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Conserved domains on  [gi|515630458|ref|WP_017063058|]
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MULTISPECIES: GGDEF and EAL domain-containing protein [Vibrio]

Protein Classification

GGDEF and EAL domain-containing protein( domain architecture ID 12983342)

GGDEF and EAL domain-containing protein with a PDC (PhoQ/DcuS/CitA) sensor domain 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 ...
 420-847 4.48e-163

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: 490.83  E-value: 4.48e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 420 HALQSQL----TYDSLTKLYSREGFIDA-----AKKHPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTL 490
Cdd:COG5001  241 KRAEERLrhlaYHDPLTGLPNRRLFLDRleqalARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 491 PSEYLLARTGGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIVnVSNLH--DITLLLRSSSIALS 568
Cdd:COG5001  321 REGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIA-LYPDDgaDAEELLRNADLAMY 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 569 NAKQD-KTSVCIYSLEMGKASRHRTKMLARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDE-GVISPLEFIPL 646
Cdd:COG5001  400 RAKAAgRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPErGLVSPAEFIPL 479

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 647 AEESGLIDDIGKQILHKSCRDTAiaiesgKWSK----DFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITES 722
Cdd:COG5001  480 AEETGLIVPLGEWVLREACRQLA------AWQDaglpDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITES 553

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 723 RIVDNDPTIIDNMLTLKALGISIAIDDFGTGYSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSL 802
Cdd:COG5001  554 ALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEV 633

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 515630458 803 VAEGVETQQQAELLKQLQCPLAQGFLYSRPVPFDQWPTDLINSKQ 847
Cdd:COG5001  634 VAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
PRK15426 super family cl36488
cellulose biosynthesis regulator YedQ;
156-547 6.65e-18

cellulose biosynthesis regulator YedQ;


The actual alignment was detected with superfamily member PRK15426:

Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 88.15  E-value: 6.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 156 DIRSVISGYDprIRPWYTPIATQKKP----LWSPIYAN--ADERQEITLSAlaPIYDDNEFKAVVVSDIKINTFNAFLRK 229
Cdd:PRK15426 194 DVPTRYYQYV--TQPWFIGQSQRRNPgrgvRWFTSQPDdaSNTEPQVTASV--PVDAGNYWYGVLAMDIPVRSLQQFLRN 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 230 -LKDRTDASVYIIDKQQRLVAHSgggsvvswgtgqtNKGQRKLATESAnpviRESASYVEQFHLiENLGEQRFsfsldNE 308
Cdd:PRK15426 270 aIDKDLDGEYQLYDSHLRLLTSS-------------APGVRTGNIFDP----RELALLARAMEH-DTRGGIRM-----GS 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 309 RYfnqitpyedehgLTW-----FIGVsipesnLLGELPENQrnswllglalsciGVIAgliAFNRATQPITSTADAAkrl 383
Cdd:PRK15426 327 RY------------VSWerldhFDGV------LVRVHTLRE-------------GVRG---DFGSISIALTLLWALF--- 369

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 384 akgdwdasmpktghiyeTSMLVESF---NEMTNNLKASFHALQSQLTYDSLTKLYSREGFIDAAKK-----HPDNEKGTL 455
Cdd:PRK15426 370 -----------------TAMLLISWyviRRMVSNMFVLQSSLQWQAWHDPLTRLYNRGALFEKARAlakrcQRDQQPFSV 432

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 456 YLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGGDEFAIYAPNvTQSDDVQLLTNRLLQTFASPFSME 535
Cdd:PRK15426 433 IQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPG-ASLAEAAQVAERIRLRINEKEILV 511

                        410
                 ....*....|....
gi 515630458 536 SESVVIK--VSMGI 547
Cdd:PRK15426 512 AKSTTIRisASLGV 525
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 62-220 5.21e-12

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


:

Pssm-ID: 350338  Cd Length: 139  Bit Score: 64.09  E-value: 5.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  62 FLEKPFHANLSLSHNIGYHHLYQAGNLSKVQDYIFYTFSDHytavPQLDAIGFGSEDGNYvgfrKEANKGYtlmvqdert 141
Cdd:cd12913    1 FLEEAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESN----PDILGVYVAFEPNAF----SDETGRF--------- 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515630458 142 ndqLVIYRGSKISEDIRSVISGYDPRIRPWYTPIATQKKPLWSPIYANADERQEITLSALAPIYDDNEFKAVVVSDIKI 220
Cdd:cd12913   64 ---APYWYRDDGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDEVGTGVLMITISVPIYDNGKFIGVVGVDISL 139
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 420-847 4.48e-163

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: 490.83  E-value: 4.48e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 420 HALQSQL----TYDSLTKLYSREGFIDA-----AKKHPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTL 490
Cdd:COG5001  241 KRAEERLrhlaYHDPLTGLPNRRLFLDRleqalARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 491 PSEYLLARTGGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIVnVSNLH--DITLLLRSSSIALS 568
Cdd:COG5001  321 REGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIA-LYPDDgaDAEELLRNADLAMY 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 569 NAKQD-KTSVCIYSLEMGKASRHRTKMLARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDE-GVISPLEFIPL 646
Cdd:COG5001  400 RAKAAgRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPErGLVSPAEFIPL 479

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 647 AEESGLIDDIGKQILHKSCRDTAiaiesgKWSK----DFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITES 722
Cdd:COG5001  480 AEETGLIVPLGEWVLREACRQLA------AWQDaglpDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITES 553

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 723 RIVDNDPTIIDNMLTLKALGISIAIDDFGTGYSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSL 802
Cdd:COG5001  554 ALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEV 633

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 515630458 803 VAEGVETQQQAELLKQLQCPLAQGFLYSRPVPFDQWPTDLINSKQ 847
Cdd:COG5001  634 VAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 596-837 1.01e-101

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: 315.25  E-value: 1.01e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 596 ARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDE-GVISPLEFIPLAEESGLIDDIGKQILHKSCRDTAiaiES 674
Cdd:cd01948    1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEgGLISPAEFIPLAEETGLIVELGRWVLEEACRQLA---RW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 675 GKWSKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGY 754
Cdd:cd01948   78 QAGGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 755 SSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRPVP 834
Cdd:cd01948  158 SSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237


                 ...
gi 515630458 835 FDQ 837
Cdd:cd01948  238 AEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 597-837 3.13e-86

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 274.48  E-value: 3.13e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458   597 RMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDE-GVISPLEFIPLAEESGLIDDIGKQILHKSCRDTAIAIESG 675
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEgGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458   676 kwSKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGYS 755
Cdd:smart00052  83 --PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458   756 SLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRPVPF 835
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240


                   ..
gi 515630458   836 DQ 837
Cdd:smart00052 241 DD 242
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
429-838 6.19e-82

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 276.95  E-value: 6.19e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 429 DSLTKLYSREG---FIDAA-KKHPDNEKGTLYLiGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGGDEF 504
Cdd:PRK10060 240 DSITGLPNRNAiqeLIDHAiNAADNNQVGIVYL-DLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 505 AIYAPNVTQSDdVQLLTNRLLQTFASPFSMESESVVIKVSMGIVnVSNLH--DITLLLRSSSIALSNAKQD-KTSVCIYS 581
Cdd:PRK10060 319 LVLASHTSQAA-LEAMASRILTRLRLPFRIGLIEVYTGCSIGIA-LAPEHgdDSESLIRSADTAMYTAKEGgRGQFCVFS 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 582 LEMGKASRHRTKMLARMNRAIELQQFEPFYQPIIDLeSGSTIGAEALARWITDE-GVISPLEFIPLAEESGLIDDIGKQI 660
Cdd:PRK10060 397 PEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPErGLIPPLEFISYAEESGLIVPLGRWV 475

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 661 LHKSCRDTAiaiesgKWSK---DFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLT 737
Cdd:PRK10060 476 MLDVVRQVA------KWRDkgiNLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQ 549

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 738 LKALGISIAIDDFGTGYSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLK 817
Cdd:PRK10060 550 FSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLT 629

                        410       420
                 ....*....|....*....|....
gi 515630458 818 QLQCPLAQGFLYSRPVP---FDQW 838
Cdd:PRK10060 630 KNGVNERQGFLFAKPMPavaFERW 653
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 599-832 8.28e-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: 254.55  E-value: 8.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  599 NRAIELQQFEPFYQPIIDLESGSTIGAEALARWIT-DEGVISPLEFIPLAEESGLIDDIGKQILHKSCRDTAiaieSGKW 677
Cdd:pfam00563   5 RRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA----QLQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  678 SKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGYSSL 757
Cdd:pfam00563  81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515630458  758 AYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRP 832
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 425-572 4.37e-18

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: 82.38  E-value: 4.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  425 QLTYDSLTKLYSR---EGFID--AAKKHPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLART 499
Cdd:TIGR00254   1 QAVRDPLTGLYNRrylEEMLDseLKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515630458  500 GGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSM-ESESVVIKVSMGIVNVSNlHDITL--LLRSSSIALSNAKQ 572
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVaGSETLTVTVSIGVACYPG-HGLTLeeLLKRADEALYQAKK 155
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
156-547 6.65e-18

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 88.15  E-value: 6.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 156 DIRSVISGYDprIRPWYTPIATQKKP----LWSPIYAN--ADERQEITLSAlaPIYDDNEFKAVVVSDIKINTFNAFLRK 229
Cdd:PRK15426 194 DVPTRYYQYV--TQPWFIGQSQRRNPgrgvRWFTSQPDdaSNTEPQVTASV--PVDAGNYWYGVLAMDIPVRSLQQFLRN 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 230 -LKDRTDASVYIIDKQQRLVAHSgggsvvswgtgqtNKGQRKLATESAnpviRESASYVEQFHLiENLGEQRFsfsldNE 308
Cdd:PRK15426 270 aIDKDLDGEYQLYDSHLRLLTSS-------------APGVRTGNIFDP----RELALLARAMEH-DTRGGIRM-----GS 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 309 RYfnqitpyedehgLTW-----FIGVsipesnLLGELPENQrnswllglalsciGVIAgliAFNRATQPITSTADAAkrl 383
Cdd:PRK15426 327 RY------------VSWerldhFDGV------LVRVHTLRE-------------GVRG---DFGSISIALTLLWALF--- 369

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 384 akgdwdasmpktghiyeTSMLVESF---NEMTNNLKASFHALQSQLTYDSLTKLYSREGFIDAAKK-----HPDNEKGTL 455
Cdd:PRK15426 370 -----------------TAMLLISWyviRRMVSNMFVLQSSLQWQAWHDPLTRLYNRGALFEKARAlakrcQRDQQPFSV 432

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 456 YLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGGDEFAIYAPNvTQSDDVQLLTNRLLQTFASPFSME 535
Cdd:PRK15426 433 IQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPG-ASLAEAAQVAERIRLRINEKEILV 511

                        410
                 ....*....|....
gi 515630458 536 SESVVIK--VSMGI 547
Cdd:PRK15426 512 AKSTTIRisASLGV 525
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 62-220 5.21e-12

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350338  Cd Length: 139  Bit Score: 64.09  E-value: 5.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  62 FLEKPFHANLSLSHNIGYHHLYQAGNLSKVQDYIFYTFSDHytavPQLDAIGFGSEDGNYvgfrKEANKGYtlmvqdert 141
Cdd:cd12913    1 FLEEAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESN----PDILGVYVAFEPNAF----SDETGRF--------- 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515630458 142 ndqLVIYRGSKISEDIRSVISGYDPRIRPWYTPIATQKKPLWSPIYANADERQEITLSALAPIYDDNEFKAVVVSDIKI 220
Cdd:cd12913   64 ---APYWYRDDGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDEVGTGVLMITISVPIYDNGKFIGVVGVDISL 139
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 153-297 1.46e-09

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 59.27  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  153 ISEDIRSVISGYDPRIRPWYT-PIATQKKPLWSPIYANAD-ERQEITLSALAPIYDD-NEFKAVVVSDIKINTFNAFLRK 229
Cdd:pfam02743  81 ASSDESPSYPGLDVSERPWYKeALKGGGGIIWVFSSPYPSsESGEPVLTIARPIYDDdGEVIGVLVADLDLDTLQELLSQ 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515630458  230 LKDRTDASVYIIDKQQRLVAHSGGGSVVSWGTGQTNKGQRKLATES---ANPVIRESASYVEQFHLIENLG 297
Cdd:pfam02743 161 IKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSLADALPGSgitEIAVDLDGEDYLVAYAPIPGTG 231
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 370-415 8.12e-06

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 43.59  E-value: 8.12e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 515630458 370 TQPITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTNNL 415
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSK-DEIGELARAFNQMAERL 45
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
367-419 1.70e-04

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 39.92  E-value: 1.70e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 515630458   367 NRATQPITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTNNLKASF 419
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGR-DEIGELARAFNEMADRLEETI 52
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
188-424 1.92e-03

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 41.93  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 188 ANADERQEITLSALAPIYDDNEFKAVVVSDIKINTFNAFLRKLKDRTDASVYIIDKQQRLVAHSGGGSVVSWGTGQTNKG 267
Cdd:COG0840   24 LLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAAL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 268 QRKLATESANPVIRESASYVEQFHLIENLGEQRFSFSLDNERYFNQITPYEDEHGLTWFIGVSIPESNLLGELPENQRNS 347
Cdd:COG0840  104 ALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALAL 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515630458 348 W-LLGLALSCIGVIAGLIAFNRATQPITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTNNLKASFHALQS 424
Cdd:COG0840  184 LaAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSK-DEIGQLADAFNRMIENLRELVGQVRE 260
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 420-847 4.48e-163

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: 490.83  E-value: 4.48e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 420 HALQSQL----TYDSLTKLYSREGFIDA-----AKKHPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTL 490
Cdd:COG5001  241 KRAEERLrhlaYHDPLTGLPNRRLFLDRleqalARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 491 PSEYLLARTGGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIVnVSNLH--DITLLLRSSSIALS 568
Cdd:COG5001  321 REGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIA-LYPDDgaDAEELLRNADLAMY 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 569 NAKQD-KTSVCIYSLEMGKASRHRTKMLARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDE-GVISPLEFIPL 646
Cdd:COG5001  400 RAKAAgRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPErGLVSPAEFIPL 479

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 647 AEESGLIDDIGKQILHKSCRDTAiaiesgKWSK----DFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITES 722
Cdd:COG5001  480 AEETGLIVPLGEWVLREACRQLA------AWQDaglpDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITES 553

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 723 RIVDNDPTIIDNMLTLKALGISIAIDDFGTGYSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSL 802
Cdd:COG5001  554 ALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEV 633

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 515630458 803 VAEGVETQQQAELLKQLQCPLAQGFLYSRPVPFDQWPTDLINSKQ 847
Cdd:COG5001  634 VAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 415-842 8.55e-112

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: 354.09  E-value: 8.55e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 415 LKASFHALQSQLTYDSLTKLYSREGFIDAAKKHPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEY 494
Cdd:COG2200  149 LLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLL 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 495 LLARTGGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIV-NVSNLHDITLLLRSSSIALSNAKQD 573
Cdd:COG2200  229 ALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAaAPDDGADAALLLAAAAAAAAAAAGG 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 574 KTSVCIYSLEMGKASRHRTKMLARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDE-GVISPLEFIPLAEESGL 652
Cdd:COG2200  309 GRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSGL 388

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 653 IDDIGKQILHKSCRDTAIAIESGKwskDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTII 732
Cdd:COG2200  389 IVELDRWVLERALRQLARWPERGL---DLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAI 465

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 733 DNMLTLKALGISIAIDDFGTGYSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQ 812
Cdd:COG2200  466 ELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQ 545

                        410       420       430
                 ....*....|....*....|....*....|
gi 515630458 813 AELLKQLQCPLAQGFLYSRPVPFDQWPTDL 842
Cdd:COG2200  546 LEALRELGCDYAQGYLFGRPLPLEELEALL 575
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 596-837 1.01e-101

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: 315.25  E-value: 1.01e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 596 ARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDE-GVISPLEFIPLAEESGLIDDIGKQILHKSCRDTAiaiES 674
Cdd:cd01948    1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEgGLISPAEFIPLAEETGLIVELGRWVLEEACRQLA---RW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 675 GKWSKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGY 754
Cdd:cd01948   78 QAGGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGY 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 755 SSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRPVP 834
Cdd:cd01948  158 SSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237


                 ...
gi 515630458 835 FDQ 837
Cdd:cd01948  238 AEE 240
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 597-837 3.13e-86

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 274.48  E-value: 3.13e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458   597 RMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDE-GVISPLEFIPLAEESGLIDDIGKQILHKSCRDTAIAIESG 675
Cdd:smart00052   3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEgGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458   676 kwSKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGYS 755
Cdd:smart00052  83 --PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458   756 SLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRPVPF 835
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240


                   ..
gi 515630458   836 DQ 837
Cdd:smart00052 241 DD 242
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
429-838 6.19e-82

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 276.95  E-value: 6.19e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 429 DSLTKLYSREG---FIDAA-KKHPDNEKGTLYLiGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGGDEF 504
Cdd:PRK10060 240 DSITGLPNRNAiqeLIDHAiNAADNNQVGIVYL-DLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 505 AIYAPNVTQSDdVQLLTNRLLQTFASPFSMESESVVIKVSMGIVnVSNLH--DITLLLRSSSIALSNAKQD-KTSVCIYS 581
Cdd:PRK10060 319 LVLASHTSQAA-LEAMASRILTRLRLPFRIGLIEVYTGCSIGIA-LAPEHgdDSESLIRSADTAMYTAKEGgRGQFCVFS 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 582 LEMGKASRHRTKMLARMNRAIELQQFEPFYQPIIDLeSGSTIGAEALARWITDE-GVISPLEFIPLAEESGLIDDIGKQI 660
Cdd:PRK10060 397 PEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPErGLIPPLEFISYAEESGLIVPLGRWV 475

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 661 LHKSCRDTAiaiesgKWSK---DFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLT 737
Cdd:PRK10060 476 MLDVVRQVA------KWRDkgiNLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQ 549

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 738 LKALGISIAIDDFGTGYSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLK 817
Cdd:PRK10060 550 FSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLT 629

                        410       420
                 ....*....|....*....|....
gi 515630458 818 QLQCPLAQGFLYSRPVP---FDQW 838
Cdd:PRK10060 630 KNGVNERQGFLFAKPMPavaFERW 653
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 588-837 2.16e-81

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: 271.79  E-value: 2.16e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 588 SRHRTKMLARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARW-ITDEGVISPLEFIPLAEESGLIDDIGKQILHKSCR 666
Cdd:COG4943  266 LRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWrDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFR 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 667 DTaiaiesGKW---SKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDnDPTIIDNMLTLKALGI 743
Cdd:COG4943  346 DL------GDLlaaDPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGH 418

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 744 SIAIDDFGTGYSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPL 823
Cdd:COG4943  419 RIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQY 498

                        250
                 ....*....|....
gi 515630458 824 AQGFLYSRPVPFDQ 837
Cdd:COG4943  499 GQGWLFAKPLPAEE 512
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 599-832 8.28e-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: 254.55  E-value: 8.28e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  599 NRAIELQQFEPFYQPIIDLESGSTIGAEALARWIT-DEGVISPLEFIPLAEESGLIDDIGKQILHKSCRDTAiaieSGKW 677
Cdd:pfam00563   5 RRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA----QLQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  678 SKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGYSSL 757
Cdd:pfam00563  81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515630458  758 AYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRP 832
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 428-839 6.22e-78

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 269.33  E-value: 6.22e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 428 YDSLTKLYSREGFIDAAKKHPDNEKG-TLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGGDEFAI 506
Cdd:PRK11359 378 FDPLTGLPNRNNLHNYLDDLVDKAVSpVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVL 457

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 507 YAPNvTQSDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIVNVSNLHDITLLLRSSSIALSNAKQDKTSVCIYSLEMGK 586
Cdd:PRK11359 458 VSLE-NDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDVGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNE 536

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 587 ASRHRTKMLARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDE-GVISPLEFIPLAEESGLIDDIGKQILHKSC 665
Cdd:PRK11359 537 MVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLhGHVPPSRFIPLAEEIGEIENIGRWVIAEAC 616

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 666 RDTAIaiesgkWsKDFSIH-----VNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLTLKA 740
Cdd:PRK11359 617 RQLAE------W-RSQNIHipalsVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRD 689

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 741 LGISIAIDDFGTGYSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQ 820
Cdd:PRK11359 690 MGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIH 769

                        410
                 ....*....|....*....
gi 515630458 821 CPLAQGFLYSRPVPFDQWP 839
Cdd:PRK11359 770 CRVIQGYFFSRPLPAEEIP 788
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 391-837 1.29e-63

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 226.13  E-value: 1.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 391 SMPKTGHIYETSMLVESFNEMTNNLKASFHALQSQLTYDSLTKLYSREGFIDAAKKH-PDNEKGTLYLIGIDRFRDINDS 469
Cdd:PRK13561 196 ALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVvARKQTTALMIITCETLRDTAGV 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 470 LGHYNGDQLLIIAAARLRGTLPSEYLLARTGGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIVN 549
Cdd:PRK13561 276 LKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAM 355

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 550 V-SNLHDITLLLRSSSIALSNAKQDKTSVCIYSLEMGKASRHRTKMLARMNRAIELQQFEPFYQPIIDLESGSTIGAEAL 628
Cdd:PRK13561 356 FyGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEAL 435

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 629 ARWITDEGVIS-PLEFIPLAEESGLIDDIGKQILHKSCRDTAIAIESGKwskDFSIHVNLSVDQLSESGFVEQVKGTLRD 707
Cdd:PRK13561 436 LRMQQPDGSWDlPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGI---MLPLSVNLSALQLMHPNMVADMLELLTR 512

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 708 TNLPASNLTLEITESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGYSSLAYLHK---LPFDCLKIDRSFVSKLDkenLD 784
Cdd:PRK13561 513 YRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFVDGLP---ED 589

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 515630458 785 SSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRPVPFDQ 837
Cdd:PRK13561 590 DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEI 642
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 400-834 5.71e-57

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 207.49  E-value: 5.71e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 400 ETSMLVESFNEMTNNLKASFHALQSQLTYDSLTKLYSREGFIDAAKKHPDNEKGT----LYLIGIDRFRDINDSLGHYNG 475
Cdd:PRK11829 206 ELGVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTdhfhLLVIGIETLQEVSGAMSEAQH 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 476 DQLLIIAAARL-RGTLPSEyLLARTGGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIVNVSNLH 554
Cdd:PRK11829 286 QQLLLTIVQRIeQCIDDSD-LLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQ 364

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 555 DIT-LLLRSSSIALSNAKQD-KTSVCIYSLEMGKASRHRTKMLARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWI 632
Cdd:PRK11829 365 DTAeSMMRNASTAMMAAHHEgRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWC 444

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 633 -TDEGVISPLEFIPLAEESGLIDDIGKQILHKSCRdtaIAIESGKWSKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLP 711
Cdd:PRK11829 445 qPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACR---ILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHID 521

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 712 ASNLTLEITESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGYSSLAYLH---KLPFDCLKIDRSFVSKLDkenLDSSIV 788
Cdd:PRK11829 522 PQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLP---EDDAIA 598

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 515630458 789 AAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRPVP 834
Cdd:PRK11829 599 RIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 421-836 1.61e-44

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 174.09  E-value: 1.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  421 ALQSQLTY----DSLTKLYSREGF-------IDAAKKHpdNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGT 489
Cdd:PRK09776  656 KMLRQLSYsashDALTHLANRASFekqlrrlLQTVNST--HQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSM 733

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  490 LPSEYLLARTGGDEFAIYAP--NVTQSDDVqllTNRLLQTFAS-PFSMESESVVIKVSMGI--VNVSNlHDITLLLRSSS 564
Cdd:PRK09776  734 LRSSDVLARLGGDEFGLLLPdcNVESARFI---ATRIISAINDyHFPWEGRVYRVGASAGItlIDANN-HQASEVMSQAD 809

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  565 IALSNAKQD-KTSVCIYSLEMGKASRHRTKML--ARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDEG-VISP 640
Cdd:PRK09776  810 IACYAAKNAgRGRVTVYEPQQAAAHSEHRALSlaEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGeIIDE 889

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  641 LEFIPLAEESGLIDDIGKQILHKSCRDTAIAIESgkwsKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEIT 720
Cdd:PRK09776  890 GAFRPAAEDPALMHALDRRVIHEFFRQAAKAVAS----KGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEIT 965

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  721 ESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGYSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKV 800
Cdd:PRK09776  966 ETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGM 1045

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 515630458  801 SLVAEGVETQQQAELLKQLQCPLAQGFLYSRPVPFD 836
Cdd:PRK09776 1046 KTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLD 1081
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
600-837 7.48e-38

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 148.99  E-value: 7.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 600 RAIELQQFEPFYQPIIDLESGSTIGAEALARWI-TDEGVISPLEFIPLAEESGLIDDIGKQILHKSCRDTAI---AIESG 675
Cdd:PRK10551 270 TGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRhPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAElqkVLPVG 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 676 KwskdfSIHVNLSVDQLSESGFVEQVKGTLrdTNLPASNLT--LEITESRIVDNDPTIiDNMLTLKALGISIAIDDFGTG 753
Cdd:PRK10551 350 A-----KLGINISPAHLHSDSFKADVQRLL--ASLPADHFQivLEITERDMVQEEEAT-KLFAWLHSQGIEIAIDDFGTG 421

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 754 YSSLAYLHKLPFDCLKIDRSFVSKLDKENLDSSIVAAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRPV 833
Cdd:PRK10551 422 HSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPL 501


                 ....
gi 515630458 834 PFDQ 837
Cdd:PRK10551 502 PLED 505
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 427-572 4.88e-35

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: 130.75  E-value: 4.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 427 TYDSLTKLYSREGFIDAAKK-----HPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGG 501
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERllaraRRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 515630458 502 DEFAIYAPNVTQsDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIVNVS-NLHDITLLLRSSSIALSNAKQ 572
Cdd:cd01949   81 DEFAILLPGTDL-EEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPeDGEDAEELLRRADEALYRAKR 151
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 323-580 1.28e-33

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: 130.48  E-value: 1.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 323 LTWFIGVSIPESNLLGELPENQRNSWLLGLALSCIGVIAGLIAFNRATQPITSTADAAKRLAKGDWDASMPKTGHIYETS 402
Cdd:COG2199   12 LLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 403 MLVESFNEMTNnLKASFHALQSQLTYDSLTKLYSREGFIDAAKKH-----PDNEKGTLYLIGIDRFRDINDSLGHYNGDQ 477
Cdd:COG2199   92 LLLLALEDITE-LRRLEERLRRLATHDPLTGLPNRRAFEERLERElararREGRPLALLLIDLDHFKRINDTYGHAAGDE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 478 LLIIAAARLRGTLPSEYLLARTGGDEFAIYAPNVTQsDDVQLLTNRLLQTFAS-PFSMESESVVIKVSMGIVNVSNLH-D 555
Cdd:COG2199  171 VLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDL-EEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGdS 249

                        250       260
                 ....*....|....*....|....*.
gi 515630458 556 ITLLLRSSSIALSNAKQD-KTSVCIY 580
Cdd:COG2199  250 AEELLRRADLALYRAKRAgRNRVVVY 275
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 428-574 1.11e-27

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: 109.65  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  428 YDSLTKLYSREGFIDAAKK-----HPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGGD 502
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQelqraLREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515630458  503 EFAIYAPNVT--QSDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIVNVSNLH-DITLLLRSSSIALSNAKQDK 574
Cdd:pfam00990  83 EFAILLPETSleGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGeDPEDLLKRADTALYQAKQAG 157
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 428-572 2.15e-27

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 108.87  E-value: 2.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458   428 YDSLTKLYSREGF-------IDAAKKHPDNekGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTG 500
Cdd:smart00267   5 RDPLTGLPNRRYFeeeleqeLQRAQRQGSP--FALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515630458   501 GDEFAIYAPNVTQSDDVQLLTnRLLQTFASPFSMESESVVIKVSMGIVNVSNLH-DITLLLRSSSIALSNAKQ 572
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAE-RILQQLREPIIIHGIPLYLTISIGVAAYPNPGeDAEDLLKRADTALYQAKK 154
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 425-572 4.37e-18

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: 82.38  E-value: 4.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  425 QLTYDSLTKLYSR---EGFID--AAKKHPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLART 499
Cdd:TIGR00254   1 QAVRDPLTGLYNRrylEEMLDseLKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515630458  500 GGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSM-ESESVVIKVSMGIVNVSNlHDITL--LLRSSSIALSNAKQ 572
Cdd:TIGR00254  81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVaGSETLTVTVSIGVACYPG-HGLTLeeLLKRADEALYQAKK 155
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
156-547 6.65e-18

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 88.15  E-value: 6.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 156 DIRSVISGYDprIRPWYTPIATQKKP----LWSPIYAN--ADERQEITLSAlaPIYDDNEFKAVVVSDIKINTFNAFLRK 229
Cdd:PRK15426 194 DVPTRYYQYV--TQPWFIGQSQRRNPgrgvRWFTSQPDdaSNTEPQVTASV--PVDAGNYWYGVLAMDIPVRSLQQFLRN 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 230 -LKDRTDASVYIIDKQQRLVAHSgggsvvswgtgqtNKGQRKLATESAnpviRESASYVEQFHLiENLGEQRFsfsldNE 308
Cdd:PRK15426 270 aIDKDLDGEYQLYDSHLRLLTSS-------------APGVRTGNIFDP----RELALLARAMEH-DTRGGIRM-----GS 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 309 RYfnqitpyedehgLTW-----FIGVsipesnLLGELPENQrnswllglalsciGVIAgliAFNRATQPITSTADAAkrl 383
Cdd:PRK15426 327 RY------------VSWerldhFDGV------LVRVHTLRE-------------GVRG---DFGSISIALTLLWALF--- 369

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 384 akgdwdasmpktghiyeTSMLVESF---NEMTNNLKASFHALQSQLTYDSLTKLYSREGFIDAAKK-----HPDNEKGTL 455
Cdd:PRK15426 370 -----------------TAMLLISWyviRRMVSNMFVLQSSLQWQAWHDPLTRLYNRGALFEKARAlakrcQRDQQPFSV 432

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 456 YLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGGDEFAIYAPNvTQSDDVQLLTNRLLQTFASPFSME 535
Cdd:PRK15426 433 IQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPG-ASLAEAAQVAERIRLRINEKEILV 511

                        410
                 ....*....|....
gi 515630458 536 SESVVIK--VSMGI 547
Cdd:PRK15426 512 AKSTTIRisASLGV 525
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 453-836 5.07e-16

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 82.22  E-value: 5.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 453 GTLYLIGIDRFRDINDSLGHYNGDQLLIiAAARLRGTLPSEY---LLARTGGDEFAIYAPNVTQSDDV----QLLtnRLL 525
Cdd:PRK11059 260 GVVMLIRLPDFDLLQEEWGESQVEELLF-ELINLLSTFVMRYpgaLLARYSRSDFAVLLPHRSLKEADslasQLL--KAV 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 526 QTFASPFSMESESVVikvSMGIVNVSNLHDITLLLRSSSIALSNAK-QDKTSVCIYS----LEMGKAS-RHRT---KMLA 596
Cdd:PRK11059 337 DALPPPKMLDRDDFL---HIGICAYRSGQSTEQVMEEAEMALRSAQlQGGNGWFVYDkaqlPEKGRGSvRWRTlleQTLV 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 597 RMNraielqqFEPFYQPIIDLEsGSTIGAEALARwITD--EGVISPLEFIPLAEESGLIDDIGKQILHKSCRDTaiaies 674
Cdd:PRK11059 414 RGG-------PRLYQQPAVTRD-GKVHHRELFCR-IRDgqGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLL------ 478

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 675 gKWSKDFSIHVNLSVDQLSESGFVEQVKGTLRDTNLP-ASNLTLEITESRIVDNdptiIDNMLT----LKALGISIAIDD 749
Cdd:PRK11059 479 -RYWPEENLSINLSVDSLLSRAFQRWLRDTLLQCPRSqRKRLIFELAEADVCQH----ISRLRPvlrmLRGLGCRLAVDQ 553

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 750 FGTGYSSLAYLHKLPFDCLKIDRSFVSKLDK--EN--LDSSIVAAIvnitKGFKVSLVAEGVETQQQAELLKQLQCPLAQ 825
Cdd:PRK11059 554 AGLTVVSTSYIKELNVELIKLHPSLVRNIHKrtENqlFVRSLVGAC----AGTETQVFATGVESREEWQTLQELGVSGGQ 629

                        410
                 ....*....|.
gi 515630458 826 GFLYSRPVPFD 836
Cdd:PRK11059 630 GDFFAESQPLD 640
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 710-834 2.71e-15

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 79.08  E-value: 2.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 710 LPASNLTLEITESriVDNDPTIIDNMLTLKALGISIAIDDFGtgySSLAYLHKLPF-DCLKIDrsfVSKLDKENLdssiv 788
Cdd:COG3434   81 LPPERVVLEILED--VEPDEELLEALKELKEKGYRIALDDFV---LDPEWDPLLPLaDIIKID---VLALDLEEL----- 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515630458 789 AAIVNITKGFKVSLVAEGVETQQQAELLKQLQCPLAQGFLYSRPVP 834
Cdd:COG3434  148 AELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
132-758 1.00e-13

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 75.15  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 132 YTLMVQDERTNDQLVIYRGSKISEDIRSVISGYDPRIRPWYTPIATQKKPLWSPIYANADERQEITLSALAPIYDDNEFK 211
Cdd:COG2770    4 LLLALLLLLLLLLLLLLLAGALLVLALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 212 AVVVSDIKINTFNAFLRKLKDRTDASVYIIDKQQRLVAHSGGGSVVSWGTGQTNKGQRKLATESANPVIRESASYVEQFH 291
Cdd:COG2770   84 LVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAA 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 292 LIENLGEQRFSFSLDNERYFNQITPYEDEHGLTWFIGVSIPESNLLGelpenQRNSWLLGLALSCIGVIAGLIAFNRATQ 371
Cdd:COG2770  164 LALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAA-----LLLLLLLALLALLLALLLALLLARRITR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 372 PITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTNNLKASFHALQSQ-------LTYDSLTKLYSREGFIDAA 444
Cdd:COG2770  239 PLRRLAEAARRIAAGDLDVRIPVSRK-DEIGELARAFNRMADSLRESIEEAEEEeelaeaeLARLLEALLELLLALLLLL 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 445 KKHPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGGDEFAIYAPNVTQSDDVQLLTNRL 524
Cdd:COG2770  318 LALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAA 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 525 LQTFASPFSMESESVVIKVSMGIVNVSNLHDITLLLRSSSIALSNAKQDKTSVCIYSLEMGKASRHRTKMLARMNRAIEL 604
Cdd:COG2770  398 LAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAA 477

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 605 QQFEPFYQPIIDLESGSTIGAEALARWITDEGVISPLEFIPLAEESGLIDDIGKQILHKSCRDTAIAIESGKWSKDFSIH 684
Cdd:COG2770  478 LLLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLA 557

                        570       580       590       600       610       620       630
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515630458 685 VNLSVDQLSESGFVEQVKGTLRDTNLPASNLTLEITESRIVDNDPTIIDNMLTLKALGISIAIDDFGTGYSSLA 758
Cdd:COG2770  558 LAAVEAAALLLAALLLAAVAALLELAALLLLLLAAAEALAALELELAAAAEAALAEAELLEVAAAAEAGAALLA 631
pleD PRK09581
response regulator PleD; Reviewed
 429-573 1.88e-13

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 73.40  E-value: 1.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 429 DSLTKLYSREGF-------IDAAKKHpdNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGG 501
Cdd:PRK09581 295 DGLTGLHNRRYFdmhlknlIERANER--GKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGG 372

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515630458 502 DEFAIYAPNVTQSDDVQlLTNRLLQTFA-SPFSMESESVVIKV--SMGIVNVSNLHD-ITLLLRSSSIALSNAKQD 573
Cdd:PRK09581 373 EEFVVVMPDTDIEDAIA-VAERIRRKIAeEPFIISDGKERLNVtvSIGVAELRPSGDtIEALIKRADKALYEAKNT 447
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 62-220 5.21e-12

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; Members of this subfamily display varying domain architectures but all contain double PDC (PhoQ/DcuS/CitA) sensor domains. This model represents the first PDC domain of Methyl-accepting chemotaxis proteins (MCPs), Histidine kinases (HKs), and other similar domains. Many members contain both HAMP (HK, Adenylyl cyclase, MCP, and Phosphatase) and MCP domains, which are signalling domains that interact with protein partners to relay a signal. MCPs are part of a transmembrane protein complex that controls bacterial chemotaxis. HK receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. In the case of HKs, signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses.


Pssm-ID: 350338  Cd Length: 139  Bit Score: 64.09  E-value: 5.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  62 FLEKPFHANLSLSHNIGYHHLYQAGNLSKVQDYIFYTFSDHytavPQLDAIGFGSEDGNYvgfrKEANKGYtlmvqdert 141
Cdd:cd12913    1 FLEEAESIAEQLASTLESLVSSGSLDRELLENLLKQVLESN----PDILGVYVAFEPNAF----SDETGRF--------- 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515630458 142 ndqLVIYRGSKISEDIRSVISGYDPRIRPWYTPIATQKKPLWSPIYANADERQEITLSALAPIYDDNEFKAVVVSDIKI 220
Cdd:cd12913   64 ---APYWYRDDGGIIDLDEPPDYDYRTRDWYKLAKETGKPVWTEPYIDEVGTGVLMITISVPIYDNGKFIGVVGVDISL 139
PRK09966 PRK09966
diguanylate cyclase DgcN;
398-546 2.08e-11

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 66.95  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 398 IYETSMLVESFNEMTNNLKA---SFHALQSQLT----YDSLTKLYSREGF---IDAAKKHPDNEKGT--LYLIGiDRFRD 465
Cdd:PRK09966 213 IAEFHRFALDFNSLLDEMEEwqlRLQAKNAQLLrtalHDPLTGLANRAAFrsgINTLMNNSDARKTSalLFLDG-DNFKY 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 466 INDSLGHYNGDQLLIIAAARLRGTLPSEYLLARTGGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSMES-ESVVIKVS 544
Cdd:PRK09966 292 INDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNgHQTTMTLS 371


                 ..
gi 515630458 545 MG 546
Cdd:PRK09966 372 IG 373
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 747-840 1.37e-10

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 62.71  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 747 IDDFGTGYSSLAYLHKLPFDCLKIDRS-FVSKLDKE---NLDSSIVAAIVNITKGfkvsLVAEGVETQQQAELLKQLQCP 822
Cdd:PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVARElFIMLRQSEegrNLFSQLLHLMNRYCRG----VIVEGVETPEEWRDVQRSPAF 232

                         90
                 ....*....|....*...
gi 515630458 823 LAQGFLYSRPVPFDQWPT 840
Cdd:PRK11596 233 AAQGYFLSRPAPFETLET 250
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 422-506 5.76e-10

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 62.15  E-value: 5.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 422 LQSQLTYDSLTKLYSREGF-------IDAAKKHpdNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSEY 494
Cdd:PRK10245 201 LQVMSTRDGMTGVYNRRHWetllrneFDNCRRH--HRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSD 278

                         90
                 ....*....|..
gi 515630458 495 LLARTGGDEFAI 506
Cdd:PRK10245 279 VIGRFGGDEFAV 290
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 153-297 1.46e-09

Cache domain; Double cache domain 1 covers the last three strands from the membrane distal PAS-like domain, the first two strands of the membrane proximal domain, and the connecting elements between the two domains. This domain when present in chemoreceptors recognize several signals such as proteinogenic amino acids, GABA, Histamine and polyamines, decanoic acid, Autoinducer-2, purine derivatives, quaternary amines, citrate and taurine, among others. When associated with histidine kinases, it recognizes C3/C4-dicarboxylic acids, Spermine, guanosine and Autoinducer-2 (Mantilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460673 [Multi-domain]  Cd Length: 237  Bit Score: 59.27  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  153 ISEDIRSVISGYDPRIRPWYT-PIATQKKPLWSPIYANAD-ERQEITLSALAPIYDD-NEFKAVVVSDIKINTFNAFLRK 229
Cdd:pfam02743  81 ASSDESPSYPGLDVSERPWYKeALKGGGGIIWVFSSPYPSsESGEPVLTIARPIYDDdGEVIGVLVADLDLDTLQELLSQ 160

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515630458  230 LKDRTDASVYIIDKQQRLVAHSGGGSVVSWGTGQTNKGQRKLATES---ANPVIRESASYVEQFHLIENLG 297
Cdd:pfam02743 161 IKLGEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSLADALPGSgitEIAVDLDGEDYLVAYAPIPGTG 231
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 349-562 4.03e-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: 59.59  E-value: 4.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 349 LLGLALSCIGVIAGLIAF-------NRATQPITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTNNLKASFHA 421
Cdd:COG5000    6 LFLLLLLLIALLLLLLALwlalllaRRLTRPLRRLAEATRAVAAGDLSVRLPVTGD-DEIGELARAFNRMTDQLKEQREE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 422 LQSQLTYdsLTKLYSRegfIDAAkkhpdnekgtlyLIGID---RFRDINDSLGhyngdQLLIIAAARLRGTLPSEYLLAR 498
Cdd:COG5000   85 LEERRRY--LETILEN---LPAG------------VIVLDadgRITLANPAAE-----RLLGIPLEELIGKPLEELLPEL 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515630458 499 TGGDEFA-IYAPNVTQSDDVQLLTNRLLQTFASPFSMESESVVIkvsmgivnvsnlHDITLLLRS 562
Cdd:COG5000  143 DLAELLReALERGWQEEIELTRDGRRTLLVRASPLRDDGYVIVF------------DDITELLRA 195
PRK09894 PRK09894
diguanylate cyclase; Provisional
 381-572 4.20e-08

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 55.84  E-value: 4.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 381 KRLAKGDWdasmpkTGHIYETSM-LVESFNEMTNNLKASFHALQSqlTYDSLTKLYSREGF---IDAAKKHPDNEKGTLY 456
Cdd:PRK09894  91 LAIVEGHW------QDAHFDAFQeGLLSFTAALTDYKIYLLTIRS--NMDVLTGLPGRRVLdesFDHQLRNREPQNLYLA 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 457 LIGIDRFRDINDSLGHYNGDQLLIIAAARL-RGTLPSEYLLaRTGGDEFAIYAPNVTQSDDVQLLtNRLLQTFA-SPFSM 534
Cdd:PRK09894 163 LLDIDRFKLVNDTYGHLIGDVVLRTLATYLaSWTRDYETVY-RYGGEEFIICLKAATDEEACRAG-ERIRQLIAnHAITH 240

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 515630458 535 ESESVVIKVSMGIVNVSNLHDITLLLRSSSIALSNAKQ 572
Cdd:PRK09894 241 SDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQ 278
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
 334-661 1.31e-07

Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 54.89  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 334 SNLLGELPENQRNSWLLGLALSCIGVIAGLIAFNRATQPITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTN 413
Cdd:COG3850  107 LLLLLAAAINRKLALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGR-DELGTLARAFNRMAD 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 414 NLKASFHALQSQLTyDSLTKLYSREGFIDAAKKHPDNEKGTLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLRGTLPSE 493
Cdd:COG3850  186 ELQELYAELEEEEE-LEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLE 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 494 YLLARTGGDEFAIYAPNVTQSDDVQLLTNRLLQTFASPFSMESESVVIKVSMGIVNVSNLHDITLLLRSSSIALSNAKQD 573
Cdd:COG3850  265 LLLALLLLLLASALLLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELA 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 574 KTSVCIYSLE-MGKASRHRTKMLARMNRAIELQQFEPFYQPIIDLESGSTIGAEALARWITDEGVISPLEFIPLAEESGL 652
Cdd:COG3850  345 SILALQAALEaAAAGAALAAAAAAAGLARALAQAGADAAEALGLLAEASEGAAGQGAGLVDVEGGVAGEGGLVVLIVSII 424


                 ....*....
gi 515630458 653 IDDIGKQIL 661
Cdd:COG3850  425 AGGEAIARG 433
HAMP cd06225
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ...
 370-415 8.12e-06

Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.


Pssm-ID: 381743 [Multi-domain]  Cd Length: 45  Bit Score: 43.59  E-value: 8.12e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 515630458 370 TQPITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTNNL 415
Cdd:cd06225    1 TRPLRRLTEAARRIAEGDLDVRVPVRSK-DEIGELARAFNQMAERL 45
HAMP pfam00672
HAMP domain;
367-417 4.08e-05

HAMP domain;


Pssm-ID: 459898 [Multi-domain]  Cd Length: 53  Bit Score: 41.84  E-value: 4.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 515630458  367 NRATQPITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTNNLKA 417
Cdd:pfam00672   4 RRILRPLRRLAEAARRIASGDLDVRLPVSGR-DEIGELARAFNQMAERLRE 53
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
 63-220 1.37e-04

first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase and similar domains; Histidine kinase (HK) receptors are part of two-component systems (TCS) in bacteria that play a critical role for sensing and adapting to environmental changes. Typically, HK receptors contain an extracellular sensing domain flanked by two transmembrane helices, an intracellular dimerization histidine phosphorylation domain (DHp), and a C-terminal kinase domain, with many variations on this theme. HK receptors in this family contain double PDC (PhoQ/DcuS/CitA) sensor domains. Signals detected by the sensor domain are transmitted through DHp to the kinase domain, resulting in the phosphorylation of a conserved histidine residue in DHp; phosphotransfer to a conserved aspartate in its cognate response regulator (RR) follows, which leads to the activation of genes for downstream cellular responses. The HK family includes not just histidine kinase receptors but also sensors for chemotaxis proteins and diguanylate cyclase receptors, implying a combinatorial molecular evolution.


Pssm-ID: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 42.55  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458  63 LEKPFHANLSLSHNIGYHHLYQAGNLSKVQDYIFYTFSDHytavPQLDAIGFGSEDGNYVGFrkeankgytlmvqdertn 142
Cdd:cd18773    1 LEEADLLLRSLASALEALAALGSADREELQALLRRLLERN----PEISGIYVVDADGRVVAS------------------ 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 143 dqlviyrgskiSEDIRSVISGYDPRIRPWYTPIATQKKPLWS-PIYANADERQEITLSalAPIYD-DNEFKAVVVSDIKI 220
Cdd:cd18773   59 -----------SDRDPGGGDDDDDRDRFWYQAAKATGKLVISePYISRVTGKPVITLS--RPIRDaDGRFIGVVGADIDL 125
HAMP smart00304
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
367-419 1.70e-04

HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;


Pssm-ID: 197640 [Multi-domain]  Cd Length: 53  Bit Score: 39.92  E-value: 1.70e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 515630458   367 NRATQPITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTNNLKASF 419
Cdd:smart00304   1 RRLLRPLRRLAEAAQRIADGDLTVRLPVDGR-DEIGELARAFNEMADRLEETI 52
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 495-551 5.22e-04

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: 41.82  E-value: 5.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 515630458 495 LLARTGGDEFAIYAPNvTQSDDVQLLTNRLLQTFASPfsmesESVVIKVSMGIVNVS 551
Cdd:COG3706  117 LVARYGGEEFAILLPG-TDLEGALAVAERIREAVAEL-----PSLRVTVSIGVAGDS 167
Tar COG0840
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
188-424 1.92e-03

Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];


Pssm-ID: 440602 [Multi-domain]  Cd Length: 533  Bit Score: 41.93  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 188 ANADERQEITLSALAPIYDDNEFKAVVVSDIKINTFNAFLRKLKDRTDASVYIIDKQQRLVAHSGGGSVVSWGTGQTNKG 267
Cdd:COG0840   24 LLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLLLLALLALALAAL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 268 QRKLATESANPVIRESASYVEQFHLIENLGEQRFSFSLDNERYFNQITPYEDEHGLTWFIGVSIPESNLLGELPENQRNS 347
Cdd:COG0840  104 ALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAALALAAAALALAL 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515630458 348 W-LLGLALSCIGVIAGLIAFNRATQPITSTADAAKRLAKGDWDASMPKTGHiYETSMLVESFNEMTNNLKASFHALQS 424
Cdd:COG0840  184 LaAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSK-DEIGQLADAFNRMIENLRELVGQVRE 260
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 454-547 7.72e-03

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: 37.34  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515630458 454 TLYLIGIDRFRDINDSLGHYNGDQLLIIAAARLR-GTLPSEYLLARTGGDEFAIYAPnVTQSDDVQLLTNRLLQTFASpf 532
Cdd:cd07556    3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDsLIRRSGDLKIKTIGDEFMVVSG-LDHPAAAVAFAEDMREAVSA-- 79

                         90
                 ....*....|....*
gi 515630458 533 SMESESVVIKVSMGI 547
Cdd:cd07556   80 LNQSEGNPVRVRIGI 94
 
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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