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Conserved domains on  [gi|2308551918|ref|WP_261243372|]
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EAL domain-containing protein [Arcobacter lacus]

Protein Classification

EAL domain-containing protein( domain architecture ID 10005623)

EAL domain-containing protein may act as a cyclic diguanylate phosphodiesterase; similar to Borreliella burgdorferi cyclic di-GMP phosphodiesterase PdeA that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to pGpG

CATH:  3.20.20.450
EC:  3.1.4.52
Gene Ontology:  GO:0071111
PubMed:  15306016|26055114|19756011
SCOP:  4002400

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 76-555 2.17e-77

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: 255.48  E-value: 2.17e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  76 EEVIGKPHSIVRGEEEDEIFRELWETIKSKKVWYGVLKNRKKNGDFYWVNINIRPILNEKDEVIEYIAIRHEITDLVLKT 155
Cdd:COG2200    68 LLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLAL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 156 EELKRNLRFDSLTHIGNRYKL-------IEDVSKYINPCIAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEELLIDKEN 228
Cdd:COG2200   148 LLLALLALLDLLLLLLLRRLLlllllllLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLL 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 229 YAIYRDHSDVFCIIAENEDKDKFLKNIEYISKTIGKVSISIKGRELYIQLSYVFSFEPKENLLETVNIIKR----YSKTN 304
Cdd:COG2200   228 LALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAaaaaAAAAG 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 305 KNTIIYDRDLELEKDYEKNIFWTLKIKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGN-NVISPYYFLDISKKSK 383
Cdd:COG2200   308 GGRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSG 387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 384 QYLQLTKTMIEKTFEYFKD-----KDFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEF 457
Cdd:COG2200   388 LIVELDRWVLERALRQLARwpergLDLRLSVNLSARSLLDPDFLERLLELLAEYGLpPERLVLEITESALLEDLEAAIEL 467

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 458 FVIIREYGCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILN 537
Cdd:COG2200   468 LARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLE 547

                         490
                  ....*....|....*...
gi 2308551918 538 KVRELGIDYVQGYYIKEP 555
Cdd:COG2200   548 ALRELGCDYAQGYLFGRP 565
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 76-555 2.17e-77

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: 255.48  E-value: 2.17e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  76 EEVIGKPHSIVRGEEEDEIFRELWETIKSKKVWYGVLKNRKKNGDFYWVNINIRPILNEKDEVIEYIAIRHEITDLVLKT 155
Cdd:COG2200    68 LLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLAL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 156 EELKRNLRFDSLTHIGNRYKL-------IEDVSKYINPCIAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEELLIDKEN 228
Cdd:COG2200   148 LLLALLALLDLLLLLLLRRLLlllllllLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLL 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 229 YAIYRDHSDVFCIIAENEDKDKFLKNIEYISKTIGKVSISIKGRELYIQLSYVFSFEPKENLLETVNIIKR----YSKTN 304
Cdd:COG2200   228 LALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAaaaaAAAAG 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 305 KNTIIYDRDLELEKDYEKNIFWTLKIKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGN-NVISPYYFLDISKKSK 383
Cdd:COG2200   308 GGRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSG 387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 384 QYLQLTKTMIEKTFEYFKD-----KDFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEF 457
Cdd:COG2200   388 LIVELDRWVLERALRQLARwpergLDLRLSVNLSARSLLDPDFLERLLELLAEYGLpPERLVLEITESALLEDLEAAIEL 467

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 458 FVIIREYGCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILN 537
Cdd:COG2200   468 LARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLE 547

                         490
                  ....*....|....*...
gi 2308551918 538 KVRELGIDYVQGYYIKEP 555
Cdd:COG2200   548 ALRELGCDYAQGYLFGRP 565
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 330-555 9.30e-65

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: 211.64  E-value: 9.30e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 330 IKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLID-GNNVISPYYFLDISKKSKQYLQLTKTMIEKTFEYFK-----DK 403
Cdd:cd01948     3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLArwqagGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 404 DFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFEY 482
Cdd:cd01948    83 DLRLSVNLSARQLRDPDFLDRLLELLAETGLpPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2308551918 483 LAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEP 555
Cdd:cd01948   163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 330-555 8.73e-64

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: 209.10  E-value: 8.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 330 IKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGNN-VISPYYFLDISKKSKQYLQLTKTMIEKTFEYFKDK----D 404
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGgLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlgpD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 405 FEFSINLTFEDIKSEYISSFIIELLKKYKIGH-RVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFEYL 483
Cdd:pfam00563  84 IKLSINLSPASLADPGFLELLRALLKQAGPPPsRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2308551918 484 AKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEP 555
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 330-556 6.41e-54

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 183.19  E-value: 6.41e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  330 IKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGNN-VISPYYFLDISKKSKQYLQLTKTMIEKTFEYFKD------ 402
Cdd:smart00052   4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGgIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEwqaqgp 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  403 KDFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFE 481
Cdd:smart00052  84 PPLLISINLSARQLISPDLVPRVLELLEETGLpPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLS 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2308551918  482 YLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEPI 556
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 38-557 2.81e-28

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 120.55  E-value: 2.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918   38 LKQYNEA----------TKDS---NIISTaDLKGNITYVNERFCDVSLYTKEEVIGKPHSIV-------RGEEEDEIFRE 97
Cdd:PRK09776   524 VRQLNEAlfqekerlhiTLDSigeAVVCT-DMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVlhitfgdNGPLMENIYSC 602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918   98 LwetiKSKKVWY----GVLKNRkkNGDFYWVNINIRPILNEKDEVIEYIAIRHEITDLVLKTEELKRNLRFDSLTHIGNR 173
Cdd:PRK09776   603 L----TSRSAAYleqdVVLHCR--SGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANR 676

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  174 YK-------LIEDVSKYINP-CIAMLDIVSFSDVNDFFGYKTGDSVLKIVARkieellidkenyaIYRDH---SDVFCII 242
Cdd:PRK09776   677 ASfekqlrrLLQTVNSTHQRhALVFIDLDRFKAVNDSAGHAAGDALLRELAS-------------LMLSMlrsSDVLARL 743

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  243 AENE----DKDKFLKNIEYISK----TIGKVSISIKGRELYIQLSYVF-----SFEPKENLLETVNIIKRYSKTN-KNTI 308
Cdd:PRK09776   744 GGDEfgllLPDCNVESARFIATriisAINDYHFPWEGRVYRVGASAGItlidaNNHQASEVMSQADIACYAAKNAgRGRV 823

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  309 -IYDRDLELEKDYEKNIFWTLKIKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGNN-VISPYYFLDISKKSKQYL 386
Cdd:PRK09776   824 tVYEPQQAAAHSEHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGeIIDEGAFRPAAEDPALMH 903

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  387 QLTKTMIEKTFEYFKD----KDFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEFFVII 461
Cdd:PRK09776   904 ALDRRVIHEFFRQAAKavasKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLpPRLLHLEITETALLNHAESASRLVQKL 983

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  462 REYGCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRE 541
Cdd:PRK09776   984 RLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSG 1063

                          570
                   ....*....|....*.
gi 2308551918  542 LGIDYVQGYYIKEPIA 557
Cdd:PRK09776  1064 IGVDLAYGYAIARPQP 1079
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 51-158 2.56e-14

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 69.63  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  51 ISTADLKGNITYVNERFCDVSLYTKEEVIGKPHSIVRGEEEDEIFRE-LWETIKSKKVWYGVLKN-RKKNGDFYWVNINI 128
Cdd:TIGR00229  16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRErIERRLEGEPEPVSEERRvRRKDGSEIWVEVSV 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 2308551918 129 RPILNEKDEVIeYIAIRHEITDLVLKTEEL 158
Cdd:TIGR00229  96 SPIRTNGGELG-VVGIVRDITERKEAEEAL 124
 
Name Accession Description Interval E-value
EAL COG2200
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ...
 76-555 2.17e-77

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: 255.48  E-value: 2.17e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  76 EEVIGKPHSIVRGEEEDEIFRELWETIKSKKVWYGVLKNRKKNGDFYWVNINIRPILNEKDEVIEYIAIRHEITDLVLKT 155
Cdd:COG2200    68 LLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLAL 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 156 EELKRNLRFDSLTHIGNRYKL-------IEDVSKYINPCIAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEELLIDKEN 228
Cdd:COG2200   148 LLLALLALLDLLLLLLLRRLLlllllllLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLL 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 229 YAIYRDHSDVFCIIAENEDKDKFLKNIEYISKTIGKVSISIKGRELYIQLSYVFSFEPKENLLETVNIIKR----YSKTN 304
Cdd:COG2200   228 LALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAaaaaAAAAG 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 305 KNTIIYDRDLELEKDYEKNIFWTLKIKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGN-NVISPYYFLDISKKSK 383
Cdd:COG2200   308 GGRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSG 387

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 384 QYLQLTKTMIEKTFEYFKD-----KDFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEF 457
Cdd:COG2200   388 LIVELDRWVLERALRQLARwpergLDLRLSVNLSARSLLDPDFLERLLELLAEYGLpPERLVLEITESALLEDLEAAIEL 467

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 458 FVIIREYGCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILN 537
Cdd:COG2200   468 LARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLE 547

                         490
                  ....*....|....*...
gi 2308551918 538 KVRELGIDYVQGYYIKEP 555
Cdd:COG2200   548 ALRELGCDYAQGYLFGRP 565
EAL cd01948
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 330-555 9.30e-65

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: 211.64  E-value: 9.30e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 330 IKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLID-GNNVISPYYFLDISKKSKQYLQLTKTMIEKTFEYFK-----DK 403
Cdd:cd01948     3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLArwqagGP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 404 DFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFEY 482
Cdd:cd01948    83 DLRLSVNLSARQLRDPDFLDRLLELLAETGLpPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2308551918 483 LAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEP 555
Cdd:cd01948   163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
EAL pfam00563
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ...
 330-555 8.73e-64

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: 209.10  E-value: 8.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 330 IKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGNN-VISPYYFLDISKKSKQYLQLTKTMIEKTFEYFKDK----D 404
Cdd:pfam00563   4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGgLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlgpD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 405 FEFSINLTFEDIKSEYISSFIIELLKKYKIGH-RVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFEYL 483
Cdd:pfam00563  84 IKLSINLSPASLADPGFLELLRALLKQAGPPPsRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2308551918 484 AKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEP 555
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
COG5001 COG5001
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ...
 123-557 6.20e-58

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: 205.39  E-value: 6.20e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 123 WVNINIRPILNEKDEVIEYIAIRHEITDLVLKTEELKRNLRFDSLTHIGNRYKLIEDVSKYINPC--------IAMLDIV 194
Cdd:COG5001   212 LLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARArrsgrrlaLLFIDLD 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 195 SFSDVNDFFGYKTGDSVLKIVARKIEELLidKENYAIYRDHSDVFCIIAEN-EDKDKFLKNIEYISKTIGKvSISIKGRE 273
Cdd:COG5001   292 RFKEINDTLGHAAGDELLREVARRLRACL--REGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAE-PFELDGHE 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 274 LYIQLS--YVFSFEPKENLLEtvnIIKR-----Y-SKTN-KNTI-IYDRD--------LELEKDyeknifwtlkIKKALD 335
Cdd:COG5001   369 LYVSASigIALYPDDGADAEE---LLRNadlamYrAKAAgRNRYrFFDPEmderarerLELEAD----------LRRALE 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 336 EDKIVPYFQAIYNLKTNKIEKYEALVRLID---GnnVISPYYFLDISKKSKQYLQLTKTMIEKTFEYFKD------KDFE 406
Cdd:COG5001   436 RGELELHYQPQVDLATGRIVGAEALLRWQHperG--LVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAwqdaglPDLR 513

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 407 FSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFEYLAK 485
Cdd:COG5001   514 VAVNLSARQLRDPDLVDRVRRALAETGLpPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKR 593

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2308551918 486 LNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEPIA 557
Cdd:COG5001   594 LPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLP 665
EAL smart00052
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ...
 330-556 6.41e-54

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


Pssm-ID: 214491 [Multi-domain]  Cd Length: 242  Bit Score: 183.19  E-value: 6.41e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  330 IKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGNN-VISPYYFLDISKKSKQYLQLTKTMIEKTFEYFKD------ 402
Cdd:smart00052   4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGgIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEwqaqgp 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  403 KDFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFE 481
Cdd:smart00052  84 PPLLISINLSARQLISPDLVPRVLELLEETGLpPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLS 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2308551918  482 YLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEPI 556
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
YjcC COG4943
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ...
 329-551 1.64e-44

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: 165.47  E-value: 1.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 329 KIKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGN-NVISPYYFLDISKKSKQYLQLTKTMIEKTFE-----YFKD 402
Cdd:COG4943   275 RLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDgSVISPDIFIPLAEQSGLISPLTRQVIEQVFRdlgdlLAAD 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 403 KDFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDsFRKINEFFVIIREYGCKIAIDDFGSGYSNFE 481
Cdd:COG4943   355 PDFHISINLSASDLLSPRFLDDLERLLARTGVaPQQIVLEITERGFID-PAKARAVIAALREAGHRIAIDDFGTGYSSLS 433

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 482 YLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYY 551
Cdd:COG4943   434 YLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
 38-557 2.81e-28

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 120.55  E-value: 2.81e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918   38 LKQYNEA----------TKDS---NIISTaDLKGNITYVNERFCDVSLYTKEEVIGKPHSIV-------RGEEEDEIFRE 97
Cdd:PRK09776   524 VRQLNEAlfqekerlhiTLDSigeAVVCT-DMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVlhitfgdNGPLMENIYSC 602

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918   98 LwetiKSKKVWY----GVLKNRkkNGDFYWVNINIRPILNEKDEVIEYIAIRHEITDLVLKTEELKRNLRFDSLTHIGNR 173
Cdd:PRK09776   603 L----TSRSAAYleqdVVLHCR--SGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANR 676

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  174 YK-------LIEDVSKYINP-CIAMLDIVSFSDVNDFFGYKTGDSVLKIVARkieellidkenyaIYRDH---SDVFCII 242
Cdd:PRK09776   677 ASfekqlrrLLQTVNSTHQRhALVFIDLDRFKAVNDSAGHAAGDALLRELAS-------------LMLSMlrsSDVLARL 743

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  243 AENE----DKDKFLKNIEYISK----TIGKVSISIKGRELYIQLSYVF-----SFEPKENLLETVNIIKRYSKTN-KNTI 308
Cdd:PRK09776   744 GGDEfgllLPDCNVESARFIATriisAINDYHFPWEGRVYRVGASAGItlidaNNHQASEVMSQADIACYAAKNAgRGRV 823

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  309 -IYDRDLELEKDYEKNIFWTLKIKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLIDGNN-VISPYYFLDISKKSKQYL 386
Cdd:PRK09776   824 tVYEPQQAAAHSEHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGeIIDEGAFRPAAEDPALMH 903

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  387 QLTKTMIEKTFEYFKD----KDFEFSINLTFEDIKSEYISSFIIELLKKYKI-GHRVVFEIVESEGIDSFRKINEFFVII 461
Cdd:PRK09776   904 ALDRRVIHEFFRQAAKavasKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLpPRLLHLEITETALLNHAESASRLVQKL 983

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  462 REYGCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRE 541
Cdd:PRK09776   984 RLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSG 1063

                          570
                   ....*....|....*.
gi 2308551918  542 LGIDYVQGYYIKEPIA 557
Cdd:PRK09776  1064 IGVDLAYGYAIARPQP 1079
PRK11359 PRK11359
cyclic-di-GMP phosphodiesterase; Provisional
 132-560 6.81e-27

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183097 [Multi-domain]  Cd Length: 799  Bit Score: 115.64  E-value: 6.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 132 LNEKDEVIEYIA-IRHEITDLVLKTEE----LKRNLRFDSLTHIGNRYKL---IED-VSKYINPCIAMLDIVSFSDVNDF 202
Cdd:PRK11359  341 GAETSAFIERVAdISQHLAALALEQEKsrqhIEQLIQFDPLTGLPNRNNLhnyLDDlVDKAVSPVVYLIGVDHFQDVIDS 420

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 203 FGYKTGDSVLKIVARKIEELLidKENYAIYRDHSDVFCIIAENEDKDKFLKNIEYISKTIGKvSISIKGRELYIQLSYVF 282
Cdd:PRK11359  421 LGYAWADQALLEVVNRFREKL--KPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK-PIMIDDKPFPLTLSIGI 497

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 283 SFE---PKENLLETVNIIKRYSKTNKNTIIYDRDLELEKDYEKNIFWTLKIKKALDEDKIVPYFQAIYNLKTNKIEKYEA 359
Cdd:PRK11359  498 SYDvgkNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEA 577

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 360 LVRLID---GNnvISPYYFLDISKKSKQYLQLTKTMIEKTFEYFKDKDFE------FSINLTFEDIKSEYISSFIIELLK 430
Cdd:PRK11359  578 LARWHDplhGH--VPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQnihipaLSVNLSALHFRSNQLPNQVSDAMQ 655

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 431 KYKI-GHRVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIKDILINTSSQN 509
Cdd:PRK11359  656 AWGIdGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILA 735

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2308551918 510 IVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEPIASID 560
Cdd:PRK11359  736 LLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
PAS COG2202
PAS domain [Signal transduction mechanisms];
48-168 8.72e-24

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 100.87  E-value: 8.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  48 SNIISTADLKGNITYVNERFCDVSLYTKEEVIGKPHSIVR-GEEEDEIFRELWETIKSKKVWYGVLKNRKKNGDFYWVNI 126
Cdd:COG2202    21 PDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLpPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVEL 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2308551918 127 NIRPILNEKDEVIEYIAIRHEITDLVLKTEELKRNLRFDSLT 168
Cdd:COG2202   101 SISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLL 142
PRK10060 PRK10060
cyclic di-GMP phosphodiesterase;
165-556 4.19e-20

cyclic di-GMP phosphodiesterase;


Pssm-ID: 236645 [Multi-domain]  Cd Length: 663  Bit Score: 94.36  E-value: 4.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 165 DSLTHIGNRYKLIEDVSKYINPC------IAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEELLidKENYAIYRDHSDV 238
Cdd:PRK10060  240 DSITGLPNRNAIQELIDHAINAAdnnqvgIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL--EEDQTLARLGGDE 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 239 FCIIAENEDKDKflknIEYISKTI---GKVSISIKGRELYIQLSYVFSFEPKE-NLLETvnIIKrysktNKNTIIYDR-- 312
Cdd:PRK10060  318 FLVLASHTSQAA----LEAMASRIltrLRLPFRIGLIEVYTGCSIGIALAPEHgDDSES--LIR-----SADTAMYTAke 386

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 313 ---------DLELEKDYEKNIFWTLKIKKALDEDKIVPYFQAIYNLkTNKIEKYEALVR-LIDGNNVISPYYFLDISKKS 382
Cdd:PRK10060  387 ggrgqfcvfSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRwQSPERGLIPPLEFISYAEES 465

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 383 KQYLQLTKTMIEKTFEY---FKDK--DFEFSINLTFEDIKSEYISSFIIELLKKYKIGHRVV-FEIVESEGID----SFR 452
Cdd:PRK10060  466 GLIVPLGRWVMLDVVRQvakWRDKgiNLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIdVELTESCLIEneelALS 545

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 453 KINEFfviiREYGCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSN 532
Cdd:PRK10060  546 VIQQF----SQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVET 621

                         410       420
                  ....*....|....*....|....
gi 2308551918 533 KDILNKVRELGIDYVQGYYIKEPI 556
Cdd:PRK10060  622 AKEDAFLTKNGVNERQGFLFAKPM 645
GGDEF COG2199
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ...
 128-280 8.42e-18

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: 83.87  E-value: 8.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 128 IRPILNEKDEVIEYIAIRHEITDLVLKTEELKRNLRFDSLTHIGNRYKLIEDVSKYINP--------CIAMLDIVSFSDV 199
Cdd:COG2199    80 VLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARarregrplALLLIDLDHFKRI 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 200 NDFFGYKTGDSVLKIVARKIEELLidKENYAIYRDHSDVFCIIAENEDKDKFLKNIEYISKTIGKVSISIKGRELYIQLS 279
Cdd:COG2199   160 NDTYGHAAGDEVLKEVARRLRASL--RESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVS 237


                  .
gi 2308551918 280 Y 280
Cdd:COG2199   238 I 238
PRK10551 PRK10551
cyclic di-GMP phosphodiesterase;
438-555 1.38e-17

cyclic di-GMP phosphodiesterase;


Pssm-ID: 182541 [Multi-domain]  Cd Length: 518  Bit Score: 85.81  E-value: 1.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 438 VVFEIVESEGIDSfRKINEFFVIIREYGCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNF 517
Cdd:PRK10551  384 IVLEITERDMVQE-EEATKLFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTL 462

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2308551918 518 AKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEP 555
Cdd:PRK10551  463 AKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRP 500
GGDEF cd01949
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ...
 163-279 3.31e-15

Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.


Pssm-ID: 143635 [Multi-domain]  Cd Length: 158  Bit Score: 73.36  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 163 RFDSLTHIGNRYKLIEDVSKYINP--------CIAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEELLidKENYAIYRD 234
Cdd:cd01949     1 YTDPLTGLPNRRAFEERLERLLARarrsgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSL--RESDLVARL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2308551918 235 HSDVFCIIAENEDKDKFLKNIEYISKTIGKVSIsIKGRELYIQLS 279
Cdd:cd01949    79 GGDEFAILLPGTDLEEAEALAERLREAIEEPFF-IDGQEIRVTAS 122
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
 51-158 2.56e-14

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


Pssm-ID: 272971 [Multi-domain]  Cd Length: 124  Bit Score: 69.63  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  51 ISTADLKGNITYVNERFCDVSLYTKEEVIGKPHSIVRGEEEDEIFRE-LWETIKSKKVWYGVLKN-RKKNGDFYWVNINI 128
Cdd:TIGR00229  16 IIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRErIERRLEGEPEPVSEERRvRRKDGSEIWVEVSV 95

                          90       100       110
                  ....*....|....*....|....*....|
gi 2308551918 129 RPILNEKDEVIeYIAIRHEITDLVLKTEEL 158
Cdd:TIGR00229  96 SPIRTNGGELG-VVGIVRDITERKEAEEAL 124
PRK11829 PRK11829
biofilm formation regulator HmsP; Provisional
 330-560 3.07e-14

biofilm formation regulator HmsP; Provisional


Pssm-ID: 183329 [Multi-domain]  Cd Length: 660  Bit Score: 75.75  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 330 IKKALDEDKIVPYFQAIYNLKTNKIEKYEALVRLI--DGNNVIsPYYFLDISKKSKQYLQLTKTMIEKTFEYFKDKD--- 404
Cdd:PRK11829  410 LLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCqpDGSYVL-PSGFVHFAEEEGMMVPLGNWVLEEACRILADWKarg 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 405 --FEFSINLTFEDIKSEYISSFIIELLKKYKIG-HRVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFE 481
Cdd:PRK11829  489 vsLPLSVNISGLQVQNKQFLPHLKTLISHYHIDpQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLR 568

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 482 YL---AKLNVDYIKIDGSLIKDILINTSSQNIVSMLvnfAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEPIAS 558
Cdd:PRK11829  569 YLnhlKSLPIHMIKLDKSFVKNLPEDDAIARIISCV---SDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPR 645


                  ..
gi 2308551918 559 ID 560
Cdd:PRK11829  646 AE 647
PRK13561 PRK13561
putative diguanylate cyclase; Provisional
 408-556 4.98e-13

putative diguanylate cyclase; Provisional


Pssm-ID: 184143 [Multi-domain]  Cd Length: 651  Bit Score: 71.67  E-value: 4.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 408 SINLTFEDIKSEYISSFIIELLKKYKIG-HRVVFEIVESEGIDSFRKINEFFVIIREYGCKIAIDDFGSGYSNFEYLAK- 485
Cdd:PRK13561  489 SVNLSALQLMHPNMVADMLELLTRYRIQpGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHm 568

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2308551918 486 --LNVDYIKIDGSLIkDILINTSSqnIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEPI 556
Cdd:PRK13561  569 ksLPIDVLKIDKMFV-DGLPEDDS--MVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARAL 638
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
 57-150 1.44e-12

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


Pssm-ID: 463873 [Multi-domain]  Cd Length: 93  Bit Score: 63.63  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  57 KGNITYVNERFCDVSLYTKEEVIGKP-HSIVRGEEEDEIFRELWETIKSkkVWYGVLKNRKKNGDFYWVNINIRPILNEK 135
Cdd:pfam13426   1 DGRIIYVNDAALRLLGYTREELLGKSiTDLFAEPEDSERLREALREGKA--VREFEVVLYRKDGEPFPVLVSLAPIRDDG 78

                          90
                  ....*....|....*
gi 2308551918 136 DEVIEYIAIRHEITD 150
Cdd:pfam13426  79 GELVGIIAILRDITE 93
YuxH COG3434
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ...
 409-555 7.42e-12

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


Pssm-ID: 442660 [Multi-domain]  Cd Length: 407  Bit Score: 67.52  E-value: 7.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 409 INLTFEDIKSEyissfIIELLKKykigHRVVFEIVESEGIDsfrkiNEFFVIIREY---GCKIAIDDFgSGYSNFEYLAK 485
Cdd:COG3434    66 INFTEELLLSD-----LPELLPP----ERVVLEILEDVEPD-----EELLEALKELkekGYRIALDDF-VLDPEWDPLLP 130

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 486 LnVDYIKIDgslikdilINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNKVRELGIDYVQGYYIKEP 555
Cdd:COG3434   131 L-ADIIKID--------VLALDLEELAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 60-145 1.66e-11

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


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 60.43  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  60 ITYVNERFCDVSLYTKEEVIGKPH---SIVRGEEEDEIFRELWETIKSKKVWYGVLKNRKKNGDFYWVNINIRPILNEKD 136
Cdd:pfam08447   1 IIYWSPRFEEILGYTPEELLGKGEswlDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80


                  ....*....
gi 2308551918 137 EVIEYIAIR 145
Cdd:pfam08447  81 KPVRVIGVA 89
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 48-148 1.75e-11

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


Pssm-ID: 238075 [Multi-domain]  Cd Length: 103  Bit Score: 61.11  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  48 SNIISTADLKGNITYVNERFCDVSLYTKEEVIGKPHS-IVRGEEEDEIFRELWETIKSKKVWYGVLKNRKKNGDFYWVNI 126
Cdd:cd00130     2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLdLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLV 81

                          90       100
                  ....*....|....*....|..
gi 2308551918 127 NIRPILNEKDEVIEYIAIRHEI 148
Cdd:cd00130    82 SLTPIRDEGGEVIGLLGVVRDI 103
PRK13558 PRK13558
bacterio-opsin activator; Provisional
 51-181 1.77e-11

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 66.78  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  51 ISTADLKGN-ITYVNERFCDVSLYTKEEVIGKPHSIVRGEEED-EIFRELWETIKSKKVWYGVLKNRKKNGDFYWVNINI 128
Cdd:PRK13558  163 IADATLPDEpLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNeERVAELREAIDEERPTSVELRNYRKDGSTFWNQVDI 242

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2308551918 129 RPILNEKDEVIEYIAIRHEITDLVLKTEELKRNLRF--DSLTHIGNrykLIEDVS 181
Cdd:PRK13558  243 APIRDEDGTVTHYVGFQTDVTERKEAELALQRERRKlqRLLERVEG---LVNDVT 294
PAS COG2202
PAS domain [Signal transduction mechanisms];
31-158 5.16e-11

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 63.51  E-value: 5.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  31 IKKENHILKQYNEATKDsnIISTADLKGNITYVNERFCDVSLYTKEEVIGKPHSIVRGEEEDEIFRELWETIKSKKVWYG 110
Cdd:COG2202   132 LRESEERLRLLVENAPD--GIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESY 209

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2308551918 111 VLKNRKKNGDFYWVNINIRPILNE-KDEVIEYIAIRHEITDLVLKTEEL 158
Cdd:COG2202   210 ELELRLKDGDGRWVWVEASAVPLRdGGEVIGVLGIVRDITERKRAEEAL 258
PRK11059 PRK11059
regulatory protein CsrD; Provisional
 309-556 5.57e-10

regulatory protein CsrD; Provisional


Pssm-ID: 236833 [Multi-domain]  Cd Length: 640  Bit Score: 62.19  E-value: 5.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 309 IYDRDLELEKDyEKNIFW-TLkIKKALDEDKIVPYFQAIYNlKTNKIEKYEALVRLIDGN-NVISPYYFLDISKKSKQYL 386
Cdd:PRK11059  388 VYDKAQLPEKG-RGSVRWrTL-LEQTLVRGGPRLYQQPAVT-RDGKVHHRELFCRIRDGQgELLSAELFMPMVQQLGLSE 464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 387 QLTKTMIEKTFEYFKDKDFE-FSINLTFED-IKSEYISSFIIELLKKYKigH---RVVFEIVES---EGIDSFRKInefF 458
Cdd:PRK11059  465 QYDRQVIERVLPLLRYWPEEnLSINLSVDSlLSRAFQRWLRDTLLQCPR--SqrkRLIFELAEAdvcQHISRLRPV---L 539

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 459 VIIREYGCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIKDILINTSSQNIVSMLVNFAKGQKVKTIAEFVSNKDILNK 538
Cdd:PRK11059  540 RMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQT 619

                         250
                  ....*....|....*...
gi 2308551918 539 VRELGIDYVQGYYIKEPI 556
Cdd:PRK11059  620 LQELGVSGGQGDFFAESQ 637
GGDEF pfam00990
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ...
 164-299 1.28e-09

Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.


Pssm-ID: 425976 [Multi-domain]  Cd Length: 160  Bit Score: 57.26  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 164 FDSLTHIGNRYKLIEDVSKYINPC--------IAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEELL--IDKenyaIYR 233
Cdd:pfam00990   3 HDPLTGLPNRRYFEEQLEQELQRAlregspvaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLrrSDL----VAR 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 234 DHSDVFCIIAENEDKDKFLKNIEYISKTIGKVSIS--IKGRELYIQLSY--VFSFEPKENLLEtvnIIKR 299
Cdd:pfam00990  79 LGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtVSGLPLYVTISIgiAAYPNDGEDPED---LLKR 145
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 51-148 3.84e-09

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


Pssm-ID: 395786 [Multi-domain]  Cd Length: 113  Bit Score: 54.73  E-value: 3.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  51 ISTADLKGNITYVNERFCDVSLYTKEEVIGKPHSIVRGEEEDEIFRE-LWETIKSKKVWYGVLKN-RKKNGDFYWVNINI 128
Cdd:pfam00989  14 IFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAElLRQALLQGEESRGFEVSfRVPDGRPRHVEVRA 93

                          90       100
                  ....*....|....*....|
gi 2308551918 129 RPILNEKDEVIEYIAIRHEI 148
Cdd:pfam00989  94 SPVRDAGGEILGFLGVLRDI 113
GGDEF smart00267
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
 163-280 2.85e-07

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


Pssm-ID: 128563 [Multi-domain]  Cd Length: 163  Bit Score: 50.32  E-value: 2.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  163 RFDSLTHIGNRY-------KLIEDVSKYINP-CIAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEELLIDKEnyAIYRD 234
Cdd:smart00267   4 FRDPLTGLPNRRyfeeeleQELQRAQRQGSPfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGD--LLARL 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2308551918  235 HSDVFCIIAENEDkdkfLKNIEYISKTIGKV---SISIKGRELYIQLSY 280
Cdd:smart00267  82 GGDEFALLLPETS----LEEAIALAERILQQlrePIIIHGIPLYLTISI 126
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 50-159 1.08e-06

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 51.51  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  50 IISTADLKGNITYVNERFCDVSLYTKEEVIGKPHSIVRGEEEDEIFRELWETIKSKKVWYGVLKN-RKKNGDFYWVNINI 128
Cdd:COG5809    27 AILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDELEFElRHKNGKRLEFSSKL 106

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2308551918 129 RPILNEKDEVIEYIAIRHEITDLVLKTEELK 159
Cdd:COG5809   107 SPIFDQNGDIEGMLAISRDITERKRMEEALR 137
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
55-167 1.93e-06

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


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 50.23  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  55 DLKGNITYVNERFCDVSLYTKEEVIGKP-HSIVrgEEEDEIFRELWETIKSKK-VWYGVLKNRKKNGDFYWVNINIRPIL 132
Cdd:COG3852    24 DADGRITYVNPAAERLLGLSAEELLGRPlAELF--PEDSPLRELLERALAEGQpVTEREVTLRRKDGEERPVDVSVSPLR 101

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2308551918 133 NEkDEVIEYIAIRHEITDLVLKTEELKRNLRFDSL 167
Cdd:COG3852   102 DA-EGEGGVLLVLRDITERKRLERELRRAEKLAAV 135
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 51-200 2.20e-06

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


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 50.15  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  51 ISTADLKGNITYVNERFCDVSLYTKEEVIGKPhsivrgeeEDEIFRE--LWETIKSKKVWYGVLknRKKNGDFYWVNINI 128
Cdd:COG3829    24 IIVVDADGRITYVNRAAERILGLPREEVIGKN--------VTELIPNspLLEVLKTGKPVTGVI--QKTGGKGKTVIVTA 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2308551918 129 RPILnEKDEVIEYIAIRHEITDLvlktEELKRNLRFDSLTHIGNRYKLIED---VSKYINPCIAMLDIVSFSDVN 200
Cdd:COG3829    94 IPIF-EDGEVIGAVETFRDITEL----KRLERKLREEELERGLSAKYTFDDiigKSPAMKELLELAKRVAKSDST 163
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
 43-171 2.29e-06

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


Pssm-ID: 444511 [Multi-domain]  Cd Length: 489  Bit Score: 50.36  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  43 EATKDSNIIStaDLKGNITYVNERFCDVSLYTKEEVIGKPHSIV-RGEEEDEIFRELWETIKSKKVWYGVLKNRKKNGDF 121
Cdd:COG5809   148 NHSPDGIIVT--DLDGRIIYANPAACKLLGISIEELIGKSILELiHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRW 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2308551918 122 YWVNINIRPIlNEKDEVIEYIAIRHEITDLVlKTEELKRNLrfDSLTHIG 171
Cdd:COG5809   226 RLLEASGAPI-KKNGEVDGIVIIFRDITERK-KLEELLRKS--EKLSVVG 271
PRK11596 PRK11596
cyclic-di-GMP phosphodiesterase; Provisional
 440-566 5.35e-06

cyclic-di-GMP phosphodiesterase; Provisional


Pssm-ID: 183222 [Multi-domain]  Cd Length: 255  Bit Score: 48.07  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 440 FEIVESEGI---DSFRKINEFfviireygCKIAIDDFGSGYSNFEYLAKLNVDYIKIDGSLIkdILINTSSQ--NIVSML 514
Cdd:PRK11596  132 FELVEHIRLpkdSPFASMCEF--------GPLWLDDFGTGMANFSALSEVRYDYIKVARELF--IMLRQSEEgrNLFSQL 201

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2308551918 515 V----NFAKGqkvkTIAEFVSNKDILNKVRELGIDYVQGYYIKEPiASIDGLNDII 566
Cdd:PRK11596  202 LhlmnRYCRG----VIVEGVETPEEWRDVQRSPAFAAQGYFLSRP-APFETLETLP 252
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
 110-151 2.74e-05

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: 41.40  E-value: 2.74e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2308551918  110 GVLKNRKKNGDFYWVNINIRPILNEKDEVIEYIAIRHEITDL 151
Cdd:smart00086   2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
 48-277 5.13e-05

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


Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 45.88  E-value: 5.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  48 SNIISTADLKGNITYVNERFCDVSLYTKEEVIGKPHSIVRGEEEDEIFRELWETIKSKKVWYGVLKNRKKNGDFYWVNIN 127
Cdd:COG5805    44 PDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIYCKDGELIYVEVK 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 128 IRPILNEKDEVIEYIAIrhEITDLVLKTEELKRNlrfdslthiGNRYKLIEDvskyinpciAMLDIVSFSD-------VN 200
Cdd:COG5805   124 LFPIYNQNGQAAILALR--DITKKKKIEEILQEQ---------EERLQTLIE---------NSPDLICVIDtdgrilfIN 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 201 DFFGYKTGDSVLKIVARKIEELLIDKENYAIYRDHSDV------FCIIAENEDKDKFLKnieYISKTIGKVsISIKGREL 274
Cdd:COG5805   184 ESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESItevwqeFIIEREIITKDGRIR---YFEAVIVPL-IDTDGSVK 259


                  ...
gi 2308551918 275 YIQ 277
Cdd:COG5805   260 GIL 262
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
 55-152 5.17e-05

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


Pssm-ID: 312075 [Multi-domain]  Cd Length: 110  Bit Score: 42.79  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  55 DLKGNITYVNERFCDVSLYTKEEVIGKP----HSIVRGEEEDEIFRELWETiksKKVWYGVLkNRKKNGDFYWVNINIRP 130
Cdd:pfam08448  12 DPDGRVRYANAAAAELFGLPPEELLGKTlaelLPPEDAARLERALRRALEG---EEPIDFLE-ELLLNGEERHYELRLTP 87

                          90       100
                  ....*....|....*....|..
gi 2308551918 131 ILNEKDEVIEYIAIRHEITDLV 152
Cdd:pfam08448  88 LRDPDGEVIGVLVISRDITERR 109
GGDEF TIGR00254
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ...
 163-274 9.15e-05

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


Pssm-ID: 272984 [Multi-domain]  Cd Length: 165  Bit Score: 43.09  E-value: 9.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 163 RFDSLTHIGNRYKLiedvskyiNPCIAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEELLiDKENYAIyRDHSDVFCII 242
Cdd:TIGR00254  19 MLDSELKRARRFQR--------SFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSV-RGSDVVG-RYGGEEFVVI 88

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2308551918 243 AENEDKDKFLKNIEYISKTIGKVSISIKGREL 274
Cdd:TIGR00254  89 LPGTPLEDALSKAERLRDAINSKPIEVAGSET 120
PRK09894 PRK09894
diguanylate cyclase; Provisional
 165-242 1.26e-04

diguanylate cyclase; Provisional


Pssm-ID: 182133 [Multi-domain]  Cd Length: 296  Bit Score: 44.29  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 165 DSLTHIGNRYKLIEDVSKYI------NPCIAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEELLIDKEnyAIYRDHSDV 238
Cdd:PRK09894  132 DVLTGLPGRRVLDESFDHQLrnrepqNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYE--TVYRYGGEE 209


                  ....
gi 2308551918 239 FCII 242
Cdd:PRK09894  210 FIIC 213
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
 48-103 2.80e-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: 39.30  E-value: 2.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2308551918   48 SNIISTADLKGNITYVNERFCDVSLYTKEEVIGKP-HSIVRGEEEDEIFRELWETIK 103
Cdd:smart00091  11 PDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSlLELIHPEDRERVQEALQRLLS 67
PRK15426 PRK15426
cellulose biosynthesis regulator YedQ;
139-219 3.79e-03

cellulose biosynthesis regulator YedQ;


Pssm-ID: 237964 [Multi-domain]  Cd Length: 570  Bit Score: 40.00  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918 139 IEYIAIRHEITDLVLKTEELKRNLRFDSLTHIGNRYKLIEDVSKYINPCIA--------MLDIVSFSDVNDFFGYKTGDS 210
Cdd:PRK15426  375 ISWYVIRRMVSNMFVLQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRdqqpfsviQLDLDHFKSINDRFGHQAGDR 454


                  ....*....
gi 2308551918 211 VLKIVARKI 219
Cdd:PRK15426  455 VLSHAAGLI 463
PRK13559 PRK13559
hypothetical protein; Provisional
 60-163 4.79e-03

hypothetical protein; Provisional


Pssm-ID: 237427 [Multi-domain]  Cd Length: 361  Bit Score: 39.42  E-value: 4.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2308551918  60 ITYVNERFCDVSLYTKEEVIGKPHSIVRGEEEDEI-FRELWETIKSKKVWYGVLKNRKKNGDFYWVNINIRPILNEKDEV 138
Cdd:PRK13559   68 IVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIaVAKIRAAIAAEREIVVELLNYRKDGEPFWNALHLGPVYGEDGRL 147

                          90       100
                  ....*....|....*....|....*
gi 2308551918 139 IEYIAIRHEITDLVlKTEELKRNLR 163
Cdd:PRK13559  148 LYFFGSQWDVTDIR-AVRALEAHER 171
pleD PRK09581
response regulator PleD; Reviewed
 165-221 8.48e-03

response regulator PleD; Reviewed


Pssm-ID: 236577 [Multi-domain]  Cd Length: 457  Bit Score: 38.73  E-value: 8.48e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2308551918 165 DSLTHIGNRY-------KLIED-VSKYINPCIAMLDIVSFSDVNDFFGYKTGDSVLKIVARKIEE 221
Cdd:PRK09581  295 DGLTGLHNRRyfdmhlkNLIERaNERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN 359
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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