|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
132-507 |
1.04e-75 |
|
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: 251.62 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 132 LMQSLALWEPLYRSIQQMQLSESALEELVNAMVADNLQLLALMNKLTNQLETAAKRQTYLLRGLQTIIVILILLSFAMAI 211
Cdd:COG5001 36 LALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 212 NRLIRREQYFSKLMEKSSDIVIGINSATSRITFISASVKLLLQRDESYYLGHPYHRLFSQESASRISHLLLLAKKFRPLP 291
Cdd:COG5001 116 LAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 292 YNRCEVQLIRADNALIDAEMLLQLNRSEDGRTIELSADIRDITERKQLELALTEMAHKDSLTGLANRAQFSLMAEQAILQ 371
Cdd:COG5001 196 LLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALAR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 372 AQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIGGDEFVVLLSDVAQNQHLQTVGDKII 451
Cdd:COG5001 276 ARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERIL 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2535555130 452 AALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKNAVAF 507
Cdd:COG5001 356 AALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
348-506 |
5.26e-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: 199.71 E-value: 5.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 348 HKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIGG 427
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2535555130 428 DEFVVLLSDVAQNQhLQTVGDKIIAALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKNAVA 506
Cdd:cd01949 81 DEFAILLPGTDLEE-AEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
347-503 |
1.72e-54 |
|
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: 180.14 E-value: 1.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 347 AHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIG 426
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2535555130 427 GDEFVVLLSDVAQN--QHLQTVGDKIIAALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKN 503
Cdd:pfam00990 81 GDEFAILLPETSLEgaQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
345-507 |
1.05e-53 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 178.21 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 345 EMAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFR 424
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 425 IGGDEFVVLLSDVAqNQHLQTVGDKIIAALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKNA 504
Cdd:smart00267 81 LGGDEFALLLPETS-LEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 2535555130 505 VAF 507
Cdd:smart00267 160 VAV 162
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
346-505 |
4.54e-43 |
|
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: 150.18 E-value: 4.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 346 MAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRI 425
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 426 GGDEFVVLLSDVAQNQHLQTVGDKIIAALSEKILIDNCPC-QIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKNA 504
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETlTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 2535555130 505 V 505
Cdd:TIGR00254 161 V 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
325-505 |
4.53e-36 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 139.27 E-value: 4.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 325 ELSADIRDITERKQLELAL-------TEMAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICG 397
Cdd:PRK09581 263 ELLARVRTQIRRKRYQDALrnnleqsIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 398 HHVGDALLVEVAQRINQRLRASDTVFRIGGDEFVVLLSDVAQNQHLqTVGDKIIAALSEK---ILIDNCPCQIGASIGIA 474
Cdd:PRK09581 343 HDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAI-AVAERIRRKIAEEpfiISDGKERLNVTVSIGVA 421
|
170 180 190
....*....|....*....|....*....|.
gi 2535555130 475 RYPEDGENIDALLKAADEAMYRVKQSGKNAV 505
Cdd:PRK09581 422 ELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
350-502 |
3.48e-16 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 81.16 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 350 DSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIGGDE 429
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2535555130 430 FVVLLSDvAQNQHLQTVGDKIIAALsEKILIDNcpcQIGASIGIarYP-EDGENIDALLKAADEAMYRVKQSGK 502
Cdd:NF040885 424 FCIILID-YEEAEAQNLIERIRQHL-RTIDPDK---RVSFSWGA--YQmQPGDTLDDAYKAADERLYLNKKQKH 490
|
|
| PilJ |
pfam13675 |
Type IV pili methyl-accepting chemotaxis transducer N-term; This domain is found on many type ... |
42-162 |
8.26e-10 |
|
Type IV pili methyl-accepting chemotaxis transducer N-term; This domain is found on many type IV pili methyl-accepting chemotaxis transducer proteins where there is also a HAMP signature towards the C-terminus. It is a monomodular four-helix bundle and recognizes nitrate and nitrite (Matilla et al. FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433397 [Multi-domain] Cd Length: 112 Bit Score: 56.33 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 42 LSAQLEASSININIAGRQRMLSQKMTKSLLLMHYqqkQGIDTQAAHQELMDAMELFDQTLTAMRYGGETLSADSRPIRVK 121
Cdd:pfam13675 2 TLWQSEGDAAAINAAGSLRMQSQRLAKSVLLALA---GNYDLAEAFADLEESIDQFDRTLAALALGDLARGLFVPAGAIR 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2535555130 122 QFNETVIQktlmqslaLWEPLYRSIQQMQLSESALEELVNA 162
Cdd:pfam13675 79 AQLEAVQP--------LWERLRKPAEAVLAQQDTLAYLAAV 111
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
132-507 |
1.04e-75 |
|
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: 251.62 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 132 LMQSLALWEPLYRSIQQMQLSESALEELVNAMVADNLQLLALMNKLTNQLETAAKRQTYLLRGLQTIIVILILLSFAMAI 211
Cdd:COG5001 36 LALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 212 NRLIRREQYFSKLMEKSSDIVIGINSATSRITFISASVKLLLQRDESYYLGHPYHRLFSQESASRISHLLLLAKKFRPLP 291
Cdd:COG5001 116 LAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 292 YNRCEVQLIRADNALIDAEMLLQLNRSEDGRTIELSADIRDITERKQLELALTEMAHKDSLTGLANRAQFSLMAEQAILQ 371
Cdd:COG5001 196 LLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALAR 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 372 AQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIGGDEFVVLLSDVAQNQHLQTVGDKII 451
Cdd:COG5001 276 ARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERIL 355
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2535555130 452 AALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKNAVAF 507
Cdd:COG5001 356 AALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
268-507 |
5.22e-64 |
|
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: 209.45 E-value: 5.22e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 268 LFSQESASRISHLLLLAKKFRPLPYNRCEVQLIRADNALIDAEM---LLQLNRSEDGRTIELSADIRDITERKQLELALT 344
Cdd:COG2199 32 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLllsLVLELLLLLLALLLLLLALEDITELRRLEERLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 345 EMAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFR 424
Cdd:COG2199 112 RLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVAR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 425 IGGDEFVVLLSDVAQnQHLQTVGDKIIAALSEK-ILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKN 503
Cdd:COG2199 192 LGGDEFAVLLPGTDL-EEAEALAERLREALEQLpFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRN 270
|
....
gi 2535555130 504 AVAF 507
Cdd:COG2199 271 RVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
348-506 |
5.26e-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: 199.71 E-value: 5.26e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 348 HKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIGG 427
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2535555130 428 DEFVVLLSDVAQNQhLQTVGDKIIAALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKNAVA 506
Cdd:cd01949 81 DEFAILLPGTDLEE-AEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
347-503 |
1.72e-54 |
|
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: 180.14 E-value: 1.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 347 AHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIG 426
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2535555130 427 GDEFVVLLSDVAQN--QHLQTVGDKIIAALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKN 503
Cdd:pfam00990 81 GDEFAILLPETSLEgaQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
345-507 |
1.05e-53 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 178.21 E-value: 1.05e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 345 EMAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFR 424
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 425 IGGDEFVVLLSDVAqNQHLQTVGDKIIAALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKNA 504
Cdd:smart00267 81 LGGDEFALLLPETS-LEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 2535555130 505 VAF 507
Cdd:smart00267 160 VAV 162
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
346-505 |
4.54e-43 |
|
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: 150.18 E-value: 4.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 346 MAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRI 425
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 426 GGDEFVVLLSDVAQNQHLQTVGDKIIAALSEKILIDNCPC-QIGASIGIARYPEDGENIDALLKAADEAMYRVKQSGKNA 504
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETlTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 2535555130 505 V 505
Cdd:TIGR00254 161 V 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
325-505 |
4.53e-36 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 139.27 E-value: 4.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 325 ELSADIRDITERKQLELAL-------TEMAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICG 397
Cdd:PRK09581 263 ELLARVRTQIRRKRYQDALrnnleqsIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 398 HHVGDALLVEVAQRINQRLRASDTVFRIGGDEFVVLLSDVAQNQHLqTVGDKIIAALSEK---ILIDNCPCQIGASIGIA 474
Cdd:PRK09581 343 HDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAI-AVAERIRRKIAEEpfiISDGKERLNVTVSIGVA 421
|
170 180 190
....*....|....*....|....*....|.
gi 2535555130 475 RYPEDGENIDALLKAADEAMYRVKQSGKNAV 505
Cdd:PRK09581 422 ELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
332-502 |
5.08e-34 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 135.96 E-value: 5.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 332 DITERKQLELALTEMAHKDSLTGLANRAQFSLMAEQAIlqAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQR 411
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAI--NAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 412 INQRLRASDTVFRIGGDEFVVLLSDVAQNQhLQTVGDKIIAALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAAD 491
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHTSQAA-LEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
170
....*....|.
gi 2535555130 492 EAMYRVKQSGK 502
Cdd:PRK10060 379 TAMYTAKEGGR 389
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
317-505 |
8.63e-32 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 130.18 E-value: 8.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 317 RSEDGRTIELSADIRDITERKQLELALTEMAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDIC 396
Cdd:PRK09776 635 STLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSA 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 397 GHHVGDALLVEVAQRINQRLRASDTVFRIGGDEFVVLLSDVAQnQHLQTVGDKIIAALSEKILI-DNCPCQIGASIGIAR 475
Cdd:PRK09776 715 GHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNV-ESARFIATRIISAINDYHFPwEGRVYRVGASAGITL 793
|
170 180 190
....*....|....*....|....*....|
gi 2535555130 476 YPEDGENIDALLKAADEAMYRVKQSGKNAV 505
Cdd:PRK09776 794 IDANNHQASEVMSQADIACYAAKNAGRGRV 823
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
342-505 |
4.59e-27 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 114.73 E-value: 4.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 342 ALTEMAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDT 421
Cdd:PRK15426 393 SLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDV 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 422 VFRIGGDEFVVLLSDVAQNQHLQtVGDKIIAALSEK-ILI-DNCPCQIGASIGIARYPEDGE-NIDALLKAADEAMYRVK 498
Cdd:PRK15426 473 AGRVGGEEFCVVLPGASLAEAAQ-VAERIRLRINEKeILVaKSTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLYLAK 551
|
....*..
gi 2535555130 499 QSGKNAV 505
Cdd:PRK15426 552 QAGRNRV 558
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
350-507 |
7.44e-26 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 107.07 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 350 DSLTGLANRAqfSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIGGDE 429
Cdd:PRK09894 132 DVLTGLPGRR--VLDESFDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2535555130 430 FVVLLSDVAQNQHLQtVGDKIIAALSEK-ILIDNCPCQIGASIGIARYPEdGENIDALLKAADEAMYRVKQSGKNAVAF 507
Cdd:PRK09894 210 FIICLKAATDEEACR-AGERIRQLIANHaITHSDGRINITATFGVSRAFP-EETLDVVIGRADRAMYEGKQTGRNRVMF 286
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
330-503 |
2.40e-20 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 92.58 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 330 IRDITERKQLELalteMAHKDSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVA 409
Cdd:PRK10245 192 TKLAEHKRRLQV----MSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALT 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 410 QRINQRLRASDTVFRIGGDEFVVLLSDvaqnqhlqTVGDKIIAALS---EKILIDNCPC----QIGASIGIARYPEDGEN 482
Cdd:PRK10245 268 RQLQITLRGSDVIGRFGGDEFAVIMSG--------TPAESAITAMSrvhEGLNTLRLPNapqvTLRISVGVAPLNPQMSH 339
|
170 180
....*....|....*....|.
gi 2535555130 483 IDALLKAADEAMYRVKQSGKN 503
Cdd:PRK10245 340 YREWLKSADLALYKAKNAGRN 360
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
350-507 |
3.09e-20 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 94.45 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 350 DSLTGLANRAQFSLMAEQaILQAQRkssSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIGGDE 429
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDD-LVDKAV---SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2535555130 430 FVVLLSDVAQNQHLQtVGDKIIAALSEKILIDNCPCQIGASIGIARypEDGENIDALLKAADEAMYRVKQSGKNAVAF 507
Cdd:PRK11359 455 FVLVSLENDVSNITQ-IADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIRKNGGNGWQF 529
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
332-499 |
2.58e-18 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 86.98 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 332 DITERKQLELA-----LTEMAHKDSLTGLANRAQFSlMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLV 406
Cdd:PRK09966 228 DEMEEWQLRLQaknaqLLRTALHDPLTGLANRAAFR-SGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 407 EVAQRINQRLRASDTVFRIGGDEFVVLLSDVAQNQHLQtvgdKIIAALSEKI-----LIDNCPCQIGASIGIARYPEDGe 481
Cdd:PRK09966 307 EIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQ----QICSALTQIFnlpfdLHNGHQTTMTLSIGYAMTIEHA- 381
|
170
....*....|....*...
gi 2535555130 482 NIDALLKAADEAMYRVKQ 499
Cdd:PRK09966 382 SAEKLQELADHNMYQAKH 399
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
350-502 |
3.48e-16 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 81.16 E-value: 3.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 350 DSLTGLANRAQFSLMAEQAILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIGGDE 429
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2535555130 430 FVVLLSDvAQNQHLQTVGDKIIAALsEKILIDNcpcQIGASIGIarYP-EDGENIDALLKAADEAMYRVKQSGK 502
Cdd:NF040885 424 FCIILID-YEEAEAQNLIERIRQHL-RTIDPDK---RVSFSWGA--YQmQPGDTLDDAYKAADERLYLNKKQKH 490
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
210-432 |
1.83e-12 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 67.36 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 210 AINRLIRREQYFSKLMEKSSDIVIgINSATSRITFISASVKLLLQRDESYYLGHPYHRLFSQESASRisHLLLLAKKFRP 289
Cdd:COG2202 2 AEEALEESERRLRALVESSPDAII-ITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDE--FLELLRAALAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 290 LPYNRCEVQLIRADNALIDAEMLLQLNRSEDGRTIELSADIRDITERKQLELALTEMAHKDSLTGLANRAQFSLMAEQA- 368
Cdd:COG2202 79 GGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGr 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2535555130 369 ILQAQRKSSSLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTVFRIGGDEFVV 432
Cdd:COG2202 159 ILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRW 222
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
343-507 |
3.63e-11 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 65.73 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 343 LTEMAHKDSLTGLANRAQF-SLMAEQAILQAQRKSSSLamMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDT 421
Cdd:PRK11829 228 MGRISHRFPVTELPNRSLFiSLLEKEIASSTRTDHFHL--LVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDL 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 422 VFRIGGDEFVVLLSDVAQNQHLQTVGDKIIAALSEKILIDNCPCQIGASIGIARYPEDGENIDALLKAADEAMYRVKQSG 501
Cdd:PRK11829 306 LAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEG 385
|
....*.
gi 2535555130 502 KNAVAF 507
Cdd:PRK11829 386 RNQIMV 391
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
343-507 |
1.33e-10 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 63.96 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 343 LTEMAHKDSLTGLANRAQFSLMAEQAILQAQRksssLAMMFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRASDTV 422
Cdd:PRK13561 227 QSRNATRFPVSDLPNKALLMALLEQVVARKQT----TALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 423 FRIGGDEFVVLLSDVAQNQHLQTVGDKIIAALSEKILIDNCPCQIGASIGIARYpEDGENIDALLKAADEAMYRVKQSGK 502
Cdd:PRK13561 303 AQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFTARRKGK 381
|
....*
gi 2535555130 503 NAVAF 507
Cdd:PRK13561 382 NQIQF 386
|
|
| PilJ |
pfam13675 |
Type IV pili methyl-accepting chemotaxis transducer N-term; This domain is found on many type ... |
42-162 |
8.26e-10 |
|
Type IV pili methyl-accepting chemotaxis transducer N-term; This domain is found on many type IV pili methyl-accepting chemotaxis transducer proteins where there is also a HAMP signature towards the C-terminus. It is a monomodular four-helix bundle and recognizes nitrate and nitrite (Matilla et al. FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433397 [Multi-domain] Cd Length: 112 Bit Score: 56.33 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 42 LSAQLEASSININIAGRQRMLSQKMTKSLLLMHYqqkQGIDTQAAHQELMDAMELFDQTLTAMRYGGETLSADSRPIRVK 121
Cdd:pfam13675 2 TLWQSEGDAAAINAAGSLRMQSQRLAKSVLLALA---GNYDLAEAFADLEESIDQFDRTLAALALGDLARGLFVPAGAIR 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2535555130 122 QFNETVIQktlmqslaLWEPLYRSIQQMQLSESALEELVNA 162
Cdd:pfam13675 79 AQLEAVQP--------LWERLRKPAEAVLAQQDTLAYLAAV 111
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
382-456 |
1.17e-08 |
|
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: 53.51 E-value: 1.17e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2535555130 382 MFIDLDNFKSVNDICGHHVGDALLVEVAQRINQRLRAS-DTVFRIGGDEFVVLLSDVaQNQHLQTVGDKIIAALSE 456
Cdd:cd07556 5 LFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVSGLD-HPAAAVAFAEDMREAVSA 79
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
218-353 |
1.34e-07 |
|
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: 53.83 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 218 EQYFSKLMEKSSDIVIGINsATSRITFISASVKLLLQRDESYYLGHPYHRLFSQESASRISHLLLLAKKFRPlpYNRCEV 297
Cdd:COG5809 140 EEKFRLIFNHSPDGIIVTD-LDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGG--IAQGEV 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2535555130 298 QLIRADNALIDAEM-LLQLNrsEDGRTIELSADIRDITERKQLELALTemaHKDSLT 353
Cdd:COG5809 217 RFWTKDGRWRLLEAsGAPIK--KNGEVDGIVIIFRDITERKKLEELLR---KSEKLS 268
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
407-496 |
4.29e-07 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 49.91 E-value: 4.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 407 EVAQRInqrlrasDTVFRIGGDEFVVLLSDVAQNQhLQTVGDKIIAALSEKIlidncPCQIGASIGIArypedgenIDAL 486
Cdd:COG3706 110 ELLARV-------DLVARYGGEEFAILLPGTDLEG-ALAVAERIREAVAELP-----SLRVTVSIGVA--------GDSL 168
|
90
....*....|
gi 2535555130 487 LKAADeAMYR 496
Cdd:COG3706 169 LKRAD-ALYQ 177
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
213-356 |
1.33e-06 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 50.62 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 213 RLIRREQYFSKLMEKSSDIVIGINsATSRITFISASVKLLLQRDESYYLGHPYHRLFSQESasRISHLLLLAKKfRPLPY 292
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLD-ADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS--PLRELLERALA-EGQPV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2535555130 293 NRCEVQLIRADNALIDAEM---LLQLNRSEDGRTIElsadIRDITERKQLELALTEMAHKDSLTGLA 356
Cdd:COG3852 77 TEREVTLRRKDGEERPVDVsvsPLRDAEGEGGVLLV----LRDITERKRLERELRRAEKLAAVGELA 139
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
196-352 |
4.18e-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: 45.88 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 196 QTIIVILILLSFAMAINRLIRR-EQYFSKLMEKSSDIVIGINSaTSRITFISASVKLLLQRDESYYLGHPYHRLFSQESA 274
Cdd:COG5805 133 QAAILALRDITKKKKIEEILQEqEERLQTLIENSPDLICVIDT-DGRILFINESIERLFGAPREELIGKNLLELLHPCDK 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2535555130 275 SRISHLL-LLAKKFRPLPYNRcevQLIRADNALIDAEMLLQLNRSEDGRTIELSADIRDITERKQLElalTEMAHKDSL 352
Cdd:COG5805 212 EEFKERIeSITEVWQEFIIER---EIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAE---ELMARSEKL 284
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
213-343 |
5.62e-05 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 45.02 E-value: 5.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 213 RLIRREQYFSKLMEKSSDIVIGINsATSRITFISASVKLLLQRDESYYLGHPYHRLFSQESASRISHLLLLAKKFRPLPY 292
Cdd:COG2202 131 ALRESEERLRLLVENAPDGIFVLD-LDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESY 209
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2535555130 293 nRCEVQLIRADNALIDAEMLLQLNRSEDGRTIELSAdIRDITERKQLELAL 343
Cdd:COG2202 210 -ELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGI-VRDITERKRAEEAL 258
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
241-335 |
1.34e-04 |
|
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: 40.91 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 241 RITFISASVKLLLQRDESYYLGHPYHRLFS-QESASRISHLLLLAKKFRPLpynrcEVQLIRADNALIDAEMLLQLNRSE 319
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLGKSITDLFAePEDSERLREALREGKAVREF-----EVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 2535555130 320 DGRTIELSADIRDITE 335
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
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|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
228-333 |
6.65e-03 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 36.46 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2535555130 228 SSDIVIGINsATSRITFISASVKLLLQRDESYYLGHPYHRLFSQEsaSRISHLLLLAKKFRPLPYNRCEVQLIRADNALI 307
Cdd:cd00130 1 LPDGVIVLD-LDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPE--DREELRERLENLLSGGEPVTLEVRLRRKDGSVI 77
|
90 100
....*....|....*....|....*.
gi 2535555130 308 DAEMLLQLNRSEDGRTIELSADIRDI 333
Cdd:cd00130 78 WVLVSLTPIRDEGGEVIGLLGVVRDI 103
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| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
295-336 |
9.42e-03 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 34.08 E-value: 9.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2535555130 295 CEVQLIRADNALIDAEMLLQLNRSEDGRTIELSADIRDITER 336
Cdd:smart00086 2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
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