|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
302-978 |
0e+00 |
|
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: 567.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 302 EFQPRGQDLWLIPRCVVEGDAFAVVKPMPMDIGPGREIFQHGQSLYVEDLALRYPQSSQLLALDAKAYVGIPFPGPNGLP 381
Cdd:COG5001 5 AALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 382 LGQLTLLLATPLADPAPLLDVLYEQRERAASELQRLANDDALRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASE 461
Cdd:COG5001 85 LLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 462 EMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKETA 541
Cdd:COG5001 165 LLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 542 RHIERLAYYDDLCDLYNRRSLTDIMQRTLQAP--SGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENL 619
Cdd:COG5001 245 ERLRHLAYHDPLTGLPNRRLFLDRLEQALARArrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 620 VLARTSGDEFALLFTALGQgyiTAKilAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVH 699
Cdd:COG5001 325 TVARLGGDEFAVLLPDLDD---PED--AEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 700 MAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPI 779
Cdd:COG5001 400 RAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPL 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 780 AEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENR 859
Cdd:COG5001 480 AEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 860 LESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVE 939
Cdd:COG5001 560 EEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVE 639
|
650 660 670
....*....|....*....|....*....|....*....
gi 780222879 940 EEEQLAVLKALGCQHYQGFLTSRPLPVKALESLLGATPA 978
Cdd:COG5001 640 TEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
399-973 |
7.46e-111 |
|
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: 354.48 E-value: 7.46e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 399 LLDVLYEQRERAASELQRLANDDALRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGD 478
Cdd:COG2200 6 ALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLAL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 479 TLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKETARHIERLAYYDDLCDLYN 558
Cdd:COG2200 86 LLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 559 R--RSLTDIMQRTLQAPSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLFTAL 636
Cdd:COG2200 166 RllLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 637 GqgyitAKILAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMAKRAGQGNHIFFSEAM 716
Cdd:COG2200 246 A-----AAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 717 AEKEKsKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKT 796
Cdd:COG2200 321 ARARR-RLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 797 ACAQYSFWLNNGLAIPhLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLI 876
Cdd:COG2200 400 ALRQLARWPERGLDLR-LSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 877 SIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQ 956
Cdd:COG2200 479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558
|
570
....*....|....*..
gi 780222879 957 GFLTSRPLPVKALESLL 973
Cdd:COG2200 559 GYLFGRPLPLEELEALL 575
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
528-978 |
6.18e-104 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 338.58 E-value: 6.18e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 528 VCSFHDITQEKETARHIERLAYYDDLCDLYNRRSLTDIMQRTLQAPSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAV 607
Cdd:PRK10060 217 ICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 608 VVRLKSLPQENLVLARTSGDEFALLFTALGQGyitakiLAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDH 687
Cdd:PRK10060 297 SLAILSCLEEDQTLARLGGDEFLVLASHTSQA------ALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDS 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 688 LVLMQQADTAVHMAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPqyRVD-NGTLSGIEALLRWQKA 766
Cdd:PRK10060 371 ESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQP--KITwRGEVRSLEALVRWQSP 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 767 DGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNNGLAIpHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRL 846
Cdd:PRK10060 449 ERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINL-RVAVNVSARQLADQTIFTALKQALQELNFEYCPI 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 847 LLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLA 926
Cdd:PRK10060 528 DVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVA 607
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 780222879 927 RVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKALESLLGATPA 978
Cdd:PRK10060 608 QALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYLK 659
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
728-966 |
1.23e-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: 322.96 E-value: 1.23e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 728 NQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNN 807
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 808 GLAIpHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSS 887
Cdd:cd01948 81 GPDL-RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879 888 LAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPV 966
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
523-965 |
2.47e-99 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 330.19 E-value: 2.47e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 523 EISHFVCSFHdITQEkETARHIERLAYYDDLCDLYNR----RSLTDIMQRTLQApsgqwgALLLLDLDNFKSINDSLGHA 598
Cdd:PRK11359 353 DISQHLAALA-LEQE-KSRQHIEQLIQFDPLTGLPNRnnlhNYLDDLVDKAVSP------VVYLIGVDHFQDVIDSLGYA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 599 CGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLFTALGQGYITakilaeHFARELMGIFRAPFDIGDHKLHCSASVGIS 678
Cdd:PRK11359 425 WADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNIT------QIADELRNVVSKPIMIDDKPFPLTLSIGIS 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 679 LFSDDDKDHLvlMQQADTAVHMAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIE 758
Cdd:PRK11359 499 YDVGKNRDYL--LSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 759 ALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPHLSVNVSARQFHTAGFVQQVEYILRD 838
Cdd:PRK11359 577 ALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQA 656
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 839 TGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAI 918
Cdd:PRK11359 657 WGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILAL 736
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 780222879 919 VKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLP 965
Cdd:PRK11359 737 LEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLP 783
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
728-966 |
1.97e-90 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 287.96 E-value: 1.97e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 728 NQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNN 807
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 808 GLAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSS 887
Cdd:smart00052 82 GPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879 888 LAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPV 966
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
728-963 |
1.05e-79 |
|
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: 258.79 E-value: 1.05e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 728 NQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNN 807
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 808 glAIPHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSS 887
Cdd:pfam00563 82 --PDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780222879 888 LAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRP 963
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
724-978 |
5.01e-73 |
|
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: 250.99 E-value: 5.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 724 LSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSF 803
Cdd:COG4943 270 LSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 804 WL--NNGLaipHLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVvLENRLESIARIRQLKALGLLISIDDF 881
Cdd:COG4943 350 LLaaDPDF---HISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERG-FIDPAKARAVIAALREAGHRIAIDDF 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 882 GTGYSSLAYLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTS 961
Cdd:COG4943 426 GTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFA 505
|
250
....*....|....*..
gi 780222879 962 RPLPVKALESLLGATPA 978
Cdd:COG4943 506 KPLPAEEFIAWLAAQRA 522
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
521-970 |
3.11e-72 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 251.94 E-value: 3.11e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 521 EEEISHFVCSFhDITQEKETARHIE--RLAYYDDLCDLYNRRSLTDIMQRTLQapSGQWGALLLLDLDNFKSINDSLGHA 598
Cdd:PRK13561 203 DDEIGMLVRSY-NLNQQLLQRQYEEqsRNATRFPVSDLPNKALLMALLEQVVA--RKQTTALMIITCETLRDTAGVLKEA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 599 CGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLftalgqgyitAKILAEHF-----ARELMGIFRAPFDIGDHKLHCSA 673
Cdd:PRK13561 280 QREILLLTLVEKLKSVLSPRMVLAQISGYDFAII----------ANGVKEPWhaitlGQQVLTIINERLPIQRIQLRPSC 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 674 SVGISLFsDDDKDHLVLMQQADTAVHMAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGT 753
Cdd:PRK13561 350 SIGIAMF-YGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 754 LSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPhLSVNVSARQFHTAGFVQQVE 833
Cdd:PRK13561 429 LVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLP-LSVNLSALQLMHPNMVADML 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 834 YILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSSLAYL---RDLPADEVKLDRSFIQTLv 910
Cdd:PRK13561 508 ELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGL- 586
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 911 hsEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKALE 970
Cdd:PRK13561 587 --PEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFE 644
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
550-971 |
1.63e-69 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 244.85 E-value: 1.63e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 550 YDDLCDLYNRRSLTDIMQRTL------QAPSGQWGA----LLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENL 619
Cdd:PRK11829 225 YADMGRISHRFPVTELPNRSLfislleKEIASSTRTdhfhLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSD 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 620 VLARTSGDEFALLftalgQGYITAKILAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVH 699
Cdd:PRK11829 305 LLAQLSKTEFAVL-----ARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMM 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 700 MAKRAGQGNHIFFSEAMAEKEKSKLSLNNQLRDALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPI 779
Cdd:PRK11829 380 AAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHF 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 780 AEETTLIQEIGYWVMKTACAQYSFWLNNGLAIPhLSVNVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENR 859
Cdd:PRK11829 460 AEEEGMMVPLGNWVLEEACRILADWKARGVSLP-LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 860 LESIARIRQLKALGLLISIDDFGTGYSSLAYLR---DLPADEVKLDRSFIQTLvhsEQDKAIVKAILDLARVFRFTVTAE 936
Cdd:PRK11829 539 DEALRLLRELQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAE 615
|
410 420 430
....*....|....*....|....*....|....*
gi 780222879 937 GVEEEEQLAVLKALGCQHYQGFLTSRPLPVKALES 971
Cdd:PRK11829 616 GVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEFEA 650
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
434-975 |
5.63e-58 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 217.23 E-value: 5.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 434 DGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDT--LKEEVIAA-VNRQGYWLGEEQCLH-REGHLFP 509
Cdd:PRK09776 547 EAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVLHITFGDNgpLMENIYSClTSRSAAYLEQDVVLHcRSGGSYD 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 510 VRLMVSGVKDEEEEISHFVCSFHDITQEKETARHIERLAYYDDLCDLYNRRSLTDIMQRTLQAPS--GQWGALLLLDLDN 587
Cdd:PRK09776 627 VHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNstHQRHALVFIDLDR 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 588 FKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLF--------TALGQGYITAkILAEHFARElmgiFR 659
Cdd:PRK09776 707 FKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLpdcnvesaRFIATRIISA-INDYHFPWE----GR 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 660 ApFDIGdhklhcsASVGISLFSDDDKDHLVLMQQADTAVHMAKRAGQGNHIF--FSEAMAEKEKSKLSLNNQLRDALRNN 737
Cdd:PRK09776 782 V-YRVG-------ASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVyePQQAAAHSEHRALSLAEQWRMIKENQ 853
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 738 ELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSFWL-NNGLAIphlSV 816
Cdd:PRK09776 854 LMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVaSKGLSI---AL 930
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 817 NVSARQFHTAGFVQQVEYILRDTGVPPSRLLLEITESVVLENRLESIARIRQLKALGLLISIDDFGTGYSSLAYLRDLPA 896
Cdd:PRK09776 931 PLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMA 1010
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 897 DEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKA-LESLLGA 975
Cdd:PRK09776 1011 DYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLlLNSSYFA 1090
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
549-705 |
8.71e-42 |
|
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: 150.01 E-value: 8.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 549 YYDDLCDLYNRRSLTDIMQRTLQAP--SGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSG 626
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARArrSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879 627 DEFALLFTAlgqgyiTAKILAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMAKRAG 705
Cdd:cd01949 81 DEFAILLPG------TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSG 153
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
436-712 |
8.92e-41 |
|
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: 151.67 E-value: 8.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 436 LLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVS 515
Cdd:COG2199 2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 516 GVKDEEEEISHFVCSFHDITQEKETARHIERLAYYDDLCDLYNRRSLTDIMQRTLQ--APSGQWGALLLLDLDNFKSIND 593
Cdd:COG2199 82 ELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELAraRREGRPLALLLIDLDHFKRIND 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 594 SLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLFTALGQGyiTAKILAEHFARElmgIFRAPFDIGDHKLHCSA 673
Cdd:COG2199 162 TYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLE--EAEALAERLREA---LEQLPFELEGKELRVTV 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 780222879 674 SVGISLFSDDDKDHLVLMQQADTAVHMAKRAGQGNHIFF 712
Cdd:COG2199 237 SIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
546-712 |
2.13e-37 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 137.76 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 546 RLAYYDDLCDLYNRRSLTDIMQRTLQA--PSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLAR 623
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRaqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 624 TSGDEFALLFTAlgqgyITAKIlAEHFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMAKR 703
Cdd:smart00267 81 LGGDEFALLLPE-----TSLEE-AIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
|
....*....
gi 780222879 704 AGQGNHIFF 712
Cdd:smart00267 155 AGRNQVAVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
548-708 |
9.05e-37 |
|
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: 135.84 E-value: 9.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 548 AYYDDLCDLYNRRSLTDIMQRTLQ--APSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTS 625
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQraLREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 626 GDEFALLFTALGQGyiTAKILAEhFARELMGIFRAPFDIGDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMAKRAG 705
Cdd:pfam00990 81 GDEFAILLPETSLE--GAQELAE-RIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAG 157
|
...
gi 780222879 706 QGN 708
Cdd:pfam00990 158 RNR 160
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
733-969 |
2.67e-33 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 135.50 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 733 ALRNNELVLHYQPQYRVDNGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTAcAQYSFWLNNGL-AI 811
Cdd:PRK10551 271 GIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELI-ARDAAELQKVLpVG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 812 PHLSVNVSARQFHTAGFVQQVEYILrdTGVPPS--RLLLEITESVVLENRlESIARIRQLKALGLLISIDDFGTGYSSLA 889
Cdd:PRK10551 350 AKLGINISPAHLHSDSFKADVQRLL--ASLPADhfQIVLEITERDMVQEE-EATKLFAWLHSQGIEIAIDDFGTGHSALI 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 890 YLRDLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKAL 969
Cdd:PRK10551 427 YLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDF 506
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
547-707 |
4.94e-25 |
|
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: 102.42 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 547 LAYYDDLCDLYNRRSLTDIMQRTLQ--APSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLART 624
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKraRRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 625 SGDEFALLF--TALGQgyitAKILAEhfaRELMGIFRAPFDI-GDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVHMA 701
Cdd:TIGR00254 81 GGEEFVVILpgTPLED----ALSKAE---RLRDAINSKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQA 153
|
....*.
gi 780222879 702 KRAGQG 707
Cdd:TIGR00254 154 KKAGRN 159
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
413-546 |
9.10e-22 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 95.86 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 413 ELQRLANDDALRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQG 492
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 780222879 493 YWLGEEQCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKETARHIER 546
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRE 134
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
550-714 |
1.88e-17 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 83.96 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 550 YDDLCDLYNRRSLTDIMQRTLQAPSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEF 629
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEF 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 630 ALLF--TALGQGYITAKILaehfaRELmgIFRAPFDIGDHKLHCSASVGIS-LFSDDDKDhlVLMQQADTAVHMAKRAGQ 706
Cdd:PRK09894 211 IICLkaATDEEACRAGERI-----RQL--IANHAITHSDGRINITATFGVSrAFPEETLD--VVIGRADRAMYEGKQTGR 281
|
....*...
gi 780222879 707 GNHIFFSE 714
Cdd:PRK09894 282 NRVMFIDE 289
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
547-705 |
2.36e-17 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 86.11 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 547 LAYYDDLCDLYNRRSLtDIMQRTLQAPSGQWG---ALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLAR 623
Cdd:PRK09581 291 MAVTDGLTGLHNRRYF-DMHLKNLIERANERGkplSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 624 TSGDEFALLF--TALGQGYITAKILAEHFARElmgifraPFDI--GDHKLHCSASVGISLFSDDDKDHLVLMQQADTAVH 699
Cdd:PRK09581 370 YGGEEFVVVMpdTDIEDAIAVAERIRRKIAEE-------PFIIsdGKERLNVTVSIGVAELRPSGDTIEALIKRADKALY 442
|
....*.
gi 780222879 700 MAKRAG 705
Cdd:PRK09581 443 EAKNTG 448
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
547-721 |
3.68e-13 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 73.51 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 547 LAYYDDLCDLYNRRSLTDIMQR--TLQAPSGQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLART 624
Cdd:PRK15426 397 QAWHDPLTRLYNRGALFEKARAlaKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 625 SGDEFALLF--TALGQgyitAKILAEHFARELMG--IFRAPfdigDHKLHCSASVGIS-LFSDDDKDHLVLMQQADTAVH 699
Cdd:PRK15426 477 GGEEFCVVLpgASLAE----AAQVAERIRLRINEkeILVAK----STTIRISASLGVSsAEEDGDYDFEQLQSLADRRLY 548
|
170 180
....*....|....*....|..
gi 780222879 700 MAKRAGQgNHIFFSEAMAEKEK 721
Cdd:PRK15426 549 LAKQAGR-NRVCASDNAHEREV 569
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
443-536 |
8.62e-13 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 65.18 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 443 GIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQgyWLGEEQCLHREGHLFPVRLMVSGVKDEEE 522
Cdd:pfam13426 2 GRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAV--REFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
|
90
....*....|....
gi 780222879 523 EISHFVCSFHDITQ 536
Cdd:pfam13426 80 ELVGIIAILRDITE 93
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
424-548 |
1.81e-12 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 69.88 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 424 RLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPtyYGDTLKEEVIAAV-NRQGYWLGEEQCLH 502
Cdd:COG3852 8 LLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFP--EDSPLRELLERALaEGQPVTEREVTLRR 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 780222879 503 REGHLFPVRLMVSGVKDEEEEIsHFVCSFHDITQEKETARHIERLA 548
Cdd:COG3852 86 KDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERELRRAE 130
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
406-544 |
2.51e-12 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 68.13 E-value: 2.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 406 QRERAASELQRLANddalRLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEvI 485
Cdd:COG2202 124 ERKRAEEALRESEE----RLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLEL-L 198
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 486 AAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDE-EEEISHFVCSFHDITQEKETARHI 544
Cdd:COG2202 199 RRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRdGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
842-968 |
2.60e-12 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 69.83 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 842 PPSRLLLEITESVVLENRLesIARIRQLKALGLLISIDDFGTGYSSLAYLRDlpADEVKLDrsfiqtlvHSEQDKAIVKA 921
Cdd:COG3434 82 PPERVVLEILEDVEPDEEL--LEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID--------VLALDLEELAE 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 780222879 922 ILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKA 968
Cdd:COG3434 150 LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
517-679 |
2.69e-12 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 70.04 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 517 VKDEE-EEISHFVCSFHDITQEKE------TARHIE--RLAYYDDLCDLYNR---RSLTDIMQRTLQAPSGQwgALLLLD 584
Cdd:PRK09966 208 VSEERiAEFHRFALDFNSLLDEMEewqlrlQAKNAQllRTALHDPLTGLANRaafRSGINTLMNNSDARKTS--ALLFLD 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 585 LDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVLARTSGDEFALLFTALGQGYITAKILAehfarELMGIFRAPFDI 664
Cdd:PRK09966 286 GDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICS-----ALTQIFNLPFDL 360
|
170
....*....|....*.
gi 780222879 665 GD-HKLHCSASVGISL 679
Cdd:PRK09966 361 HNgHQTTMTLSIGYAM 376
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
431-542 |
9.41e-12 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 63.08 E-value: 9.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 431 NTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKE--EVIAAVNRQGYWlGEEQCLHREGHLF 508
Cdd:TIGR00229 11 SSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVREriERRLEGEPEPVS-EERRVRRKDGSEI 89
|
90 100 110
....*....|....*....|....*....|....
gi 780222879 509 PVRLMVSGVkDEEEEISHFVCSFHDITQEKETAR 542
Cdd:TIGR00229 90 WVEVSVSPI-RTNGGELGVVGIVRDITERKEAEE 122
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
431-534 |
1.02e-11 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 62.43 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 431 NTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHRE-GHLFP 509
Cdd:pfam00989 9 SLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPdGRPRH 88
|
90 100
....*....|....*....|....*
gi 780222879 510 VRLMVSGVKDEEEEISHFVCSFHDI 534
Cdd:pfam00989 89 VEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
432-534 |
2.24e-11 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 61.50 E-value: 2.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 432 THDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVR 511
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 780222879 512 LMVSGVKDEEEEISHFVCSFHDI 534
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
575-966 |
3.27e-11 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 67.19 E-value: 3.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 575 GQWGALLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQE--NLVLARTSGDEFALLftaLGQgyITAKiLAEHFAR 652
Cdd:PRK11059 257 GAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRypGALLARYSRSDFAVL---LPH--RSLK-EADSLAS 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 653 ELMGIFRA----PFDIGDHKLHcsasVGISLFSDDDkDHLVLMQQADtavhMAKRAGQ---GNHIFFSEAMAEKEKSKLS 725
Cdd:PRK11059 331 QLLKAVDAlpppKMLDRDDFLH----IGICAYRSGQ-STEQVMEEAE----MALRSAQlqgGNGWFVYDKAQLPEKGRGS 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 726 LN--NQLRDALRNNELVLHYQPQYRVDnGTLSGIEALLRWQKADGTMVPPGEFIPIAEETTLIQEIGYWVMKTACAQYSF 803
Cdd:PRK11059 402 VRwrTLLEQTLVRGGPRLYQQPAVTRD-GKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRY 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 804 WLNNglaipHLSVNVSARQFHTAGFVQQveyiLRDT--GVPPS---RLLLEITESVVLEN--RLESIARIrqLKALGLLI 876
Cdd:PRK11059 481 WPEE-----NLSINLSVDSLLSRAFQRW----LRDTllQCPRSqrkRLIFELAEADVCQHisRLRPVLRM--LRGLGCRL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 877 SIDDFGTGYSSLAYLRDLPADEVKLDRSFI---------QTLVHSeqdkaIVKAILDL-ARVFrftvtAEGVEEEEQLAV 946
Cdd:PRK11059 550 AVDQAGLTVVSTSYIKELNVELIKLHPSLVrnihkrtenQLFVRS-----LVGACAGTeTQVF-----ATGVESREEWQT 619
|
410 420
....*....|....*....|
gi 780222879 947 LKALGCQHYQGFLTSRPLPV 966
Cdd:PRK11059 620 LQELGVSGGQGDFFAESQPL 639
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
421-548 |
8.96e-11 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 65.38 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 421 DALRLAEVAF-----NTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVNRQGYWL 495
Cdd:COG5809 134 EALRESEEKFrlifnHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQ 213
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 780222879 496 GEEQCLHREGHLFPVRLMVSGVKDEEEEIShFVCSFHDITQEKETA---RHIERLA 548
Cdd:COG5809 214 GEVRFWTKDGRWRLLEASGAPIKKNGEVDG-IVIIFRDITERKKLEellRKSEKLS 268
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
530-707 |
9.13e-09 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 58.69 E-value: 9.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 530 SFHDITQEKETARHIERLAYYDDLCDLYNRRSLTDIMQRTLQAPSGQW--GALLLLDLDNFKSINDSLGHACGDLLLQAV 607
Cdd:PRK10245 187 SYQTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHrdATLLIIDIDHFKSINDTWGHDVGDEAIVAL 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 608 VVRLKSLPQENLVLARTSGDEFALLFTALGQGYITAKILAEHfarELMGIFRAPfdiGDHKLHCSASVGISLFSDDDKDH 687
Cdd:PRK10245 267 TRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVH---EGLNTLRLP---NAPQVTLRISVGVAPLNPQMSHY 340
|
170 180
....*....|....*....|
gi 780222879 688 LVLMQQADTAVHMAKRAGQG 707
Cdd:PRK10245 341 REWLKSADLALYKAKNAGRN 360
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
424-539 |
5.54e-08 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 56.52 E-value: 5.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 424 RLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKE--EVIAAVNRQGYWlgEEQCL 501
Cdd:COG5809 16 RFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREilKLLKEGESRDEL--EFELR 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 780222879 502 HREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQEKE 539
Cdd:COG5809 94 HKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKR 131
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
742-972 |
1.48e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 53.85 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 742 HYQPQYRVdNGTLSGIEALLRWQKAD--GTMVPPGEF---IPIAEETTLIQE----IGYWvmktacaqYSFWLNNGLAIp 812
Cdd:PRK11596 33 TFQPIYRT-SGRLMAIELLTAVTHPSnpSQRLSPERYfaeITVSHRLDVVKEqldlLAQW--------ADFFVRHGLLA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 813 hlSVNVSARQFHTagfVQQVEYILRDTGVPPsRLLLEITESVVLENRlESIARIRQLKALGLlisiDDFGTGYSSLAYLR 892
Cdd:PRK11596 103 --SVNIDGPTLIA---LRQQPAILRLIERLP-WLRFELVEHIRLPKD-SPFASMCEFGPLWL----DDFGTGMANFSALS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 893 DLPADEVKLDRSFIQTLVHSEQDKAIVKAILDLARVFRFTVTAEGVEEEEQLAVLKALGCQHYQGFLTSRPLPVKALESL 972
Cdd:PRK11596 172 EVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETLETL 251
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
431-571 |
1.50e-07 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 55.16 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 431 NTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALrptyygdtLKEEVIAAVNRQG-YWLGEEQCLHREGhlfp 509
Cdd:COG3829 19 SLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTEL--------IPNSPLLEVLKTGkPVTGVIQKTGGKG---- 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780222879 510 VRLMVSGVK-DEEEEISHFVCSFHDITQEKETARHIERLAYYDDLCDLYnrrSLTDI------MQRTLQ 571
Cdd:COG3829 87 KTVIVTAIPiFEDGEVIGAVETFRDITELKRLERKLREEELERGLSAKY---TFDDIigkspaMKELLE 152
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
406-542 |
2.54e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 48.13 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 406 QRERAASELqrlanDDALR-LAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEV 484
Cdd:PRK13560 191 ERKRAEERI-----DEALHfLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFAPAQPADDYQEAD 265
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 485 IAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVK--DEEEEISHFVCSFHDITQEKETAR 542
Cdd:PRK13560 266 AAKFDADGSQIIEAEFQNKDGRTRPVDVIFNHAEfdDKENHCAGLVGAITDISGRRAAER 325
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
411-548 |
2.75e-05 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 48.04 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 411 ASELQRLANDDALRLAEVAfnthDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPT------YYGDTLKE-- 482
Cdd:PRK11360 254 AQALRETRSLNELILESIA----DGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPntpfasPLLDTLEHgt 329
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 780222879 483 EVIAAvnrqgywlgEEQCLHREGHLfpvRLMVSG--VKDEEEEISHFVCSFHDITQEKETARHI---ERLA 548
Cdd:PRK11360 330 EHVDL---------EISFPGRDRTI---ELSVSTslLHNTHGEMIGALVIFSDLTERKRLQRRVarqERLA 388
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
424-489 |
3.54e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 42.39 E-value: 3.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780222879 424 RLAEVAFNTHDGLLVMDHGGIILKVNASFSRITGFASEEMLGLHIDALRPTYYGDTLKEEVIAAVN 489
Cdd:smart00091 2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
580-635 |
4.25e-05 |
|
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: 44.27 E-value: 4.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 780222879 580 LLLLDLDNFKSINDSLGHACGDLLLQAVVVRLKSLPQENLVL-ARTSGDEFALLFTA 635
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLkIKTIGDEFMVVSGL 60
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
445-568 |
1.75e-04 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 45.60 E-value: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 445 ILKVNASFSRITGFASEEMLGLHIDALRptyyGDTLKEEVIAAVNRQgywLGEEQCL-------HREGHLFPVRLMVSGV 517
Cdd:PRK13558 173 LIYINDAFERITGYSPDEVLGRNCRFLQ----GEDTNEERVAELREA---IDEERPTsvelrnyRKDGSTFWNQVDIAPI 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 780222879 518 KDEEEEISHFVCSFHDITQEKETARHIERlayyddlcdlyNRRSLTDIMQR 568
Cdd:PRK13558 246 RDEDGTVTHYVGFQTDVTERKEAELALQR-----------ERRKLQRLLER 285
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
446-548 |
3.10e-04 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 44.66 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 446 LKVNASFSRITGFASEEMLGLHIDALrpTY----YGDTLKEEVIAAVNRQGYWLgEEQCLHREGHLFPVRLMVSGVKDEE 521
Cdd:PRK09776 306 LQVNKALCQFLGYSQEELRGLTFQQL--TWpedlNKDLQQVEKLLSGEINSYSM-EKRYYRRDGEVVWALLAVSLVRDTD 382
|
90 100
....*....|....*....|....*..
gi 780222879 522 EEISHFVCSFHDITQEKETARHIERLA 548
Cdd:PRK09776 383 GTPLYFIAQIEDINELKRTEQVNERLM 409
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
445-529 |
8.75e-04 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 39.24 E-value: 8.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 445 ILKVNASFSRITGFASEEMLGL---HIDALRPtYYGDTLKEEVIAAVNRQGYWLGEEQCLHREGHLFPVRLMVSGVKDEE 521
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKgesWLDLVHP-DDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
....*...
gi 780222879 522 EEISHFVC 529
Cdd:pfam08447 80 GKPVRVIG 87
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
499-537 |
2.79e-03 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 36.39 E-value: 2.79e-03
10 20 30
....*....|....*....|....*....|....*....
gi 780222879 499 QCLHREGHLFPVRLMVSGVKDEEEEISHFVCSFHDITQE 537
Cdd:smart00086 5 RLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
122-253 |
5.89e-03 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 38.23 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780222879 122 QQQYDAMLESLKECLGADRLILWHYQAHgalgGEQLTPVFTLGVDALGAIRGDSRYIRALRARGALSFSEAAHQPMLSQH 201
Cdd:pfam01590 3 EEILQTILEELRELLGADRCALYLPDAD----GLEYLPPGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPRFLDP 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 780222879 202 Y-YLADANVCSRLDGALLEQEKLIGVLSLeYAESTLISDDTLQLVRHCARLLG 253
Cdd:pfam01590 79 LlLLRNFGIRSLLAVPIIDDGELLGVLVL-HHPRPPFTEEELELLEVLADQVA 130
|
|
|