|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
494-651 |
4.03e-44 |
|
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: 155.41 E-value: 4.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 494 IDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLGGE 572
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERlLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880811218 573 EFVIMLTDTTPAEVRERVEELHYAISSTVFLSEskKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGRNCII 651
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDG--QEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
404-650 |
2.36e-43 |
|
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: 157.45 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 404 AFYFYQRYSSIQMEARDIDNRLALEALGLTHAEYEQELENSFLTHQTKLDRVQIEKMEHQRwMYNIVVILLLCAASFTVL 483
Cdd:COG2199 27 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLL-LALLLLLLALEDITELRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 484 VNKTVRAKAAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVN 562
Cdd:COG2199 106 LEERLRRLATHDPLTGLPNRRAFEERLEReLARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 563 GELFGRLGGEEFVIMLTDTTPAEVRERVEELHYAISSTVFLSESkKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQA 642
Cdd:COG2199 186 SDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEG-KELRVTVSIGVALYPEDGDSAEELLRRADLALYRA 264
|
....*...
gi 880811218 643 KSNGRNCI 650
Cdd:COG2199 265 KRAGRNRV 272
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
492-649 |
3.50e-35 |
|
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: 130.45 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 492 AAIDGLTKAYSRTEIIRRIKRV-KRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLG 570
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQElQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 571 GEEFVIMLTDTTP---AEVRERVEELHYAISSTVFLSEskKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGR 647
Cdd:pfam00990 81 GDEFAILLPETSLegaQELAERIRRLLAKLKIPHTVSG--LPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGR 158
|
..
gi 880811218 648 NC 649
Cdd:pfam00990 159 NR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
492-650 |
1.49e-34 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 128.90 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 492 AAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLG 570
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQeLQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 571 GEEFVIMLTDTTPAEVRERVEELHYAISSTVFLSEskKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGRNCI 650
Cdd:smart00267 83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHG--IPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
492-648 |
2.99e-33 |
|
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: 125.14 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 492 AAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLG 570
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSeLKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880811218 571 GEEFVIMLTDTTPAEVRERVEELHYAISSTVFLSESKKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGRN 648
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
485-650 |
1.29e-29 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 117.78 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 485 NKTVRAKAAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNG 563
Cdd:NF038266 87 NEALREASTRDPLTGLPNRRLLMERLREeVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 564 ELFGRLGGEEFVIMLTDTTPAEVRERVEELHYAISSTVFlSESKKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAK 643
Cdd:NF038266 167 DLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAV-RVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAK 245
|
....*..
gi 880811218 644 SNGRNCI 650
Cdd:NF038266 246 RAGRDRV 252
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
495-657 |
4.03e-28 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 119.35 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 495 DGLTKAYSRTEIIRRIKRV-KRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLGGEE 573
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALaKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 574 FVIMLTDTTPAEVRERVEELHYAISSTVFLSESKKSLNVTASFAYL-ATSNALSDFDDLYSVLDQALYQAKSNGRN--CI 650
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSsAEEDGDYDFEQLQSLADRRLYLAKQAGRNrvCA 560
|
....*..
gi 880811218 651 IDAYNEP 657
Cdd:PRK15426 561 SDNAHER 567
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
191-442 |
5.03e-11 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 63.98 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 191 TYRVIANNHHFRSDYQAALDTYLSLINVFPQGHDisgVYNDVGNLLKELKQYEKSAEYLHEALTLRENAsdlmkAQVHHS 270
Cdd:COG2956 44 AHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAE---ALLELAQDYLKAGLLDRAEELLEKLLELDPDD-----AEALRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 271 LADLNLNQEQSDLAIHHFQTARTLLSSSSHSYgialtsLGLGKAYTQTKDYDLARTYLveslsasselsNDVIRIN---- 346
Cdd:COG2956 116 LAEIYEQEGDWEKAIEVLERLLKLGPENAHAY------CELAELYLEQGDYDEAIEAL-----------EKALKLDpdca 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 347 -AYLAISDMFEEQKLPTEALNYAQQALGLAEQVARHkyitqsLLQLSDINQSLNDYQQAFYFYQRYSSIQMEARDIDN-- 423
Cdd:COG2956 179 rALLLLAELYLEQGDYEEAIAALERALEQDPDYLPA------LPRLAELYEKLGDPEEALELLRKALELDPSDDLLLAla 252
|
250 260
....*....|....*....|.
gi 880811218 424 RLALEALGLTHAE--YEQELE 442
Cdd:COG2956 253 DLLERKEGLEAALalLERQLR 273
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
224-295 |
1.28e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 38.14 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880811218 224 DISGVYNDVGNLLKELKQYEKSAEYLHEALTLRENASD---LMKAQVHHSLADLNLNQEQSDLAIHHFQTARTLL 295
Cdd:pfam13424 1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGpdhPLTATTLLNLGRLYLELGRYEEALELLERALALA 75
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
120-432 |
2.15e-03 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 41.22 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 120 GKGQYEEAQQGFLTLLAKMQSRSDlagkalLKYQLCRSLNEQAKYHQANyycsalqsdlyNIADPVL---PKFgtyrviA 196
Cdd:TIGR02917 137 GLGQLELAQKSYEQALAIDPRSLY------AKLGLAQLALAENRFDEAR-----------ALIDEVLtadPGN------V 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 197 NNHHFRSDYQ-------AALDTYLSLINVFPQghDISGVYNDVGNLLkELKQYEKSAEYLHEALTLRENasdlmKAQVHH 269
Cdd:TIGR02917 194 DALLLKGDLLlslgnieLALAAYRKAIALRPN--NIAVLLALATILI-EAGEFEEAEKHADALLKKAPN-----SPLAHY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 270 SLADLNLNQEQSDLAIHHFQTArtllSSSSHSYGIALtsLGLGKAYTQTKDYDLARTYLVESLSASSELSNdVIRInayL 349
Cdd:TIGR02917 266 LKALVDFQKKNYEDARETLQDA----LKSAPEYLPAL--LLAGASEYQLGNLEQAYQYLNQILKYAPNSHQ-ARRL---L 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 350 AISDMfeEQKLPTEALNYAQQALGLAEQVArhkyitQSLLQLSDINQSLNDYQQAFYFYQRYSSIQMEARDIDNRLALEA 429
Cdd:TIGR02917 336 ASIQL--RLGRVDEAIATLSPALGLDPDDP------AALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGISK 407
|
...
gi 880811218 430 LGL 432
Cdd:TIGR02917 408 LSQ 410
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
494-651 |
4.03e-44 |
|
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: 155.41 E-value: 4.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 494 IDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLGGE 572
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERlLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880811218 573 EFVIMLTDTTPAEVRERVEELHYAISSTVFLSEskKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGRNCII 651
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDG--QEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
404-650 |
2.36e-43 |
|
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: 157.45 E-value: 2.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 404 AFYFYQRYSSIQMEARDIDNRLALEALGLTHAEYEQELENSFLTHQTKLDRVQIEKMEHQRwMYNIVVILLLCAASFTVL 483
Cdd:COG2199 27 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLL-LALLLLLLALEDITELRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 484 VNKTVRAKAAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVN 562
Cdd:COG2199 106 LEERLRRLATHDPLTGLPNRRAFEERLEReLARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 563 GELFGRLGGEEFVIMLTDTTPAEVRERVEELHYAISSTVFLSESkKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQA 642
Cdd:COG2199 186 SDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEG-KELRVTVSIGVALYPEDGDSAEELLRRADLALYRA 264
|
....*...
gi 880811218 643 KSNGRNCI 650
Cdd:COG2199 265 KRAGRNRV 272
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
492-649 |
3.50e-35 |
|
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: 130.45 E-value: 3.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 492 AAIDGLTKAYSRTEIIRRIKRV-KRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLG 570
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQElQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 571 GEEFVIMLTDTTP---AEVRERVEELHYAISSTVFLSEskKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGR 647
Cdd:pfam00990 81 GDEFAILLPETSLegaQELAERIRRLLAKLKIPHTVSG--LPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGR 158
|
..
gi 880811218 648 NC 649
Cdd:pfam00990 159 NR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
492-650 |
1.49e-34 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 128.90 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 492 AAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLG 570
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQeLQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 571 GEEFVIMLTDTTPAEVRERVEELHYAISSTVFLSEskKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGRNCI 650
Cdd:smart00267 83 GDEFALLLPETSLEEAIALAERILQQLREPIIIHG--IPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
492-648 |
2.99e-33 |
|
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: 125.14 E-value: 2.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 492 AAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLG 570
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSeLKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880811218 571 GEEFVIMLTDTTPAEVRERVEELHYAISSTVFLSESKKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGRN 648
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
485-650 |
1.29e-29 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 117.78 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 485 NKTVRAKAAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNG 563
Cdd:NF038266 87 NEALREASTRDPLTGLPNRRLLMERLREeVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREY 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 564 ELFGRLGGEEFVIMLTDTTPAEVRERVEELHYAISSTVFlSESKKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAK 643
Cdd:NF038266 167 DLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAV-RVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAK 245
|
....*..
gi 880811218 644 SNGRNCI 650
Cdd:NF038266 246 RAGRDRV 252
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
368-650 |
2.06e-29 |
|
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: 124.12 E-value: 2.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 368 AQQALGLAEQVARHKYITQSLLQLSDINQSLNDYQQAFYFYQRYSSIQMEARDIDNRLALEALGLTHAEYEQELENSFLT 447
Cdd:COG5001 121 ARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 448 HQTKLDRVQIEKMEHQRWMYNIVVILLLCAASFTVLVNKTVRAKAAI------DGLTKAYSRTEIIRRIKR-VKRCKGME 520
Cdd:COG5001 201 RGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLrhlayhDPLTGLPNRRLFLDRLEQaLARARRSG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 521 KQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLGGEEFVIMLTDTT-PAEVRERVEELHYAISS 599
Cdd:COG5001 281 RRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAALAE 360
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 880811218 600 TVFLSEskKSLNVTASF--AyLATSNAlSDFDDLYSVLDQALYQAKSNGRNCI 650
Cdd:COG5001 361 PFELDG--HELYVSASIgiA-LYPDDG-ADAEELLRNADLAMYRAKAAGRNRY 409
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
495-657 |
4.03e-28 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 119.35 E-value: 4.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 495 DGLTKAYSRTEIIRRIKRV-KRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLGGEE 573
Cdd:PRK15426 401 DPLTRLYNRGALFEKARALaKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEE 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 574 FVIMLTDTTPAEVRERVEELHYAISSTVFLSESKKSLNVTASFAYL-ATSNALSDFDDLYSVLDQALYQAKSNGRN--CI 650
Cdd:PRK15426 481 FCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVSsAEEDGDYDFEQLQSLADRRLYLAKQAGRNrvCA 560
|
....*..
gi 880811218 651 IDAYNEP 657
Cdd:PRK15426 561 SDNAHER 567
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
489-651 |
1.89e-24 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 103.99 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 489 RAKAAIDGLTKAYSRTEIIRRIKRVKRCKGMEKqHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGR 568
Cdd:PRK09894 126 TIRSNMDVLTGLPGRRVLDESFDHQLRNREPQN-LYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYR 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 569 LGGEEFVIMLTDTTPAEVRERVEELHYAISSTVFLSESKKsLNVTASFAyLATSNALSDFDDLYSVLDQALYQAKSNGRN 648
Cdd:PRK09894 205 YGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGR-INITATFG-VSRAFPEETLDVVIGRADRAMYEGKQTGRN 282
|
...
gi 880811218 649 CII 651
Cdd:PRK09894 283 RVM 285
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
492-653 |
2.49e-24 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 106.52 E-value: 2.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 492 AAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLG 570
Cdd:PRK09581 292 AVTDGLTGLHNRRYFDMHLKNlIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 571 GEEFVIMLTDTTPAEVRERVEELHYAISSTVF-LSESKKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGRNC 649
Cdd:PRK09581 372 GEEFVVVMPDTDIEDAIAVAERIRRKIAEEPFiISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNR 451
|
....
gi 880811218 650 IIDA 653
Cdd:PRK09581 452 VVAL 455
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
492-648 |
1.96e-17 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 87.04 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 492 AAIDGLTKAYSRTEIIRRIKR-VKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLG 570
Cdd:PRK09776 665 ASHDALTHLANRASFEKQLRRlLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLG 744
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 880811218 571 GEEFVIMLTDTTPAEVRERVEELHYAISSTVFLSESkKSLNVTASFAYLATSNALSDFDDLYSVLDQALYQAKSNGRN 648
Cdd:PRK09776 745 GDEFGLLLPDCNVESARFIATRIISAINDYHFPWEG-RVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRG 821
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
495-648 |
3.07e-17 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 84.11 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 495 DGLTKAYSRT--EIIRRIKrVKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLGGE 572
Cdd:PRK10245 208 DGMTGVYNRRhwETLLRNE-FDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGD 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 573 EFVIMLTDtTPAE--------VRERVEELHYAISSTVFLSESKKSLNVTASFAYlatsnalsdFDDLYSVLDQALYQAKS 644
Cdd:PRK10245 287 EFAVIMSG-TPAEsaitamsrVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSH---------YREWLKSADLALYKAKN 356
|
....
gi 880811218 645 NGRN 648
Cdd:PRK10245 357 AGRN 360
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
489-647 |
6.56e-15 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 78.18 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 489 RAKAAIDGLTKAYSRTEIIRRIKRVKRCKGmEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGR 568
Cdd:PRK10060 234 RILANTDSITGLPNRNAIQELIDHAINAAD-NNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLAR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 569 LGGEEFVIMLTDTTPAEVRerveelhyAISSTVfLSESKKSLNVTASFAYLATSNALSDF----DDLYSVL---DQALYQ 641
Cdd:PRK10060 313 LGGDEFLVLASHTSQAALE--------AMASRI-LTRLRLPFRIGLIEVYTGCSIGIALApehgDDSESLIrsaDTAMYT 383
|
....*.
gi 880811218 642 AKSNGR 647
Cdd:PRK10060 384 AKEGGR 389
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
191-442 |
5.03e-11 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 63.98 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 191 TYRVIANNHHFRSDYQAALDTYLSLINVFPQGHDisgVYNDVGNLLKELKQYEKSAEYLHEALTLRENAsdlmkAQVHHS 270
Cdd:COG2956 44 AHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAE---ALLELAQDYLKAGLLDRAEELLEKLLELDPDD-----AEALRL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 271 LADLNLNQEQSDLAIHHFQTARTLLSSSSHSYgialtsLGLGKAYTQTKDYDLARTYLveslsasselsNDVIRIN---- 346
Cdd:COG2956 116 LAEIYEQEGDWEKAIEVLERLLKLGPENAHAY------CELAELYLEQGDYDEAIEAL-----------EKALKLDpdca 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 347 -AYLAISDMFEEQKLPTEALNYAQQALGLAEQVARHkyitqsLLQLSDINQSLNDYQQAFYFYQRYSSIQMEARDIDN-- 423
Cdd:COG2956 179 rALLLLAELYLEQGDYEEAIAALERALEQDPDYLPA------LPRLAELYEKLGDPEEALELLRKALELDPSDDLLLAla 252
|
250 260
....*....|....*....|.
gi 880811218 424 RLALEALGLTHAE--YEQELE 442
Cdd:COG2956 253 DLLERKEGLEAALalLERQLR 273
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
518-648 |
8.15e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 65.18 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 518 GMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLGGEEFVIMLTDTTPAEVRERVEELHYAI 597
Cdd:PRK11359 399 DKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVV 478
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 880811218 598 SSTVFLSESKKSLNVTASFAYLATSNAlsdfDDLYSVLDQALYQAKSNGRN 648
Cdd:PRK11359 479 SKPIMIDDKPFPLTLSIGISYDVGKNR----DYLLSTAHNAMDYIRKNGGN 525
|
|
| Spy |
COG3914 |
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ... |
202-465 |
1.52e-09 |
|
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443119 [Multi-domain] Cd Length: 658 Bit Score: 61.16 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 202 RSDYQAALDTYLSLINVFPQGHDISGVYNDVGNLLKELKQYEKSAEYLHEALTLRENASDLMKAQVHHSLADLNL-NQEQ 280
Cdd:COG3914 14 AAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAALLLqALGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 281 SDLAIHHFQTARTLlsssSHSYGIALtsLGLGKAYTQTKDYDLARTYLveslsasselsNDVIRIN-----AYLAISDMF 355
Cdd:COG3914 94 YEEALALYRRALAL----NPDNAEAL--FNLGNLLLALGRLEEALAAL-----------RRALALNpdfaeAYLNLGEAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 356 EEQKLPTEALNYAQQALGLAEQVAR-HKYITQSLLQLSDINQSLNDYQQA-------FYFYQRYSSIQMEARDIDNRLAL 427
Cdd:COG3914 157 RRLGRLEEAIAALRRALELDPDNAEaLNNLGNALQDLGRLEEAIAAYRRAleldpdnADAHSNLLFALRQACDWEVYDRF 236
|
250 260 270
....*....|....*....|....*....|....*...
gi 880811218 428 EALGLTHAEYEQELENSFLTHQTKLDRVQIEKmEHQRW 465
Cdd:COG3914 237 EELLAALARGPSELSPFALLYLPDDDPAELLA-LARAW 273
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
228-442 |
2.02e-09 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 58.48 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 228 VYNDVGNLLKELKQYEKSAEYLHEALTLRENAsdlmkAQVHHSLADLNLNQEQSDLAIHHFQTARTLLSSSSHSYgialt 307
Cdd:COG0457 10 AYNNLGLAYRRLGRYEEAIEDYEKALELDPDD-----AEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEAL----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 308 sLGLGKAYTQTKDYDLARTYLveslsasselsNDVIRIN-----AYLAISDMFEEQKLPTEALNYAQQALGLAEQVAR-H 381
Cdd:COG0457 80 -NNLGLALQALGRYEEALEDY-----------DKALELDpddaeALYNLGLALLELGRYDEAIEAYERALELDPDDADaL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 880811218 382 KYITQSLLQLSDINQSLNDYQQAFYFYQRYSSIQMEARDIDNRLALEALGLTHAEYEQELE 442
Cdd:COG0457 148 YNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALR 208
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
104-372 |
2.26e-09 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 58.97 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 104 DYQAIEAAFISALMKDGKGQYEEAQQGFLTLLAKMQSRsdlagkALLKYQLCRSLNEQAKYHQA-NYYCSALQSDLYNIA 182
Cdd:COG2956 38 DPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDR------AEALLELAQDYLKAGLLDRAeELLEKLLELDPDDAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 183 dpvlpkfgTYRVIANNHHFRSDYQAALDTYLSLINVFPQGHDIsgvYNDVGNLLKELKQYEKSAEYLHEALTLRENAsdl 262
Cdd:COG2956 112 --------ALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHA---YCELAELYLEQGDYDEAIEALEKALKLDPDC--- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 263 mkAQVHHSLADLNLNQEQSDLAIHHFQTARTLlsssSHSYGIALtsLGLGKAYTQTKDYDLARTYLVESLSASSELSndv 342
Cdd:COG2956 178 --ARALLLLAELYLEQGDYEEAIAALERALEQ----DPDYLPAL--PRLAELYEKLGDPEEALELLRKALELDPSDD--- 246
|
250 260 270
....*....|....*....|....*....|
gi 880811218 343 irinAYLAISDMFEEQKLPTEALNYAQQAL 372
Cdd:COG2956 247 ----LLLALADLLERKEGLEAALALLERQL 272
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
495-643 |
4.29e-09 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 59.25 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 495 DGLTKAYSRTEIIRRIKRVKRCKGMEKQHVLVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLVNGELFGRLGGEEF 574
Cdd:PRK09966 251 DPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEF 330
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 575 VIMLTDT-TPAEVRERVEELHYAISSTVFLSESKKSlNVTASFAYLATSNALSDfDDLYSVLDQALYQAK 643
Cdd:PRK09966 331 AMVLYDVqSESEVQQICSALTQIFNLPFDLHNGHQT-TMTLSIGYAMTIEHASA-EKLQELADHNMYQAK 398
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
191-442 |
4.50e-08 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 54.63 E-value: 4.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 191 TYRVIANNHHFRSDYQAALDTYLSLINVFPqghDISGVYNDVGNLLKELKQYEKSAEYLHEALTLRENAsdlmkAQVHHS 270
Cdd:COG0457 10 AYNNLGLAYRRLGRYEEAIEDYEKALELDP---DDAEALYNLGLAYLRLGRYEEALADYEQALELDPDD-----AEALNN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 271 LADLNLNQEQSDLAIHHFQTARTLLSSSSHSYgialtsLGLGKAYTQTKDYDLARTYLveslsasselsNDVIRIN---- 346
Cdd:COG0457 82 LGLALQALGRYEEALEDYDKALELDPDDAEAL------YNLGLALLELGRYDEAIEAY-----------ERALELDpdda 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 347 -AYLAISDMFEEQKLPTEALNYAQQAlgLAEQVARHKYITQSLLQLSDINQSLNDYQQAFYFYQRYSSIQMEARDIDNRL 425
Cdd:COG0457 145 dALYNLGIALEKLGRYEEALELLEKL--EAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAEL 222
|
250
....*....|....*..
gi 880811218 426 ALEALGLTHAEYEQELE 442
Cdd:COG0457 223 LLLALALLLALRLAALA 239
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
525-599 |
1.64e-07 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 50.82 E-value: 1.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880811218 525 LVLLDLDNFKKINDEHGHPTGDRALIHISEKIRKHLV-NGELFGRLGGEEFVIMLTDTTPAEVRERVEELHYAISS 599
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRrSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSA 79
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
233-442 |
6.15e-07 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 51.65 E-value: 6.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 233 GNLLKELKQYEKSAEYLHEALTLRENAsdlmkAQVHHSLADLNLNQEQSDLAIHHFQTARTLLSSSSHSYgialtsLGLG 312
Cdd:COG2956 15 GLNYLLNGQPDKAIDLLEEALELDPET-----VEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEAL------LELA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 313 KAYTQTKDYDLARTYLVESLSASSElsndviRINAYLAISDMFEEQKLPTEALNYAQQALGLAEQVArhkyitQSLLQLS 392
Cdd:COG2956 84 QDYLKAGLLDRAEELLEKLLELDPD------DAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENA------HAYCELA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 880811218 393 DINQSLNDYQQAFYFYQRysSIQMEARDIDNRLALEALGLTHAEYEQELE 442
Cdd:COG2956 152 ELYLEQGDYDEAIEALEK--ALKLDPDCARALLLLAELYLEQGDYEEAIA 199
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
564-643 |
8.03e-07 |
|
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: 49.91 E-value: 8.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 564 ELFGRLGGEEFVIMLTDTTPAEVRERVEELHYAISSTvflseskKSLNVTASFAyLATSNALSDFDdlysvldqALYQAK 643
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAEL-------PSLRVTVSIG-VAGDSLLKRAD--------ALYQAR 179
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
195-328 |
5.56e-06 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 46.34 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 195 IANNHHFRSDYQAALDTYLSLINVFPQGHDisgVYNDVGNLLKELKQYEKSAEYLHEALTLRENAsdlmkAQVHHSLADL 274
Cdd:COG4783 10 LAQALLLAGDYDEAEALLEKALELDPDNPE---AFALLGEILLQLGDLDEAIVLLHEALELDPDE-----PEARLNLGLA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 880811218 275 NLNQEQSDLAIHHFQTARTLLSSSSHSYgialtsLGLGKAYTQTKDYDLARTYL 328
Cdd:COG4783 82 LLKAGDYDEALALLEKALKLDPEHPEAY------LRLARAYRALGRPDEAIAAL 129
|
|
| TPR |
COG0457 |
Tetratricopeptide (TPR) repeat [General function prediction only]; |
265-442 |
1.33e-05 |
|
Tetratricopeptide (TPR) repeat [General function prediction only];
Pssm-ID: 440225 [Multi-domain] Cd Length: 245 Bit Score: 47.31 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 265 AQVHHSLADLNLNQEQSDLAIHHFQTARTLLSSSSHSYgialtsLGLGKAYTQTKDYDLARTYLveslsasselsNDVIR 344
Cdd:COG0457 8 AEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEAL------YNLGLAYLRLGRYEEALADY-----------EQALE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 345 IN-----AYLAISDMFEEQKLPTEALNYAQQALGLAEQVArhkyitQSLLQLSDINQSLNDYQQAFYFYQRYSSIqmear 419
Cdd:COG0457 71 LDpddaeALNNLGLALQALGRYEEALEDYDKALELDPDDA------EALYNLGLALLELGRYDEAIEAYERALEL----- 139
|
170 180
....*....|....*....|...
gi 880811218 420 DIDNRLALEALGLTHAEYEQELE 442
Cdd:COG0457 140 DPDDADALYNLGIALEKLGRYEE 162
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
271-430 |
9.10e-05 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 44.72 E-value: 9.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 271 LADLNLNQEQSDLAIHHFQTArtlLSSSSHSYGIALTslgLGKAYTQTKDYDLARTYLveslsaSSELSNDVIRINAYLA 350
Cdd:COG2956 14 KGLNYLLNGQPDKAIDLLEEA---LELDPETVEAHLA---LGNLYRRRGEYDRAIRIH------QKLLERDPDRAEALLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 351 ISDMFEEQKLPTEALNYAQQALGLAEQVArhkyitQSLLQLSDINQSLNDYQQAFYFYQRYSSIQMEARDIDNRLALEAL 430
Cdd:COG2956 82 LAQDYLKAGLLDRAEELLEKLLELDPDDA------EALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYL 155
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
224-295 |
1.28e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 38.14 E-value: 1.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 880811218 224 DISGVYNDVGNLLKELKQYEKSAEYLHEALTLRENASD---LMKAQVHHSLADLNLNQEQSDLAIHHFQTARTLL 295
Cdd:pfam13424 1 DVATALNNLAAVLRRLGRYDEALELLEKALEIARRLLGpdhPLTATTLLNLGRLYLELGRYEEALELLERALALA 75
|
|
| PEP_TPR_lipo |
TIGR02917 |
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ... |
120-432 |
2.15e-03 |
|
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.
Pssm-ID: 274350 [Multi-domain] Cd Length: 899 Bit Score: 41.22 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 120 GKGQYEEAQQGFLTLLAKMQSRSDlagkalLKYQLCRSLNEQAKYHQANyycsalqsdlyNIADPVL---PKFgtyrviA 196
Cdd:TIGR02917 137 GLGQLELAQKSYEQALAIDPRSLY------AKLGLAQLALAENRFDEAR-----------ALIDEVLtadPGN------V 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 197 NNHHFRSDYQ-------AALDTYLSLINVFPQghDISGVYNDVGNLLkELKQYEKSAEYLHEALTLRENasdlmKAQVHH 269
Cdd:TIGR02917 194 DALLLKGDLLlslgnieLALAAYRKAIALRPN--NIAVLLALATILI-EAGEFEEAEKHADALLKKAPN-----SPLAHY 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 270 SLADLNLNQEQSDLAIHHFQTArtllSSSSHSYGIALtsLGLGKAYTQTKDYDLARTYLVESLSASSELSNdVIRInayL 349
Cdd:TIGR02917 266 LKALVDFQKKNYEDARETLQDA----LKSAPEYLPAL--LLAGASEYQLGNLEQAYQYLNQILKYAPNSHQ-ARRL---L 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 350 AISDMfeEQKLPTEALNYAQQALGLAEQVArhkyitQSLLQLSDINQSLNDYQQAFYFYQRYSSIQMEARDIDNRLALEA 429
Cdd:TIGR02917 336 ASIQL--RLGRVDEAIATLSPALGLDPDDP------AALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGISK 407
|
...
gi 880811218 430 LGL 432
Cdd:TIGR02917 408 LSQ 410
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
344-410 |
4.95e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 36.21 E-value: 4.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 880811218 344 RINAYLAISDMFEEQKLPTEALNYAQQALGLAEQV--ARHKYITQSLLQLSDINQSLNDYQQAFYFYQR 410
Cdd:pfam13424 2 VATALNNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELLER 70
|
|
| BepA |
COG4783 |
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ... |
233-375 |
5.11e-03 |
|
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443813 [Multi-domain] Cd Length: 139 Bit Score: 37.86 E-value: 5.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 233 GNLLKELKQYEKSAEYLHEALTLRENAsdlmkAQVHHSLADLNLNQEQSDLAIHHFQTARTLLSSSSHSYgialtsLGLG 312
Cdd:COG4783 11 AQALLLAGDYDEAEALLEKALELDPDN-----PEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEAR------LNLG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 880811218 313 KAYTQTKDYDLARTYLVESLSASSELsndvirINAYLAISDMFEEQKLPTEALNYAQQALGLA 375
Cdd:COG4783 80 LALLKAGDYDEALALLEKALKLDPEH------PEAYLRLARAYRALGRPDEAIAALEKALELD 136
|
|
| NrfG |
COG4235 |
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ... |
233-328 |
5.46e-03 |
|
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443378 [Multi-domain] Cd Length: 131 Bit Score: 37.68 E-value: 5.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 233 GNLLKELKQYEKSAEYLHEALTLRENasdlmKAQVHHSLADLNLNQEQSDLAIHHFQTARTLLSSSSHSYGIaltslgLG 312
Cdd:COG4235 24 GRAYLRLGRYDEALAAYEKALRLDPD-----NADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYL------LG 92
|
90
....*....|....*.
gi 880811218 313 KAYTQTKDYDLARTYL 328
Cdd:COG4235 93 LAAFQQGDYAEAIAAW 108
|
|
| TPR_12 |
pfam13424 |
Tetratricopeptide repeat; |
265-328 |
6.52e-03 |
|
Tetratricopeptide repeat;
Pssm-ID: 315987 [Multi-domain] Cd Length: 77 Bit Score: 35.83 E-value: 6.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 880811218 265 AQVHHSLADLNLNQEQSDLAIHHFQTARTLLSSS--SHSYGIALTSLGLGKAYTQTKDYDLARTYL 328
Cdd:pfam13424 3 ATALNNLAAVLRRLGRYDEALELLEKALEIARRLlgPDHPLTATTLLNLGRLYLELGRYEEALELL 68
|
|
| PilF |
COG3063 |
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures]; |
199-291 |
6.73e-03 |
|
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
Pssm-ID: 442297 [Multi-domain] Cd Length: 94 Bit Score: 36.30 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 880811218 199 HHFRSDYQAALDTYLSLINVFPqghDISGVYNDVGNLLKELKQYEKsAEYLHEALTLRENasdlmKAQVHHSLADLNLNQ 278
Cdd:COG3063 2 YLKLGDLEEAEEYYEKALELDP---DNADALNNLGLLLLEQGRYDE-AIALEKALKLDPN-----NAEALLNLAELLLEL 72
|
90
....*....|...
gi 880811218 279 EQSDLAIHHFQTA 291
Cdd:COG3063 73 GDYDEALAYLERA 85
|
|
| |
