|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
71-747 |
8.89e-161 |
|
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: 480.81 E-value: 8.89e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 71 LHATSAAEARQVLACEPDLAVVLLDVVMESEDAGLQLVRYIREELKLGAVRIVLRTGQPGYAPEIETVQAYDINDYKTKS 150
Cdd:COG5001 4 LAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 151 ELTRTRLYTVLTAAIRSYRQICALEANRRGLELIVDASTELSRLRGLHRFAEGVVTQLCAMLGILPEGLVCAQVGVDNDA 230
Cdd:COG5001 84 ALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 231 EVRVIAAAGQYSGMINSPLSAVQIKTVRERLQQCLEQRQNIYDEGTCLYFGMSNGRPMAAWVDVGRDLSDTDQQLLRafc 310
Cdd:COG5001 164 LLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITER--- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 311 snisvgfenVVLYGQLLDQAYNDQLLHLPNRNRFVELLDKNLK----DPADVTLALIDIDDFSDINDAFGHHFGDQVLRA 386
Cdd:COG5001 241 ---------KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALArarrSGRRLALLFIDLDRFKEINDTLGHAAGDELLRE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 387 VVLRLGEALGLNTAMARVGADTFGLLGPS-------EHVsADNIQRVFLEPFSVSGERLQLSATTGLVRLTESAAVGSEL 459
Cdd:COG5001 312 VARRLRACLREGDTVARLGGDEFAVLLPDlddpedaEAV-AERILAALAEPFELDGHELYVSASIGIALYPDDGADAEEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 460 LLDAQIALKQAKSQHRGSSQYFSSAMGTDARERFKLLKGLRAGFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNF 539
Cdd:COG5001 391 LRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 540 VPPDQFIPLAEKSGLIISIGEFVLRTSCHQLKRMLDLGHEDFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEI 619
Cdd:COG5001 471 VSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEI 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 620 TESMAMEDTELVMHILADIKHCGVSVAIDDFGTGFSSLSHLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLN 699
Cdd:COG5001 551 TESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLG 630
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2100991512 700 LTVIAEGIETEEQRQQLLELGCHEGQGYLFARPMQADQLERWMEQPAA 747
Cdd:COG5001 631 LEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
174-743 |
9.34e-105 |
|
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: 332.52 E-value: 9.34e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 174 LEANRRGLELIVDASTELSRLRGLHRFAEGVVTQLCAMLGILPEGLVCAQVGVDNDAEVRVIAAAGQYSGMINSPLSAVQ 253
Cdd:COG2200 2 LLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 254 IKTVRERLQQCLEQRQNIYDEGTCLYFGMSNGRPMAAWVDVGRDLSDTDQQLLRAFCSNISVGFENVVLYGQLLDQAYND 333
Cdd:COG2200 82 LLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 334 QLLHLPNRNRFVELLDKNLKDPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMARVGADTFGLLG 413
Cdd:COG2200 162 LLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 414 PSEHVSAD-------NIQRVFLEPFSVSGERLQLSATTGLVRLTESAAVGSELLLDAQIALKQAKSQHRGSSQYFSSAMg 486
Cdd:COG2200 242 LLLLAAAAaaaaalrLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 487 TDARERFKLLKGLRAGFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAEKSGLIISIGEFVLRTS 566
Cdd:COG2200 321 ARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 567 CHQLKRMLDLGHeDFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESMAMEDTELVMHILADIKHCGVSVA 646
Cdd:COG2200 401 LRQLARWPERGL-DLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 647 IDDFGTGFSSLSHLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETEEQRQQLLELGCHEGQG 726
Cdd:COG2200 480 LDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQG 559
|
570
....*....|....*..
gi 2100991512 727 YLFARPMQADQLERWME 743
Cdd:COG2200 560 YLFGRPLPLEELEALLR 576
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
499-737 |
4.28e-103 |
|
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: 316.02 E-value: 4.28e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 499 LRAGFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAEKSGLIISIGEFVLRTSCHQLKRMLDLGH 578
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 579 eDFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESMAMEDTELVMHILADIKHCGVSVAIDDFGTGFSSLS 658
Cdd:cd01948 83 -DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2100991512 659 HLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETEEQRQQLLELGCHEGQGYLFARPMQADQ 737
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
333-748 |
4.33e-96 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 315.94 E-value: 4.33e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 333 DQLLHLPNRNRFVELLDKNLKDPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMARVGADTFGLL 412
Cdd:PRK11359 379 DPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLV 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 413 GPSEHVS-----ADNIQRVFLEPFSVSGERLQLSATTGLvrlteSAAVGSE---LLLDAQIALKQAKSQHRGSSQYFSSA 484
Cdd:PRK11359 459 SLENDVSnitqiADELRNVVSKPIMIDDKPFPLTLSIGI-----SYDVGKNrdyLLSTAHNAMDYIRKNGGNGWQFFSPA 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 485 MGTDARERFKLLKGLRAGFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAEKSGLIISIGEFVLR 564
Cdd:PRK11359 534 MNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIA 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 565 TSCHQLKRMLDLGHEDFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESMAMEDTELVMHILADIKHCGVS 644
Cdd:PRK11359 614 EACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVG 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 645 VAIDDFGTGFSSLSHLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETEEQRQQLLELGCHEG 724
Cdd:PRK11359 694 LSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVI 773
|
410 420
....*....|....*....|....
gi 2100991512 725 QGYLFARPMQADQLERWMEQPAAL 748
Cdd:PRK11359 774 QGYFFSRPLPAEEIPGWMSSVLPL 797
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
499-737 |
1.30e-89 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 281.03 E-value: 1.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 499 LRAGFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAEKSGLIISIGEFVLRTSCHQLKRMLDLGH 578
Cdd:smart00052 4 LRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQGP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 579 EDFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESMAMEDTELVMHILADIKHCGVSVAIDDFGTGFSSLS 658
Cdd:smart00052 84 PPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2100991512 659 HLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETEEQRQQLLELGCHEGQGYLFARPMQADQ 737
Cdd:smart00052 164 YLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
490-747 |
1.27e-85 |
|
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: 280.65 E-value: 1.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 490 RERFKLLKGLRAGFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAEKSGLIISIGEFVLRTSCHQ 569
Cdd:COG4943 267 RRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRD 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 570 LKRMLDlGHEDFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESMAMeDTELVMHILADIKHCGVSVAIDD 649
Cdd:COG4943 347 LGDLLA-ADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDD 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 650 FGTGFSSLSHLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETEEQRQQLLELGCHEGQGYLF 729
Cdd:COG4943 425 FGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLF 504
|
250
....*....|....*...
gi 2100991512 730 ARPMQADQLERWMEQPAA 747
Cdd:COG4943 505 AKPLPAEEFIAWLAAQRA 522
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
326-744 |
2.94e-77 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 261.93 E-value: 2.94e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 326 LLDQAYNDQLLHLPNRNRFVELLDKNL--KDPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMAR 403
Cdd:PRK10060 233 LRILANTDSITGLPNRNAIQELIDHAInaADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLAR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 404 VGADTFGLLgpSEHVSADNI----QRVFlepfsvsgERLQLSATTGLVRLTESAAVG----------SELLL-DAQIALK 468
Cdd:PRK10060 313 LGGDEFLVL--ASHTSQAALeamaSRIL--------TRLRLPFRIGLIEVYTGCSIGialapehgddSESLIrSADTAMY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 469 QAKSQHRGSSQYFSSAMGTDARERFKLLKGLRAGFEENRLFVVYQPQVRLSdAKAIGAEALLRWRTEEGNFVPPDQFIPL 548
Cdd:PRK10060 383 TAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 549 AEKSGLIISIGEFVLRTSCHQLKRMLDLGHeDFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESMAMEDT 628
Cdd:PRK10060 462 AEESGLIVPLGRWVMLDVVRQVAKWRDKGI-NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 629 ELVMHILADIKHCGVSVAIDDFGTGFSSLSHLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIE 708
Cdd:PRK10060 541 ELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVE 620
|
410 420 430
....*....|....*....|....*....|....*.
gi 2100991512 709 TEEQRQQLLELGCHEGQGYLFARPMQADQLERWMEQ 744
Cdd:PRK10060 621 TAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
499-732 |
5.77e-72 |
|
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: 234.52 E-value: 5.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 499 LRAGFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAEKSGLIISIGEFVLRTSCHQLKRMLDLGH 578
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 579 EDFRmcVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESMAMEDTELVMHILADIKHCGVSVAIDDFGTGFSSLS 658
Cdd:pfam00563 84 IKLS--INLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2100991512 659 HLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETEEQRQQLLELGCHEGQGYLFARP 732
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
325-745 |
2.48e-64 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 226.52 E-value: 2.48e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 325 QLLDQAYNDQ--------LLHLPNRNRFVELLDKNLKDPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALG 396
Cdd:PRK13561 218 QLLQRQYEEQsrnatrfpVSDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 397 LNTAMARVGADTFGLLG-----PSEHVS-ADNIQRVFLEPFSVSGERLQLSATTGlVRLTESAAVGSELLLDAQIALKQA 470
Cdd:PRK13561 298 PRMVLAQISGYDFAIIAngvkePWHAITlGQQVLTIINERLPIQRIQLRPSCSIG-IAMFYGDLTAEQLYSRAISAAFTA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 471 KSQHRGSSQYFSSAMGTDARERFKLLKGLRAGFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAE 550
Cdd:PRK13561 377 RRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 551 KSGLIISIGEFVLRTSCHQLKRMLDLGHEdFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESMAMEDTEL 630
Cdd:PRK13561 457 SCGLMVTVGHWVLEESCRLLAAWQERGIM-LPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 631 VMHILADIKHCGVSVAIDDFGTGFSSLSHLRQ---LDVDRLKIDRAFVreaQTSSAGSTIAQMVINLGRGLNLTVIAEGI 707
Cdd:PRK13561 536 AVAILRPLRNAGVRVALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFV---DGLPEDDSMVAAIIMLAQSLNLQVIAEGV 612
|
410 420 430
....*....|....*....|....*....|....*....
gi 2100991512 708 ETEEQRQQLLELGCHEGQGYLFARPMQADQLE-RWMEQP 745
Cdd:PRK13561 613 ETEAQRDWLLKAGVGIAQGFLFARALPIEIFEeRYLEEK 651
|
|
| DUF3369 |
pfam11849 |
Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain ... |
161-326 |
1.65e-59 |
|
Domain of unknown function (DUF3369); This domain is functionally uncharacterized. This domain is found in bacteria. This presumed domain is about 170 amino acids in length. The domain appears to be related to the GAF domain.
Pssm-ID: 432127 [Multi-domain] Cd Length: 168 Bit Score: 198.53 E-value: 1.65e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 161 LTAAIRSYRQICALEANRRGLELIVDASTELSRLRGLHRFAEGVVTQLCAMLGILPEGLVCAQVGV-DNDAEVRVIAAAG 239
Cdd:pfam11849 1 VTAALRSYRDLRTIERSRRGLEKIIEASADLFELRSLQEFAEGVLTQLAALLNLKKDGLVCVSSGIaAASGNFYVLAATG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 240 QYSGMINSPLSAVQIKTVRERLQQCLEQRQNIY-DEGTCLYFGMSNGRPMAAWVDVGRDLSDTDQQLLRAFCSNISVGFE 318
Cdd:pfam11849 81 KFESLIGKPLSDLLDPEVRELLERALASKRSIFeDDYVGLYFRTSSGSEGVIYLETTRPLSELDRELLEVFCNNISVAFD 160
|
....*...
gi 2100991512 319 NVVLYGQL 326
Cdd:pfam11849 161 NVYLNEEL 168
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
325-741 |
6.75e-55 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 200.17 E-value: 6.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 325 QLLDQAYND--QLLH------LPNRNRFVELLDKNLKDPADVT---LALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGE 393
Cdd:PRK11829 219 QLLADAYADmgRISHrfpvteLPNRSLFISLLEKEIASSTRTDhfhLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQ 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 394 ALGLNTAMARVGADTFGLLGPSEHVSADNIQR------VFLEPFSVSGERLQLSATTGLVRLTESAAVGSELLLDAQIAL 467
Cdd:PRK11829 299 CIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLarrimsQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAM 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 468 KQAKSQHRGSSQYFSSAMGTDARERF----KLLKGLRAG-FEenrLFVvyQPQVRLSDAKAIGAEALLRWRTEEGNFVPP 542
Cdd:PRK11829 379 MAAHHEGRNQIMVFEPHLIEKTHKRLtqenDLLQAIENHdFT---LFL--QPQWDMKRQQVIGAEALLRWCQPDGSYVLP 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 543 DQFIPLAEKSGLIISIGEFVLRTSCHQL----KRMLDLghedfRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELE 618
Cdd:PRK11829 454 SGFVHFAEEEGMMVPLGNWVLEEACRILadwkARGVSL-----PLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 619 ITESMAMEDTELVMHILADIKHCGVSVAIDDFGTGFSSLS---HLRQLDVDRLKIDRAFVREAQTSSAgstIAQMVINLG 695
Cdd:PRK11829 529 ITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRylnHLKSLPIHMIKLDKSFVKNLPEDDA---IARIISCVS 605
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2100991512 696 RGLNLTVIAEGIETEEQRQQLLELGCHEGQGYLFARPM-QADQLERW 741
Cdd:PRK11829 606 DVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLpRAEFEAQY 652
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
502-748 |
6.55e-43 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 163.24 E-value: 6.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 502 GFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAEKSGLIISIG----EFVLRTScHQLKRMLDLG 577
Cdd:PRK10551 271 GIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTqhlfELIARDA-AELQKVLPVG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 578 hedFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESmAMEDTELVMHILADIKHCGVSVAIDDFGTGFSSL 657
Cdd:PRK10551 350 ---AKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITER-DMVQEEEATKLFAWLHSQGIEIAIDDFGTGHSAL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 658 SHLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETEEQRQQLLELGCHEGQGYLFARPMQADQ 737
Cdd:PRK10551 426 IYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLED 505
|
250
....*....|.
gi 2100991512 738 LERWMEQPAAL 748
Cdd:PRK10551 506 FVRWLKEPYTP 516
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
325-738 |
2.68e-34 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 140.96 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 325 QLLDQAYNDQLLHLPNRNRFVELLDKNLKDPADV----TLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTA 400
Cdd:PRK09776 660 QLSYSASHDALTHLANRASFEKQLRRLLQTVNSThqrhALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDV 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 401 MARVGADTFGLLGP------SEHVSADNIQRVFLEPFSVSGERLQLSATTGLVRLTESAAVGSELLLDAQIALKQAKSQH 474
Cdd:PRK09776 740 LARLGGDEFGLLLPdcnvesARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAG 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 475 RGSSQYF----SSAMGtdARERFKLLKGLRAGFEENRLFVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAE 550
Cdd:PRK09776 820 RGRVTVYepqqAAAHS--EHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 551 KSGLIISIGEFVLRTSCHQLKRMLdlGHEDFRMCVNVSLAQFRHPGFMEVLTSALRDTGVNGRNLELEITESMAMEDTEL 630
Cdd:PRK09776 898 DPALMHALDRRVIHEFFRQAAKAV--ASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAES 975
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 631 VMHILADIKHCGVSVAIDDFGTGFSSLSHLRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETE 710
Cdd:PRK09776 976 ASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELP 1055
|
410 420
....*....|....*....|....*...
gi 2100991512 711 EQRQQLLELGCHEGQGYLFARPMQADQL 738
Cdd:PRK09776 1056 LVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
333-476 |
7.20e-29 |
|
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: 112.65 E-value: 7.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 333 DQLLHLPNRNRFVELLDKNLKDPA----DVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMARVGADT 408
Cdd:cd01949 3 DPLTGLPNRRAFEERLERLLARARrsgrPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2100991512 409 FGLLGPSEHVS-----ADNIQRVFLEPFSVSGERLQLSATTGLVRLTESAAVGSELLLDAQIALKQAKSQHRG 476
Cdd:cd01949 83 FAILLPGTDLEeaealAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRN 155
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
325-476 |
2.62e-27 |
|
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: 111.99 E-value: 2.62e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 325 QLLDQAYNDQLLHLPNRNRFVELLDKNLKD----PADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTA 400
Cdd:COG2199 109 RLRRLATHDPLTGLPNRRAFEERLERELARarreGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 401 MARVGADTFGLLGPSEHVS-----ADNIQRVFLE-PFSVSGERLQLSATTGLVRLTESAAVGSELLLDAQIALKQAKSQH 474
Cdd:COG2199 189 VARLGGDEFAVLLPGTDLEeaealAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAG 268
|
..
gi 2100991512 475 RG 476
Cdd:COG2199 269 RN 270
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
330-477 |
1.28e-25 |
|
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: 103.49 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 330 AYNDQLLHLPNRNRFVE----LLDKNLKDPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMARVG 405
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEqleqELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 406 ADTFGLL--GPSEHVSADNIQRV------FLEPFSVSGERLQLSATTGLVRLTESAAVGSELLLDAQIALKQAKSQHRGS 477
Cdd:pfam00990 81 GDEFAILlpETSLEGAQELAERIrrllakLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
329-481 |
5.78e-25 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 101.94 E-value: 5.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 329 QAYNDQLLHLPNRNRFVELLDKNLK----DPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMARV 404
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQraqrQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 405 GADTFGLLGPSEHVS-----ADNIQRVFLEPFSVSGERLQLSATTGLVRLTESAAVGSELLLDAQIALKQAKSQHRGSSQ 479
Cdd:smart00267 82 GGDEFALLLPETSLEeaialAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 2100991512 480 YF 481
Cdd:smart00267 162 VY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
329-481 |
1.90e-16 |
|
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: 77.38 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 329 QAYNDQLLHLPNRNRFVELLDKNLK----DPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMARV 404
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKrarrFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 405 GADTFGLLGP-----SEHVSADNIQRVFL-EPFSVSG-ERLQLSATTGLVRLTESAAVGSELLLDAQIALKQAKSQHRGS 477
Cdd:TIGR00254 81 GGEEFVVILPgtpleDALSKAERLRDAINsKPIEVAGsETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....
gi 2100991512 478 SQYF 481
Cdd:TIGR00254 161 VVVA 164
|
|
| CitB |
COG4565 |
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ... |
38-176 |
1.28e-13 |
|
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];
Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 68.46 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 38 PWRVLIVDDDGDVHKATELAMQGllVEGLPLsFLHATSAAEARQVLA-CEPDLavVLLDVVMESEDaGLQLVRYIREELK 116
Cdd:COG4565 3 MIRVLIVEDDPMVAELLRRYLER--LPGFEV-VGVASSGEEALALLAeHRPDL--ILLDIYLPDGD-GLELLRELRARGP 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2100991512 117 lgAVRIVLRTGqpgyAPEIETVQ---AYDINDYKTKsELTRTRLYTVLTAAIRSYRQICALEA 176
Cdd:COG4565 77 --DVDVIVITA----ARDPETVRealRAGVVDYLIK-PFTFERLREALERYLEYRRLLREDQE 132
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
333-475 |
4.63e-11 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 64.32 E-value: 4.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 333 DQLLHLPNRNRFVELLDKNLKD--PADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMARVGADTFG 410
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQLRNrePQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFI 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2100991512 411 LLGPSE-----HVSADNIQRVFLE-PFSVSGERLQLSATTGLVRLTESAAVgSELLLDAQIALKQAKSQHR 475
Cdd:PRK09894 212 ICLKAAtdeeaCRAGERIRQLIANhAITHSDGRINITATFGVSRAFPEETL-DVVIGRADRAMYEGKQTGR 281
|
|
| CheY |
COG0784 |
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ... |
37-170 |
8.55e-11 |
|
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];
Pssm-ID: 440547 [Multi-domain] Cd Length: 128 Bit Score: 59.86 E-value: 8.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 37 HPWRVLIVDDDGDVHKATELamqglLVEGLPLSFLHATSAAEARQVL-ACEPDLavVLLDVVMESEDaGLQLVRYIREEL 115
Cdd:COG0784 4 GGKRILVVDDNPDNRELLRR-----LLERLGYEVTTAEDGAEALELLrAGPPDL--ILLDINMPGMD-GLELLRRIRALP 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2100991512 116 KLGAVRIVLRTGQPGyAPEIETVQAYDINDYKTKSeLTRTRLYTVLTAAIRSYRQ 170
Cdd:COG0784 76 RLPDIPIIALTAYAD-EEDRERALEAGADDYLTKP-VDPEELLEALRRLLARASA 128
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
505-736 |
1.73e-10 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 64.50 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 505 ENRL----FVVYQPQVRLSDAKAIGAEALLRWRTEEGNFVPPDQFIPLAEKSGLIISIGEFVLRTSchqLKRMLDLGHED 580
Cdd:PRK11059 409 EQTLvrggPRLYQQPAVTRDGKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERV---LPLLRYWPEEN 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 581 FrmCVNVSLAQFRHPGFMEVLTSALRDTGVNGRN-LELEITESMAMEDTELVMHILADIKHCGVSVAIDDFGTGFSSLSH 659
Cdd:PRK11059 486 L--SINLSVDSLLSRAFQRWLRDTLLQCPRSQRKrLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSY 563
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2100991512 660 LRQLDVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETEEQRQQLLELGCHEGQGYLFARPMQAD 736
Cdd:PRK11059 564 IKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPLD 640
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
325-473 |
3.62e-10 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 62.72 E-value: 3.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 325 QLLDQAYNDQLLHLPNRNRFVELLDKNLKDPA---DVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAM 401
Cdd:PRK09966 243 QLLRTALHDPLTGLANRAAFRSGINTLMNNSDarkTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 402 ARVGADTFGLLGPSEHvSADNIQRV-------FLEPFSV-SGERLQLSATTGLVrLTESAAVGSELLLDAQIALKQAKSQ 473
Cdd:PRK09966 323 YRLGGDEFAMVLYDVQ-SESEVQQIcsaltqiFNLPFDLhNGHQTTMTLSIGYA-MTIEHASAEKLQELADHNMYQAKHQ 400
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
325-475 |
6.28e-10 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 62.23 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 325 QLLDQAYNDQLLHLPNR----NRFVELLDKNLKDPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTA 400
Cdd:PRK09581 287 QSIEMAVTDGLTGLHNRryfdMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDL 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 401 MARVGADTFGLLGPSEHVS-----ADNIQR-VFLEPFSVSG--ERLQLSATTGLVRLTESAAVGSELLLDAQIALKQAKS 472
Cdd:PRK09581 367 IARYGGEEFVVVMPDTDIEdaiavAERIRRkIAEEPFIISDgkERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKN 446
|
...
gi 2100991512 473 QHR 475
Cdd:PRK09581 447 TGR 449
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
647-739 |
1.41e-09 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 59.24 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 647 IDDFGTG---FSSLSHLRqldVDRLKIDRAFVREAQTSSAGSTIAQMVINLGRGLNLTVIAEGIETEEQRQQLLELGCHE 723
Cdd:PRK11596 157 LDDFGTGmanFSALSEVR---YDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFA 233
|
90
....*....|....*.
gi 2100991512 724 GQGYLFARPMQADQLE 739
Cdd:PRK11596 234 AQGYFLSRPAPFETLE 249
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
617-732 |
2.82e-09 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 59.82 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 617 LEITESMamEDTELVMHILADIKHCGVSVAIDDFgTGFSSLSHLRQLdVDRLKIDrafVREAQTSSAGSTIAQMvinlgR 696
Cdd:COG3434 88 LEILEDV--EPDEELLEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID---VLALDLEELAELVARL-----K 155
|
90 100 110
....*....|....*....|....*....|....*.
gi 2100991512 697 GLNLTVIAEGIETEEQRQQLLELGCHEGQGYLFARP 732
Cdd:COG3434 156 RYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
341-479 |
9.75e-09 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 57.92 E-value: 9.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 341 RNRFvellDKNLKDPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMARVGADTFGLL---GPSEH 417
Cdd:PRK10245 224 RNEF----DNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVImsgTPAES 299
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2100991512 418 VSAdNIQRVF--LEPFSVSG---ERLQLSatTGLVRLTESAAVGSELLLDAQIALKQAKSQHRGSSQ 479
Cdd:PRK10245 300 AIT-AMSRVHegLNTLRLPNapqVTLRIS--VGVAPLNPQMSHYREWLKSADLALYKAKNAGRNRTE 363
|
|
| RpfG |
COG3437 |
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
40-183 |
3.27e-08 |
|
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];
Pssm-ID: 442663 [Multi-domain] Cd Length: 224 Bit Score: 54.79 E-value: 3.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVHKATElamqgLLVEGLPLSFLHATSAAEA-RQVLACEPDLavVLLDVVMESEDaGLQLVRYIREELKLG 118
Cdd:COG3437 8 TVLIVDDDPENLELLR-----QLLRTLGYDVVTAESGEEAlELLLEAPPDL--ILLDVRMPGMD-GFELLRLLRADPSTR 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2100991512 119 AVRIVLRTgqpGYAPEIETVQAYD--INDYKTKSeLTRTRLYTVLTAAIRSYRQICALEANRRGLEL 183
Cdd:COG3437 80 DIPVIFLT---ALADPEDRERALEagADDYLTKP-FDPEELLARVRNALELRRLQRELDDLVLYLKL 142
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
38-149 |
9.26e-08 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 52.60 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 38 PWRVLIVDDDGDVHKATELAMqgllvEGLPLSFLHATSAAEARQVLACE-PDLavVLLDVVMESEDaGLQLVRYIREELK 116
Cdd:COG3706 1 PARILVVDDDPTNRKLLRRLL-----EAAGYEVVEAADGEEALELLQEHrPDL--ILLDLEMPDMD-GLELCRRLRADPR 72
|
90 100 110
....*....|....*....|....*....|....*
gi 2100991512 117 LGAVRIVLRTGQPGyapEIETVQAYDI--NDYKTK 149
Cdd:COG3706 73 TADIPIIFLTALDD---EEDRARALEAgaDDYLTK 104
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
329-414 |
1.52e-06 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 51.55 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 329 QAYNDQLLHLPNRNRFVELLDKNLK----DPADVTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAMARV 404
Cdd:PRK15426 397 QAWHDPLTRLYNRGALFEKARALAKrcqrDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
|
90
....*....|
gi 2100991512 405 GADTFGLLGP 414
Cdd:PRK15426 477 GGEEFCVVLP 486
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
40-197 |
2.04e-06 |
|
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];
Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 50.73 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVHKATE--LAMQGLLVEglplsflHATSAAEARQVL-ACEPDlaVVLLDVVMESEDaGLQLVRYIREELK 116
Cdd:COG2204 4 RILVVDDDPDIRRLLKelLERAGYEVE-------TAASGEEALALLrEEPPD--LVLLDLRMPGMD-GLELLRELRALDP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 117 lgAVRIVLRTGQPGYAPEIETVQAyDINDYKTKSeLTRTRLYTVLTAAIRSYRqicaLEANRRGLELIVDASTELSRLRG 196
Cdd:COG2204 74 --DLPVILLTGYGDVETAVEAIKA-GAFDYLTKP-FDLEELLAAVERALERRR----LRRENAEDSGLIGRSPAMQEVRR 145
|
.
gi 2100991512 197 L 197
Cdd:COG2204 146 L 146
|
|
| COG4567 |
COG4567 |
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ... |
40-140 |
1.44e-05 |
|
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 443624 [Multi-domain] Cd Length: 177 Bit Score: 46.06 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVHKATELAMQ--GLLVEglplsflHATSAAEARQVLA-CEPDLAVVllDVVMESEDaGLQLVRYIREelK 116
Cdd:COG4567 6 SLLLVDDDEAFARVLARALErrGFEVT-------TAASVEEALALLEqAPPDYAVL--DLRLGDGS-GLDLIEALRE--R 73
|
90 100
....*....|....*....|....
gi 2100991512 117 LGAVRIVLRTgqpGYAPEIETVQA 140
Cdd:COG4567 74 DPDARIVVLT---GYASIATAVEA 94
|
|
| REC_RegA-like |
cd17563 |
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ... |
40-132 |
5.93e-05 |
|
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381111 [Multi-domain] Cd Length: 112 Bit Score: 42.81 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVHKATELAMQ--GLLVEglplsflHATSAAEARQVL-ACEPDLAVvlLDVVMEsEDAGLQLVRYIREelK 116
Cdd:cd17563 2 SLLLVDDDEVFAERLARALErrGFEVE-------TAHSVEEALALArEEKPDYAV--LDLRLG-GDSGLDLIPPLRA--L 69
|
90
....*....|....*.
gi 2100991512 117 LGAVRIVLRTgqpGYA 132
Cdd:cd17563 70 QPDARIVVLT---GYA 82
|
|
| REC_hyHK_blue-like |
cd18161 |
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ... |
41-113 |
6.44e-05 |
|
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381145 [Multi-domain] Cd Length: 102 Bit Score: 42.72 E-value: 6.44e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2100991512 41 VLIVDDDGDVHKATE--LAMQGLLVeglplsfLHATSAAEARQVLACEPDLAVVLLDVVMESEDAGLQLVRYIRE 113
Cdd:cd18161 1 VLVVEDDPDVRRLTAevLEDLGYTV-------LEAASGDEALDLLESGPDIDLLVTDVIMPGGMNGSQLAEEARR 68
|
|
| AmiR |
COG3707 |
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ... |
38-182 |
8.97e-05 |
|
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 442921 [Multi-domain] Cd Length: 194 Bit Score: 44.18 E-value: 8.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 38 PWRVLIVDDDGDVHKATE--LAMQGLLVEGlplsflHATSAAEA-RQVLACEPDLavVLLDVVMESEDaGLQLVRYIREE 114
Cdd:COG3707 3 GLRVLVVDDEPLRRADLRegLREAGYEVVA------EAADGEDAvELVRELKPDL--VIVDIDMPDRD-GLEAARQISEE 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2100991512 115 lKLGAVRIVLRTGQPGYapeIETVQAYDINDYKTKsELTRTRLYTVLTAAIRSYRQICALEANRRGLE 182
Cdd:COG3707 74 -RPAPVILLTAYSDPEL---IERALEAGVSAYLVK-PLDPEDLLPALELALARFRELRALRRELAKLR 136
|
|
| YesN |
COG4753 |
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ... |
40-146 |
1.17e-04 |
|
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 443786 [Multi-domain] Cd Length: 103 Bit Score: 41.68 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVHKatelAMQGLLVEGLPLSFLH-ATSAAEA-RQVLACEPDLavVLLDVVMESEDaGLQLVRYIREElKL 117
Cdd:COG4753 1 KVLIVDDEPLIRE----GLKRILEWEAGFEVVGeAENGEEAlELLEEHKPDL--VITDINMPGMD-GLELLEAIREL-DP 72
|
90 100 110
....*....|....*....|....*....|..
gi 2100991512 118 GAVRIVLrTgqpGYApEIETVQ---AYDINDY 146
Cdd:COG4753 73 DTKIIIL-S---GYS-DFEYAQeaiKLGADDY 99
|
|
| REC_TrrA-like |
cd17554 |
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ... |
40-131 |
1.95e-04 |
|
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381106 [Multi-domain] Cd Length: 113 Bit Score: 41.44 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVHK--ATELAMQGLLVEGlplsflhATSAAEARQVLACE-PDLavVLLDVVMESEDaGLQLVRYIREELK 116
Cdd:cd17554 2 KILVVDDEENIRElyKEELEDEGYEVVT-------AGNGEEALEKLESEdPDL--VILDIKMPGMD-GLETLRKIREKKP 71
|
90
....*....|....*
gi 2100991512 117 lgAVRIVLRTGQPGY 131
Cdd:cd17554 72 --DLPVIICTAYSEY 84
|
|
| REC_OmpR |
cd17574 |
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ... |
42-149 |
2.22e-04 |
|
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381116 [Multi-domain] Cd Length: 99 Bit Score: 40.85 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 42 LIVDDDGDVHK--ATELAMQGLLVEglplsflHATSAAEA-RQVLACEPDLavVLLDVVMESEDaGLQLVRYIREELKlg 118
Cdd:cd17574 1 LVVEDDEEIAEllSDYLEKEGYEVD-------TAADGEEAlELAREEQPDL--IILDVMLPGMD-GFEVCRRLREKGS-- 68
|
90 100 110
....*....|....*....|....*....|...
gi 2100991512 119 AVRIVLRTGQPGyapEIETVQAYDI--NDYKTK 149
Cdd:cd17574 69 DIPIIMLTAKDE---EEDKVLGLELgaDDYITK 98
|
|
| REC_citrate_TCS |
cd19925 |
phosphoacceptor receiver (REC) domain of citrate family two-component system response ... |
39-163 |
2.27e-04 |
|
phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381152 [Multi-domain] Cd Length: 118 Bit Score: 41.46 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 39 WRVLIVDDD---GDVHKATELAMQGLLVEGLplsflhATSAAEARQVLAcEPDLAVVLLDVVMESEDaGLQLVRYIREel 115
Cdd:cd19925 1 INVLIVEDDpmvAEIHRAYVEQVPGFTVIGT------AGTGEEALKLLK-ERQPDLILLDIYLPDGN-GLDLLRELRA-- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2100991512 116 KLGAVRIVLRTGqpgyAPEIETVQA---YDINDYKTKSeLTRTRLYTVLTA 163
Cdd:cd19925 71 AGHDVDVIVVTA----ANDVETVREalrLGVVDYLIKP-FTFERLRQRLER 116
|
|
| OmpR |
COG0745 |
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ... |
40-149 |
2.33e-04 |
|
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 440508 [Multi-domain] Cd Length: 204 Bit Score: 43.02 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVHKATE--LAMQGLLVEglplsflHATSAAEA-RQVLACEPDLavVLLDVVMESEDaGLQLVRYIREELK 116
Cdd:COG0745 3 RILVVEDDPDIRELLAdaLEREGYEVD-------TAADGEEAlELLEEERPDL--ILLDLMLPGMD-GLEVCRRLRARPS 72
|
90 100 110
....*....|....*....|....*....|....*
gi 2100991512 117 lgAVRIVLRTgqpGYAPEIETVQAYDI--NDYKTK 149
Cdd:COG0745 73 --DIPIIMLT---ARDDEEDRVRGLEAgaDDYLTK 102
|
|
| REC_CpdR_CckA-like |
cd18160 |
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ... |
40-113 |
2.40e-04 |
|
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381144 [Multi-domain] Cd Length: 103 Bit Score: 40.95 E-value: 2.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2100991512 40 RVLIVDDDGDVHKATELAMQ--GLLVEglplsflHATSAAEARQVLACEPDLAVVLLDVVMESEDaGLQLVRYIRE 113
Cdd:cd18160 1 TILLADDEPSVRKFIVTTLKkaGYAVT-------EAESGAEALEKLQQGKDIDIVVTDIVMPEMD-GIELAREARK 68
|
|
| LytT |
COG3279 |
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ... |
40-170 |
2.99e-04 |
|
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];
Pssm-ID: 442510 [Multi-domain] Cd Length: 235 Bit Score: 42.88 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDgdvhkatELAMQGL--LVEGLP-LSFL-HATSAAEARQVL-ACEPDLavVLLDVVMESEDaGLQLVRYIREE 114
Cdd:COG3279 3 KILIVDDE-------PLARERLerLLEKYPdLEVVgEASNGEEALELLeEHKPDL--VFLDIQMPGLD-GFELARQLREL 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2100991512 115 LKlgAVRIVLRTGQPGYApeietVQAYDIN--DYKTKsELTRTRLYTVLTAAIRSYRQ 170
Cdd:COG3279 73 DP--PPPIIFTTAYDEYA-----LEAFEVNavDYLLK-PIDEERLAKALEKAKERLEA 122
|
|
| REC_2_DhkD-like |
cd17580 |
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ... |
41-127 |
8.95e-04 |
|
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381118 [Multi-domain] Cd Length: 112 Bit Score: 39.36 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 41 VLIVDDDGDVHK--ATELAMQGLLVEGlplsflhATSAAEARQVLACE-PDlaVVLLDVVMESEDaGLQLVRYIREELKL 117
Cdd:cd17580 1 ILVVDDNEDAAEmlALLLELEGAEVTT-------AHSGEEALEAAQRFrPD--VILSDIGMPGMD-GYELARRLRELPWL 70
|
90
....*....|
gi 2100991512 118 GAVRIVLRTG 127
Cdd:cd17580 71 ANTPAIALTG 80
|
|
| Response_reg |
pfam00072 |
Response regulator receiver domain; This domain receives the signal from the sensor partner in ... |
41-149 |
1.89e-03 |
|
Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.
Pssm-ID: 395025 [Multi-domain] Cd Length: 111 Bit Score: 38.67 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 41 VLIVDDDGDVHKATE--LAMQGLLVEGlplsflhATSAAEARQVLACE-PDLavVLLDVVMESEDaGLQLVRYIREELKl 117
Cdd:pfam00072 1 VLIVDDDPLIRELLRqlLEKEGYVVAE-------ADDGKEALELLKEErPDL--ILLDINMPGMD-GLELLKRIRRRDP- 69
|
90 100 110
....*....|....*....|....*....|....
gi 2100991512 118 gAVRIVLRTgqpGYAPEIETVQAYD--INDYKTK 149
Cdd:pfam00072 70 -TTPVIILT---AHGDEDDAVEALEagADDFLSK 99
|
|
| REC_RpfG-like |
cd17551 |
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ... |
40-129 |
2.01e-03 |
|
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381103 [Multi-domain] Cd Length: 118 Bit Score: 38.58 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDgdvhKATELAMQGLLVEglpLSFLHATSAAEARQVLA-CE---PDLavVLLDVVMESEDaGLQLVRYIREEL 115
Cdd:cd17551 2 RILIVDDN----PTNLLLLEALLRS---AGYLEVVSFTDPREALAwCRenpPDL--ILLDYMMPGMD-GLEFIRRLRALP 71
|
90
....*....|....
gi 2100991512 116 KLGAVRIVLRTGQP 129
Cdd:cd17551 72 GLEDVPIVMITADT 85
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
358-429 |
3.24e-03 |
|
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: 38.49 E-value: 3.24e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2100991512 358 VTLALIDIDDFSDINDAFGHHFGDQVLRAVVLRLGEALGLNTAM-ARVGADTFGLLGPSEHVS-----ADNIQRVFLE 429
Cdd:cd07556 2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLkIKTIGDEFMVVSGLDHPAaavafAEDMREAVSA 79
|
|
| REC_DctD-like |
cd17549 |
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ... |
41-113 |
4.27e-03 |
|
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381101 [Multi-domain] Cd Length: 130 Bit Score: 37.85 E-value: 4.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2100991512 41 VLIVDDDGDVHKATElamQGLLVEGLPlsflhATSAAEARQVLA-CEPDLA-VVLLDVVMESEDaGLQLVRYIRE 113
Cdd:cd17549 1 VLLVDDDADVREALQ---QTLELAGFR-----VRAFADAEEALAaLSPDFPgVVISDIRMPGMD-GLELLAQIRE 66
|
|
| REC_DC-like |
cd17534 |
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ... |
40-115 |
4.45e-03 |
|
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381089 [Multi-domain] Cd Length: 117 Bit Score: 37.77 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVhkATELAMQ----GLLVEGlplsflHATSAAEA-RQVLACEPDLavVLLDVVMESEDAGLQLVRYIREE 114
Cdd:cd17534 2 KILIVEDEAII--ALDLKEIleslGYEVVG------IADSGEEAiELAEENKPDL--ILMDINLKGDMDGIEAAREIREK 71
|
.
gi 2100991512 115 L 115
Cdd:cd17534 72 F 72
|
|
| PRK13856 |
PRK13856 |
two-component response regulator VirG; Provisional |
41-109 |
5.19e-03 |
|
two-component response regulator VirG; Provisional
Pssm-ID: 172377 [Multi-domain] Cd Length: 241 Bit Score: 39.41 E-value: 5.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2100991512 41 VLIVDDDgdvhkateLAMQGLLVEGLPLSFLHATSAAEARQ---VLACEPdLAVVLLDVVMESEDaGLQLVR 109
Cdd:PRK13856 4 VLVIDDD--------VAMRHLIVEYLTIHAFKVTAVADSQQfnrVLASET-VDVVVVDLNLGRED-GLEIVR 65
|
|
| REC_HupR-like |
cd17569 |
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ... |
40-145 |
7.81e-03 |
|
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381113 [Multi-domain] Cd Length: 118 Bit Score: 37.00 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVHKAtelaMQGLLvEGLPLSFLHATSAAEARQVLACEPdLAVVLLDVVMESEDaGLQLVRYIREELKlGA 119
Cdd:cd17569 2 TILLVDDEPNILKA----LKRLL-RREGYEVLTATSGEEALEILKQEP-VDVVISDQRMPGMD-GAELLKRVRERYP-DT 73
|
90 100
....*....|....*....|....*..
gi 2100991512 120 VRIVLrTgqpGYApEIETV-QAydIND 145
Cdd:cd17569 74 VRILL-T---GYA-DLDAAiEA--INE 93
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
40-132 |
9.32e-03 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 39.27 E-value: 9.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVhkaTELAmqGLLVEGLPLSFLHATSAAEARQVLACEPDLAVVLLDVVMESEDAGLQLVRYIREelKLGA 119
Cdd:PRK13557 417 TILIVDDRPDV---AELA--RMILEDFGYRTLVASNGREALEILDSHPEVDLLFTDLIMPGGMNGVMLAREARR--RQPK 489
|
90
....*....|...
gi 2100991512 120 VRIVLRTgqpGYA 132
Cdd:PRK13557 490 IKVLLTT---GYA 499
|
|
| PRK11361 |
PRK11361 |
acetoacetate metabolism transcriptional regulator AtoC; |
40-140 |
9.64e-03 |
|
acetoacetate metabolism transcriptional regulator AtoC;
Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 39.06 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2100991512 40 RVLIVDDDGDVHK--ATELAMQGLLVEGlplsflhATSAAEARQVLACEPdLAVVLLDVVMESEDaGLQLVRYIREELKL 117
Cdd:PRK11361 6 RILIVDDEDNVRRmlSTAFALQGFETHC-------ANNGRTALHLFADIH-PDVVLMDIRMPEMD-GIKALKEMRSHETR 76
|
90 100
....*....|....*....|....
gi 2100991512 118 GAVriVLRTgqpGYApEIET-VQA 140
Cdd:PRK11361 77 TPV--ILMT---AYA-EVETaVEA 94
|
|
| |
