|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
271-906 |
0e+00 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 639.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 271 IRLSLPYISVVMLIVFILVEYVFAPIVVIGLMITFSFVLIRHSLVRKQNKILLLAQMQFNLELEKQIELRTEDLVEQKNE 350
Cdd:COG5001 43 LLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 351 LYHNQQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHVKKGKSISLEV 430
Cdd:COG5001 123 ALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 431 RAYHKNRDIYYLHVTAVPIFLKDHISGVYLMIKDITESKQQQEQINFLAYRDTLTELANRRAFHQYVEQAIARSEISKRP 510
Cdd:COG5001 203 GRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 511 FAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARLAGDEFTILIENYKKRPDVKKIADTIVAAMNEPF 590
Cdd:COG5001 283 LALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 591 EIENQHLQISPSIGIAIYPEAGEDPLSILQHADMAMYEAKNKGKNGSSLYTKELYKKMERKARIEKDLPLALVNKEFYLV 670
Cdd:COG5001 363 ELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELH 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 671 YQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIPIVEETPQVVPLGHWVLKESCLQLKIWHTFGYQDLKISVNLSAKE 750
Cdd:COG5001 443 YQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQ 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 751 FQQEHLIENISQILTDVKVDPKYVTLELTERIAMINEKETLSRLKQLKEYGIQTSIDDFGTGYSSLAYLSLFPIDTLKVP 830
Cdd:COG5001 523 LRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKID 602
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1452482265 831 REFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKNNCKYMQGYYFSKPLTSHQFIKFLQKTPS 906
Cdd:COG5001 603 RSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
413-902 |
5.71e-112 |
|
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: 355.63 E-value: 5.71e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 413 IINAFRHVKKGKSISLEVRAYHKNRDIYYLHVTAVPIFLKDHISGVYLMIKDITESKQQQEQINFLAYRDTLTELANRRA 492
Cdd:COG2200 89 LLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 493 FHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARLAGDEFTILIENYKKR 572
Cdd:COG2200 169 LLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAA 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 573 PDVKKIADTIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDPLSILQHADMAMYEAKnKGKNGSSLYTKELYKKMERKA 652
Cdd:COG2200 249 AAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAA-GGGRGRVVFFAAAEARARRRL 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 653 RIEKDLPLALVNKEFYLVYQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIPIVEETPQVVPLGHWVLKESCLQLKIW 732
Cdd:COG2200 328 ALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARW 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 733 HTFGYqDLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERIAMINEKETLSRLKQLKEYGIQTSIDDFGTG 812
Cdd:COG2200 408 PERGL-DLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTG 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 813 YSSLAYLSLFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKNNCKYMQGYYFSKPL 892
Cdd:COG2200 487 YSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPL 566
|
490
....*....|
gi 1452482265 893 TSHQFIKFLQ 902
Cdd:COG2200 567 PLEELEALLR 576
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
464-905 |
7.03e-112 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 358.22 E-value: 7.03e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 464 DITESKQQQEQINFLAYRDTLTELANRRAFHQYVEQAIARSEISKrpFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKR 543
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQ--VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 544 LEDISTPNMKLARLAGDEFTILIENyKKRPDVKKIADTIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDPLSILQHAD 623
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASH-TSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 624 MAMYEAKNKGKNGSSLYTKELYKKMERKARIEKDLPLALVNKEFYLVYQPQIDITtKKIIGAEALIRWKHPLLGEIPPCE 703
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 704 FIPIVEETPQVVPLGHWVLKESCLQLKIWHTFGYqDLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERIA 783
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI-NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 784 MINEKETLSRLKQLKEYGIQTSIDDFGTGYSSLAYLSLFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVA 863
Cdd:PRK10060 537 IENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIA 616
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1452482265 864 EGIETEKQLKFLQKNNCKYMQGYYFSKPLTSHQFIKFLQKTP 905
Cdd:PRK10060 617 EGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYL 658
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
657-892 |
7.26e-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: 319.49 E-value: 7.26e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 657 DLPLALVNKEFYLVYQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIPIVEETPQVVPLGHWVLKESCLQLKIWHTfG 736
Cdd:cd01948 2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 737 YQDLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERIAMINEKETLSRLKQLKEYGIQTSIDDFGTGYSSL 816
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1452482265 817 AYLSLFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKNNCKYMQGYYFSKPL 892
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
655-892 |
4.76e-93 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 293.74 E-value: 4.76e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 655 EKDLPLALVNKEFYLVYQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIPIVEETPQVVPLGHWVLKESCLQLKIWHT 734
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 735 FGYQDLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERIAMINEKETLSRLKQLKEYGIQTSIDDFGTGYS 814
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1452482265 815 SLAYLSLFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKNNCKYMQGYYFSKPL 892
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
467-892 |
3.65e-88 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 298.22 E-value: 3.65e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 467 ESKQQQEQINFLAYRDTLTELANRRAFHQYVEQAIARSeiskRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLED 546
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKA----VSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 547 ISTPNMKLARLAGDEFtILIENYKKRPDVKKIADTIVAAMNEPFEIENQHLQISPSIGIAIypEAGEDPLSILQHADMAM 626
Cdd:PRK11359 440 KLKPDQYLCRIEGTQF-VLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAM 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 627 YEAKNKGKNGSSLYTKELYKKMERKARIEKDLPLALVNKEFYLVYQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIP 706
Cdd:PRK11359 517 DYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIP 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 707 IVEETPQVVPLGHWVLKESCLQLKIWHTFGYQDLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERIAMIN 786
Cdd:PRK11359 597 LAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEH 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 787 EKETLSRLKQLKEYGIQTSIDDFGTGYSSLAYLSLFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGI 866
Cdd:PRK11359 677 DTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGV 756
|
410 420
....*....|....*....|....*.
gi 1452482265 867 ETEKQLKFLQKNNCKYMQGYYFSKPL 892
Cdd:PRK11359 757 ETKEQFEMLRKIHCRVIQGYFFSRPL 782
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
469-897 |
7.22e-80 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 271.97 E-value: 7.22e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 469 KQQQEQINFLAYRDTLTELANRRAFHQYVEQAIARSEiskrPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDIS 548
Cdd:PRK13561 221 QRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQ----TTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 549 TPNMKLARLAGDEFTILIENYKKRPDVKKIADTIVAAMNEPFEIENQHLQISPSIGIAIYpEAGEDPLSILQHADMAMYE 628
Cdd:PRK13561 297 SPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 629 AKNKGKNGSSLYTKELYKKMERKARIEKDLPLALVNKEFYLVYQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIPIV 708
Cdd:PRK13561 376 ARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 709 EETPQVVPLGHWVLKESCLQLKIWHTFGYqDLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERIAMINEK 788
Cdd:PRK13561 456 ESCGLMVTVGHWVLEESCRLLAAWQERGI-MLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPH 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 789 ETLSRLKQLKEYGIQTSIDDFGTGYSSLAYLSLF---PIDTLKVPREFTqlaDHRPEERAIVSTILSLANTLNLSVVAEG 865
Cdd:PRK13561 535 AAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFV---DGLPEDDSMVAAIIMLAQSLNLQVIAEG 611
|
410 420 430
....*....|....*....|....*....|..
gi 1452482265 866 IETEKQLKFLQKNNCKYMQGYYFSKPLTSHQF 897
Cdd:PRK13561 612 VETEAQRDWLLKAGVGIAQGFLFARALPIEIF 643
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
655-891 |
2.23e-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: 240.68 E-value: 2.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 655 EKDLPLALVNKEFYLVYQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIPIVEETPQVVPLGHWVLKESCLQLKIWHT 734
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 735 FGyqDLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERIAMINEKETLSRLKQLKEYGIQTSIDDFGTGYS 814
Cdd:pfam00563 81 GP--DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1452482265 815 SLAYLSLFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKNNCKYMQGYYFSKP 891
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
478-898 |
2.73e-73 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 254.10 E-value: 2.73e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 478 LAYRDTLTELANRRAFHQYVEQAIArSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARL 557
Cdd:PRK11829 231 ISHRFPVTELPNRSLFISLLEKEIA-SSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 558 AGDEFTILIENYKKRPDVKKIADTIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDPLSILQHADMAMYEAKNKGKNGS 637
Cdd:PRK11829 310 SKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQI 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 638 SLYTKELYKKMERKARIEKDLPLALVNKEFYLVYQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIPIVEETPQVVPL 717
Cdd:PRK11829 390 MVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 718 GHWVLKESCLQLKIWHTFGYQdLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERIAMINEKETLSRLKQL 797
Cdd:PRK11829 470 GNWVLEEACRILADWKARGVS-LPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLREL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 798 KEYGIQTSIDDFGTGYSSLAYL---SLFPIDTLKVPREFTqlaDHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKF 874
Cdd:PRK11829 549 QGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFV---KNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQW 625
|
410 420
....*....|....*....|....
gi 1452482265 875 LQKNNCKYMQGYYFSKPLTSHQFI 898
Cdd:PRK11829 626 LLEHGIQCGQGFLFSPPLPRAEFE 649
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
654-907 |
9.23e-72 |
|
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: 246.37 E-value: 9.23e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 654 IEKDLPLALVNKEFYLVYQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIPIVEETPQVVPLGHWVLKESCLQLKIWH 733
Cdd:COG4943 272 PRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 734 TfGYQDLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERiAMINEKETLSRLKQLKEYGIQTSIDDFGTGY 813
Cdd:COG4943 352 A-ADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITER-GFIDPAKARAVIAALREAGHRIAIDDFGTGY 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 814 SSLAYLSLFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKNNCKYMQGYYFSKPLT 893
Cdd:COG4943 430 SSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLP 509
|
250
....*....|....
gi 1452482265 894 SHQFIKFLQKTPSM 907
Cdd:COG4943 510 AEEFIAWLAAQRAP 523
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
428-640 |
2.71e-63 |
|
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: 214.84 E-value: 2.71e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 428 LEVRAYHKNRDIYYLHVTAVPIFLKDHISGVYLMIKDITESKQQQEQINFLAYRDTLTELANRRAFHQYVEQAIARSEIS 507
Cdd:COG2199 63 LLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARRE 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 508 KRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARLAGDEFTILIENyKKRPDVKKIADTIVAAMN 587
Cdd:COG2199 143 GRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPG-TDLEEAEALAERLREALE 221
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1452482265 588 E-PFEIENQHLQISPSIGIAIYPEAGEDPLSILQHADMAMYEAKNKGKNGSSLY 640
Cdd:COG2199 222 QlPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
480-635 |
4.35e-60 |
|
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: 201.63 E-value: 4.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 480 YRDTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARLAG 559
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1452482265 560 DEFTILIENyKKRPDVKKIADTIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDPLSILQHADMAMYEAKNKGKN 635
Cdd:cd01949 81 DEFAILLPG-TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRN 155
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
479-635 |
5.28e-52 |
|
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: 178.99 E-value: 5.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 479 AYRDTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARLA 558
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1452482265 559 GDEFTILIE--NYKKRPDVKKIADTIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDPLSILQHADMAMYEAKNKGKN 635
Cdd:pfam00990 81 GDEFAILLPetSLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
645-906 |
1.46e-51 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 189.43 E-value: 1.46e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 645 YKKMERKARIEKDLPLALVNKEFYLVYQPQIDITTKKIIGAEALIRWKHPLLGEIPPCEFIPIVEETPQVVPLGHWVLke 724
Cdd:PRK10551 255 YYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLF-- 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 725 sclQLKIWHTFGYQDL-----KISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERiAMINEKETLSRLKQLKE 799
Cdd:PRK10551 333 ---ELIARDAAELQKVlpvgaKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITER-DMVQEEEATKLFAWLHS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 800 YGIQTSIDDFGTGYSSLAYLSLFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKNN 879
Cdd:PRK10551 409 QGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERG 488
|
250 260
....*....|....*....|....*..
gi 1452482265 880 CKYMQGYYFSKPLTSHQFIKFLQKTPS 906
Cdd:PRK10551 489 VNFLQGYWISRPLPLEDFVRWLKEPYT 515
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
478-640 |
5.53e-51 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 176.28 E-value: 5.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 478 LAYRDTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARL 557
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 558 AGDEFTILIenykKRPDV---KKIADTIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDPLSILQHADMAMYEAKNKGK 634
Cdd:smart00267 82 GGDEFALLL----PETSLeeaIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGR 157
|
....*.
gi 1452482265 635 NGSSLY 640
Cdd:smart00267 158 NQVAVY 163
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
440-891 |
5.50e-47 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 182.18 E-value: 5.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 440 YYLHVTAVPIFLKD-HISGVYLMIKDITESKQQQEQINFLAYRDTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDL 518
Cdd:PRK09776 625 YDVHYSITPLSTLDgENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 519 DRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARLAGDEFTILIenykkrPD-----VKKIADTIVAAMNE-PFEI 592
Cdd:PRK09776 705 DRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLL------PDcnvesARFIATRIISAINDyHFPW 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 593 ENQHLQISPSIGIAIY----PEAGEdplsILQHADMAMYEAKNKGKNGSSLYTKELYKKMERKARIEKD--LPLALVNKE 666
Cdd:PRK09776 779 EGRVYRVGASAGITLIdannHQASE----VMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSLAeqWRMIKENQL 854
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 667 FYLVYQ---PQIDITTKKIigaEALIRWKHPLlGE-IPPCEFIPIVEETPQVVPLGHWVLKEsclqlkIWHTFGYQ---- 738
Cdd:PRK09776 855 MMLAHGvasPRIPEARNHW---LISLRLWDPE-GEiIDEGAFRPAAEDPALMHALDRRVIHE------FFRQAAKAvask 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 739 DLKISVNLSAKEFQQEHLIENISQILTDVKVDPKYVTLELTERiAMINEKETLSR-LKQLKEYGIQTSIDDFGTGYSSLA 817
Cdd:PRK09776 925 GLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITET-ALLNHAESASRlVQKLRLAGCRVVLSDFGRGLSSFN 1003
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1452482265 818 YLSLFPIDTLKVPREF-TQLADHrPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKNNCKYMQGYYFSKP 891
Cdd:PRK09776 1004 YLKAFMADYLKLDGELvANLHGN-LMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
478-637 |
1.27e-35 |
|
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: 132.85 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 478 LAYRDTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRL------EDIstpn 551
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILqssvrgSDV---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 552 mkLARLAGDEFTILIENyKKRPDVKKIADTIVAAMN-EPFEIEN-QHLQISPSIGIAIYPEAGEDPLSILQHADMAMYEA 629
Cdd:TIGR00254 77 --VGRYGGEEFVVILPG-TPLEDALSKAERLRDAINsKPIEVAGsETLTVTVSIGVACYPGHGLTLEELLKRADEALYQA 153
|
....*...
gi 1452482265 630 KNKGKNGS 637
Cdd:TIGR00254 154 KKAGRNRV 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
478-635 |
5.86e-31 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 127.32 E-value: 5.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 478 LAYRDTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDistpNMK---- 553
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRN----NIRgtdl 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 554 LARLAGDEFTILIenykkrPDV-----KKIADTIVAAM-NEPFEIENQ--HLQISPSIGIAIYPEAGEDPLSILQHADMA 625
Cdd:PRK09581 367 IARYGGEEFVVVM------PDTdiedaIAVAERIRRKIaEEPFIISDGkeRLNVTVSIGVAELRPSGDTIEALIKRADKA 440
|
170
....*....|
gi 1452482265 626 MYEAKNKGKN 635
Cdd:PRK09581 441 LYEAKNTGRN 450
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
479-632 |
7.63e-25 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 108.17 E-value: 7.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 479 AYRDTLTELANRRAFHQYVeQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARLA 558
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1452482265 559 GDEFTILIENYKKRPDVKKIADTIVAAMNEPFEIENQHL-QISPSIGIAIYPE-AGEDPLSILqhADMAMYEAKNK 632
Cdd:PRK09966 327 GDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQtTMTLSIGYAMTIEhASAEKLQEL--ADHNMYQAKHQ 400
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
476-635 |
2.32e-24 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 104.38 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 476 NFLAYRDTLTELANRRAFHQYVEQAIARSEisKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLA 555
Cdd:PRK09894 126 TIRSNMDVLTGLPGRRVLDESFDHQLRNRE--PQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVY 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 556 RLAGDEFTILIENYKKRPDVKKIADTIVAAMNEPFEIENQHLQISPSIGIAIYpEAGEDPLSILQHADMAMYEAKNKGKN 635
Cdd:PRK09894 204 RYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRA-FPEETLDVVIGRADRAMYEGKQTGRN 282
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
472-635 |
3.29e-22 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 102.02 E-value: 3.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 472 QEQINFLAYRDTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAK------RLE 545
Cdd:PRK15426 391 QSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGlissslRAQ 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 546 DIstpnmkLARLAGDEFTILIENYKKRpDVKKIADTIVAAMNEPfEIE---NQHLQISPSIGIAIYPEAGEDPLSILQH- 621
Cdd:PRK15426 471 DV------AGRVGGEEFCVVLPGASLA-EAAQVAERIRLRINEK-EILvakSTTIRISASLGVSSAEEDGDYDFEQLQSl 542
|
170
....*....|....
gi 1452482265 622 ADMAMYEAKNKGKN 635
Cdd:PRK15426 543 ADRRLYLAKQAGRN 556
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
346-567 |
6.94e-18 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 84.31 E-value: 6.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 346 EQKNELYHNQQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHV-KKGK 424
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAAlAGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 425 SISLEVRAYHKNRDIYYLHVTAVPIFLKD-HISGVYLMIKDITESKQQQEQINFLAYRDTLTELANRRAFHQYVEQAIAR 503
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVRDEDgEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1452482265 504 sEISKRpFAVMF---LDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTP-NMKLARLAGDEFTILIE 567
Cdd:COG2202 161 -YVNPA-AEELLgysPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESyELELRLKDGDGRWVWVE 226
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
342-475 |
8.78e-18 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 84.31 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 342 EDLVEQK---NELYHNQQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFR 418
Cdd:COG2202 120 RDITERKraeEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLR 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1452482265 419 HVKKG--KSISLEVRAYHKNRDIYYLHVTAVPIFLKDHISGVYLMIKDITESKQQQEQI 475
Cdd:COG2202 200 RLLEGgrESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
355-475 |
2.20e-15 |
|
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: 73.48 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 355 QQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHVKKGKS--ISLEVRA 432
Cdd:TIGR00229 2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPepVSEERRV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1452482265 433 YHKNRDIYYLHVTAVPIFLKDHISGVYLMIKDITESKQQQEQI 475
Cdd:TIGR00229 82 RRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
342-488 |
1.28e-14 |
|
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: 77.32 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 342 EDLVEQKN---ELYHNQQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFR 418
Cdd:COG5809 124 RDITERKRmeeALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFIS 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1452482265 419 HVKKGKSIS-LEVRAYHKNRDIYYLHVTAVPIFLKDHISGVYLMIKDITESKQQQEQINflaYRDTLT---ELA 488
Cdd:COG5809 204 QLLKDGGIAqGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKLEELLR---KSEKLSvvgELA 274
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
470-635 |
1.43e-14 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 76.41 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 470 QQQEQINFLAYRDTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDIST 549
Cdd:PRK10245 196 EHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 550 PNMKLARLAGDEFTILIENYKkrpdvkkiADTIVAAMNEPFEIENqHLQISPSIGIAIYPEAGEDPLSI--------LQH 621
Cdd:PRK10245 276 GSDVIGRFGGDEFAVIMSGTP--------AESAITAMSRVHEGLN-TLRLPNAPQVTLRISVGVAPLNPqmshyrewLKS 346
|
170
....*....|....
gi 1452482265 622 ADMAMYEAKNKGKN 635
Cdd:PRK10245 347 ADLALYKAKNAGRN 360
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
479-891 |
6.54e-14 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 75.67 E-value: 6.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 479 AYRDTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVakrLEDIST-----PNMK 553
Cdd:PRK11059 228 AFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFEL---INLLSTfvmryPGAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 554 LARLAGDEFTILIenykkrP-----DVKKIAD---TIVAAMNEPfEIENQ----HlqispsIGIAIYpEAGEDPLSILQH 621
Cdd:PRK11059 305 LARYSRSDFAVLL------PhrslkEADSLASqllKAVDALPPP-KMLDRddflH------IGICAY-RSGQSTEQVMEE 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 622 ADMAMYEAKNKGKNGSSLYTKELykkMERKAR--------IEKdlplALVNKEFYLVYQPQIDiTTKKIIGAEALIRWKH 693
Cdd:PRK11059 371 AEMALRSAQLQGGNGWFVYDKAQ---LPEKGRgsvrwrtlLEQ----TLVRGGPRLYQQPAVT-RDGKVHHRELFCRIRD 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 694 PLLGEIPPCEFIPIVEE---TPQ--------VVPLghwvlkesclqLKIWhtfgyQDLKISVNLSAKEFQQEHLIenisQ 762
Cdd:PRK11059 443 GQGELLSAELFMPMVQQlglSEQydrqvierVLPL-----------LRYW-----PEENLSINLSVDSLLSRAFQ----R 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 763 ILTDV-----KVDPKYVTLELTERIAMINEKETLSRLKQLKEYGIQTSIDDFGTGYSSLAYLSLFPIDTLKVPREFTQLA 837
Cdd:PRK11059 503 WLRDTllqcpRSQRKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNI 582
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1452482265 838 DHRPEERAIV-STILSLANTlNLSVVAEGIETEKQLKFLQKNNCKYMQGYYFSKP 891
Cdd:PRK11059 583 HKRTENQLFVrSLVGACAGT-ETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
350-488 |
2.41e-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: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 350 ELYHNQQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSL-TYEEDLEDIINafRHVKKGKSIS- 427
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELfPEDSPLRELLE--RALAEGQPVTe 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1452482265 428 LEVRAYHKNRDIYYLHVTAVPIFLKDHISGVYLMIKDITESKQQQEQINFLAYRDTLTELA 488
Cdd:COG3852 79 REVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAEKLAAVGELA 139
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
721-892 |
9.45e-12 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 66.18 E-value: 9.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 721 VLKESCLQLKIWHT-FGYQDLKISVNLSAkefQQEHLIENISQILTDVKVDPkYVTLELTERIAMINEketlSRLKQLKE 799
Cdd:PRK11596 80 VVKEQLDLLAQWADfFVRHGLLASVNIDG---PTLIALRQQPAILRLIERLP-WLRFELVEHIRLPKD----SPFASMCE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 800 YGiQTSIDDFGTGYSSLAYLSLFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKNN 879
Cdd:PRK11596 152 FG-PLWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSP 230
|
170
....*....|...
gi 1452482265 880 CKYMQGYYFSKPL 892
Cdd:PRK11596 231 AFAAQGYFLSRPA 243
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
346-476 |
4.20e-11 |
|
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: 66.33 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 346 EQKNELYHNQQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIInafrhvKKGKS 425
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVL------KTGKP 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1452482265 426 ISLEVraYHKNRDIYYLHVTAVPIFLKDHISGVYLMIKDITESKQQQEQIN 476
Cdd:COG3829 75 VTGVI--QKTGGKGKTVIVTAIPIFEDGEVIGAVETFRDITELKRLERKLR 123
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
355-475 |
9.64e-11 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 65.38 E-value: 9.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 355 QQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHVKKGKSIS-LEVRAY 433
Cdd:COG5809 14 EQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDeLEFELR 93
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1452482265 434 HKNRDIYYLHVTAVPIF-LKDHISGVYLMIKDITESKQQQEQI 475
Cdd:COG5809 94 HKNGKRLEFSSKLSPIFdQNGDIEGMLAISRDITERKRMEEAL 136
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
751-891 |
2.68e-10 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 63.28 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 751 FQQEHLIENISQILtdvkvDPKYVTLELTERIAmiNEKETLSRLKQLKEYGIQTSIDDFGtgySSLAYLSLFP-IDTLKV 829
Cdd:COG3434 68 FTEELLLSDLPELL-----PPERVVLEILEDVE--PDEELLEALKELKEKGYRIALDDFV---LDPEWDPLLPlADIIKI 137
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1452482265 830 prEFTQLAdhrPEERAivsTILSLANTLNLSVVAEGIETEKQLKFLQKNNCKYMQGYYFSKP 891
Cdd:COG3434 138 --DVLALD---LEELA---ELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
376-467 |
8.56e-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: 8.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 376 GNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHVKKgKSISLEVRAYHKNRDIYYLHVTAVPIFLKD-H 454
Cdd:pfam13426 2 GRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGK-AVREFEVVLYRKDGEPFPVLVSLAPIRDDGgE 80
|
90
....*....|...
gi 1452482265 455 ISGVYLMIKDITE 467
Cdd:pfam13426 81 LVGIIAILRDITE 93
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
378-463 |
9.99e-10 |
|
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: 56.19 E-value: 9.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 378 FLNVNNAGTTLLGYQTNELL--KQPYYSLTYEEDLEDIINAF-RHVKKGKSISLEVRAYHKNRDIYYLHVTAVPIFLKDH 454
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLgkGESWLDLVHPDDRERVREALwEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80
|
....*....
gi 1452482265 455 isGVYLMIK 463
Cdd:pfam08447 81 --KPVRVIG 87
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
366-465 |
1.88e-09 |
|
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: 55.72 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 366 PDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHV-KKGKSISLEVRAYHKNRDIYYLHV 444
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLlSGGEPVTLEVRLRRKDGSVIWVLV 81
|
90 100
....*....|....*....|..
gi 1452482265 445 TAVPIF-LKDHISGVYLMIKDI 465
Cdd:cd00130 82 SLTPIRdEGGEVIGLLGVVRDI 103
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
354-475 |
2.66e-09 |
|
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: 60.52 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 354 NQQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHVKKGKSISLEVRAY 433
Cdd:COG5805 32 ITEELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIY 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1452482265 434 HKNRDIYYLHVTAVPIFLKDHISGVYLmIKDITESKQQQEQI 475
Cdd:COG5805 112 CKDGELIYVEVKLFPIYNQNGQAAILA-LRDITKKKKIEEIL 152
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
482-569 |
1.69e-08 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 58.05 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 482 DTLTELANRRAFHQYVEQAIARSEISKRPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLEDISTPNMKLARLAGDE 561
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
....*...
gi 1452482265 562 FTILIENY 569
Cdd:NF040885 424 FCIILIDY 431
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
356-465 |
3.98e-08 |
|
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: 52.42 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 356 QMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSL---TYEEDLEDIINAFRHVKKGKSISLEVRA 432
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLipeEDDAEVAELLRQALLQGEESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|....
gi 1452482265 433 YHKNRdIYYLHVTAVPIFLKDH-ISGVYLMIKDI 465
Cdd:pfam00989 81 VPDGR-PRHVEVRASPVRDAGGeILGFLGVLRDI 113
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
376-484 |
1.47e-07 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 55.45 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 376 GNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHVKKGK--SISLEVRAYHKNRDIYYLHVtAVPIFLKD 453
Cdd:PRK09776 303 GQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSGEinSYSMEKRYYRRDGEVVWALL-AVSLVRDT 381
|
90 100 110
....*....|....*....|....*....|...
gi 1452482265 454 HISGVYLM--IKDITESKQQQEQINFLAYRDTL 484
Cdd:PRK09776 382 DGTPLYFIaqIEDINELKRTEQVNERLMERITL 414
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
363-470 |
1.91e-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 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: 50.11 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 363 EHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHVKKGKSISLEVRAYHKNRDIYYL 442
Cdd:pfam08448 2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEERHY 81
|
90 100
....*....|....*....|....*....
gi 1452482265 443 HVTAVPIFLKD-HISGVYLMIKDITESKQ 470
Cdd:pfam08448 82 ELRLTPLRDPDgEVIGVLVISRDITERRR 110
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
284-473 |
1.01e-06 |
|
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: 52.27 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 284 IVFILVeYVFAPIVVIGLMITFSFVLIRhSLVRKQNKILLLAQ------MQFNLELEKQIELR---------TEDLVEQK 348
Cdd:COG5000 5 ILFLLL-LLLIALLLLLLALWLALLLAR-RLTRPLRRLAEATRavaagdLSVRLPVTGDDEIGelarafnrmTDQLKEQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 349 NELYHNQQMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDII-NAFRHVKKGksis 427
Cdd:COG5000 83 EELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLrEALERGWQE---- 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1452482265 428 lEVRAYHKNRDIYYLHVTAVPiflkdhISGVYLMIKDITESKQQQE 473
Cdd:COG5000 159 -EIELTRDGRRTLLVRASPLR------DDGYVIVFDDITELLRAER 197
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
356-420 |
2.42e-05 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 42.77 E-value: 2.42e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1452482265 356 QMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFRHV 420
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRL 65
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
350-475 |
2.43e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 48.13 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 350 ELYHNQQMFKSLYEHHPDPIFTLDLYGNFLNV-NNAGTTLLGYQTNELLKQPYYSLTYEEDLEDIINAFR---------- 418
Cdd:PRK13560 326 ELLEKEDMLRAIIEAAPIAAIGLDADGNICFVnNNAAERMLGWSAAEVMGKPLPGMDPELNEEFWCGDFQewypdgrpma 405
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1452482265 419 --------HVKKGKSIS-LEVRAyHKNRDiYYLHVTAVPIFLKD---HISGVYLMIKDITESKQQQEQI 475
Cdd:PRK13560 406 fdacpmakTIKGGKIFDgQEVLI-EREDD-GPADCSAYAEPLHDadgNIIGAIALLVDITERKQVEEQL 472
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
554-630 |
2.00e-04 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 42.97 E-value: 2.00e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1452482265 554 LARLAGDEFTILIENyKKRPDVKKIADTIVAAMNEPFEIenqhlQISPSIGIAIypeagedpLSILQHADmAMYEAK 630
Cdd:COG3706 118 VARYGGEEFAILLPG-TDLEGALAVAERIREAVAELPSL-----RVTVSIGVAG--------DSLLKRAD-ALYQAR 179
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
297-528 |
3.91e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 44.19 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 297 VVIGLMITFSFVlirHSLVRKQNKILL-LAQMQFNL------------ELEKQIELRTEDLVEQKNelyHNQQMFKSLye 363
Cdd:PRK11360 200 LVIGLLLIFLLS---RRFSANVDIIKDgLSTLENDLstrlpplpgelgEISQAINNLAQALRETRS---LNELILESI-- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 364 hhPDPIFTLDLYGNFLNVNNAGTTLLGYQTNELLKQPYYSL-TYEEDLEDII-NAFRHVKkgKSISLEVRAYHKNRDIYY 441
Cdd:PRK11360 272 --ADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELfPPNTPFASPLlDTLEHGT--EHVDLEISFPGRDRTIEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 442 LHVTAVPIFLKDHISGVYLMIKDITESKQQQEQINFLAYRDTLTELAN------R------RAFHQYVEQAIARSEiSKR 509
Cdd:PRK11360 348 SVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQERLAALGELVAgvaheiRnpltaiRGYVQIWRQQTSDPP-SQE 426
|
250 260
....*....|....*....|
gi 1452482265 510 PFAVMFLDLDRF-KVINDTL 528
Cdd:PRK11360 427 YLSVVLREVDRLnKVIDQLL 446
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
356-392 |
6.65e-03 |
|
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: 35.99 E-value: 6.65e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1452482265 356 QMFKSLYEHHPDPIFTLDLYGNFLNVNNAGTTLLGYQ 392
Cdd:pfam13188 1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYE 37
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
270-475 |
7.65e-03 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 39.83 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 270 SIRLSLPYISVVMLIVFILVEYVFAPIVVIGLMITFSFVLIRHSLVRKQNKILLLAQMQFNLELEKQIELRTEDLVEQKN 349
Cdd:COG3290 2 LLLLLLLLLLLILLILILILLLLLLIILLLILLLVLLLLLFLLFVIILLLLLLILLLILLLLLLLLLAALLLKLLEEIAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1452482265 350 ELYHNQQMFKSLYEhhpdPIFTLDLYGNFLNVNNAGTTLLGYqtnellkqpyysltyEEDLEDIINAFRHVKKGKSISLE 429
Cdd:COG3290 82 LVEEREAVLESIRE----GVIAVDRDGRITLINDAARRLLGL---------------DAIGRPIDEVLAEVLETGERDEE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1452482265 430 VRAYHKnrdiyYLHVTAVPIFLKDHISGVYLMIKDITESKQQQEQI 475
Cdd:COG3290 143 ILLNGR-----VLVVNRVPIRDDGRVVGAVATFRDRTELERLEEEL 183
|
|
| |
