NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|768329941|gb|KJH61875|]
View 

histidine kinase [Pantoea agglomerans]

Protein Classification

GGDEF and EAL domain-containing protein( domain architecture ID 10482068)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COG5001 super family cl34859
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 167-585 1.82e-90

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


The actual alignment was detected with superfamily member COG5001:

Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 293.22  E-value: 1.82e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 167 DPVTGLPNRQRLIRDLQFLAASGDTTPRRLVLIdCIDmprayeLAR------SMG--MGpvESLLKDVATLLPLRLRPAp 238
Cdd:COG5001  254 DPLTGLPNRRLFLDRLEQALARARRSGRRLALL-FID------LDRfkeindTLGhaAG--DELLREVARRLRACLREG- 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 239 gemlYTVAtgRF------ALLTRQESRLTANWVANK-LAGISA--DLgDGLSVALMTHTGEASFNTGEMPAQEILRRAVS 309
Cdd:COG5001  324 ----DTVA--RLggdefaVLLPDLDDPEDAEAVAERiLAALAEpfEL-DGHELYVSASIGIALYPDDGADAEELLRNADL 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 310 ALHEA--ITRDVASMpFSEATDTRHTQDFTLMHDLAIAIRQDkGLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPA 387
Cdd:COG5001  397 AMYRAkaAGRNRYRF-FDPEMDERARERLELEADLRRALERG-ELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPA 474

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 388 QFLPFAVQTELLSELTTWVTEHAIARLSRLRNSYIQ-LPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLgieCLE-T 465
Cdd:COG5001  475 EFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRL---ELEiT 551

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 466 ERIL--ESATAMRGLEMLKLRGFGISLDDFGTGYSNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDY 543
Cdd:COG5001  552 ESALleDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGL 631

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 768329941 544 MVLAEGVENAETVTALTEFGCDQAQGFFYSRPLPEAALDEWL 585
Cdd:COG5001  632 EVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALL 673
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 25-153 2.84e-13

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


:

Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 67.12  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   25 SRDDVLRQFVRLASQALGIPGSFISVLDDEMQHV--KAAQNFTLTQSSRQDSLCRHAVDSDSTVVVPDTLLDTRFAEHPL 102
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYlpPGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPRFLDPLL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768329941  103 IVGAPFIRFYAGVPLKsSTGLILGTLCVTDTAPhPFNADQVAMLKMLAALV 153
Cdd:pfam01590  81 LLRNFGIRSLLAVPII-DDGELLGVLVLHHPRP-PFTEEELELLEVLADQV 129
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 167-585 1.82e-90

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


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 293.22  E-value: 1.82e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 167 DPVTGLPNRQRLIRDLQFLAASGDTTPRRLVLIdCIDmprayeLAR------SMG--MGpvESLLKDVATLLPLRLRPAp 238
Cdd:COG5001  254 DPLTGLPNRRLFLDRLEQALARARRSGRRLALL-FID------LDRfkeindTLGhaAG--DELLREVARRLRACLREG- 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 239 gemlYTVAtgRF------ALLTRQESRLTANWVANK-LAGISA--DLgDGLSVALMTHTGEASFNTGEMPAQEILRRAVS 309
Cdd:COG5001  324 ----DTVA--RLggdefaVLLPDLDDPEDAEAVAERiLAALAEpfEL-DGHELYVSASIGIALYPDDGADAEELLRNADL 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 310 ALHEA--ITRDVASMpFSEATDTRHTQDFTLMHDLAIAIRQDkGLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPA 387
Cdd:COG5001  397 AMYRAkaAGRNRYRF-FDPEMDERARERLELEADLRRALERG-ELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPA 474

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 388 QFLPFAVQTELLSELTTWVTEHAIARLSRLRNSYIQ-LPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLgieCLE-T 465
Cdd:COG5001  475 EFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRL---ELEiT 551

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 466 ERIL--ESATAMRGLEMLKLRGFGISLDDFGTGYSNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDY 543
Cdd:COG5001  552 ESALleDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGL 631

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 768329941 544 MVLAEGVENAETVTALTEFGCDQAQGFFYSRPLPEAALDEWL 585
Cdd:COG5001  632 EVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALL 673
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 340-580 2.63e-87

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


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 270.96  E-value: 2.63e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 340 HDLAIAIRQDKgLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLRN 419
Cdd:cd01948    1 ADLRRALERGE-FELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 420 SYIQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGLEMLKLRGFGISLDDFGTGYSN 499
Cdd:cd01948   80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 500 ISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRPLPEA 579
Cdd:cd01948  160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239


                 .
gi 768329941 580 A 580
Cdd:cd01948  240 E 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 341-575 6.33e-74

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


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 236.06  E-value: 6.33e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  341 DLAIAIRQdKGLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLRNS 420
Cdd:pfam00563   3 ALRRALEN-GEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  421 yIQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGLEMLKLRGFGISLDDFGTGYSNI 500
Cdd:pfam00563  82 -PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329941  501 SYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRP 575
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 339-580 3.30e-71

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 229.03  E-value: 3.30e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   339 MHDLAIAIRQDkGLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLR 418
Cdd:smart00052   1 ERELRQALENG-QFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   419 NSYI-QLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGLEMLKLRGFGISLDDFGTGY 497
Cdd:smart00052  80 AQGPpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   498 SNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRPLP 577
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239


                   ...
gi 768329941   578 EAA 580
Cdd:smart00052 240 LDD 242
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
345-585 1.89e-53

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 193.36  E-value: 1.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 345 AIRQDKgLWLAYQPKICLhSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLRNSYIQL 424
Cdd:PRK10060 416 ALENDQ-LVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINL 493

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 425 PITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERIlESATAMRGLeMLKLRGFG--ISLDDFGTGYSNISY 502
Cdd:PRK10060 494 RVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLI-ENEELALSV-IQQFSQLGaqVHLDDFGTGYSSLSQ 571

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 503 LRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRPLPEAALD 582
Cdd:PRK10060 572 LARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFE 651


                 ...
gi 768329941 583 EWL 585
Cdd:PRK10060 652 RWY 654
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 25-153 2.84e-13

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


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 67.12  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   25 SRDDVLRQFVRLASQALGIPGSFISVLDDEMQHV--KAAQNFTLTQSSRQDSLCRHAVDSDSTVVVPDTLLDTRFAEHPL 102
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYlpPGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPRFLDPLL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768329941  103 IVGAPFIRFYAGVPLKsSTGLILGTLCVTDTAPhPFNADQVAMLKMLAALV 153
Cdd:pfam01590  81 LLRNFGIRSLLAVPII-DDGELLGVLVLHHPRP-PFTEEELELLEVLADQV 129
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 27-153 1.32e-07

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 51.23  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941    27 DDVLRQFVRLASQALGIPGSFISVLD--DEMQHV-KAAQNFTLTQSSRQ----DSLCRHAVDSDSTVVVPDTLLDTRFAE 99
Cdd:smart00065   3 EELLQTILEELRQLLGADRVLIYLVDenDRGELVlVAADGLTLPTLGIRfpldEGLAGRVAETGRPLNIPDVEADPLFAE 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 768329941   100 HPLiVGAPFIRFYAGVPLKSStGLILGTLCV-TDTAPHPFNADQVAMLKMLAALV 153
Cdd:smart00065  83 DLL-GRYQGVRSFLAVPLVAD-GELVGVLALhNKKSPRPFTEEDEELLQALANQL 135
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
14-158 1.85e-05

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 45.66  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  14 RTLHALR---SNDESRDDVLRQFVRLASQALGIPGSFISVLDDEMQH--VKAAQNftLTQSSRQ-------DSLCRHAVD 81
Cdd:COG3605    4 KALRRISeavASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRleLRATEG--LNPEAVGkvrlplgEGLVGLVAE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329941  82 SDSTVVVPDTLLDTRFAEHPLIVGAPFIRFYaGVPLKSStGLILGTLCVTDTAPHPFNADQVAMLKMLAALVMSFLE 158
Cdd:COG3605   82 RGEPLNLADAASHPRFKYFPETGEEGFRSFL-GVPIIRR-GRVLGVLVVQSREPREFTEEEVEFLVTLAAQLAEAIA 156
 
Name Accession Description Interval E-value
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 167-585 1.82e-90

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


Pssm-ID: 444025 [Multi-domain]  Cd Length: 678  Bit Score: 293.22  E-value: 1.82e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 167 DPVTGLPNRQRLIRDLQFLAASGDTTPRRLVLIdCIDmprayeLAR------SMG--MGpvESLLKDVATLLPLRLRPAp 238
Cdd:COG5001  254 DPLTGLPNRRLFLDRLEQALARARRSGRRLALL-FID------LDRfkeindTLGhaAG--DELLREVARRLRACLREG- 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 239 gemlYTVAtgRF------ALLTRQESRLTANWVANK-LAGISA--DLgDGLSVALMTHTGEASFNTGEMPAQEILRRAVS 309
Cdd:COG5001  324 ----DTVA--RLggdefaVLLPDLDDPEDAEAVAERiLAALAEpfEL-DGHELYVSASIGIALYPDDGADAEELLRNADL 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 310 ALHEA--ITRDVASMpFSEATDTRHTQDFTLMHDLAIAIRQDkGLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPA 387
Cdd:COG5001  397 AMYRAkaAGRNRYRF-FDPEMDERARERLELEADLRRALERG-ELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPA 474

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 388 QFLPFAVQTELLSELTTWVTEHAIARLSRLRNSYIQ-LPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLgieCLE-T 465
Cdd:COG5001  475 EFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRL---ELEiT 551

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 466 ERIL--ESATAMRGLEMLKLRGFGISLDDFGTGYSNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDY 543
Cdd:COG5001  552 ESALleDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGL 631

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 768329941 544 MVLAEGVENAETVTALTEFGCDQAQGFFYSRPLPEAALDEWL 585
Cdd:COG5001  632 EVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALL 673
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 14-585 8.87e-88

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


Pssm-ID: 441802 [Multi-domain]  Cd Length: 576  Bit Score: 283.60  E-value: 8.87e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  14 RTLHALRSNDESRDDVLRQFVRLASQALGIPGSFISVLDDEMQHVKAAQNFTLTQSSRQDSLCRHAVDSDSTVVVPDTLL 93
Cdd:COG2200    6 ALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  94 DTRFAEHPLIVGAPFIRFYAGVPLKSSTGLILGTLCVTDTAPHPFNADQVAMLKMLAALVMSFLEAWYSAGFADPVTGLP 173
Cdd:COG2200   86 LLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 174 NRQRLIRDLQFLAASGDTTPRRLVLIDCIDMPRAYELARSMGMGPVESLLKDVATLLPLRLRPAPGEMLYTVATGRFALL 253
Cdd:COG2200  166 RLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLL 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 254 TRQESRLTANWVANKLAGISADLGDGLSVALmTHTGEASFNTGEMPAQEILRRAVSALHEAITRDVASMPFSEATDTRHT 333
Cdd:COG2200  246 AAAAAAAAALRLLLLLLLEPLLLGGGLVVVA-SSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARAR 324

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 334 QDFTLMHDLAIAIRQDKgLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIAR 413
Cdd:COG2200  325 RRLALESELREALEEGE-LRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQ 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 414 LSRLRNSYIQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGLEMLKLRGFGISLDDF 493
Cdd:COG2200  404 LARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDF 483

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 494 GTGYSNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYS 573
Cdd:COG2200  484 GTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFG 563

                        570
                 ....*....|..
gi 768329941 574 RPLPEAALDEWL 585
Cdd:COG2200  564 RPLPLEELEALL 575
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 340-580 2.63e-87

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


Pssm-ID: 238923 [Multi-domain]  Cd Length: 240  Bit Score: 270.96  E-value: 2.63e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 340 HDLAIAIRQDKgLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLRN 419
Cdd:cd01948    1 ADLRRALERGE-FELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 420 SYIQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGLEMLKLRGFGISLDDFGTGYSN 499
Cdd:cd01948   80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 500 ISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRPLPEA 579
Cdd:cd01948  160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239


                 .
gi 768329941 580 A 580
Cdd:cd01948  240 E 240
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 341-575 6.33e-74

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


Pssm-ID: 425752 [Multi-domain]  Cd Length: 235  Bit Score: 236.06  E-value: 6.33e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  341 DLAIAIRQdKGLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLRNS 420
Cdd:pfam00563   3 ALRRALEN-GEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  421 yIQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGLEMLKLRGFGISLDDFGTGYSNI 500
Cdd:pfam00563  82 -PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768329941  501 SYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRP 575
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 339-580 3.30e-71

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 229.03  E-value: 3.30e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   339 MHDLAIAIRQDkGLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLR 418
Cdd:smart00052   1 ERELRQALENG-QFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQ 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   419 NSYI-QLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGLEMLKLRGFGISLDDFGTGY 497
Cdd:smart00052  80 AQGPpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   498 SNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRPLP 577
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239


                   ...
gi 768329941   578 EAA 580
Cdd:smart00052 240 LDD 242
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 340-585 6.12e-59

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


Pssm-ID: 443970 [Multi-domain]  Cd Length: 528  Bit Score: 205.54  E-value: 6.12e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 340 HDLAIAIRQdKGLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLRN 419
Cdd:COG4943  274 RRLRRAIKR-REFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLA 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 420 SYIQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECleTER-ILESATAMRGLEMLKLRGFGISLDDFGTGYS 498
Cdd:COG4943  353 ADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEI--TERgFIDPAKARAVIAALREAGHRIAIDDFGTGYS 430

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 499 NISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRPLPE 578
Cdd:COG4943  431 SLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPA 510


                 ....*..
gi 768329941 579 AALDEWL 585
Cdd:COG4943  511 EEFIAWL 517
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
345-585 1.89e-53

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 193.36  E-value: 1.89e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 345 AIRQDKgLWLAYQPKICLhSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLRNSYIQL 424
Cdd:PRK10060 416 ALENDQ-LVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINL 493

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 425 PITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERIlESATAMRGLeMLKLRGFG--ISLDDFGTGYSNISY 502
Cdd:PRK10060 494 RVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLI-ENEELALSV-IQQFSQLGaqVHLDDFGTGYSSLSQ 571

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 503 LRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRPLPEAALD 582
Cdd:PRK10060 572 LARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFE 651


                 ...
gi 768329941 583 EWL 585
Cdd:PRK10060 652 RWY 654
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 167-585 3.24e-42

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 162.63  E-value: 3.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 167 DPVTGLPNRQRLIRDLQFLaasgdTTPRRLVLIDCIDMPRAYELARSMGMGPVESLLKDVATLLPLRLRPapGEMLYTVA 246
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDL-----VDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKP--DQYLCRIE 451

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 247 TGRFALLTRQESRLTANWVANKLAGISAD--LGDGLSVALMTHTGeASFNTGEmPAQEILRRAVSALhEAITRDVAS--M 322
Cdd:PRK11359 452 GTQFVLVSLENDVSNITQIADELRNVVSKpiMIDDKPFPLTLSIG-ISYDVGK-NRDYLLSTAHNAM-DYIRKNGGNgwQ 528

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 323 PFSEATDTRHTQDFTLMHDLAIAIRQDKgLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSEL 402
Cdd:PRK11359 529 FFSPAMNEMVKERLVLGAALKEAISNNQ-LKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENI 607

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 403 TTWVTEHAIARLSRLRNSYIQLP-ITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIEcleterILESATAMRGLEML 481
Cdd:PRK11359 608 GRWVIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVE------ITESMMMEHDTEIF 681

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 482 K----LR--GFGISLDDFGTGYSNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAET 555
Cdd:PRK11359 682 KriqiLRdmGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQ 761

                        410       420       430
                 ....*....|....*....|....*....|
gi 768329941 556 VTALTEFGCDQAQGFFYSRPLPEAALDEWL 585
Cdd:PRK11359 762 FEMLRKIHCRVIQGYFFSRPLPAEEIPGWM 791
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 168-579 7.05e-42

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 160.49  E-value: 7.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 168 PVTGLPNRQRLIRDLQFLAASGDTTPRRLVLIdcIDMPRAYELARSMGMGPVESLLKDVATLLPLRLRPApgEMLYTVAT 247
Cdd:PRK11829 236 PVTELPNRSLFISLLEKEIASSTRTDHFHLLV--IGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDS--DLLAQLSK 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 248 GRFALLTRQESR-LTANWVANKLAGISAD--LGDGLSVALMTHTGEASFNTGEMPAQEILRRAVSALHEAITRDVASMPF 324
Cdd:PRK11829 312 TEFAVLARGTRRsFPAMQLARRIMSQVTQplFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMV 391

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 325 -----SEATDTRHTQDftlmHDLAIAIRQ-DKGLWLayQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTEL 398
Cdd:PRK11829 392 fephlIEKTHKRLTQE----NDLLQAIENhDFTLFL--QPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGM 465

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 399 LSELTTWVTEHAIARLSRLRNSYIQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGL 478
Cdd:PRK11829 466 MVPLGNWVLEEACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLL 545

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 479 EMLKLRGFGISLDDFGTGYSNISYLR---RIPLDVIKLDRSLISEISSDTAsrvIARSIIAMLKDLDYMVLAEGVENAET 555
Cdd:PRK11829 546 RELQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLPEDDA---IARIISCVSDVLKVRVMAEGVETEEQ 622

                        410       420
                 ....*....|....*....|....
gi 768329941 556 VTALTEFGCDQAQGFFYSRPLPEA 579
Cdd:PRK11829 623 RQWLLEHGIQCGQGFLFSPPLPRA 646
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 168-585 3.52e-41

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 158.34  E-value: 3.52e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 168 PVTGLPNRQRLIRDLQFLAASGDTTPrrLVLIDCIDMPRAyelarsmgmgpvESLLKDV---ATLLPL--RLRP--APGE 240
Cdd:PRK13561 235 PVSDLPNKALLMALLEQVVARKQTTA--LMIITCETLRDT------------AGVLKEAqreILLLTLveKLKSvlSPRM 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 241 MLYTVATGRFALLTRqesRLTANWVANKLA-GISADLGDGLSVALMTHTGEASFNT----GEMPAQEILRRAVSALHEAI 315
Cdd:PRK13561 301 VLAQISGYDFAIIAN---GVKEPWHAITLGqQVLTIINERLPIQRIQLRPSCSIGIamfyGDLTAEQLYSRAISAAFTAR 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 316 TR--------DVASMpfsEATDTRHTQDFTLMHDLAiaiRQDKGLWLayQPKICLHSGKPIGLEALIRWQHPQRGELSPA 387
Cdd:PRK13561 378 RKgknqiqffDPQQM---EAAQKRLTEESDILNALE---NHQFAIWL--QPQVEMRSGKLVSAEALLRMQQPDGSWDLPE 449

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 388 QFLPFAVQTELLSELTTWVTEHAIARLSRLRNSYIQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETER 467
Cdd:PRK13561 450 GLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRR 529

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 468 ILESATAMRGLEMLKLRGFGISLDDFGTGYSNISYLRR---IPLDVIKLDRSLISEISSDTAsrvIARSIIAMLKDLDYM 544
Cdd:PRK13561 530 IDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFVDGLPEDDS---MVAAIIMLAQSLNLQ 606

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 768329941 545 VLAEGVENAETVTALTEFGCDQAQGFFYSRPLPEAAL-DEWL 585
Cdd:PRK13561 607 VIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFeERYL 648
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
345-585 4.19e-38

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 147.45  E-value: 4.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 345 AIRQDKgLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEhAIAR-LSRLRNSyiq 423
Cdd:PRK10551 271 GIKRGQ-FYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFE-LIARdAAELQKV--- 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 424 LP----ITINVSSSDFSRDGFADELEEqmIRAKLPVSLLGIeCLE-TER-ILESATAMRGLEMLKLRGFGISLDDFGTGY 497
Cdd:PRK10551 346 LPvgakLGINISPAHLHSDSFKADVQR--LLASLPADHFQI-VLEiTERdMVQEEEATKLFAWLHSQGIEIAIDDFGTGH 422

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 498 SNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRPLP 577
Cdd:PRK10551 423 SALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLP 502


                 ....*...
gi 768329941 578 EAALDEWL 585
Cdd:PRK10551 503 LEDFVRWL 510
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 112-581 2.56e-21

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 98.98  E-value: 2.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  112 YAGVPLKSSTGLILGTLCVTDTAphpfnADQVAMLKMLAalvmsfleawYSAGFaDPVTGLPNRQRLIRDLQFLAASGDT 191
Cdd:PRK09776  629 YSITPLSTLDGENIGSVLVIQDV-----TESRKMLRQLS----------YSASH-DALTHLANRASFEKQLRRLLQTVNS 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  192 TPRRLVLIdCIDMPRAYELARSMGMGPVESLLKDVATLLPLRLRPApgEMLYTVATGRFALLTRQESRLTANWVANKLag 271
Cdd:PRK09776  693 THQRHALV-FIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSS--DVLARLGGDEFGLLLPDCNVESARFIATRI-- 767

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  272 ISA-------------DLGDGLSVALMTHTGEasfntgemPAQEILRRAVSALHEAIT--RDVASM-PFSEATDTRHTQD 335
Cdd:PRK09776  768 ISAindyhfpwegrvyRVGASAGITLIDANNH--------QASEVMSQADIACYAAKNagRGRVTVyEPQQAAAHSEHRA 839

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  336 FTLMHDLAIAIRQDKGL--WLAYQPKICLHSGKpigLEALIRWQHPQrGEL-SPAQFLPFAVQTELLSELTTWVTE---- 408
Cdd:PRK09776  840 LSLAEQWRMIKENQLMMlaHGVASPRIPEARNH---WLISLRLWDPE-GEIiDEGAFRPAAEDPALMHALDRRVIHeffr 915

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  409 HAIARLSRLrnsyiQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGLEMLKLRGFGI 488
Cdd:PRK09776  916 QAAKAVASK-----GLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRV 990

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  489 SLDDFGTGYSNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQ 568
Cdd:PRK09776  991 VLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAY 1070

                         490
                  ....*....|...
gi 768329941  569 GFFYSRPLPEAAL 581
Cdd:PRK09776 1071 GYAIARPQPLDLL 1083
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
 25-153 2.84e-13

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


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 67.12  E-value: 2.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   25 SRDDVLRQFVRLASQALGIPGSFISVLDDEMQHV--KAAQNFTLTQSSRQDSLCRHAVDSDSTVVVPDTLLDTRFAEHPL 102
Cdd:pfam01590   1 DLEEILQTILEELRELLGADRCALYLPDADGLEYlpPGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPRFLDPLL 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 768329941  103 IVGAPFIRFYAGVPLKsSTGLILGTLCVTDTAPhPFNADQVAMLKMLAALV 153
Cdd:pfam01590  81 LLRNFGIRSLLAVPII-DDGELLGVLVLHHPRP-PFTEEELELLEVLADQV 129
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 435-575 4.74e-11

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 64.82  E-value: 4.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 435 FSRDGFADELEEQmirakLPVSLLGIECLETERIleSATAMRGLEMLKLRGFGISLDDFGTGYSNISYLRRIplDVIKLD 514
Cdd:COG3434   68 FTEELLLSDLPEL-----LPPERVVLEILEDVEP--DEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLA--DIIKID 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768329941 515 rslISEISSDTASRVIARsiiamLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRP 575
Cdd:COG3434  139 ---VLALDLEELAELVAR-----LKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
GAF COG2203
GAF domain [Signal transduction mechanisms];
21-536 4.79e-11

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 65.60  E-value: 4.79e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  21 SNDESRDDVLRQFVRLASQALGIPGSFISVLDDEMQHVKAAQNFTLTQS-----SRQDSLCRHAVDSDSTVVVPDTLLDT 95
Cdd:COG2203  203 RSALDLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEelgrlPLGEGLAGRALRTGEPVVVNDASTDP 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  96 RFAEHPL-IVGAPFIRFYAGVPLKSStGLILGTLCVTDTAPHPFNADQVAMLKMLAALVMSFLEAWYSagfadpvtglpn 174
Cdd:COG2203  283 RFAPSLReLLLALGIRSLLCVPLLVD-GRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARL------------ 349

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 175 RQRLIRDLQFLAASGDTTPRRLVLIDCIDMPRAYELARSMGMGPVESLLKDVATLLPLRLRPAPGEMLYTVATGRFALLT 254
Cdd:COG2203  350 YEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLL 429

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 255 RQESRLTANWVANKLAGISADLGDGLSVALMTHTGEASFNTGEMPAQEILRRAVSALHEAITRDVASMPFSEATDTRHTQ 334
Cdd:COG2203  430 LLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASL 509

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 335 DFTLMHDLAIAIRQDKGLWLAYQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARL 414
Cdd:COG2203  510 LLALLLLLLLLLLLLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALAL 589

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 415 SRLRNSYIQLPITINVSSSDFSRDGFADELEEQMIRAKLPVSLLGIECLETERILESATAMRGLEMLKLRGFGISLDDFG 494
Cdd:COG2203  590 LELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALALASLVLLRALLATELDLILD 669

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|..
gi 768329941 495 TGYSNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIA 536
Cdd:COG2203  670 SSLLLGLLLLGALLLLGGGLALLLSIGLGLGVARLLQLSVLE 711
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
 27-153 1.32e-07

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 51.23  E-value: 1.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941    27 DDVLRQFVRLASQALGIPGSFISVLD--DEMQHV-KAAQNFTLTQSSRQ----DSLCRHAVDSDSTVVVPDTLLDTRFAE 99
Cdd:smart00065   3 EELLQTILEELRQLLGADRVLIYLVDenDRGELVlVAADGLTLPTLGIRfpldEGLAGRVAETGRPLNIPDVEADPLFAE 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 768329941   100 HPLiVGAPFIRFYAGVPLKSStGLILGTLCV-TDTAPHPFNADQVAMLKMLAALV 153
Cdd:smart00065  83 DLL-GRYQGVRSFLAVPLVAD-GELVGVLALhNKKSPRPFTEEDEELLQALANQL 135
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
 23-158 2.61e-07

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 50.16  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   23 DESRDDVLRQFVRLASQALGIPGSFIsVLDDEMQHVKAAQNFTLTQSSRQD-----SLCRHAVDSDSTVVVPDTLLDTRF 97
Cdd:pfam13185   1 AADLEELLDAVLEAAVELGASAVGFI-LLVDDDGRLAAWGGAADELSAALDdppgeGLVGEALRTGRPVIVNDLAADPAK 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768329941   98 AEHPLivGAPFIRFYAGVPLKSStGLILGTLCVTDTAPHPFNADQVAMLKMLAALVMSFLE 158
Cdd:pfam13185  80 KGLPA--GHAGLRSFLSVPLVSG-GRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 490-577 7.70e-07

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 50.77  E-value: 7.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 490 LDDFGTGYSNISYLRRIPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQG 569
Cdd:PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQG 236


                 ....*...
gi 768329941 570 FFYSRPLP 577
Cdd:PRK11596 237 YFLSRPAP 244
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 142-314 1.11e-06

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


Pssm-ID: 441801 [Multi-domain]  Cd Length: 275  Bit Score: 50.36  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 142 QVAMLKMLAALVMSFLEAWYSAGFaDPVTGLPNRQRLIRDLQFLAASGDTTPRRLVLIdCIDMPRAYELARSMGMGPVES 221
Cdd:COG2199   93 LLLALEDITELRRLEERLRRLATH-DPLTGLPNRRAFEERLERELARARREGRPLALL-LIDLDHFKRINDTYGHAAGDE 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 222 LLKDVATLLPLRLRpaPGEMLYTVATGRFALLTRQESRLTANWVANKL-AGISAD--LGDGLSVALMTHTGEASFNTGEM 298
Cdd:COG2199  171 VLKEVARRLRASLR--ESDLVARLGGDEFAVLLPGTDLEEAEALAERLrEALEQLpfELEGKELRVTVSIGVALYPEDGD 248

                        170
                 ....*....|....*.
gi 768329941 299 PAQEILRRAVSALHEA 314
Cdd:COG2199  249 SAEELLRRADLALYRA 264
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 356-578 3.70e-06

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 49.86  E-value: 3.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 356 YQPKICLHSGKPIGLEALIRWQHPQRGELSPAQFLPFAVQTELLSELTTWVTEHAIARLSRLRnsyiQLPITINVSSSDF 435
Cdd:PRK11059 420 YQQPAVTRDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWP----EENLSINLSVDSL 495

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941 436 SRDGFADELEEqmiraklpvSLLGIECLETERIL-ESATA--MRGLEMLK-----LRGFGISL--DDFGTGYSNISYLRR 505
Cdd:PRK11059 496 LSRAFQRWLRD---------TLLQCPRSQRKRLIfELAEAdvCQHISRLRpvlrmLRGLGCRLavDQAGLTVVSTSYIKE 566

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768329941 506 IPLDVIKLDRSLISEISSDTASRVIARSIIAMLKDLDYMVLAEGVENAETVTALTEFGCDQAQGFFYSRPLPE 578
Cdd:PRK11059 567 LNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
14-158 1.85e-05

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 45.66  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941  14 RTLHALR---SNDESRDDVLRQFVRLASQALGIPGSFISVLDDEMQH--VKAAQNftLTQSSRQ-------DSLCRHAVD 81
Cdd:COG3605    4 KALRRISeavASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRleLRATEG--LNPEAVGkvrlplgEGLVGLVAE 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768329941  82 SDSTVVVPDTLLDTRFAEHPLIVGAPFIRFYaGVPLKSStGLILGTLCVTDTAPHPFNADQVAMLKMLAALVMSFLE 158
Cdd:COG3605   82 RGEPLNLADAASHPRFKYFPETGEEGFRSFL-GVPIIRR-GRVLGVLVVQSREPREFTEEEVEFLVTLAAQLAEAIA 156
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 167-315 1.68e-04

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 42.23  E-value: 1.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768329941   167 DPVTGLPNRQRLIRDLQFLAASGDTTPRRLVLIdCIDMPRAYELARSMGMGPVESLLKDVATLLPLRLRpaPGEMLYTVA 246
Cdd:smart00267   6 DPLTGLPNRRYFEEELEQELQRAQRQGSPFALL-LIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLR--PGDLLARLG 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768329941   247 TGRFALLTRQESRLTANWVANKL-AGISAD-LGDGLSVALMTHTGEASFNTGEMPAQEILRRAVSALHEAI 315
Cdd:smart00267  83 GDEFALLLPETSLEEAIALAERIlQQLREPiIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAK 153
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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