|
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: 649.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 271 IRLSLPYISVVMLIVFILVEYVFAPIIVIGLIITFSFVLIRHSLVRKQNKILLLAQMQFNSELEKQIKLRTEDLVEQKNE 350
Cdd:COG5001 43 LLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLAR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 351 LYHNQQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRVKKGYSISLEI 430
Cdd:COG5001 123 ALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 431 RAYHKNRDIYYLHVTAVPIFLKEKISGVYLMIKDITESKQQQEQINFLAYHDTLTELANRRAFHQHLEQAIARAKISKKP 510
Cdd:COG5001 203 GRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRR 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 511 FAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARLAGDEFTILIENYKKKPDVQKIADRIVAAMNEPF 590
Cdd:COG5001 283 LALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPF 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 591 EIENQHLQISPSIGIAIYPEAGEDALSILQHADMAMYEAKNKGKNGSSLYTKELYKKMERKARIEKDLPIALVNKEFYLV 670
Cdd:COG5001 363 ELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELH 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 671 YQPQIDTTTNKIIGAEALIRWKHPLLGDISPCEFIPIVEETPQVVPLGHWVLQEACLQLKIWHTFGYQNLKISVNLSAKE 750
Cdd:COG5001 443 YQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPDLRVAVNLSARQ 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 751 FRQDQLIENISQILNDVQVDPKYVTLELTERIAMIDEKETLLRLKQLKEYGIQTSIDDFGTGYSSLAYLSIFPIDTLKVP 830
Cdd:COG5001 523 LRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKID 602
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446667655 831 REFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKPLTSNQFIKFLQKTPS 906
Cdd:COG5001 603 RSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
425-902 |
2.04e-111 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 354.09 E-value: 2.04e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 425 SISLEIRAYHKNRDIYYLHVTAVPIFLKEKISGVYLMIKDITESKQQQEQINFLAYHDTLTELANRRAFHQHLEQAIARA 504
Cdd:COG2200 101 LLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLL 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 505 KISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARLAGDEFTILIENYKKKPDVQKIADRIVA 584
Cdd:COG2200 181 ALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLL 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 585 AMNEPFEIENQHLQISPSIGIAIYPEAGEDALSILQHADMAMYEAKnKGKNGSSLYTKELYKKMERKARIEKDLPIALVN 664
Cdd:COG2200 261 LLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAA-GGGRGRVVFFAAAEARARRRLALESELREALEE 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 665 KEFYLVYQPQIDTTTNKIIGAEALIRWKHPLLGDISPCEFIPIVEETPQVVPLGHWVLQEACLQLKIWHTFGYqNLKISV 744
Cdd:COG2200 340 GELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGL-DLRLSV 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 745 NLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERIAMIDEKETLLRLKQLKEYGIQTSIDDFGTGYSSLAYLSIFPI 824
Cdd:COG2200 419 NLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPP 498
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446667655 825 DTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKPLTSNQFIKFLQ 902
Cdd:COG2200 499 DYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALLR 576
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
464-905 |
1.93e-110 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 354.37 E-value: 1.93e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 464 DITESKQQQEQINFLAYHDTLTELANRRAFHQHLEQAIARAKISKkpFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKR 543
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQ--VGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 544 LERIATSNMKLARLAGDEFTILIENyKKKPDVQKIADRIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDALSILQHAD 623
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASH-TSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 624 MAMYEAKNKGKNGSSLYTKELYKKMERKARIEKDLPIALVNKEFYLVYQPQIDTTtNKIIGAEALIRWKHPLLGDISPCE 703
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 704 FIPIVEETPQVVPLGHWVLQEACLQLKIWHTFGYqNLKISVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERIA 783
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGI-NLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 784 MIDEKETLLRLKQLKEYGIQTSIDDFGTGYSSLAYLSIFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVA 863
Cdd:PRK10060 537 IENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIA 616
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 446667655 864 EGIETEKQLKFLQKHNCKYMQGYYFSKPLTSNQFIKFLQKTP 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 |
5.61e-101 |
|
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: 314.48 E-value: 5.61e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 657 DLPIALVNKEFYLVYQPQIDTTTNKIIGAEALIRWKHPLLGDISPCEFIPIVEETPQVVPLGHWVLQEACLQLKIWHTfG 736
Cdd:cd01948 2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA-G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 737 YQNLKISVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERIAMIDEKETLLRLKQLKEYGIQTSIDDFGTGYSSL 816
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446667655 817 AYLSIFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKPL 892
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPL 236
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
467-895 |
5.43e-92 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 308.62 E-value: 5.43e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 467 ESKQQQEQINFLAYHDTLTELANRRAFHQHLEQAIARAKiskkPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLER 546
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAV----SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 547 IATSNMKLARLAGDEFtILIENYKKKPDVQKIADRIVAAMNEPFEIENQHLQISPSIGIAIypEAGEDALSILQHADMAM 626
Cdd:PRK11359 440 KLKPDQYLCRIEGTQF-VLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAM 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 627 YEAKNKGKNGSSLYTKELYKKMERKARIEKDLPIALVNKEFYLVYQPQIDTTTNKIIGAEALIRWKHPLLGDISPCEFIP 706
Cdd:PRK11359 517 DYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIP 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 707 IVEETPQVVPLGHWVLQEACLQLKIWHTFGYQNLKISVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERIAMID 786
Cdd:PRK11359 597 LAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEH 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 787 EKETLLRLKQLKEYGIQTSIDDFGTGYSSLAYLSIFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGI 866
Cdd:PRK11359 677 DTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGV 756
|
410 420
....*....|....*....|....*....
gi 446667655 867 ETEKQLKFLQKHNCKYMQGYYFSKPLTSN 895
Cdd:PRK11359 757 ETKEQFEMLRKIHCRVIQGYFFSRPLPAE 785
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
655-892 |
1.90e-90 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 286.81 E-value: 1.90e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 655 EKDLPIALVNKEFYLVYQPQIDTTTNKIIGAEALIRWKHPLLGDISPCEFIPIVEETPQVVPLGHWVLQEACLQLKIWHT 734
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 735 FGYQNLKISVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERIAMIDEKETLLRLKQLKEYGIQTSIDDFGTGYS 814
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446667655 815 SLAYLSIFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKPL 892
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
469-897 |
6.26e-84 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 283.14 E-value: 6.26e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 469 KQQQEQINFLAYHDTLTELANRRAFHQHLEQAIARakisKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIA 548
Cdd:PRK13561 221 QRQYEEQSRNATRFPVSDLPNKALLMALLEQVVAR----KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 549 TSNMKLARLAGDEFTILIENYKKKPDVQKIADRIVAAMNEPFEIENQHLQISPSIGIAIYpEAGEDALSILQHADMAMYE 628
Cdd:PRK13561 297 SPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 629 AKNKGKNGSSLYTKELYKKMERKARIEKDLPIALVNKEFYLVYQPQIDTTTNKIIGAEALIRWKHPllgDIS---PCEFI 705
Cdd:PRK13561 376 ARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQP---DGSwdlPEGLI 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 706 PIVEETPQVVPLGHWVLQEACLQLKIWHTFGYqNLKISVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERIAMI 785
Cdd:PRK13561 453 DRIESCGLMVTVGHWVLEESCRLLAAWQERGI-MLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRID 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 786 DEKETLLRLKQLKEYGIQTSIDDFGTGYSSLAYLSIF---PIDTLKVPREFTqlaDHRPEERAIVSTILSLANTLNLSVV 862
Cdd:PRK13561 532 DPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFV---DGLPEDDSMVAAIIMLAQSLNLQVI 608
|
410 420 430
....*....|....*....|....*....|....*
gi 446667655 863 AEGIETEKQLKFLQKHNCKYMQGYYFSKPLTSNQF 897
Cdd:PRK13561 609 AEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIF 643
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
485-898 |
1.50e-73 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 254.87 E-value: 1.50e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 485 TELANRRAFHQHLEQAIArAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARLAGDEFTI 564
Cdd:PRK11829 238 TELPNRSLFISLLEKEIA-SSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 565 LIENYKKKPDVQKIADRIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDALSILQHADMAMYEAKNKGKNGSSLYTKEL 644
Cdd:PRK11829 317 LARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 645 YKKMERKARIEKDLPIALVNKEFYLVYQPQIDTTTNKIIGAEALIRWKHPLLGDISPCEFIPIVEETPQVVPLGHWVLQE 724
Cdd:PRK11829 397 IEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 725 ACLQLKIWHTFGYqNLKISVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERIAMIDEKETLLRLKQLKEYGIQT 804
Cdd:PRK11829 477 ACRILADWKARGV-SLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLI 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 805 SIDDFGTGYSSLAYL---SIFPIDTLKVPREFTqlaDHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHNCK 881
Cdd:PRK11829 556 ALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFV---KNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQ 632
|
410
....*....|....*..
gi 446667655 882 YMQGYYFSKPLTSNQFI 898
Cdd:PRK11829 633 CGQGFLFSPPLPRAEFE 649
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
654-907 |
1.04e-71 |
|
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: 1.04e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 654 IEKDLPIALVNKEFYLVYQPQIDTTTNKIIGAEALIRWKHPLLGDISPCEFIPIVEETPQVVPLGHWVLQEACLQLKIWH 733
Cdd:COG4943 272 PRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 734 TfGYQNLKISVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERiAMIDEKETLLRLKQLKEYGIQTSIDDFGTGY 813
Cdd:COG4943 352 A-ADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITER-GFIDPAKARAVIAALREAGHRIAIDDFGTGY 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 814 SSLAYLSIFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKPLT 893
Cdd:COG4943 430 SSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLP 509
|
250
....*....|....
gi 446667655 894 SNQFIKFLQKTPSM 907
Cdd:COG4943 510 AEEFIAWLAAQRAP 523
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
655-891 |
2.25e-71 |
|
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: 235.29 E-value: 2.25e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 655 EKDLPIALVNKEFYLVYQPQIDTTTNKIIGAEALIRWKHPLLGDISPCEFIPIVEETPQVVPLGHWVLQEACLQLKIWHT 734
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 735 FGYqnLKISVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERIAMIDEKETLLRLKQLKEYGIQTSIDDFGTGYS 814
Cdd:pfam00563 81 GPD--IKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446667655 815 SLAYLSIFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKP 891
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
410-640 |
6.05e-65 |
|
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: 219.46 E-value: 6.05e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 410 LEEMINAFHRVKKGYSISLEIRAYHKNRDIYYLHVTAVPIFLKEKISGVYLMIKDITESKQQQEQINFLAYHDTLTELAN 489
Cdd:COG2199 45 LLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 490 RRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARLAGDEFTILIENy 569
Cdd:COG2199 125 RRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPG- 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446667655 570 KKKPDVQKIADRIVAAMNE-PFEIENQHLQISPSIGIAIYPEAGEDALSILQHADMAMYEAKNKGKNGSSLY 640
Cdd:COG2199 204 TDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
480-635 |
6.05e-63 |
|
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: 209.34 E-value: 6.05e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 480 YHDTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARLAG 559
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446667655 560 DEFTILIENYKKKpDVQKIADRIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDALSILQHADMAMYEAKNKGKN 635
Cdd:cd01949 81 DEFAILLPGTDLE-EAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRN 155
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
479-635 |
8.22e-56 |
|
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: 189.77 E-value: 8.22e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 479 AYHDTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARLA 558
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446667655 559 GDEFTILIENYKKKP--DVQKIADRIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDALSILQHADMAMYEAKNKGKN 635
Cdd:pfam00990 81 GDEFAILLPETSLEGaqELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
478-640 |
2.66e-54 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 185.53 E-value: 2.66e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 478 LAYHDTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARL 557
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 558 AGDEFTILIenykKKPDVQ---KIADRIVAAMNEPFEIENQHLQISPSIGIAIYPEAGEDALSILQHADMAMYEAKNKGK 634
Cdd:smart00267 82 GGDEFALLL----PETSLEeaiALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGR 157
|
....*.
gi 446667655 635 NGSSLY 640
Cdd:smart00267 158 NQVAVY 163
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
645-906 |
3.75e-52 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 190.97 E-value: 3.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 645 YKKMERKARIEKDLPIALVNKEFYLVYQPQIDTTTNKIIGAEALIRWKHPLLGDISPCEFIPIVEETPQVVPLGHWVLQe 724
Cdd:PRK10551 255 YYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFE- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 725 aclqLKIWHTFGYQNL-----KISVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERiAMIDEKETLLRLKQLKE 799
Cdd:PRK10551 334 ----LIARDAAELQKVlpvgaKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITER-DMVQEEEATKLFAWLHS 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 800 YGIQTSIDDFGTGYSSLAYLSIFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHN 879
Cdd:PRK10551 409 QGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERG 488
|
250 260
....*....|....*....|....*..
gi 446667655 880 CKYMQGYYFSKPLTSNQFIKFLQKTPS 906
Cdd:PRK10551 489 VNFLQGYWISRPLPLEDFVRWLKEPYT 515
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
440-891 |
6.72e-51 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 194.51 E-value: 6.72e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 440 YYLHVTAVPIF-LKEKISGVYLMIKDITESKQQQEQINFLAYHDTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDL 518
Cdd:PRK09776 625 YDVHYSITPLStLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 519 DRFKVINDTLGHRVGDLLLIAVAK-RLERIATSNMkLARLAGDEFTILIenykkkPD-----VQKIADRIVAAMNE-PFE 591
Cdd:PRK09776 705 DRFKAVNDSAGHAAGDALLRELASlMLSMLRSSDV-LARLGGDEFGLLL------PDcnvesARFIATRIISAINDyHFP 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 592 IENQHLQISPSIGIAIYPEAGEDALSILQHADMAMYEAKNKGKNGSSLYTKELYKKMERKARIEKD--LPIALVNKEFYL 669
Cdd:PRK09776 778 WEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSLAeqWRMIKENQLMML 857
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 670 VYQ---PQIDTTTNKIigaEALIRWKHPLLGDISPCEFIPIVEETPQVVPLGHWVLQEAclqlkiWHTFGYQ----NLKI 742
Cdd:PRK09776 858 AHGvasPRIPEARNHW---LISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEF------FRQAAKAvaskGLSI 928
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 743 SVNLSAKEFRQDQLIENISQILNDVQVDPKYVTLELTERiAMIDEKETLLR-LKQLKEYGIQTSIDDFGTGYSSLAYLSI 821
Cdd:PRK09776 929 ALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITET-ALLNHAESASRlVQKLRLAGCRVVLSDFGRGLSSFNYLKA 1007
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 822 FPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKP 891
Cdd:PRK09776 1008 FMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
478-637 |
6.92e-38 |
|
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: 139.01 E-value: 6.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 478 LAYHDTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARL 557
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 558 AGDEFTILIENyKKKPDVQKIADRIVAAMN-EPFEIEN-QHLQISPSIGIAIYPEAGEDALSILQHADMAMYEAKNKGKN 635
Cdd:TIGR00254 81 GGEEFVVILPG-TPLEDALSKAERLRDAINsKPIEVAGsETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
..
gi 446667655 636 GS 637
Cdd:TIGR00254 160 RV 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
478-635 |
6.41e-34 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 136.18 E-value: 6.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 478 LAYHDTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARL 557
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 558 AGDEFTILIenykkkPDVQ-----KIADRIVAAM-NEPFEIENQ--HLQISPSIGIAIYPEAGEDALSILQHADMAMYEA 629
Cdd:PRK09581 371 GGEEFVVVM------PDTDiedaiAVAERIRRKIaEEPFIISDGkeRLNVTVSIGVAELRPSGDTIEALIKRADKALYEA 444
|
....*.
gi 446667655 630 KNKGKN 635
Cdd:PRK09581 445 KNTGRN 450
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
479-632 |
7.12e-27 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 114.33 E-value: 7.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 479 AYHDTLTELANRRAFHQHLeQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARLA 558
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446667655 559 GDEFTILIENYKKKPDVQKIADRIVAAMNEPFEIENQHL-QISPSIGIAIYPE-AGEDALSILqhADMAMYEAKNK 632
Cdd:PRK09966 327 GDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQtTMTLSIGYAMTIEhASAEKLQEL--ADHNMYQAKHQ 400
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
482-635 |
9.68e-27 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 111.31 E-value: 9.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 482 DTLTELANRRAFHQHLEQAIARAkiSKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSNMKLARLAGDE 561
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQLRNR--EPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446667655 562 FTILIenyKKKPDVQ--KIADRI-VAAMNEPFEIENQHLQISPSIGIAIYpEAGEDALSILQHADMAMYEAKNKGKN 635
Cdd:PRK09894 210 FIICL---KAATDEEacRAGERIrQLIANHAITHSDGRINITATFGVSRA-FPEETLDVVIGRADRAMYEGKQTGRN 282
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
472-635 |
5.64e-26 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 113.57 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 472 QEQINFLAYHDTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATSN 551
Cdd:PRK15426 391 QSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQ 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 552 MKLARLAGDEFTILIENYKKKpDVQKIADRIVAAMNEPfEIE---NQHLQISPSIGIAiypEAGEDA---LSILQH-ADM 624
Cdd:PRK15426 471 DVAGRVGGEEFCVVLPGASLA-EAAQVAERIRLRINEK-EILvakSTTIRISASLGVS---SAEEDGdydFEQLQSlADR 545
|
170
....*....|.
gi 446667655 625 AMYEAKNKGKN 635
Cdd:PRK15426 546 RLYLAKQAGRN 556
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
346-584 |
1.26e-17 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 83.54 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 346 EQKNELYHNQQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRV-KKGY 424
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAAlAGGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 425 SISLEIRAYHKNRDIYYLHVTAVPIFLKE-KISGVYLMIKDITESKQQQEQINFLAYHDTLTELANRRAFHQHLEQAIAR 503
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVRDEDgEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 504 AkISKKpFAVMF---LDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATS-NMKLARLAGDEFTILIENYKKKPDVQKIA 579
Cdd:COG2202 161 Y-VNPA-AEELLgysPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESyELELRLKDGDGRWVWVEASAVPLRDGGEV 238
|
....*
gi 446667655 580 DRIVA 584
Cdd:COG2202 239 IGVLG 243
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
342-475 |
2.96e-17 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 82.77 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 342 EDLVEQK---NELYHNQQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFH 418
Cdd:COG2202 120 RDITERKraeEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLR 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 446667655 419 RVKKG--YSISLEIRAYHKNRDIYYLHVTAVPIFLKEKISGVYLMIKDITESKQQQEQI 475
Cdd:COG2202 200 RLLEGgrESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
342-488 |
2.71e-16 |
|
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: 82.72 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 342 EDLVEQKN---ELYHNQQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFH 418
Cdd:COG5809 124 RDITERKRmeeALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFIS 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446667655 419 RVKKGYSIS-LEIRAYHKNRDIYYLHVTAVPIFLKEKISGVYLMIKDITESKQQQEQINflaYHDTLT---ELA 488
Cdd:COG5809 204 QLLKDGGIAqGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIFRDITERKKLEELLR---KSEKLSvvgELA 274
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
355-475 |
3.82e-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: 72.71 E-value: 3.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 355 QQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRVKKGYS--ISLEIRA 432
Cdd:TIGR00229 2 EERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPepVSEERRV 81
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446667655 433 YHKNRDIYYLHVTAVPIFLKEKISGVYLMIKDITESKQQQEQI 475
Cdd:TIGR00229 82 RRKDGSEIWVEVSVSPIRTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
350-488 |
1.67e-14 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 76.04 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 350 ELYHNQQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDleEMINAFHRV-KKGYSIS- 427
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS--PLRELLERAlAEGQPVTe 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446667655 428 LEIRAYHKNRDIYYLHVTAVPIFLKEKISGVYLMIKDITESKQQQEQINFLAYHDTLTELA 488
Cdd:COG3852 79 REVTLRRKDGEERPVDVSVSPLRDAEGEGGVLLVLRDITERKRLERELRRAEKLAAVGELA 139
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
470-635 |
3.94e-14 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 74.87 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 470 QQQEQINFLAYHDTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIAT 549
Cdd:PRK10245 196 EHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 550 SNMKLARLAGDEFTILIENykkKPdvqkiADRIVAAMNEPFE-IENQHLQISP------SIGIA-IYPEAGEdALSILQH 621
Cdd:PRK10245 276 GSDVIGRFGGDEFAVIMSG---TP-----AESAITAMSRVHEgLNTLRLPNAPqvtlriSVGVApLNPQMSH-YREWLKS 346
|
170
....*....|....
gi 446667655 622 ADMAMYEAKNKGKN 635
Cdd:PRK10245 347 ADLALYKAKNAGRN 360
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
479-891 |
2.13e-13 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 74.13 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 479 AYHDTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRLERIATS--NMKLAR 556
Cdd:PRK11059 228 AFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRypGALLAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 557 LAGDEFTILIENYKKKpDVQKIAD---RIVAAMNEPfEIENQ----HlqispsIGIAIYpEAGEDALSILQHADMAMYEA 629
Cdd:PRK11059 308 YSRSDFAVLLPHRSLK-EADSLASqllKAVDALPPP-KMLDRddflH------IGICAY-RSGQSTEQVMEEAEMALRSA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 630 KNKGKNGSSLYTKELykkMERKAR--------IEKdlpiALVNKEFYLVYQPqIDTTTNKIIGAEALIRWKHPLLGDISP 701
Cdd:PRK11059 379 QLQGGNGWFVYDKAQ---LPEKGRgsvrwrtlLEQ----TLVRGGPRLYQQP-AVTRDGKVHHRELFCRIRDGQGELLSA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 702 CEFIPIVEE---TPQ--------VVPLghwvlqeaclqLKIWhtfgyQNLKISVNLSA-----KEFR---QDQLIENISQ 762
Cdd:PRK11059 451 ELFMPMVQQlglSEQydrqvierVLPL-----------LRYW-----PEENLSINLSVdsllsRAFQrwlRDTLLQCPRS 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 763 ILndvqvdpKYVTLELTERIAM--IDEKETLLRLkqLKEYGIQTSIDDFGTGYSSLAYLSIFPIDTLKVPREFTQLADHR 840
Cdd:PRK11059 515 QR-------KRLIFELAEADVCqhISRLRPVLRM--LRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKR 585
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 446667655 841 PEERAIV-STILSLANTlNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKP 891
Cdd:PRK11059 586 TENQLFVrSLVGACAGT-ETQVFATGVESREEWQTLQELGVSGGQGDFFAES 636
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
355-481 |
2.13e-12 |
|
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: 70.39 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 355 QQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRVKKG-YSISLEIRAY 433
Cdd:COG5809 14 EQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGeSRDELEFELR 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446667655 434 HKNRDIYYLHVTAVPIFLKEK-ISGVYLMIKDITESK-------QQQEQINFLAYH 481
Cdd:COG5809 94 HKNGKRLEFSSKLSPIFDQNGdIEGMLAISRDITERKrmeealrESEEKFRLIFNH 149
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
482-634 |
9.25e-12 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 68.45 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 482 DTLTELANRRAFHQHLEQAIARAKISKKPFAVMFLDLDRFKVINDTLGHRVGDLLLIAVAKRlerIATSNMKL---ARLA 558
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQA---ISASIRKSdygIRLG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 559 GDEFTILIENYkKKPDVQKIADRIvaamnepfeieNQHLQ-------ISPSIGiaIYPEAGEDAL-SILQHADMAMYEAK 630
Cdd:NF040885 421 GDEFCIILIDY-EEAEAQNLIERI-----------RQHLRtidpdkrVSFSWG--AYQMQPGDTLdDAYKAADERLYLNK 486
|
....
gi 446667655 631 NKGK 634
Cdd:NF040885 487 KQKH 490
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
346-476 |
1.32e-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: 67.87 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 346 EQKNELYHNQQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMInafhrvKKGYS 425
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVL------KTGKP 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446667655 426 ISLEIraYHKNRDIYYLHVTAVPIFLKEKISGVYLMIKDITESKQQQEQIN 476
Cdd:COG3829 75 VTGVI--QKTGGKGKTVIVTAIPIFEDGEVIGAVETFRDITELKRLERKLR 123
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
354-475 |
9.36e-11 |
|
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: 65.14 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 354 NQQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRVKKGYSISLEIRAY 433
Cdd:COG5805 32 ITEELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIY 111
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446667655 434 HKNRDIYYLHVTAVPIFLKEKISGVYLmIKDITESKQQQEQI 475
Cdd:COG5805 112 CKDGELIYVEVKLFPIYNQNGQAAILA-LRDITKKKKIEEIL 152
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
376-467 |
2.68e-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: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 376 GNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRVKKGySISLEIRAYHKNRDIYYLHVTAVPIFLKEK- 454
Cdd:pfam13426 2 GRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKA-VREFEVVLYRKDGEPFPVLVSLAPIRDDGGe 80
|
90
....*....|...
gi 446667655 455 ISGVYLMIKDITE 467
Cdd:pfam13426 81 LVGIIAILRDITE 93
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
671-892 |
9.94e-10 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 60.01 E-value: 9.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 671 YQPqIDTTTNKIIGAEALIRWKHPLLGD--ISPCEFIPIVEetpqvVPLGHWVLQEACLQLKIWHT-FGYQNLKISVN-- 745
Cdd:PRK11596 34 FQP-IYRTSGRLMAIELLTAVTHPSNPSqrLSPERYFAEIT-----VSHRLDVVKEQLDLLAQWADfFVRHGLLASVNid 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 746 ---LSAkeFRQD----QLIENISqilndvqvdpkYVTLELTERIAMIDEketlLRLKQLKEYGiQTSIDDFGTGYSSLAY 818
Cdd:PRK11596 108 gptLIA--LRQQpailRLIERLP-----------WLRFELVEHIRLPKD----SPFASMCEFG-PLWLDDFGTGMANFSA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446667655 819 LSIFPIDTLKVPREFTQLADHRPEERAIVSTILSLANTLNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKPL 892
Cdd:PRK11596 170 LSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPA 243
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
378-463 |
1.15e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 55.81 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 378 FLKVNNAGTTLLGYQTNELLN--QPYYSLIYEEDLEEMINAFHR-VKKGYSISLEIRAYHKNRDIYYLHVTAVPIFLKEk 454
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGkgESWLDLVHPDDRERVREALWEaLKGGEPYSGEYRIRRKDGEYRWVEARARPIRDEN- 79
|
....*....
gi 446667655 455 iSGVYLMIK 463
Cdd:pfam08447 80 -GKPVRVIG 87
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
366-465 |
1.31e-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: 56.10 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 366 PDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRV-KKGYSISLEIRAYHKNRDIYYLHV 444
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLlSGGEPVTLEVRLRRKDGSVIWVLV 81
|
90 100
....*....|....*....|..
gi 446667655 445 TAVPIF-LKEKISGVYLMIKDI 465
Cdd:cd00130 82 SLTPIRdEGGEVIGLLGVVRDI 103
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
356-465 |
1.44e-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 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: 56.27 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 356 QMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRVKKGYSISLEIRA--- 432
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVsfr 80
|
90 100 110
....*....|....*....|....*....|....
gi 446667655 433 YHKNRdIYYLHVTAVPI-FLKEKISGVYLMIKDI 465
Cdd:pfam00989 81 VPDGR-PRHVEVRASPVrDAGGEILGFLGVLRDI 113
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
770-891 |
2.61e-09 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 60.20 E-value: 2.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 770 DPKYVTLELTERIAmIDEkETLLRLKQLKEYGIQTSIDDFGTGYSSLAYLSIfpIDTLKVprEFTQLAdhrPEERAivsT 849
Cdd:COG3434 82 PPERVVLEILEDVE-PDE-ELLEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKI--DVLALD---LEELA---E 149
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446667655 850 ILSLANTLNLSVVAEGIETEKQLKFLQKHNCKYMQGYYFSKP 891
Cdd:COG3434 150 LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
284-473 |
2.48e-07 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 54.20 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 284 IVFILVeYVFAPIIVIGLIITFSFVLIRhSLVRKQNKILLLAQMQFNSELEKQIKLRTED---------------LVEQK 348
Cdd:COG5000 5 ILFLLL-LLLIALLLLLLALWLALLLAR-RLTRPLRRLAEATRAVAAGDLSVRLPVTGDDeigelarafnrmtdqLKEQR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 349 NELYHNQQMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRVkkgySISL 428
Cdd:COG5000 83 EELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALER----GWQE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446667655 429 EIRAYHKNRDIYYLHVTAVPiflkekISGVYLMIKDITESKQQQE 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 |
1.58e-06 |
|
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: 46.24 E-value: 1.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446667655 356 QMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRV 420
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRL 65
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
363-470 |
5.63e-06 |
|
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: 45.87 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 363 EHHPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRVKKGYSISLEIRAYHKNRDIYYL 442
Cdd:pfam08448 2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEERHY 81
|
90 100
....*....|....*....|....*....
gi 446667655 443 HVTAVPIFLKE-KISGVYLMIKDITESKQ 470
Cdd:pfam08448 82 ELRLTPLRDPDgEVIGVLVISRDITERRR 110
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
376-484 |
1.81e-05 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 48.90 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 376 GNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEDLEEMINAFHRVKKG--YSISLEIRAYHKNRDIYYLHVtAVPIFLKE 453
Cdd:PRK09776 303 GQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSGeiNSYSMEKRYYRRDGEVVWALL-AVSLVRDT 381
|
90 100 110
....*....|....*....|....*....|...
gi 446667655 454 KISGVYLM--IKDITESKQQQEQINFLAYHDTL 484
Cdd:PRK09776 382 DGTPLYFIaqIEDINELKRTEQVNERLMERITL 414
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
554-630 |
2.36e-05 |
|
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: 45.67 E-value: 2.36e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446667655 554 LARLAGDEFTILIENyKKKPDVQKIADRIVAAMNEPFEIenqhlQISPSIGIAiypeagedALSILQHADmAMYEAK 630
Cdd:COG3706 118 VARYGGEEFAILLPG-TDLEGALAVAERIREAVAELPSL-----RVTVSIGVA--------GDSLLKRAD-ALYQAR 179
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
342-528 |
8.30e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 43.03 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 342 EDLVEQKNelyHNQQMFKSLyehhPDPIFTLDLYGNFLKVNNAGTTLLGYQTNELLNQPYYSLIYEEdlEEMINAFHRvk 421
Cdd:PRK11360 255 QALRETRS---LNELILESI----ADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPN--TPFASPLLD-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 422 kgysiSLEIRAYHKNRDIYY--------LHVTAVPIF-LKEKISGVYLMIKDITESKQQQEQINFLAYHDTLTELAN--- 489
Cdd:PRK11360 324 -----TLEHGTEHVDLEISFpgrdrtieLSVSTSLLHnTHGEMIGALVIFSDLTERKRLQRRVARQERLAALGELVAgva 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446667655 490 ---R------RAFHQHLEQAIARaKISKKPFAVMFLDLDRF-KVINDTL 528
Cdd:PRK11360 399 heiRnpltaiRGYVQIWRQQTSD-PPSQEYLSVVLREVDRLnKVIDQLL 446
|
|
| PTPS_related |
pfam10131 |
6-pyruvoyl-tetrahydropterin synthase related domain; membrane protein; This domain is found in ... |
111-277 |
1.19e-03 |
|
6-pyruvoyl-tetrahydropterin synthase related domain; membrane protein; This domain is found in various bacterial hypothetical membrane proteins, as well as in tetratricopeptide TPR_2 repeat protein. The exact function of the domain has not, as yet, been established.
Pssm-ID: 401941 Cd Length: 621 Bit Score: 42.40 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 111 LVSFTFAFLYEIIyNRDLLEKLFMLCDICI-IVTAQFTLsYYLLIERTIHIFTTSYIDIFVQLTYPMADLLF-------- 181
Cdd:pfam10131 128 LAIFLFLLIYEIR-RKRFLRNLFALVAIGLgIAISSFWL-YPALKGGLTSIDSGSVSWVMKSLTVPLTVSLDpflrlrng 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446667655 182 -----LLIGINLLFKPLSLLPKKVGALLGSALILYATTDAIYAYIKYfIPEYSMFT---VTPFYQVtLVLVAIACILhTK 253
Cdd:pfam10131 206 ffyfgLSIGLLILAGILLAKKRRTPGFVALIIYLVGTTGAALPILVK-LPLNQLFWmirFTPFAAV-LALLLSALLL-WK 282
|
170 180
....*....|....*....|....
gi 446667655 254 KPEKQEQVLLTPKIGESIRLSLPY 277
Cdd:pfam10131 283 VLKKAVLVALAIILAILIVDSSPS 306
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
356-392 |
5.30e-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: 36.37 E-value: 5.30e-03
10 20 30
....*....|....*....|....*....|....*..
gi 446667655 356 QMFKSLYEHHPDPIFTLDLYGNFLKVNNAGTTLLGYQ 392
Cdd:pfam13188 1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYE 37
|
|
| |
