTLQAPSGQwgALLLLD 584
Cdd:PRK09966 208 VSEERiAEFHRFALDFNSLLDEMEewqlrlQAKNAQllRTALHDPLTGLANRaafRSGINTLMNNSDARKTS--ALLFLD 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 585 LDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLFTALGQGYITAKILAehfarELMGIFRAPFDI 664
Cdd:PRK09966 286 GDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICS-----ALTQIFNLPFDL 360
                        170
                 ....*....|....*.
gi 780222879 665 GD-HKLHCSASVGISL 679
Cdd:PRK09966 361 HNgHQTTMTLSIGYAM 376
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
431-542 9.41e-12

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: 63.08  E-value: 9.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  431 NTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKE--EVIAAVNRQGYWlGEEQCLHREGHLF 508
Cdd:TIGR00229  11 SSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVREriERRLEGEPEPVS-EERRVRRKDGSEI 89
                          90       100       110
                  ....*....|....*....|....*....|....
gi 780222879  509 PVRLMVSGVkDEEEEISHFVCSFHDITQEKETAR 542
Cdd:TIGR00229  90 WVEVSVSPI-RTNGGELGVVGIVRDITERKEAEE 122
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
431-534 1.02e-11

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: 62.43  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  431 NTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHRE-GHLFP 509
Cdd:pfam00989   9 SLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPdGRPRH 88
                          90       100
                  ....*....|....*....|....*
gi 780222879  510 VRLMVSGVKDEEEEISHFVCSFHDI 534
Cdd:pfam00989  89 VEVRASPVRDAGGEILGFLGVLRDI 113
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
432-534 2.24e-11

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: 61.50  E-value: 2.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 432 THDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVR 511
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                         90       100
                 ....*....|....*....|...
gi 780222879 512 LMVSGVKDEEEEISHFVCSFHDI 534
Cdd:cd00130   81 VSLTPIRDEGGEVIGLLGVVRDI 103
PRK11059 PRK11059
regulatory protein CsrD; Provisional
575-966 3.27e-11

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 67.19  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 575 GQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQE--NLVLARTSGDEFALLftaLGQgyITAKiLAEHFAR 652
Cdd:PRK11059 257 GAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRypGALLARYSRSDFAVL---LPH--RSLK-EADSLAS 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 653 ELMGIFRA----PFDIGDHKLHcsasVGISLFSDDDkDHLVLMQQADtavhMAKRAGQ---GNHIFFSEAMAEKEKSKLS 725
Cdd:PRK11059 331 QLLKAVDAlpppKMLDRDDFLH----IGICAYRSGQ-STEQVMEEAE----MALRSAQlqgGNGWFVYDKAQLPEKGRGS 401
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 726 LN--NQLRDALRNNELVLHYQPQYRVDnGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSF 803
Cdd:PRK11059 402 VRwrTLLEQTLVRGGPRLYQQPAVTRD-GKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRY 480
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 804 WLNNglaipHLSVNVSARQFHTAGFVQQveyiLRDT--GVPPS---RLLLEITESVVLEN--RLESIARIrqLKALGLLI 876
Cdd:PRK11059 481 WPEE-----NLSINLSVDSLLSRAFQRW----LRDTllQCPRSqrkRLIFELAEADVCQHisRLRPVLRM--LRGLGCRL 549
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 877 SIDDFGTGYSSLAYLRDLPADEVKLDRSFI---------QTLVHSeqdkaIVKAILDL-ARVFrftvtAEGVEEEEQLAV 946
Cdd:PRK11059 550 AVDQAGLTVVSTSYIKELNVELIKLHPSLVrnihkrtenQLFVRS-----LVGACAGTeTQVF-----ATGVESREEWQT 619
                        410       420
                 ....*....|....*....|
gi 780222879 947 LKALGCQHYQGFLTSRPLPV 966
Cdd:PRK11059 620 LQELGVSGGQGDFFAESQPL 639
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
421-548 8.96e-11

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: 65.38  E-value: 8.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 421 DALRLAEVAF-----NTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWL 495
Cdd:COG5809  134 EALRESEEKFrlifnHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQ 213
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 780222879 496 GEEQCLHREGHLFPVRLMVSGVKDEEEEIShFVCSFHDITQEKETA---RHIERLA 548
Cdd:COG5809  214 GEVRFWTKDGRWRLLEASGAPIKKNGEVDG-IVIIFRDITERKKLEellRKSEKLS 268
adrA PRK10245
diguanylate cyclase AdrA; Provisional
530-707 9.13e-09

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 58.69  E-value: 9.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 530 SFHDITQEKETARHIERLAYYDDLCDLYNRRSLTDIMQRTLQAPSGQW--GALLLLDLDNFKSINDSLGHACGDLLLQAV 607
Cdd:PRK10245 187 SYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHrdATLLIIDIDHFKSINDTWGHDVGDEAIVAL 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 608 VVRLKSLPQENLVLARTSGDEFALLFTALGQGYITAKILAEHfarELMGIFRAPfdiGDHKLHCSASVGISLFSDDDKDH 687
Cdd:PRK10245 267 TRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVH---EGLNTLRLP---NAPQVTLRISVGVAPLNPQMSHY 340
                        170       180
                 ....*....|....*....|
gi 780222879 688 LVLMQQADTAVHMAKRAGQG 707
Cdd:PRK10245 341 REWLKSADLALYKAKNAGRN 360
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
424-539 5.54e-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: 56.52  E-value: 5.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 424 RLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKE--EVIAAVNRQGYWlgEEQCL 501
Cdd:COG5809   16 RFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREilKLLKEGESRDEL--EFELR 93
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 780222879 502 HREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKE 539
Cdd:COG5809   94 HKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKR 131
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
742-972 1.48e-07

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 53.85  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 742 HYQPQYRVdNGTLSGIEALLRWQKAD--GTMVPPGEF---IPIAEETTLIQE----IGYWvmktacaqYSFWLNNGLAIp 812
Cdd:PRK11596  33 TFQPIYRT-SGRLMAIELLTAVTHPSnpSQRLSPERYfaeITVSHRLDVVKEqldlLAQW--------ADFFVRHGLLA- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 813 hlSVNVSARQFHTagfVQQVEYILRDTGVPPsRLLLEITESVVLENRlESIARIRQLKALGLlisiDDFGTGYSSLAYLR 892
Cdd:PRK11596 103 --SVNIDGPTLIA---LRQQPAILRLIERLP-WLRFELVEHIRLPKD-SPFASMCEFGPLWL----DDFGTGMANFSALS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 893 DLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKALESL 972
Cdd:PRK11596 172 EVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETLETL 251
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
431-571 1.50e-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: 55.16  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 431 NTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALrptyygdtLKEEVIAAVNRQG-YWLGEEQCLHREGhlfp 509
Cdd:COG3829   19 SLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTEL--------IPNSPLLEVLKTGkPVTGVIQKTGGKG---- 86
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879 510 VRLMVSGVK-DEEEEISHFVCSFHDITQEKETARHIERLAYYDDLCDLYnrrSLTDI------MQRTLQ 571
Cdd:COG3829   87 KTVIVTAIPiFEDGEVIGAVETFRDITELKRLERKLREEELERGLSAKY---TFDDIigkspaMKELLE 152
PRK13560 PRK13560
hypothetical protein; Provisional
406-542 2.54e-05

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 48.13  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 406 QRERAASELqrlanDDALR-LAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEV 484
Cdd:PRK13560 191 ERKRAEERI-----DEALHfLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYQEAD 265
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 485 IAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVK--DEEEEISHFVCSFHDITQEKETAR 542
Cdd:PRK13560 266 AAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHAEfdDKENHCAGLVGAITDISGRRAAER 325
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
411-548 2.75e-05

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 48.04  E-value: 2.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 411 ASELQRLANDDALRLAEVAfnthDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPT------YYGDTLKE-- 482
Cdd:PRK11360 254 AQALRETRSLNELILESIA----DGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPntpfasPLLDTLEHgt 329
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 780222879 483 EVIAAvnrqgywlgEEQCLHREGHLfpvRLMVSG--VKDEEEEISHFVCSFHDITQEKETARHI---ERLA 548
Cdd:PRK11360 330 EHVDL---------EISFPGRDRTI---ELSVSTslLHNTHGEMIGALVIFSDLTERKRLQRRVarqERLA 388
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
424-489 3.54e-05

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: 42.39  E-value: 3.54e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780222879   424 RLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVN 489
Cdd:smart00091   2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
580-635 4.25e-05

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: 44.27  E-value: 4.25e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 780222879 580 LLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVL-ARTSGDEFALLFTA 635
Cdd:cd07556    4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLkIKTIGDEFMVVSGL 60
PRK13558 PRK13558
bacterio-opsin activator; Provisional
445-568 1.75e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 45.60  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 445 ILKVNASFSRITGFASEEMLGLHIDALRptyyGDTLKEEVIAAVNRQgywLGEEQCL-------HREGHLFPVRLMVSGV 517
Cdd:PRK13558 173 LIYINDAFERITGYSPDEVLGRNCRFLQ----GEDTNEERVAELREA---IDEERPTsvelrnyRKDGSTFWNQVDIAPI 245
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 780222879 518 KDEEEEISHFVCSFHDITQEKETARHIERlayyddlcdlyNRRSLTDIMQR 568
Cdd:PRK13558 246 RDEDGTVTHYVGFQTDVTERKEAELALQR-----------ERRKLQRLLER 285
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
446-548 3.10e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 44.66  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  446 LKVNASFSRITGFASEEMLGLHIDALrpTY----YGDTLKEEVIAAVNRQGYWLgEEQCLHREGHLFPVRLMVSGVKDEE 521
Cdd:PRK09776  306 LQVNKALCQFLGYSQEELRGLTFQQL--TWpedlNKDLQQVEKLLSGEINSYSM-EKRYYRRDGEVVWALLAVSLVRDTD 382
                          90       100
                  ....*....|....*....|....*..
gi 780222879  522 EEISHFVCSFHDITQEKETARHIERLA 548
Cdd:PRK09776  383 GTPLYFIAQIEDINELKRTEQVNERLM 409
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
445-529 8.75e-04

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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 39.24  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  445 ILKVNASFSRITGFASEEMLGL---HIDALRPtYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDEE 521
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKgesWLDLVHP-DDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79

                  ....*...
gi 780222879  522 EEISHFVC 529
Cdd:pfam08447  80 GKPVRVIG 87
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
499-537 2.79e-03

Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.


Pssm-ID: 197509  Cd Length: 43  Bit Score: 36.39  E-value: 2.79e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 780222879   499 QCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQE 537
Cdd:smart00086   5 RLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
122-253 5.89e-03

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 38.23  E-value: 5.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879  122 QQQYDAMLESLKECLGADRLILWHYQAHgalgGEQLTPVFTLGVDALGAIRGDSRYIRALRARGALSFSEAAHQPMLSQH 201
Cdd:pfam01590   3 EEILQTILEELRELLGADRCALYLPDAD----GLEYLPPGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPRFLDP 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 780222879  202 Y-YLADANVCSRLDGALLEQEKLIGVLSLeYAESTLISDDTLQLVRHCARLLG 253
Cdd:pfam01590  79 LlLLRNFGIRSLLAVPIIDDGELLGVLVL-HHPRPPFTEEELELLEVLADQVA 130
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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