|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
321-529 |
1.70e-73 |
|
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: 246.22 E-value: 1.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 321 ILFWYVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDL 400
Cdd:COG5001 211 RLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 401 NRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDEFAIIVHN-QTEQQLLDLCKTLFRITEEPFVVNQHSFY 479
Cdd:COG5001 291 DRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEPFELDGHELY 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2278473191 480 LSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAVCMYDETLSQKV 529
Cdd:COG5001 371 VSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERA 420
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
362-519 |
7.72e-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: 200.09 E-value: 7.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 362 FHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGG 441
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2278473191 442 DEFAIIVHNQTEQQLLDLCKTLFRITEEPFVVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAVC 519
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
361-516 |
4.29e-58 |
|
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: 190.16 E-value: 4.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 361 AFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIG 440
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2278473191 441 GDEFAIIV-HNQTE--QQLLDLCKTLFRITEEPFVVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNN 516
Cdd:pfam00990 81 GDEFAILLpETSLEgaQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
359-521 |
7.83e-55 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 181.68 E-value: 7.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 359 YLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLAR 438
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 439 IGGDEFAIIVHNQTEQQLLDLCKTLFRITEEPFVVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAV 518
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 2278473191 519 CMY 521
Cdd:smart00267 161 AVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
360-522 |
8.33e-36 |
|
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: 131.31 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 360 LAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARI 439
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 440 GGDEFAIIVHNQTEQQLLDLCKTLFR-ITEEPF-VVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNA 517
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDaINSKPIeVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 2278473191 518 VCMYD 522
Cdd:TIGR00254 161 VVVAD 165
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
250-529 |
1.61e-33 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 134.81 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 250 ILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLdedkSELEAAikkgkrCSSSSLQLRVKNNNEKDILFWYVTIv 329
Cdd:PRK10060 124 IVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKLFM----SRREAA------ASRRNIRGFFRSGNAYEVERWIKTR- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 330 pimiEGQTF----------GS-----YVMVK--DITRMKQQQEEINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQdk 392
Cdd:PRK10060 193 ----KGQRLflfrnkfvhsGSgkneiFLICSgtDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQ-- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 393 FGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDEFaIIVHNQTEQQLLDlcKTLFRITE---E 469
Cdd:PRK10060 267 VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF-LVLASHTSQAALE--AMASRILTrlrL 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 470 PFVVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAVCMYDETLSQKV 529
Cdd:PRK10060 344 PFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRV 403
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
231-357 |
8.24e-15 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 76.04 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 231 DLVKNQERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDK--SELEAAIKKGKRCSSSS 308
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPlrELLERALAEGQPVTERE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2278473191 309 LQLRVKNNNEKDILfwyVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEI 357
Cdd:COG3852 81 VTLRRKDGEERPVD---VSVSPLRDAEGEGGVLLVLRDITERKRLEREL 126
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
236-357 |
5.58e-12 |
|
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: 62.69 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 236 QERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKK--GKRCSSSSLQLRV 313
Cdd:TIGR00229 2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERrlEGEPEPVSEERRV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2278473191 314 KNNNEKdiLFW-YVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEI 357
Cdd:TIGR00229 82 RRKDGS--EIWvEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
256-348 |
1.66e-07 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 49.00 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 256 NGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSE-LEAAIKKGKRCSSSSLQLRVKNNNEkdilFWY-VTIVPIMI 333
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSErLREALREGKAVREFEVVLYRKDGEP----FPVlVSLAPIRD 76
|
90
....*....|....*.
gi 2278473191 334 EGQTFGSYV-MVKDIT 348
Cdd:pfam13426 77 DGGELVGIIaILRDIT 92
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
364-474 |
7.93e-07 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 51.50 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 364 DTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDE 443
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
90 100 110
....*....|....*....|....*....|....
gi 2278473191 444 FAIIVHNQTE---QQLLDLCKTLFRITEEPFVVN 474
Cdd:NF040885 424 FCIILIDYEEaeaQNLIERIRQHLRTIDPDKRVS 457
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
237-301 |
2.19e-06 |
|
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: 45.08 E-value: 2.19e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2278473191 237 ERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKKG 301
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRL 65
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
247-347 |
1.52e-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. 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: 43.78 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 247 PDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKKGKRCSSS-SLQLRVKNNNEKDILfWY 325
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPvTLEVRLRRKDGSVIW-VL 80
|
90 100
....*....|....*....|...
gi 2278473191 326 VTIVPIMIEGQTFGSYVM-VKDI 347
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGvVRDI 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
321-529 |
1.70e-73 |
|
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: 246.22 E-value: 1.70e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 321 ILFWYVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDL 400
Cdd:COG5001 211 RLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 401 NRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDEFAIIVHN-QTEQQLLDLCKTLFRITEEPFVVNQHSFY 479
Cdd:COG5001 291 DRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDlDDPEDAEAVAERILAALAEPFELDGHELY 370
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2278473191 480 LSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAVCMYDETLSQKV 529
Cdd:COG5001 371 VSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERA 420
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
320-521 |
4.23e-65 |
|
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: 212.92 E-value: 4.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 320 DILFWYVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYID 399
Cdd:COG2199 73 ALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLID 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 400 LNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDEFAIIVHNQTEQQLLDLCKTLFR-ITEEPFVVNQHSF 478
Cdd:COG2199 153 LDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREaLEQLPFELEGKEL 232
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2278473191 479 YLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAVCMY 521
Cdd:COG2199 233 RVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
362-519 |
7.72e-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: 200.09 E-value: 7.72e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 362 FHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGG 441
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2278473191 442 DEFAIIVHNQTEQQLLDLCKTLFRITEEPFVVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAVC 519
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
361-516 |
4.29e-58 |
|
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: 190.16 E-value: 4.29e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 361 AFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIG 440
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2278473191 441 GDEFAIIV-HNQTE--QQLLDLCKTLFRITEEPFVVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNN 516
Cdd:pfam00990 81 GDEFAILLpETSLEgaQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
359-521 |
7.83e-55 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 181.68 E-value: 7.83e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 359 YLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLAR 438
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 439 IGGDEFAIIVHNQTEQQLLDLCKTLFRITEEPFVVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAV 518
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 2278473191 519 CMY 521
Cdd:smart00267 161 AVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
360-522 |
8.33e-36 |
|
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: 131.31 E-value: 8.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 360 LAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARI 439
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 440 GGDEFAIIVHNQTEQQLLDLCKTLFR-ITEEPF-VVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNA 517
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDaINSKPIeVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 2278473191 518 VCMYD 522
Cdd:TIGR00254 161 VVVAD 165
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
250-529 |
1.61e-33 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 134.81 E-value: 1.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 250 ILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLdedkSELEAAikkgkrCSSSSLQLRVKNNNEKDILFWYVTIv 329
Cdd:PRK10060 124 IVILDSRGNIQRFNRLCEEYTGLKEHDVIGQSVFKLFM----SRREAA------ASRRNIRGFFRSGNAYEVERWIKTR- 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 330 pimiEGQTF----------GS-----YVMVK--DITRMKQQQEEINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQdk 392
Cdd:PRK10060 193 ----KGQRLflfrnkfvhsGSgkneiFLICSgtDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQ-- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 393 FGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDEFaIIVHNQTEQQLLDlcKTLFRITE---E 469
Cdd:PRK10060 267 VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF-LVLASHTSQAALE--AMASRILTrlrL 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 470 PFVVNQHSFYLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAVCMYDETLSQKV 529
Cdd:PRK10060 344 PFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRV 403
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
248-521 |
2.25e-31 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 129.41 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 248 DPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIF--LDEDKSELEAAIKKGKRCSSSS-LQ----LRVKNNNEKD 320
Cdd:PRK09776 547 EAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVLhiTFGDNGPLMENIYSCLTSRSAAyLEqdvvLHCRSGGSYD 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 321 ILFwyvTIVPIM-IEGQTFGSYVMVKDITRMKQQQEEINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYID 399
Cdd:PRK09776 627 VHY---SITPLStLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFID 703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 400 LNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDEFAIIVHNQTEQQLLDLCKTLFR-ITEEPFVVNQHSF 478
Cdd:PRK09776 704 LDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISaINDYHFPWEGRVY 783
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2278473191 479 YLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNNAVCMY 521
Cdd:PRK09776 784 RVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVY 826
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
346-522 |
1.47e-27 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 115.38 E-value: 1.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 346 DITRMKQQQEeINyLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKR 425
Cdd:PRK09581 279 DALRNNLEQS-IE-MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKR 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 426 FRTCLSPTVPLARIGGDEFAIIVHNQTEQQLLDLCKTLFR-ITEEPFVVNQHSFYLSL--SIGIAVYPFGGINTTTLLQH 502
Cdd:PRK09581 357 LRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRkIAEEPFIISDGKERLNVtvSIGVAELRPSGDTIEALIKR 436
|
170 180
....*....|....*....|
gi 2278473191 503 ADIAMYSAKEKGNNAVCMYD 522
Cdd:PRK09581 437 ADKALYEAKNTGRNRVVALA 456
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
347-515 |
3.64e-23 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 103.70 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 347 ITRMKQQQEeINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKTqdkfGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRF 426
Cdd:PRK11359 363 LEQEKSRQH-IEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRF 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 427 RTCLSPTVPLARIGGDEFAIIVHNQTEQQLLDLCKTLFRITEEPFVVNQHSFYLSLSIGIAvYPFGGiNTTTLLQHADIA 506
Cdd:PRK11359 438 REKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGIS-YDVGK-NRDYLLSTAHNA 515
|
170
....*....|
gi 2278473191 507 M-YSAKEKGN 515
Cdd:PRK11359 516 MdYIRKNGGN 525
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
364-526 |
8.21e-22 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 95.90 E-value: 8.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 364 DTVTEIGNRIFFQQELDRSikRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDE 443
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQ--LRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 444 FAIIVHNQTEQQ----LLDLCKTlfrITEEPFVVNQHSFYLSLSIGIAVYpFGGINTTTLLQHADIAMYSAKEKGNNAVC 519
Cdd:PRK09894 210 FIICLKAATDEEacraGERIRQL---IANHAITHSDGRINITATFGVSRA-FPEETLDVVIGRADRAMYEGKQTGRNRVM 285
|
....*..
gi 2278473191 520 MYDETLS 526
Cdd:PRK09894 286 FIDEQNV 292
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
354-529 |
3.40e-20 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 93.93 E-value: 3.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 354 QEEINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPT 433
Cdd:PRK15426 391 QSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQ 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 434 VPLARIGGDEFAIIVHNQTEQQLLDLCKTL-FRITEEP-FVVNQHSFYLSLSIGIA-VYPFGGINTTTLLQHADIAMYSA 510
Cdd:PRK15426 471 DVAGRVGGEEFCVVLPGASLAEAAQVAERIrLRINEKEiLVAKSTTIRISASLGVSsAEEDGDYDFEQLQSLADRRLYLA 550
|
170
....*....|....*....
gi 2278473191 511 KEKGNNAVCMYDETLSQKV 529
Cdd:PRK15426 551 KQAGRNRVCASDNAHEREV 569
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
349-513 |
8.64e-20 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 91.61 E-value: 8.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 349 RMKQQQEEINYLAFHDTVTEIGNRIFFQQELDrSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRT 428
Cdd:PRK09966 236 RLQAKNAQLLRTALHDPLTGLANRAAFRSGIN-TLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 429 CLSPTVPLARIGGDEFAIIVHN-QTEQQLLDLCKTLFRITEEPFVV-NQHSFYLSLSIGIAVyPFGGINTTTLLQHADIA 506
Cdd:PRK09966 315 FGGLRHKAYRLGGDEFAMVLYDvQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGYAM-TIEHASAEKLQELADHN 393
|
....*..
gi 2278473191 507 MYSAKEK 513
Cdd:PRK09966 394 MYQAKHQ 400
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
349-528 |
2.23e-18 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 88.62 E-value: 2.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 349 RMKQQQEEINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKtqdkFGLLYIdlnRFKTINDTLGhsigdkVLKE------- 421
Cdd:PRK13561 219 LLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQT----TALMII---TCETLRDTAG------VLKEaqreill 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 422 --VAKRFRTCLSPTVPLARIGGDEFAIIVHN-QTEQQLLDLCKTLFRITEEPFVVNQHSFYLSLSIGIAVYpFGGINTTT 498
Cdd:PRK13561 286 ltLVEKLKSVLSPRMVLAQISGYDFAIIANGvKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQ 364
|
170 180 190
....*....|....*....|....*....|
gi 2278473191 499 LLQHADIAMYSAKEKGNNAVCMYDETLSQK 528
Cdd:PRK13561 365 LYSRAISAAFTARRKGKNQIQFFDPQQMEA 394
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
231-357 |
8.24e-15 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 76.04 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 231 DLVKNQERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDK--SELEAAIKKGKRCSSSS 308
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPlrELLERALAEGQPVTERE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2278473191 309 LQLRVKNNNEKDILfwyVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEI 357
Cdd:COG3852 81 VTLRRKDGEERPVD---VSVSPLRDAEGEGGVLLVLRDITERKRLEREL 126
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
322-516 |
3.00e-14 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 74.09 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 322 LFWYVTIVPIMIEGQTFGsYVMVKDITRMKQQQEEINYLAFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLN 401
Cdd:PRK10245 167 LEWWLSLPVIVIYPLLFA-WVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDID 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 402 RFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDEFAIIVHNQTEQQLL-------DLCKTLfRITEEPFVVn 474
Cdd:PRK10245 246 HFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAItamsrvhEGLNTL-RLPNAPQVT- 323
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2278473191 475 qhsfyLSLSIGIAVYPFGGINTTTLLQHADIAMYSAKEKGNN 516
Cdd:PRK10245 324 -----LRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRN 360
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
231-358 |
4.10e-14 |
|
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: 74.42 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 231 DLVKNQERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFldeDKSELEAAIKKGKrcsSSSLQ 310
Cdd:COG3829 5 ELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELI---PNSPLLEVLKTGK---PVTGV 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2278473191 311 LRVKNNNEKDILfwyVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEIN 358
Cdd:COG3829 79 IQKTGGKGKTVI---VTAIPIFEDGEVIGAVETFRDITELKRLERKLR 123
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
224-370 |
1.01e-13 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 73.47 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 224 DLINKSNDLVKNQERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKKGKR 303
Cdd:COG5809 128 ERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLK 207
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2278473191 304 CSS-SSLQLRVKNNNEKDILFwYVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEINYLafhDTVTEIG 370
Cdd:COG5809 208 DGGiAQGEVRFWTKDGRWRLL-EASGAPIKKNGEVDGIVIIFRDITERKKLEELLRKS---EKLSVVG 271
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
232-357 |
5.67e-13 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 68.90 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 232 LVKNQERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKKGKRCSSSSLQL 311
Cdd:COG2202 132 LRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYEL 211
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2278473191 312 RVKNNNEKDILFW-YVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEI 357
Cdd:COG2202 212 ELRLKDGDGRWVWvEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
236-357 |
5.58e-12 |
|
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: 62.69 E-value: 5.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 236 QERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKK--GKRCSSSSLQLRV 313
Cdd:TIGR00229 2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERrlEGEPEPVSEERRV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2278473191 314 KNNNEKdiLFW-YVTIVPIMIEGQTFGSYVMVKDITRMKQQQEEI 357
Cdd:TIGR00229 82 RRKDGS--EIWvEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
361-522 |
1.48e-11 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 66.81 E-value: 1.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 361 AFHDTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKrfrtCLS------PTV 434
Cdd:PRK11059 228 AFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELIN----LLStfvmryPGA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 435 PLARIGGDEFAIIVHNQTE-------QQLLDLCKTLfritEEPFVVNQHSFylsLSIGIAVYPfGGINTTTLLQHADIAM 507
Cdd:PRK11059 304 LLARYSRSDFAVLLPHRSLkeadslaSQLLKAVDAL----PPPKMLDRDDF---LHIGICAYR-SGQSTEQVMEEAEMAL 375
|
170
....*....|....*
gi 2278473191 508 YSAKEKGNNAVCMYD 522
Cdd:PRK11059 376 RSAQLQGGNGWFVYD 390
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
236-449 |
2.58e-11 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 63.89 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 236 QERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSE----LEAAIKKGKRCSSSSLQL 311
Cdd:COG2202 10 ERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEflelLRAALAGGGVWRGELRNR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 312 RvknnneKD--ILFWYVTIVPIMIE-GQTFGSYVMVKDITRMKQQQEEINYLA--FHDTVTEIGNRIFFQQELDRSIKRA 386
Cdd:COG2202 90 R------KDgsLFWVELSISPVRDEdGEITGFVGIARDITERKRAEEALRESEerLRLLVENAPDGIFVLDLDGRILYVN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2278473191 387 QKTQDKFGLLYIDLNRfKTINDTLGHSIGDKVLKEVAKRFRTCLSP-TVPLARIGGDEFAIIVH 449
Cdd:COG2202 164 PAAEELLGYSPEELLG-KSLLDLLHPEDRERLLELLRRLLEGGRESyELELRLKDGDGRWVWVE 226
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
232-358 |
2.99e-09 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 59.36 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 232 LVKNQERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKKGKRC-SSSSLQ 310
Cdd:COG5805 152 LQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVwQEFIIE 231
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2278473191 311 LRVKNNNEKDILFwYVTIVPIM-IEGQTFGSYVMVKDITRMKQQQEEIN 358
Cdd:COG5805 232 REIITKDGRIRYF-EAVIVPLIdTDGSVKGILVILRDITEKKEAEELMA 279
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
231-357 |
7.23e-09 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 58.06 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 231 DLVKNQERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKKGKRCSSSSLQ 310
Cdd:COG5809 9 QLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDEL 88
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2278473191 311 LRVKNNNEKDILFWYVTIVPIMIE-GQTFGSYVMVKDITRMKQQQEEI 357
Cdd:COG5809 89 EFELRHKNGKRLEFSSKLSPIFDQnGDIEGMLAISRDITERKRMEEAL 136
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
436-511 |
3.52e-08 |
|
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: 53.37 E-value: 3.52e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2278473191 436 LARIGGDEFAIIVHNQTEQQLLDLCKtlfRITEEpfVVNQHSFYLSLSIGIAvypfgginTTTLLQHADiAMYSAK 511
Cdd:COG3706 118 VARYGGEEFAILLPGTDLEGALAVAE---RIREA--VAELPSLRVTVSIGVA--------GDSLLKRAD-ALYQAR 179
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
342-529 |
9.75e-08 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 54.95 E-value: 9.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 342 VMVKDITRMKQQQEE----INYLAFHDTVTEIGNRIFFQQELDRSIKrAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDK 417
Cdd:PRK11829 209 VLVRNYNRNQQLLADayadMGRISHRFPVTELPNRSLFISLLEKEIA-SSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 418 VLKEVAKRFRTCLSPTVPLARIGGDEFAIIVHNQTEQ-QLLDLCKTLFRITEEPFVVNQHSFYLSLSIGIAVYPFGGINT 496
Cdd:PRK11829 288 LLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSfPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTA 367
|
170 180 190
....*....|....*....|....*....|...
gi 2278473191 497 TTLLQHADIAMYSAKEKGNNAVCMYDETLSQKV 529
Cdd:PRK11829 368 ESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKT 400
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
256-348 |
1.66e-07 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 49.00 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 256 NGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSE-LEAAIKKGKRCSSSSLQLRVKNNNEkdilFWY-VTIVPIMI 333
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSErLREALREGKAVREFEVVLYRKDGEP----FPVlVSLAPIRD 76
|
90
....*....|....*.
gi 2278473191 334 EGQTFGSYV-MVKDIT 348
Cdd:pfam13426 77 DGGELVGIIaILRDIT 92
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
247-348 |
7.15e-07 |
|
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 is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 47.79 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 247 PDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKK---GKRcSSSSLQLRVKNnneKDILF 323
Cdd:pfam08448 5 PDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRaleGEE-PIDFLEELLLN---GEERH 80
|
90 100
....*....|....*....|....*.
gi 2278473191 324 WYVTIVPIM-IEGQTFGSYVMVKDIT 348
Cdd:pfam08448 81 YELRLTPLRdPDGEVIGVLVISRDIT 106
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
364-474 |
7.93e-07 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 51.50 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 364 DTVTEIGNRIFFQQELDRSIKRAQKTQDKFGLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPTVPLARIGGDE 443
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
90 100 110
....*....|....*....|....*....|....
gi 2278473191 444 FAIIVHNQTE---QQLLDLCKTLFRITEEPFVVN 474
Cdd:NF040885 424 FCIILIDYEEaeaQNLIERIRQHLRTIDPDKRVS 457
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
212-355 |
1.08e-06 |
|
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: 51.12 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 212 NQLEQTVSQRTRDLINKSNDLVKNQERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDk 291
Cdd:COG5000 65 GELARAFNRMTDQLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELD- 143
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2278473191 292 seLEAAIKKGKRcSSSSLQLRVKNNNEKDILfwyVTIVPIMIEGQtfgsYVMVKDITRMKQQQE 355
Cdd:COG5000 144 --LAELLREALE-RGWQEEIELTRDGRRTLL---VRASPLRDDGY----VIVFDDITELLRAER 197
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
237-301 |
2.19e-06 |
|
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: 45.08 E-value: 2.19e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2278473191 237 ERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKKG 301
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRL 65
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
394-487 |
2.49e-06 |
|
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: 46.97 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 394 GLLYIDLNRFKTINDTLGHSIGDKVLKEVAKRFRTCLSPT-VPLARIGGDEFAIIVHNQTEQQLLDLCKTLFRITEEpfv 472
Cdd:cd07556 3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSA--- 79
|
90
....*....|....*.
gi 2278473191 473 VNQHSF-YLSLSIGIA 487
Cdd:cd07556 80 LNQSEGnPVRVRIGIH 95
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
247-347 |
1.52e-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. 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: 43.78 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 247 PDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKKGKRCSSS-SLQLRVKNNNEKDILfWY 325
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPvTLEVRLRRKDGSVIW-VL 80
|
90 100
....*....|....*....|...
gi 2278473191 326 VTIVPIMIEGQTFGSYVM-VKDI 347
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGvVRDI 103
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
237-347 |
3.70e-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: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 237 ERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAAIKK---GKRCSSSSLQLRV 313
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQallQGEESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|....*
gi 2278473191 314 KNNNEkdILFWYVTIVPIM-IEGQTFGSYVMVKDI 347
Cdd:pfam00989 81 VPDGR--PRHVEVRASPVRdAGGEILGFLGVLRDI 113
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
233-357 |
9.37e-05 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 45.11 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 233 VKNQERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFsIFLDEDKSELEAAIKKGKRCSSSSLQLR 312
Cdd:COG5805 30 IEITEELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIF-DFLEKEYHYRVKTRIERLQKGYDVVMIE 108
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2278473191 313 VKNNNEKDILFWYVTIVPIMIEGQTFGSYVmVKDITRMKQQQEEI 357
Cdd:COG5805 109 QIYCKDGELIYVEVKLFPIYNQNGQAAILA-LRDITKKKKIEEIL 152
|
|
| TyrR |
COG3283 |
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ... |
236-353 |
1.83e-03 |
|
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];
Pssm-ID: 442513 [Multi-domain] Cd Length: 514 Bit Score: 40.94 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278473191 236 QER----FKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKEC--------FSIFLDEDKSELEaaikkgkr 303
Cdd:COG3283 75 SERehleLDALLEALPDPVFSIDLKGKIELANPAALSLLGLSEEELIGQPLsellkgfnFSRWLESNEPRPQ-------- 146
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2278473191 304 csssSLQLRVKNNNekdilfWYVTIVPIMI-----EGQTFGSYVMVKDITRMKQQ 353
Cdd:COG3283 147 ----SERVVINGQD------YLADILPIYLpdeegKSILAGAVVTLKSAARLGEQ 191
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
237-297 |
7.75e-03 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 35.22 E-value: 7.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2278473191 237 ERFKSLYEYHPDPILTIDSNGIVLNINQAGSMLLGKESAALIGKECFSIFLDEDKSELEAA 297
Cdd:pfam13188 1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALELL 61
|
|
| |
