|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
4-549 |
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: 553.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 4 DHLTDIAYRHFIESVKDYAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEAEQLSRVPAKNLQIALRSGQFE 83
Cdd:COG5001 120 LARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 84 GEGWRYRKDGSRFWAHVmINAIRDEQHNLLGFAKITRDISEQKAINDRIAWMARYDALTGLPNRVEFFERVEKLITGNDA 163
Cdd:COG5001 200 LRGGRLLRLALRLLLGL-LLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARR 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 164 --RRFAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEFVAVKP-FADESEVDAFATRLWHCF 240
Cdd:COG5001 279 sgRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPdLDDPEDAEAVAERILAAL 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 241 SGKQTFAATEVILSASIGISVYPEDGTDINTVLSNSDLAMYRAKSSLDHKICWYEREMDDKTRQRNMMAADIRRGIQAGE 320
Cdd:COG5001 359 AEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGE 438
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 321 FSLHYQAIRNIKDRRITGYEALLRWQHPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVCSE----SLDNRLNKKISVNI 396
Cdd:COG5001 439 LELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQlaawQDAGLPDLRVAVNL 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 397 SPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFIINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDV 476
Cdd:COG5001 519 SARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDT 598
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556283197 477 IKLDRSFMQDVESNPQVRSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEPVDVKHLPR 549
Cdd:COG5001 599 LKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
22-541 |
2.15e-113 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 351.29 E-value: 2.15e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 22 AIYMLSADGTVISWNEGARRAKGYLSDEIVGR-YFGLFYSEAE-QLSRvpaKNLQIALRSGQ-FEGEGWRYRKDGSRFW- 97
Cdd:PRK10060 123 VIVILDSRGNIQRFNRLCEEYTGLKEHDVIGQsVFKLFMSRREaAASR---RNIRGFFRSGNaYEVERWIKTRKGQRLFl 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 98 ---AHVMINAIRDEQHnlLGFAKItrDISEQKAINDRIAWMARYDALTGLPNRVEFFERVEKLITGNDARRFAVFTIDLD 174
Cdd:PRK10060 200 frnKFVHSGSGKNEIF--LICSGT--DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLD 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 175 KFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEFVAVKPFADESEVDAFATRLWHCFsgKQTFAA--TEVI 252
Cdd:PRK10060 276 NFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRL--RLPFRIglIEVY 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 253 LSASIGISVYPEDGTDINTVLSNSDLAMYRAKSSLDHKICWYEREMDDKTRQRNMMAADIRRGIQAGEFSLHYQAIRNIK 332
Cdd:PRK10060 354 TGCSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWR 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 333 DRrITGYEALLRWQHPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVCSESLDNR---LNKKISVNISPVQLRHRSFIEK 409
Cdd:PRK10060 434 GE-VRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRdkgINLRVAVNVSARQLADQTIFTA 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 410 VREILMRTAYPVSLLEFEVTETAFIINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDVIKLDRSFMQDVES 489
Cdd:PRK10060 513 LKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHK 592
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 556283197 490 NPQVRSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEP 541
Cdd:PRK10060 593 QPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
20-549 |
4.50e-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: 340.22 E-value: 4.50e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 20 DYAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEAEQLSRVPAKNLQIALRSGQFEGEGWRYRKDGSRFWAH 99
Cdd:COG2200 40 ALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 100 VMINAIRDEQHNLLGFAkITRDISEQKAINDRIAWMARYDALTGLPNRVEFFERVEKLITGNDARRFAVFTIDLDKFKEI 179
Cdd:COG2200 120 LLLLLLLSLLLLLVLVL-LRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 180 NDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDE---FVAVKPFADESEVDAFATRLWHCFSGKQTFAATEVILSAS 256
Cdd:COG2200 199 LDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGggfLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 257 IGISVYPEDGTDInTVLSNSDLAMYRAKSSLDHKICWYEREMDDKTRQRNMMAADIRRGIQAGEFSLHYQAIRNIKDRRI 336
Cdd:COG2200 279 GGGAAAPDDGADA-ALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRV 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 337 TGYEALLRWQHPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVC---SESLDNRLNKKISVNISPVQLRHRSFIEKVREI 413
Cdd:COG2200 358 VGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALrqlARWPERGLDLRLSVNLSARSLLDPDFLERLLEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 414 LMRTAYPVSLLEFEVTETAFIINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDVIKLDRSFMQDVESNPQV 493
Cdd:COG2200 438 LAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRD 517
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 556283197 494 RSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEPVDVKHLPR 549
Cdd:COG2200 518 QAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEA 573
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
310-544 |
5.27e-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: 5.27e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 310 ADIRRGIQAGEFSLHYQAIRNIKDRRITGYEALLRWQHPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVC---SESLDN 386
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACrqlARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 387 RLNKKISVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFIINKQLAFSVLHHLQKMGISIALDDFGTGYSSL 466
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556283197 467 SMLRDFHFDVIKLDRSFMQDVESNPQVRSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEPVDV 544
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
311-542 |
1.55e-92 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 282.95 E-value: 1.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 311 DIRRGIQAGEFSLHYQAIRNIKDRRITGYEALLRWQHPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVCSESLDNR--- 387
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQaqg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 388 -LNKKISVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFIINKQLAFSVLHHLQKMGISIALDDFGTGYSSL 466
Cdd:smart00052 83 pPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556283197 467 SMLRDFHFDVIKLDRSFMQDVESNPQVRSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEPV 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 |
2.62e-85 |
|
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: 264.18 E-value: 2.62e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 309 AADIRRGIQAGEFSLHYQAIRNIKDRRITGYEALLRWQHPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVCSESLDNRL 388
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 389 N--KKISVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFIINKQLAFSVLHHLQKMGISIALDDFGTGYSSL 466
Cdd:pfam00563 81 GpdIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556283197 467 SMLRDFHFDVIKLDRSFMQDVESNPQVRSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEP 541
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
124-548 |
1.53e-84 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 278.96 E-value: 1.53e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 124 EQKAINDRIAWMARYDALTGLPNRVEFFERVEKLItgNDARRFAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTL 203
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLV--DKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 204 QKEEMVARFGGDEFVAVKPFADESEVDAFATRLWHCFSGKQTFAATEVILSASIGISVypEDGTDINTVLSNSDLAMYRA 283
Cdd:PRK11359 442 KPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 284 KSSLDHKICWYEREMDDKTRQRNMMAADIRRGIQAGEFSLHYQAIRNIKDRRITGYEALLRWQHPQLGAIPPEVFIPIAE 363
Cdd:PRK11359 520 RKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 364 ESGAIVPLGYWVLEQVCSESLDNRLN----KKISVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFIINKQL 439
Cdd:PRK11359 600 EIGEIENIGRWVIAEACRQLAEWRSQnihiPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTE 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 440 AFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDVIKLDRSFMQDVESNPQVRSFVRAIISLGNSINTPLIAEGVETE 519
Cdd:PRK11359 680 IFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETK 759
|
410 420
....*....|....*....|....*....
gi 556283197 520 GQRQILEEEGCDEMQGFLFGEPVDVKHLP 548
Cdd:PRK11359 760 EQFEMLRKIHCRVIQGYFFSRPLPAEEIP 788
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
302-549 |
4.54e-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: 236.74 E-value: 4.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 302 TRQRNMMAADIRRGIQAGEFSLHYQAIRNIKDRRITGYEALLRWQHPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVCS 381
Cdd:COG4943 266 LRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 382 EsLDNRLNK----KISVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFIINKQLAfSVLHHLQKMGISIALD 457
Cdd:COG4943 346 D-LGDLLAAdpdfHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR-AVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 458 DFGTGYSSLSMLRDFHFDVIKLDRSFMQDVESNPQVRSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFL 537
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
250
....*....|..
gi 556283197 538 FGEPVDVKHLPR 549
Cdd:COG4943 504 FAKPLPAEEFIA 515
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
126-542 |
4.64e-64 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 221.13 E-value: 4.64e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 126 KAINDRIAWMARYDALTGLPNRVEFFERVEKLITGNDArrFAVFTIDLDKFKEINdlqGHLIGDQ----LLQRVAGavLK 201
Cdd:PRK13561 221 QRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARKQT--TALMIITCETLRDTA---GVLKEAQreilLLTLVEK--LK 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 202 TLQKEEMV-ARFGGDEFVAVKPFADESevdafatrlWHCFS-GKQTFAATEVIL---------SASIGISVYpEDGTDIN 270
Cdd:PRK13561 294 SVLSPRMVlAQISGYDFAIIANGVKEP---------WHAITlGQQVLTIINERLpiqriqlrpSCSIGIAMF-YGDLTAE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 271 TVLSNSDLAMYRAKSSLDHKICWYEREMDDKTRQRNMMAADIRRGIQAGEFSLHYQAIRNIKDRRITGYEALLRWQHPQL 350
Cdd:PRK13561 364 QLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDG 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 351 GAIPPEVFIPIAEESGAIVPLGYWVLEQVC---SESLDNRLNKKISVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFE 427
Cdd:PRK13561 444 SWDLPEGLIDRIESCGLMVTVGHWVLEESCrllAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 428 VTETAFIINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFH---FDVIKLDRSFmqdVESNPQVRSFVRAIISLG 504
Cdd:PRK13561 524 VTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMF---VDGLPEDDSMVAAIIMLA 600
|
410 420 430
....*....|....*....|....*....|....*...
gi 556283197 505 NSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEPV 542
Cdd:PRK13561 601 QSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARAL 638
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
125-542 |
6.43e-61 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 212.88 E-value: 6.43e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 125 QKAINDRIAWMARYD---ALTGLPNRVEFFERVEKLITGNDARR-FAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVL 200
Cdd:PRK11829 218 QQLLADAYADMGRIShrfPVTELPNRSLFISLLEKEIASSTRTDhFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIE 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 201 KTLQKEEMVARFGGDEF-VAVKPFADESEVDAFATRLWHCFSGKQTFAATEVILSASIGISVYPEDGTDINTVLSNSDLA 279
Cdd:PRK11829 298 QCIDDSDLLAQLSKTEFaVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 280 MYRAKSSLDHKICWYEREMDDKTRQRNMMAADIRRGIQAGEFSLHYQAIRNIKDRRITGYEALLRWQHPQLGAIPPEVFI 359
Cdd:PRK11829 378 MMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFV 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 360 PIAEESGAIVPLGYWVLEQVCSESLDNR---LNKKISVNISPVQLRHRSFIEKVREILMRTAYPVSLLEFEVTETAFIIN 436
Cdd:PRK11829 458 HFAEEEGMMVPLGNWVLEEACRILADWKargVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQD 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 437 KQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFH---FDVIKLDRSFMQDVesnPQVRSFVRAIISLGNSINTPLIA 513
Cdd:PRK11829 538 LDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHLKslpIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMA 614
|
410 420
....*....|....*....|....*....
gi 556283197 514 EGVETEGQRQILEEEGCDEMQGFLFGEPV 542
Cdd:PRK11829 615 EGVETEEQRQWLLEHGIQCGQGFLFSPPL 643
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
310-549 |
7.64e-53 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 187.89 E-value: 7.64e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 310 ADIRRGIQAGEFSLHYQAIRNIKDRRITGYEALLRWQHPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVCSES--LDNR 387
Cdd:PRK10551 266 KEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAaeLQKV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 388 LNK--KISVNISPVQLRHRSFIEKVREilMRTAYPVSLLE--FEVTETAfIINKQLAFSVLHHLQKMGISIALDDFGTGY 463
Cdd:PRK10551 346 LPVgaKLGINISPAHLHSDSFKADVQR--LLASLPADHFQivLEITERD-MVQEEEATKLFAWLHSQGIEIAIDDFGTGH 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 464 SSLSMLRDFHFDVIKLDRSFMQDVESNPQVRSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEPVD 543
Cdd:PRK10551 423 SALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLP 502
|
....*.
gi 556283197 544 VKHLPR 549
Cdd:PRK10551 503 LEDFVR 508
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
92-542 |
3.41e-51 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 189.11 E-value: 3.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 92 DGSRFWAHVMINAIRDEQHNLLGFAKITRDISEQKAINDRIAWMARYDALTGLPNRVEFFERVEKLI-TGND-ARRFAVF 169
Cdd:PRK09776 621 SGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLqTVNStHQRHALV 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 170 TIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEFVAVKPFADESEVDAFATRLWHCFSGKQ-TFAA 248
Cdd:PRK09776 701 FIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHfPWEG 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 249 TEVILSASIGISVYPEDGTDINTVLSNSDLAMYRAKSSLDHKICWYEREMDDKTRQRNMM--AADIRRGIQAGEFSLHYQ 326
Cdd:PRK09776 781 RVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALslAEQWRMIKENQLMMLAHG 860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 327 AIRNIKDRRITGYEALLRWQHPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVCSESLDnRLNKK---ISVNISPVQLRH 403
Cdd:PRK09776 861 VASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAK-AVASKglsIALPLSVAGLSS 939
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 404 RSFIEKVREILMRTAYPVSLLEFEVTETAFIINKQLAFSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDVIKLDRSF 483
Cdd:PRK09776 940 PTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGEL 1019
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 556283197 484 MQDVESNPQVRSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEPV 542
Cdd:PRK09776 1020 VANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQ 1078
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
137-286 |
7.08e-51 |
|
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: 171.59 E-value: 7.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 137 RYDALTGLPNRVEFFERVEKLI--TGNDARRFAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGG 214
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLarARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556283197 215 DEFVAVKPFADESEVDAFATRLWHCFSGKQTFAATEVILSASIGISVYPEDGTDINTVLSNSDLAMYRAKSS 286
Cdd:cd01949 81 DEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRS 152
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
61-294 |
8.25e-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: 170.16 E-value: 8.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 61 EAEQLSRVPAKNLQIALRSGQFEGEGWRYRKDGSRFWAHVMINAIRDEQHNLLGFAKITRDISEQKAINDRIAWMARYDA 140
Cdd:COG2199 39 LLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 141 LTGLPNRVEFFERVEKLItgNDARR----FAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDE 216
Cdd:COG2199 119 LTGLPNRRAFEERLEREL--ARARRegrpLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDE 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556283197 217 FVAVKPFADESEVDAFATRLWHCFSGKQ-TFAATEVILSASIGISVYPEDGTDINTVLSNSDLAMYRAKSSLDHKICWY 294
Cdd:COG2199 197 FAVLLPGTDLEEAEALAERLREALEQLPfELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
134-294 |
1.86e-41 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 146.62 E-value: 1.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 134 WMARYDALTGLPNRVEFFERVEKLITGNDAR--RFAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVAR 211
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQgsPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 212 FGGDEFVAVKPFADESEVDAFATRLWHCFSGKQTFAATEVILSASIGISVYPEDGTDINTVLSNSDLAMYRAKSSLDHKI 291
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 556283197 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 |
1.14e-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: 138.92 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 136 ARYDALTGLPNRVEFFERVEKLItgNDARR----FAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVAR 211
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQEL--QRALRegspVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVAR 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556283197 212 FGGDEFVAVKPFADESEVDAFATRLWHCFSGKQTF---AATEVILSASIGISVYPEDGTDINTVLSNSDLAMYRAK 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 |
4.06e-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: 123.99 E-value: 4.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 135 MARYDALTGLPNRVEFFERVEKLItgNDARR----FAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVA 210
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSEL--KRARRfqrsFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVG 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556283197 211 RFGGDEFVAVKPFADESEVDAFATRLWHCFSGKQTFAATE--VILSASIGISVYPEDGTDINTVLSNSDLAMYRAKSS 286
Cdd:TIGR00254 79 RYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSetLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKA 156
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
134-293 |
9.70e-25 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 108.18 E-value: 9.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 134 WMARYDALTGLPNRVEFFERVEKLIT--GNDARRFAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVAR 211
Cdd:PRK15426 396 WQAWHDPLTRLYNRGALFEKARALAKrcQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGR 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 212 FGGDEFVAVKPFADESEVDAFATRLWHCFSGKQTFAATEVIL--SASIGISVYPEDGT-DINTVLSNSDLAMYRAKSSLD 288
Cdd:PRK15426 476 VGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIriSASLGVSSAEEDGDyDFEQLQSLADRRLYLAKQAGR 555
|
....*
gi 556283197 289 HKICW 293
Cdd:PRK15426 556 NRVCA 560
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
139-544 |
6.81e-22 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 99.55 E-value: 6.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 139 DALTGLPNRVEFFERVEKLI--TGNDARRFAVFTIDLDKFKEINDLQGHLIGD-----------QLLQRVAGAVLktlqk 205
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLedQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEellfelinllsTFVMRYPGALL----- 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 206 eemvARFGGDEFVAVKPFADESEVDAFATRLWH-CfsgkQTFAATEVILSAS---IGISVYPEdGTDINTVLSNSDLAMY 281
Cdd:PRK11059 306 ----ARYSRSDFAVLLPHRSLKEADSLASQLLKaV----DALPPPKMLDRDDflhIGICAYRS-GQSTEQVMEEAEMALR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 282 RAK----SSldhkicWYereMDDKTRQrnmmaADIRRG-----------IQAGEFSLHYQAIRNiKDRRITGYEALLRWQ 346
Cdd:PRK11059 377 SAQlqggNG------WF---VYDKAQL-----PEKGRGsvrwrtlleqtLVRGGPRLYQQPAVT-RDGKVHHRELFCRIR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 347 HPQLGAIPPEVFIPIAEESGAIVPLGYWVLEQVCSEsLDNRLNKKISVNISPVQLRHRSFIEKVREILMRtaYPVSLLE- 425
Cdd:PRK11059 442 DGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPL-LRYWPEENLSINLSVDSLLSRAFQRWLRDTLLQ--CPRSQRKr 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 426 --FEVTEtAFIIN--KQLAfSVLHHLQKMGISIALDDFGTGYSSLSMLRDFHFDVIKLDRSFMQDVESNPQVRSFVRAII 501
Cdd:PRK11059 519 liFELAE-ADVCQhiSRLR-PVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLV 596
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 556283197 502 SLGNSINTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEPVDV 544
Cdd:PRK11059 597 GACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
135-286 |
2.54e-21 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 96.89 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 135 MARYDALTGLPNRvEFFER-----VEKLITGNdaRRFAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMV 209
Cdd:PRK09581 291 MAVTDGLTGLHNR-RYFDMhlknlIERANERG--KPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLI 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 210 ARFGGDEFVAVKPFADESEVDAFATRLwhcfsgKQTFAATEVILS---------ASIGISVYPEDGTDINTVLSNSDLAM 280
Cdd:PRK09581 368 ARYGGEEFVVVMPDTDIEDAIAVAERI------RRKIAEEPFIISdgkerlnvtVSIGVAELRPSGDTIEALIKRADKAL 441
|
....*.
gi 556283197 281 YRAKSS 286
Cdd:PRK09581 442 YEAKNT 447
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
11-220 |
9.44e-21 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 92.01 E-value: 9.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEaEQLSRVPAKNLQIALRSGQFEGEGWRYR 90
Cdd:COG2202 13 LRALVESSPD-AIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPP-EDDDEFLELLRAALAGGGVWRGELRNRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 91 KDGSRFWAHVMINAIRDEQHNLLGFAKITRDISEQKAINDRIAWMARYDALTGLPNRVEFFERVE--KLITGNDA-RRFA 167
Cdd:COG2202 91 KDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLdgRILYVNPAaEELL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 556283197 168 VFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGGDEFVAV 220
Cdd:COG2202 171 GYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWV 223
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
138-286 |
3.68e-18 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 85.12 E-value: 3.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 138 YDALTGLPNR---VEFFERVEKLITGndaRRFAVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEEMVARFGG 214
Cdd:PRK09894 131 MDVLTGLPGRrvlDESFDHQLRNREP---QNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556283197 215 DEFVAVKPFADESEVDAFATRLWHCFSGKQ-TFAATEVILSASIGISVYPEDGTdINTVLSNSDLAMYRAKSS 286
Cdd:PRK09894 208 EEFIICLKAATDEEACRAGERIRQLIANHAiTHSDGRINITATFGVSRAFPEET-LDVVIGRADRAMYEGKQT 279
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
29-124 |
1.35e-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: 66.72 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 29 DGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEAEQLSRVPAknlQIALRSGQFEGEGWRYRKDGSRFWAHVMINAIRDE 108
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLRE---ALREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 556283197 109 QHNLLGFAKITRDISE 124
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
122-286 |
3.03e-13 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 71.40 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 122 ISEQKAI-----NDRIAWMARYDALTGLPNRV--EFFERVEKLITGNDARRFAVFTIDLDKFKEINDLQGHLIGDQLLQR 194
Cdd:PRK10245 186 VSYQTATklaehKRRLQVMSTRDGMTGVYNRRhwETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVA 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 195 VAGAVLKTLQKEEMVARFGGDEFVAVKPFADESEVDAFATRLWHCFSGKQTFAATEVILSASIGISVYPEDGTDINTVLS 274
Cdd:PRK10245 266 LTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLK 345
|
170
....*....|..
gi 556283197 275 NSDLAMYRAKSS 286
Cdd:PRK10245 346 SADLALYKAKNA 357
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
126-284 |
2.81e-11 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 65.41 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 126 KAINDRIAWMARYDALTGLPNRVEFFERVEKLITGNDARRF-AVFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQ 204
Cdd:PRK09966 238 QAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTsALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGG 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 205 KEEMVARFGGDEFVAV-KPFADESEVDAFATRLWHCFSGK-QTFAATEVILSASIGISVYPEDGTdINTVLSNSDLAMYR 282
Cdd:PRK09966 318 LRHKAYRLGGDEFAMVlYDVQSESEVQQICSALTQIFNLPfDLHNGHQTTMTLSIGYAMTIEHAS-AEKLQELADHNMYQ 396
|
..
gi 556283197 283 AK 284
Cdd:PRK09966 397 AK 398
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
11-144 |
5.74e-11 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 64.10 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEAEQLsrvpAKNLQIALRSGQ--FEGEGWR 88
Cdd:COG3852 9 LRAILDSLPD-AVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPL----RELLERALAEGQpvTEREVTL 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 556283197 89 YRKDGSRFWAHVMINAIRDEQHNlLGFAKITRDISEQKAINDRIAWMARYDALTGL 144
Cdd:COG3852 84 RRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
11-126 |
1.09e-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: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEaEQLSRVPAK-NLQIALRSGQFEGEGWRY 89
Cdd:TIGR00229 5 YRAIFESSPD-AIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPE-EDREEVRERiERRLEGEPEPVSEERRVR 82
|
90 100 110
....*....|....*....|....*....|....*..
gi 556283197 90 RKDGSRFWAHVMINAIRDEQhNLLGFAKITRDISEQK 126
Cdd:TIGR00229 83 RKDGSEIWVEVSVSPIRTNG-GELGVVGIVRDITERK 118
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
326-545 |
4.75e-10 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 61.74 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 326 QAIRNiKDRRITGYEALLRwqhpqlgaIPPEVFIPIAEESGAIVPLgywVLEQVCSESLDNRLNKKIS-VNISpvqlrHR 404
Cdd:COG3434 9 QPILD-RDQRVVGYELLFR--------SGLENSAPDVDGDQATARV---LLNAFLEIGLDRLLGGKLAfINFT-----EE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 405 SFIEKVREILmrtayPVSLLEFEVTETAfIINKQLaFSVLHHLQKMGISIALDDFGTGYSSLSMLRdfHFDVIKLDrsFM 484
Cdd:COG3434 72 LLLSDLPELL-----PPERVVLEILEDV-EPDEEL-LEALKELKEKGYRIALDDFVLDPEWDPLLP--LADIIKID--VL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556283197 485 QDveSNPQVRSFVRAIISLgnsiNTPLIAEGVETEGQRQILEEEGCDEMQGFLFGEPVDVK 545
Cdd:COG3434 141 AL--DLEELAELVARLKRY----GIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILK 195
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
11-122 |
1.85e-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: 55.50 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEAEQLSRVPAKNLQIALRSGQFEGEGWRYR 90
Cdd:pfam00989 3 LRAILESLPD-GIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRV 81
|
90 100 110
....*....|....*....|....*....|..
gi 556283197 91 KDGSRFWAHVMINAIRDEQHNLLGFAKITRDI 122
Cdd:pfam00989 82 PDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
168-260 |
8.17e-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: 51.20 E-value: 8.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 168 VFTIDLDKFKEINDLQGHLIGDQLLQRVAGAVLKTLQKEE-MVARFGGDEFVAVKPFADESEVDAFATRLWHCFSGKQtf 246
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALN-- 81
|
90
....*....|....
gi 556283197 247 AATEVILSASIGIS 260
Cdd:cd07556 82 QSEGNPVRVRIGIH 95
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
11-132 |
8.26e-08 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 53.49 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEAEQLSRvpAKNLQIALRSGQFEGEGWRYR 90
Cdd:COG2202 139 LRLLVENAPD-GIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERL--LELLRRLLEGGRESYELELRL 215
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 556283197 91 KDGSRFWAHVMINAIRDE-QHNLLGFAKITRDISEQKAINDRI 132
Cdd:COG2202 216 KDGDGRWVWVEASAVPLRdGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
11-130 |
1.36e-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: 54.21 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLF-YSEAEQLSRVPAKNLQIALRSGQFEGEgwRY 89
Cdd:COG5809 17 FRSLFENAPD-AILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFlHPDDEKELREILKLLKEGESRDELEFE--LR 93
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 556283197 90 RKDGSRFWAHVMINAIRDEQHNLLGFAKITRDISEQKAIND 130
Cdd:COG5809 94 HKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEE 134
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
20-122 |
1.37e-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: 49.94 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 20 DYAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEaEQLSRVPAKNLQIALRSGQFEGEGWRYRKDGSRFWAH 99
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHP-EDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 556283197 100 VMINAIRDEQHNLLGFAKITRDI 122
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
196-284 |
6.53e-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: 49.52 E-value: 6.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 196 AGA---VLKTLQKEE------MVARFGGDEFVAVKPFADESEVDAFATRLWHCFSgkqtfAATEVILSASIGISvypedg 266
Cdd:COG3706 96 AGAddyLTKPFDPEEllarvdLVARYGGEEFAILLPGTDLEGALAVAERIREAVA-----ELPSLRVTVSIGVA------ 164
|
90
....*....|....*...
gi 556283197 267 tdINTVLSNSDlAMYRAK 284
Cdd:COG3706 165 --GDSLLKRAD-ALYQAR 179
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
456-542 |
4.40e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 48.46 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 456 LDDFGTGYSSLSMLRDFHFDVIKLDRSFMQDVESNPQVRSFVRAIISLGNSINTPLIAEGVETEGQRQILEEEGCDEMQG 535
Cdd:PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQG 236
|
....*..
gi 556283197 536 FLFGEPV 542
Cdd:PRK11596 237 YFLSRPA 243
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
32-118 |
2.62e-05 |
|
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: 42.71 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 32 VISWNEGARRAKGYLSDEIVGRYFGLF-YSEAEQLSRVpAKNLQIALRSGQ-FEGEGWRYRKDGSRFWAHVMINAIRDEQ 109
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGESWLdLVHPDDRERV-REALWEALKGGEpYSGEYRIRRKDGEYRWVEARARPIRDEN 79
|
....*....
gi 556283197 110 HNLLGFAKI 118
Cdd:pfam08447 80 GKPVRVIGV 88
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
11-132 |
4.86e-05 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 45.92 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFglfyseaeqLSRVPAKNLQIALRSGQ-FEGEGWRY 89
Cdd:COG3829 13 LEAILDSLDD-GIIVVDADGRITYVNRAAERILGLPREEVIGKNV---------TELIPNSPLLEVLKTGKpVTGVIQKT 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 556283197 90 RKDGSrfwaHVMINAIR-DEQHNLLGFAKITRDISEQKAINDRI 132
Cdd:COG3829 83 GGKGK----TVIVTAIPiFEDGEVIGAVETFRDITELKRLERKL 122
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
29-164 |
2.77e-04 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 43.67 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 29 DGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEAEQLSRVPA--------KNLQIALRSgqfegegwrYRKDGSRFWAHV 100
Cdd:PRK13558 170 DEPLIYINDAFERITGYSPDEVLGRNCRFLQGEDTNEERVAElreaideeRPTSVELRN---------YRKDGSTFWNQV 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556283197 101 MINAIRDEQHNLLGFAKITRDISEQKAINDRIAwmARYDALTGLPNRVE-FFERVEKLITGNDAR 164
Cdd:PRK13558 241 DIAPIRDEDGTVTHYVGFQTDVTERKEAELALQ--RERRKLQRLLERVEgLVNDVTSALVRATDR 303
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
15-144 |
6.67e-04 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 42.65 E-value: 6.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 15 IESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEAEQLSRVpaknLQIALRSGQFE-GEGWRYRKDG 93
Cdd:PRK11360 268 LESIAD-GVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELFPPNTPFASP----LLDTLEHGTEHvDLEISFPGRD 342
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 556283197 94 SRFWAHVMINAIRDEQHNLLGFAKITRDISEQKAINDRiawMARYDALTGL 144
Cdd:PRK11360 343 RTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRR---VARQERLAAL 390
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
11-126 |
8.17e-04 |
|
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: 41.88 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSEAEQlSRVPAKNLQIALRSGQFEGEGWRYR 90
Cdd:COG5809 143 FRLIFNHSPD-GIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQ-ENVAAFISQLLKDGGIAQGEVRFWT 220
|
90 100 110
....*....|....*....|....*....|....*..
gi 556283197 91 KDGSRFWAHVMINAI-RDEQHNllGFAKITRDISEQK 126
Cdd:COG5809 221 KDGRWRLLEASGAPIkKNGEVD--GIVIIFRDITERK 255
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
89-125 |
8.43e-04 |
|
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: 37.16 E-value: 8.43e-04
10 20 30
....*....|....*....|....*....|....*..
gi 556283197 89 YRKDGSRFWAHVMINAIRDEQHNLLGFAKITRDISEQ 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 |
2.49e-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: 37.78 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 22 AIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFGLFYSE--AEQLSRvpakNLQIALRSGQFEGEGWRYRKDGSRFWAH 99
Cdd:pfam08448 7 ALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPedAARLER----ALRRALEGEEPIDFLEELLLNGEERHYE 82
|
90 100
....*....|....*....|....*...
gi 556283197 100 VMINAIRDEQHNLLGFAKITRDISEQKA 127
Cdd:pfam08448 83 LRLTPLRDPDGEVIGVLVISRDITERRR 110
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
11-126 |
3.33e-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: 40.10 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKDyAIYMLSADGTVISWNEGARRAKGYLSDEIVGRYFgLFYSEAEQLSRVPAKNLQIALRSGQFEGEGWRYR 90
Cdd:COG5805 159 LQTLIENSPD-LICVIDTDGRILFINESIERLFGAPREELIGKNL-LELLHPCDKEEFKERIESITEVWQEFIIEREIIT 236
|
90 100 110
....*....|....*....|....*....|....*.
gi 556283197 91 KDGSRFWAHVMINAIRDEQHNLLGFAKITRDISEQK 126
Cdd:COG5805 237 KDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKK 272
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
11-132 |
8.68e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 38.89 E-value: 8.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556283197 11 YRHFIESVKdYAIYMLSADGTVIS-WNEGARRAKGYLSDEIVG----------------RYFGLFYSEAEQLSrVPAKNL 73
Cdd:PRK13560 334 LRAIIEAAP-IAAIGLDADGNICFvNNNAAERMLGWSAAEVMGkplpgmdpelneefwcGDFQEWYPDGRPMA-FDACPM 411
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556283197 74 QIALRSGQ-FEG-EGWRYRKDGSrfWAHVMINA--IRDEQHNLLGFAKITRDISEQKAINDRI 132
Cdd:PRK13560 412 AKTIKGGKiFDGqEVLIEREDDG--PADCSAYAepLHDADGNIIGAIALLVDITERKQVEEQL 472
|
|
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