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Conserved domains on  [gi|1737075318|emb|VAC93189|]
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diguanylate cyclase/phosphodiesterase (GGDEF & EAL domains) with PAS/PAC sensor(s) [Klebsiella aerogenes]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 18-336 3.82e-77

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


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 249.69  E-value: 3.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  18 VEERIRFFSLSLAEMHRELQESISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIG 97
Cdd:COG5001    86 LAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  98 NNLGEMIVPEEFREQHARGLMRFQAAQPSNILNRTIEITALHRTKGKFPIELSIWPHQQSGKQIFSAFIRDITDRKQREQ 177
Cdd:COG5001   166 LLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEE 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 178 VVWLHANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDT 257
Cdd:COG5001   246 RLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDT 325

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737075318 258 VARLGGDEFIALLPDLKANDPLpRQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:COG5001   326 VARLGGDEFAVLLPDLDDPEDA-EAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKA 403
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 18-336 3.82e-77

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: 249.69  E-value: 3.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  18 VEERIRFFSLSLAEMHRELQESISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIG 97
Cdd:COG5001    86 LAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  98 NNLGEMIVPEEFREQHARGLMRFQAAQPSNILNRTIEITALHRTKGKFPIELSIWPHQQSGKQIFSAFIRDITDRKQREQ 177
Cdd:COG5001   166 LLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEE 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 178 VVWLHANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDT 257
Cdd:COG5001   246 RLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDT 325

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737075318 258 VARLGGDEFIALLPDLKANDPLpRQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:COG5001   326 VARLGGDEFAVLLPDLDDPEDA-EAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKA 403
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 184-336 2.11e-61

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: 193.54  E-value: 2.11e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 184 NFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGG 263
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737075318 264 DEFIALLPDLKANDPLprQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:cd01949    81 DEFAILLPGTDLEEAE--ALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKR 151
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 183-336 2.27e-52

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: 170.13  E-value: 2.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 183 ANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLG 262
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737075318 263 GDEFIALLPDlkANDPLPRQTAEKIS---NALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:pfam00990  81 GDEFAILLPE--TSLEGAQELAERIRrllAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQ 155
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 181-336 6.26e-52

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 169.35  E-value: 6.26e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  181 LHANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVAR 260
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737075318  261 LGGDEFIALLPDLKANDPLprQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:smart00267  81 LGGDEFALLLPETSLEEAI--ALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
41-337 1.21e-39

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 147.91  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  41 SEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPEEFREQHARGLMRF 120
Cdd:PRK10060   97 HDTPSVARDLSHGLSFAEQVVSEANSVIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKLFMSRREAAASRRNIRGF 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 121 QAAQPSNILNRTIEITALHRT---KGKFPielsiwpHQQSGK-QIFsaFI---RDITDRKQREQVVWLHANFDALTGLPN 193
Cdd:PRK10060  177 FRSGNAYEVERWIKTRKGQRLflfRNKFV-------HSGSGKnEIF--LIcsgTDITEERRAQERLRILANTDSITGLPN 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 194 RRLLSNRLELAITQAiaNETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDEFIALLPDl 273
Cdd:PRK10060  248 RNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASH- 324

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737075318 274 kANDPLPRQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKKG 337
Cdd:PRK10060  325 -TSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEG 387
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 186-336 5.61e-37

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


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 130.53  E-value: 5.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 186 DALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDE 265
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737075318 266 FIALLPDLKANDPLprQTAEKISNALTQSFLIHEH--VITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:TIGR00254  85 FVVILPGTPLEDAL--SKAERLRDAINSKPIEVAGseTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKK 155
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
169-335 7.28e-28

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 109.30  E-value: 7.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 169 ITDRKQ---REQVVWLH--ANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRL 243
Cdd:NF038266   75 ISDRYQrmmRDLNEALReaSTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVE 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 244 VAFRLQSVLREGDTVARLGGDEFIALLPDLKANDPLprQTAEKISNAL-TQSFLIHEHVITISGSIGIALFPHDAADADT 322
Cdd:NF038266  155 IARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQ--VVLERLREAVrALAVRVGDDVLSVTASAGLAEHRPPEEGLSA 232

                         170
                  ....*....|...
gi 1737075318 323 LLNSADKAMYSSK 335
Cdd:NF038266  233 TLSRADQALYQAK 245
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 18-336 3.82e-77

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: 249.69  E-value: 3.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  18 VEERIRFFSLSLAEMHRELQESISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIG 97
Cdd:COG5001    86 LAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  98 NNLGEMIVPEEFREQHARGLMRFQAAQPSNILNRTIEITALHRTKGKFPIELSIWPHQQSGKQIFSAFIRDITDRKQREQ 177
Cdd:COG5001   166 LLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEE 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 178 VVWLHANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDT 257
Cdd:COG5001   246 RLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDT 325

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737075318 258 VARLGGDEFIALLPDLKANDPLpRQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:COG5001   326 VARLGGDEFAVLLPDLDDPEDA-EAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKA 403
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 184-336 2.11e-61

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: 193.54  E-value: 2.11e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 184 NFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGG 263
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737075318 264 DEFIALLPDLKANDPLprQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:cd01949    81 DEFAILLPGTDLEEAE--ALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKR 151
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 78-336 2.33e-61

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: 197.51  E-value: 2.33e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  78 INWNQAAERMFGWSAGEAIGNNLGEMIVPEEFREQHARGLMRFQAAQPSNILNRTIEITALHRTKGKFPIELSIWPHQQS 157
Cdd:COG2199     9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 158 GKQIFSAFIRDITDRKQREQVVWLHANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVG 237
Cdd:COG2199    89 ALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 238 DELLRLVAFRLQSVLREGDTVARLGGDEFIALLPDLKANDplPRQTAEKISNALTQ-SFLIHEHVITISGSIGIALFPHD 316
Cdd:COG2199   169 DEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEE--AEALAERLREALEQlPFELEGKELRVTVSIGVALYPED 246

                         250       260
                  ....*....|....*....|
gi 1737075318 317 AADADTLLNSADKAMYSSKK 336
Cdd:COG2199   247 GDSAEELLRRADLALYRAKR 266
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 183-336 2.27e-52

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: 170.13  E-value: 2.27e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 183 ANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLG 262
Cdd:pfam00990   1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737075318 263 GDEFIALLPDlkANDPLPRQTAEKIS---NALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:pfam00990  81 GDEFAILLPE--TSLEGAQELAERIRrllAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQ 155
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 181-336 6.26e-52

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 169.35  E-value: 6.26e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  181 LHANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVAR 260
Cdd:smart00267   1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737075318  261 LGGDEFIALLPDLKANDPLprQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:smart00267  81 LGGDEFALLLPETSLEEAI--ALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
41-337 1.21e-39

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 147.91  E-value: 1.21e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  41 SEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPEEFREQHARGLMRF 120
Cdd:PRK10060   97 HDTPSVARDLSHGLSFAEQVVSEANSVIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKLFMSRREAAASRRNIRGF 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 121 QAAQPSNILNRTIEITALHRT---KGKFPielsiwpHQQSGK-QIFsaFI---RDITDRKQREQVVWLHANFDALTGLPN 193
Cdd:PRK10060  177 FRSGNAYEVERWIKTRKGQRLflfRNKFV-------HSGSGKnEIF--LIcsgTDITEERRAQERLRILANTDSITGLPN 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 194 RRLLSNRLELAITQAiaNETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDEFIALLPDl 273
Cdd:PRK10060  248 RNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASH- 324

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737075318 274 kANDPLPRQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKKG 337
Cdd:PRK10060  325 -TSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEG 387
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 40-335 4.30e-39

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 147.51  E-value: 4.30e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318   40 ISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEM--IVPEE---FREQHA 114
Cdd:PRK09776   521 MTEVRQLNEALFQEKERLHITLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVlhITFGDngpLMENIY 600

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  115 RGLMRFQAAQPSNilnrtiEITALHRTKGKFPIELSIWP-HQQSGKQIFSAF-IRDITD-RKQREQVVWlHANFDALTGL 191
Cdd:PRK09776   601 SCLTSRSAAYLEQ------DVVLHCRSGGSYDVHYSITPlSTLDGENIGSVLvIQDVTEsRKMLRQLSY-SASHDALTHL 673

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  192 PNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDEFIALLP 271
Cdd:PRK09776   674 ANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLP 753

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737075318  272 DlkANDPLPRQTAEKISNALTQ-SFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAMYSSK 335
Cdd:PRK09776   754 D--CNVESARFIATRIISAINDyHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAK 816
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 186-336 5.61e-37

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


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 130.53  E-value: 5.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 186 DALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDE 265
Cdd:TIGR00254   5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1737075318 266 FIALLPDLKANDPLprQTAEKISNALTQSFLIHEH--VITISGSIGIALFPHDAADADTLLNSADKAMYSSKK 336
Cdd:TIGR00254  85 FVVILPGTPLEDAL--SKAERLRDAINSKPIEVAGseTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKK 155
pleD PRK09581
response regulator PleD; Reviewed
 186-337 1.20e-31

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 123.47  E-value: 1.20e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 186 DALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDE 265
Cdd:PRK09581  295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737075318 266 FIALLPDLKANDPLprQTAEKISNALTQS-FLIH--EHVITISGSIGIALFPHDAADADTLLNSADKAMYSSKKG 337
Cdd:PRK09581  375 FVVVMPDTDIEDAI--AVAERIRRKIAEEpFIISdgKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNT 447
diguan_SiaD NF038266
biofilm regulation diguanylate cyclase SiaD;
169-335 7.28e-28

biofilm regulation diguanylate cyclase SiaD;


Pssm-ID: 468439 [Multi-domain]  Cd Length: 252  Bit Score: 109.30  E-value: 7.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 169 ITDRKQ---REQVVWLH--ANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRL 243
Cdd:NF038266   75 ISDRYQrmmRDLNEALReaSTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVE 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 244 VAFRLQSVLREGDTVARLGGDEFIALLPDLKANDPLprQTAEKISNAL-TQSFLIHEHVITISGSIGIALFPHDAADADT 322
Cdd:NF038266  155 IARTLRAELREYDLCGRWGGEEFLLLLPETGLEEAQ--VVLERLREAVrALAVRVGDDVLSVTASAGLAEHRPPEEGLSA 232

                         170
                  ....*....|...
gi 1737075318 323 LLNSADKAMYSSK 335
Cdd:NF038266  233 TLSRADQALYQAK 245
PRK09894 PRK09894
diguanylate cyclase; Provisional
 183-342 7.84e-26

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 104.76  E-value: 7.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 183 ANFDALTGLPNRRLLSNRLELAITQAiaNETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLG 262
Cdd:PRK09894  129 SNMDVLTGLPGRRVLDESFDHQLRNR--EPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYG 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 263 GDEFIALLPDlkANDPLPRQTAEKISNAL-TQSFLIHEHVITISGSIGIALFpHDAADADTLLNSADKAMYSSKKgTPRE 341
Cdd:PRK09894  207 GEEFIICLKA--ATDEEACRAGERIRQLIaNHAITHSDGRINITATFGVSRA-FPEETLDVVIGRADRAMYEGKQ-TGRN 282


                  .
gi 1737075318 342 R 342
Cdd:PRK09894  283 R 283
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
180-337 8.40e-24

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 102.02  E-value: 8.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 180 WLhANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVA 259
Cdd:PRK15426  396 WQ-AWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAG 474

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 260 RLGGDEFIALLPDLKANDplPRQTAEKISNALT-QSFLIHEHV-ITISGSIGIALFPHDAA-DADTLLNSADKAMYSSKK 336
Cdd:PRK15426  475 RVGGEEFCVVLPGASLAE--AAQVAERIRLRINeKEILVAKSTtIRISASLGVSSAEEDGDyDFEQLQSLADRRLYLAKQ 552


                  .
gi 1737075318 337 G 337
Cdd:PRK15426  553 A 553
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 169-337 1.16e-23

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 102.16  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 169 ITDRKQREQVVWLhANFDALTGLPNRRLLSNRLElaitQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRL 248
Cdd:PRK11359  363 LEQEKSRQHIEQL-IQFDPLTGLPNRNNLHNYLD----DLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRF 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 249 QSVLREGDTVARLGGDEFIALLPDLKANDplPRQTAEKISNALTQSFLIHEHVITISGSIGIAlfpHDAA-DADTLLNSA 327
Cdd:PRK11359  438 REKLKPDQYLCRIEGTQFVLVSLENDVSN--ITQIADELRNVVSKPIMIDDKPFPLTLSIGIS---YDVGkNRDYLLSTA 512

                         170
                  ....*....|.
gi 1737075318 328 DKAM-YSSKKG 337
Cdd:PRK11359  513 HNAMdYIRKNG 523
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 53-177 1.31e-21

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 88.50  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  53 SEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLgEMIVPEEFREQHARglmRFQAAQPSNILNRT 132
Cdd:TIGR00229   1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNV-LELIPEEDREEVRE---RIERRLEGEPEPVS 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1737075318 133 IEITALHRTKGKFPIELSIWPHQQSGKQI-FSAFIRDITDRKQREQ 177
Cdd:TIGR00229  77 EERRVRRKDGSEIWVEVSVSPIRTNGGELgVVGIVRDITERKEAEE 122
PAS COG2202
PAS domain [Signal transduction mechanisms];
47-267 8.52e-19

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 84.69  E-value: 8.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  47 QRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPEEFREQHARGLMRFQAAQPs 126
Cdd:COG2202     3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGV- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 127 nilnRTIEITALHRTKGKFPIELSIWPHQQSGKQI--FSAFIRDITDRKQREQVVWLHANFDALTGLPNRR-LLSNRLEL 203
Cdd:COG2202    82 ----WRGELRNRRKDGSLFWVELSISPVRDEDGEItgFVGIARDITERKRAEEALRESEERLRLLVENAPDgIFVLDLDG 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1737075318 204 AITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDEFI 267
Cdd:COG2202   158 RILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGR 221
PRK09966 PRK09966
diguanylate cyclase DgcN;
186-335 1.07e-18

diguanylate cyclase DgcN;


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 86.21  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 186 DALTGLPNRRLLSNRLELAITQAIANETEvALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDE 265
Cdd:PRK09966  251 DPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDE 329

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1737075318 266 FIALLPDLKANDPLPRqtaekISNALTQSF-----LIHEHVITISGSIGIALfPHDAADADTLLNSADKAMYSSK 335
Cdd:PRK09966  330 FAMVLYDVQSESEVQQ-----ICSALTQIFnlpfdLHNGHQTTMTLSIGYAM-TIEHASAEKLQELADHNMYQAK 398
PAS COG2202
PAS domain [Signal transduction mechanisms];
40-177 4.85e-18

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 82.38  E-value: 4.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  40 ISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPEEfreqHARGLMR 119
Cdd:COG2202   122 ITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPED----RERLLEL 197

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737075318 120 FQAAQPSNILNRTIEITALHRTKGKFPIELSIWPHQQSGKQI-FSAFIRDITDRKQREQ 177
Cdd:COG2202   198 LRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGGEVIgVLGIVRDITERKRAEE 256
adrA PRK10245
diguanylate cyclase AdrA; Provisional
 169-336 2.57e-16

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 79.10  E-value: 2.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 169 ITDRKQREQVVwlhANFDALTGLPNRR----LLSNRLELAITQaianETEVALLFIDLDRFKPVNDVYGHAVGDELLRLV 244
Cdd:PRK10245  194 LAEHKRRLQVM---STRDGMTGVYNRRhwetLLRNEFDNCRRH----HRDATLLIIDIDHFKSINDTWGHDVGDEAIVAL 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 245 AFRLQSVLREGDTVARLGGDEFIALLPDLKANdplprqtaekisNALTQSFLIHEHV----------ITISGSIGIALFP 314
Cdd:PRK10245  267 TRQLQITLRGSDVIGRFGGDEFAVIMSGTPAE------------SAITAMSRVHEGLntlrlpnapqVTLRISVGVAPLN 334

                         170       180
                  ....*....|....*....|..
gi 1737075318 315 HDAADADTLLNSADKAMYSSKK 336
Cdd:PRK10245  335 PQMSHYREWLKSADLALYKAKN 356
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
49-177 3.69e-16

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 78.35  E-value: 3.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  49 ALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEmIVPEEFREQHArglmrFQAAQPSNI 128
Cdd:COG3852     1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAE-LFPEDSPLREL-----LERALAEGQ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1737075318 129 LNRTIEITALHRTKGKFPIELSIWP-HQQSGKQIFSAFIRDITDRKQREQ 177
Cdd:COG3852    75 PVTEREVTLRRKDGEERPVDVSVSPlRDAEGEGGVLLVLRDITERKRLER 124
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 44-256 5.92e-15

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 75.40  E-value: 5.92e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  44 ESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPEEFREQHArgLMRFQAA 123
Cdd:COG5809     4 SKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELRE--ILKLLKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 124 QPSnilNRTIEITALHRTKGKFPIELSIWP--HQQSGKQIFSAFIRDITDRKQREQvvwlhanfdALtglpnrRLLSNRL 201
Cdd:COG5809    82 GES---RDELEFELRHKNGKRLEFSSKLSPifDQNGDIEGMLAISRDITERKRMEE---------AL------RESEEKF 143

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1737075318 202 ELaitqaIANETEVALLFIDLD-RFKPVNDVYGHAVGDELLRLVAFRLQSVLREGD 256
Cdd:COG5809   144 RL-----IFNHSPDGIIVTDLDgRIIYANPAACKLLGISIEELIGKSILELIHSDD 194
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 58-169 6.11e-15

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 70.14  E-value: 6.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  58 RQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPEEFREQHARGLMRFQAAQPSNILNRTIEITa 137
Cdd:pfam00989   4 RAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVP- 82

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1737075318 138 lhrTKGKFPIELSIWPHQQSGKQI--FSAFIRDI 169
Cdd:pfam00989  83 ---DGRPRHVEVRASPVRDAGGEIlgFLGVLRDI 113
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
 214-291 9.98e-12

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: 61.60  E-value: 9.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 214 EVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLRE-GDTVARLGGDEFIALLPdlkANDPLP-RQTAEKISNAL 291
Cdd:cd07556     1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSG---LDHPAAaVAFAEDMREAV 77
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 66-169 2.71e-11

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 59.57  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  66 DAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPE---EFREQHARGLmrfqaaqpSNILNRTIEITALHRTK 142
Cdd:cd00130     3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEdreELRERLENLL--------SGGEPVTLEVRLRRKDG 74

                          90       100
                  ....*....|....*....|....*....
gi 1737075318 143 GKFPIELSI--WPHQQSGKQIFSAFIRDI 169
Cdd:cd00130    75 SVIWVLVSLtpIRDEGGEVIGLLGVVRDI 103
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 40-177 4.90e-11

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 63.46  E-value: 4.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  40 ISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIvPEEFREQHARGLMr 119
Cdd:COG5809   126 ITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELI-HSDDQENVAAFIS- 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737075318 120 fQAAQPSNILNrtIEITALHRTKGKFPIELSIWPHQQSGKQ-IFSAFIRDITDRKQREQ 177
Cdd:COG5809   204 -QLLKDGGIAQ--GEVRFWTKDGRWRLLEASGAPIKKNGEVdGIVIIFRDITERKKLEE 259
PRK13560 PRK13560
hypothetical protein; Provisional
 40-177 2.75e-10

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 61.61  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  40 ISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVIN-WNQAAERMFGWSAGEAIGNNLGEMiVPE--------EFR 110
Cdd:PRK13560  317 ISGRRAAERELLEKEDMLRAIIEAAPIAAIGLDADGNICFvNNNAAERMLGWSAAEVMGKPLPGM-DPElneefwcgDFQ 395

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737075318 111 EQHARGLMRFQAAQPSNILNRTIEI-----TALHRTKGKfPIELSIWP---HQQSGKQIFS-AFIRDITDRKQREQ 177
Cdd:PRK13560  396 EWYPDGRPMAFDACPMAKTIKGGKIfdgqeVLIEREDDG-PADCSAYAeplHDADGNIIGAiALLVDITERKQVEE 470
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 55-117 3.34e-10

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 55.48  E-value: 3.34e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737075318   55 ENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPE---EFREQHARGL 117
Cdd:smart00091   1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEdreRVQEALQRLL 66
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 39-177 3.99e-09

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 57.82  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  39 SISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEmIVPEEFREQHARGLM 118
Cdd:COG5805   141 DITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLE-LLHPCDKEEFKERIE 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737075318 119 RFQAAQPSNILNRTIeitaLHRTKGKFPIELSIWP--HQQSGKQIFSAFIRDITDRKQREQ 177
Cdd:COG5805   220 SITEVWQEFIIEREI----ITKDGRIRYFEAVIVPliDTDGSVKGILVILRDITEKKEAEE 276
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
 28-176 1.44e-08

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: 55.74  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  28 SLAEMHRELQESISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPE 107
Cdd:COG5000    63 EIGELARAFNRMTDQLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPEL 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1737075318 108 EFREQHARGLMRFQAAQpsnilnrtIEITalhrTKGKFPIELSIWPHQQSGKQIfsaFIRDITDRKQRE 176
Cdd:COG5000   143 DLAELLREALERGWQEE--------IELT----RDGRRTLLVRASPLRDDGYVI---VFDDITELLRAE 196
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 187-336 6.14e-08

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 54.33  E-value: 6.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 187 ALTGLPNRRLLSNRLElaitQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDEF 266
Cdd:PRK13561  235 PVSDLPNKALLMALLE----QVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDF 310

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1737075318 267 iALLPDlKANDPLPRQT-AEKISNALTQSFLIHEHVITISGSIGIALFPHDAAdADTLLNSADKAMYSSKK 336
Cdd:PRK13561  311 -AIIAN-GVKEPWHAITlGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLT-AEQLYSRAISAAFTARR 378
PleD COG3706
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ...
 226-335 8.72e-08

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: 51.45  E-value: 8.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 226 KPVNDvyghavgDELLRLVafrlqsvlregDTVARLGGDEFIALLPDLKANDplPRQTAEKISNALTQSFLIHehvitIS 305
Cdd:COG3706   104 KPFDP-------EELLARV-----------DLVARYGGEEFAILLPGTDLEG--ALAVAERIREAVAELPSLR-----VT 158

                          90       100       110
                  ....*....|....*....|....*....|
gi 1737075318 306 GSIGIAlfphdaadADTLLNSADkAMYSSK 335
Cdd:COG3706   159 VSIGVA--------GDSLLKRAD-ALYQAR 179
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 45-104 3.64e-07

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 51.31  E-value: 3.64e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  45 SMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMI 104
Cdd:COG3829     1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELI 60
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 75-171 6.22e-06

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 43.99  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  75 GVVINWNQAAERMFGWSAGEAIGNNLGEMIVPEEFREqharglmRFQAAQPSNILNRTIEITALHRTKGKFPIELSIWP- 153
Cdd:pfam13426   2 GRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSE-------RLREALREGKAVREFEVVLYRKDGEPFPVLVSLAPi 74

                          90
                  ....*....|....*....
gi 1737075318 154 HQQSGK-QIFSAFIRDITD 171
Cdd:pfam13426  75 RDDGGElVGIIAILRDITE 93
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
26-102 8.14e-06

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 47.66  E-value: 8.14e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1737075318  26 SLSLAEMHRELQESISEIESMQRALAESEENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGE 102
Cdd:PRK11360  233 STRLPPLPGELGEISQAINNLAQALRETRSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSE 309
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
 55-113 1.29e-05

PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 463802 [Multi-domain]  Cd Length: 65  Bit Score: 42.54  E-value: 1.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1737075318  55 ENHRQLVETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMIVPEEFREQH 113
Cdd:pfam13188   1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALE 59
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 189-331 1.55e-05

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 46.47  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 189 TGLPNRRLLSNRLElaitQAIANETEV---ALLFIDLDRFKPVNDVYGHAVGDELLRLVAFRLQSVLREGDTVARLGGDE 265
Cdd:PRK11829  238 TELPNRSLFISLLE----KEIASSTRTdhfHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTE 313

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1737075318 266 FIALLPDLKANDPlPRQTAEKISNALTQSFLIHEHVITISGSIGIALFPHDAADADTLLNSADKAM 331
Cdd:PRK11829  314 FAVLARGTRRSFP-AMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAM 378
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 61-174 1.59e-05

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


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 43.56  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  61 VETAQDAVITINHAGVVINWNQAAERMFGWSAGEAIGNNLGEMiVPEEFREQHARgLMRfQAAQpsniLNRTIEITALHR 140
Cdd:pfam08448   1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAARLER-ALR-RALE----GEEPIDFLEELL 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1737075318 141 TKGKF-PIELSIWP-HQQSGKQIFSAFI-RDITDRKQ 174
Cdd:pfam08448  74 LNGEErHYELRLTPlRDPDGEVIGVLVIsRDITERRR 110
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 67-177 2.16e-04

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 43.22  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318  67 AVITINHAGVVINWNQAAERMFGWSAGEAIGNNLgEMIVPEEFREQHARGLMRFQAAQPSNILNRTIEITALHRTKGKFP 146
Cdd:PRK11359   24 GAVLINENDEVLFFNPAAEKLWGYKREEVIGNNI-DMLIPRDLRPAHPEYIRHNREGGKARVEGMSRELQLEKKDGSKIW 102

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1737075318 147 IELSIWPHQQSGKQIFSAFIRDITDR-KQREQ 177
Cdd:PRK11359  103 TRFALSKVSAEGKVYYLALVRDASVEmAQKEQ 134
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 166-271 3.03e-04

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 42.54  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737075318 166 IRDITD-RKQREQVVWL---HANFDALTGLPNRRLLSNRLELAITQAIANETEVALLFIDLDRFKPVNDVYGHAVGDELL 241
Cdd:PRK11059  207 LSELQDaREERSRFDTFirsNAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELL 286

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1737075318 242 -RLVAFRLQSVLREGDTV-ARLGGDEFIALLP 271
Cdd:PRK11059  287 fELINLLSTFVMRYPGALlARYSRSDFAVLLP 318
 
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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