|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
123-316 |
6.89e-69 |
|
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: 216.00 E-value: 6.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 123 EVSHICIILYDVTDVAVNKKELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKIND 202
Cdd:COG2199 82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 203 EYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLA 282
Cdd:COG2199 162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA 241
|
170 180 190
....*....|....*....|....*....|....
gi 639310448 283 GSSNDFKNHERWIEAADKALYQSKNTGRNKVIAY 316
Cdd:COG2199 242 LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
156-314 |
4.27e-62 |
|
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: 194.70 E-value: 4.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 156 QTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGG 235
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448 236 EEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHfEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVI 314
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQ-EIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
155-312 |
7.90e-57 |
|
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: 181.30 E-value: 7.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 155 SQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYG 234
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 235 GEEFAVTLLDTDKEGAFVFAERLRVLIETN--PVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLkiPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
155-313 |
3.93e-56 |
|
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: 179.46 E-value: 3.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 155 SQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYG 234
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 235 GEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFE-ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKV 313
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
153-316 |
5.71e-53 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 171.28 E-value: 5.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 153 QVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGR 232
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 233 YGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHfEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGI-PLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 639310448 313 VIAY 316
Cdd:smart00267 160 VAVY 163
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
157-315 |
1.45e-46 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 163.15 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 157 TDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGE 236
Cdd:PRK09581 294 TDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 237 EFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFE--ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVI 314
Cdd:PRK09581 374 EFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRVV 453
|
.
gi 639310448 315 A 315
Cdd:PRK09581 454 A 454
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
144-313 |
4.07e-44 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 151.29 E-value: 4.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 144 LEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTT 223
Cdd:NF038266 83 MRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 224 LRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALY 303
Cdd:NF038266 163 LREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALY 242
|
170
....*....|
gi 639310448 304 QSKNTGRNKV 313
Cdd:NF038266 243 QAKRAGRDRV 252
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
148-313 |
2.06e-42 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 149.51 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 148 NKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRET 227
Cdd:NF041606 171 NALLLEMTTTDMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 228 DVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKN 307
Cdd:NF041606 251 DMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGVAEYNFDVESAKSLVERADKALYESKQ 330
|
....*.
gi 639310448 308 TGRNKV 313
Cdd:NF041606 331 NGRNRV 336
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
16-134 |
2.16e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 43.17 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 16 MFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFRSKSESVFVLKNRSFTIWeqqpYIFRF 95
Cdd:pfam00989 6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFE----VSFRV 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 639310448 96 KNYRPItgkadYMYQNATfiPLTNTMGEVSHICIILYDV 134
Cdd:pfam00989 82 PDGRPR-----HVEVRAS--PVRDAGGEILGFLGVLRDI 113
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
6-164 |
3.22e-05 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 45.22 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 6 EMNEIH-WLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEkwFRSKSESVfVLKNRSFT 84
Cdd:COG3852 1 ALRESEeLLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP--LRELLERA-LAEGQPVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 85 IWEqqpYIFRFKNYRPITgkADYmyqnaTFIPLTNTMGEVsHICIILYDVTDvavnKKELEElnkKLEQVSQTDSLTQLA 164
Cdd:COG3852 78 ERE---VTLRRKDGEERP--VDV-----SVSPLRDAEGEG-GVLLVLRDITE----RKRLER---ELRRAEKLAAVGELA 139
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
11-69 |
9.85e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 36.99 E-value: 9.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448 11 HWLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFR 69
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQ 59
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
123-316 |
6.89e-69 |
|
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: 216.00 E-value: 6.89e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 123 EVSHICIILYDVTDVAVNKKELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKIND 202
Cdd:COG2199 82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRIND 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 203 EYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLA 282
Cdd:COG2199 162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVA 241
|
170 180 190
....*....|....*....|....*....|....
gi 639310448 283 GSSNDFKNHERWIEAADKALYQSKNTGRNKVIAY 316
Cdd:COG2199 242 LYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
156-314 |
4.27e-62 |
|
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: 194.70 E-value: 4.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 156 QTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGG 235
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448 236 EEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHfEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVI 314
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQ-EIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
155-312 |
7.90e-57 |
|
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: 181.30 E-value: 7.90e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 155 SQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYG 234
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 235 GEEFAVTLLDTDKEGAFVFAERLRVLIETN--PVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLkiPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
155-313 |
3.93e-56 |
|
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: 179.46 E-value: 3.93e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 155 SQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYG 234
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 235 GEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFE-ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKV 313
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
153-316 |
5.71e-53 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 171.28 E-value: 5.71e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 153 QVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGR 232
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 233 YGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHfEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGI-PLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 639310448 313 VIAY 316
Cdd:smart00267 160 VAVY 163
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
157-315 |
1.45e-46 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 163.15 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 157 TDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGE 236
Cdd:PRK09581 294 TDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 237 EFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFE--ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVI 314
Cdd:PRK09581 374 EFVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDGKerLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRVV 453
|
.
gi 639310448 315 A 315
Cdd:PRK09581 454 A 454
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
144-313 |
4.07e-44 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 151.29 E-value: 4.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 144 LEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTT 223
Cdd:NF038266 83 MRDLNEALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 224 LRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALY 303
Cdd:NF038266 163 LREYDLCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALY 242
|
170
....*....|
gi 639310448 304 QSKNTGRNKV 313
Cdd:NF038266 243 QAKRAGRDRV 252
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
129-318 |
2.26e-43 |
|
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: 158.01 E-value: 2.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 129 IILYDVTDVAVNKKELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSC 208
Cdd:COG5001 225 LLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAA 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 209 GDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLD-TDKEGAFVFAERLRVLIETnPVKYKHFEITMTVSIGLAGSSND 287
Cdd:COG5001 305 GDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAE-PFELDGHELYVSASIGIALYPDD 383
|
170 180 190
....*....|....*....|....*....|.
gi 639310448 288 FKNHERWIEAADKALYQSKNTGRNKVIAYED 318
Cdd:COG5001 384 GADAEELLRNADLAMYRAKAAGRNRYRFFDP 414
|
|
| dguan_cyc_DgcA |
NF041606 |
diguanylate cyclase DgcA; |
148-313 |
2.06e-42 |
|
diguanylate cyclase DgcA;
Pssm-ID: 469490 [Multi-domain] Cd Length: 340 Bit Score: 149.51 E-value: 2.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 148 NKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRET 227
Cdd:NF041606 171 NALLLEMTTTDMMTHLKLKHYFYTVLMEKLDTINSQGEPLSILMLDIDFFKQINDTYGHACGDLVLQMVASIIQSCTRTQ 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 228 DVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKN 307
Cdd:NF041606 251 DMAARYGGEEFVVMLSNTSSKTAKKIAERIRKSIENLSILYDEQHIRVTISIGVAEYNFDVESAKSLVERADKALYESKQ 330
|
....*.
gi 639310448 308 TGRNKV 313
Cdd:NF041606 331 NGRNRV 336
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
147-315 |
1.85e-40 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 148.62 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 147 LNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRE 226
Cdd:PRK15426 390 LQSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRA 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 227 TDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIETNPV-KYKHFEITMTVSIGLAGSSNDFK-NHERWIEAADKALYQ 304
Cdd:PRK15426 470 QDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEIlVAKSTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLYL 549
|
170
....*....|.
gi 639310448 305 SKNTGRNKVIA 315
Cdd:PRK15426 550 AKQAGRNRVCA 560
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
144-312 |
5.69e-40 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 143.82 E-value: 5.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 144 LEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTT 223
Cdd:PRK10245 194 LAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQIT 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 224 LRETDVAGRYGGEEFAVTLLDTDKEGAFV----FAERLRVL-IETNPvkykhfEITMTVSIGLAGSSNDFKNHERWIEAA 298
Cdd:PRK10245 274 LRGSDVIGRFGGDEFAVIMSGTPAESAITamsrVHEGLNTLrLPNAP------QVTLRISVGVAPLNPQMSHYREWLKSA 347
|
170
....*....|....
gi 639310448 299 DKALYQSKNTGRNK 312
Cdd:PRK10245 348 DLALYKAKNAGRNR 361
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
155-318 |
7.69e-36 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 130.96 E-value: 7.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 155 SQTDSLTQLANR-GHWEGTLRQEFLRVKRsgGCStLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRY 233
Cdd:PRK09894 129 SNMDVLTGLPGRrVLDESFDHQLRNREPQ--NLY-LALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 234 GGEEFAVTLLDTDKEGAFVFAERLRVLIETNPVKYKHFEITMTVSIGLAGSSNDfKNHERWIEAADKALYQSKNTGRNKV 313
Cdd:PRK09894 206 GGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPE-ETLDVVIGRADRAMYEGKQTGRNRV 284
|
....*
gi 639310448 314 IAYED 318
Cdd:PRK09894 285 MFIDE 289
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
116-317 |
5.81e-23 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 99.75 E-value: 5.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 116 PLTNTMGEVSHICIILYDVTdvavnkkELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDID 195
Cdd:PRK09776 633 PLSTLDGENIGSVLVIQDVT-------ESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLD 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 196 HFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLrvlieTNPVKYKHFE--- 272
Cdd:PRK09776 706 RFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRI-----ISAINDYHFPweg 780
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 639310448 273 --ITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNKVIAYE 317
Cdd:PRK09776 781 rvYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYE 827
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
24-312 |
1.24e-20 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 92.44 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 24 LVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFRSKSESVFVLKNRSF-------TIWEQQPYIFRFK 96
Cdd:PRK10060 124 IVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKLFMSRREAAASRRNIRGFFRSGNAYeverwikTRKGQRLFLFRNK 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 97 NYRPITGKadymyqNATFIpltntmgevshICiilyDVTDVAvnkkelEELN--KKLEQVSQTDSLTQLANRghwegTLR 174
Cdd:PRK10060 204 FVHSGSGK------NEIFL-----------IC----SGTDIT------EERRaqERLRILANTDSITGLPNR-----NAI 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 175 QEFLR---VKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVTLLDTDKEG-- 249
Cdd:PRK10060 252 QELIDhaiNAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAAle 331
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 639310448 250 --AFVFAERLRVlietnPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEAADKALYQSKNTGRNK 312
Cdd:PRK10060 332 amASRILTRLRL-----PFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQ 391
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
228-306 |
1.68e-16 |
|
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: 76.10 E-value: 1.68e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448 228 DVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIEtnpvkyKHFEITMTVSIGLAGSSndfknherWIEAADkALYQSK 306
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVA------ELPSLRVTVSIGVAGDS--------LLKRAD-ALYQAR 179
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
143-311 |
2.08e-15 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 76.73 E-value: 2.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 143 ELEELNKKLEQVSQTDSLTQLANRGHWEGTLrQEFLRVKRSggcSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRT 222
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYL-DDLVDKAVS---PVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 223 TLRETDVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIeTNPVKYKHFEITMTVSIGLAGSSNdfKNHERWIEAADKAL 302
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVV-SKPIMIDDKPFPLTLSIGISYDVG--KNRDYLLSTAHNAM 516
|
....*....
gi 639310448 303 YQSKNTGRN 311
Cdd:PRK11359 517 DYIRKNGGN 525
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
144-314 |
4.05e-14 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 72.35 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 144 LEELNKKLEQVSQTDSLTQLANRGHWEGTLrQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTT 223
Cdd:PRK09966 237 LQAKNAQLLRTALHDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEF 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 224 LRETDVAGRYGGEEFAVTLLDTDKEgafvfAERLRVLIETNPVKYKHFE------ITMTVSIGLAgSSNDFKNHERWIEA 297
Cdd:PRK09966 316 GGLRHKAYRLGGDEFAMVLYDVQSE-----SEVQQICSALTQIFNLPFDlhnghqTTMTLSIGYA-MTIEHASAEKLQEL 389
|
170
....*....|....*..
gi 639310448 298 ADKALYQSKNTGRNKVI 314
Cdd:PRK09966 390 ADHNMYQAKHQRAEKLV 406
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
186-307 |
6.67e-12 |
|
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: 61.99 E-value: 6.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 186 CSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRET-DVAGRYGGEEFAVTLLDTDKEGAFVFAERLRVLIET- 263
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAl 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 639310448 264 NPVKYKHFEI-----TMTVSIGLAGSSNDFKNHERWIEAADKALYQSKN 307
Cdd:cd07556 81 NQSEGNPVRVrigihTGPVVVGVIGSRPQYDVWGALVNLASRMESQAKA 129
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
2-245 |
1.61e-08 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 54.65 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 2 AADLEMNEIHWLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFRsksesvfvlKNR 81
Cdd:COG2202 2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFL---------ELL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 82 SFTIWEQQPYIFRFKNYRPiTGKadYMYQNATFIPLTNTMGEVSHICIILYDVTDvavnKKELEELNKKLEQvsQTDSLT 161
Cdd:COG2202 73 RAALAGGGVWRGELRNRRK-DGS--LFWVELSISPVRDEDGEITGFVGIARDITE----RKRAEEALRESEE--RLRLLV 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 162 QLANRGHWEGTLRQEFLRVKRSGGCSTLLMFDIDHFKKINDEYGHSCGDESLRHLSNLLRTTLRETDVAGRYGGEEFAVT 241
Cdd:COG2202 144 ENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWV 223
|
....
gi 639310448 242 LLDT 245
Cdd:COG2202 224 WVEA 227
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
16-134 |
2.16e-05 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain 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: 43.17 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 16 MFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFRSKSESVFVLKNRSFTIWeqqpYIFRF 95
Cdd:pfam00989 6 ILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFE----VSFRV 81
|
90 100 110
....*....|....*....|....*....|....*....
gi 639310448 96 KNYRPItgkadYMYQNATfiPLTNTMGEVSHICIILYDV 134
Cdd:pfam00989 82 PDGRPR-----HVEVRAS--PVRDAGGEILGFLGVLRDI 113
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
6-164 |
3.22e-05 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 45.22 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 6 EMNEIH-WLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEkwFRSKSESVfVLKNRSFT 84
Cdd:COG3852 1 ALRESEeLLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSP--LRELLERA-LAEGQPVT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 85 IWEqqpYIFRFKNYRPITgkADYmyqnaTFIPLTNTMGEVsHICIILYDVTDvavnKKELEElnkKLEQVSQTDSLTQLA 164
Cdd:COG3852 78 ERE---VTLRRKDGEERP--VDV-----SVSPLRDAEGEG-GVLLVLRDITE----RKRLER---ELRRAEKLAAVGELA 139
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
140-317 |
2.85e-04 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 42.62 E-value: 2.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 140 NKKELEELNKKLEQVSQTDSLTQLANRGHWEGTLRQEFL-RVKRSGGCstLLMFDIDHFKKINDEYGHSCGDESLRHLSN 218
Cdd:PRK11829 217 NQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIAsSTRTDHFH--LLVIGIETLQEVSGAMSEAQHQQLLLTIVQ 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 219 LLRTTLRETDVAGRYGGEEFAVTLLDTDKEG-AFVFAERLRVLIeTNPVKYKHFEITMTVSIGLAGSSNDFKNHERWIEA 297
Cdd:PRK11829 295 RIEQCIDDSDLLAQLSKTEFAVLARGTRRSFpAMQLARRIMSQV-TQPLFFDEITLRPSASIGITRYQAQQDTAESMMRN 373
|
170 180
....*....|....*....|
gi 639310448 298 ADKALYQSKNTGRNKVIAYE 317
Cdd:PRK11829 374 ASTAMMAAHHEGRNQIMVFE 393
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
2-153 |
3.11e-04 |
|
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: 42.07 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 639310448 2 AADLEMNEIH-WLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPaidekwfrsKSESVFVLKN 80
Cdd:COG3829 1 AEELELKELEeELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIP---------NSPLLEVLKT 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 639310448 81 RsftiweqQPYIFRFKNYRPitgkaDYMYQNATFIPLTNTmGEVSHICIILYDVTdvavnkkELEELNKKLEQ 153
Cdd:COG3829 72 G-------KPVTGVIQKTGG-----KGKTVIVTAIPIFED-GEVIGAVETFRDIT-------ELKRLERKLRE 124
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
11-69 |
9.85e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 36.99 E-value: 9.85e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 639310448 11 HWLMDMFNTVDVGLVVLDRDYKVCVWNGFMENHSGLLPSAVKDKDLFDLFPAIDEKWFR 69
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQ 59
|
|
|