|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
223-396 |
2.93e-57 |
|
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: 198.85 E-value: 2.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 223 LLEEIQIWDNQLQKENRKLSFQAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEV 301
Cdd:COG5001 229 AVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRlALLFIDLDRFKEINDTLGHAAGDEL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 302 LKEMANRLQTRLRHQDFIARLGGDEFAVILHSISHADHLISIAENLLESCKEPLHLNGQTIYFSFSVGIALS-QFASSPE 380
Cdd:COG5001 309 LREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYpDDGADAE 388
|
170
....*....|....*.
gi 1955935882 381 DFIMQADQAMYKAKNS 396
Cdd:COG5001 389 ELLRNADLAMYRAKAA 404
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
3-395 |
3.79e-56 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 189.83 E-value: 3.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 3 SKLYQSTSLHALFRKSQFTIFaITFFICSFTFVSISVFTMETYAKQNLQLLSHTLLERIQPAVVFNDKITIEQILNEYTK 82
Cdd:PRK09966 6 SLNKRPTFKRALRNISMTSIF-ITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 83 DHSIRTIHIYDSEHHLIAqSFKLSSQTS--ILEGWFDHWFLNEPVHLTIYHHEQNVGELTLFGSSEKILQFlkmIMVGLA 160
Cdd:PRK09966 85 QGQFSTAEVRDKQQNILA-SWHYTRKDPgdTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHF---IWFSLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 161 IAMLFIVCALWWSVNLT---YRQIMQAIYPLTNIAQIVSEQKAYNLRFPYNRIKEFQDLNTVFNELLEEIQIWDNQLQKE 237
Cdd:PRK09966 161 VLTGCILLASGIAITLTrhlHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 238 NRKLSFQAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKSALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQT--RLRH 315
Cdd:PRK09966 241 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEfgGLRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 316 QDFiaRLGGDEFAVILHSISHADHLISIAENLLESCKEPLHL-NGQTIYFSFSVGIALSQFASSPEDFIMQADQAMYKAK 394
Cdd:PRK09966 321 KAY--RLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
|
.
gi 1955935882 395 N 395
Cdd:PRK09966 399 H 399
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
246-396 |
1.32e-53 |
|
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: 175.44 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 246 HHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARLGG 324
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPlALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955935882 325 DEFAVILHSISHADhLISIAENLLESCKEPLHLNGQTIYFSFSVGIALSQF-ASSPEDFIMQADQAMYKAKNS 396
Cdd:cd01949 81 DEFAILLPGTDLEE-AEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRS 152
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
245-396 |
1.30e-46 |
|
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: 157.41 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 245 AHHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARLG 323
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955935882 324 GDEFAVILHSIS--HADHLISIAENLLESCKEPLHLNGQTIYFSFSVGIALSQF-ASSPEDFIMQADQAMYKAKNS 396
Cdd:pfam00990 81 GDEFAILLPETSleGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNdGEDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
244-396 |
3.00e-45 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 153.94 E-value: 3.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 244 QAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARL 322
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955935882 323 GGDEFAVILHSISHaDHLISIAENLLESCKEPLHLNGQTIYFSFSVGIAL-SQFASSPEDFIMQADQAMYKAKNS 396
Cdd:smart00267 82 GGDEFALLLPETSL-EEAIALAERILQQLREPIIIHGIPLYLTISIGVAAyPNPGEDAEDLLKRADTALYQAKKA 155
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
244-396 |
9.02e-39 |
|
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: 137.08 E-value: 9.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 244 QAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARL 322
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955935882 323 GGDEFAVILHSISHADHLiSIAENLLE--SCKEPLHLNGQTIYFSFSVGIA-LSQFASSPEDFIMQADQAMYKAKNS 396
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDAL-SKAERLRDaiNSKPIEVAGSETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKA 156
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
248-396 |
1.44e-29 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 119.24 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 248 DQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARLGGDE 326
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPlSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955935882 327 FAVILHSISHADhLISIAENLLESC-KEPLHLNGQ--TIYFSFSVGIA-LSQFASSPEDFIMQADQAMYKAKNS 396
Cdd:PRK09581 375 FVVVMPDTDIED-AIAVAERIRRKIaEEPFIISDGkeRLNVTVSIGVAeLRPSGDTIEALIKRADKALYEAKNT 447
|
|
| CHASE8 |
pfam17152 |
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine ... |
42-141 |
1.95e-20 |
|
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine kinases, diguanylate cyclases/phosphodiesterases and methyl-accepting chemotaxis proteins, including the diguanylate cyclase DgcN (YfiN) that regulates biofilm formation and motility in Escherichia coli. In Pseudomonas aeruginosa, CHASE8 is the sensor domain in the diguanylate cyclase TpbB that regulates biofilm formation by controlling the levels of extracellular DNA.
Pssm-ID: 435752 Cd Length: 102 Bit Score: 85.38 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 42 METYAKQNLQLLSHTLLERIQPAVVFNDKITIEQILNEYTKDHSIRTIHIYDSEHHLIAQ-SFKLSSQTSILEGWFDHWF 120
Cdd:pfam17152 1 LRRYAQQNLELLARSIAYNVEAALVFGDPAAARETLAALGAQPQIASAAVYDAQGRLFASyARPGTDPPEPLEALLARWL 80
|
90 100
....*....|....*....|.
gi 1955935882 121 LNEPVHLTIYHHEQNVGELTL 141
Cdd:pfam17152 81 LPAPVLQPIVHDGERIGSVVL 101
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
149-245 |
4.23e-05 |
|
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: 45.34 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 149 LQFLkMIMVGLAIAMLFIVCALWWSVNLtYRQIMQAIYPLTNIAQIVSEQKaYNLRFPYNRIKEFQDLNTVFNELLEEIQ 228
Cdd:COG5000 3 LQIL-FLLLLLLIALLLLLLALWLALLL-ARRLTRPLRRLAEATRAVAAGD-LSVRLPVTGDDEIGELARAFNRMTDQLK 79
|
90
....*....|....*..
gi 1955935882 229 iwDNQLQKENRKLSFQA 245
Cdd:COG5000 80 --EQREELEERRRYLET 94
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
223-396 |
2.93e-57 |
|
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: 198.85 E-value: 2.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 223 LLEEIQIWDNQLQKENRKLSFQAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEV 301
Cdd:COG5001 229 AVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRlALLFIDLDRFKEINDTLGHAAGDEL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 302 LKEMANRLQTRLRHQDFIARLGGDEFAVILHSISHADHLISIAENLLESCKEPLHLNGQTIYFSFSVGIALS-QFASSPE 380
Cdd:COG5001 309 LREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYpDDGADAE 388
|
170
....*....|....*.
gi 1955935882 381 DFIMQADQAMYKAKNS 396
Cdd:COG5001 389 ELLRNADLAMYRAKAA 404
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
3-395 |
3.79e-56 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 189.83 E-value: 3.79e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 3 SKLYQSTSLHALFRKSQFTIFaITFFICSFTFVSISVFTMETYAKQNLQLLSHTLLERIQPAVVFNDKITIEQILNEYTK 82
Cdd:PRK09966 6 SLNKRPTFKRALRNISMTSIF-ITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 83 DHSIRTIHIYDSEHHLIAqSFKLSSQTS--ILEGWFDHWFLNEPVHLTIYHHEQNVGELTLFGSSEKILQFlkmIMVGLA 160
Cdd:PRK09966 85 QGQFSTAEVRDKQQNILA-SWHYTRKDPgdTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHF---IWFSLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 161 IAMLFIVCALWWSVNLT---YRQIMQAIYPLTNIAQIVSEQKAYNLRFPYNRIKEFQDLNTVFNELLEEIQIWDNQLQKE 237
Cdd:PRK09966 161 VLTGCILLASGIAITLTrhlHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 238 NRKLSFQAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKSALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQT--RLRH 315
Cdd:PRK09966 241 NAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEfgGLRH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 316 QDFiaRLGGDEFAVILHSISHADHLISIAENLLESCKEPLHL-NGQTIYFSFSVGIALSQFASSPEDFIMQADQAMYKAK 394
Cdd:PRK09966 321 KAY--RLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGYAMTIEHASAEKLQELADHNMYQAK 398
|
.
gi 1955935882 395 N 395
Cdd:PRK09966 399 H 399
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
148-396 |
1.66e-54 |
|
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: 181.72 E-value: 1.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 148 ILQFLKMIMVGLAIAMLFIVCALWWSVNLTYRQIMQAIYPLTNIAQIVSEQKAYNLRFPYNRIKEFQDLNTVFNELLEEI 227
Cdd:COG2199 18 LLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 228 QIWdNQLQKENRKLSFQAHHDQLTLLPNRHYFYQILLDMFDD-KDFDNKSALLFIDNNNFKAINDQFGHLAGDEVLKEMA 306
Cdd:COG2199 98 EDI-TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARaRREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 307 NRLQTRLRHQDFIARLGGDEFAVILHSIShADHLISIAENLLESCKE-PLHLNGQTIYFSFSVGIA-LSQFASSPEDFIM 384
Cdd:COG2199 177 RRLRASLRESDLVARLGGDEFAVLLPGTD-LEEAEALAERLREALEQlPFELEGKELRVTVSIGVAlYPEDGDSAEELLR 255
|
250
....*....|..
gi 1955935882 385 QADQAMYKAKNS 396
Cdd:COG2199 256 RADLALYRAKRA 267
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
246-396 |
1.32e-53 |
|
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: 175.44 E-value: 1.32e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 246 HHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARLGG 324
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPlALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955935882 325 DEFAVILHSISHADhLISIAENLLESCKEPLHLNGQTIYFSFSVGIALSQF-ASSPEDFIMQADQAMYKAKNS 396
Cdd:cd01949 81 DEFAILLPGTDLEE-AEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEdGEDAEELLRRADEALYRAKRS 152
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
245-396 |
1.30e-46 |
|
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: 157.41 E-value: 1.30e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 245 AHHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARLG 323
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955935882 324 GDEFAVILHSIS--HADHLISIAENLLESCKEPLHLNGQTIYFSFSVGIALSQF-ASSPEDFIMQADQAMYKAKNS 396
Cdd:pfam00990 81 GDEFAILLPETSleGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNdGEDPEDLLKRADTALYQAKQA 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
244-396 |
3.00e-45 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 153.94 E-value: 3.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 244 QAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARL 322
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955935882 323 GGDEFAVILHSISHaDHLISIAENLLESCKEPLHLNGQTIYFSFSVGIAL-SQFASSPEDFIMQADQAMYKAKNS 396
Cdd:smart00267 82 GGDEFALLLPETSL-EEAIALAERILQQLREPIIIHGIPLYLTISIGVAAyPNPGEDAEDLLKRADTALYQAKKA 155
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
244-396 |
9.02e-39 |
|
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: 137.08 E-value: 9.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 244 QAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARL 322
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1955935882 323 GGDEFAVILHSISHADHLiSIAENLLE--SCKEPLHLNGQTIYFSFSVGIA-LSQFASSPEDFIMQADQAMYKAKNS 396
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDAL-SKAERLRDaiNSKPIEVAGSETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKA 156
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
248-396 |
1.44e-29 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 119.24 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 248 DQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARLGGDE 326
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPlSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1955935882 327 FAVILHSISHADhLISIAENLLESC-KEPLHLNGQ--TIYFSFSVGIA-LSQFASSPEDFIMQADQAMYKAKNS 396
Cdd:PRK09581 375 FVVVMPDTDIED-AIAVAERIRRKIaEEPFIISDGkeRLNVTVSIGVAeLRPSGDTIEALIKRADKALYEAKNT 447
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
239-396 |
1.26e-27 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 115.54 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 239 RKLSFQAHHDQLTLLPNRHYFYQILLDMFDD-KDFDNKSALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQD 317
Cdd:PRK09776 659 RQLSYSASHDALTHLANRASFEKQLRRLLQTvNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 318 FIARLGGDEFAVILH--SISHADhliSIAENLLES-CKEPLHLNGQTIYFSFSVGIALSQFASSPEDFIM-QADQAMYKA 393
Cdd:PRK09776 739 VLARLGGDEFGLLLPdcNVESAR---FIATRIISAiNDYHFPWEGRVYRVGASAGITLIDANNHQASEVMsQADIACYAA 815
|
...
gi 1955935882 394 KNS 396
Cdd:PRK09776 816 KNA 818
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
239-394 |
9.22e-26 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 109.33 E-value: 9.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 239 RKLSFQAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKS-ALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQD 317
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPfSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 318 FIARLGGDEFAVILHSISHADHLiSIAENLLES--CKEPLHLNGQTIYFSFSVGIALSQfASSPEDF---IMQADQAMYK 392
Cdd:PRK15426 472 VAGRVGGEEFCVVLPGASLAEAA-QVAERIRLRinEKEILVAKSTTIRISASLGVSSAE-EDGDYDFeqlQSLADRRLYL 549
|
..
gi 1955935882 393 AK 394
Cdd:PRK15426 550 AK 551
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
240-406 |
3.12e-25 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 107.85 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 240 KLSFQAHHDQLTLLPNRHYFYQILLDMFDDKDfDNKSALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFI 319
Cdd:PRK10060 232 RLRILANTDSITGLPNRNAIQELIDHAINAAD-NNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 320 ARLGGDEFAViLHSISHADHLISIAENLLESCKEPLHLNGQTIYFSFSVGIALS-QFASSPEDFIMQADQAMYKAKNSDE 398
Cdd:PRK10060 311 ARLGGDEFLV-LASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALApEHGDDSESLIRSADTAMYTAKEGGR 389
|
....*....
gi 1955935882 399 HWF-IYKPE 406
Cdd:PRK10060 390 GQFcVFSPE 398
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
235-406 |
7.55e-23 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 101.00 E-value: 7.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 235 QKENRKLSFQ-AHHDQLTLLPNRHYFYQILLDMFDDkdfDNKSALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRL 313
Cdd:PRK11359 365 QEKSRQHIEQlIQFDPLTGLPNRNNLHNYLDDLVDK---AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 314 RHQDFIARLGGDEFAVI-----LHSISH-ADHLISIAenllescKEPLHLNGQTIYFSFSVGIALSqFASSPEDFIMQAD 387
Cdd:PRK11359 442 KPDQYLCRIEGTQFVLVslendVSNITQiADELRNVV-------SKPIMIDDKPFPLTLSIGISYD-VGKNRDYLLSTAH 513
|
170 180
....*....|....*....|
gi 1955935882 388 QAM-YKAKNSDEHWFIYKPE 406
Cdd:PRK11359 514 NAMdYIRKNGGNGWQFFSPA 533
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
233-396 |
3.72e-21 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 94.13 E-value: 3.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 233 QLQKENRKLSFQAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKSA-LLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQT 311
Cdd:PRK10245 193 KLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDAtLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQI 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 312 RLRHQDFIARLGGDEFAVILhSISHADHLISIAENLLESCKEPLHLNGQTIYFSFSVGIA--LSQFASSPEdFIMQADQA 389
Cdd:PRK10245 273 TLRGSDVIGRFGGDEFAVIM-SGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAplNPQMSHYRE-WLKSADLA 350
|
....*..
gi 1955935882 390 MYKAKNS 396
Cdd:PRK10245 351 LYKAKNA 357
|
|
| CHASE8 |
pfam17152 |
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine ... |
42-141 |
1.95e-20 |
|
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine kinases, diguanylate cyclases/phosphodiesterases and methyl-accepting chemotaxis proteins, including the diguanylate cyclase DgcN (YfiN) that regulates biofilm formation and motility in Escherichia coli. In Pseudomonas aeruginosa, CHASE8 is the sensor domain in the diguanylate cyclase TpbB that regulates biofilm formation by controlling the levels of extracellular DNA.
Pssm-ID: 435752 Cd Length: 102 Bit Score: 85.38 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 42 METYAKQNLQLLSHTLLERIQPAVVFNDKITIEQILNEYTKDHSIRTIHIYDSEHHLIAQ-SFKLSSQTSILEGWFDHWF 120
Cdd:pfam17152 1 LRRYAQQNLELLARSIAYNVEAALVFGDPAAARETLAALGAQPQIASAAVYDAQGRLFASyARPGTDPPEPLEALLARWL 80
|
90 100
....*....|....*....|.
gi 1955935882 121 LNEPVHLTIYHHEQNVGELTL 141
Cdd:pfam17152 81 LPAPVLQPIVHDGERIGSVVL 101
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
248-396 |
4.26e-18 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 83.96 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 248 DQLTLLPNRhyfyQILLDMFDDKDF---DNKSALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDFIARLGG 324
Cdd:PRK09894 132 DVLTGLPGR----RVLDESFDHQLRnrePQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955935882 325 DEFAVILHSISHADHLiSIAENLLESCKE-PLHLNGQTIYFSFSVGIALSQFASSPEDFIMQADQAMYKAKNS 396
Cdd:PRK09894 208 EEFIICLKAATDEEAC-RAGERIRQLIANhAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQT 279
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
309-394 |
5.48e-10 |
|
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: 58.00 E-value: 5.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 309 LQTRLrhqDFIARLGGDEFAVILHSIShADHLISIAENLLESCKEPlhlngQTIYFSFSVGIAlsqfassPEDFIMQADq 388
Cdd:COG3706 111 LLARV---DLVARYGGEEFAILLPGTD-LEGALAVAERIREAVAEL-----PSLRVTVSIGVA-------GDSLLKRAD- 173
|
....*.
gi 1955935882 389 AMYKAK 394
Cdd:COG3706 174 ALYQAR 179
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
278-371 |
7.37e-10 |
|
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: 56.60 E-value: 7.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 278 LLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRL-RHQDFIARLGGDEFAVILhSISHADHLISIAENLLESCKEplh 356
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVS-GLDHPAAAVAFAEDMREAVSA--- 79
|
90
....*....|....*.
gi 1955935882 357 LNGQTI-YFSFSVGIA 371
Cdd:cd07556 80 LNQSEGnPVRVRIGIH 95
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
97-394 |
2.79e-06 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 49.33 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 97 HLIAQSFKLSSQTSilegwfdhwflnepvhLTIYHHE-----QNVGELTLFGSSEKILQFL-----KMIMVGLAIAMLFI 166
Cdd:PRK13561 97 VMVTRLFELPVQIS----------------LPVYSLErpanpQPLAYLVLQADSFRMYKFVmsalsTLVTIYLLLSLILT 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 167 VcALWWSVNltyRQImqaIYPLTNIA---QIVSEQKA--YNLRFP-YNRIKEFQDLNTVFNElleeiqiwdNQ--LQKEN 238
Cdd:PRK13561 161 V-AISWCIN---RLI---VHPLRNIArelNDIPPQELvgHQLALPrLHQDDEIGMLVRSYNL---------NQqlLQRQY 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 239 RKLSFQAHHDQLTLLPNRHYFYQILLDMFDDKDfdnKSALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRHQDF 318
Cdd:PRK13561 225 EEQSRNATRFPVSDLPNKALLMALLEQVVARKQ---TTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMV 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955935882 319 IARLGGDEFAVILHSISHADHLISIAENLLESCKEPLHLNGQTIYFSFSVGIALSQFASSPEDFIMQADQAMYKAK 394
Cdd:PRK13561 302 LAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTAR 377
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
29-393 |
1.49e-05 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 47.24 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 29 ICSFTFVSISVFTME---TYAKQnLQLLSHTLLERIQPAVVFNDKITIEQILNeytkdhSIRTIHIydsehhLIAQSFKL 105
Cdd:PRK11829 12 ICIFIILQLFHFVQQrkdDYANQ-LESIAYSVRQPLSEAILSVDIPQAKKILN------SLLPIGI------LSRAEVIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 106 SSQTSILEGWFD------HW---FLNEPVHLT--IYHHE------QNVGELTLFGSSEKILQFL-----KMIMVGLAIAM 163
Cdd:PRK11829 79 PNQIQVLHANFPterpipHWakrVFSLPVQITvpLYALErvpanpQPLAHLVLRADSFRMYQFIlsalsAMLSTYLLLAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 164 LFIVcALWWSVNltyRQImqaIYPLTNIAQIVSEQKAYNLRF------PYNRIKEFQDLNTVFNElleeiqiwdNQ--LQ 235
Cdd:PRK11829 159 VLSV-SIAWCIN---RLI---IHPLRAMAKELEDIGDHGVLHhqltlpAHHQDDELGVLVRNYNR---------NQqlLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 236 KENRKLSFQAHHDQLTLLPNRHYFYQILLDMFDDKDFDNKSALLFIDNNNFKAINDQFGHLAGDEVLKEMANRLQTRLRH 315
Cdd:PRK11829 223 DAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDD 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1955935882 316 QDFIARLGGDEFAVILHSISHADHLISIAENLLESCKEPLHLNGQTIYFSFSVGIALSQFA-SSPEDFIMQADQAMYKA 393
Cdd:PRK11829 303 SDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQqDTAESMMRNASTAMMAA 381
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
149-245 |
4.23e-05 |
|
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: 45.34 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 149 LQFLkMIMVGLAIAMLFIVCALWWSVNLtYRQIMQAIYPLTNIAQIVSEQKaYNLRFPYNRIKEFQDLNTVFNELLEEIQ 228
Cdd:COG5000 3 LQIL-FLLLLLLIALLLLLLALWLALLL-ARRLTRPLRRLAEATRAVAAGD-LSVRLPVTGDDEIGELARAFNRMTDQLK 79
|
90
....*....|....*..
gi 1955935882 229 iwDNQLQKENRKLSFQA 245
Cdd:COG5000 80 --EQREELEERRRYLET 94
|
|
| AhpA |
COG3726 |
Uncharacterized membrane protein Smp affecting hemolysin expression [Function unknown]; |
14-102 |
4.90e-04 |
|
Uncharacterized membrane protein Smp affecting hemolysin expression [Function unknown];
Pssm-ID: 442940 Cd Length: 208 Bit Score: 41.06 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955935882 14 LFRKSQFTIFAITFFICSFTFVSISVFTMETYAKQNLQL--LSHTLLERI----QPAVVFNDKI-TIEQILNEYTKDHSI 86
Cdd:COG3726 8 KKRLHRTLIVLICLALLVILLQGASYFSLGSQLALSNQVenLARLLVRQAafsaSPLLVNNDKNeRLTALLNQLTKESRI 87
|
90
....*....|....*.
gi 1955935882 87 RTIHIYDSEHHLIAQS 102
Cdd:COG3726 88 LDASVYDADGELLAQS 103
|
|
| |
