|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
10-410 |
6.35e-91 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 281.12 E-value: 6.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 10 SNPSLRRVLYRAHLGVALVAVFTAGLAVTLVGLLTLRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESLALIASSEEV 89
Cdd:PRK09966 9 KRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQQGQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 90 SSAIVYDRQGQTLASWHRESTGPLHLLEQQLAHWLLSAPTEQPILHDGQKIGSVEVKGSGGSLLRFLLTGFAGMVLCLLL 169
Cdd:PRK09966 89 STAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLAVLTGCILL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 170 TALGAFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQDENASLAHQA 249
Cdd:PRK09966 169 ASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRTA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 250 HHDSLTSLPNRAFFEGRLSRALRDaNEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIR--GQLRESDLvaRL 327
Cdd:PRK09966 249 LHDPLTGLANRAAFRSGINTLMNN-SDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAefGGLRHKAY--RL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 328 GGDEFAVLLAPLASGADALRIADNIIASMQAPIRLSDGSTVSTSLTIGIALYPEHAdTPAALLHDADMAMYIAKRQaRGS 407
Cdd:PRK09966 326 GGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHA-SAEKLQELADHNMYQAKHQ-RAE 403
|
...
gi 15596317 408 RRL 410
Cdd:PRK09966 404 KLV 406
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
14-410 |
6.01e-69 |
|
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: 231.20 E-value: 6.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 14 LRRVLYRAHLGVALVAVFTAGLAVTLVGLLTLRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESLALIASSEEVSSAI 93
Cdd:COG5001 21 LALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 94 VYDRQGQTLASWHRESTGPLHLLEQQLAHWLLSAPTEQPILHDGQKIGSVEVKGSGGSLLRFLLTGFAGMVLCLLLTALG 173
Cdd:COG5001 101 VLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 174 AFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQdenasLAHQAHHDS 253
Cdd:COG5001 181 LLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEER-----LRHLAYHDP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 254 LTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLGGDEFA 333
Cdd:COG5001 256 LTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFA 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596317 334 VLLAPLASGADALRIADNIIASMQAPIRLsDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARGSRRL 410
Cdd:COG5001 336 VLLPDLDDPEDAEAVAERILAALAEPFEL-DGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
250-406 |
2.34e-59 |
|
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: 190.85 E-value: 2.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 250 HHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLGG 329
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596317 330 DEFAVLLaPLASGADALRIADNIIASMQAPIRLsDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARG 406
Cdd:cd01949 81 DEFAILL-PGTDLEEAEALAERLREAIEEPFFI-DGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRN 155
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
249-407 |
1.58e-53 |
|
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: 175.90 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 249 AHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLG 328
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 329 GDEFAVLL--APLASGADALRIADNIIASMQAPIRLSdGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARG 406
Cdd:pfam00990 81 GDEFAILLpeTSLEGAQELAERIRRLLAKLKIPHTVS-GLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
.
gi 15596317 407 S 407
Cdd:pfam00990 160 R 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
247-407 |
7.88e-51 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 168.97 E-value: 7.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 247 HQAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVAR 326
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 327 LGGDEFAVLLaPLASGADALRIADNIIASMQAPIrLSDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARG 406
Cdd:smart00267 81 LGGDEFALLL-PETSLEEAIALAERILQQLREPI-IIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRN 158
|
.
gi 15596317 407 S 407
Cdd:smart00267 159 Q 159
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
248-412 |
5.81e-46 |
|
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: 156.34 E-value: 5.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 248 QAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARL 327
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 328 GGDEFAVLLaPLASGADALRIADNI---IASMqaPIRLSDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQA 404
Cdd:TIGR00254 81 GGEEFVVIL-PGTPLEDALSKAERLrdaINSK--PIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAG 157
|
....*...
gi 15596317 405 RGSRRLAE 412
Cdd:TIGR00254 158 RNRVVVAD 165
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
10-410 |
6.35e-91 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 281.12 E-value: 6.35e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 10 SNPSLRRVLYRAHLGVALVAVFTAGLAVTLVGLLTLRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESLALIASSEEV 89
Cdd:PRK09966 9 KRPTFKRALRNISMTSIFITMMLIWLLLSVTSVLTLKQYAQKNLALTAATMTYSLEAAVVFADGPAATETLAALGQQGQF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 90 SSAIVYDRQGQTLASWHRESTGPLHLLEQQLAHWLLSAPTEQPILHDGQKIGSVEVKGSGGSLLRFLLTGFAGMVLCLLL 169
Cdd:PRK09966 89 STAEVRDKQQNILASWHYTRKDPGDTFSNFISHWLFPAPIIQPIRHNGETIGEVRLTARDSSISHFIWFSLAVLTGCILL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 170 TALGAFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQDENASLAHQA 249
Cdd:PRK09966 169 ASGIAITLTRHLHNGLVEALKNITDVVHDVRSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQLRLQAKNAQLLRTA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 250 HHDSLTSLPNRAFFEGRLSRALRDaNEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIR--GQLRESDLvaRL 327
Cdd:PRK09966 249 LHDPLTGLANRAAFRSGINTLMNN-SDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAefGGLRHKAY--RL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 328 GGDEFAVLLAPLASGADALRIADNIIASMQAPIRLSDGSTVSTSLTIGIALYPEHAdTPAALLHDADMAMYIAKRQaRGS 407
Cdd:PRK09966 326 GGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTTMTLSIGYAMTIEHA-SAEKLQELADHNMYQAKHQ-RAE 403
|
...
gi 15596317 408 RRL 410
Cdd:PRK09966 404 KLV 406
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
14-410 |
6.01e-69 |
|
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: 231.20 E-value: 6.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 14 LRRVLYRAHLGVALVAVFTAGLAVTLVGLLTLRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESLALIASSEEVSSAI 93
Cdd:COG5001 21 LALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 94 VYDRQGQTLASWHRESTGPLHLLEQQLAHWLLSAPTEQPILHDGQKIGSVEVKGSGGSLLRFLLTGFAGMVLCLLLTALG 173
Cdd:COG5001 101 VLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 174 AFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQdenasLAHQAHHDS 253
Cdd:COG5001 181 LLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEER-----LRHLAYHDP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 254 LTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLGGDEFA 333
Cdd:COG5001 256 LTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFA 335
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596317 334 VLLAPLASGADALRIADNIIASMQAPIRLsDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARGSRRL 410
Cdd:COG5001 336 VLLPDLDDPEDAEAVAERILAALAEPFEL-DGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRF 411
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
250-406 |
2.34e-59 |
|
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: 190.85 E-value: 2.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 250 HHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLGG 329
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15596317 330 DEFAVLLaPLASGADALRIADNIIASMQAPIRLsDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARG 406
Cdd:cd01949 81 DEFAILL-PGTDLEEAEALAERLREAIEEPFFI-DGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRN 155
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
152-411 |
8.90e-59 |
|
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: 193.66 E-value: 8.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 152 LLRFLLTGFAGMVLCLLLTALGAFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGEDFNALLDEL 231
Cdd:COG2199 18 LLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLAL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 232 ESwQARLQDENASLAHQAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIA 311
Cdd:COG2199 98 ED-ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 312 MRIRGQLRESDLVARLGGDEFAVLLaPLASGADALRIADNIIASMQAPIRLSDGSTVSTSLTIGIALYPEHADTPAALLH 391
Cdd:COG2199 177 RRLRASLRESDLVARLGGDEFAVLL-PGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGDSAEELLR 255
|
250 260
....*....|....*....|
gi 15596317 392 DADMAMYIAKRQARGSRRLA 411
Cdd:COG2199 256 RADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
249-407 |
1.58e-53 |
|
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: 175.90 E-value: 1.58e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 249 AHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLG 328
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 329 GDEFAVLL--APLASGADALRIADNIIASMQAPIRLSdGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARG 406
Cdd:pfam00990 81 GDEFAILLpeTSLEGAQELAERIRRLLAKLKIPHTVS-GLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
.
gi 15596317 407 S 407
Cdd:pfam00990 160 R 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
247-407 |
7.88e-51 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 168.97 E-value: 7.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 247 HQAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVAR 326
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 327 LGGDEFAVLLaPLASGADALRIADNIIASMQAPIrLSDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQARG 406
Cdd:smart00267 81 LGGDEFALLL-PETSLEEAIALAERILQQLREPI-IIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRN 158
|
.
gi 15596317 407 S 407
Cdd:smart00267 159 Q 159
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
248-412 |
5.81e-46 |
|
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: 156.34 E-value: 5.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 248 QAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARL 327
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 328 GGDEFAVLLaPLASGADALRIADNI---IASMqaPIRLSDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQA 404
Cdd:TIGR00254 81 GGEEFVVIL-PGTPLEDALSKAERLrdaINSK--PIEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAG 157
|
....*...
gi 15596317 405 RGSRRLAE 412
Cdd:TIGR00254 158 RNRVVVAD 165
|
|
| CHASE8 |
pfam17152 |
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine ... |
45-145 |
4.28e-41 |
|
Periplasmic sensor domain; CHASE8 is a conserved periplasmic sensor domain found in histidine kinases, diguanylate cyclases/phosphodiesterases and methyl-accepting chemotaxis proteins, including the diguanylate cyclase DgcN (YfiN) that regulates biofilm formation and motility in Escherichia coli. In Pseudomonas aeruginosa, CHASE8 is the sensor domain in the diguanylate cyclase TpbB that regulates biofilm formation by controlling the levels of extracellular DNA.
Pssm-ID: 435752 Cd Length: 102 Bit Score: 141.24 E-value: 4.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 45 LRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESLALIASSEEVSSAIVYDRQGQTLASWHRESTGPLHLLEQQLAHWL 124
Cdd:pfam17152 1 LRRYAQQNLELLARSIAYNVEAALVFGDPAAARETLAALGAQPQIASAAVYDAQGRLFASYARPGTDPPEPLEALLARWL 80
|
90 100
....*....|....*....|.
gi 15596317 125 LSAPTEQPILHDGQKIGSVEV 145
Cdd:pfam17152 81 LPAPVLQPIVHDGERIGSVVL 101
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
245-435 |
3.77e-34 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 135.57 E-value: 3.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 245 LAHQAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLV 324
Cdd:PRK09776 661 LSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVL 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 325 ARLGGDEFAVLLaPLASGADALRIADNIIASMQAPIRLSDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKR-- 402
Cdd:PRK09776 741 ARLGGDEFGLLL-PDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNag 819
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15596317 403 ------------QARGSRRLAELNDP-RILQEEKEIDSATPEAPPK 435
Cdd:PRK09776 820 rgrvtvyepqqaAAHSEHRALSLAEQwRMIKENQLMMLAHGVASPR 865
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
252-405 |
1.03e-33 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 131.56 E-value: 1.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 252 DSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLGGDE 331
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596317 332 FAVLLaPLASGADALRIADNI---IASMqaPIRLSDGST-VSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQAR 405
Cdd:PRK09581 375 FVVVM-PDTDIEDAIAVAERIrrkIAEE--PFIISDGKErLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGR 449
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
245-414 |
1.02e-31 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 127.88 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 245 LAHQAHHDSLTSLPNRAFFEGRLSRALRDANEHreQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLV 324
Cdd:PRK10060 233 LRILANTDSITGLPNRNAIQELIDHAINAADNN--QVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTL 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 325 ARLGGDEFAVlLAPLASGADALRIADNIIASMQAPIRLsdG-STVSTSLTIGIALYPEHADTPAALLHDADMAMYIAKRQ 403
Cdd:PRK10060 311 ARLGGDEFLV-LASHTSQAALEAMASRILTRLRLPFRI--GlIEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEG 387
|
170
....*....|...
gi 15596317 404 ARGSRRL--AELN 414
Cdd:PRK10060 388 GRGQFCVfsPEMN 400
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
244-405 |
7.44e-29 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 118.96 E-value: 7.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 244 SLAHQAHHDSLTSLPNR-AFFEgRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESD 322
Cdd:PRK15426 393 SLQWQAWHDPLTRLYNRgALFE-KARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 323 LVARLGGDEFAVLLaPLASGADALRIADNIIASMQA-PIRLSDGSTVSTSLTIGIALYPEHAD-TPAALLHDADMAMYIA 400
Cdd:PRK15426 472 VAGRVGGEEFCVVL-PGASLAEAAQVAERIRLRINEkEILVAKSTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLYLA 550
|
....*
gi 15596317 401 KRQAR 405
Cdd:PRK15426 551 KQAGR 555
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
223-405 |
1.51e-20 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 91.28 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 223 DFNALLDELESWQARLQD-ENASLAHQAHHDSLTSLPNRAFFEGRLSRALRDANEhrEQLAVLFIDSDRFKEINDRLGHA 301
Cdd:PRK09894 102 HFDAFQEGLLSFTAALTDyKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNREP--QNLYLALLDIDRFKLVNDTYGHL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 302 AGDTVLVNIAMRIRGQLRESDLVARLGGDEFAVLLaPLASGADALRIADNI-IASMQAPIRLSDGS---TVSTSLTIGIA 377
Cdd:PRK09894 180 IGDVVLRTLATYLASWTRDYETVYRYGGEEFIICL-KAATDEEACRAGERIrQLIANHAITHSDGRiniTATFGVSRAFP 258
|
170 180
....*....|....*....|....*...
gi 15596317 378 LypehaDTPAALLHDADMAMYIAKRQAR 405
Cdd:PRK09894 259 E-----ETLDVVIGRADRAMYEGKQTGR 281
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
252-401 |
9.91e-19 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 88.67 E-value: 9.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 252 DSLTSLPNRaffeGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDLVARLGGDE 331
Cdd:PRK11359 379 DPLTGLPNR----NNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15596317 332 FaVLLAPLASGADALRIADNIIASMQAPIRLsDGSTVSTSLTIGIALypEHADTPAALLHDADMAM-YIAK 401
Cdd:PRK11359 455 F-VLVSLENDVSNITQIADELRNVVSKPIMI-DDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMdYIRK 521
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
152-421 |
4.21e-18 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 86.92 E-value: 4.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 152 LLRFLLTGFAGMVLCLLLTALG-AFYLSRRLVRGIVGPLDQLAKVAHTVRRERDFEKRVPEAGIAELSQLGedfnALLDE 230
Cdd:PRK11829 138 MYQFILSALSAMLSTYLLLALVlSVSIAWCINRLIIHPLRAMAKELEDIGDHGVLHHQLTLPAHHQDDELG----VLVRN 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 231 LESWQARLQDENASLAHQAHHDSLTSLPNRAFFEGRLSRALRDANEHrEQLAVLFIDSDRFKEINDRLGHAAGDTVLVNI 310
Cdd:PRK11829 214 YNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRT-DHFHLLVIGIETLQEVSGAMSEAQHQQLLLTI 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 311 AMRIRGQLRESDLVARLGGDEFAVLLAPLASGADALRIADNIIASMQAPIRLsDGSTVSTSLTIGIALYPEHADTPAALL 390
Cdd:PRK11829 293 VQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFF-DEITLRPSASIGITRYQAQQDTAESMM 371
|
250 260 270
....*....|....*....|....*....|....*.
gi 15596317 391 HDADMAMYIAKRQARG-----SRRLAELNDPRILQE 421
Cdd:PRK11829 372 RNASTAMMAAHHEGRNqimvfEPHLIEKTHKRLTQE 407
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
237-411 |
1.07e-17 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 84.11 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 237 RLQDENASLAHQAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRG 316
Cdd:PRK10245 193 KLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQI 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 317 QLRESDLVARLGGDEFAVLLaplaSGADalriADNIIASMQ------APIRLSDGSTVSTSLTIGIA-LYPEHADTpAAL 389
Cdd:PRK10245 273 TLRGSDVIGRFGGDEFAVIM----SGTP----AESAITAMSrvheglNTLRLPNAPQVTLRISVGVApLNPQMSHY-REW 343
|
170 180
....*....|....*....|..
gi 15596317 390 LHDADMAMYIAKRQARGSRRLA 411
Cdd:PRK10245 344 LKSADLALYKAKNAGRNRTEVA 365
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
280-401 |
9.08e-11 |
|
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: 59.29 E-value: 9.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 280 QLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRES-DLVARLGGDEFAVLLaPLASGADALRIADNIIASMQa 358
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgDLKIKTIGDEFMVVS-GLDHPAAAVAFAEDMREAVS- 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15596317 359 piRLSDGSTVSTSLTIGIALYPEHA---------DTPAALLHDADMAMYIAK 401
Cdd:cd07556 79 --ALNQSEGNPVRVRIGIHTGPVVVgvigsrpqyDVWGALVNLASRMESQAK 128
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
24-403 |
1.65e-10 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 63.19 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 24 GVALVAVFTAgLAVTLVGLLTLRAYaDPNQQL--IARSISYTVEAAVVFGDAQAAEESLALIASSEEVSSA-IVYDRQGQ 100
Cdd:PRK13561 6 AVVLVFVFIF-CTVLLFHLVQQNRY-NTATQLesIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRAdVVLPNQFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 101 TL-ASWHRESTGP-----LHLLEQQLAHWLLSapTEQPIlhDGQKIGSVEVKGSGGSLLRFLLTGFAGMV-LCLLLTALG 173
Cdd:PRK13561 84 ALrKSFIPERPVPvmvtrLFELPVQISLPVYS--LERPA--NPQPLAYLVLQADSFRMYKFVMSALSTLVtIYLLLSLIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 174 AFYLSRRLVRGIVGPLDQLAkvahtvrreRDFEKRVPEAGIA---ELSQLGEDfnallDEL----ESW---QARLQDENA 243
Cdd:PRK13561 160 TVAISWCINRLIVHPLRNIA---------RELNDIPPQELVGhqlALPRLHQD-----DEIgmlvRSYnlnQQLLQRQYE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 244 SLAHQAHHDSLTSLPNRAFFEGRLSRALRDanehREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRESDL 323
Cdd:PRK13561 226 EQSRNATRFPVSDLPNKALLMALLEQVVAR----KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMV 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 324 VARLGGDEFAVLLAPLASGADALRIADNIIASMQAPIRLsDGSTVSTSLTIGIALYpeHADTPA-ALLHDADMAMYIAKR 402
Cdd:PRK13561 302 LAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPI-QRIQLRPSCSIGIAMF--YGDLTAeQLYSRAISAAFTARR 378
|
.
gi 15596317 403 Q 403
Cdd:PRK13561 379 K 379
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
155-245 |
6.89e-09 |
|
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: 57.66 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 155 FLLTGFAGMVLCLLLTALGAFYLSRRLVRgivgPLDQLAKVAHTVRrERDFEKRVPEAGIAELSQLGEDFNALLDELESW 234
Cdd:COG5000 7 FLLLLLLIALLLLLLALWLALLLARRLTR----PLRRLAEATRAVA-AGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQ 81
|
90
....*....|.
gi 15596317 235 QARLQDENASL 245
Cdd:COG5000 82 REELEERRRYL 92
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
322-401 |
6.68e-06 |
|
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: 46.44 E-value: 6.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 322 DLVARLGGDEFAVLLaPLASGADALRIADNIIASMQAPIRLSdgSTVStsltIGIAlypehadtPAALLHDADmAMYIAK 401
Cdd:COG3706 116 DLVARYGGEEFAILL-PGTDLEGALAVAERIREAVAELPSLR--VTVS----IGVA--------GDSLLKRAD-ALYQAR 179
|
|
| HAMP |
pfam00672 |
HAMP domain; |
180-232 |
2.04e-05 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 41.84 E-value: 2.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15596317 180 RLVRGIVGPLDQLAKVAHTVRrERDFEKRVPEAGIAELSQLGEDFNALLDELE 232
Cdd:pfam00672 1 LLARRILRPLRRLAEAARRIA-SGDLDVRLPVSGRDEIGELARAFNQMAERLR 52
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
248-396 |
2.17e-05 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 46.78 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 248 QAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLV-------NIAMRirgqlRE 320
Cdd:PRK11059 227 NAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFelinllsTFVMR-----YP 301
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15596317 321 SDLVARLGGDEFAVLLaPLASGADALRIADNIIASMQA--PIRLSDGSTVstsLTIGIALYPEhADTPAALLHDADMA 396
Cdd:PRK11059 302 GALLARYSRSDFAVLL-PHRSLKEADSLASQLLKAVDAlpPPKMLDRDDF---LHIGICAYRS-GQSTEQVMEEAEMA 374
|
|
| PRK10600 |
PRK10600 |
nitrate/nitrite two-component system sensor histidine kinase NarX; |
164-248 |
2.18e-05 |
|
nitrate/nitrite two-component system sensor histidine kinase NarX;
Pssm-ID: 182581 [Multi-domain] Cd Length: 569 Bit Score: 46.59 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 164 VLCLLLTALGAFYLSRRLVRgivgPLDQLAKVAHTVRReRDFEKRVPEAGIAELSQLGEDFNALLDEL-ESW---QARLQ 239
Cdd:PRK10600 132 VFMALLLVFTIIWLRRRLLQ----PWRQLLSMANAVSH-RDFTQRANISGRDEMAMLGTALNNMSAELaESYavlEQRVQ 206
|
....*....
gi 15596317 240 DENASLAHQ 248
Cdd:PRK10600 207 EKTAGLEQK 215
|
|
| HAMP |
smart00304 |
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain; |
183-232 |
3.84e-05 |
|
HAMP (Histidine kinases, Adenylyl cyclases, Methyl binding proteins, Phosphatases) domain;
Pssm-ID: 197640 [Multi-domain] Cd Length: 53 Bit Score: 41.08 E-value: 3.84e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 15596317 183 RGIVGPLDQLAKVAHTVRrERDFEKRVPEAGIAELSQLGEDFNALLDELE 232
Cdd:smart00304 1 RRLLRPLRRLAEAAQRIA-DGDLTVRLPVDGRDEIGELARAFNEMADRLE 49
|
|
| cztS_silS_copS |
TIGR01386 |
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ... |
152-282 |
4.68e-05 |
|
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.
Pssm-ID: 273593 [Multi-domain] Cd Length: 457 Bit Score: 45.46 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 152 LLRFLLTGFAGMVLCLLLTALGAFYLSRRLVRgivgPLDQLAKVAHTVRRERdFEKRVPEAGI-AELSQLGEDFNALLDE 230
Cdd:TIGR01386 159 LDALRKWLILIAVLLVLLTALLGWWITRLGLE----PLRRLSAVAARISPES-LDQRLDPSRApAELRELAQSFNAMLGR 233
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 15596317 231 LESWQARLQDENASLAHQAhHDSLTSLPNRAffEGRLSRAlRDANEHREQLA 282
Cdd:TIGR01386 234 LEDAFQRLSQFSADLAHEL-RTPLTNLLGQT--QVALSQP-RTGEEYREVLE 281
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
163-426 |
8.57e-05 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 44.87 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 163 MVLCLLLTALGAFYLSRRLVRGIVGPLDQLAKVAHTVRReRDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQDEN 242
Cdd:COG3850 120 ALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIAR-GDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 243 ASLAHQAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHA--AGDTVLVNIAMRIRGQLRE 320
Cdd:COG3850 199 ELEAELELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNilAGLLELLLALLLLLLASAL 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 321 SDLVARLGGDEFAVLLAPLASGADALRIADNIIASMQAPIRLSDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIA 400
Cdd:COG3850 279 LLLELELLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAA 358
|
250 260
....*....|....*....|....*.
gi 15596317 401 KRQARGSRRLAELNDPRILQEEKEID 426
Cdd:COG3850 359 GAALAAAAAAAGLARALAQAGADAAE 384
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
186-231 |
1.73e-04 |
|
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.
Pssm-ID: 381743 [Multi-domain] Cd Length: 45 Bit Score: 38.96 E-value: 1.73e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 15596317 186 VGPLDQLAKVAHTVRrERDFEKRVPEAGIAELSQLGEDFNALLDEL 231
Cdd:cd06225 1 TRPLRRLTEAARRIA-EGDLDVRVPVRSKDEIGELARAFNQMAERL 45
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
1-428 |
8.17e-04 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 41.64 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 1 MNRRRRYTGSNPSLRRVLYRAHLGVALVAVFTAGLAVTLVGLLTLRAYADPNQQLIARSISYTVEAAVVFGDAQAAEESL 80
Cdd:COG2770 56 LLLLLLAALVLLALLLAAALLLLLLLLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 81 ALIASSEEVSSAIVYDRQGQTLASWHRESTGPLHLLEQQLAHWLLSAPTEQPILHDGQKIGSVEVKGSGGSLLRFLLTGF 160
Cdd:COG2770 136 LALALLALLLGLAAARLLLAALLALAAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALAALLLLL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 161 AGMVLCLLLTALGAFYLSRRLVRgivgPLDQLAKVAHTVRReRDFEKRVPEAGIAELSQLGEDFNALLDELESWQARLQD 240
Cdd:COG2770 216 LLALLALLLALLLALLLARRITR----PLRRLAEAARRIAA-GDLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEE 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 241 ENASLAHQAHHDSLTSLPNRAFFEGRLSRALRDANEHREQLAVLFIDSDRFKEINDRLGHAAGDTVLVNIAMRIRGQLRE 320
Cdd:COG2770 291 EEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLE 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15596317 321 SDLVARLGGDEFAVLLAPLASGADALRIADNIIASMQAPIRLSDGSTVSTSLTIGIALYPEHADTPAALLHDADMAMYIA 400
Cdd:COG2770 371 AELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAA 450
|
410 420
....*....|....*....|....*...
gi 15596317 401 KRQARGSRRLAELNDPRILQEEKEIDSA 428
Cdd:COG2770 451 AEAEGGLAELEAEELVAAAEALLLLAAL 478
|
|
| |
