|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
77-494 |
6.30e-109 |
|
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: 338.29 E-value: 6.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 77 DSVTGLHSPSVFYRYLNKRLKNSQASDHYV-LFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSDG 155
Cdd:COG5001 254 DPLTGLPNRRLFLDRLEQALARARRSGRRLaLLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 156 FACLVK-LNHTEHIESYIALVHRRF---YQCAyRYDIHATCCIGAALFPSDGNNAKQLMASATHALTEAKKS-KDTIEFH 230
Cdd:COG5001 334 FAVLLPdLDDPEDAEAVAERILAALaepFELD-GHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAgRNRYRFF 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 231 DPKLTELERQRQEMVQELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTL 310
Cdd:COG5001 413 DPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEW 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 311 VLEKTASQLRANGLLGNELNSVSVNISAVELNSVDDMNHLNEYLRK---DPEfarLLCLEITETAILKDIDQCAIAVQKL 387
Cdd:COG5001 493 VLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAEtglPPS---RLELEITESALLEDPEEALETLRAL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 388 KKQGVSFSIDDFGVGYTSFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKT 467
Cdd:COG5001 570 RALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRE 649
|
410 420
....*....|....*....|....*..
gi 515648682 468 LNCEQAQGYYLGYPMPYKQLKESLTSE 494
Cdd:COG5001 650 LGCDYAQGYLFSRPLPAEELEALLRAR 676
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
246-483 |
1.92e-80 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 250.54 E-value: 1.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 246 QELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTLVLEKTASQLRANGLL 325
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 326 GNELnSVSVNISAVELNSVDDMNHLNEYLRKDPEFARLLCLEITETAILKDIDQCAIAVQKLKKQGVSFSIDDFGVGYTS 405
Cdd:cd01948 81 GPDL-RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515648682 406 FGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYPMP 483
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
245-481 |
1.23e-70 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 224.89 E-value: 1.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 245 VQELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTLVLEKTASQLRANGL 324
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 325 LGNElnSVSVNISAVELNSVDDMNHLNEYLRKDPEFARLLCLEITETAILKDIDQCAIAVQKLKKQGVSFSIDDFGVGYT 404
Cdd:pfam00563 81 GPDI--KLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515648682 405 SFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYP 481
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
246-483 |
2.99e-63 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 205.91 E-value: 2.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 246 QELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTLVLEKTASQLRANGLL 325
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 326 GNELNSVSVNISAVELNSVDDMNHLNEYLRKDPEFARLLCLEITETAILKDIDQCAIAVQKLKKQGVSFSIDDFGVGYTS 405
Cdd:smart00052 82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515648682 406 FGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYPMP 483
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
64-483 |
2.59e-50 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 183.82 E-value: 2.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 64 QKNNRDLEDANDLDSVTGLHSPSVFYRYLNKRLKNSQASdhyVLFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIE 143
Cdd:PRK11359 366 EKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSP---VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 144 HQPLSSRVHSDGFAcLVKLNHTEHIESYIALVHRRFYQCAYRYDIHA---TCCIGAALfpSDGNNAKQLMASATHALTEA 220
Cdd:PRK11359 443 PDQYLCRIEGTQFV-LVSLENDVSNITQIADELRNVVSKPIMIDDKPfplTLSIGISY--DVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 221 KKSK-DTIEFHDPKLTELERQRQEMVQELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAE 299
Cdd:PRK11359 520 RKNGgNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 300 ENYFCRDLTTLVLEKTASQLRANGLLGNELNSVSVNISAVELNSVDDMNHLNEYLRkdpEFA---RLLCLEITETAILKD 376
Cdd:PRK11359 600 EIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQ---AWGidgHQLTVEITESMMMEH 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 377 IDQCAIAVQKLKKQGVSFSIDDFGVGYTSFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGV 456
Cdd:PRK11359 677 DTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGV 756
|
410 420
....*....|....*....|....*..
gi 515648682 457 ENAQQLSILKTLNCEQAQGYYLGYPMP 483
Cdd:PRK11359 757 ETKEQFEMLRKIHCRVIQGYFFSRPLP 783
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
77-224 |
5.33e-08 |
|
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: 52.34 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 77 DSVTGLHSPSVFYRYLNKRLKNSQASDHYV-LFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSDG 155
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 156 FACLVK---LNHT--------EHIESYIALVhrrfyqcAYRYDIHATCCIGAALFPSDGNNAKQLMASATHALTEAKKSK 224
Cdd:TIGR00254 85 FVVILPgtpLEDAlskaerlrDAINSKPIEV-------AGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAG 157
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
77-494 |
6.30e-109 |
|
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: 338.29 E-value: 6.30e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 77 DSVTGLHSPSVFYRYLNKRLKNSQASDHYV-LFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSDG 155
Cdd:COG5001 254 DPLTGLPNRRLFLDRLEQALARARRSGRRLaLLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 156 FACLVK-LNHTEHIESYIALVHRRF---YQCAyRYDIHATCCIGAALFPSDGNNAKQLMASATHALTEAKKS-KDTIEFH 230
Cdd:COG5001 334 FAVLLPdLDDPEDAEAVAERILAALaepFELD-GHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAgRNRYRFF 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 231 DPKLTELERQRQEMVQELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTL 310
Cdd:COG5001 413 DPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEW 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 311 VLEKTASQLRANGLLGNELNSVSVNISAVELNSVDDMNHLNEYLRK---DPEfarLLCLEITETAILKDIDQCAIAVQKL 387
Cdd:COG5001 493 VLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAEtglPPS---RLELEITESALLEDPEEALETLRAL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 388 KKQGVSFSIDDFGVGYTSFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKT 467
Cdd:COG5001 570 RALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRE 649
|
410 420
....*....|....*....|....*..
gi 515648682 468 LNCEQAQGYYLGYPMPYKQLKESLTSE 494
Cdd:COG5001 650 LGCDYAQGYLFSRPLPAEELEALLRAR 676
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
16-491 |
3.70e-90 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 286.68 E-value: 3.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 16 LILSSLWVLFSDLAVESLSNNLHEHALAQTVKGLIFIILTSILLWVMVQKNNRDLEDANDLDSVTGLHSPSVFYRYLNKR 95
Cdd:COG2200 95 LLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 96 LKNSQASDH---YVLFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSDGFACLVKLNHTEHIESYI 172
Cdd:COG2200 175 LLLLLLALAllaLLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAA 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 173 A---LVHRRFYQCAYRYDIHATCCIGAALFPSDGNNAKQLMASATHALTEAKKSKDTIEFHDPKLTELERQRQEMVQELR 249
Cdd:COG2200 255 LrllLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRLALESELR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 250 KAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTLVLEKTASQLRANGLLGNEL 329
Cdd:COG2200 335 EALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 330 nSVSVNISAVELNSVDDMNHLNEYLRKDPEFARLLCLEITETAILKDIDQCAIAVQKLKKQGVSFSIDDFGVGYTSFGIF 409
Cdd:COG2200 415 -RLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYL 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 410 SKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYPMPYKQLKE 489
Cdd:COG2200 494 KRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEA 573
|
..
gi 515648682 490 SL 491
Cdd:COG2200 574 LL 575
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
246-483 |
1.92e-80 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 250.54 E-value: 1.92e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 246 QELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTLVLEKTASQLRANGLL 325
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 326 GNELnSVSVNISAVELNSVDDMNHLNEYLRKDPEFARLLCLEITETAILKDIDQCAIAVQKLKKQGVSFSIDDFGVGYTS 405
Cdd:cd01948 81 GPDL-RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515648682 406 FGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYPMP 483
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
245-481 |
1.23e-70 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 224.89 E-value: 1.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 245 VQELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTLVLEKTASQLRANGL 324
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 325 LGNElnSVSVNISAVELNSVDDMNHLNEYLRKDPEFARLLCLEITETAILKDIDQCAIAVQKLKKQGVSFSIDDFGVGYT 404
Cdd:pfam00563 81 GPDI--KLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 515648682 405 SFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYP 481
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
246-483 |
2.99e-63 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 205.91 E-value: 2.99e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 246 QELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTLVLEKTASQLRANGLL 325
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 326 GNELNSVSVNISAVELNSVDDMNHLNEYLRKDPEFARLLCLEITETAILKDIDQCAIAVQKLKKQGVSFSIDDFGVGYTS 405
Cdd:smart00052 82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515648682 406 FGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYPMP 483
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
239-492 |
5.90e-60 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 205.92 E-value: 5.90e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 239 RQRQEMVQELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTLVLEKTASQ 318
Cdd:COG4943 267 RRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRD 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 319 LRANgLLGNELNSVSVNISAVELNSVDDMNHLNEYLRKDPEFARLLCLEITETAILkDIDQCAIAVQKLKKQGVSFSIDD 398
Cdd:COG4943 347 LGDL-LAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDD 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 399 FGVGYTSFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYL 478
Cdd:COG4943 425 FGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLF 504
|
250
....*....|....
gi 515648682 479 GYPMPYKQLKESLT 492
Cdd:COG4943 505 AKPLPAEEFIAWLA 518
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
64-483 |
2.59e-50 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 183.82 E-value: 2.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 64 QKNNRDLEDANDLDSVTGLHSPSVFYRYLNKRLKNSQASdhyVLFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIE 143
Cdd:PRK11359 366 EKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSP---VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 144 HQPLSSRVHSDGFAcLVKLNHTEHIESYIALVHRRFYQCAYRYDIHA---TCCIGAALfpSDGNNAKQLMASATHALTEA 220
Cdd:PRK11359 443 PDQYLCRIEGTQFV-LVSLENDVSNITQIADELRNVVSKPIMIDDKPfplTLSIGISY--DVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 221 KKSK-DTIEFHDPKLTELERQRQEMVQELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAE 299
Cdd:PRK11359 520 RKNGgNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 300 ENYFCRDLTTLVLEKTASQLRANGLLGNELNSVSVNISAVELNSVDDMNHLNEYLRkdpEFA---RLLCLEITETAILKD 376
Cdd:PRK11359 600 EIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQ---AWGidgHQLTVEITESMMMEH 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 377 IDQCAIAVQKLKKQGVSFSIDDFGVGYTSFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGV 456
Cdd:PRK11359 677 DTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGV 756
|
410 420
....*....|....*....|....*..
gi 515648682 457 ENAQQLSILKTLNCEQAQGYYLGYPMP 483
Cdd:PRK11359 757 ETKEQFEMLRKIHCRVIQGYFFSRPLP 783
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
77-483 |
9.27e-44 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 164.08 E-value: 9.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 77 DSVTGLHSPSVFYRYLNKRLKNSQASDHYVLFLlDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSDGF 156
Cdd:PRK10060 240 DSITGLPNRNAIQELIDHAINAADNNQVGIVYL-DLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEF 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 157 ACLVKLNHTEHIESYIALVHRRFYQcAYRY---DIHATCCIGAALFPSDGNNAKQLMASATHALTEAKKS-KDTIEFHDP 232
Cdd:PRK10060 319 LVLASHTSQAALEAMASRILTRLRL-PFRIgliEVYTGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGgRGQFCVFSP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 233 kltELERQRQEMV---QELRKAIDDKAIDIVFQPKFNIESRlVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTT 309
Cdd:PRK10060 398 ---EMNQRVFEYLwldTNLRKALENDQLVIHYQPKITWRGE-VRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGR 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 310 LVLEKTASQL---RANGLlgnELNsVSVNISAVELNSVDDMNHLNEYLrKDPEFAR-LLCLEITETAILKDiDQCAIAV- 384
Cdd:PRK10060 474 WVMLDVVRQVakwRDKGI---NLR-VAVNVSARQLADQTIFTALKQAL-QELNFEYcPIDVELTESCLIEN-EELALSVi 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 385 QKLKKQGVSFSIDDFGVGYTSFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSI 464
Cdd:PRK10060 548 QQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAF 627
|
410
....*....|....*....
gi 515648682 465 LKTLNCEQAQGYYLGYPMP 483
Cdd:PRK10060 628 LTKNGVNERQGFLFAKPMP 646
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
59-483 |
2.70e-41 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 157.03 E-value: 2.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 59 LWVMVQKNNRD---LEDA-------NDLDSVTGLHSPSVFYRYLNKRLKNSQASDHYVLFLLDIDNFKSVADQIGFENTN 128
Cdd:PRK11829 207 LGVLVRNYNRNqqlLADAyadmgriSHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQ 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 129 SFLKDIARSIELPIEHQPLSSRVHSDGFACLVK-----LNHTEHIESYIALVHR--RFYQCAYRydihATCCIGAALFPS 201
Cdd:PRK11829 287 QLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARgtrrsFPAMQLARRIMSQVTQplFFDEITLR----PSASIGITRYQA 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 202 DGNNAKQLMASATHALTEA-KKSKDTIEFHDPKLTELERQRQEMVQELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSR 280
Cdd:PRK11829 363 QQDTAESMMRNASTAMMAAhHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLR 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 281 WTHERYGVVSPDIFVSLAEENYFCRDLTTLVLEKTASQL---RANGLLgnelNSVSVNISAVELNSVDDMNHLNEYLRKD 357
Cdd:PRK11829 443 WCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILadwKARGVS----LPLSVNISGLQVQNKQFLPHLKTLISHY 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 358 PEFARLLCLEITETAILKDIDQCAIAVQKLKKQGVSFSIDDFGVGYTSFGIF---SKLDVDEIKVDRSYISGL-EDDYRS 433
Cdd:PRK11829 519 HIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLpEDDAIA 598
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 515648682 434 RAITSgiidIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYPMP 483
Cdd:PRK11829 599 RIISC----VSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
192-489 |
8.88e-40 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 152.56 E-value: 8.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 192 CCIGAALFPSDgNNAKQLMASATHALTEAK-KSKDTIEFHDPKLTELERQRQEMVQELRKAIDDKAIDIVFQPKFNIESR 270
Cdd:PRK13561 349 CSIGIAMFYGD-LTAEQLYSRAISAAFTARrKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSG 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 271 LVAGVEVLSRWTHERYGVVSPDIFVSLAEEnyfCRDLTTL---VLEKTASQLRANGLLGNELnSVSVNISAVEL---NSV 344
Cdd:PRK13561 428 KLVSAEALLRMQQPDGSWDLPEGLIDRIES---CGLMVTVghwVLEESCRLLAAWQERGIML-PLSVNLSALQLmhpNMV 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 345 DDMNHLNEYLRKDPefaRLLCLEITETAILKDIDQCAIAVQKLKKQGVSFSIDDFGVGYTSFGIFSK---LDVDEIKVDR 421
Cdd:PRK13561 504 ADMLELLTRYRIQP---GTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHmksLPIDVLKIDK 580
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515648682 422 SYISGLEDDyrsRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYPMPYKQLKE 489
Cdd:PRK13561 581 MFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEE 645
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
77-495 |
1.28e-32 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 132.49 E-value: 1.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 77 DSVTGLHSPSVFYRYLNKRLKNSQASDH-YVLFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSDG 155
Cdd:PRK09776 668 DALTHLANRASFEKQLRRLLQTVNSTHQrHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 156 FACLVK---LNHTEHIESYI--ALVHRRFYQCAYRYDIHATccIGAALFPSDGNNAKQLMASATHALTEAKKS-KDTIEF 229
Cdd:PRK09776 748 FGLLLPdcnVESARFIATRIisAINDYHFPWEGRVYRVGAS--AGITLIDANNHQASEVMSQADIACYAAKNAgRGRVTV 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 230 HDPKLTELERQRQEMVQE--LRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDL 307
Cdd:PRK09776 826 YEPQQAAAHSEHRALSLAeqWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHAL 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 308 TTLV----LEKTASQLRANGLlgnelnSVSVNISAVELNSVDDMNHLNEYLRKDPEFARLLCLEITETAILKDIDQCAIA 383
Cdd:PRK09776 906 DRRVihefFRQAAKAVASKGL------SIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRL 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 384 VQKLKKQGVSFSIDDFGVGYTSFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLS 463
Cdd:PRK09776 980 VQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLD 1059
|
410 420 430
....*....|....*....|....*....|..
gi 515648682 464 ILKTLNCEQAQGYYLGYPMPYKQLKESLTSEI 495
Cdd:PRK09776 1060 TLSGIGVDLAYGYAIARPQPLDLLLNSSYFAI 1091
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
239-489 |
4.22e-27 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 114.32 E-value: 4.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 239 RQRQEmvQELRKAIDDKAIDIVFQPKFNIESRLVAGVEVLSRWTHERYGVVSPDIFVSLAEENYFCRDLTTLVLE---KT 315
Cdd:PRK10551 261 RMRPG--KEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFEliaRD 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 316 ASQLRANGLLGNELnsvSVNISAVELNS---VDDMNHLNEYLRKDpEFarLLCLEITETAILKdiDQCAIAV-QKLKKQG 391
Cdd:PRK10551 339 AAELQKVLPVGAKL---GINISPAHLHSdsfKADVQRLLASLPAD-HF--QIVLEITERDMVQ--EEEATKLfAWLHSQG 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 392 VSFSIDDFGVGYTSFGIFSKLDVDEIKVDRSYIS--GLEddyrsrAITSGIID----IARGFGISVVAEGVENAQQLSIL 465
Cdd:PRK10551 411 IEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQaiGTE------TVTSPVLDavltLAKRLNMLTVAEGVETPEQARWL 484
|
250 260
....*....|....*....|....
gi 515648682 466 KTLNCEQAQGYYLGYPMPYKQLKE 489
Cdd:PRK10551 485 RERGVNFLQGYWISRPLPLEDFVR 508
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
11-230 |
2.84e-20 |
|
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: 90.81 E-value: 2.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 11 IVFSYLILSSLWVLFSDLAVESLSNNLHEHALAQTVKGLIFIILTSILLWVMVQKNNRDLEDANDLDSVTGLHSPSVFYR 90
Cdd:COG2199 51 LLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEE 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 91 YLNKRLKNSQASDH-YVLFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSDGFACLVKLNHTEHIE 169
Cdd:COG2199 131 RLERELARARREGRpLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAE 210
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515648682 170 SYIALVHRRFYQCAYRYD---IHATCCIGAALFPSDGNNAKQLMASATHALTEAKKS-KDTIEFH 230
Cdd:COG2199 211 ALAERLREALEQLPFELEgkeLRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAgRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
77-224 |
2.14e-17 |
|
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: 79.14 E-value: 2.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 77 DSVTGLHSPSVFYRYLNKRLKNSQASDHYV-LFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSDG 155
Cdd:cd01949 3 DPLTGLPNRRAFEERLERLLARARRSGRPLaLLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515648682 156 FACLVKLNHTEHIESYIALVHRRFYQCAYRYD--IHATCCIGAALFPSDGNNAKQLMASATHALTEAKKSK 224
Cdd:cd01949 83 FAILLPGTDLEEAEALAERLREAIEEPFFIDGqeIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSG 153
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
75-224 |
2.51e-16 |
|
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: 76.14 E-value: 2.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 75 DLDSVTGLHSPSVFYRYLNKRLKNSQASDHYV-LFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHS 153
Cdd:pfam00990 2 AHDPLTGLPNRRYFEEQLEQELQRALREGSPVaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515648682 154 DGFACLVK-------LNHTEHIESYIALVHRRFYqcAYRYDIHATCCIGAALFPSDGNNAKQLMASATHALTEAKKSK 224
Cdd:pfam00990 82 DEFAILLPetslegaQELAERIRRLLAKLKIPHT--VSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAG 157
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
76-230 |
1.14e-15 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 74.59 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 76 LDSVTGLHSPSVFYRYLNKRLKNSQASDHYV-LFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSD 154
Cdd:smart00267 5 RDPLTGLPNRRYFEEELEQELQRAQRQGSPFaLLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLGGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 155 GFACLVKLNHTEHIESyIA---LVHRRFYQCAYRYDIHATCCIGAALFPSDGNNAKQLMASATHALTEAKKS-KDTIEFH 230
Cdd:smart00267 85 EFALLLPETSLEEAIA-LAeriLQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAgRNQVAVY 163
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
261-487 |
1.63e-08 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 55.39 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 261 FQPKFNIESRLVAgVEVLSRWTHERygvvSPDIFVSlaEENYFCRDLTTLVLEKTASQLRA----------NGLLgneln 330
Cdd:PRK11596 34 FQPIYRTSGRLMA-IELLTAVTHPS----NPSQRLS--PERYFAEITVSHRLDVVKEQLDLlaqwadffvrHGLL----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 331 sVSVNISAVELNSvddmnhlneyLRKDPEFARL------LCLEITETAIL--KDIdqcaiaVQKLKKQGvSFSIDDFGVG 402
Cdd:PRK11596 102 -ASVNIDGPTLIA----------LRQQPAILRLierlpwLRFELVEHIRLpkDSP------FASMCEFG-PLWLDDFGTG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 403 YTSFGIFSKLDVDEIKVDRSYISGLEDDYRSRAITSGIIDIARGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYPM 482
Cdd:PRK11596 164 MANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPA 243
|
....*
gi 515648682 483 PYKQL 487
Cdd:PRK11596 244 PFETL 248
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
77-224 |
5.33e-08 |
|
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: 52.34 E-value: 5.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 77 DSVTGLHSPSVFYRYLNKRLKNSQASDHYV-LFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRVHSDG 155
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARRFQRSFsVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 156 FACLVK---LNHT--------EHIESYIALVhrrfyqcAYRYDIHATCCIGAALFPSDGNNAKQLMASATHALTEAKKSK 224
Cdd:TIGR00254 85 FVVILPgtpLEDAlskaerlrDAINSKPIEV-------AGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAG 157
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
366-486 |
2.70e-07 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 52.88 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 366 LEITETAilkDIDQCAI-AVQKLKKQGVSFSIDDFGVGYTSFGIFSKLDVdeIKVDrsyISGLEDDYRSRaitsgIIDIA 444
Cdd:COG3434 88 LEILEDV---EPDEELLeALKELKEKGYRIALDDFVLDPEWDPLLPLADI--IKID---VLALDLEELAE-----LVARL 154
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 515648682 445 RGFGISVVAEGVENAQQLSILKTLNCEQAQGYYLGYPMPYKQ 486
Cdd:COG3434 155 KRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
77-224 |
1.34e-04 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 44.23 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 77 DSVTGLHSPSVFYRYLNKRLKNSQASDHYVLFLLDIDNFKSVADQIGFENTNSFLKDIARSIEL--PIEHQPLssRVHSD 154
Cdd:PRK09966 251 DPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEfgGLRHKAY--RLGGD 328
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515648682 155 GFACLVKLNHTEH----IESYIALVHRRFYQCAYRYDIHATCCIGAALfPSDGNNAKQLMASATHALTEAKKSK 224
Cdd:PRK09966 329 EFAMVLYDVQSESevqqICSALTQIFNLPFDLHNGHQTTMTLSIGYAM-TIEHASAEKLQELADHNMYQAKHQR 401
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
77-223 |
9.05e-04 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 41.81 E-value: 9.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515648682 77 DSVTGLHSpsvfYRYLNKRLKN----SQASDHYV-LFLLDIDNFKSVADQIGFENTNSFLKDIARSIELPIEHQPLSSRV 151
Cdd:PRK09581 295 DGLTGLHN----RRYFDMHLKNlierANERGKPLsLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515648682 152 HSDGFacLVKLNHTE-HIESYIALVHRR------FYQCAYRYDIHATCCIGAALFPSDGNNAKQLMASATHALTEAKKS 223
Cdd:PRK09581 371 GGEEF--VVVMPDTDiEDAIAVAERIRRkiaeepFIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNT 447
|
|
| |
