|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
238-469 |
8.18e-32 |
|
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: 122.78 E-value: 8.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 238 LTDLFAQRLLAAEAVQLDPVDLPSRLRAEGLHGALLLPVRAGETLMVLGAYRREPLAWTPVERDLLSVAAQVVQVSLERR 317
Cdd:COG2199 25 ALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 318 DTLAGLRSAAVTDPLTGLGNRRAFESDLREALAR-----GPLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVT 392
Cdd:COG2199 105 RLEERLRRLATHDPLTGLPNRRAFEERLERELARarregRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 393 SGDGAYRVGGDEFCLLLRGAPGQIPDLDAAFAALAGEGFGPAGASAGWA--------SAPQDGQDPEVLWQLADERMYRE 464
Cdd:COG2199 185 ESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRvtvsigvaLYPEDGDSAEELLRRADLALYRA 264
|
....*
gi 1801329334 465 KARRR 469
Cdd:COG2199 265 KRAGR 269
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
329-469 |
1.90e-31 |
|
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: 118.43 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 329 TDPLTGLGNRRAFESDLREALAR-----GPLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVGGD 403
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARarrsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 404 EFCLLLRGAP--------GQIPDLDAAFAALAGEG------FGpagasagWASAPQDGQDPEVLWQLADERMYREKARRR 469
Cdd:cd01949 82 EFAILLPGTDleeaealaERLREAIEEPFFIDGQEirvtasIG-------IATYPEDGEDAEELLRRADEALYRAKRSGR 154
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
327-469 |
9.01e-28 |
|
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: 108.11 E-value: 9.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 327 AVTDPLTGLGNRRAFESDLREALARG-----PLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVG 401
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRAlregsPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 402 GDEFCLLLRGAPGQ-----------------IPDLDAAFAALAGEGFGpagasagWASAPQDGQDPEVLWQLADERMYRE 464
Cdd:pfam00990 81 GDEFAILLPETSLEgaqelaerirrllaklkIPHTVSGLPLYVTISIG-------IAAYPNDGEDPEDLLKRADTALYQA 153
|
....*
gi 1801329334 465 KARRR 469
Cdd:pfam00990 154 KQAGR 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
327-469 |
1.60e-25 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 102.33 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 327 AVTDPLTGLGNRRAFESDLREALAR-----GPLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVG 401
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRaqrqgSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801329334 402 GDEFCLLLRGAP-GQIPDLDAAFAALAGEGFGPAGASAGW------ASAPQDGQDPEVLWQLADERMYREKARRR 469
Cdd:smart00267 83 GDEFALLLPETSlEEAIALAERILQQLREPIIIHGIPLYLtisigvAAYPNPGEDAEDLLKRADTALYQAKKAGR 157
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
327-469 |
4.10e-23 |
|
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: 95.48 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 327 AVTDPLTGLGNRRAFESDLREALARG-----PLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVG 401
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRArrfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801329334 402 GDEFCLLLRGAP--GQIPDLDAAFAALAGEGFGPAGASAGWASA-------PQDGQDPEVLWQLADERMYREKARRR 469
Cdd:TIGR00254 82 GEEFVVILPGTPleDALSKAERLRDAINSKPIEVAGSETLTVTVsigvacyPGHGLTLEELLKRADEALYQAKKAGR 158
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
309-409 |
3.10e-17 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 84.72 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 309 VVQVSLERRDTLAGLRSAAVTDPLTGLGNRRAFESDLREALARGPLT-----LVALDVDGLKAVNDTLGHARGDDLLRGV 383
Cdd:PRK09776 647 VIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSThqrhaLVFIDLDRFKAVNDSAGHAAGDALLREL 726
|
90 100
....*....|....*....|....*.
gi 1801329334 384 ARVLAGVVTSGDGAYRVGGDEFCLLL 409
Cdd:PRK09776 727 ASLMLSMLRSSDVLARLGGDEFGLLL 752
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
328-409 |
3.82e-17 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 83.85 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 328 VTDPLTGLGNR----RAFESDLREALARG-PLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVGG 402
Cdd:NF040885 342 ISDSMTGLYNRkiltPTLEQRLQRLTEKGiPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGG 421
|
....*..
gi 1801329334 403 DEFCLLL 409
Cdd:NF040885 422 DEFCIIL 428
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
28-180 |
1.64e-07 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 53.43 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 28 LRDLGWALRHLLS-FAAQASALRGLEEQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLGGTL 106
Cdd:COG5000 64 IGELARAFNRMTDqLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELD 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801329334 107 NLSELRADLAAGQERRQEVTLAGRVYDTQRVRLPRGSGTLGVAFDVTDLVesraqarRAQRhAETLLDLTQVMA 180
Cdd:COG5000 144 LAELLREALERGWQEEIELTRDGRRTLLVRASPLRDDGYVIVFDDITELL-------RAER-LAAWGELARRIA 209
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
53-102 |
1.27e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 42.77 E-value: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1801329334 53 EQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVL 102
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI 50
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
53-127 |
1.39e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 38.55 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1801329334 53 EQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLGGTLNL---SELRADLAAGQERR-QEVTL 127
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAevaELLRQALLQGEESRgFEVSF 79
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
62-164 |
6.74e-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: 36.07 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 62 LPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLggtlnlseLRADLAAGQERRQEVTLAGRVYDTQRVRLPR 141
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI--------HPEDREELRERLENLLSGGEPVTLEVRLRRK 72
|
90 100
....*....|....*....|...
gi 1801329334 142 GSGTLGVAFDVTDLVESRAQARR 164
Cdd:cd00130 73 DGSVIWVLVSLTPIRDEGGEVIG 95
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
52-161 |
9.29e-03 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 36.11 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 52 EEQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLggtlnLSELRADLAAGQERRQEVTLAGrV 131
Cdd:TIGR00229 2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELI-----PEEDREEVRERIERRLEGEPEP-V 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1801329334 132 YDTQRVRLPRGS------------------GTLGVAFDVTDLVESRAQ 161
Cdd:TIGR00229 76 SEERRVRRKDGSeiwvevsvspirtnggelGVVGIVRDITERKEAEEA 123
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
238-469 |
8.18e-32 |
|
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: 122.78 E-value: 8.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 238 LTDLFAQRLLAAEAVQLDPVDLPSRLRAEGLHGALLLPVRAGETLMVLGAYRREPLAWTPVERDLLSVAAQVVQVSLERR 317
Cdd:COG2199 25 ALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 318 DTLAGLRSAAVTDPLTGLGNRRAFESDLREALAR-----GPLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVT 392
Cdd:COG2199 105 RLEERLRRLATHDPLTGLPNRRAFEERLERELARarregRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 393 SGDGAYRVGGDEFCLLLRGAPGQIPDLDAAFAALAGEGFGPAGASAGWA--------SAPQDGQDPEVLWQLADERMYRE 464
Cdd:COG2199 185 ESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRvtvsigvaLYPEDGDSAEELLRRADLALYRA 264
|
....*
gi 1801329334 465 KARRR 469
Cdd:COG2199 265 KRAGR 269
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
329-469 |
1.90e-31 |
|
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: 118.43 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 329 TDPLTGLGNRRAFESDLREALAR-----GPLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVGGD 403
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARarrsgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 404 EFCLLLRGAP--------GQIPDLDAAFAALAGEG------FGpagasagWASAPQDGQDPEVLWQLADERMYREKARRR 469
Cdd:cd01949 82 EFAILLPGTDleeaealaERLREAIEEPFFIDGQEirvtasIG-------IATYPEDGEDAEELLRRADEALYRAKRSGR 154
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
327-469 |
9.01e-28 |
|
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: 108.11 E-value: 9.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 327 AVTDPLTGLGNRRAFESDLREALARG-----PLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVG 401
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRAlregsPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 402 GDEFCLLLRGAPGQ-----------------IPDLDAAFAALAGEGFGpagasagWASAPQDGQDPEVLWQLADERMYRE 464
Cdd:pfam00990 81 GDEFAILLPETSLEgaqelaerirrllaklkIPHTVSGLPLYVTISIG-------IAAYPNDGEDPEDLLKRADTALYQA 153
|
....*
gi 1801329334 465 KARRR 469
Cdd:pfam00990 154 KQAGR 158
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
71-411 |
7.99e-27 |
|
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: 114.10 E-value: 7.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 71 ARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLGGTLNLSELRADLAAGQERRQEVTLAGRVYDTQRVRLPRGSGTLGVAF 150
Cdd:COG5001 3 ALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 151 DVTDLVESRAQARRAQRHAETLLDLTQVMALTGSLPDVTRQALEVLLPALPHSWLVLWFRDGPLLRPLVSCGEQPAAVAQ 230
Cdd:COG5001 83 AALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 231 WQRQGVPLTDLFAQRLLAAEAVQLDPVDLPSRLRAEGLHGALLLPVRAGETLMVLGAYRREplawtpveRDLLSVAAQVV 310
Cdd:COG5001 163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLL--------LLLLVAVLAIA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 311 QVSLERRDTLAGLRSAAVTDPLTGLGNRRAFESDLREALAR-----GPLTLVALDVDGLKAVNDTLGHARGDDLLRGVAR 385
Cdd:COG5001 235 RLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARarrsgRRLALLFIDLDRFKEINDTLGHAAGDELLREVAR 314
|
330 340
....*....|....*....|....*.
gi 1801329334 386 VLAGVVTSGDGAYRVGGDEFCLLLRG 411
Cdd:COG5001 315 RLRACLREGDTVARLGGDEFAVLLPD 340
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
327-469 |
1.60e-25 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 102.33 E-value: 1.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 327 AVTDPLTGLGNRRAFESDLREALAR-----GPLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVG 401
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRaqrqgSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1801329334 402 GDEFCLLLRGAP-GQIPDLDAAFAALAGEGFGPAGASAGW------ASAPQDGQDPEVLWQLADERMYREKARRR 469
Cdd:smart00267 83 GDEFALLLPETSlEEAIALAERILQQLREPIIIHGIPLYLtisigvAAYPNPGEDAEDLLKRADTALYQAKKAGR 157
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
327-469 |
4.10e-23 |
|
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: 95.48 E-value: 4.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 327 AVTDPLTGLGNRRAFESDLREALARG-----PLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVG 401
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRArrfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1801329334 402 GDEFCLLLRGAP--GQIPDLDAAFAALAGEGFGPAGASAGWASA-------PQDGQDPEVLWQLADERMYREKARRR 469
Cdd:TIGR00254 82 GEEFVVILPGTPleDALSKAERLRDAINSKPIEVAGSETLTVTVsigvacyPGHGLTLEELLKRADEALYQAKKAGR 158
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
309-409 |
3.10e-17 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 84.72 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 309 VVQVSLERRDTLAGLRSAAVTDPLTGLGNRRAFESDLREALARGPLT-----LVALDVDGLKAVNDTLGHARGDDLLRGV 383
Cdd:PRK09776 647 VIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSThqrhaLVFIDLDRFKAVNDSAGHAAGDALLREL 726
|
90 100
....*....|....*....|....*.
gi 1801329334 384 ARVLAGVVTSGDGAYRVGGDEFCLLL 409
Cdd:PRK09776 727 ASLMLSMLRSSDVLARLGGDEFGLLL 752
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
327-409 |
3.16e-17 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 83.80 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 327 AVTDPLTGLGNRRAFESDLR----EALARG-PLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVG 401
Cdd:PRK09581 292 AVTDGLTGLHNRRYFDMHLKnlieRANERGkPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYG 371
|
....*...
gi 1801329334 402 GDEFCLLL 409
Cdd:PRK09581 372 GEEFVVVM 379
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
328-409 |
3.82e-17 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 83.85 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 328 VTDPLTGLGNR----RAFESDLREALARG-PLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVGG 402
Cdd:NF040885 342 ISDSMTGLYNRkiltPTLEQRLQRLTEKGiPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGG 421
|
....*..
gi 1801329334 403 DEFCLLL 409
Cdd:NF040885 422 DEFCIIL 428
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
323-413 |
6.86e-17 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 83.14 E-value: 6.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 323 LRSAAVTDPLTGLGNRRAFESDLREALAR-----GPLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGA 397
Cdd:PRK15426 394 LQWQAWHDPLTRLYNRGALFEKARALAKRcqrdqQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473
|
90
....*....|....*.
gi 1801329334 398 YRVGGDEFCLLLRGAP 413
Cdd:PRK15426 474 GRVGGEEFCVVLPGAS 489
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
311-411 |
4.43e-16 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 80.05 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 311 QVSLERRDtlAGLRSAAVTDPLTGLGNRRAFESDLREAL----ARGPLTLVALDVDGLKAVNDTLGHARGDDLLRGVARV 386
Cdd:PRK09966 234 QLRLQAKN--AQLLRTALHDPLTGLANRAAFRSGINTLMnnsdARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKR 311
|
90 100
....*....|....*....|....*
gi 1801329334 387 LAGVVTSGDGAYRVGGDEFCLLLRG 411
Cdd:PRK09966 312 LAEFGGLRHKAYRLGGDEFAMVLYD 336
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
295-412 |
4.57e-15 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 75.49 E-value: 4.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 295 WTPVERDLLSVAAQVvqvsleRRDTLAGLRSAAVTDPLTGLGNRRAFESDLREALARG---PLTLVALDVDGLKAVNDTL 371
Cdd:PRK09894 103 FDAFQEGLLSFTAAL------TDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNRepqNLYLALLDIDRFKLVNDTY 176
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1801329334 372 GHARGDDLLRGVARVLAGVVTSGDGAYRVGGDEFCLLLRGA 412
Cdd:PRK09894 177 GHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAA 217
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
315-408 |
1.53e-13 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 72.79 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 315 ERRDTLAGLRSAAVTDPLTGLGNRRAFESDLREALA---RGPLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVV 391
Cdd:PRK10060 225 EERRAQERLRILANTDSITGLPNRNAIQELIDHAINaadNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCL 304
|
90
....*....|....*..
gi 1801329334 392 TSGDGAYRVGGDEFCLL 408
Cdd:PRK10060 305 EEDQTLARLGGDEFLVL 321
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
330-415 |
3.76e-09 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 58.30 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 330 DPLTGLGNRRAFESDLR---EALARG--PLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVGGDE 404
Cdd:PRK10245 208 DGMTGVYNRRHWETLLRnefDNCRRHhrDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDE 287
|
90
....*....|.
gi 1801329334 405 FCLLLRGAPGQ 415
Cdd:PRK10245 288 FAVIMSGTPAE 298
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
28-180 |
1.64e-07 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 53.43 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 28 LRDLGWALRHLLS-FAAQASALRGLEEQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLGGTL 106
Cdd:COG5000 64 IGELARAFNRMTDqLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELD 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1801329334 107 NLSELRADLAAGQERRQEVTLAGRVYDTQRVRLPRGSGTLGVAFDVTDLVesraqarRAQRhAETLLDLTQVMA 180
Cdd:COG5000 144 LAELLREALERGWQEEIELTRDGRRTLLVRASPLRDDGYVIVFDDITELL-------RAER-LAAWGELARRIA 209
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
330-408 |
1.85e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 50.54 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 330 DPLTGLGNRRAFESDLREALARGP-LTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVGGDEFCLL 408
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDLVDKAVsPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLV 458
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
47-169 |
2.29e-06 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 49.46 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 47 ALRGLEEQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLGGTLNLSELRAD-LAAGQE-RRQE 124
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERaLAEGQPvTERE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1801329334 125 VTLAGRVYDTQRVRL--------PRGSGTLGVAFDVTDLVESRAQARRAQRHA 169
Cdd:COG3852 81 VTLRRKDGEERPVDVsvsplrdaEGEGGVLLVLRDITERKRLERELRRAEKLA 133
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
43-196 |
2.66e-06 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 48.87 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 43 AQASALRGLEEQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLGGTLN---LSELRADLAAGQ 119
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDdefLELLRAALAGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 120 ERRQEVTLA---GRVYDTQRVRLP------RGSGTLGVAFDVTDLVESRAQARRAQRHAETLLDLTQVMALT----GSLP 186
Cdd:COG2202 81 VWRGELRNRrkdGSLFWVELSISPvrdedgEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVldldGRIL 160
|
170
....*....|
gi 1801329334 187 DVTRQALEVL 196
Cdd:COG2202 161 YVNPAAEELL 170
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
53-102 |
1.27e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 42.77 E-value: 1.27e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1801329334 53 EQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVL 102
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI 50
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
353-409 |
3.39e-04 |
|
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: 40.42 E-value: 3.39e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801329334 353 PLTLVALDVDGLKAVNDTLGHARGDDLLRGVARVLAGVVT-SGDGAYRVGGDEFCLLL 409
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRrSGDLKIKTIGDEFMVVS 58
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
47-161 |
3.53e-04 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 42.32 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 47 ALRGLEEQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLGGTL--NLSELRADLAAGQERRQE 124
Cdd:COG2202 131 ALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDreRLLELLRRLLEGGRESYE 210
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1801329334 125 VTLAGRVYDTQRVRL----------PRGSGTLGVAFDVTDLVESRAQ 161
Cdd:COG2202 211 LELRLKDGDGRWVWVeasavplrdgGEVIGVLGIVRDITERKRAEEA 257
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
101-472 |
1.21e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 41.40 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 101 VLGGTLNLSELRADlaagqERRQEVTLAG------RVYDTQRVRLPRGSGTLGVAFDVTDLVESRAQARRAQRHAETLLD 174
Cdd:COG3321 842 VAGVPVDWSALYPG-----RGRRRVPLPTypfqreDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAA 916
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 175 LTQVMALTGSLPDVTRQALEVLLPALPHSWLVLWFRDGPLLRPLVSCGEQPAAVAQWQRQGVPLTDLFAQRLLAAEAVQL 254
Cdd:COG3321 917 AALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAAL 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 255 DPVDLPSRLRAEGLHGALLLPVRAGETLMVLGAYRREPLAWTPVERDLLSVAAQVVQVSLERRDTLAGLRSAAVTDPLTG 334
Cdd:COG3321 997 AAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAE 1076
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 335 LGNRRAFESDLREALARGPLTLVALDVDGLKAVnDTLGHARGDDLLRGVARVLAGVVTSGDGAYRVGGDEFCLLLRGAPG 414
Cdd:COG3321 1077 LALAAAALALAAALAAAALALALAALAAALLLL-ALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAA 1155
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1801329334 415 QIPDLDAAFAALAGEGFGPAGASAGWASAPQDGQDPEVLWQLADERMYREKARRRPGR 472
Cdd:COG3321 1156 AAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALAL 1213
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
53-127 |
1.39e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 38.55 E-value: 1.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1801329334 53 EQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLGGTLNL---SELRADLAAGQERR-QEVTL 127
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAevaELLRQALLQGEESRgFEVSF 79
|
|
| GAF_2 |
pfam13185 |
GAF domain; The GAF domain is named after some of the proteins it is found in, including ... |
184-315 |
3.40e-03 |
|
GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433019 [Multi-domain] Cd Length: 137 Bit Score: 37.83 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 184 SLPDVTRQALEVL--LPALPHSWLVLWFRDGPLLRPLVSCGEQPAAVAQWQRQGVPLTDLFAQRLLAAEAVQLDPVDLPS 261
Cdd:pfam13185 3 DLEELLDAVLEAAveLGASAVGFILLVDDDGRLAAWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDLAADPAKKGL 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1801329334 262 RLRAEGLHGALLLPVRA-GETLMVLGAYRREPLAWTPVERDLLSVAAQVVQVSLE 315
Cdd:pfam13185 83 PAGHAGLRSFLSVPLVSgGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
43-167 |
6.33e-03 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 38.98 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 43 AQASALRGLEEQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLGGtlnlSELRADLAAGQ--- 119
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPN----SPLLEVLKTGKpvt 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1801329334 120 ERRQEVTLAGRVYDTQRVRLPRGS---GTLGVAFDVTDLVESRAQARRAQR 167
Cdd:COG3829 77 GVIQKTGGKGKTVIVTAIPIFEDGeviGAVETFRDITELKRLERKLREEEL 127
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
62-164 |
6.74e-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: 36.07 E-value: 6.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 62 LPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLggtlnlseLRADLAAGQERRQEVTLAGRVYDTQRVRLPR 141
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI--------HPEDREELRERLENLLSGGEPVTLEVRLRRK 72
|
90 100
....*....|....*....|...
gi 1801329334 142 GSGTLGVAFDVTDLVESRAQARR 164
Cdd:cd00130 73 DGSVIWVLVSLTPIRDEGGEVIG 95
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
52-161 |
9.29e-03 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 36.11 E-value: 9.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1801329334 52 EEQLQFALRSLPMILWVTDARGRLVVAEGSGLTQLGLRREQVLGRSMEDVLggtlnLSELRADLAAGQERRQEVTLAGrV 131
Cdd:TIGR00229 2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELI-----PEEDREEVRERIERRLEGEPEP-V 75
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90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1801329334 132 YDTQRVRLPRGS------------------GTLGVAFDVTDLVESRAQ 161
Cdd:TIGR00229 76 SEERRVRRKDGSeiwvevsvspirtnggelGVVGIVRDITERKEAEEA 123
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