|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
4-550 |
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: 550.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 4 DHLTDIAYRHFIESVKDYAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQLSGVPAKNLEIALRSGQFE 83
Cdd:COG5001 120 LARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 84 GEGWRYRKDGSRFWAHVmIDTIRDEQNTLLGFAKITRDISEQKAINDRIAWMARYDALTGLPNRVEFFERVEKLITGNDA 163
Cdd:COG5001 200 LRGGRLLRLALRLLLGL-LLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARR 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 164 --RRFAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEFVAVKP-FSDEGEVDAFAARLWHCF 240
Cdd:COG5001 279 sgRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPdLDDPEDAEAVAERILAAL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 241 SGKQTFAATEVVLSASIGISVYPEDGTDINTILSNSDLAMYRAKSSLDHKICWYEREMDDKTRQRNMMAADIRRGIHAGE 320
Cdd:COG5001 359 AEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 321 FSLHYQAIRNIKDRSITGYEALLRWQHPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVCNES---LENGLNR-KVSVNI 396
Cdd:COG5001 439 LELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLaawQDAGLPDlRVAVNL 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 397 SPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFVINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDV 476
Cdd:COG5001 519 SARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDT 598
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490245256 477 IKLDRSFMTDVESNPQVRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEPVDIKHLPDR 550
Cdd:COG5001 599 LKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEAL 672
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
22-541 |
2.56e-114 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 353.60 E-value: 2.56e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 22 AIYMLSADGTVISWNEGARRAKGYLSDEIIGR-YFGLFYSEAEqlSGVPAKNLEIALRSGQ-FEGEGWRYRKDGSRFW-- 97
Cdd:PRK10060 123 VIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQsVFKLFMSRRE--AAASRRNIRGFFRSGNaYEVERWIKTRKGQRLFlf 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 98 --AHVMIDTIRDEQntLLGFAKItrDISEQKAINDRIAWMARYDALTGLPNRVEFFERVEKLITGNDARRFAIFTIDLDK 175
Cdd:PRK10060 201 rnKFVHSGSGKNEI--FLICSGT--DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDN 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 176 FKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEFVAVKPFSDEGEVDAFAARLWHCFsgKQTFAA--TEVVL 253
Cdd:PRK10060 277 FKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRL--RLPFRIglIEVYT 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 254 SASIGISVYPEDGTDINTILSNSDLAMYRAKSSLDHKICWYEREMDDKTRQRNMMAADIRRGIHAGEFSLHYQAIRNIKD 333
Cdd:PRK10060 355 GCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRG 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 334 RsITGYEALLRWQHPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVCNESL---ENGLNRKVSVNISPVQLRHRSFIEKV 410
Cdd:PRK10060 435 E-VRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAkwrDKGINLRVAVNVSARQLADQTIFTAL 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 411 REILMRTAYPVSLLEFEVTETAFVINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDVIKLDRSFMTDVESN 490
Cdd:PRK10060 514 KQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQ 593
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 490245256 491 PQVRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEP 541
Cdd:PRK10060 594 PVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
20-550 |
1.89e-110 |
|
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: 340.99 E-value: 1.89e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 20 DYAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQLsgVPAKNLEIALRSGQFEGEGWRYRKDGSRFWAH 99
Cdd:COG2200 40 ALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLAL--LLLLLLLLLLLLLLLLLLALLLAALLALLLLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 100 VMIDTIRDEQNTLLGFAKITRDISEQKAINDRIAWMARYDALTGLPNRVEFFER---VEKLITGNDARRFAIFTIDLDKF 176
Cdd:COG2200 118 LLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLlllLLLLLLALALLALLLLLLLLLLL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 177 KEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEFVAV-KPFSDEGEVDAFAARLWHCFSGKQTFAATEVVLSA 255
Cdd:COG2200 198 LLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLlLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVAS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 256 SIGISVYPEDGTDINTILSNSDLAMYRAKSSlDHKICWYEREMDDKTRQRNMMAADIRRGIHAGEFSLHYQAIRNIKDRS 335
Cdd:COG2200 278 SGGGAAAPDDGADAALLLAAAAAAAAAAAGG-GRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGR 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 336 ITGYEALLRWQHPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVC---NESLENGLNRKVSVNISPVQLRHRSFIEKVRE 412
Cdd:COG2200 357 VVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALrqlARWPERGLDLRLSVNLSARSLLDPDFLERLLE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 413 ILMRTAYPVSLLEFEVTETAFVINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDVIKLDRSFMTDVESNPQ 492
Cdd:COG2200 437 LLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPR 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 490245256 493 VRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEPVDIKHLPDR 550
Cdd:COG2200 517 DQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEAL 574
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
310-544 |
4.94e-106 |
|
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: 317.57 E-value: 4.94e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 310 ADIRRGIHAGEFSLHYQAIRNIKDRSITGYEALLRWQHPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVC---NESLEN 386
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACrqlARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 387 GLNRKVSVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFVINKQLAFSVLHHLQKMGISIALDDFGTGYSSL 466
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490245256 467 SMLRDFHFDVIKLDRSFMTDVESNPQVRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEPVDI 544
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
311-542 |
1.32e-92 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 283.34 E-value: 1.32e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 311 DIRRGIHAGEFSLHYQAIRNIKDRSITGYEALLRWQHPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVCNESLE----N 386
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEwqaqG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 387 GLNRKVSVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFVINKQLAFSVLHHLQKMGISIALDDFGTGYSSL 466
Cdd:smart00052 83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490245256 467 SMLRDFHFDVIKLDRSFMTDVESNPQVRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEPV 542
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
309-541 |
8.94e-86 |
|
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: 265.33 E-value: 8.94e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 309 AADIRRGIHAGEFSLHYQAIRNIKDRSITGYEALLRWQHPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVCNESLENGL 388
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 389 N--RKVSVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFVINKQLAFSVLHHLQKMGISIALDDFGTGYSSL 466
Cdd:pfam00563 81 GpdIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490245256 467 SMLRDFHFDVIKLDRSFMTDVESNPQVRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEP 541
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
124-548 |
6.35e-84 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 277.42 E-value: 6.35e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 124 EQKAINDRIAWMARYDALTGLPNRVEFFERVEKLItgNDARRFAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTL 203
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLV--DKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 204 QKEEMVARFGGDEFVAVKPFSDEGEVDAFAARLWHCFSGKQTFAATEVVLSASIGISVypEDGTDINTILSNSDLAMYRA 283
Cdd:PRK11359 442 KPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 284 KSSLDHKICWYEREMDDKTRQRNMMAADIRRGIHAGEFSLHYQAIRNIKDRSITGYEALLRWQHPQLGTIPPDVFIPIAE 363
Cdd:PRK11359 520 RKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 364 ESGAIVPLGYWVLEQVCNESLE---NGLN-RKVSVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFVINKQL 439
Cdd:PRK11359 600 EIGEIENIGRWVIAEACRQLAEwrsQNIHiPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTE 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 440 AFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDVIKLDRSFMTDVESNPQVRSFVRAIISLGNSINTPLIAEGVETA 519
Cdd:PRK11359 680 IFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETK 759
|
410 420
....*....|....*....|....*....
gi 490245256 520 GQLQILEEEGCDEMQGFLFGEPVDIKHLP 548
Cdd:PRK11359 760 EQFEMLRKIHCRVIQGYFFSRPLPAEEIP 788
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
302-549 |
1.30e-69 |
|
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: 232.88 E-value: 1.30e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 302 TRQRNMMAADIRRGIHAGEFSLHYQAIRNIKDRSITGYEALLRWQHPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVCN 381
Cdd:COG4943 266 LRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 382 EsLENGLNR----KVSVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFvINKQLAFSVLHHLQKMGISIALD 457
Cdd:COG4943 346 D-LGDLLAAdpdfHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGF-IDPAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 458 DFGTGYSSLSMLRDFHFDVIKLDRSFMTDVESNPQVRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFL 537
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
250
....*....|..
gi 490245256 538 FGEPVDIKHLPD 549
Cdd:COG4943 504 FAKPLPAEEFIA 515
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
126-542 |
2.14e-63 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 219.20 E-value: 2.14e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 126 KAINDRIAWMARYDALTGLPNRVEFFERVEKLITGNDArrFAIFTIDLDKFKEINdlqGHLIGDQ----LLQRVAGavLK 201
Cdd:PRK13561 221 QRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQT--TALMIITCETLRDTA---GVLKEAQreilLLTLVEK--LK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 202 TLQKEEMV-ARFGGDEFV-----AVKPFSdegevdafAARLwhcfsGKQTFAATEVVL---------SASIGISVYpEDG 266
Cdd:PRK13561 294 SVLSPRMVlAQISGYDFAiiangVKEPWH--------AITL-----GQQVLTIINERLpiqriqlrpSCSIGIAMF-YGD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 267 TDINTILSNSDLAMYRAKSSLDHKICWYEREMDDKTRQRNMMAADIRRGIHAGEFSLHYQAIRNIKDRSITGYEALLRWQ 346
Cdd:PRK13561 360 LTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 347 HPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVCNESL---ENGLNRKVSVNISPVQLRHRSFIEKVREILMRTAYPVSL 423
Cdd:PRK13561 440 QPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAawqERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGT 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 424 LEFEVTETAFVINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFH---FDVIKLDRSFmtdVESNPQVRSFVRAI 500
Cdd:PRK13561 520 LILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMF---VDGLPEDDSMVAAI 596
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 490245256 501 ISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEPV 542
Cdd:PRK13561 597 IMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARAL 638
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
125-542 |
1.45e-57 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 203.64 E-value: 1.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 125 QKAINDRIAWMARYD---ALTGLPNRVEFFERVEKLITGNDARR-FAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVL 200
Cdd:PRK11829 218 QQLLADAYADMGRIShrfPVTELPNRSLFISLLEKEIASSTRTDhFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 201 KTLQKEEMVARFGGDEFV-----AVKPFsdegevDAF--AARLWHCFSGKQTFAATEVVLSASIGISVYPEDGTDINTIL 273
Cdd:PRK11829 298 QCIDDSDLLAQLSKTEFAvlargTRRSF------PAMqlARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMM 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 274 SNSDLAMYRAKSSLDHKICWYEREMDDKTRQRNMMAADIRRGIHAGEFSLHYQAIRNIKDRSITGYEALLRWQHPQLGTI 353
Cdd:PRK11829 372 RNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYV 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 354 PPDVFIPIAEESGAIVPLGYWVLEQVCN---ESLENGLNRKVSVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTE 430
Cdd:PRK11829 452 LPSGFVHFAEEEGMMVPLGNWVLEEACRilaDWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITE 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 431 TAFVINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFH---FDVIKLDRSFMTDVesnPQVRSFVRAIISLGNSI 507
Cdd:PRK11829 532 TAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHLKslpIHMIKLDKSFVKNL---PEDDAIARIISCVSDVL 608
|
410 420 430
....*....|....*....|....*....|....*
gi 490245256 508 NTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEPV 542
Cdd:PRK11829 609 KVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPL 643
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
310-549 |
1.34e-52 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 187.12 E-value: 1.34e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 310 ADIRRGIHAGEFSLHYQAIRNIKDRSITGYEALLRWQHPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVCNES--LENG 387
Cdd:PRK10551 266 KEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAaeLQKV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 388 LNR--KVSVNISPVQLRHRSFIEKVREilMRTAYPVSLLE--FEVTETAfVINKQLAFSVLHHLQKMGISIALDDFGTGY 463
Cdd:PRK10551 346 LPVgaKLGINISPAHLHSDSFKADVQR--LLASLPADHFQivLEITERD-MVQEEEATKLFAWLHSQGIEIAIDDFGTGH 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 464 SSLSMLRDFHFDVIKLDRSFMTDVESNPQVRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEPVD 543
Cdd:PRK10551 423 SALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLP 502
|
....*.
gi 490245256 544 IKHLPD 549
Cdd:PRK10551 503 LEDFVR 508
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
67-542 |
1.32e-51 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 190.27 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 67 GVPAKNLEIAL--RSGQFEGEGW-RYRKDGSRFWAHVMIDTIRDEQNTLLGFAKITRDISEQKAINDRIAWMARYDALTG 143
Cdd:PRK09776 593 GPLMENIYSCLtsRSAAYLEQDVvLHCRSGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTH 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 144 LPNRVEFFERVEKLI-TGND-ARRFAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEFVAVK 221
Cdd:PRK09776 673 LANRASFEKQLRRLLqTVNStHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLL 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 222 PFSDEGEVDAFAARLWHCFSGKQ-TFAATEVVLSASIGISVYPEDGTDINTILSNSDLAMYRAKSSLDHKICWYEREMDD 300
Cdd:PRK09776 753 PDCNVESARFIATRIISAINDYHfPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAA 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 301 KTRQRNMM--AADIRRGIHAGEFSLHYQAIRNIKDRSITGYEALLRWQHPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQ 378
Cdd:PRK09776 833 AHSEHRALslAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHE 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 379 VCNESLE----NGLNrkVSVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFVINKQLAFSVLHHLQKMGISI 454
Cdd:PRK09776 913 FFRQAAKavasKGLS--IALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRV 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 455 ALDDFGTGYSSLSMLRDFHFDVIKLDRSFMTDVESNPQVRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQ 534
Cdd:PRK09776 991 VLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAY 1070
|
....*...
gi 490245256 535 GFLFGEPV 542
Cdd:PRK09776 1071 GYAIARPQ 1078
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
137-286 |
2.38e-50 |
|
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: 170.04 E-value: 2.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 137 RYDALTGLPNRVEFFERVEKLI--TGNDARRFAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGG 214
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490245256 215 DEFVAVKPFSDEGEVDAFAARLWHCFSGKQTFAATEVVLSASIGISVYPEDGTDINTILSNSDLAMYRAKSS 286
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRS 152
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
25-294 |
4.61e-49 |
|
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: 170.93 E-value: 4.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 25 MLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQLSGVPAKNLEIALRSGQFEGEGWRYRKDGSRFWAHVMIDT 104
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 105 IRDEQNTLLGFAKIT--RDISEQKAINDRIAWMARYDALTGLPNRVEFFERVEKLItgNDARR----FAIFTIDLDKFKE 178
Cdd:COG2199 81 LELLLLLLALLLLLLalEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLEREL--ARARRegrpLALLLIDLDHFKR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 179 INDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEFVAVKPFSDEGEVDAFAARLWHCFSGKQ-TFAATEVVLSASI 257
Cdd:COG2199 159 INDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPfELEGKELRVTVSI 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 490245256 258 GISVYPEDGTDINTILSNSDLAMYRAKSSLDHKICWY 294
Cdd:COG2199 239 GVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
134-294 |
8.49e-40 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 142.00 E-value: 8.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 134 WMARYDALTGLPNRVEFFERVEKLITGNDAR--RFAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVAR 211
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 212 FGGDEFVAVKPFSDEGEVDAFAARLWHCFSGKQTFAATEVVLSASIGISVYPEDGTDINTILSNSDLAMYRAKSSLDHKI 291
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 490245256 292 CWY 294
Cdd:smart00267 161 AVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
136-284 |
3.69e-38 |
|
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: 137.77 E-value: 3.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 136 ARYDALTGLPNRVEFFERVEKLItgNDARR----FAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVAR 211
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQEL--QRALRegspVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVAR 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490245256 212 FGGDEFVAVKPFSDEGEVDAFAARLWHCFSGKQTF---AATEVVLSASIGISVYPEDGTDINTILSNSDLAMYRAK 284
Cdd:pfam00990 79 LGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPhtvSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAK 154
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
135-286 |
3.57e-33 |
|
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: 124.37 E-value: 3.57e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 135 MARYDALTGLPNRVEFFERVEKLItgNDARR----FAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVA 210
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSEL--KRARRfqrsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490245256 211 RFGGDEFVAVKPFSDEGEVDAFAARLWHCFSGKQTFAATE--VVLSASIGISVYPEDGTDINTILSNSDLAMYRAKSS 286
Cdd:TIGR00254 79 RYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSetLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKA 156
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
134-293 |
2.04e-23 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 103.94 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 134 WMARYDALTGLPNRVEFFERVEKLIT--GNDARRFAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVAR 211
Cdd:PRK15426 396 WQAWHDPLTRLYNRGALFEKARALAKrcQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGR 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 212 FGGDEFVAVKPFSDEGEVDAFAARLWHCFSGKQTFAATEVVL--SASIGISVYPEDGT-DINTILSNSDLAMYRAKSSLD 288
Cdd:PRK15426 476 VGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIriSASLGVSSAEEDGDyDFEQLQSLADRRLYLAKQAGR 555
|
....*
gi 490245256 289 HKICW 293
Cdd:PRK15426 556 NRVCA 560
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
139-542 |
2.12e-20 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 94.93 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 139 DALTGLPNRVEFFERVEKLI--TGNDARRFAIFTIDLDKFKEINDLQGHLIGD-----------QLLQRVAGAVLktlqk 205
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLedQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEellfelinllsTFVMRYPGALL----- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 206 eemvARFGGDEFVAVKPFSDEGEVDAFAARLWH-CfsgkQTFAATEVVLSAS---IGISVYPEdGTDINTILSNSDLAMY 281
Cdd:PRK11059 306 ----ARYSRSDFAVLLPHRSLKEADSLASQLLKaV----DALPPPKMLDRDDflhIGICAYRS-GQSTEQVMEEAEMALR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 282 RAK----SSldhkicWYereMDDKTRQrnmmaADIRRG-----------IHAGEFSLHYQAIRNiKDRSITGYEALLRWQ 346
Cdd:PRK11059 377 SAQlqggNG------WF---VYDKAQL-----PEKGRGsvrwrtlleqtLVRGGPRLYQQPAVT-RDGKVHHRELFCRIR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 347 HPQLGTIPPDVFIPIAEESGAIVPLGYWVLEQVCNEsLENGLNRKVSVNISPVQLRHRSFIEKVREILMRtaYPVSLLE- 425
Cdd:PRK11059 442 DGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPL-LRYWPEENLSINLSVDSLLSRAFQRWLRDTLLQ--CPRSQRKr 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 426 --FEVTEtAFVIN--KQLAfSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDVIKLDRSFMTDVESNPQVRSFVRAII 501
Cdd:PRK11059 519 liFELAE-ADVCQhiSRLR-PVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLV 596
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 490245256 502 SLGNSINTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEPV 542
Cdd:PRK11059 597 GACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQ 637
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
135-286 |
2.63e-20 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 93.81 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 135 MARYDALTGLPNRvEFFER-----VEKLITGNdaRRFAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMV 209
Cdd:PRK09581 291 MAVTDGLTGLHNR-RYFDMhlknlIERANERG--KPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 210 ARFGGDEFVAVKPFSDEGEVDAFAARLWHCFSGKQtFA----ATEVVLSASIGISVYPEDGTDINTILSNSDLAMYRAKS 285
Cdd:PRK09581 368 ARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEP-FIisdgKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKN 446
|
.
gi 490245256 286 S 286
Cdd:PRK09581 447 T 447
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
11-234 |
4.13e-20 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 90.08 E-value: 4.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEaEQLSGVPAKNLEIALRSGQFEGEGWRYR 90
Cdd:COG2202 13 LRALVESSPD-AIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPP-EDDDEFLELLRAALAGGGVWRGELRNRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 91 KDGSRFWAHVMIDTIRDEQNTLLGFAKITRDISEQKAINDRIAWMARYDALTGLPNRVEFFERVE--KLITGNDA-RRFA 167
Cdd:COG2202 91 KDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLdgRILYVNPAaEELL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490245256 168 IFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEF------VAVKPFSDEGEVDAFAA 234
Cdd:COG2202 171 GYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGrwvwveASAVPLRDGGEVIGVLG 243
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
138-286 |
3.47e-17 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 82.42 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 138 YDALTGLPNR---VEFFERVEKLITGndaRRFAIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGG 214
Cdd:PRK09894 131 MDVLTGLPGRrvlDESFDHQLRNREP---QNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490245256 215 DEFVAVKPFSDEGEVDAFAARLWHCFSGKQ-TFAATEVVLSASIGISVYPEDGTdINTILSNSDLAMYRAKSS 286
Cdd:PRK09894 208 EEFIICLKAATDEEACRAGERIRQLIANHAiTHSDGRINITATFGVSRAFPEET-LDVVIGRADRAMYEGKQT 279
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
122-286 |
3.72e-13 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 71.01 E-value: 3.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 122 ISEQKAI-----NDRIAWMARYDALTGLPNRV--EFFERVEKLITGNDARRFAIFTIDLDKFKEINDLQGHLIGDQLLQR 194
Cdd:PRK10245 186 VSYQTATklaehKRRLQVMSTRDGMTGVYNRRhwETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 195 VAGAVLKTLQKEEMVARFGGDEFVAVKPFSDEGEVDAFAARLWHCFSGKQTFAATEVVLSASIGISVYPEDGTDINTILS 274
Cdd:PRK10245 266 LTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLK 345
|
170
....*....|..
gi 490245256 275 NSDLAMYRAKSS 286
Cdd:PRK10245 346 SADLALYKAKNA 357
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
29-124 |
4.51e-13 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 65.18 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 29 DGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQlsgvpAKNLEIALRSGQ--FEGEGWRYRKDGSRFWAHVMIDTIR 106
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPED-----SERLREALREGKavREFEVVLYRKDGEPFPVLVSLAPIR 75
|
90
....*....|....*...
gi 490245256 107 DEQNTLLGFAKITRDISE 124
Cdd:pfam13426 76 DDGGELVGIIAILRDITE 93
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
126-284 |
1.30e-11 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 66.57 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 126 KAINDRIAWMARYDALTGLPNRVEFFERVEKLITGNDARRF-AIFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQ 204
Cdd:PRK09966 238 QAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTsALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 205 KEEMVARFGGDEFVAV-KPFSDEGEVDAFAARLWHCFSGK-QTFAATEVVLSASIGISVYPEDGTdINTILSNSDLAMYR 282
Cdd:PRK09966 318 LRHKAYRLGGDEFAMVlYDVQSESEVQQICSALTQIFNLPfDLHNGHQTTMTLSIGYAMTIEHAS-AEKLQELADHNMYQ 396
|
..
gi 490245256 283 AK 284
Cdd:PRK09966 397 AK 398
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
11-126 |
1.08e-10 |
|
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: 59.23 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFglFYSEAEQLSGVPAKNLEIALRSGQ--FEGEGWR 88
Cdd:TIGR00229 5 YRAIFESSPD-AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNV--LELIPEEDREEVRERIERRLEGEPepVSEERRV 81
|
90 100 110
....*....|....*....|....*....|....*...
gi 490245256 89 YRKDGSRFWAHVmIDTIRDEQNTLLGFAKITRDISEQK 126
Cdd:TIGR00229 82 RRKDGSEIWVEV-SVSPIRTNGGELGVVGIVRDITERK 118
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
11-144 |
1.89e-10 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 62.56 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQLsgvpAKNLEIALRSGQ--FEGEGWR 88
Cdd:COG3852 9 LRAILDSLPD-AVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPL----RELLERALAEGQpvTEREVTL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 490245256 89 YRKDGSRFWAHVMIDTIRDEQNTlLGFAKITRDISEQKAINDRIAWMARYDALTGL 144
Cdd:COG3852 84 RRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
426-545 |
2.50e-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: 59.43 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 426 FEVTETAfVINKQLaFSVLHHLQKMGISIALDDFGTGYSSLSMLRdfHFDVIKLDrsFMTDveSNPQVRSFVRAIISLgn 505
Cdd:COG3434 88 LEILEDV-EPDEEL-LEALKELKEKGYRIALDDFVLDPEWDPLLP--LADIIKID--VLAL--DLEELAELVARLKRY-- 157
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 490245256 506 siNTPLIAEGVETAGQLQILEEEGCDEMQGFLFGEPVDIK 545
Cdd:COG3434 158 --GIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILK 195
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
168-260 |
3.33e-08 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 52.36 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 168 IFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEE-MVARFGGDEFVAVKPFSDEGEVDAFAARLWHCFSGKQtf 246
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALN-- 81
|
90
....*....|....
gi 490245256 247 AATEVVLSASIGIS 260
Cdd:cd07556 82 QSEGNPVRVRIGIH 95
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
11-122 |
7.47e-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: 50.88 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQLSGVPAKNLEIALRSGQFEGEGWRYR 90
Cdd:pfam00989 3 LRAILESLPD-GIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRV 81
|
90 100 110
....*....|....*....|....*....|..
gi 490245256 91 KDGSRFWAHVMIDTIRDEQNTLLGFAKITRDI 122
Cdd:pfam00989 82 PDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
11-132 |
8.65e-08 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 53.49 E-value: 8.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQLSGVPAKNLEIALRSGQFEGEGWRYR 90
Cdd:COG2202 139 LRLLVENAPD-GIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKD 217
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 490245256 91 KDGSRFWAHVMIDTIRDEQNtLLGFAKITRDISEQKAINDRI 132
Cdd:COG2202 218 GDGRWVWVEASAVPLRDGGE-VIGVLGIVRDITERKRAEEAL 258
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
456-549 |
1.69e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 52.70 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 456 LDDFGTGYSSLSMLRDFHFDVIKLDRSFMTDVESNPQVRSFVRAIISLGNSINTPLIAEGVETAGQLQILEEEGCDEMQG 535
Cdd:PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQG 236
|
90
....*....|....
gi 490245256 536 FLFGEPVDIKHLPD 549
Cdd:PRK11596 237 YFLSRPAPFETLET 250
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
20-122 |
4.81e-07 |
|
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: 48.40 E-value: 4.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 20 DYAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQLsgVPAKNLEIALRSGQFEGEGWRYR-KDGSRFWA 98
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDRE--ELRERLENLLSGGEPVTLEVRLRrKDGSVIWV 79
|
90 100
....*....|....*....|....
gi 490245256 99 HVMIDTIRDEQNTLLGFAKITRDI 122
Cdd:cd00130 80 LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
196-284 |
4.87e-07 |
|
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: 49.91 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 196 AGA---VLKTLQKEE------MVARFGGDEFVAVKPFSDEGEVDAFAARLWHCFSgkqtfAATEVVLSASIGISvypedg 266
Cdd:COG3706 96 AGAddyLTKPFDPEEllarvdLVARYGGEEFAILLPGTDLEGALAVAERIREAVA-----ELPSLRVTVSIGVA------ 164
|
90
....*....|....*...
gi 490245256 267 tdINTILSNSDlAMYRAK 284
Cdd:COG3706 165 --GDSLLKRAD-ALYQAR 179
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
11-130 |
6.52e-07 |
|
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: 51.90 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLF-YSEAEQLSGVPAKNLEIALRSGQFEGEgwRY 89
Cdd:COG5809 17 FRSLFENAPD-AILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFlHPDDEKELREILKLLKEGESRDELEFE--LR 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 490245256 90 RKDGSRFWAHVMIDTIRDEQNTLLGFAKITRDISEQKAIND 130
Cdd:COG5809 94 HKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEE 134
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
29-164 |
1.21e-04 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 44.83 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 29 DGTVISWNEGARRAKGYLSDEIIGRyfGLFYSEAEQLSGVPAKNLEIAL---RSGQFEGEGwrYRKDGSRFWAHVMIDTI 105
Cdd:PRK13558 170 DEPLIYINDAFERITGYSPDEVLGR--NCRFLQGEDTNEERVAELREAIdeeRPTSVELRN--YRKDGSTFWNQVDIAPI 245
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 106 RDEQNTLLGFAKITRDISEQKAINDRIAwmARYDALTGLPNRVE-FFERVEKLITGNDAR 164
Cdd:PRK13558 246 RDEDGTVTHYVGFQTDVTERKEAELALQ--RERRKLQRLLERVEgLVNDVTSALVRATDR 303
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
15-144 |
1.86e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 44.19 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 15 IESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQLSGVpaknLEIALRSGQFE-GEGWRYRKDG 93
Cdd:PRK11360 268 LESIAD-GVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASP----LLDTLEHGTEHvDLEISFPGRD 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490245256 94 SRFWAHVMIDTIRDEQNTLLGFAKITRDISEQKAINDRiawMARYDALTGL 144
Cdd:PRK11360 343 RTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRR---VARQERLAAL 390
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
11-128 |
2.93e-04 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 43.57 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDYAIyMLSADGTVISWNEGARRAKGYLSDEIIGRY-FGLFYSEAEQLSGVPAKNLEIALRSGQFEgegWRY 89
Cdd:COG5805 36 LETILENLPDAII-AVNREGKVIYINPAMEKLLGYTSEEIIGKTiFDFLEKEYHYRVKTRIERLQKGYDVVMIE---QIY 111
|
90 100 110
....*....|....*....|....*....|....*....
gi 490245256 90 RKDGSRFWAHVMIDTIRDEQNTLLGFAkiTRDISEQKAI 128
Cdd:COG5805 112 CKDGELIYVEVKLFPIYNQNGQAAILA--LRDITKKKKI 148
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
11-132 |
3.50e-04 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 43.22 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYseaeqlsgvPAKNLEIALRSGQ-FEGEGWRY 89
Cdd:COG3829 13 LEAILDSLDD-GIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELI---------PNSPLLEVLKTGKpVTGVIQKT 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 490245256 90 RKDGSrfwaHVMIDT--IRDEQNtLLGFAKITRDISEQKAINDRI 132
Cdd:COG3829 83 GGKGK----TVIVTAipIFEDGE-VIGAVETFRDITELKRLERKL 122
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
11-126 |
1.35e-03 |
|
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: 41.50 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSEAEQLSgVPAKNLEIALRSGQFEGEGWRYR 90
Cdd:COG5809 143 FRLIFNHSPD-GIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQEN-VAAFISQLLKDGGIAQGEVRFWT 220
|
90 100 110
....*....|....*....|....*....|....*.
gi 490245256 91 KDGSRFWAHVMIDTIrDEQNTLLGFAKITRDISEQK 126
Cdd:COG5809 221 KDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERK 255
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
89-125 |
1.95e-03 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 36.01 E-value: 1.95e-03
10 20 30
....*....|....*....|....*....|....*..
gi 490245256 89 YRKDGSRFWAHVMIDTIRDEQNTLLGFAKITRDISEQ 125
Cdd:smart00086 7 RRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
22-127 |
3.90e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. 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: 37.39 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 22 AIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFGLFYSE--AEQLS---------GVPAKNLEIALRSGQFEGEGWRYR 90
Cdd:pfam08448 7 ALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPedAARLEralrralegEEPIDFLEELLLNGEERHYELRLT 86
|
90 100 110
....*....|....*....|....*....|....*..
gi 490245256 91 kdgsrfwahvmidTIRDEQNTLLGFAKITRDISEQKA 127
Cdd:pfam08448 87 -------------PLRDPDGEVIGVLVISRDITERRR 110
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
11-126 |
5.18e-03 |
|
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: 39.33 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIIGRYFgLFYSEAEQLSGVPAKNLEIALRSGQFEGEGWRYR 90
Cdd:COG5805 159 LQTLIENSPD-LICVIDTDGRILFINESIERLFGAPREELIGKNL-LELLHPCDKEEFKERIESITEVWQEFIIEREIIT 236
|
90 100 110
....*....|....*....|....*....|....*.
gi 490245256 91 KDGSRFWAHVMIDTIRDEQNTLLGFAKITRDISEQK 126
Cdd:COG5805 237 KDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKK 272
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
32-118 |
6.62e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 36.16 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490245256 32 VISWNEGARRAKGYLSDEIIGRYFGLF-YSEAEQLSGVpAKNLEIALRSGQ-FEGEGWRYRKDGSRFWAHVMIDTIRDEQ 109
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLdLVHPDDRERV-REALWEALKGGEpYSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
....*....
gi 490245256 110 NTLLGFAKI 118
Cdd:pfam08447 80 GKPVRVIGV 88
|
|
| |
