|
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: 1539.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 1 MKLTDADNAADGIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGG 80
Cdd:PRK11359 1 MKLTDADNAADGIFFPALEQNMMGAVLINENDEVLFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 81 KARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQ 160
Cdd:PRK11359 81 KARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERRIVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 161 CNRAFTEMFGYCINEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQN 240
Cdd:PRK11359 161 CNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 241 LVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEVQNAQSWS 320
Cdd:PRK11359 241 LVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEYQNAQSWS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 321 ATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDK 400
Cdd:PRK11359 321 ATIRQRDGAPAGTLQIKTSSGAETSAFIERVADISQHLAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 401 AVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGASFVLVSLENDVSNITQIADELRNVVSK 480
Cdd:PRK11359 401 AVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSK 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 481 PIMIDDKPFPLTLSIGISYDVGKNRDYLLSTAHNAMDFIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLV 560
Cdd:PRK11359 481 PIMIDDKPFPLTLSIGISYDVGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLV 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 561 YQPQIFAETGELYGIEALARWYDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALH 640
Cdd:PRK11359 561 YQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALH 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 641 FRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGIGLSVDDFGTGFSGLSRLVSLPVTEIKID 720
Cdd:PRK11359 641 FRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKID 720
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 485653290 721 KSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGIETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLKI 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 |
1.32e-157 |
|
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: 474.65 E-value: 1.32e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 192 ADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGNILAAMCSSPPF 271
Cdd:COG5001 67 LLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 272 HEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEVQNAQSWSATIRQRDGAPAGILQIKTSSGAETSAFIERV 351
Cdd:COG5001 147 AALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 352 ADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWAD 427
Cdd:COG5001 227 LVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSgrrlALLFIDLDRFKEINDTLGHAAGD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 428 QALLEVVNRFREKLKPDQYLCRIEGASFVLVsLEN--DVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGK 503
Cdd:COG5001 307 ELLREVARRLRACLREGDTVARLGGDEFAVL-LPDldDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALypDDGA 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 504 NRDYLLSTAHNAMDFIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWYD 583
Cdd:COG5001 386 DAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQH 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 584 PLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQ 663
Cdd:COG5001 466 PERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSR 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 664 LTVEITESMMMEHDTEIFKRIQILRDMGIGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSI 743
Cdd:COG5001 546 LELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIAL 625
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 485653290 744 GQSLNLTVVAEGIETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSS 793
Cdd:COG5001 626 AHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
320-791 |
5.00e-104 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 332.13 E-value: 5.00e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 320 SATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVD 399
Cdd:COG2200 103 LALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 400 KAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGASFVLVSLENDVSNITQIADELRNVVS 479
Cdd:COG2200 183 ALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 480 KPIMIDDKPFPLTLSIGIS--YDVGKNRDYLLSTAHNAMDFIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQL 557
Cdd:COG2200 263 LEPLLLGGGLVVVASSGGGaaAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRLALESELREALEEGEL 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 558 KLVYQPQIFAETGELYGIEALARWYDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPaLSVNLS 637
Cdd:COG2200 343 RLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLR-LSVNLS 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 638 ALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGIGLSVDDFGTGFSGLSRLVSLPVTEI 717
Cdd:COG2200 422 ARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYL 501
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 485653290 718 KIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGIETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWM 791
Cdd:COG2200 502 KIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALL 575
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
547-786 |
5.78e-104 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 319.55 E-value: 5.78e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 547 ALKEAISNNQLKLVYQPQIFAETGELYGIEALARWYDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQN 626
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 627 IHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGIGLSVDDFGTGFSGL 706
Cdd:smart00052 83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 707 SRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGIETKEQFEMLRKIHCRVIQGYFFSRPLPAEE 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 |
1.70e-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: 318.34 E-value: 1.70e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 546 AALKEAISNNQLKLVYQPQIFAETGELYGIEALARWYDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQ 625
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 626 NIHIPaLSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGIGLSVDDFGTGFSG 705
Cdd:cd01948 81 GPDLR-LSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 706 LSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGIETKEQFEMLRKIHCRVIQGYFFSRPLPAE 785
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 485653290 786 E 786
Cdd:cd01948 240 E 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
364-799 |
1.12e-80 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 272.33 E-value: 1.12e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 364 EQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP---VVYLiGVDHIQDVIDSLGYAWADQALLEVVNRFREK 440
Cdd:PRK10060 225 EERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNqvgIVYL-DLDNFKKVNDAYGHMFGDQLLQDVSLAILSC 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 441 LKPDQYLCRIEGASFVLVSLENDVSNI----TQIADELRnvvskpimiddKPFPLTL-------SIGISY--DVGKNRDY 507
Cdd:PRK10060 304 LEEDQTLARLGGDEFLVLASHTSQAALeamaSRILTRLR-----------LPFRIGLievytgcSIGIALapEHGDDSES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 508 LLSTAHNAMdFIRKNGGNGwQF--FSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAeTGELYGIEALARWYDPL 585
Cdd:PRK10060 373 LIRSADTAM-YTAKEGGRG-QFcvFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 586 HGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIpALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLT 665
Cdd:PRK10060 450 RGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINL-RVAVNVSARQLADQTIFTALKQALQELNFEYCPID 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 666 VEITESMMMEHDTEIFKRIQILRDMGIGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQ 745
Cdd:PRK10060 529 VELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQ 608
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 485653290 746 SLNLTVVAEGIETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLKI 799
Cdd:PRK10060 609 ALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYLKRKL 662
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
537-791 |
2.41e-75 |
|
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: 254.07 E-value: 2.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 537 MVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWYDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEAC 616
Cdd:COG4943 265 LLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 617 RQLAEWRSQN--IHIpalSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDtEIFKRIQILRDMGIGL 694
Cdd:COG4943 345 RDLGDLLAADpdFHI---SINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPA-KARAVIAALREAGHRI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 695 SVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGIETKEQFEMLRKIHCRVIQ 774
Cdd:COG4943 421 AIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQ 500
|
250
....*....|....*..
gi 485653290 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 |
1.74e-72 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 236.83 E-value: 1.74e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 546 AALKEAISNNQLKLVYQPQIFAETGELYGIEALARWYDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWrsQ 625
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL--Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 626 NIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGIGLSVDDFGTGFSG 705
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485653290 706 LSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGIETKEQFEMLRKIHCRVIQGYFFSRP 781
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
364-786 |
1.06e-68 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 239.23 E-value: 1.06e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 364 EQEKSRQHIEQLIQ---FdPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREK 440
Cdd:PRK13561 217 QQLLQRQYEEQSRNatrF-PVSDLPNKALLMALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSV 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 441 LKPDQYLCRIEGASFVLV--SLENDVSNITqIADELRNVVSKPIMIDDKPFPLTLSIGIS-YDVGKNRDYLLSTAHNAMD 517
Cdd:PRK13561 296 LSPRMVLAQISGYDFAIIanGVKEPWHAIT-LGQQVLTIINERLPIQRIQLRPSCSIGIAmFYGDLTAEQLYSRAISAAF 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 518 FIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWYDPLHGHVPPSRFIPL 597
Cdd:PRK13561 375 TARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDR 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 598 AEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHD 677
Cdd:PRK13561 455 IESCGLMVTVGHWVLEESCRLLAAWQERGIMLP-LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDP 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 678 TEIFKRIQILRDMGIGLSVDDFGTGFSGLSRL---VSLPVTEIKIDKSFVDRCLTEKrilALLEAITSIGQSLNLTVVAE 754
Cdd:PRK13561 534 HAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAE 610
|
410 420 430
....*....|....*....|....*....|..
gi 485653290 755 GIETKEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
Cdd:PRK13561 611 GVETEAQRDWLLKAGVGIAQGFLFARALPIEI 642
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
366-786 |
1.34e-67 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 236.38 E-value: 1.34e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 366 EKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLV---DKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLK 442
Cdd:PRK11829 222 ADAYADMGRISHRFPVTELPNRSLFISLLEKEIassTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCID 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 443 PDQYLCRIEGASFVLvsLENDV---SNITQIADELRNVVSKPIMIDDKPFPLTLSIGI-----SYDVGKNrdyLLSTAHN 514
Cdd:PRK11829 302 DSDLLAQLSKTEFAV--LARGTrrsFPAMQLARRIMSQVTQPLFFDEITLRPSASIGItryqaQQDTAES---MMRNAST 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 515 AMDFIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWYDPLHGHVPPSRF 594
Cdd:PRK11829 377 AMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGF 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 595 IPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMM 674
Cdd:PRK11829 457 VHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLP-LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQI 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 675 EHDTEIFKRIQILRDMGIGLSVDDFGTGFSGLSRL---VSLPVTEIKIDKSFVDRCLTEKrilALLEAITSIGQSLNLTV 751
Cdd:PRK11829 536 QDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLPEDD---AIARIISCVSDVLKVRV 612
|
410 420 430
....*....|....*....|....*....|....*..
gi 485653290 752 VAEGIETKEQFEML--RKIHCrvIQGYFFSRPLPAEE 786
Cdd:PRK11829 613 MAEGVETEEQRQWLleHGIQC--GQGFLFSPPLPRAE 647
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
541-792 |
7.57e-39 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 151.68 E-value: 7.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 541 RLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWYDPLHGHVPPSRFIPLAEEIGEIENIGRWV---IAEACR 617
Cdd:PRK10551 261 RMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLfelIARDAA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 618 QLAEwrsqniHIPA---LSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHD--TEIFkriQILRDMGI 692
Cdd:PRK10551 341 ELQK------VLPVgakLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEeaTKLF---AWLHSQGI 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 693 GLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGIETKEQFEMLRKIHCRV 772
Cdd:PRK10551 412 EIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNF 491
|
250 260
....*....|....*....|
gi 485653290 773 IQGYFFSRPLPAEEIPGWMS 792
Cdd:PRK10551 492 LQGYWISRPLPLEDFVRWLK 511
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
374-530 |
1.12e-37 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 138.15 E-value: 1.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 374 QLIQFDPMTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCR 449
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQrqgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 450 IEGASFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDFIRKNGGNGW 527
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAypNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 485653290 528 QFF 530
Cdd:smart00267 161 AVY 163
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
379-787 |
1.29e-30 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 129.79 E-value: 1.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 379 DPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGAS 454
Cdd:PRK09776 668 DALTHLANRASFEKQLRRLLQTVNSThqrhALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 455 FVLVSLENDVSNITQIADELRNVV-SKPIMIDDKPFPLTLSIGISYDVGKNRDY--LLSTAHNAMdFIRKNGGNG-WQFF 530
Cdd:PRK09776 748 FGLLLPDCNVESARFIATRIISAInDYHFPWEGRVYRVGASAGITLIDANNHQAseVMSQADIAC-YAAKNAGRGrVTVY 826
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 531 SPAMNEMVKER--LVLGAALKEAISNNQLKLVYQ--PQIFAETGELYgiEALARWYDPlHGH-VPPSRFIPLAEEIGEIE 605
Cdd:PRK09776 827 EPQQAAAHSEHraLSLAEQWRMIKENQLMMLAHGvaSPRIPEARNHW--LISLRLWDP-EGEiIDEGAFRPAAEDPALMH 903
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 606 NIGRWVIAEACRQLAEwrsqNIHIPALSV--NLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKR 683
Cdd:PRK09776 904 ALDRRVIHEFFRQAAK----AVASKGLSIalPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRL 979
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 684 IQILRDMGIGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFV--------DRcltekrilALLEAITSIGQSLNLTVVAEG 755
Cdd:PRK09776 980 VQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVanlhgnlmDE--------MLISIIQGHAQRLGMKTIAGP 1051
|
410 420 430
....*....|....*....|....*....|..
gi 485653290 756 IETKEQFEMLRKIHCRVIQGYFFSRPLPAEEI 787
Cdd:PRK09776 1052 VELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
285-530 |
1.34e-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: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 285 VLNESHVSLFALRNGMPIHWASSSHGAEVQNAQSWSATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQHMAALAL- 363
Cdd:COG2199 14 LLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 364 --------EQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWADQALL 431
Cdd:COG2199 94 llaleditELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREgrplALLLIDLDHFKRINDTYGHAAGDEVLK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 432 EVVNRFREKLKPDQYLCRIEGASFVLVSLENDVSNITQIADELRNVVSK-PIMIDDKPFPLTLSIGISY--DVGKNRDYL 508
Cdd:COG2199 174 EVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALypEDGDSAEEL 253
|
250 260
....*....|....*....|..
gi 485653290 509 LSTAHNAMDFIRKNGGNGWQFF 530
Cdd:COG2199 254 LRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
377-528 |
5.50e-29 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 113.42 E-value: 5.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 377 QFDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEG 452
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSgrplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485653290 453 ASFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDFIRKNGGNGWQ 528
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATypEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
17-256 |
1.33e-28 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 115.51 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 17 ALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARvegmSRELQLEKK 96
Cdd:COG2202 16 LVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVW----RGELRNRRK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 97 DGSKIWTRFALSKV-SAEGKV-YYLALVRDAS----VEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFG 170
Cdd:COG2202 92 DGSLFWVELSISPVrDEDGEItGFVGIARDITerkrAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 171 YCINEASGMQPDTLLnIPEFPADNRIRLQQLLWKTARDQD-EFLLLTRTGEKIWIKASISPVYDVlAHLQNLVMTFSDIT 249
Cdd:COG2202 172 YSPEELLGKSLLDLL-HPEDRERLLELLRRLLEGGRESYElELRLKDGDGRWVWVEASAVPLRDG-GEVIGVLGIVRDIT 249
|
....*..
gi 485653290 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 |
1.45e-21 |
|
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: 91.93 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 378 FDPMTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGA 453
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQELQRALREgspvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485653290 454 SFVLVSLE---NDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDVGKNRDY--LLSTAHNAMDFIRKNGGN 525
Cdd:pfam00990 83 EFAILLPEtslEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPedLLKRADTALYQAKQAGRN 159
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
128-258 |
7.82e-18 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 83.92 E-value: 7.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 128 EMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGmQPDTLLNIPEFPADNRIRLQQLLWKTAR 207
Cdd:COG2202 3 EEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLG-KTLRDLLPPEDDDEFLELLRAALAGGGV 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 485653290 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 |
2.12e-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: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 26 VLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGgkaRVEGMSRELQLEKKDGSKIWTRF 105
Cdd:TIGR00229 17 IVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEG---EPEPVSEERRVRRKDGSEIWVEV 93
|
90 100 110
....*....|....*....|....*....|...
gi 485653290 106 ALSKVSAEGKV-YYLALVRDASvemaQKEQTRQ 137
Cdd:TIGR00229 94 SVSPIRTNGGElGVVGIVRDIT----ERKEAEE 122
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
365-784 |
1.03e-13 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 74.90 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 365 QEKSRqhIEQLIQ----FDPMTGLPNR----NNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVN- 435
Cdd:PRK11059 215 EERSR--FDTFIRsnafQDAKTGLGNRlffdNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINl 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 436 ------RFreklkPDQYLCRIEGASFVLVSLENDVSNITQIADELRNVVSK---PIMIDDKPFpltLSIGIS-YDVGKNR 505
Cdd:PRK11059 293 lstfvmRY-----PGALLARYSRSDFAVLLPHRSLKEADSLASQLLKAVDAlppPKMLDRDDF---LHIGICaYRSGQST 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 506 DYLLSTAHNAMDFIRKNGGNGWQFFSPAMNE-----MVKERLVLGAALkeaiSNNQLKLVYQPQIFAEtGELYGIEALAR 580
Cdd:PRK11059 365 EQVMEEAEMALRSAQLQGGNGWFVYDKAQLPekgrgSVRWRTLLEQTL----VRGGPRLYQQPAVTRD-GKVHHRELFCR 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 581 WYDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNihipaLSVNLSA---LH------FRSNQLPNQVS 651
Cdd:PRK11059 440 IRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEEN-----LSINLSVdslLSrafqrwLRDTLLQCPRS 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 652 DAMhawgidghQLTVEITESMMMEHDTEIFKRIQILRDMGIGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRclTEK 731
Cdd:PRK11059 515 QRK--------RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRN--IHK 584
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 485653290 732 R------ILALLEAITSIGqslnLTVVAEGIETKEQFEMLRKIHCRVIQGYFFSRPLPA 784
Cdd:PRK11059 585 RtenqlfVRSLVGACAGTE----TQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
659-781 |
1.19e-13 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 73.68 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 659 IDGHQLTVEITESMmmEHDTEIFKRIQILRDMGIGLSVDDFgTGFSGLSRLVSLpVTEIKIDksfVDRcLTEKRILALLE 738
Cdd:COG3434 81 LPPERVVLEILEDV--EPDEELLEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID---VLA-LDLEELAELVA 152
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 485653290 739 AItsigQSLNLTVVAEGIETKEQFEMLRKIHCRVIQGYFFSRP 781
Cdd:COG3434 153 RL----KRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
128-258 |
2.25e-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: 2.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 128 EMAQKEQTRQLIIavDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLLNIPEfpadnriRLQQLLWKTAR 207
Cdd:COG3852 1 ALRESEELLRAIL--DSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS-------PLRELLERALA 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 208 DQD-----EFLLLTRTGEKIWIKASISPVYDVLAHlQNLVMTFSDITE----ERQIRQLE 258
Cdd:COG3852 72 EGQpvterEVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITErkrlERELRRAE 130
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
28-257 |
1.59e-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: 70.53 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 28 INENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGgkarvEGMSRELQLEKKDGSKIWTRFAL 107
Cdd:COG5805 50 VNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKG-----YDVVMIEQIYCKDGELIYVEVKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 108 SKVSAEGKVYYLALVRDAS----VEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGmqpDT 183
Cdd:COG5805 125 FPIYNQNGQAAILALRDITkkkkIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIG---KN 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485653290 184 LLNIpeFPADNRIRLQQLLWKTARDQDEFLL----LTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQL 257
Cdd:COG5805 202 LLEL--LHPCDKEEFKERIESITEVWQEFIIereiITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEEL 277
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
145-248 |
1.68e-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: 64.19 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 145 LDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLLnIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWI 224
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLI-HPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWV 79
|
90 100
....*....|....*....|....
gi 485653290 225 KASISPVYDVLAHLQNLVMTFSDI 248
Cdd:cd00130 80 LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
24-139 |
2.68e-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: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 24 GAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDlrPAHPEYIRHNREGGKARVEgmsRELQLEKKDGSKIWT 103
Cdd:COG3852 19 AVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPED--SPLRELLERALAEGQPVTE---REVTLRRKDGEERPV 93
|
90 100 110
....*....|....*....|....*....|....*..
gi 485653290 104 RFALSKVS-AEGKVYYLALVRDASvemAQKEQTRQLI 139
Cdd:COG3852 94 DVSVSPLRdAEGEGGVLLVLRDIT---ERKRLERELR 127
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
379-526 |
4.49e-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: 65.05 E-value: 4.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 379 DPMTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGAS 454
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARrfqrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGEE 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485653290 455 FVLVSLENDVSNITQIADELRNVV-SKPIMIDDKP-FPLTLSIGISYDVGKNRDY--LLSTAHNAMDFIRKNGGNG 526
Cdd:TIGR00254 85 FVVILPGTPLEDALSKAERLRDAInSKPIEVAGSEtLTVTVSIGVACYPGHGLTLeeLLKRADEALYQAKKAGRNR 160
|
|
| 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 485653290 23 MGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGkarvEGMSRELQLEKKDGSKIW 102
Cdd:cd00130 3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGG----EPVTLEVRLRRKDGSVIW 78
|
90 100
....*....|....*....|....
gi 485653290 103 --TRFALSKVSAEGKVYYLALVRD 124
Cdd:cd00130 79 vlVSLTPIRDEGGEVIGLLGVVRD 102
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
369-498 |
7.36e-12 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 68.39 E-value: 7.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 369 RQHIEQLIQF---DPMTGLPNRNNLHNYLDDLVDKAVS---PV-VYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKL 441
Cdd:PRK09581 282 RNNLEQSIEMavtDGLTGLHNRRYFDMHLKNLIERANErgkPLsLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNI 361
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 442 KPDQYLCRIEGASFVLVSLENDVSNITQIADELRNVVSK---PIMIDDKPFPLTLSIGIS 498
Cdd:PRK09581 362 RGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEepfIISDGKERLNVTVSIGVA 421
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
534-788 |
1.04e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 65.79 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 534 MNEMVKERLVLGAALKEAISNN------QLKLVYQPqIFAETGELYGIEALARWYDPLHghvpPSRFIPLAEEIGEIENI 607
Cdd:PRK11596 1 MIRQVIQRISLPEASIESLQERrywlqcERAYTFQP-IYRTSGRLMAIELLTAVTHPSN----PSQRLSPERYFAEITVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 608 GRW-VIAEACRQLAEWRSQNIHIPAL-SVNL--SALHFRSNQLPNQVSDAMHAWgidghqLTVEITESMMMEHDtEIFKR 683
Cdd:PRK11596 76 HRLdVVKEQLDLLAQWADFFVRHGLLaSVNIdgPTLIALRQQPAILRLIERLPW------LRFELVEHIRLPKD-SPFAS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 684 IQILRDmgigLSVDDFGTGFSGLSRLVSLPVTEIKIDKS-FVDRCLTEK-RIL--ALLEAITSIGQSlnltVVAEGIETK 759
Cdd:PRK11596 149 MCEFGP----LWLDDFGTGMANFSALSEVRYDYIKVARElFIMLRQSEEgRNLfsQLLHLMNRYCRG----VIVEGVETP 220
|
250 260
....*....|....*....|....*....
gi 485653290 760 EQFEMLRKIHCRVIQGYFFSRPLPAEEIP 788
Cdd:PRK11596 221 EEWRDVQRSPAFAAQGYFLSRPAPFETLE 249
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
124-377 |
1.75e-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: 67.31 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 124 DASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMqPDTLLNIPEFPADNRIRLQQLLW 203
Cdd:COG5809 3 SSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGT-NILDFLHPDDEKELREILKLLKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 204 KTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITE----ERQIRQLEGNILAAMCSSPpfheMGEIIC 279
Cdd:COG5809 82 GESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITErkrmEEALRESEEKFRLIFNHSP----DGIIVT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 280 RNIESVL--NESHVSLFALRNGMPIHWASSS--HGAEVQNAQSWSATIRQRDGAPAGILQIKTSSG----AETSAFiERV 351
Cdd:COG5809 158 DLDGRIIyaNPAACKLLGISIEELIGKSILEliHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGrwrlLEASGA-PIK 236
|
250 260
....*....|....*....|....*.
gi 485653290 352 ADISQHMAALALEQEKSRQHIEQLIQ 377
Cdd:COG5809 237 KNGEVDGIVIIFRDITERKKLEELLR 262
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
157-250 |
2.44e-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: 57.86 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 157 HIVQCNRAFTEMFGYCINEASGMQPDTLLNIPEFPADNRIRLQQllwKTARDQDEFLLLTRTGEKIWIKASISPVYDVLA 236
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALRE---GKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGG 79
|
90
....*....|....
gi 485653290 237 HLQNLVMTFSDITE 250
Cdd:pfam13426 80 ELVGIIAILRDITE 93
|
|
| 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 485653290 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 ... |
31-124 |
8.65e-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: 8.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 31 NDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPrdlRPAHPEYIRHNREGGKARVEGmsrELQLEKKDGSKIWTRFALSKV 110
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFA---EPEDSERLREALREGKAVREF---EVVLYRKDGEPFPVLVSLAPI 74
|
90
....*....|....*.
gi 485653290 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 |
7.59e-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: 7.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 142 VDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLLniPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEK 221
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELL--PPEDAARLERALRRALEGEEPIDFLEELLLNGEE 78
|
90 100 110
....*....|....*....|....*....|..
gi 485653290 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 |
5.29e-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: 51.91 E-value: 5.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 141 AVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLLNiPEFPADNRIRLQQLLWKTARD-QDEFLLLTRTG 219
Cdd:TIGR00229 8 IFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIP-EEDREEVRERIERRLEGEPEPvSEERRVRRKDG 86
|
90 100 110
....*....|....*....|....*....|....*..
gi 485653290 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 485653290 7 DNAADGIFfpaleqnmmgavLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKarvEG 86
Cdd:pfam00989 8 ESLPDGIF------------VVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGE---ES 72
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 485653290 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 |
2.56e-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: 49.72 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 142 VDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMqpdtLLNIPEFPADNRIRlQQLLWKTARDQD-----EFLLLT 216
Cdd:pfam00989 7 LESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGK----SLLDLIPEEDDAEV-AELLRQALLQGEesrgfEVSFRV 81
|
90 100 110
....*....|....*....|....*....|..
gi 485653290 217 RTGEKIWIKASISPVYDVLAHLQNLVMTFSDI 248
Cdd:pfam00989 82 PDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
130-258 |
3.03e-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: 53.43 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 130 AQKEQTRQLIIAV-DHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLLnipefpadNRIRLQQLLWKTARD 208
Cdd:COG5000 83 EELEERRRYLETIlENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELL--------PELDLAELLREALER 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 485653290 209 QDEFLLLTRTGEKIWIKASISPVYDvlahlQNLVMTFSDITEERQIRQLE 258
Cdd:COG5000 155 GWQEEIELTRDGRRTLLVRASPLRD-----DGYVIVFDDITELLRAERLA 199
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
5-144 |
1.05e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 51.74 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 5 DADNAADGIFFPALEQNMMGAVLIN--ENDE-VMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRhnreGGK 81
Cdd:PRK13559 36 DFRGASGRLFEQAMEQTRMAMCITDphQPDLpIVLANQAFLDLTGYAAEEVVGRNCRFLQGAATDPIAVAKIR----AAI 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 485653290 82 ARVEGMSRELQLEKKDGSKIWTRFALSKVSAE-GKV-YYLALVRDAS---VEMAQKEQTRQLIIAVDH 144
Cdd:PRK13559 112 AAEREIVVELLNYRKDGEPFWNALHLGPVYGEdGRLlYFFGSQWDVTdirAVRALEAHERRLAREVDH 179
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
14-137 |
1.30e-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: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 14 FFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEgmsrELQL 93
Cdd:COG5809 143 FRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLKDGGIAQG----EVRF 218
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 485653290 94 EKKDGSKIWTRFALSKVSAEGKVY-YLALVRDASVEMAQKEQTRQ 137
Cdd:COG5809 219 WTKDGRWRLLEASGAPIKKNGEVDgIVIIFRDITERKKLEELLRK 263
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
7-256 |
1.31e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 48.90 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 7 DNAADGIFFpaleqnmmgavlINENDEVMFFNPAAEKLWGYKREEVIGNNIdmlipRDLRPAHPEYIRHNREGGKARVEG 86
Cdd:PRK13560 211 DNIADPAFW------------KDEDAKVFGCNDAACLACGFRREEIIGMSI-----HDFAPAQPADDYQEADAAKFDADG 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 87 MS-RELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVI--------VLDPERH 157
Cdd:PRK13560 274 SQiIEAEFQNKDGRTRPVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIeaapiaaiGLDADGN 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 158 IVQCNRAFTE-MFGYCINEAS-----GMQPD-----TLLNIPEFPADNRIRLQQL--LWKTAR-----DQDEFLLLTRTG 219
Cdd:PRK13560 354 ICFVNNNAAErMLGWSAAEVMgkplpGMDPElneefWCGDFQEWYPDGRPMAFDAcpMAKTIKggkifDGQEVLIEREDD 433
|
250 260 270
....*....|....*....|....*....|....*..
gi 485653290 220 EKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQ 256
Cdd:PRK13560 434 GPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEE 470
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
136-202 |
1.52e-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: 43.16 E-value: 1.52e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 485653290 136 RQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLLnIPEFPADNRIRLQQLL 202
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELI-HPEDRERVQEALQRLL 66
|
|
| 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 485653290 4 TDADNAADGIFFPALEQNMMGAVLI--NENDE-VMFFNPAAEKLWGYKREEVIGNNIDMLIPRDlrpAHPEYIRHNREGG 80
Cdd:PRK13557 22 GDVSDHRSDIFFAAVETTRMPMIVTdpNQPDNpIVFANRAFLEMTGYAAEEIIGNNCRFLQGPE---TDRATVAEVRDAI 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 485653290 81 KARVEgMSRELQLEKKDGSKIWTRFALSKV-SAEGK-VYYLA------LVRDA--SVEMAQK-EQTRQLI--IAVD 143
Cdd:PRK13557 99 AERRE-IATEILNYRKDGSSFWNALFVSPVyNDAGDlVYFFGsqldvsRRRDAedALRQAQKmEALGQLTggIAHD 173
|
|
| 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 485653290 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 |
8.36e-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: 8.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 128 EMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLlnIPEFPadnrirLQQLLwKTAR 207
Cdd:COG3829 3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTEL--IPNSP------LLEVL-KTGK 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 485653290 208 DQDEFLLLTRTGEKIWIkASISPVYD----VLAhlqnlVMTFSDITEERQIRQ 256
Cdd:COG3829 74 PVTGVIQKTGGKGKTVI-VTAIPIFEdgevIGA-----VETFRDITELKRLER 120
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
141-200 |
1.08e-04 |
|
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: 41.00 E-value: 1.08e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 141 AVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLLNIPEFPADNRIRLQQ 200
Cdd:pfam13188 6 LFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALELLRELR 65
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
7-62 |
1.30e-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: 1.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 485653290 7 DNAADGIFfpaleqnmmgavLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIP 62
Cdd:COG3829 18 DSLDDGII------------VVDADGRITYVNRAAERILGLPREEVIGKNVTELIP 61
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
379-516 |
1.43e-04 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 44.67 E-value: 1.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 379 DPMTGLPNRNNLHNYLD-DLVDKAVSPV-VYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGASFV 456
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDhQLRNREPQNLyLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFI 211
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 485653290 457 LVSLENDVSNITQIADELRNVVS-KPIMIDDKPFPLTLSIGIS-YDVGKNRDYLLSTAHNAM 516
Cdd:PRK09894 212 ICLKAATDEEACRAGERIRQLIAnHAITHSDGRINITATFGVSrAFPEETLDVVIGRADRAM 273
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
349-498 |
2.84e-04 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 44.23 E-value: 2.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 349 ERVADI---SQHMAALALEQEKSRQHIE----QLIQ---FDPMTGLPNRNNLHNYLDDLVD----KAVSPVVYLIGvDHI 414
Cdd:PRK09966 211 ERIAEFhrfALDFNSLLDEMEEWQLRLQaknaQLLRtalHDPLTGLANRAAFRSGINTLMNnsdaRKTSALLFLDG-DNF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 415 QDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGASFVLVSLE-NDVSNITQIADELRNVVSKPIMIDD-KPFPLT 492
Cdd:PRK09966 290 KYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDvQSESEVQQICSALTQIFNLPFDLHNgHQTTMT 369
|
....*.
gi 485653290 493 LSIGIS 498
Cdd:PRK09966 370 LSIGYA 375
|
|
| 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 485653290 30 ENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDlrpAHPEYIRHNREGGKARvEGMSRELQLEKKDGSKIWTRFALSK 109
Cdd:PRK13558 169 PDEPLIYINDAFERITGYSPDEVLGRNCRFLQGED---TNEERVAELREAIDEE-RPTSVELRNYRKDGSTFWNQVDIAP 244
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 485653290 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 |
9.10e-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: 9.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 142 VDHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLLNipefPADNRIRLQQLLWKTARDQDEFLLLTRT--G 219
Cdd:COG5805 40 LENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLE----KEYHYRVKTRIERLQKGYDVVMIEQIYCkdG 115
|
90 100 110
....*....|....*....|....*....|....*.
gi 485653290 220 EKIWIKASISPVYDVLAHLQnlVMTFSDITEERQIR 255
Cdd:COG5805 116 ELIYVEVKLFPIYNQNGQAA--ILALRDITKKKKIE 149
|
|
| PRK13559 |
PRK13559 |
hypothetical protein; Provisional |
133-258 |
1.37e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237427 [Multi-domain] Cd Length: 361 Bit Score: 41.73 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 133 EQTRQLIIAVD--HLDRPvivldperhIVQCNRAFTEMFGYCINEASGMQPDTLlnipEFPADNRIRLQQLLWKTARDQD 210
Cdd:PRK13559 50 EQTRMAMCITDphQPDLP---------IVLANQAFLDLTGYAAEEVVGRNCRFL----QGAATDPIAVAKIRAAIAAERE 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 485653290 211 ---EFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLE 258
Cdd:PRK13559 117 ivvELLNYRKDGEPFWNALHLGPVYGEDGRLLYFFGSQWDVTDIRAVRALE 167
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
141-253 |
2.29e-03 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 41.19 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 141 AVDHLDRPVIVLDPERH---IVQCNRAFTEMFGYCINEASG-----MQ-PDTllnipefpadNRIRLQQLLWKTARDQD- 210
Cdd:PRK13557 35 AVETTRMPMIVTDPNQPdnpIVFANRAFLEMTGYAAEEIIGnncrfLQgPET----------DRATVAEVRDAIAERREi 104
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 485653290 211 --EFLLLTRTGEKIWIKASISPVYDVLAhlqNLVMTFS---DITEERQ 253
Cdd:PRK13557 105 atEILNYRKDGSSFWNALFVSPVYNDAG---DLVYFFGsqlDVSRRRD 149
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
158-233 |
2.84e-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: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 158 IVQCNRAFTEMFGYCINEASGMqPDTLLNIPeFPADnRIRLQQLLWKTARDQD----EFLLLTRTGEKIWIKASISPVYD 233
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGK-GESWLDLV-HPDD-RERVREALWEALKGGEpysgEYRIRRKDGEYRWVEARARPIRD 77
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
137-258 |
7.72e-03 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 39.57 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 485653290 137 QLIIAvdHLDRPVIVLDPERHIVQCNRAFTEMFGYCINEASGMQPDTLlnipeFPADNRIR--LQQLLWKTARDQDEFLL 214
Cdd:PRK11360 265 ELILE--SIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSEL-----FPPNTPFAspLLDTLEHGTEHVDLEIS 337
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 485653290 215 LTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITE----ERQIRQLE 258
Cdd:PRK11360 338 FPGRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTErkrlQRRVARQE 385
|
|
| |
