|
Name |
Accession |
Description |
Interval |
E-value |
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
1-799 |
0e+00 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 1545.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 1 MKLTDADNAADGIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGG 80
Cdd:PRK11359 1 MKLTDADNAADGIFFPALEQNMMGAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 81 KARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQ 160
Cdd:PRK11359 81 KARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERRIVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 161 CNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQN 240
Cdd:PRK11359 161 CNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 241 LVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWS 320
Cdd:PRK11359 241 LVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEYQNAQSWS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 321 ATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDK 400
Cdd:PRK11359 321 ATIRQRDGAPAGTLQIKTSSGAETSAFIERVADISQHLAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 401 AVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK 480
Cdd:PRK11359 401 AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 481 PIMIDDKPFPLTLSIGISYDLGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLV 560
Cdd:PRK11359 481 PIMIDDKPFPLTLSIGISYDVGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 561 YQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALH 640
Cdd:PRK11359 561 YQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALH 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 641 FRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKID 720
Cdd:PRK11359 641 FRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKID 720
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 162135902 721 KSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLKI 799
Cdd:PRK11359 721 KSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLKI 799
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
192-793 |
4.28e-160 |
|
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: 4.28e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 192 ADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGNILAAMCSSPPF 271
Cdd:COG5001 67 LLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 272 HEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPAGILQIKTSSGAETSAFIERV 351
Cdd:COG5001 147 AALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 352 ADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWAD 427
Cdd:COG5001 227 LVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSgrrlALLFIDLDRFKEINDTLGHAAGD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 428 QALLEVVNRFREKLKPDQYLCRIEGTQFVLVsLEN--DVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DLGK 503
Cdd:COG5001 307 ELLREVARRLRACLREGDTVARLGGDEFAVL-LPDldDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALypDDGA 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 504 NRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHD 583
Cdd:COG5001 386 DAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQH 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 584 PLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQ 663
Cdd:COG5001 466 PERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSR 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 664 LTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSI 743
Cdd:COG5001 546 LELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIAL 625
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 162135902 744 GQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSS 793
Cdd:COG5001 626 AHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
293-791 |
3.02e-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: 335.22 E-value: 3.02e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 293 LFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHI 372
Cdd:COG2200 76 LLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLAL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 373 EQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEG 452
Cdd:COG2200 156 LDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGG 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 453 TQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGIS--YDLGKNRDYLLSTAHNAMDYIRKNGGNGWQFF 530
Cdd:COG2200 236 GGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGaaAPDDGADAALLLAAAAAAAAAAAGGGRGRVVF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 531 SPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRW 610
Cdd:COG2200 316 FAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRW 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 611 VIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDM 690
Cdd:COG2200 396 VLERALRQLARWPERGLDLR-LSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRAL 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 691 GVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHC 770
Cdd:COG2200 475 GVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGC 554
|
490 500
....*....|....*....|.
gi 162135902 771 RVIQGYFFSRPLPAEEIPGWM 791
Cdd:COG2200 555 DYAQGYLFGRPLPLEELEALL 575
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
547-786 |
5.26e-105 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 322.24 E-value: 5.26e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 547 ALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQN 626
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 627 IHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGL 706
Cdd:smart00052 83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 707 SRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
546-786 |
1.91e-104 |
|
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: 321.03 E-value: 1.91e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 546 AALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQ 625
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 626 NIHIPaLSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSG 705
Cdd:cd01948 81 GPDLR-LSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 706 LSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAE 785
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 162135902 786 E 786
Cdd:cd01948 240 E 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
364-799 |
9.50e-83 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 277.72 E-value: 9.50e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 364 EQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP---VVYLiGVDHIQDVIDSLGYAWADQALLEVVNRFREK 440
Cdd:PRK10060 225 EERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNqvgIVYL-DLDNFKKVNDAYGHMFGDQLLQDVSLAILSC 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 441 LKPDQYLCRIEGTQFVLVSLENDVSNI----TQIADELRnvvskpimiddKPFPLTL-------SIGISY--DLGKNRDY 507
Cdd:PRK10060 304 LEEDQTLARLGGDEFLVLASHTSQAALeamaSRILTRLR-----------LPFRIGLievytgcSIGIALapEHGDDSES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 508 LLSTAHNAMdYIRKNGGNGwQF--FSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAeTGELYGIEALARWHDPL 585
Cdd:PRK10060 373 LIRSADTAM-YTAKEGGRG-QFcvFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 586 HGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIpALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLT 665
Cdd:PRK10060 450 RGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINL-RVAVNVSARQLADQTIFTALKQALQELNFEYCPID 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 666 VEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQ 745
Cdd:PRK10060 529 VELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQ 608
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 162135902 746 SLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLKI 799
Cdd:PRK10060 609 ALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYLKRKL 662
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
537-791 |
5.00e-76 |
|
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: 256.00 E-value: 5.00e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 537 MVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEAC 616
Cdd:COG4943 265 LLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 617 RQLAEWRSQN--IHIpalSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDtEIFKRIQILRDMGVGL 694
Cdd:COG4943 345 RDLGDLLAADpdFHI---SINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPA-KARAVIAALREAGHRI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 695 SVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQ 774
Cdd:COG4943 421 AIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQ 500
|
250
....*....|....*..
gi 162135902 775 GYFFSRPLPAEEIPGWM 791
Cdd:COG4943 501 GWLFAKPLPAEEFIAWL 517
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
546-781 |
3.77e-73 |
|
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: 238.37 E-value: 3.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 546 AALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWrsQ 625
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL--Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 626 NIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSG 705
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162135902 706 LSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
364-786 |
8.83e-70 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 242.31 E-value: 8.83e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 364 EQEKSRQHIEQLIQ---FdPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREK 440
Cdd:PRK13561 217 QQLLQRQYEEQSRNatrF-PVSDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSV 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 441 LKPDQYLCRIEGTQFVLV--SLENDVSNITqIADELRNVVSKPIMIDDKPFPLTLSIGIS-YDLGKNRDYLLSTAHNAMD 517
Cdd:PRK13561 296 LSPRMVLAQISGYDFAIIanGVKEPWHAIT-LGQQVLTIINERLPIQRIQLRPSCSIGIAmFYGDLTAEQLYSRAISAAF 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 518 YIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPL 597
Cdd:PRK13561 375 TARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDR 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 598 AEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHD 677
Cdd:PRK13561 455 IESCGLMVTVGHWVLEESCRLLAAWQERGIMLP-LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 678 TEIFKRIQILRDMGVGLSVDDFGTGFSGLSRL---VSLPVTEIKIDKSFVDRCLTEKrilALLEAITSIGQSLNLTVVAE 754
Cdd:PRK13561 534 HAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAE 610
|
410 420 430
....*....|....*....|....*....|..
gi 162135902 755 GVETKEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
Cdd:PRK13561 611 GVETEAQRDWLLKAGVGIAQGFLFARALPIEI 642
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
366-786 |
1.46e-69 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 242.16 E-value: 1.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 366 EKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLV---DKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLK 442
Cdd:PRK11829 222 ADAYADMGRISHRFPVTELPNRSLFISLLEKEIassTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCID 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 443 PDQYLCRIEGTQFVLvsLENDV---SNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDLGKNR--DYLLSTAHNAMD 517
Cdd:PRK11829 302 DSDLLAQLSKTEFAV--LARGTrrsFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDtaESMMRNASTAMM 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 518 YIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPL 597
Cdd:PRK11829 380 AAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHF 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 598 AEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHD 677
Cdd:PRK11829 460 AEEEGMMVPLGNWVLEEACRILADWKARGVSLP-LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 678 TEIFKRIQILRDMGVGLSVDDFGTGFSGLSRL---VSLPVTEIKIDKSFVDRCLTEKrilALLEAITSIGQSLNLTVVAE 754
Cdd:PRK11829 539 DEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLPEDD---AIARIISCVSDVLKVRVMAE 615
|
410 420 430
....*....|....*....|....*....|....
gi 162135902 755 GVETKEQFEML--RKIHCrvIQGYFFSRPLPAEE 786
Cdd:PRK11829 616 GVETEEQRQWLleHGIQC--GQGFLFSPPLPRAE 647
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
374-530 |
3.28e-40 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 145.47 E-value: 3.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 374 QLIQFDPMTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCR 449
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQrqgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 450 IEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DLGKNRDYLLSTAHNAMDYIRKNGGNGW 527
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAypNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 162135902 528 QFF 530
Cdd:smart00267 161 AVY 163
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
541-792 |
6.58e-39 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 151.68 E-value: 6.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 541 RLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWV---IAEACR 617
Cdd:PRK10551 261 RMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLfelIARDAA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 618 QLAEwrsqniHIPA---LSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHD--TEIFkriQILRDMGV 692
Cdd:PRK10551 341 ELQK------VLPVgakLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEeaTKLF---AWLHSQGI 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 693 GLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRV 772
Cdd:PRK10551 412 EIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNF 491
|
250 260
....*....|....*....|
gi 162135902 773 IQGYFFSRPLPAEEIPGWMS 792
Cdd:PRK10551 492 LQGYWISRPLPLEDFVRWLK 511
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
379-787 |
1.47e-31 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 132.87 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 379 DPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454
Cdd:PRK09776 668 DALTHLANRASFEKQLRRLLQTVNSThqrhALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 455 FVLVSLENDVSNITQIADELRNVV-SKPIMIDDKPFPLTLSIGISYDLGKNRDY--LLSTAHNAMdYIRKNGGNG-WQFF 530
Cdd:PRK09776 748 FGLLLPDCNVESARFIATRIISAInDYHFPWEGRVYRVGASAGITLIDANNHQAseVMSQADIAC-YAAKNAGRGrVTVY 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 531 SPAMNEMVKER--LVLGAALKEAISNNQLKLVYQ--PQIFAETGELYgiEALARWHDPlHGH-VPPSRFIPLAEEIGEIE 605
Cdd:PRK09776 827 EPQQAAAHSEHraLSLAEQWRMIKENQLMMLAHGvaSPRIPEARNHW--LISLRLWDP-EGEiIDEGAFRPAAEDPALMH 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 606 NIGRWVIAEACRQLAEwrsqNIHIPALSV--NLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKR 683
Cdd:PRK09776 904 ALDRRVIHEFFRQAAK----AVASKGLSIalPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRL 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 684 IQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFV--------DRcltekrilALLEAITSIGQSLNLTVVAEG 755
Cdd:PRK09776 980 VQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVanlhgnlmDE--------MLISIIQGHAQRLGMKTIAGP 1051
|
410 420 430
....*....|....*....|....*....|..
gi 162135902 756 VETKEQFEMLRKIHCRVIQGYFFSRPLPAEEI 787
Cdd:PRK09776 1052 VELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
377-528 |
7.84e-31 |
|
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: 118.43 E-value: 7.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 377 QFDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEG 452
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162135902 453 TQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DLGKNRDYLLSTAHNAMDYIRKNGGNGWQ 528
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATypEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
277-530 |
1.25e-29 |
|
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: 118.93 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 277 IICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQ 356
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 357 HMAALAL------EQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWA 426
Cdd:COG2199 89 ALLLLLLaleditELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREgrplALLLIDLDHFKRINDTYGHAAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 427 DQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK-PIMIDDKPFPLTLSIGISY--DLGK 503
Cdd:COG2199 169 DEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALypEDGD 248
|
250 260
....*....|....*....|....*..
gi 162135902 504 NRDYLLSTAHNAMDYIRKNGGNGWQFF 530
Cdd:COG2199 249 SAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
17-256 |
1.04e-28 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 115.89 E-value: 1.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 17 ALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARvegmSRELQLEKK 96
Cdd:COG2202 16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW----RGELRNRRK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 97 DGSKIWTRFALSKV-SAEGKV-YYLALVRDAS----VEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFG 170
Cdd:COG2202 92 DGSLFWVELSISPVrDEDGEItGFVGIARDITerkrAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 171 YCISEASGMQPDTLLnIPEFPADNRIRLQQLLWKTARDQD-EFLLLTRTGEKIWIKASISPVYDVlAHLQNLVMTFSDIT 249
Cdd:COG2202 172 YSPEELLGKSLLDLL-HPEDRERLLELLRRLLEGGRESYElELRLKDGDGRWVWVEASAVPLRDG-GEVIGVLGIVRDIT 249
|
....*..
gi 162135902 250 EERQIRQ 256
Cdd:COG2202 250 ERKRAEE 256
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
378-525 |
8.96e-23 |
|
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: 95.40 E-value: 8.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 378 FDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGT 453
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQELQRALREgspvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162135902 454 QFVLVSLE---NDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DLGKNRDYLLSTAHNAMDYIRKNGGN 525
Cdd:pfam00990 83 EFAILLPEtslEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAypNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
128-258 |
5.78e-18 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 84.31 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 128 EMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGmQPDTLLNIPEFPADNRIRLQQLLWKTAR 207
Cdd:COG2202 3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLG-KTLRDLLPPEDDDEFLELLRAALAGGGV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 162135902 208 DQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITE----ERQIRQLE 258
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITErkraEEALRESE 136
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
26-137 |
2.04e-17 |
|
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: 78.87 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 26 VLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGgkaRVEGMSRELQLEKKDGSKIWTRF 105
Cdd:TIGR00229 17 IVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEG---EPEPVSEERRVRRKDGSEIWVEV 93
|
90 100 110
....*....|....*....|....*....|...
gi 162135902 106 ALSKVSAEGKV-YYLALVRDASvemaQKEQTRQ 137
Cdd:TIGR00229 94 SVSPIRTNGGElGVVGIVRDIT----ERKEAEE 122
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
365-784 |
2.87e-14 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 76.44 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 365 QEKSRqhIEQLIQ----FDPMTGLPNR----NNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVN- 435
Cdd:PRK11059 215 EERSR--FDTFIRsnafQDAKTGLGNRlffdNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINl 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 436 ------RFreklkPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK---PIMIDDKPFpltLSIGIS-YDLGKNR 505
Cdd:PRK11059 293 lstfvmRY-----PGALLARYSRSDFAVLLPHRSLKEADSLASQLLKAVDAlppPKMLDRDDF---LHIGICaYRSGQST 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 506 DYLLSTAHNAMDYIRKNGGNGWQFFSPAMNE-----MVKERLVLGAALkeaiSNNQLKLVYQPQIFAEtGELYGIEALAR 580
Cdd:PRK11059 365 EQVMEEAEMALRSAQLQGGNGWFVYDKAQLPekgrgSVRWRTLLEQTL----VRGGPRLYQQPAVTRD-GKVHHRELFCR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 581 WHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNihipaLSVNLSA---LH------FRSNQLPNQVS 651
Cdd:PRK11059 440 IRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEEN-----LSINLSVdslLSrafqrwLRDTLLQCPRS 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 652 DAMhawgidghQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRclTEK 731
Cdd:PRK11059 515 QRK--------RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRN--IHK 584
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 162135902 732 R------ILALLEAITSIGqslnLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPA 784
Cdd:PRK11059 585 RtenqlfVRSLVGACAGTE----TQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
659-781 |
5.00e-14 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 74.84 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 659 IDGHQLTVEITESMmmEHDTEIFKRIQILRDMGVGLSVDDFgTGFSGLSRLVSLpVTEIKIDksfVDRcLTEKRILALLE 738
Cdd:COG3434 81 LPPERVVLEILEDV--EPDEELLEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID---VLA-LDLEELAELVA 152
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 162135902 739 AItsigQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
Cdd:COG3434 153 RL----KRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
128-258 |
1.95e-13 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 72.57 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 128 EMAQKEQTRQLIIavDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEfpadnriRLQQLLWKTAR 207
Cdd:COG3852 1 ALRESEELLRAIL--DSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS-------PLRELLERALA 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 208 DQD-----EFLLLTRTGEKIWIKASISPVYDVLAHlQNLVMTFSDITE----ERQIRQLE 258
Cdd:COG3852 72 EGQpvterEVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITErkrlERELRRAE 130
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
369-524 |
4.43e-13 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 72.24 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 369 RQHIEQLIQF---DPMTGLPNRNNLHNYLDDLVDKAVS---PV-VYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKL 441
Cdd:PRK09581 282 RNNLEQSIEMavtDGLTGLHNRRYFDMHLKNLIERANErgkPLsLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNI 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 442 KPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK---PIMIDDKPFPLTLSIGISYDLGK--NRDYLLSTAHNAM 516
Cdd:PRK09581 362 RGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEepfIISDGKERLNVTVSIGVAELRPSgdTIEALIKRADKAL 441
|
....*...
gi 162135902 517 dYIRKNGG 524
Cdd:PRK09581 442 -YEAKNTG 448
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
145-248 |
1.44e-12 |
|
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: 64.58 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 145 LDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLnIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWI 224
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI-HPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWV 79
|
90 100
....*....|....*....|....
gi 162135902 225 KASISPVYDVLAHLQNLVMTFSDI 248
Cdd:cd00130 80 LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
28-257 |
2.17e-12 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 70.15 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 28 INENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGgkarvEGMSRELQLEKKDGSKIWTRFAL 107
Cdd:COG5805 50 VNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKG-----YDVVMIEQIYCKDGELIYVEVKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 108 SKVSAEGKVYYLALVRDAS----VEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGmqpDT 183
Cdd:COG5805 125 FPIYNQNGQAAILALRDITkkkkIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIG---KN 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162135902 184 LLNIpeFPADNRIRLQQLLWKTARDQDEFLL----LTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQL 257
Cdd:COG5805 202 LLEL--LHPCDKEEFKERIESITEVWQEFIIereiITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEEL 277
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
24-139 |
2.72e-12 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 69.10 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 24 GAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDlrPAHPEYIRHNREGGKARVEgmsRELQLEKKDGSKIWT 103
Cdd:COG3852 19 AVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED--SPLRELLERALAEGQPVTE---REVTLRRKDGEERPV 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 162135902 104 RFALSKVS-AEGKVYYLALVRDASvemAQKEQTRQLI 139
Cdd:COG3852 94 DVSVSPLRdAEGEGGVLLVLRDIT---ERKRLERELR 127
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
23-124 |
5.35e-12 |
|
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: 63.04 E-value: 5.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 23 MGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGkarvEGMSRELQLEKKDGSKIW 102
Cdd:cd00130 3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGG----EPVTLEVRLRRKDGSVIW 78
|
90 100
....*....|....*....|....
gi 162135902 103 --TRFALSKVSAEGKVYYLALVRD 124
Cdd:cd00130 79 vlVSLTPIRDEGGEVIGLLGVVRD 102
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
379-526 |
5.70e-12 |
|
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: 64.67 E-value: 5.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 379 DPMTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQ 454
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARrfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162135902 455 FVLVSLENDVSNITQIADELRNVV-SKPIMIDDKP-FPLTLSIGISYDLGKNRDY--LLSTAHNAMDYIRKNGGNG 526
Cdd:TIGR00254 85 FVVILPGTPLEDALSKAERLRDAInSKPIEVAGSEtLTVTVSIGVACYPGHGLTLeeLLKRADEALYQAKKAGRNR 160
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
534-788 |
9.52e-12 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 66.18 E-value: 9.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 534 MNEMVKERLVLGAALKEAISNN------QLKLVYQPqIFAETGELYGIEALARWHDPLHghvpPSRFIPLAEEIGEIENI 607
Cdd:PRK11596 1 MIRQVIQRISLPEASIESLQERrywlqcERAYTFQP-IYRTSGRLMAIELLTAVTHPSN----PSQRLSPERYFAEITVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 608 GRW-VIAEACRQLAEWRSQNIHIPAL-SVNL--SALHFRSNQLPNQVSDAMHAWgidghqLTVEITESMMMEHDtEIFKR 683
Cdd:PRK11596 76 HRLdVVKEQLDLLAQWADFFVRHGLLaSVNIdgPTLIALRQQPAILRLIERLPW------LRFELVEHIRLPKD-SPFAS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 684 IQILrdmgVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKS-FVDRCLTEK-RIL--ALLEAITSIGQSlnltVVAEGVETK 759
Cdd:PRK11596 149 MCEF----GPLWLDDFGTGMANFSALSEVRYDYIKVARElFIMLRQSEEgRNLfsQLLHLMNRYCRG----VIVEGVETP 220
|
250 260
....*....|....*....|....*....
gi 162135902 760 EQFEMLRKIHCRVIQGYFFSRPLPAEEIP 788
Cdd:PRK11596 221 EEWRDVQRSPAFAAQGYFLSRPAPFETLE 249
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
124-377 |
5.02e-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: 65.77 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 124 DASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMqPDTLLNIPEFPADNRIRLQQLLW 203
Cdd:COG5809 3 SSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGT-NILDFLHPDDEKELREILKLLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 204 KTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITE----ERQIRQLEGNILAAMCSSPpfheMGEIIC 279
Cdd:COG5809 82 GESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITErkrmEEALRESEEKFRLIFNHSP----DGIIVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 280 RNIESVL--NESHVSLFALRNGMPIHWASSS--HGAEIQNAQSWSATIRQRDGAPAGILQIKTSSG----AETSAFiERV 351
Cdd:COG5809 158 DLDGRIIyaNPAACKLLGISIEELIGKSILEliHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGrwrlLEASGA-PIK 236
|
250 260
....*....|....*....|....*.
gi 162135902 352 ADISQHMAALALEQEKSRQHIEQLIQ 377
Cdd:COG5809 237 KNGEVDGIVIIFRDITERKKLEELLR 262
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
17-78 |
4.35e-10 |
|
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: 56.25 E-value: 4.35e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 162135902 17 ALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNRE 78
Cdd:smart00091 6 ILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
157-250 |
4.37e-10 |
|
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: 57.09 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 157 HIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQllwKTARDQDEFLLLTRTGEKIWIKASISPVYDVLA 236
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
|
90
....*....|....
gi 162135902 237 HLQNLVMTFSDITE 250
Cdd:pfam13426 80 ELVGIIAILRDITE 93
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
31-124 |
7.77e-10 |
|
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: 56.32 E-value: 7.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 31 NDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPrdlRPAHPEYIRHNREGGKARVEGmsrELQLEKKDGSKIWTRFALSKV 110
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREGKAVREF---EVVLYRKDGEPFPVLVSLAPI 74
|
90
....*....|....*.
gi 162135902 111 SAEGK--VYYLALVRD 124
Cdd:pfam13426 75 RDDGGelVGIIAILRD 90
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
142-253 |
8.20e-09 |
|
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 is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 53.96 E-value: 8.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 142 VDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLniPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEK 221
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELL--PPEDAARLERALRRALEGEEPIDFLEELLLNGEE 78
|
90 100 110
....*....|....*....|....*....|..
gi 162135902 222 IWIKASISPVYDVLAHLQNLVMTFSDITEERQ 253
Cdd:pfam08448 79 RHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
141-256 |
3.05e-08 |
|
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: 52.68 E-value: 3.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 141 AVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNiPEFPADNRIRLQQLLWKTARD-QDEFLLLTRTG 219
Cdd:TIGR00229 8 IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIP-EEDREEVRERIERRLEGEPEPvSEERRVRRKDG 86
|
90 100 110
....*....|....*....|....*....|....*..
gi 162135902 220 EKIWIKASISPVYDVLAHLqNLVMTFSDITEERQIRQ 256
Cdd:TIGR00229 87 SEIWVEVSVSPIRTNGGEL-GVVGIVRDITERKEAEE 122
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
7-124 |
1.07e-07 |
|
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: 50.88 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 7 DNAADGIFfpaleqnmmgavLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKarvEG 86
Cdd:pfam00989 8 ESLPDGIF------------VVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGE---ES 72
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 162135902 87 MSRELQLEKKDGSKIWTR-FALSKVSAEGKV-YYLALVRD 124
Cdd:pfam00989 73 RGFEVSFRVPDGRPRHVEvRASPVRDAGGEIlGFLGVLRD 112
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
142-248 |
1.58e-07 |
|
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: 50.49 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 142 VDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMqpdtLLNIPEFPADNRIRlQQLLWKTARDQD-----EFLLLT 216
Cdd:pfam00989 7 LESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGK----SLLDLIPEEDDAEV-AELLRQALLQGEesrgfEVSFRV 81
|
90 100 110
....*....|....*....|....*....|..
gi 162135902 217 RTGEKIWIKASISPVYDVLAHLQNLVMTFSDI 248
Cdd:pfam00989 82 PDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
130-258 |
2.06e-07 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 54.20 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 130 AQKEQTRQLIIAV-DHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLnipefpadNRIRLQQLLWKTARD 208
Cdd:COG5000 83 EELEERRRYLETIlENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELL--------PELDLAELLREALER 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 162135902 209 QDEFLLLTRTGEKIWIKASISPVYDvlahlQNLVMTFSDITEERQIRQLE 258
Cdd:COG5000 155 GWQEEIELTRDGRRTLLVRASPLRD-----DGYVIVFDDITELLRAERLA 199
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
5-144 |
1.06e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 51.74 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 5 DADNAADGIFFPALEQNMMGAVLIN--ENDE-VMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRhnreGGK 81
Cdd:PRK13559 36 DFRGASGRLFEQAMEQTRMAMCITDphQPDLpIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIR----AAI 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 162135902 82 ARVEGMSRELQLEKKDGSKIWTRFALSKVSAE-GKV-YYLALVRDAS---VEMAQKEQTRQLIIAVDH 144
Cdd:PRK13559 112 AAEREIVVELLNYRKDGEPFWNALHLGPVYGEdGRLlYFFGSQWDVTdirAVRALEAHERRLAREVDH 179
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
7-256 |
9.42e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 49.29 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 7 DNAADGIFFpaleqnmmgavlINENDEVMFFNPAAEKLWGYKREEVIGNNIdmlipRDLRPAHPEYIRHNREGGKARVEG 86
Cdd:PRK13560 211 DNIADPAFW------------KDEDAKVFGCNDAACLACGFRREEIIGMSI-----HDFAPAQPADDYQEADAAKFDADG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 87 MS-RELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVI--------VLDPERH 157
Cdd:PRK13560 274 SQiIEAEFQNKDGRTRPVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIeaapiaaiGLDADGN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 158 IVQCNRAFTE-MFGYCISEAS-----GMQPD-----TLLNIPEFPADNRIRLQQL--LWKTAR-----DQDEFLLLTRTG 219
Cdd:PRK13560 354 ICFVNNNAAErMLGWSAAEVMgkplpGMDPElneefWCGDFQEWYPDGRPMAFDAcpMAKTIKggkifDGQEVLIEREDD 433
|
250 260 270
....*....|....*....|....*....|....*..
gi 162135902 220 EKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQ 256
Cdd:PRK13560 434 GPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEE 470
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
14-137 |
1.28e-05 |
|
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: 48.43 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 14 FFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEgmsrELQL 93
Cdd:COG5809 143 FRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQG----EVRF 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 162135902 94 EKKDGSKIWTRFALSKVSAEGKVY-YLALVRDASVEMAQKEQTRQ 137
Cdd:COG5809 219 WTKDGRWRLLEASGAPIKKNGEVDgIVIIFRDITERKKLEELLRK 263
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
136-202 |
1.34e-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: 43.54 E-value: 1.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 162135902 136 RQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLnIPEFPADNRIRLQQLL 202
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI-HPEDRERVQEALQRLL 66
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
379-524 |
1.61e-05 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 47.37 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 379 DPMTGLPNRNNLHNYLD-DLVDKAVSPV-VYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFV 456
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDhQLRNREPQNLyLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFI 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 457 LVSLENDVSNITQIADELRNVVS-KPIMIDDKPFPLTLSIGIS-YDLGKNRDYLLSTAHNAMdYIRKNGG 524
Cdd:PRK09894 212 ICLKAATDEEACRAGERIRQLIAnHAITHSDGRINITATFGVSrAFPEETLDVVIGRADRAM-YEGKQTG 280
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
4-143 |
3.93e-05 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 46.97 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 4 TDADNAADGIFFPALEQNMMGAVLI--NENDE-VMFFNPAAEKLWGYKREEVIGNNIDMLIPRDlrpAHPEYIRHNREGG 80
Cdd:PRK13557 22 GDVSDHRSDIFFAAVETTRMPMIVTdpNQPDNpIVFANRAFLEMTGYAAEEIIGNNCRFLQGPE---TDRATVAEVRDAI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 162135902 81 KARVEgMSRELQLEKKDGSKIWTRFALSKV-SAEGK-VYYLA------LVRDA--SVEMAQK-EQTRQLI--IAVD 143
Cdd:PRK13557 99 AERRE-IATEILNYRKDGSSFWNALFVSPVyNDAGDlVYFFGsqldvsRRRDAedALRQAQKmEALGQLTggIAHD 173
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
141-200 |
5.61e-05 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 41.77 E-value: 5.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 141 AVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQ 200
Cdd:pfam13188 6 LFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALELLRELR 65
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
211-251 |
5.63e-05 |
|
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: 41.01 E-value: 5.63e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 162135902 211 EFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEE 251
Cdd:smart00086 3 EYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
128-256 |
6.97e-05 |
|
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: 45.92 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 128 EMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLlnIPEFPadnrirLQQLLwKTAR 207
Cdd:COG3829 3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTEL--IPNSP------LLEVL-KTGK 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 162135902 208 DQDEFLLLTRTGEKIWIkASISPVYD----VLAhlqnlVMTFSDITEERQIRQ 256
Cdd:COG3829 74 PVTGVIQKTGGKGKTVI-VTAIPIFEdgevIGA-----VETFRDITELKRLER 120
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
349-498 |
1.21e-04 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 45.38 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 349 ERVADI---SQHMAALALEQEKSRQHIE----QLIQ---FDPMTGLPNRNNLHNYLDDLVD----KAVSPVVYLIGvDHI 414
Cdd:PRK09966 211 ERIAEFhrfALDFNSLLDEMEEWQLRLQaknaQLLRtalHDPLTGLANRAAFRSGINTLMNnsdaRKTSALLFLDG-DNF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 415 QDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLE-NDVSNITQIADELRNVVSKPIMIDD-KPFPLT 492
Cdd:PRK09966 290 KYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDvQSESEVQQICSALTQIFNLPFDLHNgHQTTMT 369
|
....*.
gi 162135902 493 LSIGIS 498
Cdd:PRK09966 370 LSIGYA 375
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
7-62 |
1.29e-04 |
|
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: 45.15 E-value: 1.29e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 162135902 7 DNAADGIFfpaleqnmmgavLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIP 62
Cdd:COG3829 18 DSLDDGII------------VVDADGRITYVNRAAERILGLPREEVIGKNVTELIP 61
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
30-146 |
4.74e-04 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 43.67 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 30 ENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDlrpAHPEYIRHNREGGKARvEGMSRELQLEKKDGSKIWTRFALSK 109
Cdd:PRK13558 169 PDEPLIYINDAFERITGYSPDEVLGRNCRFLQGED---TNEERVAELREAIDEE-RPTSVELRNYRKDGSTFWNQVDIAP 244
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 162135902 110 VSAE-GKV-YYLALVRDAS----VEMAQKEQTRQLIIAVDHLD 146
Cdd:PRK13558 245 IRDEdGTVtHYVGFQTDVTerkeAELALQRERRKLQRLLERVE 287
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
142-255 |
8.95e-04 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 42.80 E-value: 8.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 142 VDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNipefPADNRIRLQQLLWKTARDQDEFLLLTRT--G 219
Cdd:COG5805 40 LENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLE----KEYHYRVKTRIERLQKGYDVVMIEQIYCkdG 115
|
90 100 110
....*....|....*....|....*....|....*.
gi 162135902 220 EKIWIKASISPVYDVLAHLQnlVMTFSDITEERQIR 255
Cdd:COG5805 116 ELIYVEVKLFPIYNQNGQAA--ILALRDITKKKKIE 149
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
133-258 |
1.56e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 41.73 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 133 EQTRQLIIAVD--HLDRPvivldperhIVQCNRAFTEMFGYCISEASGMQPDTLlnipEFPADNRIRLQQLLWKTARDQD 210
Cdd:PRK13559 50 EQTRMAMCITDphQPDLP---------IVLANQAFLDLTGYAAEEVVGRNCRFL----QGAATDPIAVAKIRAAIAAERE 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 162135902 211 ---EFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLE 258
Cdd:PRK13559 117 ivvELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAVRALE 167
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
158-233 |
2.43e-03 |
|
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: 37.70 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 158 IVQCNRAFTEMFGYCISEASGMqPDTLLNIPeFPADnRIRLQQLLWKTARDQD----EFLLLTRTGEKIWIKASISPVYD 233
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGK-GESWLDLV-HPDD-RERVREALWEALKGGEpysgEYRIRRKDGEYRWVEARARPIRD 77
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
141-253 |
2.69e-03 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 41.19 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 141 AVDHLDRPVIVLDPERH---IVQCNRAFTEMFGYCISEASG-----MQ-PDTllnipefpadNRIRLQQLLWKTARDQD- 210
Cdd:PRK13557 35 AVETTRMPMIVTDPNQPdnpIVFANRAFLEMTGYAAEEIIGnncrfLQgPET----------DRATVAEVRDAIAERREi 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 162135902 211 --EFLLLTRTGEKIWIKASISPVYDVLAhlqNLVMTFS---DITEERQ 253
Cdd:PRK13557 105 atEILNYRKDGSSFWNALFVSPVYNDAG---DLVYFFGsqlDVSRRRD 149
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
137-258 |
4.82e-03 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 40.34 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 162135902 137 QLIIAvdHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLlnipeFPADNRIR--LQQLLWKTARDQDEFLL 214
Cdd:PRK11360 265 ELILE--SIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSEL-----FPPNTPFAspLLDTLEHGTEHVDLEIS 337
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 162135902 215 LTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITE----ERQIRQLE 258
Cdd:PRK11360 338 FPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTErkrlQRRVARQE 385
|
|
| |
