|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
116-687 |
1.42e-63 |
|
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: 221.58 E-value: 1.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 116 LLSVLRNTWADLHARRGLRRIEAQMRETERRCDALIASSRDPIAYIHEGMHIRANDAYLEMFGFESFDDVEGVSLLDMVA 195
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 196 PQHVEEFKQLLKSLGKGEPPPAQYQVDARTMEGESFPATMEFATASYEGEACVQVVFRRREEFDPELAREVEDLRQRDQV 275
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 276 TGLLNRPTFMLALENAVAQVGRGDGYYGFLLVEPDHYTRLLADIGLDSADALVAALARHLAAAIDGDVQAARFGEHNFAL 355
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 356 LLQGDYGRTSAQAERLLNAYAAHVFSVGERSATVTVSIGGVQIGEKIATVGQVLARASENVQATIELGGNACKIFDPGAA 435
Cdd:COG2200 241 LLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 436 DRVEEARiqRWVQQLREALAGDGFLLHYQPVLNLQGEPHELYEAYLRLERND-EIIGPTTFLGIAAEHGLMAEIDRWVVA 514
Cdd:COG2200 321 ARARRRL--ALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSGLIVELDRWVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 515 RAIAVIGARQRAGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKV 594
Cdd:COG2200 399 RALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 595 GLEQFGSGLDSFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQ 674
Cdd:COG2200 479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558
|
570
....*....|...
gi 822551857 675 GEFVGLAGPEMTF 687
Cdd:COG2200 559 GYLFGRPLPLEEL 571
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
447-679 |
1.67e-55 |
|
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: 189.45 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 447 VQQLREALAGDGFLLHYQPVLNLQGEPHELYEAYLRLE-RNDEIIGPTTFLGIAAEHGLMAEIDRWVVARAIAVIgARQR 525
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQhPDGGLISPARFLPLAEELGLIAELDRWVLEQALADL-AQLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 526 AGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSGLDS 605
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822551857 606 FQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQGEFVG 679
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFS 233
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
448-675 |
6.98e-52 |
|
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: 179.66 E-value: 6.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 448 QQLREALAGDGFLLHYQPVLNLQGepHEL--YEAYLRLERND-EIIGPTTFLGIAAEHGLMAEIDRWVVARAIAVIGARQ 524
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRT--GRIvgYEALLRWRHPEgGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 525 RAGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSGLD 604
Cdd:cd01948 79 AGGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822551857 605 SFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQG 675
Cdd:cd01948 159 SLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQG 229
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
448-684 |
2.86e-41 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 150.45 E-value: 2.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 448 QQLREALAGDGFLLHYQPVLNLQGEPHELYEAYLRLE-RNDEIIGPTTFLGIAAEHGLMAEIDRWVVARAIAVIG-ARQR 525
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQhPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAeWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 526 AGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSGLDS 605
Cdd:smart00052 82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822551857 606 FQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQGEFVGLAGPE 684
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
346-683 |
2.12e-32 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 134.41 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 346 ARFGEHNFALLLQG---DYGRTSAQaeRLLNAYAAHVFSVGERSATVTVSIGGVQIGEKIATVGQVLARASENVQATIEL 422
Cdd:PRK09776 741 ARLGGDEFGLLLPDcnvESARFIAT--RIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNA 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 423 GGNACKIFDPGAADRVEEARIQRWVQQLREALAGDGFLLHYQPVLNLQGEPHELYEAYLRLERND-EIIGPTTFLGIAAE 501
Cdd:PRK09776 819 GRGRVTVYEPQQAAAHSEHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEgEIIDEGAFRPAAED 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 502 HGLMAEIDRWVVARAIAVIGARQRAgHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQ 581
Cdd:PRK09776 899 PALMHALDRRVIHEFFRQAAKAVAS-KGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESAS 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 582 QFLSAATGLGCKVGLEQFGSGLDSFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATS 661
Cdd:PRK09776 978 RLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLV 1057
|
330 340
....*....|....*....|..
gi 822551857 662 MSLLFSAGVDYVQGEFVGLAGP 683
Cdd:PRK09776 1058 LDTLSGIGVDLAYGYAIARPQP 1079
|
|
| RpfG |
COG3437 |
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
1-148 |
8.43e-07 |
|
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];
Pssm-ID: 442663 [Multi-domain] Cd Length: 224 Bit Score: 50.55 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 1 MQTGKDttLRLMIVDDSGENAEAIVSSLRNSGIAVRPSrpQHAEELGAMLAAQPIDLVLSarsqAIPLP-----QVLQRV 75
Cdd:COG3437 1 MRTGQA--PTVLIVDDDPENLELLRQLLRTLGYDVVTA--ESGEEALELLLEAPPDLILL----DVRMPgmdgfELLRLL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822551857 76 GA--SGKDIPVILLADSIDENEWVEAVAGGARAIaLRQ--RPEHLLSVLRNTWADLHARRGLRRIEAQMRETERRCD 148
Cdd:COG3437 73 RAdpSTRDIPVIFLTALADPEDRERALEAGADDY-LTKpfDPEELLARVRNALELRRLQRELDDLVLYLKLAAPLHD 148
|
|
| REC |
cd00156 |
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ... |
12-104 |
1.05e-06 |
|
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381085 [Multi-domain] Cd Length: 99 Bit Score: 47.22 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 12 MIVDDSGENAEAIVSSLRNSGIAVRpsRPQHAEELGAMLAAQPIDLVLSArsqaIPLP-----QVLQRVGASGKDIPVIL 86
Cdd:cd00156 1 LIVDDDPAIRELLKSLLEREGYEVD--TAADGEEALELLREERPDLVLLD----LMMPgmdglELLRKLRELPPDIPVIV 74
|
90
....*....|....*...
gi 822551857 87 LADSIDENEWVEAVAGGA 104
Cdd:cd00156 75 LTAKADEEDAVRALELGA 92
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
144-233 |
8.60e-06 |
|
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: 45.36 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 144 ERRCDALIASSRDPIAYIHEGMHIR-ANDAYLEMFGFESfDDVEGVSLLDMVAPQHVEEFKQLLKSLGKGEPPPAQYQVD 222
Cdd:TIGR00229 2 EERYRAIFESSPDAIIVIDLEGNILyVNPAFEEIFGYSA-EELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERR 80
|
90
....*....|.
gi 822551857 223 ARTMEGESFPA 233
Cdd:TIGR00229 81 VRRKDGSEIWV 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
116-687 |
1.42e-63 |
|
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: 221.58 E-value: 1.42e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 116 LLSVLRNTWADLHARRGLRRIEAQMRETERRCDALIASSRDPIAYIHEGMHIRANDAYLEMFGFESFDDVEGVSLLDMVA 195
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 196 PQHVEEFKQLLKSLGKGEPPPAQYQVDARTMEGESFPATMEFATASYEGEACVQVVFRRREEFDPELAREVEDLRQRDQV 275
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 276 TGLLNRPTFMLALENAVAQVGRGDGYYGFLLVEPDHYTRLLADIGLDSADALVAALARHLAAAIDGDVQAARFGEHNFAL 355
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 356 LLQGDYGRTSAQAERLLNAYAAHVFSVGERSATVTVSIGGVQIGEKIATVGQVLARASENVQATIELGGNACKIFDPGAA 435
Cdd:COG2200 241 LLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 436 DRVEEARiqRWVQQLREALAGDGFLLHYQPVLNLQGEPHELYEAYLRLERND-EIIGPTTFLGIAAEHGLMAEIDRWVVA 514
Cdd:COG2200 321 ARARRRL--ALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDgGLISPAEFIPAAERSGLIVELDRWVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 515 RAIAVIGARQRAGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKV 594
Cdd:COG2200 399 RALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 595 GLEQFGSGLDSFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQ 674
Cdd:COG2200 479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558
|
570
....*....|...
gi 822551857 675 GEFVGLAGPEMTF 687
Cdd:COG2200 559 GYLFGRPLPLEEL 571
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
447-679 |
1.67e-55 |
|
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: 189.45 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 447 VQQLREALAGDGFLLHYQPVLNLQGEPHELYEAYLRLE-RNDEIIGPTTFLGIAAEHGLMAEIDRWVVARAIAVIgARQR 525
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQhPDGGLISPARFLPLAEELGLIAELDRWVLEQALADL-AQLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 526 AGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSGLDS 605
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 822551857 606 FQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQGEFVG 679
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFS 233
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
448-675 |
6.98e-52 |
|
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: 179.66 E-value: 6.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 448 QQLREALAGDGFLLHYQPVLNLQGepHEL--YEAYLRLERND-EIIGPTTFLGIAAEHGLMAEIDRWVVARAIAVIGARQ 524
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRT--GRIvgYEALLRWRHPEgGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 525 RAGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSGLD 604
Cdd:cd01948 79 AGGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822551857 605 SFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQG 675
Cdd:cd01948 159 SLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQG 229
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
41-679 |
6.99e-47 |
|
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: 176.50 E-value: 6.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 41 QHAEELGAMLAAQPIDLVLSARSQAIPLPQVLQRVGASGKDIPVILLADSIDENEWVEAVAGGARAIALRQRPEHLLSVL 120
Cdd:COG5001 20 LLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLAL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 121 RNTWADLHARRGLRRIEAQMRETERRcDALIASSRDPIAYIHEGMHIRANDAYLEMFGFESFDDVEGVSLLDMVAPQHVE 200
Cdd:COG5001 100 LVLLLLLLLLLALLALLAALLARALA-ALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 201 EFKQLLKSLGKGEPPPAQYQVDARTMEGESFPATMEFATASYEGEACVQVVFRRREEFDPELAREVEDLRQ---RDQVTG 277
Cdd:COG5001 179 LLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHlayHDPLTG 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 278 LLNRPTFMLALENAVAQVGRGDGYYGFLLVEPDHY--------------------TRLLADIGldsadalvaalarhlaa 337
Cdd:COG5001 259 LPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFkeindtlghaagdellrevaRRLRACLR----------------- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 338 aiDGDVqAARFG--EhnFALLLQGDYGRTSAQ--AERLLNAyAAHVFSVGERSATVTVSIGGVQIGEKIATVGQVLARAs 413
Cdd:COG5001 322 --EGDT-VARLGgdE--FAVLLPDLDDPEDAEavAERILAA-LAEPFELDGHELYVSASIGIALYPDDGADAEELLRNA- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 414 envqaTI------ELGGNACKIFDPGAADRVEEARiqRWVQQLREALAGDGFLLHYQPVLNLQ-GEPHElYEAYLRLERN 486
Cdd:COG5001 395 -----DLamyrakAAGRNRYRFFDPEMDERARERL--ELEADLRRALERGELELHYQPQVDLAtGRIVG-AEALLRWQHP 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 487 DE-IIGPTTFLGIAAEHGLMAEIDRWVVARAIAVIGARQRAGHAT-SLLVKISPDAFADLQMVELIRRELAAHGVPGERL 564
Cdd:COG5001 467 ERgLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDlRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRL 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 565 WLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSGLDSFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERA 644
Cdd:COG5001 547 ELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALA 626
|
650 660 670
....*....|....*....|....*....|....*
gi 822551857 645 QSAGIRSIAEFVADATSMSLLFSAGVDYVQGEFVG 679
Cdd:COG5001 627 HSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFS 661
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
448-684 |
2.86e-41 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 150.45 E-value: 2.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 448 QQLREALAGDGFLLHYQPVLNLQGEPHELYEAYLRLE-RNDEIIGPTTFLGIAAEHGLMAEIDRWVVARAIAVIG-ARQR 525
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQhPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAeWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 526 AGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSGLDS 605
Cdd:smart00052 82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822551857 606 FQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQGEFVGLAGPE 684
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
346-683 |
2.12e-32 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 134.41 E-value: 2.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 346 ARFGEHNFALLLQG---DYGRTSAQaeRLLNAYAAHVFSVGERSATVTVSIGGVQIGEKIATVGQVLARASENVQATIEL 422
Cdd:PRK09776 741 ARLGGDEFGLLLPDcnvESARFIAT--RIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNA 818
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 423 GGNACKIFDPGAADRVEEARIQRWVQQLREALAGDGFLLHYQPVLNLQGEPHELYEAYLRLERND-EIIGPTTFLGIAAE 501
Cdd:PRK09776 819 GRGRVTVYEPQQAAAHSEHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEgEIIDEGAFRPAAED 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 502 HGLMAEIDRWVVARAIAVIGARQRAgHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQ 581
Cdd:PRK09776 899 PALMHALDRRVIHEFFRQAAKAVAS-KGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESAS 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 582 QFLSAATGLGCKVGLEQFGSGLDSFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITERAQSAGIRSIAEFVADATS 661
Cdd:PRK09776 978 RLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLV 1057
|
330 340
....*....|....*....|..
gi 822551857 662 MSLLFSAGVDYVQGEFVGLAGP 683
Cdd:PRK09776 1058 LDTLSGIGVDLAYGYAIARPQP 1079
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
269-687 |
9.53e-22 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 100.02 E-value: 9.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 269 LRQRDQVTGLLNRPTFMLALENAVAQVGRGDGYYGFLLVEPdhyTRLLADIGLDSA--DALVAALARHLAAAIDGDVQAA 346
Cdd:PRK11829 231 ISHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVIGIE---TLQEVSGAMSEAqhQQLLLTIVQRIEQCIDDSDLLA 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 347 RFGEHNFaLLLQGDYGRTS---AQAERLLNAYAAHVFsVGERSATVTVSIGGVQIGEKIATVGQVLARASENVQATIELG 423
Cdd:PRK11829 308 QLSKTEF-AVLARGTRRSFpamQLARRIMSQVTQPLF-FDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEG 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 424 GNACKIFDPGAADRVEEARIQRwvQQLREALAGDGFLLHYQPVLNLQGEPHELYEAYLRLERND-EIIGPTTFLGIAAEH 502
Cdd:PRK11829 386 RNQIMVFEPHLIEKTHKRLTQE--NDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDgSYVLPSGFVHFAEEE 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 503 GLMAEIDRWVVARAIAVIGARQRAGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGERLWLQTPEAKVFTHLRNAQQ 582
Cdd:PRK11829 464 GMMVPLGNWVLEEACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALR 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 583 FLSAATGLGCKVGLEQFGSGLDSFQLLAHFQP---SFLKLDRGFTQDLAqtrEHQEKIREITERAQSAGIRSIAEFVADA 659
Cdd:PRK11829 544 LLRELQGLGLLIALDDFGIGYSSLRYLNHLKSlpiHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAEGVETE 620
|
410 420
....*....|....*....|....*...
gi 822551857 660 TSMSLLFSAGVDYVQGEFVGLAGPEMTF 687
Cdd:PRK11829 621 EQRQWLLEHGIQCGQGFLFSPPLPRAEF 648
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
273-675 |
5.22e-19 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 91.28 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 273 DQVTGLLNRPTFMLALENAVAQvgRGDGYYGFLLVEPDHYTRLLADIGLDSADALVAALARHLAAAIDGDVQAARFGEHN 352
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINA--ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDE 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 353 FALLL-QGDYGRTSAQAERLLNAYAaHVFSVGERSATVTVSIG---GVQIGEKIATvgqvLARASENVQATIELGGNAC- 427
Cdd:PRK10060 318 FLVLAsHTSQAALEAMASRILTRLR-LPFRIGLIEVYTGCSIGialAPEHGDDSES----LIRSADTAMYTAKEGGRGQf 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 428 KIFDPGAADRVEEariQRWVQ-QLREALAGDGFLLHYQPVLNLQGEPHELyEAYLRLERNDE-IIGPTTFLGIAAEHGLM 505
Cdd:PRK10060 393 CVFSPEMNQRVFE---YLWLDtNLRKALENDQLVIHYQPKITWRGEVRSL-EALVRWQSPERgLIPPLEFISYAEESGLI 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 506 AEIDRWVVARAIAVIGARQRAGHATSLLVKISPDAFADLQMVE------------------------LIRRELAAHGVpg 561
Cdd:PRK10060 469 VPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTalkqalqelnfeycpidveltescLIENEELALSV-- 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 562 erlwlqtpeakvfthlrnAQQFlsaaTGLGCKVGLEQFGSGLDSFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREIT 641
Cdd:PRK10060 547 ------------------IQQF----SQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIV 604
|
410 420 430
....*....|....*....|....*....|....
gi 822551857 642 ERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQG 675
Cdd:PRK10060 605 AVAQALNLQVIAEGVETAKEDAFLTKNGVNERQG 638
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
261-677 |
6.55e-15 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 78.66 E-value: 6.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 261 ELAREVEDLRQR-------DQVTGLLNRPTFMLALENAVAQvgrgDGYYGFLLVEPDHYTRLLADIGLDSADALVAALAR 333
Cdd:PRK11359 360 ALALEQEKSRQHieqliqfDPLTGLPNRNNLHNYLDDLVDK----AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 334 HLAAAIDGDVQAARFGEHNFALLLQG-DYGRTSAQAERLLNAYAAHVfSVGERSATVTVSIGgvqIGEKIATVGQVLARA 412
Cdd:PRK11359 436 RFREKLKPDQYLCRIEGTQFVLVSLEnDVSNITQIADELRNVVSKPI-MIDDKPFPLTLSIG---ISYDVGKNRDYLLST 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 413 SENVQATI-ELGGNACKIFDPGaadrVEEARIQRWV--QQLREALAGDGFLLHYQPvlNLQGEPHELY--EAYLRLerND 487
Cdd:PRK11359 512 AHNAMDYIrKNGGNGWQFFSPA----MNEMVKERLVlgAALKEAISNNQLKLVYQP--QIFAETGELYgiEALARW--HD 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 488 EIIG---PTTFLGIAAEHGLMAEIDRWVVARAIAVIGA-RQRAGHATSLLVKISPDAFADLQMVELIRRELAAHGVPGER 563
Cdd:PRK11359 584 PLHGhvpPSRFIPLAEEIGEIENIGRWVIAEACRQLAEwRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQ 663
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 564 LWLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSGLDSFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITER 643
Cdd:PRK11359 664 LTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSI 743
|
410 420 430
....*....|....*....|....*....|....
gi 822551857 644 AQSAGIRSIAEFVADATSMSLLFSAGVDYVQGEF 677
Cdd:PRK11359 744 GQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYF 777
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
404-688 |
1.61e-13 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 73.98 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 404 TVGQVLARASENVQATIELGGNACKIFDPGAADRVEeariQRWVQQ--LREALAGDGFLLHYQPVLNLQGEPHELYEAYL 481
Cdd:PRK13561 361 TAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQ----KRLTEEsdILNALENHQFAIWLQPQVEMRSGKLVSAEALL 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 482 RLERNDEIIG-PTTFLGIAAEHGLMAEIDRWVVARAIAVIGARQRAGHATSLLVKISPDAFADLQMVELIRRELAAHGVP 560
Cdd:PRK13561 437 RMQQPDGSWDlPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQ 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 561 GERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSGLDSFQLLAHFQP---SFLKLDRGFTQDLAqtrEHQEKI 637
Cdd:PRK13561 517 PGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSlpiDVLKIDKMFVDGLP---EDDSMV 593
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 822551857 638 REITERAQSAGIRSIAEFVADATSMSLLFSAGVDYVQGEFVGLAGPEMTFD 688
Cdd:PRK13561 594 AAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFE 644
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
261-430 |
5.88e-12 |
|
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: 66.93 E-value: 5.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 261 ELAREVEDLRQRDQVTGLLNRPTFMLALENAVAQVGRGDGYYGFLLVEPDHYTRLLADIGLDSADALVAALARHLAAAID 340
Cdd:COG2199 105 RLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLR 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 341 GDVQAARFGEHNFALLLQG-DYGRTSAQAERLLNAYAAHVFSVGERSATVTVSIGGVQIGEKIATVGQVLARASENVQAT 419
Cdd:COG2199 185 ESDLVARLGGDEFAVLLPGtDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRA 264
|
170
....*....|.
gi 822551857 420 IELGGNACKIF 430
Cdd:COG2199 265 KRAGRNRVVVY 275
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
445-677 |
7.02e-10 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 62.19 E-value: 7.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 445 RWVQQLREALAGDGFLLHYQPVLNLQGEPHElYEAYLRL-ERNDEIIGPTTFLGIAAEHGLMAEIDRWVVARAIAVIGAR 523
Cdd:PRK11059 403 RWRTLLEQTLVRGGPRLYQQPAVTRDGKVHH-RELFCRIrDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYW 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 524 QraghATSLLVKISPDAFADLQMVELIRRELAAHGVP-GERLWLQTPEAKVFTHLRNAQQFLSAATGLGCKVGLEQFGSG 602
Cdd:PRK11059 482 P----EENLSINLSVDSLLSRAFQRWLRDTLLQCPRSqRKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLT 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 603 LDSFQLLAHFQPSFLKLDRGFTQDLAQTREHQEKIREITE-----RAQ--SAGIRSIAEFvadatsmSLLFSAGVDYVQG 675
Cdd:PRK11059 558 VVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGacagtETQvfATGVESREEW-------QTLQELGVSGGQG 630
|
..
gi 822551857 676 EF 677
Cdd:PRK11059 631 DF 632
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
271-412 |
1.17e-08 |
|
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: 54.48 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 271 QRDQVTGLLNRPTFMLALENAVAQVGRGDGYYGFLLVEPDHYTRLLADIGLDSADALVAALARHLAAAIDGDVQAARFGE 350
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 822551857 351 HNFALLLQG-DYGRTSAQAERLLNAYAAHVFsVGERSATVTVSIGGVQIGEKIATVGQVLARA 412
Cdd:cd01949 81 DEFAILLPGtDLEEAEALAERLREAIEEPFF-IDGQEIRVTASIGIATYPEDGEDAEELLRRA 142
|
|
| RpfG |
COG3437 |
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
1-148 |
8.43e-07 |
|
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];
Pssm-ID: 442663 [Multi-domain] Cd Length: 224 Bit Score: 50.55 E-value: 8.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 1 MQTGKDttLRLMIVDDSGENAEAIVSSLRNSGIAVRPSrpQHAEELGAMLAAQPIDLVLSarsqAIPLP-----QVLQRV 75
Cdd:COG3437 1 MRTGQA--PTVLIVDDDPENLELLRQLLRTLGYDVVTA--ESGEEALELLLEAPPDLILL----DVRMPgmdgfELLRLL 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 822551857 76 GA--SGKDIPVILLADSIDENEWVEAVAGGARAIaLRQ--RPEHLLSVLRNTWADLHARRGLRRIEAQMRETERRCD 148
Cdd:COG3437 73 RAdpSTRDIPVIFLTALADPEDRERALEAGADDY-LTKpfDPEELLARVRNALELRRLQRELDDLVLYLKLAAPLHD 148
|
|
| REC |
cd00156 |
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ... |
12-104 |
1.05e-06 |
|
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381085 [Multi-domain] Cd Length: 99 Bit Score: 47.22 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 12 MIVDDSGENAEAIVSSLRNSGIAVRpsRPQHAEELGAMLAAQPIDLVLSArsqaIPLP-----QVLQRVGASGKDIPVIL 86
Cdd:cd00156 1 LIVDDDPAIRELLKSLLEREGYEVD--TAADGEEALELLREERPDLVLLD----LMMPgmdglELLRKLRELPPDIPVIV 74
|
90
....*....|....*...
gi 822551857 87 LADSIDENEWVEAVAGGA 104
Cdd:cd00156 75 LTAKADEEDAVRALELGA 92
|
|
| OmpR |
COG0745 |
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ... |
8-104 |
5.37e-06 |
|
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 440508 [Multi-domain] Cd Length: 204 Bit Score: 47.64 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 8 TLRLMIVDDSGENAEAIVSSLRNSGIAVRPSRpqHAEELGAMLAAQPIDLVLSARSqaipLP-----QVLQRVGASGKDI 82
Cdd:COG0745 1 MPRILVVEDDPDIRELLADALEREGYEVDTAA--DGEEALELLEEERPDLILLDLM----LPgmdglEVCRRLRARPSDI 74
|
90 100
....*....|....*....|..
gi 822551857 83 PVILLADSIDENEWVEAVAGGA 104
Cdd:COG0745 75 PIIMLTARDDEEDRVRGLEAGA 96
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
144-233 |
8.60e-06 |
|
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: 45.36 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 144 ERRCDALIASSRDPIAYIHEGMHIR-ANDAYLEMFGFESfDDVEGVSLLDMVAPQHVEEFKQLLKSLGKGEPPPAQYQVD 222
Cdd:TIGR00229 2 EERYRAIFESSPDAIIVIDLEGNILyVNPAFEEIFGYSA-EELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERR 80
|
90
....*....|.
gi 822551857 223 ARTMEGESFPA 233
Cdd:TIGR00229 81 VRRKDGSEIWV 91
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
112-252 |
1.05e-05 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 47.71 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 112 RPEHLLSVLRntwaDLHARRglrRIEAQMRETERRCDALIASSRDPIAYI-HEGMHIRANDAYLEMFGFESfDDVEGVSL 190
Cdd:COG2202 111 EITGFVGIAR----DITERK---RAEEALRESEERLRLLVENAPDGIFVLdLDGRILYVNPAAEELLGYSP-EELLGKSL 182
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 822551857 191 LDMVAPQHVEEFKQLLKSLGKGEPPPaqYQVDARTMEGESFPATMEFATASYEGEACVQVVF 252
Cdd:COG2202 183 LDLLHPEDRERLLELLRRLLEGGRES--YELELRLKDGDGRWVWVEASAVPLRDGGEVIGVL 242
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
7-158 |
1.90e-05 |
|
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];
Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 47.65 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 7 TTLRLMIVDDSGENAEAIVSSLRNSGIAVRPSrpQHAEELGAMLAAQPIDLVLSArsqaIPLP-----QVLQRVGASGKD 81
Cdd:COG2204 1 SMARILVVDDDPDIRRLLKELLERAGYEVETA--ASGEEALALLREEPPDLVLLD----LRMPgmdglELLRELRALDPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 82 IPVILLADSIDENEWVEAVAGGARA-IALRQRPEHLLSVLRNTWADLHARRGLRRIE------AQMRETERRCdALIASS 154
Cdd:COG2204 75 LPVILLTGYGDVETAVEAIKAGAFDyLTKPFDLEELLAAVERALERRRLRRENAEDSgligrsPAMQEVRRLI-EKVAPS 153
|
....
gi 822551857 155 RDPI 158
Cdd:COG2204 154 DATV 157
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
135-213 |
3.17e-05 |
|
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: 46.89 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 135 RIEAQMRETERRCDALIASSRDPIAYIHEGMHI-RANDAYLEMFGFESfDDVEGVSLLDMVAPQHVEEFKQLLKSLGKGE 213
Cdd:COG5809 5 KMELQLRKSEQRFRSLFENAPDAILILDLEGKIlKVNPAAERIFGYTE-DELLGTNILDFLHPDDEKELREILKLLKEGE 83
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
139-274 |
4.58e-05 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 46.38 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 139 QMRETERRCDALIASSRDPIAYIHEGMHIR-ANDAYLEMFGFeSFDDVEGVSLLDMVAPQhvEEFKQLLKSLGKGEPPPA 217
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITyVNPAAERLLGL-SAEELLGRPLAELFPED--SPLRELLERALAEGQPVT 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 822551857 218 QYQVDARTMEGESFPATMEFAT-ASYEGEACVQVVFRRREEFDpELAREvedLRQRDQ 274
Cdd:COG3852 78 EREVTLRRKDGEERPVDVSVSPlRDAEGEGGVLLVLRDITERK-RLERE---LRRAEK 131
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
272-430 |
5.52e-05 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 44.16 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 272 RDQVTGLLNRPTFMLALENAVAQVGRGDGYYGFLLVEPDHYTRLLADIGLDSADALVAALARHLAAAI-DGDVqAARFGE 350
Cdd:smart00267 5 RDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLrPGDL-LARLGG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 351 HNFALLLQGdygrTSAQ-----AERLLNAYAAHVFsVGERSATVTVSIGGVQIGEKIATVGQVLARASENVQATIELGGN 425
Cdd:smart00267 84 DEFALLLPE----TSLEeaialAERILQQLREPII-IHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRN 158
|
....*
gi 822551857 426 ACKIF 430
Cdd:smart00267 159 QVAVY 163
|
|
| CheY |
COG0784 |
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ... |
9-121 |
2.87e-04 |
|
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];
Pssm-ID: 440547 [Multi-domain] Cd Length: 128 Bit Score: 41.37 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 9 LRLMIVDDSGENAEAIVSSLRNSGIAVRPSRpqHAEELGAMLAAQPIDLVLSarsqAIPLP-----QVLQRV--GASGKD 81
Cdd:COG0784 6 KRILVVDDNPDNRELLRRLLERLGYEVTTAE--DGAEALELLRAGPPDLILL----DINMPgmdglELLRRIraLPRLPD 79
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 822551857 82 IPVILLADSIDENEWVEAVAGGARA-IALRQRPEHLLSVLR 121
Cdd:COG0784 80 IPIIALTAYADEEDRERALEAGADDyLTKPVDPEELLEALR 120
|
|
| AmiR |
COG3707 |
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ... |
9-146 |
3.81e-04 |
|
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 442921 [Multi-domain] Cd Length: 194 Bit Score: 42.25 E-value: 3.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 9 LRLMIVDDSGENAEAIVSSLRNSGIAVRPSRPQHAEELGAMLAAQPIDLVLSARSQAIPLPQVLQRVGASgKDIPVILLA 88
Cdd:COG3707 4 LRVLVVDDEPLRRADLREGLREAGYEVVAEAADGEDAVELVRELKPDLVIVDIDMPDRDGLEAARQISEE-RPAPVILLT 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 822551857 89 DSIDENEWVEAVAGGARAIALRQ-RPEHLLSVLRNTWADLHARRGLRRIEAQMRET--ERR 146
Cdd:COG3707 83 AYSDPELIERALEAGVSAYLVKPlDPEDLLPALELALARFRELRALRRELAKLREAleERK 143
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
271-431 |
4.92e-04 |
|
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: 41.17 E-value: 4.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 271 QRDQVTGLLNRPTFMLALENAVAQVGRGDGYYGFLLVEPDHYTRLLADIGLDSADALVAALARHLAAAIDGDVQAARFGE 350
Cdd:TIGR00254 3 VRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 351 HNFALLLQG-DYGRTSAQAERLLNAYAAHVFSVGERSA-TVTVSIGGVQIGEKIATVGQVLARASENVQATIELGGNACK 428
Cdd:TIGR00254 83 EEFVVILPGtPLEDALSKAERLRDAINSKPIEVAGSETlTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRVV 162
|
...
gi 822551857 429 IFD 431
Cdd:TIGR00254 163 VAD 165
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
8-104 |
7.18e-04 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 41.05 E-value: 7.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 8 TLRLMIVDDSGENAEAIVSSLRNSGIAVRPSrpQHAEELGAMLAAQPIDLVLSarsqAIPLP-----QVLQRV--GASGK 80
Cdd:COG3706 1 PARILVVDDDPTNRKLLRRLLEAAGYEVVEA--ADGEEALELLQEHRPDLILL----DLEMPdmdglELCRRLraDPRTA 74
|
90 100
....*....|....*....|....
gi 822551857 81 DIPVILLADSIDENEWVEAVAGGA 104
Cdd:COG3706 75 DIPIIFLTALDDEEDRARALEAGA 98
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
145-209 |
1.11e-03 |
|
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: 37.76 E-value: 1.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 822551857 145 RRCDALIASSRDPIAYIHEGMHIR-ANDAYLEMFGFeSFDDVEGVSLLDMVAPQHVEEFKQLLKSL 209
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILyANPAAEELLGY-SPEELIGKSLLELIHPEDRERVQEALQRL 65
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
272-425 |
1.45e-03 |
|
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: 39.93 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 272 RDQVTGLLNRPTFMLALENAVAQVGRGDGYYGFLLVEPDHYTRLLADIGLDSADALVAALARHLAAAI-DGDVqAARFGE 350
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLrRSDL-VARLGG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 822551857 351 HNFALLLQG---DYGRTSAQ-AERLLNAYAAHvFSVGERSATVTVSIGGVQIGEKIATVGQVLARASENVQATIELGGN 425
Cdd:pfam00990 82 DEFAILLPEtslEGAQELAErIRRLLAKLKIP-HTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
169-251 |
2.67e-03 |
|
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: 38.00 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 169 ANDAYLEMFGFeSFDDVEGVSLLDMVAPQHVEEFKQLLKSLGKGEPPPaQYQVDARTMEGESFPATMEFATASYEGEACV 248
Cdd:cd00130 17 ANPAAEQLLGY-SPEELIGKSLLDLIHPEDREELRERLENLLSGGEPV-TLEVRLRRKDGSVIWVLVSLTPIRDEGGEVI 94
|
...
gi 822551857 249 QVV 251
Cdd:cd00130 95 GLL 97
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
273-416 |
4.13e-03 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 40.27 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 273 DQVTGLLNRPTFMLALENAVAQVGRGDGYYGFLLVEPDHYTRLLADIGLDSADALVAALARHLAAAIDGDVQAARFGEHN 352
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 353 FALLL----QGDYGRTsaqAERLLNAYAAHVFSV--GERSATVTVSIGGVQIGEKIATVGQVLARASENV 416
Cdd:PRK09581 375 FVVVMpdtdIEDAIAV---AERIRRKIAEEPFIIsdGKERLNVTVSIGVAELRPSGDTIEALIKRADKAL 441
|
|
| CitB |
COG4565 |
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ... |
7-104 |
6.43e-03 |
|
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];
Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 37.64 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 7 TTLRLMIVDDSGENAEAIVSSLRNSGIAVRPSRPQHAEELGAMLAAQPIDLVLSarsqAIPLP-----QVLQRVGASGKD 81
Cdd:COG4565 2 KMIRVLIVEDDPMVAELLRRYLERLPGFEVVGVASSGEEALALLAEHRPDLILL----DIYLPdgdglELLRELRARGPD 77
|
90 100
....*....|....*....|...
gi 822551857 82 IPVILLADSIDENEWVEAVAGGA 104
Cdd:COG4565 78 VDVIVITAARDPETVREALRAGV 100
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
135-215 |
6.62e-03 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 38.85 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 822551857 135 RIEAQMRETERRCDALIASSRDPIAYI-HEGMHIRANDAYLEMFGFeSFDDVEGVSLLDMVAPQHVEEFKQLLKSLGKGE 213
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITdLDGRILYVNPAFERLTGY-SAEELLGKTLRDLLPPEDDDEFLELLRAALAGG 79
|
..
gi 822551857 214 PP 215
Cdd:COG2202 80 GV 81
|
|
| |
