|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
45-686 |
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: 538.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 45 RRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGAIRRVFECGEASLEAPLLTRSGQTPVFRYSGQLVDVDGEPLIA 124
Cdd:COG5001 18 LLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 125 GIGVDISEQKAAERASARQTEQFRHVAGQVPGVIYQLRYEPGTGIFSMPYASAKLFEVFGVEHSEVVENAQALFDRIAPE 204
Cdd:COG5001 98 ALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 205 DEARVQRAAEQSRQSLcRFHEQFRMLPPGGQLEHAEWVEVDSSPERDQDGAVTWHGFARLITGRRRMEDELVRLAYEDAL 284
Cdd:COG5001 178 LLLLLALLLLLLLALL-LRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 285 TGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDRGLVGRLGGDEFLI 364
Cdd:COG5001 257 TGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 365 IVQGESVEGPAARLASALCAAMDSPVSVDDRLLRVTASIGMSLFPKDGETAEDLLRHADAALYRAKEEGPSNWASYTPEL 444
Cdd:COG5001 337 LLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEM 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 445 TAAAMARRYLETELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIALAESRGLVAALGEQVYRK 524
Cdd:COG5001 417 DERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLRE 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 525 AMRAVARIDATS----RLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAFMDELADKLEQLESLRRQGIAI 600
Cdd:COG5001 497 ACRQLAAWQDAGlpdlRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRI 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 601 AIDDFGTGYSSLAYLRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSVTAEGVQSAEELEEVRAHGCDCAQ 680
Cdd:COG5001 577 ALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQ 656
|
....*.
gi 1839367027 681 GWHLGR 686
Cdd:COG5001 657 GYLFSR 662
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
122-691 |
5.87e-101 |
|
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: 320.96 E-value: 5.87e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 122 LIAGIGVDISEQKAAERASARQTEQFRHVAGQVPGVIYQLRYEPGTGIFSMPYASAKLFEVFGVEHSEVVENAQALFDRI 201
Cdd:COG2200 3 LLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 202 APEDEARVQRAAEQSRQSLCRFHEQFRMLPPGGQLEHAEWVEVDSSPERDQDGavtwhgFARLITGRRRMEDELVRLAYE 281
Cdd:COG2200 83 LALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLV------LLRLALELLLALLLLALLALL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 282 DALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDR-GLVGRLGGD 360
Cdd:COG2200 157 DLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLlLALLGGGGG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 361 EFLIIVQGESVEGPAARLASALCAAMDSPVSVDDRLLRVTASIGMSLFPKDGETAEDLLRHADAALYRAKEEGPSNWASY 440
Cdd:COG2200 237 GFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 441 TPELtAAAMARRYLETELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIALAESRGLVAALGEQ 520
Cdd:COG2200 317 AAAE-ARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRW 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 521 VYRKAMRAVARIDATS---RLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAFMDELADKLEQLESLRRQG 597
Cdd:COG2200 396 VLERALRQLARWPERGldlRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 598 IAIAIDDFGTGYSSLAYLRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSVTAEGVQSAEELEEVRAHGCD 677
Cdd:COG2200 476 VRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCD 555
|
570
....*....|....
gi 1839367027 678 CAQGWHLGRGQLVE 691
Cdd:COG2200 556 YAQGYLFGRPLPLE 569
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
456-686 |
7.77e-94 |
|
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: 290.60 E-value: 7.77e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 456 TELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIALAESRGLVAALGEQVYRKAMRAVARIDAT 535
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 536 S---RLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAFMDELADKLEQLESLRRQGIAIAIDDFGTGYSSL 612
Cdd:cd01948 81 GpdlRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1839367027 613 AYLRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSVTAEGVQSAEELEEVRAHGCDCAQGWHLGR 686
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSR 234
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
265-686 |
5.49e-93 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 302.37 E-value: 5.49e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 265 ITGRRRMEDELVRLAYEDALTGMPNRTSLQLRLEEQIAEAsiVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRL 344
Cdd:PRK10060 223 ITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAA--DNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 345 REVVGDRGLVGRLGGDEFLIIVQGESVEGPAArLASALCAAMDSPVSVDdrLLRV--TASIGMSLFPKDGETAEDLLRHA 422
Cdd:PRK10060 301 LSCLEEDQTLARLGGDEFLVLASHTSQAALEA-MASRILTRLRLPFRIG--LIEVytGCSIGIALAPEHGDDSESLIRSA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 423 DAALYRAKEEGPSNWASYTPELTAAAMARRYLETELRGAVDRDEIQVALQPVVDLSsGEVVAYEALARWHHREDGWIDPE 502
Cdd:PRK10060 378 DTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 503 QFIALAESRGLVAALGEQVYRKAMRAVARIDATS---RLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAF 579
Cdd:PRK10060 457 EFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGinlRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCL 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 580 MDELADKLEQLESLRRQGIAIAIDDFGTGYSSLAYLRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSVTA 659
Cdd:PRK10060 537 IENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIA 616
|
410 420
....*....|....*....|....*..
gi 1839367027 660 EGVQSAEELEEVRAHGCDCAQGWHLGR 686
Cdd:PRK10060 617 EGVETAKEDAFLTKNGVNERQGFLFAK 643
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
455-692 |
1.24e-80 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 256.38 E-value: 1.24e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 455 ETELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIALAESRGLVAALGEQVYRKAMRAVARIDA 534
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 535 TS----RLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAFMDELADKLEQLESLRRQGIAIAIDDFGTGYS 610
Cdd:smart00052 81 QGppplLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 611 SLAYLRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSVTAEGVQSAEELEEVRAHGCDCAQGWHLGRGQLV 690
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 1839367027 691 EL 692
Cdd:smart00052 241 DD 242
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
267-686 |
8.55e-80 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 270.49 E-value: 8.55e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 267 GRRRMEdELVRLayeDALTGMPNRTSLQLRLEEQIAEAsivgQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLRE 346
Cdd:PRK11359 368 SRQHIE-QLIQF---DPLTGLPNRNNLHNYLDDLVDKA----VSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 347 VVGDRGLVGRLGGDEFLIIVQGESVEGpAARLASALCAAMDSPVSVDDRLLRVTASIGMSLfpKDGETAEDLLRHADAAL 426
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVLVSLENDVSN-ITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAM 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 427 YRAKEEGPSNWASYTPELTAAAMARRYLETELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIA 506
Cdd:PRK11359 517 DYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIP 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 507 LAESRGLVAALGEQVYRKAMRAVARIDA----TSRLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAFMDE 582
Cdd:PRK11359 597 LAEEIGEIENIGRWVIAEACRQLAEWRSqnihIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEH 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 583 LADKLEQLESLRRQGIAIAIDDFGTGYSSLAYLRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSVTAEGV 662
Cdd:PRK11359 677 DTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGV 756
|
410 420
....*....|....*....|....
gi 1839367027 663 QSAEELEEVRAHGCDCAQGWHLGR 686
Cdd:PRK11359 757 ETKEQFEMLRKIHCRVIQGYFFSR 780
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
270-686 |
6.64e-75 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 253.87 E-value: 6.64e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 270 RMEDELVRLAYEDALTGMPNRTSLQLRLEEQIAEasivGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVG 349
Cdd:PRK13561 222 RQYEEQSRNATRFPVSDLPNKALLMALLEQVVAR----KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 350 DRGLVGRLGGDEFLIIVQGesVEGP--AARLASALCAAMDSPVSVDDRLLRVTASIGMSLFpKDGETAEDLLRHADAALY 427
Cdd:PRK13561 298 PRMVLAQISGYDFAIIANG--VKEPwhAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAF 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 428 RAKEEGPSNWASYTPELTAAAMARRYLETELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIAL 507
Cdd:PRK13561 375 TARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDR 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 508 AESRGLVAALGEQVYRKAMRAVARIDA---TSRLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAFMDELA 584
Cdd:PRK13561 455 IESCGLMVTVGHWVLEESCRLLAAWQErgiMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPH 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 585 DKLEQLESLRRQGIAIAIDDFGTGYSSLAYLRH---LPVQRLKIDQVFVRGLasnPKNSAIMKAIVTLARELGFSVTAEG 661
Cdd:PRK13561 535 AAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEG 611
|
410 420
....*....|....*....|....*
gi 1839367027 662 VQSAEELEEVRAHGCDCAQGWHLGR 686
Cdd:PRK13561 612 VETEAQRDWLLKAGVGIAQGFLFAR 636
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
457-686 |
1.09e-74 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 240.30 E-value: 1.09e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 457 ELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIALAESRGLVAALGEQVYRKAMRAVARIDATS 536
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 537 --RLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAFMDELADKLEQLESLRRQGIAIAIDDFGTGYSSLAY 614
Cdd:pfam00563 83 diKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1839367027 615 LRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSVTAEGVQSAEELEEVRAHGCDCAQGWHLGR 686
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSK 234
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
277-682 |
2.91e-72 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 247.16 E-value: 2.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 277 RLAYEDALTGMPNRTSLQLRLEEQIAeASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDRGLVGR 356
Cdd:PRK11829 230 RISHRFPVTELPNRSLFISLLEKEIA-SSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 357 LGGDEFLIIVQGESVEGPAARLASALCAAMDSPVSVDDRLLRVTASIGMSLFPKDGETAEDLLRHADAALYRAKEEGPSN 436
Cdd:PRK11829 309 LSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQ 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 437 WASYTPELTAAAMARRYLETELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIALAESRGLVAA 516
Cdd:PRK11829 389 IMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVP 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 517 LGEQVYRKAMRAVA---RIDATSRLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAFMDELADKLEQLESL 593
Cdd:PRK11829 469 LGNWVLEEACRILAdwkARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLREL 548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 594 RRQGIAIAIDDFGTGYSSLAYLRH---LPVQRLKIDQVFVRGLasnPKNSAIMKAIVTLARELGFSVTAEGVQSAEELEE 670
Cdd:PRK11829 549 QGLGLLIALDDFGIGYSSLRYLNHlksLPIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQW 625
|
410
....*....|..
gi 1839367027 671 VRAHGCDCAQGW 682
Cdd:PRK11829 626 LLEHGIQCGQGF 637
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
451-686 |
1.36e-68 |
|
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: 233.65 E-value: 1.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 451 RRYLETELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIALAESRGLVAALGEQVYRKAMRAVA 530
Cdd:COG4943 269 RLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 531 RIDATSR---LSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITERAFMDeLADKLEQLESLRRQGIAIAIDDFGT 607
Cdd:COG4943 349 DLLAADPdfhISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFID-PAKARAVIAALREAGHRIAIDDFGT 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1839367027 608 GYSSLAYLRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSVTAEGVQSAEELEEVRAHGCDCAQGWHLGR 686
Cdd:COG4943 428 GYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAK 506
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
265-688 |
2.14e-58 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 213.77 E-value: 2.14e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 265 ITGRRRMEDELVRLAYEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRL 344
Cdd:PRK09776 651 VTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLM 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 345 REVVGDRGLVGRLGGDEFLIIVQG---ESVEGPAARLASALCaamDSPVSVDDRLLRVTASIGMSLFPKDGETAEDLLRH 421
Cdd:PRK09776 731 LSMLRSSDVLARLGGDEFGLLLPDcnvESARFIATRIISAIN---DYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQ 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 422 ADAALYRAKEEGPSNWASYTPELTAAAMARRYLE--TELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWI 499
Cdd:PRK09776 808 ADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSlaEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEII 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 500 DPEQFIALAESRGLVAALGEQVYRKAMR-AVARIDATS-RLSINVAPVQLKDPQFARRLVRMARDCGLQPARLEVEITER 577
Cdd:PRK09776 888 DEGAFRPAAEDPALMHALDRRVIHEFFRqAAKAVASKGlSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITET 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 578 AFMDELADKLEQLESLRRQGIAIAIDDFGTGYSSLAYLRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSV 657
Cdd:PRK09776 968 ALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKT 1047
|
410 420 430
....*....|....*....|....*....|.
gi 1839367027 658 TAEGVQSAEELEEVRAHGCDCAQGWHLGRGQ 688
Cdd:PRK09776 1048 IAGPVELPLVLDTLSGIGVDLAYGYAIARPQ 1078
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
173-440 |
4.38e-57 |
|
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: 195.20 E-value: 4.38e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 173 PYASAKLFEVFGVEHSEVVENAQALFDRIAPEDEARVQRAAEQSRQSLCRFHEQFRMLPPGGQLEHAEWVEVDSSPERDQ 252
Cdd:COG2199 8 LLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 253 DGAVTWHGFARLITGRRRMEDELVRLAYEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGS 332
Cdd:COG2199 88 LALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 333 GDRLLEELAGRLREVVGDRGLVGRLGGDEFLIIVQGESVEGpAARLASALCAAMDS-PVSVDDRLLRVTASIGMSLFPKD 411
Cdd:COG2199 168 GDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEE-AEALAERLREALEQlPFELEGKELRVTVSIGVALYPED 246
|
250 260
....*....|....*....|....*....
gi 1839367027 412 GETAEDLLRHADAALYRAKEEGPSNWASY 440
Cdd:COG2199 247 GDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
280-433 |
5.31e-56 |
|
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: 187.76 E-value: 5.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 280 YEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDRGLVGRLGG 359
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1839367027 360 DEFLIIVQGESVEGpAARLASALCAAMDSPVSVDDRLLRVTASIGMSLFPKDGETAEDLLRHADAALYRAKEEG 433
Cdd:cd01949 81 DEFAILLPGTDLEE-AEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSG 153
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
277-440 |
5.89e-51 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 174.36 E-value: 5.89e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 277 RLAYEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDRGLVGR 356
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 357 LGGDEFLIIVQGESVEGpAARLASALCAAMDSPVSVDDRLLRVTASIGMSLFPKDGETAEDLLRHADAALYRAKEEGPSN 436
Cdd:smart00267 81 LGGDEFALLLPETSLEE-AIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 1839367027 437 WASY 440
Cdd:smart00267 160 VAVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
279-433 |
1.22e-50 |
|
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: 173.59 E-value: 1.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 279 AYEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDRGLVGRLG 358
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1839367027 359 GDEFLIIVQGESVEGP--AARLASALCAAMDSPVSVDDRLLRVTASIGMSLFPKDGETAEDLLRHADAALYRAKEEG 433
Cdd:pfam00990 81 GDEFAILLPETSLEGAqeLAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAG 157
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
278-433 |
1.58e-40 |
|
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: 145.94 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 278 LAYEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDRGLVGRL 357
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1839367027 358 GGDEFLIIVQGESVEGpAARLASALCAAMDS-PVSV-DDRLLRVTASIGMSLFPKDGETAEDLLRHADAALYRAKEEG 433
Cdd:TIGR00254 81 GGEEFVVILPGTPLED-ALSKAERLRDAINSkPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAG 157
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
455-691 |
1.93e-39 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 152.45 E-value: 1.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 455 ETELRGAVDRDEIQVALQPVVDLSSGEVVAYEALARWHHREDGWIDPEQFIALAESRGLVAALG----EQVYRKAMRAVA 530
Cdd:PRK10551 265 GKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTqhlfELIARDAAELQK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 531 RIDATSRLSINVAPVQLKDPQF---ARRLVRMardcgLQPARLEV--EITERAFMDElADKLEQLESLRRQGIAIAIDDF 605
Cdd:PRK10551 345 VLPVGAKLGINISPAHLHSDSFkadVQRLLAS-----LPADHFQIvlEITERDMVQE-EEATKLFAWLHSQGIEIAIDDF 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 606 GTGYSSLAYLRHLPVQRLKIDQVFVRGLASNPKNSAIMKAIVTLARELGFSVTAEGVQSAEELEEVRAHGCDCAQGWHLG 685
Cdd:PRK10551 419 GTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWIS 498
|
250
....*....|
gi 1839367027 686 R----GQLVE 691
Cdd:PRK10551 499 RplplEDFVR 508
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
261-433 |
1.38e-30 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 125.40 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 261 FARLITG--RRRMEDEL-------VRLAYEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHG 331
Cdd:PRK09581 265 LARVRTQirRKRYQDALrnnleqsIEMAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHD 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 332 SGDRLLEELAGRLREVVgdRG--LVGRLGGDEFLIIVQGESVEgPAARLASAL---CAAMDSPVSVDDRLLRVTASIGMS 406
Cdd:PRK09581 345 AGDEVLREFAKRLRNNI--RGtdLIARYGGEEFVVVMPDTDIE-DAIAVAERIrrkIAEEPFIISDGKERLNVTVSIGVA 421
|
170 180
....*....|....*....|....*..
gi 1839367027 407 LFPKDGETAEDLLRHADAALYRAKEEG 433
Cdd:PRK09581 422 ELRPSGDTIEALIKRADKALYEAKNTG 448
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
249-433 |
4.61e-26 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 109.00 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 249 ERDQDGAVTWHGFARLITGR-------RRMEDELVRLAYE-DALTGMPNRTSLQLRLEEQIAEASivGQELALLHLDLDN 320
Cdd:PRK09894 91 LAIVEGHWQDAHFDAFQEGLlsftaalTDYKIYLLTIRSNmDVLTGLPGRRVLDESFDHQLRNRE--PQNLYLALLDIDR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 321 FKDINDIWGHGSGDRLLEELAGRLREVVGDRGLVGRLGGDEFLIIVQGESVEgPAARLASALCAA-MDSPVSVDDRLLRV 399
Cdd:PRK09894 169 FKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDE-EACRAGERIRQLiANHAITHSDGRINI 247
|
170 180 190
....*....|....*....|....*....|....*
gi 1839367027 400 TASIGMS-LFPkdGETAEDLLRHADAALYRAKEEG 433
Cdd:PRK09894 248 TATFGVSrAFP--EETLDVVIGRADRAMYEGKQTG 280
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
274-432 |
1.42e-25 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 109.71 E-value: 1.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 274 ELVRLAYEDALTGMPNRTSLQLRLEEQIAEASIVGQElALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDRGL 353
Cdd:PRK09966 243 QLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 354 VGRLGGDEFLIIVQGESVEGPAARLASALCAAMDSPVSVDD-RLLRVTASIGMSLfPKDGETAEDLLRHADAALYRAKEE 432
Cdd:PRK09966 322 AYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNgHQTTMTLSIGYAM-TIEHASAEKLQELADHNMYQAKHQ 400
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
278-433 |
3.91e-24 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 107.02 E-value: 3.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 278 LAYEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDRGLVGRL 357
Cdd:PRK15426 397 QAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1839367027 358 GGDEFLIIVQGESVEGpAARLASALCAAMDSP--VSVDDRLLRVTASIGMSLFPKDGE-TAEDLLRHADAALYRAKEEG 433
Cdd:PRK15426 477 GGEEFCVVLPGASLAE-AAQVAERIRLRINEKeiLVAKSTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLYLAKQAG 554
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
23-275 |
4.94e-24 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 102.03 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 23 LLDAVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGAIRRVFECGEA-SLEAPLLTR 101
Cdd:COG2202 12 RLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGGVwRGELRNRRK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 102 SGQT-PVFRYSGQLVDVDGEPL-IAGIGVDISEQKAAERASARQTEQFRHVAGQVPGVIYQLRYEpgtGIFSmpYASAKL 179
Cdd:COG2202 92 DGSLfWVELSISPVRDEDGEITgFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLD---GRIL--YVNPAA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 180 FEVFGVEHSEVVEnaQALFDRIAPEDEARVQRAAEQSRQSLCRFHE-QFRMLPPGGqleHAEWVEVDSSPERDQDGAVTW 258
Cdd:COG2202 167 EELLGYSPEELLG--KSLLDLLHPEDRERLLELLRRLLEGGRESYElELRLKDGDG---RWVWVEASAVPLRDGGEVIGV 241
|
250
....*....|....*..
gi 1839367027 259 HGFARLITGRRRMEDEL 275
Cdd:COG2202 242 LGIVRDITERKRAEEAL 258
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
268-681 |
2.90e-16 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 82.60 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 268 RRRMeDELVR-LAYEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLRE 346
Cdd:PRK11059 217 RSRF-DTFIRsNAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLST 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 347 VVgDR---GLVGRLGGDEFLIIVQGESVEgPAARLASALCAAMDS-----PVSVDDRLlrvtaSIGMSLFpKDGETAEDL 418
Cdd:PRK11059 296 FV-MRypgALLARYSRSDFAVLLPHRSLK-EADSLASQLLKAVDAlpppkMLDRDDFL-----HIGICAY-RSGQSTEQV 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 419 LRHADAALYRAKEEGPSNWASY----TPELTAAAMA-RRYLETELRgavdRDEIQVALQPVVDlSSGEVVAYEALARWHH 493
Cdd:PRK11059 368 MEEAEMALRSAQLQGGNGWFVYdkaqLPEKGRGSVRwRTLLEQTLV----RGGPRLYQQPAVT-RDGKVHHRELFCRIRD 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 494 REDGWIDPEQFIALAESRGLVAALGEQVYRKAMrAVARIDATSRLSINVAPVQLKDPQFARRLvrmaRDCGLQ-----PA 568
Cdd:PRK11059 443 GQGELLSAELFMPMVQQLGLSEQYDRQVIERVL-PLLRYWPEENLSINLSVDSLLSRAFQRWL----RDTLLQcprsqRK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 569 RLEVEITErafmDELADKLEQLES----LRRQGIAIAIDDFGTGYSSLAYLRHLPVQRLKIDQVFVRGLASNPKNSAIMK 644
Cdd:PRK11059 518 RLIFELAE----ADVCQHISRLRPvlrmLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVR 593
|
410 420 430
....*....|....*....|....*....|....*..
gi 1839367027 645 AIVTLARELGFSVTAEGVQSAEELEEVRAHGCDCAQG 681
Cdd:PRK11059 594 SLVGACAGTETQVFATGVESREEWQTLQELGVSGGQG 630
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
256-433 |
3.05e-15 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 77.95 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 256 VTWHGFARLITGRRRMEdelvRLAYEDALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDR 335
Cdd:PRK10245 186 VSYQTATKLAEHKRRLQ----VMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 336 LLEELAGRLREVVGDRGLVGRLGGDEFLIIVQGESVEgpaarlaSALcAAMDspvSVDDRL----------LRVTASIGM 405
Cdd:PRK10245 262 AIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAE-------SAI-TAMS---RVHEGLntlrlpnapqVTLRISVGV 330
|
170 180
....*....|....*....|....*....
gi 1839367027 406 S-LFPKDGETAEdLLRHADAALYRAKEEG 433
Cdd:PRK10245 331 ApLNPQMSHYRE-WLKSADLALYKAKNAG 358
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
22-275 |
2.10e-14 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 76.17 E-value: 2.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 22 NLLDAVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHrEEVRGAIRRVFECGEAS--LEAPLL 99
Cdd:COG5809 15 QRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDD-EKELREILKLLKEGESRdeLEFELR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 100 TRSG--------QTPVFRYSGQLVdvdgepLIAGIGVDISEQKAAERASARQTEQFRHVAGQVPGVIYQLRYEpGTGIFS 171
Cdd:COG5809 94 HKNGkrlefsskLSPIFDQNGDIE------GMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLD-GRIIYA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 172 MPYASaklfEVFGVEHSEVVEnaQALFDRIAPEDEARVQRAAEQSRQSLCRFHEQFRMLPPGGQLehaEWVEVDSSP--- 248
Cdd:COG5809 167 NPAAC----KLLGISIEELIG--KSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRW---RLLEASGAPikk 237
|
250 260
....*....|....*....|....*..
gi 1839367027 249 ERDQDGAVTwhgFARLITGRRRMEDEL 275
Cdd:COG5809 238 NGEVDGIVI---IFRDITERKKLEELL 261
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
282-430 |
7.26e-13 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 71.53 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 282 DALTGMPNRTSLQLRLEEQIAEASIVGQELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVV--GDRGLvgRLGG 359
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIrkSDYGI--RLGG 421
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1839367027 360 DEFLIIVQGESVEgpaarLASALCAAMDSPVSVDDRLLRVTASIG---MslfpKDGETAEDLLRHADAALYRAK 430
Cdd:NF040885 422 DEFCIILIDYEEA-----EAQNLIERIRQHLRTIDPDKRVSFSWGayqM----QPGDTLDDAYKAADERLYLNK 486
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
26-139 |
1.72e-12 |
|
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: 64.62 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 26 AVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGAIRRVF--ECGEASLEAPLLTRSG 103
Cdd:TIGR00229 7 AIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLegEPEPVSEERRVRRKDG 86
|
90 100 110
....*....|....*....|....*....|....*..
gi 1839367027 104 QTPVFRYSGQLVDVDGEPL-IAGIGVDISEQKAAERA 139
Cdd:TIGR00229 87 SEIWVEVSVSPIRTNGGELgVVGIVRDITERKEAEEA 123
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
22-148 |
4.93e-11 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 64.87 E-value: 4.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 22 NLLDAVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFApeHREEVRGAIRRVFECGEASL--EAPLL 99
Cdd:COG3852 7 ELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFP--EDSPLRELLERALAEGQPVTerEVTLR 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1839367027 100 TRSGQTPVFRYSGQ-LVDVDGEPLIAGIGVDISEQKAAERAsARQTEQFR 148
Cdd:COG3852 85 RKDGEERPVDVSVSpLRDAEGEGGVLLVLRDITERKRLERE-LRRAEKLA 133
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
22-153 |
5.34e-10 |
|
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: 62.44 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 22 NLLDAVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGAIRRVFECG-EASLEAPLLT 100
Cdd:COG5805 157 ERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWqEFIIEREIIT 236
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1839367027 101 RSGQTPVFRYSGQ-LVDVDG-EPLIAGIGVDISEQKAAERAsARQTEQFRhVAGQ 153
Cdd:COG5805 237 KDGRIRYFEAVIVpLIDTDGsVKGILVILRDITEKKEAEEL-MARSEKLS-IAGQ 289
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
22-275 |
5.86e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 62.77 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 22 NLLDAVLQTVPGIFYLIDSKQRFRR-WNASFEQVTGYSASEIAAmSPLDLFAPEHREEVR-GAIRRVFECGE--ASLEAP 97
Cdd:PRK13560 332 DMLRAIIEAAPIAAIGLDADGNICFvNNNAAERMLGWSAAEVMG-KPLPGMDPELNEEFWcGDFQEWYPDGRpmAFDACP 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 98 LLTRSGQTPVFR------------------YSGQLVDVDGEpLIAGIG--VDISEQKAAERasarQTEQFRHVAGQVPGV 157
Cdd:PRK13560 411 MAKTIKGGKIFDgqevliereddgpadcsaYAEPLHDADGN-IIGAIAllVDITERKQVEE----QLLLANLIVENSPLV 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 158 IYQLRYEPGTGIFSMpyasAKLFEVFGVEHSEVVENAQALFDRIAPEDEARVQR-AAEQSRQSLCRFHEQFRMLPPGGQL 236
Cdd:PRK13560 486 LFRWKAEEGWPVELV----SKNITQFGYEPDEFISGKRMFAAIIHPADLEQVAAeVAEFAAQGVDRFEQEYRILGKGGAV 561
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1839367027 237 ehaEWVEVDSSPERDQDGAVT-WHGFARLITGRRRMEDEL 275
Cdd:PRK13560 562 ---CWIDDQSAAERDEEGQIShFEGIVIDISERKHAEEKI 598
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
338-430 |
7.47e-09 |
|
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: 55.69 E-value: 7.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 338 EELAGRLrevvgdrGLVGRLGGDEFLIIVQGESVEGpAARLASALCAAMDSPVSVddrllRVTASIGMSlfpkdgetAED 417
Cdd:COG3706 109 EELLARV-------DLVARYGGEEFAILLPGTDLEG-ALAVAERIREAVAELPSL-----RVTVSIGVA--------GDS 167
|
90
....*....|...
gi 1839367027 418 LLRHADaALYRAK 430
Cdd:COG3706 168 LLKRAD-ALYQAR 179
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
23-88 |
1.46e-08 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 51.63 E-value: 1.46e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1839367027 23 LLDAVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGAIRRVFE 88
Cdd:smart00091 2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
174-262 |
1.61e-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.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 52.34 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 174 YASAKLFEVFGVEHSEVVENAQALFDRIAPEDEARVQRAAEQSRQSLCRFHEQFRMLPPGGQLehaEWVEVDSSPERDQD 253
Cdd:pfam08447 3 YWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEY---RWVEARARPIRDEN 79
|
90
....*....|
gi 1839367027 254 GAVT-WHGFA 262
Cdd:pfam08447 80 GKPVrVIGVA 89
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
122-275 |
3.53e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 53.52 E-value: 3.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 122 LIAGIGVDISEQKAAERASARQTEQfRHVAGQVPGVIYQLRYEPgTGIFSMPYASAKLFEVFGVEHSEVVENAQALFDRI 201
Cdd:PRK13560 46 LLRGHAYDARAIAEAEAQDCREQCE-RNLKANIPGGMFLFALDG-DGTFSFPSLLDANGELAAIAKHDLMADKGLLAMLI 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1839367027 202 APEDEARVQRAAEQSRQSLCRFHEQFRMLPPGGQLEHAE--WVEVDSSPERDQDGAVTWHGFARLITGRRRMEDEL 275
Cdd:PRK13560 124 GGDDGDFFFANPFRSAETIAMALQSDDWQEEEGHFRCGDgrFIDCCLRFERHAHADDQVDGFAEDITERKRAEERI 199
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
32-130 |
3.80e-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: 48.78 E-value: 3.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 32 PGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGAIRRVFECGEA-SLEAPLLTRSGQT-PVFR 109
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPvTLEVRLRRKDGSViWVLV 81
|
90 100
....*....|....*....|..
gi 1839367027 110 YSGQLVDVDGEP-LIAGIGVDI 130
Cdd:cd00130 82 SLTPIRDEGGEViGLLGVVRDI 103
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
31-135 |
3.90e-07 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 48.95 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 31 VPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGAIRRVFECGEASLEAPLLTRSGQT-PVFR 109
Cdd:pfam08448 4 LPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEErHYEL 83
|
90 100
....*....|....*....|....*..
gi 1839367027 110 YSGQLVDVDGEPL-IAGIGVDISEQKA 135
Cdd:pfam08448 84 RLTPLRDPDGEVIgVLVISRDITERRR 110
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
310-430 |
4.39e-07 |
|
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: 49.66 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 310 ELALLHLDLDNFKDINDIWGHGSGDRLLEELAGRLREVVGDRG-LVGRLGGDEFLIIVQGESVeGPAARLASALCAAMDS 388
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEFMVVSGLDHP-AAAVAFAEDMREAVSA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1839367027 389 pvSVDDRLLRVTASIGMSLFP---------KDGETAEDLLRHADAALYRAK 430
Cdd:cd07556 80 --LNQSEGNPVRVRIGIHTGPvvvgvigsrPQYDVWGALVNLASRMESQAK 128
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
22-93 |
2.39e-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. 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: 43.95 E-value: 2.39e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1839367027 22 NLLDAVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGAIRRVFECGEAS 93
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEES 72
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
46-132 |
5.41e-05 |
|
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: 42.45 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 46 RWNASFEQVTGYSASEIAAMSPLDLFAPEHREEvrgAIRRVFECGEASLEAPLL--TRSGQTPVFRYSGQLVDVDGEPLI 123
Cdd:pfam13426 6 YVNDAALRLLGYTREELLGKSITDLFAEPEDSE---RLREALREGKAVREFEVVlyRKDGEPFPVLVSLAPIRDDGGELV 82
|
90
....*....|.
gi 1839367027 124 AGIGV--DISE 132
Cdd:pfam13426 83 GIIAIlrDITE 93
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
22-151 |
1.27e-03 |
|
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: 41.68 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 22 NLLDAVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEhreevrgAIRRVFECGEASLEAPLLTR 101
Cdd:COG3829 11 EELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNS-------PLLEVLKTGKPVTGVIQKTG 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1839367027 102 SGQTPVFrYSGQLVDVDGEpLIAGIGV--DISEQKAAERASARQTEQFRHVA 151
Cdd:COG3829 84 GKGKTVI-VTAIPIFEDGE-VIGAVETfrDITELKRLERKLREEELERGLSA 133
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
47-126 |
2.01e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 37.70 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 47 WNASFEQVTGYSASEIAAM--SPLDLFAPEHREEVRGAIRRVFECGEA-SLEAPLLTRSGQTPVFRYSGQLV-DVDGEPL 122
Cdd:pfam08447 4 WSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEPySGEYRIRRKDGEYRWVEARARPIrDENGKPV 83
|
....*
gi 1839367027 123 -IAGI 126
Cdd:pfam08447 84 rVIGV 88
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
22-141 |
7.88e-03 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 39.17 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1839367027 22 NLLDAVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGAIRRVFECGEASLEAP-LLT 100
Cdd:COG5000 90 RYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREALERGWQEEIELTRDgRRT 169
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1839367027 101 RSGQTPVFRYSGQLVDVDgepliagigvDISEQKAAERASA 141
Cdd:COG5000 170 LLVRASPLRDDGYVIVFD----------DITELLRAERLAA 200
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
22-82 |
8.42e-03 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 35.22 E-value: 8.42e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1839367027 22 NLLDAVLQTVPGIFYLIDSKQRFRRWNASFEQVTGYSASEIAAMSPLDLFAPEHREEVRGA 82
Cdd:pfam13188 1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLEDALELL 61
|
|
| |
