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Conserved domains on  [gi|56752384|ref|YP_173085|]
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hypothetical protein syc2375_d [Synechococcus elongatus PCC 6301]

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List of domain hits

Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
986-1225 3.55e-105

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  Cd Length: 240  Bit Score: 333.36  E-value: 3.55e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  986 DLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWIDHe 1065
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1066 GFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYSSL 1145
Cdd:cd01948   81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1146 GYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPEAE 1225
Cdd:cd01948  161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
809-967 9.05e-55

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  Cd Length: 158  Bit Score: 189.31  E-value: 9.05e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  809 THDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLSS 888
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56752384  889 DEFVILLTDLDVQSkARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKNLWC 967
Cdd:cd01949   81 DEFAILLPGTDLEE-AEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
693-794 6.36e-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. 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: 58.03  E-value: 6.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  693 IIIADaqqPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLRSYRKDGSLFWNQI 772
Cdd:cd00130    5 VIVLD---LDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81
                         90       100
                 ....*....|....*....|..
gi 56752384  773 SLAPVRDQKGHLTHMVASQTDV 794
Cdd:cd00130   82 SLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
559-669 1.12e-05

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


:

Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 45.32  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  559 TNDAVWDRNLLTNEIWYSANYSRLFGGEEKEITQKlvqtvdlQWRDRLDPDQRERIMASLSGAIANGFSTWSEqYRFLRQ 638
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGK-------SLLDLIHPEDREELRERLENLLSGGEPVTLE-VRLRRK 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 56752384  639 DGTYAHVLDRGYIVRDENGRAIRAVGAMQDI 669
Cdd:cd00130   73 DGSVIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
443-511 2.89e-04

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: 40.69  E-value: 2.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56752384  443 SDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWDLFPVELGATLQSELQPLQHQSSTRTFELWID 511
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLR 70
PAS_9 pfam13426
PAS domain;
691-796 3.94e-27

PAS domain;


:

Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 108.24  E-value: 3.94e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    691 NSIIIADAQqpdMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLRSYRKDGSLFWN 770
Cdd:pfam13426    2 DGILVLDPE---GRIVYANPAALRLLGYTREELLGKSIRDLFGPGTDEEAVARLREALRNGGEVEVELELRRKDGEPFPV 78
                           90       100
                   ....*....|....*....|....*.
gi 56752384    771 QISLAPVRDQKGHLTHMVASQTDVSE 796
Cdd:pfam13426   79 LVSASPVRDEDGEVVGIVGILRDITE 104
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
573-666 4.21e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


:

Pssm-ID: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 70.10  E-value: 4.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    573 IWYSANYSRLFGGEEKEITQKLVQtvdlqWRDRLDPDQRERIMASLSGAIANGFSTWSEQYRFLRQDGTYAHVLDRGYIV 652
Cdd:pfam08447    2 IYWSPRFEEILGYTPEELKSSYEG-----WLDLVHPEDRERVRRALQELLLKKGEPYSGEYRIRRKDGSYRWVEARGRPI 76
                           90
                   ....*....|....
gi 56752384    653 RDENGRAIRAVGAM 666
Cdd:pfam08447   77 RDENGKPVRVIGVA 90
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
331-557 5.05e-06

FOG: PAS/PAC domain [Signal transduction mechanisms]


:

Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 47.92  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  331 PIYIKDYRGEILLQNRACLDLQPFVMPEVIKQEDIND----------LATIASGLPIINEEWTINPENWPSQHFLISKVP 400
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEELLGLLLALHpedrdrlrelLRRLLAGEELLSEELRLVRKDGEERWVELSAAP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  401 LRNELGQILGLLGIRRNvTRWRRAEQARNALSDQLEQTLAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWD 480
Cdd:COG2202   81 LRDGEGRVLGLLGLRDI-TERKRAEEALRESEERLRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSD 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56752384  481 LFPVELGATLQSELQPLqhqsstrtfELWIDPLSTCWEVNVHRSTAEISLYFRDISDRVMSRQLLEEMAERFQLVTR 557
Cdd:COG2202  160 LIHPEDEERRELELARA---------LAEGRGGPLEIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITE 227
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
234-425 4.39e-04

FOG: PAS/PAC domain [Signal transduction mechanisms]


:

Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 42.14  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  234 WLEHFQLSDRLRLEQAIDTGMQTGRPIQATYALASDSQDRQLVELRAVIVRDLAGNVRSLRGVLEPKHQAPLtsLEPLPL 313
Cdd:COG2202   32 LLLALHPEDRDRLRELLRRLLAGEELLSEELRLVRKDGEERWVELSAAPLRDGEGRVLGLLGLRDITERKRA--EEALRE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  314 SLDHpavLRRILEAIPDPIYIKDYRGEILLQNRACLDL-------------QPFVMPEVIKQEDINDLATIASG--LPII 378
Cdd:COG2202  110 SEER---LRALLEASPDGIWVLDEDGRILYANPAAEELlgyspeeelgrglSDLIHPEDEERRELELARALAEGrgGPLE 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 56752384  379 NEEWTINPENWPSQHFLISKVPLRNElGQILGLLGIRRNVTRWRRAE 425
Cdd:COG2202  187 IEYRVRRKDGERVRWILSRISPVRDD-GEIVGVVGIARDITERKQAE 232
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
986-1225 3.55e-105

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  Cd Length: 240  Bit Score: 333.36  E-value: 3.55e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  986 DLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWIDHe 1065
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1066 GFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYSSL 1145
Cdd:cd01948   81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1146 GYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPEAE 1225
Cdd:cd01948  161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
809-967 9.05e-55

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  Cd Length: 158  Bit Score: 189.31  E-value: 9.05e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  809 THDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLSS 888
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56752384  889 DEFVILLTDLDVQSkARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKNLWC 967
Cdd:cd01949   81 DEFAILLPGTDLEE-AEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
693-794 6.36e-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. 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: 58.03  E-value: 6.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  693 IIIADaqqPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLRSYRKDGSLFWNQI 772
Cdd:cd00130    5 VIVLD---LDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81
                         90       100
                 ....*....|....*....|..
gi 56752384  773 SLAPVRDQKGHLTHMVASQTDV 794
Cdd:cd00130   82 SLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
559-669 1.12e-05

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 45.32  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  559 TNDAVWDRNLLTNEIWYSANYSRLFGGEEKEITQKlvqtvdlQWRDRLDPDQRERIMASLSGAIANGFSTWSEqYRFLRQ 638
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGK-------SLLDLIHPEDREELRERLENLLSGGEPVTLE-VRLRRK 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 56752384  639 DGTYAHVLDRGYIVRDENGRAIRAVGAMQDI 669
Cdd:cd00130   73 DGSVIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
443-511 2.89e-04

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: 40.69  E-value: 2.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56752384  443 SDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWDLFPVELGATLQSELQPLQHQSSTRTFELWID 511
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLR 70
Rtn COG2200
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms]
980-1236 2.80e-100

c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms]


Pssm-ID: 225110  Cd Length: 256  Bit Score: 320.78  E-value: 2.80e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  980 RIDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLR 1059
Cdd:COG2200    1 RLQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1060 RWIDHEGFtgSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESPERFVQWLQEARSMGFQVALDDFG 1139
Cdd:COG2200   81 TWPRAGPL--RLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1140 TGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGP 1219
Cdd:COG2200  159 TGYSSLSYLKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSR 238
                        250
                 ....*....|....*..
gi 56752384 1220 PLPEAEALAFLHRSASP 1236
Cdd:COG2200  239 PLPADALDALLSSSQSR 255
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
984-1225 7.78e-90

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


Pssm-ID: 214491  Cd Length: 242  Bit Score: 290.66  E-value: 7.78e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384     984 EKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWID 1063
Cdd:smart00052    1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    1064 HEGFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYS 1143
Cdd:smart00052   81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    1144 SLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPE 1223
Cdd:smart00052  161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240

                    ..
gi 56752384    1224 AE 1225
Cdd:smart00052  241 DD 242
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
984-1220 5.24e-69

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: 249961  Cd Length: 231  Bit Score: 232.28  E-value: 5.24e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    984 EKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWID 1063
Cdd:pfam00563    1 EEALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLISPDEFLPLAERLGLIAELDRWVLEKALAQLAEWLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   1064 HegfTGSLSFNISARQFIRQNiFLKLFDVLQEFQIPPHQLEIELTESSLIESPeRFVQWLQEARSMGFQVALDDFGTGYS 1143
Cdd:pfam00563   81 P---DLPLSVNLSPASLLDPS-FLEALLALKQGGLPPSRLVLEITESALDEDL-RLLEALARLRSLGFRLALDDFGTGYS 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56752384   1144 SLGYLKRLPINALKIDRSFIRDLpHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPP 1220
Cdd:pfam00563  156 SLSLLSRLPPDYIKIDRSFIKDL-SDPESRALLRALIALARSLGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 231
GGDEF pfam00990
GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a ...
808-964 5.30e-54

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.


Pssm-ID: 250276  Cd Length: 159  Bit Score: 187.06  E-value: 5.30e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    808 ATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLS 887
Cdd:pfam00990    1 AAHDPLTGLPNRRYFEEELEQELQRARRQQSPLALLLIDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    888 SDEFVILLTDLDVQSKARVkAAMIQSLMAK---PFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKN 964
Cdd:pfam00990   81 GEEFAILLPDTSLEGAQEL-AERIRRLLAAlaiPHTLSGLPLYVTISIGIAAYPNDGEDPEDLLKRADQALYQAKQQGRN 159
COG2199 COG2199
c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms]
791-969 7.42e-50

c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms]


Pssm-ID: 225109  Cd Length: 181  Bit Score: 176.10  E-value: 7.42e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  791 QTDVSESKAFEEMLLQQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAA 870
Cdd:COG2199    3 LRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  871 GRLQQCIQEHETVARLSSDEFVILLTDLDvQSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDG-QSGSELLQ 949
Cdd:COG2199   83 RRLRSNLREGDLVARLGGDEFAVLLPGTS-LEEAARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDGsDDAELLLR 161
                        170       180
                 ....*....|....*....|
gi 56752384  950 AADLAVCAAKQQGKNLWCSF 969
Cdd:COG2199  162 RADLALYRAKRAGRNRVVVF 181
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
806-969 1.02e-49

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


Pssm-ID: 128563  Cd Length: 163  Bit Score: 175.13  E-value: 1.02e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384     806 QQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVAR 885
Cdd:smart00267    1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384     886 LSSDEFVILLTDLDVQSKARVKAAMIQSLmAKPFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKNL 965
Cdd:smart00267   81 LGGDEFALLLPETSLEEAIALAERILQQL-REPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159

                    ....
gi 56752384     966 WCSF 969
Cdd:smart00267  160 VAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
807-965 4.24e-40

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: 232895  Cd Length: 165  Bit Score: 147.48  E-value: 4.24e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    807 QATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARL 886
Cdd:TIGR00254    1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    887 SSDEFVILLTDLDVQSKARVKAAMIQSLMAKPFEVMGNP-IELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKNL 965
Cdd:TIGR00254   81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
755-796 4.53e-06

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 45.64  E-value: 4.53e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 56752384     755 EVTLRSYRKDGSLFWNQISLAPVRDQKGHLTHMVASQTDVSE 796
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
433-499 1.05e-04

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 42.00  E-value: 1.05e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56752384     433 DQLEQTLAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWDLFPVELGATLQSELQPLQH 499
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
632-671 3.91e-04

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 39.86  E-value: 3.91e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 56752384     632 QYRFLRQDGTYAHVLDRGYIVRDENGRAIRAVGAMQDISA 671
Cdd:smart00086    3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PAS_9 pfam13426
PAS domain;
691-796 3.94e-27

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 108.24  E-value: 3.94e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    691 NSIIIADAQqpdMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLRSYRKDGSLFWN 770
Cdd:pfam13426    2 DGILVLDPE---GRIVYANPAALRLLGYTREELLGKSIRDLFGPGTDEEAVARLREALRNGGEVEVELELRRKDGEPFPV 78
                           90       100
                   ....*....|....*....|....*.
gi 56752384    771 QISLAPVRDQKGHLTHMVASQTDVSE 796
Cdd:pfam13426   79 LVSASPVRDEDGEVVGIVGILRDITE 104
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
573-666 4.21e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 70.10  E-value: 4.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    573 IWYSANYSRLFGGEEKEITQKLVQtvdlqWRDRLDPDQRERIMASLSGAIANGFSTWSEQYRFLRQDGTYAHVLDRGYIV 652
Cdd:pfam08447    2 IYWSPRFEEILGYTPEELKSSYEG-----WLDLVHPEDRERVRRALQELLLKKGEPYSGEYRIRRKDGSYRWVEARGRPI 76
                           90
                   ....*....|....
gi 56752384    653 RDENGRAIRAVGAM 666
Cdd:pfam08447   77 RDENGKPVRVIGVA 90
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
331-557 5.05e-06

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 47.92  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  331 PIYIKDYRGEILLQNRACLDLQPFVMPEVIKQEDIND----------LATIASGLPIINEEWTINPENWPSQHFLISKVP 400
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEELLGLLLALHpedrdrlrelLRRLLAGEELLSEELRLVRKDGEERWVELSAAP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  401 LRNELGQILGLLGIRRNvTRWRRAEQARNALSDQLEQTLAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWD 480
Cdd:COG2202   81 LRDGEGRVLGLLGLRDI-TERKRAEEALRESEERLRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSD 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56752384  481 LFPVELGATLQSELQPLqhqsstrtfELWIDPLSTCWEVNVHRSTAEISLYFRDISDRVMSRQLLEEMAERFQLVTR 557
Cdd:COG2202  160 LIHPEDEERRELELARA---------LAEGRGGPLEIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITE 227
PRK10060 PRK10060
RNase II stability modulator; Provisional
787-1232 4.26e-114

RNase II stability modulator; Provisional


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 373.25  E-value: 4.26e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   787 MVASQTDVSESKAFEEMLLQQATHDALTGLPNRLLFLDRLDQAAARArgGGSPIAVLFIDLDNFKAINDGFSHSEGDAVL 866
Cdd:PRK10060  216 LICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   867 QIAAGRLQQCIQEHETVARLSSDEFVILLTDLDvQSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDGQSGSE 946
Cdd:PRK10060  294 QDVSLAILSCLEEDQTLARLGGDEFLVLASHTS-QAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSES 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   947 LLQAADLAVCAAKQQGKNLWCSFSEAMREQLRSRIDIEKDLRQALIDNSLELYFQPQVDLvTHRLLGFETLVRWNHPERG 1026
Cdd:PRK10060  373 LIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERG 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1027 LVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWIDhEGFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIE 1106
Cdd:PRK10060  452 LIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRD-KGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVE 530
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1107 LTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVL 1186
Cdd:PRK10060  531 LTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQAL 610
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 56752384  1187 KLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPEAEALAFLHR 1232
Cdd:PRK10060  611 NLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
COG5001 COG5001
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain ...
785-1225 1.34e-97

Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms]


Pssm-ID: 227334 [Multi-domain]  Cd Length: 663  Bit Score: 327.62  E-value: 1.34e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  785 THMVASQTDVS----ESKAFEEMLLQQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHS 860
Cdd:COG5001  201 SDMVQSQVTLTqraeETRRLSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHA 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  861 EGDAVLQIAAGRLQQCIQEHETVARLSSDEFVILLTDL-DVQSKARVKAAMIQSLMAkPFEVMGNPIELTASIGVATFPH 939
Cdd:COG5001  281 TGDRLLIEVGRRLKAFDGAPILAARLGGDEFALIIPALeDDALRVAGARALCESLQA-PYDLRGVRVQVGASIGIAPFPS 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  940 DGQSGSELLQAADLAVCAAKQQGKNLWCSFSEAMREQLRSRIDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVR 1019
Cdd:COG5001  360 GADTSEQLFERADYALYHAKQNGKGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALEALAR 439
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1020 WNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWIDhegfTGSLSFNISARQFIRQNIFLKLFDVLQEFQIP 1099
Cdd:COG5001  440 WHSPEIGPVPPDVFIGIAERSGQIVELTRLLLAKALREARAWPM----DVRVSINLSARDLASMENVRRLLAIVSESCIA 515
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1100 PHQLEIELTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAI 1179
Cdd:COG5001  516 PHRLDFEITETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTV 595
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 56752384 1180 VAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPEAE 1225
Cdd:COG5001  596 LQLGRNLRMECVVEGVETEAQRDRVAALGATVMQGYHYARPMPAEE 641
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
519-1228 1.31e-88

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 311.22  E-value: 1.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   519 VNVHRSTAEISLYF----RDISDRVMSRQLLEEMAERFQLVTRATNDAVWDRNLLTNEIWYSANYSRLFGgeekeITQKL 594
Cdd:PRK09776  375 VSLVRDTDGTPLYFiaqiEDINELKRTEQVNERLMERITLANEAGGIGIWEWDLKPNIISWDKRMFELYE-----IPPHI 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   595 VQTVDlQWRDRLDPDQRERIMASLSGAIAnGFSTWSEQYRFLRQDGTYaHVLDRGYIVRDENGRAIRAVGAMQDISAIVA 674
Cdd:PRK09776  450 KPTWQ-VWYACLHPEDRQRVEKEIRDALQ-GRSPFKLEFRIVVKDGVR-HIRALANRVLNKDGEVERLLGINMDMTEVRQ 526
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   675 ANEQL-----RLWLrAIESTGNSIIIADAqqpDMPIIYVNPAFEKITGFSAAEVIG----RNFRFL---QGLETQQAELE 742
Cdd:PRK09776  527 LNEALfqekeRLHI-TLDSIGEAVVCTDM---AMKVTFMNPVAEKMTGWTQEEALGvpllTVLHITfgdNGPLMENIYSC 602
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   743 EMRRA---LEEGtyceVTLRSyrKDGSLFWNQISLAPVRDQKGHLTHMVASQTDVSESKAFEEMLLQQATHDALTGLPNR 819
Cdd:PRK09776  603 LTSRSaayLEQD----VVLHC--RSGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANR 676
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   820 LLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLSSDEFVILLTDLD 899
Cdd:PRK09776  677 ASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCN 756
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   900 VQSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKNLwCSFSEAMREQLRS 979
Cdd:PRK09776  757 VESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGR-VTVYEPQQAAAHS 835
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   980 R---IDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAgl 1056
Cdd:PRK09776  836 EhraLSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEF-- 913
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1057 tLRRWIDHEGFTG-SLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESPERFVQWLQEARSMGFQVAL 1135
Cdd:PRK09776  914 -FRQAAKAVASKGlSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVL 992
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1136 DDFGTGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGF 1215
Cdd:PRK09776  993 SDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGY 1072
                         730
                  ....*....|...
gi 56752384  1216 FYGPPLPEAEALA 1228
Cdd:PRK09776 1073 AIARPQPLDLLLN 1085
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
682-804 3.13e-17

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: 232884 [Multi-domain]  Cd Length: 124  Bit Score: 80.02  E-value: 3.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    682 WLRAI-ESTGNSIIIADaqqPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALE-EGTYCEVTLR 759
Cdd:TIGR00229    4 RYRAIfESSPDAIIVID---LEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEgEREPVSEERR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 56752384    760 SYRKDGSLFWNQISLAPVRDQKGHlTHMVASQTDVSESKAFEEML 804
Cdd:TIGR00229   81 VRRKDGSEIWVEVSVSPIRTNGGE-LGVVGIVRDITERKQAEEAL 124
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
562-801 1.01e-14

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 74.50  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  562 AVWDRNLLTNEIWYSANYSRLFGGEEKEItqklvqtvdLQWRDRLDPDQRERIMAsLSGAIANGFSTWSEQYRFLRQDGT 641
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEEL---------LGLLLALHPEDRDRLRE-LLRRLLAGEELLSEELRLVRKDGE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  642 YAHVLDRGYIVRDENGRAIRAVGAMQD---ISAIVAANEQLRLWLRAIESTGNSIIIADaqqPDMPIIYVNPAFEKITGF 718
Cdd:COG2202   71 ERWVELSAAPLRDGEGRVLGLLGLRDIterKRAEEALRESEERLRALLEASPDGIWVLD---EDGRILYANPAAEELLGY 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  719 SAAEVIGRNFRFLQGLETQQAELEEMRRAL--EEGTYCEVTLRSYRKDGS-LFWNQISLAPVRDQkGHLTHMVASQTDVS 795
Cdd:COG2202  148 SPEEELGRGLSDLIHPEDEERRELELARALaeGRGGPLEIEYRVRRKDGErVRWILSRISPVRDD-GEIVGVVGIARDIT 226

                 ....*.
gi 56752384  796 ESKAFE 801
Cdd:COG2202  227 ERKQAE 232
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
445-675 4.97e-09

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 56.78  E-value: 4.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  445 GVVVLDQNFVVRALNSQAAQQLKKTSEQIIGrVFWDLFPVELGATLQSELQPLQHQSSTRTFELWIDPLSTCWEVNVHRS 524
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEELLG-LLLALHPEDRDRLRELLRRLLAGEELLSEELRLVRKDGEERWVELSAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  525 T-------AEISLYFRDISDRVMSRQLLEEMAERFQLVTRATNDAVWDRNLLTNEIWYSANYSRLFGGEEKEITQKLVQT 597
Cdd:COG2202   80 PlrdgegrVLGLLGLRDITERKRAEEALRESEERLRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSD 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56752384  598 VDLQWRDRLDPDQRERIMASLSGAIangfstWSEQYRFLRQDGTYAHVLDRGYIVRDENGRAIRAVGAMQDISAIVAA 675
Cdd:COG2202  160 LIHPEDEERRELELARALAEGRGGP------LEIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITERKQA 231
PRK13560 PRK13560
hypothetical protein; Provisional
321-680 4.26e-08

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 56.22  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   321 LRRILEAIPDPIYIKDYRGEILLQNRACLDLQPFVMPEVIKQEdINDLATI---------------ASGLPIINEEWTIN 385
Cdd:PRK13560  206 LQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMS-IHDFAPAqpaddyqeadaakfdADGSQIIEAEFQNK 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   386 PENWPSQHFLISKVPLRNELGQILGLLGIRRNVTRWRRAEQARNALSDQLEQTLAAVSDGVVVLDQNFVVRALNSQAAQQ 465
Cdd:PRK13560  285 DGRTRPVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPIAAIGLDADGNICFVNNNAAER 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   466 -LKKTSEQIIGRVFWDLFPvelgatlqselqPLQHQSSTRTFELWIDPLSTCW-------------------EVNVHR-- 523
Cdd:PRK13560  365 mLGWSAAEVMGKPLPGMDP------------ELNEEFWCGDFQEWYPDGRPMAfdacpmaktikggkifdgqEVLIERed 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   524 -STAEISLYFRDISDR----VMSRQLLEEMAERFQL--VTRATNDAVWDRNLL-----TNEIW----YSANYSRlFGGEE 587
Cdd:PRK13560  433 dGPADCSAYAEPLHDAdgniIGAIALLVDITERKQVeeQLLLANLIVENSPLVlfrwkAEEGWpvelVSKNITQ-FGYEP 511
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   588 KEITQKLVQTVDLqwrdrLDPDQRERIMASLSGAIANGFSTWSEQYRFLRQDGTYAHVLDRGYIVRDENGRAIRAVGAMQ 667
Cdd:PRK13560  512 DEFISGKRMFAAI-----IHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVI 586
                         410
                  ....*....|...
gi 56752384   668 DISAIVAANEQLR 680
Cdd:PRK13560  587 DISERKHAEEKIK 599
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
439-539 9.05e-06

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 45.48  E-value: 9.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    439 LAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWDLFPVELGATLQSELQPL--QHQSSTRTFELwIDPLSTC 516
Cdd:pfam08448    1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRAleGEEPIDFLEEL-LLNGEER 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 56752384    517 -WEVNVHRSTAE------ISLYFRDISDRV 539
Cdd:pfam08448   80 hYELRLTPLRDPdgevigVLVISRDITERR 109
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
234-425 4.39e-04

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 42.14  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  234 WLEHFQLSDRLRLEQAIDTGMQTGRPIQATYALASDSQDRQLVELRAVIVRDLAGNVRSLRGVLEPKHQAPLtsLEPLPL 313
Cdd:COG2202   32 LLLALHPEDRDRLRELLRRLLAGEELLSEELRLVRKDGEERWVELSAAPLRDGEGRVLGLLGLRDITERKRA--EEALRE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  314 SLDHpavLRRILEAIPDPIYIKDYRGEILLQNRACLDL-------------QPFVMPEVIKQEDINDLATIASG--LPII 378
Cdd:COG2202  110 SEER---LRALLEASPDGIWVLDEDGRILYANPAAEELlgyspeeelgrglSDLIHPEDEERRELELARALAEGrgGPLE 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 56752384  379 NEEWTINPENWPSQHFLISKVPLRNElGQILGLLGIRRNVTRWRRAE 425
Cdd:COG2202  187 IEYRVRRKDGERVRWILSRISPVRDD-GEIVGVVGIARDITERKQAE 232
PRK11360 PRK11360
sensory histidine kinase AtoS; Provisional
400-551 1.00e-03

sensory histidine kinase AtoS; Provisional


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 41.88  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   400 PLRNELGQILGllgirrnvtrwrraeqARNALSDQLEQT-------LAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQ 472
Cdd:PRK11360  238 PLPGELGEISQ----------------AINNLAQALRETrslneliLESIADGVIAIDRQGKITTMNPAAEVITGLQRHE 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   473 IIGRVFWDLFPVE------LGATLQ----SELQPLQHQSSTRTFELwidPLSTCWEVNVHRSTAEISLYFRDISDRvmsR 542
Cdd:PRK11360  302 LVGKPYSELFPPNtpfaspLLDTLEhgteHVDLEISFPGRDRTIEL---SVSTSLLHNTHGEMIGALVIFSDLTER---K 375
                         170
                  ....*....|.
gi 56752384   543 QLLEEMA--ER 551
Cdd:PRK11360  376 RLQRRVArqER 386
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
581-679 2.19e-03

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: 232884 [Multi-domain]  Cd Length: 124  Bit Score: 38.03  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    581 RLFGGEEKEItqklvqtVDLQWRDRLDPDQRERIMASLSGAIANGFSTWSEQYRFLRQDGTYAHVLDRGYIVRdENGRAI 660
Cdd:TIGR00229   34 EIFGYSAEEL-------IGRNVLELIPEEDREEVRERIERRLEGEREPVSEERRVRRKDGSEIWVEVSVSPIR-TNGGEL 105
                           90
                   ....*....|....*....
gi 56752384    661 RAVGAMQDISAIVAANEQL 679
Cdd:TIGR00229  106 GVVGIVRDITERKQAEEAL 124
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
318-512 4.13e-03

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions].


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 39.89  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    318 PAVLRRILEAIPDPIYIKDYRGEILLQNRACLDLQPFVMPEVI-KQEDIndLATIASGLPIINEEWTINPENWPSQHFLI 396
Cdd:TIGR02938    3 PEAYRQTVDQAPLAISITDLKANILYANDAFTRITGYTKEEIIgKNESV--LSNHTTPPEVYQALWGSLAEQKPWAGKLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    397 SK-------------VPLRNELGQILGLLGIRRNVTRWRRAEQARNALSDQLEQTLAAVSDGVVVLDQNFVVRALNSQAA 463
Cdd:TIGR02938   81 NRrkdgelylaeltvAPVLNEAGETTHFLGMHRDITELHRLEQVVANQKLLIESVVDAAPVAFVLLDPTGRVILDNQEYK 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 56752384    464 QQLKKTSEQIIGRVFWDLFPVELGATLqSELQPlqHQSSTRTFELWIDP 512
Cdd:TIGR02938  161 KLATDLRVKEPAHTVLDLLREAWREAL-AENWP--QQLAFSNREARFDR 206
 
Name Accession Description Interval E-value
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
986-1225 3.55e-105

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  Cd Length: 240  Bit Score: 333.36  E-value: 3.55e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  986 DLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWIDHe 1065
Cdd:cd01948    2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1066 GFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYSSL 1145
Cdd:cd01948   81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1146 GYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPEAE 1225
Cdd:cd01948  161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
809-967 9.05e-55

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  Cd Length: 158  Bit Score: 189.31  E-value: 9.05e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  809 THDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLSS 888
Cdd:cd01949    1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56752384  889 DEFVILLTDLDVQSkARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKNLWC 967
Cdd:cd01949   81 DEFAILLPGTDLEE-AEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
693-794 6.36e-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. 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: 58.03  E-value: 6.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  693 IIIADaqqPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLRSYRKDGSLFWNQI 772
Cdd:cd00130    5 VIVLD---LDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81
                         90       100
                 ....*....|....*....|..
gi 56752384  773 SLAPVRDQKGHLTHMVASQTDV 794
Cdd:cd00130   82 SLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
559-669 1.12e-05

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 45.32  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  559 TNDAVWDRNLLTNEIWYSANYSRLFGGEEKEITQKlvqtvdlQWRDRLDPDQRERIMASLSGAIANGFSTWSEqYRFLRQ 638
Cdd:cd00130    1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGK-------SLLDLIHPEDREELRERLENLLSGGEPVTLE-VRLRRK 72
                         90       100       110
                 ....*....|....*....|....*....|.
gi 56752384  639 DGTYAHVLDRGYIVRDENGRAIRAVGAMQDI 669
Cdd:cd00130   73 DGSVIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
443-511 2.89e-04

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: 40.69  E-value: 2.89e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56752384  443 SDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWDLFPVELGATLQSELQPLQHQSSTRTFELWID 511
Cdd:cd00130    2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLR 70
Rtn COG2200
c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms]
980-1236 2.80e-100

c-di-GMP phosphodiesterase class I (EAL domain) [Signal transduction mechanisms]


Pssm-ID: 225110  Cd Length: 256  Bit Score: 320.78  E-value: 2.80e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  980 RIDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLR 1059
Cdd:COG2200    1 RLQLERDLRQALENGEFSLYYQPIVDLATGRIVGYEALLRWRHPDGGLISPGEFIPLAEETGLIVELGRWVLEEACRQLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1060 RWIDHEGFtgSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESPERFVQWLQEARSMGFQVALDDFG 1139
Cdd:COG2200   81 TWPRAGPL--RLAVNLSPVQLRSPGLVDLLLRLLARLGLPPHRLVLEITESALIDDLDTALALLRQLRELGVRIALDDFG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1140 TGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGP 1219
Cdd:COG2200  159 TGYSSLSYLKRLPPDILKIDRSFVRDLETDARDQAIVRAIVALAHKLGLTVVAEGVETEEQLDLLRELGCDYLQGYLFSR 238
                        250
                 ....*....|....*..
gi 56752384 1220 PLPEAEALAFLHRSASP 1236
Cdd:COG2200  239 PLPADALDALLSSSQSR 255
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
984-1225 7.78e-90

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


Pssm-ID: 214491  Cd Length: 242  Bit Score: 290.66  E-value: 7.78e-90
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384     984 EKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWID 1063
Cdd:smart00052    1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    1064 HEGFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYS 1143
Cdd:smart00052   81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    1144 SLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPE 1223
Cdd:smart00052  161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240

                    ..
gi 56752384    1224 AE 1225
Cdd:smart00052  241 DD 242
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
984-1220 5.24e-69

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: 249961  Cd Length: 231  Bit Score: 232.28  E-value: 5.24e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    984 EKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWID 1063
Cdd:pfam00563    1 EEALREALENGEFSLYFQPIVDLRTGKVLGYEALLRWQHPDGGLISPDEFLPLAERLGLIAELDRWVLEKALAQLAEWLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   1064 HegfTGSLSFNISARQFIRQNiFLKLFDVLQEFQIPPHQLEIELTESSLIESPeRFVQWLQEARSMGFQVALDDFGTGYS 1143
Cdd:pfam00563   81 P---DLPLSVNLSPASLLDPS-FLEALLALKQGGLPPSRLVLEITESALDEDL-RLLEALARLRSLGFRLALDDFGTGYS 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56752384   1144 SLGYLKRLPINALKIDRSFIRDLpHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPP 1220
Cdd:pfam00563  156 SLSLLSRLPPDYIKIDRSFIKDL-SDPESRALLRALIALARSLGIKVVAEGVETEEQLELLKELGIDYVQGYLFSKP 231
GGDEF pfam00990
GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a ...
808-964 5.30e-54

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.


Pssm-ID: 250276  Cd Length: 159  Bit Score: 187.06  E-value: 5.30e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    808 ATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLS 887
Cdd:pfam00990    1 AAHDPLTGLPNRRYFEEELEQELQRARRQQSPLALLLIDLDNFKRINDTYGHAVGDEVLQEVAQRLSSSLRRSDLVARLG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    888 SDEFVILLTDLDVQSKARVkAAMIQSLMAK---PFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKN 964
Cdd:pfam00990   81 GEEFAILLPDTSLEGAQEL-AERIRRLLAAlaiPHTLSGLPLYVTISIGIAAYPNDGEDPEDLLKRADQALYQAKQQGRN 159
COG2199 COG2199
c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms]
791-969 7.42e-50

c-di-GMP synthetase (diguanylate cyclase, GGDEF domain) [Signal transduction mechanisms]


Pssm-ID: 225109  Cd Length: 181  Bit Score: 176.10  E-value: 7.42e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  791 QTDVSESKAFEEMLLQQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAA 870
Cdd:COG2199    3 LRLLTRLRKAEERLERLALHDPLTGLPNRRAFEERLERALARARRHGEPLALLLLDLDHFKQINDTYGHAAGDEVLREVA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  871 GRLQQCIQEHETVARLSSDEFVILLTDLDvQSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDG-QSGSELLQ 949
Cdd:COG2199   83 RRLRSNLREGDLVARLGGDEFAVLLPGTS-LEEAARLAERIRAALEEPFFLGGEELRVTVSIGVALYPEDGsDDAELLLR 161
                        170       180
                 ....*....|....*....|
gi 56752384  950 AADLAVCAAKQQGKNLWCSF 969
Cdd:COG2199  162 RADLALYRAKRAGRNRVVVF 181
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
806-969 1.02e-49

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


Pssm-ID: 128563  Cd Length: 163  Bit Score: 175.13  E-value: 1.02e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384     806 QQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVAR 885
Cdd:smart00267    1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384     886 LSSDEFVILLTDLDVQSKARVKAAMIQSLmAKPFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKNL 965
Cdd:smart00267   81 LGGDEFALLLPETSLEEAIALAERILQQL-REPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159

                    ....
gi 56752384     966 WCSF 969
Cdd:smart00267  160 VAVY 163
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
807-965 4.24e-40

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: 232895  Cd Length: 165  Bit Score: 147.48  E-value: 4.24e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    807 QATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARL 886
Cdd:TIGR00254    1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    887 SSDEFVILLTDLDVQSKARVKAAMIQSLMAKPFEVMGNP-IELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKNL 965
Cdd:TIGR00254   81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
Nucleotidyl_cyc_III cd07556
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ...
839-936 7.58e-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  Cd Length: 133  Bit Score: 64.30  E-value: 7.58e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  839 PIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHE-TVARLSSDEFVILLTDLDVQSKARVKAAMIQSLMAK 917
Cdd:cd07556    1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAL 80
                         90
                 ....*....|....*....
gi 56752384  918 PFEvMGNPIELtaSIGVAT 936
Cdd:cd07556   81 NQS-EGNPVRV--RIGIHT 96
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
755-796 4.53e-06

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 45.64  E-value: 4.53e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 56752384     755 EVTLRSYRKDGSLFWNQISLAPVRDQKGHLTHMVASQTDVSE 796
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
684-749 5.17e-05

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 42.77  E-value: 5.17e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 56752384     684 RAIESTGNSIIIADaqqPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALE 749
Cdd:smart00091    5 AILESLPDGIFVLD---LDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
433-499 1.05e-04

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


Pssm-ID: 214512  Cd Length: 67  Bit Score: 42.00  E-value: 1.05e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56752384     433 DQLEQTLAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWDLFPVELGATLQSELQPLQH 499
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
632-671 3.91e-04

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


Pssm-ID: 197509  Cd Length: 43  Bit Score: 39.86  E-value: 3.91e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 56752384     632 QYRFLRQDGTYAHVLDRGYIVRDENGRAIRAVGAMQDISA 671
Cdd:smart00086    3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
PAS_9 pfam13426
PAS domain;
691-796 3.94e-27

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 108.24  E-value: 3.94e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    691 NSIIIADAQqpdMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLRSYRKDGSLFWN 770
Cdd:pfam13426    2 DGILVLDPE---GRIVYANPAALRLLGYTREELLGKSIRDLFGPGTDEEAVARLREALRNGGEVEVELELRRKDGEPFPV 78
                           90       100
                   ....*....|....*....|....*.
gi 56752384    771 QISLAPVRDQKGHLTHMVASQTDVSE 796
Cdd:pfam13426   79 LVSASPVRDEDGEVVGIVGILRDITE 104
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
573-666 4.21e-14

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 70.10  E-value: 4.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    573 IWYSANYSRLFGGEEKEITQKLVQtvdlqWRDRLDPDQRERIMASLSGAIANGFSTWSEQYRFLRQDGTYAHVLDRGYIV 652
Cdd:pfam08447    2 IYWSPRFEEILGYTPEELKSSYEG-----WLDLVHPEDRERVRRALQELLLKKGEPYSGEYRIRRKDGSYRWVEARGRPI 76
                           90
                   ....*....|....
gi 56752384    653 RDENGRAIRAVGAM 666
Cdd:pfam08447   77 RDENGKPVRVIGVA 90
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
331-557 5.05e-06

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 47.92  E-value: 5.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  331 PIYIKDYRGEILLQNRACLDLQPFVMPEVIKQEDIND----------LATIASGLPIINEEWTINPENWPSQHFLISKVP 400
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEELLGLLLALHpedrdrlrelLRRLLAGEELLSEELRLVRKDGEERWVELSAAP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  401 LRNELGQILGLLGIRRNvTRWRRAEQARNALSDQLEQTLAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWD 480
Cdd:COG2202   81 LRDGEGRVLGLLGLRDI-TERKRAEEALRESEERLRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSD 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56752384  481 LFPVELGATLQSELQPLqhqsstrtfELWIDPLSTCWEVNVHRSTAEISLYFRDISDRVMSRQLLEEMAERFQLVTR 557
Cdd:COG2202  160 LIHPEDEERRELELARA---------LAEGRGGPLEIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITE 227
PRK10060 PRK10060
RNase II stability modulator; Provisional
787-1232 4.26e-114

RNase II stability modulator; Provisional


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 373.25  E-value: 4.26e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   787 MVASQTDVSESKAFEEMLLQQATHDALTGLPNRLLFLDRLDQAAARArgGGSPIAVLFIDLDNFKAINDGFSHSEGDAVL 866
Cdd:PRK10060  216 LICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLL 293
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   867 QIAAGRLQQCIQEHETVARLSSDEFVILLTDLDvQSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDGQSGSE 946
Cdd:PRK10060  294 QDVSLAILSCLEEDQTLARLGGDEFLVLASHTS-QAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSES 372
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   947 LLQAADLAVCAAKQQGKNLWCSFSEAMREQLRSRIDIEKDLRQALIDNSLELYFQPQVDLvTHRLLGFETLVRWNHPERG 1026
Cdd:PRK10060  373 LIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERG 451
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1027 LVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWIDhEGFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIE 1106
Cdd:PRK10060  452 LIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRD-KGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVE 530
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1107 LTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVL 1186
Cdd:PRK10060  531 LTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQAL 610
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 56752384  1187 KLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPEAEALAFLHR 1232
Cdd:PRK10060  611 NLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
COG5001 COG5001
Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain ...
785-1225 1.34e-97

Predicted signal transduction protein containing a membrane domain, an EAL and a GGDEF domain [Signal transduction mechanisms]


Pssm-ID: 227334 [Multi-domain]  Cd Length: 663  Bit Score: 327.62  E-value: 1.34e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  785 THMVASQTDVS----ESKAFEEMLLQQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHS 860
Cdd:COG5001  201 SDMVQSQVTLTqraeETRRLSDENDRLANLDSLTGLPNRRRFFAELDARLAAARQSGRRLVLGVIDLDGFKPVNDAFGHA 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  861 EGDAVLQIAAGRLQQCIQEHETVARLSSDEFVILLTDL-DVQSKARVKAAMIQSLMAkPFEVMGNPIELTASIGVATFPH 939
Cdd:COG5001  281 TGDRLLIEVGRRLKAFDGAPILAARLGGDEFALIIPALeDDALRVAGARALCESLQA-PYDLRGVRVQVGASIGIAPFPS 359
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  940 DGQSGSELLQAADLAVCAAKQQGKNLWCSFSEAMREQLRSRIDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVR 1019
Cdd:COG5001  360 GADTSEQLFERADYALYHAKQNGKGAAVLFDARHEAAIRDMAVVEQALRSADLEQELSVHFQPIVDIVSGKTIALEALAR 439
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1020 WNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWIDhegfTGSLSFNISARQFIRQNIFLKLFDVLQEFQIP 1099
Cdd:COG5001  440 WHSPEIGPVPPDVFIGIAERSGQIVELTRLLLAKALREARAWPM----DVRVSINLSARDLASMENVRRLLAIVSESCIA 515
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1100 PHQLEIELTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAI 1179
Cdd:COG5001  516 PHRLDFEITETAIVCDFDQARDALAALHELGVRTALDDFGTGYSSLSHLRALPLDKIKIDRSFVSDLEENPTSEDIVRTV 595
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 56752384 1180 VAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPEAE 1225
Cdd:COG5001  596 LQLGRNLRMECVVEGVETEAQRDRVAALGATVMQGYHYARPMPAEE 641
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
785-1237 9.88e-90

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 309.01  E-value: 9.88e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   785 THMVASQTDVSESKAFEEMLLQqatHDALTGLPNRLLFLDRLDQAAARARgggsPIAVLFIDLDNFKAINDGFSHSEGDA 864
Cdd:PRK11359  356 QHLAALALEQEKSRQHIEQLIQ---FDPLTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHFQDVIDSLGYAWADQ 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   865 VLQIAAGRLQQCIQEHETVARLSSDEFVILLTDLDVqSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVAtfpHDGQSG 944
Cdd:PRK11359  429 ALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDV-SNITQIADELRNVVSKPIMIDDKPFPLTLSIGIS---YDVGKN 504
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   945 SE-LLQAADLAVCAAKQQGKNLWCSFSEAMREQLRSRIDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHP 1023
Cdd:PRK11359  505 RDyLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDP 584
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1024 ERGLVAPGEFIPIAEESDLIDAIGLWVMRAAGLTLRRWIDHEGFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQL 1103
Cdd:PRK11359  585 LHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQL 664
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1104 EIELTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMA 1183
Cdd:PRK11359  665 TVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIG 744
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 56752384  1184 KVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPEAEALAFLhRSASPG 1237
Cdd:PRK11359  745 QSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWM-SSVLPL 797
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
519-1228 1.31e-88

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 311.22  E-value: 1.31e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   519 VNVHRSTAEISLYF----RDISDRVMSRQLLEEMAERFQLVTRATNDAVWDRNLLTNEIWYSANYSRLFGgeekeITQKL 594
Cdd:PRK09776  375 VSLVRDTDGTPLYFiaqiEDINELKRTEQVNERLMERITLANEAGGIGIWEWDLKPNIISWDKRMFELYE-----IPPHI 449
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   595 VQTVDlQWRDRLDPDQRERIMASLSGAIAnGFSTWSEQYRFLRQDGTYaHVLDRGYIVRDENGRAIRAVGAMQDISAIVA 674
Cdd:PRK09776  450 KPTWQ-VWYACLHPEDRQRVEKEIRDALQ-GRSPFKLEFRIVVKDGVR-HIRALANRVLNKDGEVERLLGINMDMTEVRQ 526
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   675 ANEQL-----RLWLrAIESTGNSIIIADAqqpDMPIIYVNPAFEKITGFSAAEVIG----RNFRFL---QGLETQQAELE 742
Cdd:PRK09776  527 LNEALfqekeRLHI-TLDSIGEAVVCTDM---AMKVTFMNPVAEKMTGWTQEEALGvpllTVLHITfgdNGPLMENIYSC 602
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   743 EMRRA---LEEGtyceVTLRSyrKDGSLFWNQISLAPVRDQKGHLTHMVASQTDVSESKAFEEMLLQQATHDALTGLPNR 819
Cdd:PRK09776  603 LTSRSaayLEQD----VVLHC--RSGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANR 676
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   820 LLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLSSDEFVILLTDLD 899
Cdd:PRK09776  677 ASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCN 756
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   900 VQSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQGKNLwCSFSEAMREQLRS 979
Cdd:PRK09776  757 VESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGR-VTVYEPQQAAAHS 835
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   980 R---IDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAAgl 1056
Cdd:PRK09776  836 EhraLSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEF-- 913
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1057 tLRRWIDHEGFTG-SLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESPERFVQWLQEARSMGFQVAL 1135
Cdd:PRK09776  914 -FRQAAKAVASKGlSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVL 992
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1136 DDFGTGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGF 1215
Cdd:PRK09776  993 SDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGY 1072
                         730
                  ....*....|...
gi 56752384  1216 FYGPPLPEAEALA 1228
Cdd:PRK09776 1073 AIARPQPLDLLLN 1085
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
797-1225 7.43e-81

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 279.29  E-value: 7.43e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   797 SKAFEEMLlQQATHDALTGLPNRLLFLDRLDQAAARarggGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQC 876
Cdd:PRK13561  221 QRQYEEQS-RNATRFPVSDLPNKALLMALLEQVVAR----KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSV 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   877 IQEHETVARLSSDEFVILLTDLDVQSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFpHDGQSGSELLQAADLAVC 956
Cdd:PRK13561  296 LSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAF 374
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   957 AAKQQGKNLWCSFSEAMREQLRSRIDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPI 1036
Cdd:PRK13561  375 TARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDR 454
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1037 AEESDLIDAIGLWVMRAAGLTLRRWIDHeGFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESP 1116
Cdd:PRK13561  455 IESCGLMVTVGHWVLEESCRLLAAWQER-GIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDP 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1117 ERFVQWLQEARSMGFQVALDDFGTGYSSLGYL---KRLPINALKIDRSFIRDLPhdhDDQAIVQAIVAMAKVLKLRTIAE 1193
Cdd:PRK13561  534 HAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLP---EDDSMVAAIIMLAQSLNLQVIAE 610
                         410       420       430
                  ....*....|....*....|....*....|..
gi 56752384  1194 GVERLEQAAFLEAIGCDAVQGFFYGPPLPEAE 1225
Cdd:PRK13561  611 GVETEAQRDWLLKAGVGIAQGFLFARALPIEI 642
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
797-1228 5.96e-75

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 262.57  E-value: 5.96e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   797 SKAFEEMLlQQATHDALTGLPNRLLFLDRLDQAAArARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQC 876
Cdd:PRK11829  222 ADAYADMG-RISHRFPVTELPNRSLFISLLEKEIA-SSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQC 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   877 IQEHETVARLSSDEFVILLTDLDVQSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLAVC 956
Cdd:PRK11829  300 IDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMM 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   957 AAKQQGKNLWCSFSEAMREQLRSRIDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPI 1036
Cdd:PRK11829  380 AAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHF 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1037 AEESDLIDAIGLWVMRAAGLTLRRWiDHEGFTGSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIESP 1116
Cdd:PRK11829  460 AEEEGMMVPLGNWVLEEACRILADW-KARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDL 538
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1117 ERFVQWLQEARSMGFQVALDDFGTGYSSLGYL---KRLPINALKIDRSFIRDLPhdhDDQAIVQAIVAMAKVLKLRTIAE 1193
Cdd:PRK11829  539 DEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAE 615
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 56752384  1194 GVERLEQAAFLEAIGCDAVQGFFYGPPLPEAEALA 1228
Cdd:PRK11829  616 GVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEFEA 650
COG4943 COG4943
Predicted signal transduction protein containing sensor and EAL domains [Signal transduction ...
977-1236 6.94e-53

Predicted signal transduction protein containing sensor and EAL domains [Signal transduction mechanisms]


Pssm-ID: 227279 [Multi-domain]  Cd Length: 524  Bit Score: 195.34  E-value: 6.94e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  977 LRSRIDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLIDAIGLWVMRAA-- 1054
Cdd:COG4943  263 RRRYLSPRRRLQRAIERRELCVHYQPIVDLATGKCVGAEALARWPQEDGTVVSPDVFIPLAEESGMIEQITDYVIRNVfr 342
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1055 --GLTLRRwidHEGFtgSLSFNISARQFIRQNIFLKLFDVLQEFQIPPHQLEIELTESSLIEsPERFVQWLQEARSMGFQ 1132
Cdd:COG4943  343 dlGDLLRQ---HRDL--HVSINLSASDLASPRLIDRLNRKLAQYQVRPQQIALELTERTFAD-PKKMTPIILRLREAGHE 416
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1133 VALDDFGTGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAV 1212
Cdd:COG4943  417 IYIDDFGTGYSNLHYLQSLPVDALKIDKSFVDTLGTDSASHLIAPHIIEMAKSLGLKIVAEGVETEEQVDWLRKRGVHYG 496
                        250       260
                 ....*....|....*....|....
gi 56752384 1213 QGFFYGPPLPEAEALAFLHRSASP 1236
Cdd:COG4943  497 QGWLFSKALPAQAFLDWAEQQPAR 520
PRK13558 PRK13558
bacterio-opsin activator; Provisional
675-801 7.50e-38

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 150.76  E-value: 7.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   675 ANEQLRLWLRAIESTGNSIIIADAQQPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYC 754
Cdd:PRK13558  143 VESDRRLKERALDEAPVGITIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAELREAIDEERPT 222
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 56752384   755 EVTLRSYRKDGSLFWNQISLAPVRDQKGHLTHMVASQTDVSESKAFE 801
Cdd:PRK13558  223 SVELRNYRKDGSTFWNQVDIAPIRDEDGTVTHYVGFQTDVTERKEAE 269
PRK13559 PRK13559
hypothetical protein; Provisional
680-833 4.53e-33

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 132.63  E-value: 4.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   680 RLWLRAIESTGNSIIIADAQQPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLR 759
Cdd:PRK13559   43 RLFEQAMEQTRMAMCITDPHQPDLPIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIRAAIAAEREIVVELL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   760 SYRKDGSLFWNQISLAPVRDQKGHLTHMVASQTDVSESKAFEEM------LLQQATH---------DALTGLPNRL---- 820
Cdd:PRK13559  123 NYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAVRALeaherrLAREVDHrsknvfavvDSIVRLTGRAddps 202
                         170
                  ....*....|....*.
gi 56752384   821 LFLDRLD---QAAARA 833
Cdd:PRK13559  203 LYAAAIQervQALARA 218
PRK10551 PRK10551
phage resistance protein; Provisional
977-1236 1.96e-32

phage resistance protein; Provisional


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 132.42  E-value: 1.96e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   977 LRSRIDIEKDLRQALIDNSLELYFQPQVDLVTHRLLGFETLVRWNHPERGLVAPGEFIPIAEESDLI------------- 1043
Cdd:PRK10551  258 LSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIvpltqhlfeliar 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1044 DAIGLWVMRAAGLtlrrwidhegftgSLSFNISARQFIRQNiFLKlfDVLQEF-QIPPHQLEI--ELTESSLI---ESPE 1117
Cdd:PRK10551  338 DAAELQKVLPVGA-------------KLGINISPAHLHSDS-FKA--DVQRLLaSLPADHFQIvlEITERDMVqeeEATK 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1118 RFvQWLQEArsmGFQVALDDFGTGYSSLGYLKRLPINALKIDRSFIRDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVER 1197
Cdd:PRK10551  402 LF-AWLHSQ---GIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVET 477
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 56752384  1198 LEQAAFLEAIGCDAVQGFFYGPPLPEAEALAFLHRSASP 1236
Cdd:PRK10551  478 PEQARWLRERGVNFLQGYWISRPLPLEDFVRWLKEPYTP 516
PleD COG3706
Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal ...
798-964 2.88e-32

Response regulator containing a CheY-like receiver domain and a GGDEF domain [Signal transduction mechanisms]


Pssm-ID: 226229 [Multi-domain]  Cd Length: 435  Bit Score: 131.29  E-value: 2.88e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  798 KAFEEMLLQQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCI 877
Cdd:COG3706  260 RESLERLQELALVDGLTGLFNRRYFDEHLADLWKRALREGRPLSLLMLDIDDFKEINDTYGHDVGDEVLRQVARRLRQTV 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  878 QEHETVARLSSDEFVILLTDLDvQSKARVKAAMIQ---SLMAKPFEVMGNPIELTASIGVATFPHDGQSGSELLQAADLA 954
Cdd:COG3706  340 RGLDLVARYGGEEFAVVLPDTD-LEAAIAIAERIRqkiNELPFVHELSREPLEVTISIGVAEGKPGEDSIEELLKRADKA 418
                        170
                 ....*....|
gi 56752384  955 VCAAKQQGKN 964
Cdd:COG3706  419 LYKAKASGRN 428
PRK13557 PRK13557
histidine kinase; Provisional
685-815 7.43e-31

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 127.86  E-value: 7.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   685 AIESTGNSIIIADAQQPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLRSYRKD 764
Cdd:PRK13557   35 AVETTRMPMIVTDPNQPDNPIVFANRAFLEMTGYAAEEIIGNNCRFLQGPETDRATVAEVRDAIAERREIATEILNYRKD 114
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 56752384   765 GSLFWNQISLAPVRDQKGHLTHMVASQTDVSESKAFEEMLLQQATHDA---LTG 815
Cdd:PRK13557  115 GSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALRQAQKMEAlgqLTG 168
pleD PRK09581
response regulator PleD; Reviewed
805-964 2.69e-29

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 122.32  E-value: 2.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   805 LQQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVA 884
Cdd:PRK09581  289 IEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIA 368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   885 RLSSDEFVILLTDLDVQSKARVkAAMIQSLMAK-PFEVMG--NPIELTASIGVATFPHDGQSGSELLQAADLAVCAAKQQ 961
Cdd:PRK09581  369 RYGGEEFVVVMPDTDIEDAIAV-AERIRRKIAEePFIISDgkERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNT 447

                  ...
gi 56752384   962 GKN 964
Cdd:PRK09581  448 GRN 450
PRK15426 PRK15426
putative diguanylate cyclase YedQ; Provisional
772-972 3.82e-27

putative diguanylate cyclase YedQ; Provisional


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 116.65  E-value: 3.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   772 ISLAPVRdqkGHLTHMVASQtdvseskafeEMLLQQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFK 851
Cdd:PRK15426  375 ISWYVIR---RMVSNMFVLQ----------SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFK 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   852 AINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLSSDEFVILLTDLDVQSKARVKAAMIQSLMAKPFEVMGN-PIELTA 930
Cdd:PRK15426  442 SINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKStTIRISA 521
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 56752384   931 SIGVATFPHDGQSGSELLQA-ADLAVCAAKQQGKNLWCSFSEA 972
Cdd:PRK15426  522 SLGVSSAEEDGDYDFEQLQSlADRRLYLAKQAGRNRVCASDNA 564
PRK11059 PRK11059
regulatory protein CsrD; Provisional
784-1223 1.08e-24

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 109.57  E-value: 1.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   784 LTHMVASQTDVSESKA-FEEMLLQQATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEG 862
Cdd:PRK11059  203 LDHLLSELQDAREERSrFDTFIRSNAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   863 DAVLQIAAGRLQQCIQEHETV--ARLSSDEFVILLTDLDVQSKARVKAAMIQSLMAKPFEVMGNPIELTaSIGVATFpHD 940
Cdd:PRK11059  283 EELLFELINLLSTFVMRYPGAllARYSRSDFAVLLPHRSLKEADSLASQLLKAVDALPPPKMLDRDDFL-HIGICAY-RS 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   941 GQSGSELLQAADLAVCAAKQQGKNLWCSFSEAMREQL-----RSRIDIEkdlrQALIDNSLELYFQPQVDL---VTHRll 1012
Cdd:PRK11059  361 GQSTEQVMEEAEMALRSAQLQGGNGWFVYDKAQLPEKgrgsvRWRTLLE----QTLVRGGPRLYQQPAVTRdgkVHHR-- 434
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1013 gfETLVRWNHPERGLVAPGEFIPIAEESDLIDAIG-LWVMRAAGLtLRRWIDHegftgSLSFNISA-----RQFIRQnif 1086
Cdd:PRK11059  435 --ELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDrQVIERVLPL-LRYWPEE-----NLSINLSVdsllsRAFQRW--- 503
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1087 lkLFDVLqeFQIPPHQLE---IELTESSLIESPERFVQWLQEARSMGFQVALDDFGTGYSSLGYLKRLPINALKIDRSFI 1163
Cdd:PRK11059  504 --LRDTL--LQCPRSQRKrliFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLV 579
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  1164 RDLPHDHDDQAIVQAIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPPLPE 1223
Cdd:PRK11059  580 RNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
PRK09894 PRK09894
diguanylate cyclase; Provisional
808-964 5.15e-22

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 97.83  E-value: 5.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   808 ATHDALTGLPNRLLFLDRLDQAaaRARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLS 887
Cdd:PRK09894  129 SNMDVLTGLPGRRVLDESFDHQ--LRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYG 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 56752384   888 SDEFVILLTDLDVQSKARVKAAMIQSLMAKPFEVMGNPIELTASIGVATFpHDGQSGSELLQAADLAVCAAKQQGKN 964
Cdd:PRK09894  207 GEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRA-FPEETLDVVIGRADRAMYEGKQTGRN 282
PRK09966 PRK09966
putative inner membrane diguanylate cyclase; Provisional
804-961 6.60e-18

putative inner membrane diguanylate cyclase; Provisional


Pssm-ID: 182171 [Multi-domain]  Cd Length: 407  Bit Score: 86.21  E-value: 6.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   804 LLQQATHDALTGLPNRLLFLDRLDqAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETV 883
Cdd:PRK09966  244 LLRTALHDPLTGLANRAAFRSGIN-TLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKA 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   884 ARLSSDEFVILLTDLDVQSKARVKAAMIQSLMAKPFEVM-GNPIELTASIGVA-TFPHdgQSGSELLQAADLAVCAAKQQ 961
Cdd:PRK09966  323 YRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAmTIEH--ASAEKLQELADHNMYQAKHQ 400
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
682-804 3.13e-17

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: 232884 [Multi-domain]  Cd Length: 124  Bit Score: 80.02  E-value: 3.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    682 WLRAI-ESTGNSIIIADaqqPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALE-EGTYCEVTLR 759
Cdd:TIGR00229    4 RYRAIfESSPDAIIVID---LEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEgEREPVSEERR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 56752384    760 SYRKDGSLFWNQISLAPVRDQKGHlTHMVASQTDVSESKAFEEML 804
Cdd:TIGR00229   81 VRRKDGSEIWVEVSVSPIRTNGGE-LGVVGIVRDITERKQAEEAL 124
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
562-801 1.01e-14

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 74.50  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  562 AVWDRNLLTNEIWYSANYSRLFGGEEKEItqklvqtvdLQWRDRLDPDQRERIMAsLSGAIANGFSTWSEQYRFLRQDGT 641
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEEL---------LGLLLALHPEDRDRLRE-LLRRLLAGEELLSEELRLVRKDGE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  642 YAHVLDRGYIVRDENGRAIRAVGAMQD---ISAIVAANEQLRLWLRAIESTGNSIIIADaqqPDMPIIYVNPAFEKITGF 718
Cdd:COG2202   71 ERWVELSAAPLRDGEGRVLGLLGLRDIterKRAEEALRESEERLRALLEASPDGIWVLD---EDGRILYANPAAEELLGY 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  719 SAAEVIGRNFRFLQGLETQQAELEEMRRAL--EEGTYCEVTLRSYRKDGS-LFWNQISLAPVRDQkGHLTHMVASQTDVS 795
Cdd:COG2202  148 SPEEELGRGLSDLIHPEDEERRELELARALaeGRGGPLEIEYRVRRKDGErVRWILSRISPVRDD-GEIVGVVGIARDIT 226

                 ....*.
gi 56752384  796 ESKAFE 801
Cdd:COG2202  227 ERKQAE 232
PRK13560 PRK13560
hypothetical protein; Provisional
413-802 8.93e-11

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 65.08  E-value: 8.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   413 GIRRNVTRWRRAEQArnaLSDQL---EQTLAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWDLFPVELGAT 489
Cdd:PRK13560  184 GFAEDITERKRAEER---IDEALhflQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADD 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   490 LQSELQPLQHQSSTRTFELWI---DPLSTCWEVNVHRST--------AEISLYFRDISDRVMSRQLLEEMAERFQLVTRA 558
Cdd:PRK13560  261 YQEADAAKFDADGSQIIEAEFqnkDGRTRPVDVIFNHAEfddkenhcAGLVGAITDISGRRAAERELLEKEDMLRAIIEA 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   559 TNDAVWDRNLLTNEIWYSANYS-RLFGGEEKEITQKLVQTVDLQWRDRL--------DPDQRERIMASLSGA--IANGFS 627
Cdd:PRK13560  341 APIAAIGLDADGNICFVNNNAAeRMLGWSAAEVMGKPLPGMDPELNEEFwcgdfqewYPDGRPMAFDACPMAktIKGGKI 420
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   628 TWSEQYRFLRQDGTYAHVLDRGYIVRDENGRAIRAVGAMQDISAIVAANEQLRLWLRAIESTGNSIIIADAqQPDMPIIY 707
Cdd:PRK13560  421 FDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLANLIVENSPLVLFRWKA-EEGWPVEL 499
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   708 VNPAFEKItGFSAAEVIG--RNFRFL---QGLETQQAELEEM-RRALEEgtyCEVTLRSYRKDGSLFWNQISLAPVRDQK 781
Cdd:PRK13560  500 VSKNITQF-GYEPDEFISgkRMFAAIihpADLEQVAAEVAEFaAQGVDR---FEQEYRILGKGGAVCWIDDQSAAERDEE 575
                         410       420
                  ....*....|....*....|.
gi 56752384   782 GHLTHMVASQTDVSESKAFEE 802
Cdd:PRK13560  576 GQISHFEGIVIDISERKHAEE 596
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
705-807 8.99e-10

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions].


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 61.07  E-value: 8.99e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    705 IIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLRSYRKDGSLFWNQISLAPVRDQKGHL 784
Cdd:TIGR02938   26 ILYANDAFTRITGYTKEEIIGKNESVLSNHTTPPEVYQALWGSLAEQKPWAGKLLNRRKDGELYLAELTVAPVLNEAGET 105
                           90       100
                   ....*....|....*....|...
gi 56752384    785 THMVASQTDVSESKAFEEMLLQQ 807
Cdd:TIGR02938  106 THFLGMHRDITELHRLEQVVANQ 128
adrA PRK10245
diguanylate cyclase AdrA; Provisional
808-964 1.98e-09

diguanylate cyclase AdrA; Provisional


Pssm-ID: 182329 [Multi-domain]  Cd Length: 366  Bit Score: 59.46  E-value: 1.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   808 ATHDALTGLPNRLLFLDRLDQAAARARGGGSPIAVLFIDLDNFKAINDGFSHSEGDAVLQIAAGRLQQCIQEHETVARLS 887
Cdd:PRK10245  205 STRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFG 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   888 SDEFVILLTDLDVQSKARVKAAMIQSLMAkpFEVMGNP-IELTASIGVAtfPHDGQSG--SELLQAADLAVCAAKQQGKN 964
Cdd:PRK10245  285 GDEFAVIMSGTPAESAITAMSRVHEGLNT--LRLPNAPqVTLRISVGVA--PLNPQMShyREWLKSADLALYKAKNAGRN 360
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
445-675 4.97e-09

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 56.78  E-value: 4.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  445 GVVVLDQNFVVRALNSQAAQQLKKTSEQIIGrVFWDLFPVELGATLQSELQPLQHQSSTRTFELWIDPLSTCWEVNVHRS 524
Cdd:COG2202    1 LILVLDRDGRIIYANEAAEELLGYSAEELLG-LLLALHPEDRDRLRELLRRLLAGEELLSEELRLVRKDGEERWVELSAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  525 T-------AEISLYFRDISDRVMSRQLLEEMAERFQLVTRATNDAVWDRNLLTNEIWYSANYSRLFGGEEKEITQKLVQT 597
Cdd:COG2202   80 PlrdgegrVLGLLGLRDITERKRAEEALRESEERLRALLEASPDGIWVLDEDGRILYANPAAEELLGYSPEEELGRGLSD 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56752384  598 VDLQWRDRLDPDQRERIMASLSGAIangfstWSEQYRFLRQDGTYAHVLDRGYIVRDENGRAIRAVGAMQDISAIVAA 675
Cdd:COG2202  160 LIHPEDEERRELELARALAEGRGGP------LEIEYRVRRKDGERVRWILSRISPVRDDGEIVGVVGIARDITERKQA 231
PRK13560 PRK13560
hypothetical protein; Provisional
321-680 4.26e-08

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 56.22  E-value: 4.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   321 LRRILEAIPDPIYIKDYRGEILLQNRACLDLQPFVMPEVIKQEdINDLATI---------------ASGLPIINEEWTIN 385
Cdd:PRK13560  206 LQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMS-IHDFAPAqpaddyqeadaakfdADGSQIIEAEFQNK 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   386 PENWPSQHFLISKVPLRNELGQILGLLGIRRNVTRWRRAEQARNALSDQLEQTLAAVSDGVVVLDQNFVVRALNSQAAQQ 465
Cdd:PRK13560  285 DGRTRPVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPIAAIGLDADGNICFVNNNAAER 364
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   466 -LKKTSEQIIGRVFWDLFPvelgatlqselqPLQHQSSTRTFELWIDPLSTCW-------------------EVNVHR-- 523
Cdd:PRK13560  365 mLGWSAAEVMGKPLPGMDP------------ELNEEFWCGDFQEWYPDGRPMAfdacpmaktikggkifdgqEVLIERed 432
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   524 -STAEISLYFRDISDR----VMSRQLLEEMAERFQL--VTRATNDAVWDRNLL-----TNEIW----YSANYSRlFGGEE 587
Cdd:PRK13560  433 dGPADCSAYAEPLHDAdgniIGAIALLVDITERKQVeeQLLLANLIVENSPLVlfrwkAEEGWpvelVSKNITQ-FGYEP 511
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   588 KEITQKLVQTVDLqwrdrLDPDQRERIMASLSGAIANGFSTWSEQYRFLRQDGTYAHVLDRGYIVRDENGRAIRAVGAMQ 667
Cdd:PRK13560  512 DEFISGKRMFAAI-----IHPADLEQVAAEVAEFAAQGVDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVI 586
                         410
                  ....*....|...
gi 56752384   668 DISAIVAANEQLR 680
Cdd:PRK13560  587 DISERKHAEEKIK 599
PAS_9 pfam13426
PAS domain;
573-671 5.38e-08

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 52.39  E-value: 5.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    573 IWYSANYSRLFGGEEKEITQKlvqtvdlQWRDRLDPDQRERIMASLSGAIANGfSTWSEQYRFLRQDGTYAHVLDRGYIV 652
Cdd:pfam13426   14 VYANPAALRLLGYTREELLGK-------SIRDLFGPGTDEEAVARLREALRNG-GEVEVELELRRKDGEPFPVLVSASPV 85
                           90
                   ....*....|....*....
gi 56752384    653 RDENGRAIRAVGAMQDISA 671
Cdd:pfam13426   86 RDEDGEVVGIVGILRDITE 104
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
684-782 7.55e-08

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 250275 [Multi-domain]  Cd Length: 111  Bit Score: 52.02  E-value: 7.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    684 RAIESTGNSIIIADAqqpDMPIIYVNPAFEKITGFSAAEVIGRNFR--FLQGLETQQAELEEMRRALEEGTYCEVTLRsy 761
Cdd:pfam00989    5 AILESLPDGIFVVDE---DGRILYVNAAAEELLGLSREEVIGKSLLdlIPEEDDAVAELLRQALLQGEESRGFEVSFR-- 79
                           90       100
                   ....*....|....*....|.
gi 56752384    762 RKDGSLFWNQISLAPVRDQKG 782
Cdd:pfam00989   80 VRDGRPRHVEVRASPVRDAGG 100
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
705-789 2.63e-07

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254805 [Multi-domain]  Cd Length: 90  Bit Score: 50.07  E-value: 2.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    705 IIYVNPAFEKITGFSAAEVIGRNFRFLQGL--ETQQAELEEMRRA-LEEGTYCEVTLRSYRKDGSLFWNQISLAPVRDQK 781
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELKSSYEGWLDLVhpEDRERVRRALQELlLKKGEPYSGEYRIRRKDGSYRWVEARGRPIRDEN 80

                   ....*...
gi 56752384    782 GHLTHMVA 789
Cdd:pfam08447   81 GKPVRVIG 88
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
687-799 6.55e-07

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 48.95  E-value: 6.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    687 ESTGNSIIIADaqqPDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRALEEGTYCEVTLRsYRKDGS 766
Cdd:pfam08448    2 DSLPDALAVLD---PDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEE-LLLNGE 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 56752384    767 LFWNQISLAPVRDQKGHLTHMVASQTDVSESKA 799
Cdd:pfam08448   78 ERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
439-539 9.05e-06

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 45.48  E-value: 9.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    439 LAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWDLFPVELGATLQSELQPL--QHQSSTRTFELwIDPLSTC 516
Cdd:pfam08448    1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRAleGEEPIDFLEEL-LLNGEER 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 56752384    517 -WEVNVHRSTAE------ISLYFRDISDRV 539
Cdd:pfam08448   80 hYELRLTPLRDPdgevigVLVISRDITERR 109
PRK11360 PRK11360
sensory histidine kinase AtoS; Provisional
653-807 1.60e-05

sensory histidine kinase AtoS; Provisional


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 47.66  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   653 RDENGRAIRAVGAM-QDISAIVAANEQLrlwlraIESTGNSIIIADAQQPdmpIIYVNPAFEKITGFSAAEVIGRNFRFL 731
Cdd:PRK11360  240 PGELGEISQAINNLaQALRETRSLNELI------LESIADGVIAIDRQGK---ITTMNPAAEVITGLQRHELVGKPYSEL 310
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 56752384   732 QGLETQQAELeeMRRALEEGTYC-EVTLRSYRKDGSLfwnQISL--APVRDQKGHLTHMVASQTDVSESKAFEEMLLQQ 807
Cdd:PRK11360  311 FPPNTPFASP--LLDTLEHGTEHvDLEISFPGRDRTI---ELSVstSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQ 384
PRK13560 PRK13560
hypothetical protein; Provisional
534-806 2.67e-05

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 46.97  E-value: 2.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   534 DISDRVMSRQLLEEMAERFQLVTRATNDAVWDRNLLTNEIWYSANYSRLFGGEEKEITQKLVQtvdlqwrdRLDPDQRER 613
Cdd:PRK13560  188 DITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIH--------DFAPAQPAD 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   614 IMASLSGAI--ANGFSTWSEQYRflRQDGTYAHV---LDRGYIVRDENgRAIRAVGAMQDISAIVAANEQLRL---WLRA 685
Cdd:PRK13560  260 DYQEADAAKfdADGSQIIEAEFQ--NKDGRTRPVdviFNHAEFDDKEN-HCAGLVGAITDISGRRAAERELLEkedMLRA 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   686 I-ESTGNSIIIADAqqpDMPIIYV-NPAFEKITGFSAAEVIG----------------RNFR-FLQGLETQQAELEEMRR 746
Cdd:PRK13560  337 IiEAAPIAAIGLDA---DGNICFVnNNAAERMLGWSAAEVMGkplpgmdpelneefwcGDFQeWYPDGRPMAFDACPMAK 413
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 56752384   747 ALEEGTYCE-VTLRSYRKDGSLFWNQISLAPVRDQKGHLTHMVASQTDVSESKAFEEMLLQ 806
Cdd:PRK13560  414 TIKGGKIFDgQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLL 474
PAS_9 pfam13426
PAS domain;
443-510 2.82e-05

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 43.91  E-value: 2.82e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 56752384    443 SDGVVVLDQNFVVRALNSQAAQQLKKTSEQIIGRVFWDLFPVELGATLQSELQPLQHQSSTRTFELWI 510
Cdd:pfam13426    1 PDGILVLDPEGRIVYANPAALRLLGYTREELLGKSIRDLFGPGTDEEAVARLREALRNGGEVEVELEL 68
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
708-808 1.21e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 45.05  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   708 VNPAFEKITGFSAAEVIGRNFRFLQGLETQQAELEEMRRAL--EEGTYcEVTLRSYRKDGSLFWNQISLAPVRDQKGHLT 785
Cdd:PRK09776  308 VNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLsgEINSY-SMEKRYYRRDGEVVWALLAVSLVRDTDGTPL 386
                          90       100
                  ....*....|....*....|...
gi 56752384   786 HMVASQTDVSESKAFEEMLLQQA 808
Cdd:PRK09776  387 YFIAQIEDINELKRTEQVNERLM 409
AtoS COG2202
FOG: PAS/PAC domain [Signal transduction mechanisms]
234-425 4.39e-04

FOG: PAS/PAC domain [Signal transduction mechanisms]


Pssm-ID: 225112 [Multi-domain]  Cd Length: 232  Bit Score: 42.14  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  234 WLEHFQLSDRLRLEQAIDTGMQTGRPIQATYALASDSQDRQLVELRAVIVRDLAGNVRSLRGVLEPKHQAPLtsLEPLPL 313
Cdd:COG2202   32 LLLALHPEDRDRLRELLRRLLAGEELLSEELRLVRKDGEERWVELSAAPLRDGEGRVLGLLGLRDITERKRA--EEALRE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  314 SLDHpavLRRILEAIPDPIYIKDYRGEILLQNRACLDL-------------QPFVMPEVIKQEDINDLATIASG--LPII 378
Cdd:COG2202  110 SEER---LRALLEASPDGIWVLDEDGRILYANPAAEELlgyspeeelgrglSDLIHPEDEERRELELARALAEGrgGPLE 186
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 56752384  379 NEEWTINPENWPSQHFLISKVPLRNElGQILGLLGIRRNVTRWRRAE 425
Cdd:COG2202  187 IEYRVRRKDGERVRWILSRISPVRDD-GEIVGVVGIARDITERKQAE 232
PRK13560 PRK13560
hypothetical protein; Provisional
608-807 5.77e-04

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 42.74  E-value: 5.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   608 PDQRERIMASL-----SGAIANGFSTW-SEQYRFLRQDGTYAHVLDRgyIVRDENGRaIRAVGAMQDIS----AIVAANE 677
Cdd:PRK13560  125 GDDGDFFFANPfrsaeTIAMALQSDDWqEEEGHFRCGDGRFIDCCLR--FERHAHAD-DQVDGFAEDITerkrAEERIDE 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   678 QLRLWLRAIESTGNSIIIADAqqpDMPIIYVNPAFEKITGFSAAEVIGRNFRFLQglETQQAEL-EEMRRALEEGTYCEV 756
Cdd:PRK13560  202 ALHFLQQLLDNIADPAFWKDE---DAKVFGCNDAACLACGFRREEIIGMSIHDFA--PAQPADDyQEADAAKFDADGSQI 276
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 56752384   757 TLRSYR-KDGSLFWNQISLAPVR--DQKGHLTHMVASQTDVSESKAFEEMLLQQ 807
Cdd:PRK13560  277 IEAEFQnKDGRTRPVDVIFNHAEfdDKENHCAGLVGAITDISGRRAAERELLEK 330
COG3434 COG3434
Predicted signal transduction protein containing EAL and modified HD-GYP domains [Signal ...
1099-1220 8.09e-04

Predicted signal transduction protein containing EAL and modified HD-GYP domains [Signal transduction mechanisms]


Pssm-ID: 225968 [Multi-domain]  Cd Length: 407  Bit Score: 42.01  E-value: 8.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384 1099 PPHQLEIELTESslIESPERFVQWLQEARSMGFQVALDDFgTGYSSLGYLKRLP-INALKIDrsfIRDLPHDHDDqaivq 1177
Cdd:COG3434   82 PPDKVVIEILED--CPPTEKLLSAIKELKQKGYLLALDDF-IFSNVSEWKPLLPlSDIVKID---FKRVTFDKAR----- 150
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 56752384 1178 AIVAMAKVLKLRTIAEGVERLEQAAFLEAIGCDAVQGFFYGPP 1220
Cdd:COG3434  151 LFDRDLGYINKKFLAEKVETEEEFEQAKKAGFDLFQGYFFSKP 193
PRK11360 PRK11360
sensory histidine kinase AtoS; Provisional
400-551 1.00e-03

sensory histidine kinase AtoS; Provisional


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 41.88  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   400 PLRNELGQILGllgirrnvtrwrraeqARNALSDQLEQT-------LAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSEQ 472
Cdd:PRK11360  238 PLPGELGEISQ----------------AINNLAQALRETrslneliLESIADGVIAIDRQGKITTMNPAAEVITGLQRHE 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384   473 IIGRVFWDLFPVE------LGATLQ----SELQPLQHQSSTRTFELwidPLSTCWEVNVHRSTAEISLYFRDISDRvmsR 542
Cdd:PRK11360  302 LVGKPYSELFPPNtpfaspLLDTLEhgteHVDLEISFPGRDRTIEL---SVSTSLLHNTHGEMIGALVIFSDLTER---K 375
                         170
                  ....*....|.
gi 56752384   543 QLLEEMA--ER 551
Cdd:PRK11360  376 RLQRRVArqER 386
CitA COG3290
Signal transduction histidine kinase regulating citrate/malate metabolism [Signal transduction ...
405-500 2.10e-03

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


Pssm-ID: 225827 [Multi-domain]  Cd Length: 537  Bit Score: 40.74  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  405 LGQILGLLGIRRNVTRWRRA-------EQARnaLSDQLEQTLAAVSDGVVVLDQNFVVRALNSQAAQQL--KKTSEQIIG 475
Cdd:COG3290  182 LGLLIGLLGAWILARHIKRQmlglepeEIAT--LLEERQAMLQSIKEGVIAVDKKGVITLINQAAQKLLglRQPSGDPIG 259
                         90       100
                 ....*....|....*....|....*.
gi 56752384  476 RVFWDLFPVELG-ATLQSELQPLQHQ 500
Cdd:COG3290  260 RSIVEVLPPDSDlPEVLETGKPQHDE 285
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
581-679 2.19e-03

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: 232884 [Multi-domain]  Cd Length: 124  Bit Score: 38.03  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    581 RLFGGEEKEItqklvqtVDLQWRDRLDPDQRERIMASLSGAIANGFSTWSEQYRFLRQDGTYAHVLDRGYIVRdENGRAI 660
Cdd:TIGR00229   34 EIFGYSAEEL-------IGRNVLELIPEEDREEVRERIERRLEGEREPVSEERRVRRKDGSEIWVEVSVSPIR-TNGGEL 105
                           90
                   ....*....|....*....
gi 56752384    661 RAVGAMQDISAIVAANEQL 679
Cdd:TIGR00229  106 GVVGIVRDITERKQAEEAL 124
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
325-423 2.43e-03

PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.


Pssm-ID: 254806 [Multi-domain]  Cd Length: 110  Bit Score: 37.78  E-value: 2.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    325 LEAIPDPIYIKDYRGEILLQNRACLDLQPF------------VMPEVIKQEDINDLATIASGLPIInEEWTINPENWPSQ 392
Cdd:pfam08448    1 LDSLPDALAVLDPDGRVRYANAAAAELFGLppeellgktlaeLLPPEDAARLERALRRALEGEEPI-DFLEELLLNGEER 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 56752384    393 HFLISKVPLRNELGQILGLLGIRRNVTRWRR 423
Cdd:pfam08448   80 HYELRLTPLRDPDGEVIGVLVISRDITERRR 110
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
318-512 4.13e-03

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions].


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 39.89  E-value: 4.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    318 PAVLRRILEAIPDPIYIKDYRGEILLQNRACLDLQPFVMPEVI-KQEDIndLATIASGLPIINEEWTINPENWPSQHFLI 396
Cdd:TIGR02938    3 PEAYRQTVDQAPLAISITDLKANILYANDAFTRITGYTKEEIIgKNESV--LSNHTTPPEVYQALWGSLAEQKPWAGKLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    397 SK-------------VPLRNELGQILGLLGIRRNVTRWRRAEQARNALSDQLEQTLAAVSDGVVVLDQNFVVRALNSQAA 463
Cdd:TIGR02938   81 NRrkdgelylaeltvAPVLNEAGETTHFLGMHRDITELHRLEQVVANQKLLIESVVDAAPVAFVLLDPTGRVILDNQEYK 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 56752384    464 QQLKKTSEQIIGRVFWDLFPVELGATLqSELQPlqHQSSTRTFELWIDP 512
Cdd:TIGR02938  161 KLATDLRVKEPAHTVLDLLREAWREAL-AENWP--QQLAFSNREARFDR 206
RocR COG3829
Transcriptional regulator containing PAS, AAA-type ATPase, and DNA-binding domains ...
393-490 4.47e-03

Transcriptional regulator containing PAS, AAA-type ATPase, and DNA-binding domains [Transcription / Signal transduction mechanisms]


Pssm-ID: 226350 [Multi-domain]  Cd Length: 560  Bit Score: 39.59  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384  393 HFLISKVPLRNELGQILGLLGIRRNVTRWRRAEQARNA-LSDQLEQTLAAVSDGVVVLDQNFVVRALNSQAAQQLKKTSE 471
Cdd:COG3829   76 RIVVVGKTPVDEQGRVVGVLEVFLDISEALELIEENLRqLRQRLEAILDSIDDGLLVVDEDGIIIYYNKAYAKLLGLSPE 155
                         90
                 ....*....|....*....
gi 56752384  472 QIIGRVFWDLFPVELGATL 490
Cdd:COG3829  156 EVLGKHLLDVVSAGEDSTL 174
PAS_9 pfam13426
PAS domain;
329-419 9.33e-03

PAS domain;


Pssm-ID: 257751 [Multi-domain]  Cd Length: 104  Bit Score: 35.82  E-value: 9.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56752384    329 PDPIYIKDYRGEILLQNRACLDLQPFVMPEVIKQeDINDLATIASGLPIINE-------------EWTINPENWPSQHFL 395
Cdd:pfam13426    1 PDGILVLDPEGRIVYANPAALRLLGYTREELLGK-SIRDLFGPGTDEEAVARlrealrnggevevELELRRKDGEPFPVL 79
                           90       100
                   ....*....|....*....|....
gi 56752384    396 ISKVPLRNELGQILGLLGIRRNVT 419
Cdd:pfam13426   80 VSASPVRDEDGEVVGIVGILRDIT 103
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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