|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
228-907 |
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: 645.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 228 RMHDVMASLYGEQPAGVSLAVYDGVAASDAALLYRTPAANGWHAPALMSANEYLVVDGRDWMLSMDASDEFRSRLGSNAE 307
Cdd:COG5001 2 LALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 308 PLIAGAGIGLSLLLALLTWLMVTGRERAIRLASGMTRELRESEEKFRAIADCTVNLEIWWGPDGKPRWINPSVDHYTGYT 387
Cdd:COG5001 82 LAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 388 VAECMAMPNFARTLIHPDDVERVAPEFQKGLQGFRGDDLEFRCVRKDGSLLWLSLsWVPISNARGDFVGFRTSGRDITER 467
Cdd:COG5001 162 LALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGL-LLLGLLLLLLLVAVLAIARLITER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 468 KKSEEKIRELAFYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSV 547
Cdd:COG5001 241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 548 SKGDTVARVGGDEFVVVLGNLSlnkaaATAETEAAGEKILAVLGRAYELNGVQFRSTASIGVTVFNGEQTSTDELFKQAD 627
Cdd:COG5001 321 REGDTVARLGGDEFAVLLPDLD-----DPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 628 LAMYKSKERGRNAMCFFDPAMQTTVLKRAELEVGLRSAIEENRFVLHYQAQV-VDGDHITGAEALVRWEHPVCGLIPPAE 706
Cdd:COG5001 396 LAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVdLATGRIVGAEALLRWQHPERGLVSPAE 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 707 FIPLAEETGLILEIGRMVLESACAQLALWATEpQMAHLSIAVNVSARQFREPDFVESVLGVINRKGARADRLKLELTESV 786
Cdd:COG5001 476 FIPLAEETGLIVPLGEWVLREACRQLAAWQDA-GLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 787 LVENVEDIIEKMGALRARGVTFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALARSFDLGVI 866
Cdd:COG5001 555 LLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVV 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 740671249 867 AEGVETEAQRDFLAVAGCHAYQGFLFCKPLPVRSFEQFVAS 907
Cdd:COG5001 635 AEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
460-907 |
1.86e-115 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 368.24 E-value: 1.86e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 460 SGRDITERKKSEEKIRELAFYDTLTRLPNRALLLDRLRESMAASRENNVcgALMFIDLDHFKTLNDTLGHDKGDLLLRHV 539
Cdd:PRK10060 219 SGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQV--GIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 540 AYRLSSSVSKGDTVARVGGDEFVVVLGNLSLnkaaatAETEAAGEKILAVLGRAYELNGVQFRSTASIGVTVFNGEQTST 619
Cdd:PRK10060 297 SLAILSCLEEDQTLARLGGDEFLVLASHTSQ------AALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDS 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 620 DELFKQADLAMYKSKERGRNAMCFFDPAMQTTVLKRAELEVGLRSAIEENRFVLHYQAQVVDGDHITGAEALVRWEHPVC 699
Cdd:PRK10060 371 ESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRGEVRSLEALVRWQSPER 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 700 GLIPPAEFIPLAEETGLILEIGRMVLESACAQLALWatEPQMAHLSIAVNVSARQFREPDFVESVLGVINRKGARADRLK 779
Cdd:PRK10060 451 GLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKW--RDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPID 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 780 LELTESVLVENVEDIIEKMGALRARGVTFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALAR 859
Cdd:PRK10060 529 VELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQ 608
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 740671249 860 SFDLGVIAEGVETEAQRDFLAVAGCHAYQGFLFCKPLPVRSFEQFVAS 907
Cdd:PRK10060 609 ALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
328-906 |
3.46e-115 |
|
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: 364.88 E-value: 3.46e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 328 MVTGRERAIRLASGMTRELRESEEKFRAIADCTVNLEIWWGPDGKPRWINPSVDHYTGYTVAECMAMPNFARTLIHPDDV 407
Cdd:COG2200 5 LALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 408 ERVAPEFQKGLQGFRGDDLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITERKKSEEKIRELAFYDTLTRLP 487
Cdd:COG2200 85 LLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 488 NRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVGGDEFVVVLGN 567
Cdd:COG2200 165 RRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 568 LslnkaAATAETEAAGEKILAVLGRAYELNGVQFRSTASIGVTVFNGEQTSTDELFKQADLAMYKSKERGRNAMCFFDPA 647
Cdd:COG2200 245 L-----AAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 648 MQTtVLKRAELEVGLRSAIEENRFVLHYQAQV-VDGDHITGAEALVRWEHPVCGLIPPAEFIPLAEETGLILEIGRMVLE 726
Cdd:COG2200 320 EAR-ARRRLALESELREALEEGELRLYYQPIVdLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 727 SACAQLALWATepQMAHLSIAVNVSARQFREPDFVESVLGVINRKGARADRLKLELTESVLVENVEDIIEKMGALRARGV 806
Cdd:COG2200 399 RALRQLARWPE--RGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGV 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 807 TFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALARSFDLGVIAEGVETEAQRDFLAVAGCHA 886
Cdd:COG2200 477 RIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDY 556
|
570 580
....*....|....*....|
gi 740671249 887 YQGFLFCKPLPVRSFEQFVA 906
Cdd:COG2200 557 AQGYLFGRPLPLEELEALLR 576
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
662-898 |
9.42e-110 |
|
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: 337.98 E-value: 9.42e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 662 LRSAIEENRFVLHYQAQV-VDGDHITGAEALVRWEHPVCGLIPPAEFIPLAEETGLILEIGRMVLESACAQLALWATepQ 740
Cdd:cd01948 3 LRRALERGEFELYYQPIVdLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA--G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 741 MAHLSIAVNVSARQFREPDFVESVLGVINRKGARADRLKLELTESVLVENVEDIIEKMGALRARGVTFSLDDFGIGYSSL 820
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 740671249 821 SYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALARSFDLGVIAEGVETEAQRDFLAVAGCHAYQGFLFCKPLPV 898
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| CHASE1 |
COG3614 |
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms]; |
3-564 |
2.04e-103 |
|
Extracytoplasmic sensor domain CHASE1 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442832 [Multi-domain] Cd Length: 588 Bit Score: 333.96 E-value: 2.04e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 3 RVRSVLLPLFVLTASLCVTWTVWNHERQATSKELRTQFDYTLGDAVSRIEQRMASYELMLRGVQSLFAANGTIDRDRFRR 82
Cdd:COG3614 7 LLRRRLLPLLVLLLGLLLTALAWWAVRRAEEQRARARFERLADELASALEERLDAYEQVLRGLAGLFAASDDVTRAEFRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 83 YVGALNLDANFSGIHAVGVVEWVPAAQKAGHVARMREEGVPGYTILPEGQREDYAPLVQREPYVGITQSSPGFDTWSDPV 162
Cdd:COG3614 87 YVASLDLLRRYPGIQGLGWAPRVPAAERAAFEAAARAEGFPDFRIRPAGERDEYFPITYIEPLDARNRRALGFDMASEPV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 163 RRAAMERARDSGMAALSGTVHLLIDADSdlRPGFIMYLPIYASGETQESVLQRRAHITGWVYASFRMHDVMASLYGE-QP 241
Cdd:COG3614 167 RRAAMERARDTGRPAASGPVTLVQETDG--QPGFLLYLPVYRGGAPPDTVAERRAALRGFVYAPFRMDDLLAGVLGRlAD 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 242 AGVSLAVYDGVAASDAALLYRTPAANGWHAPALMSANEYLVVDGRDWMLSMDASDEFRSRLGSNAEPLIAGAGIGLSLLL 321
Cdd:COG3614 245 RDLDLRLYDGTDPGPPQLLYDSSPAAPAAAAPALSATRTLEVAGRTWTLEFRPTPAFEAALRSWLPWLVLLGGLLLSLLL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 322 ALLTWLMVTGRERAIRLASGMTRELRESEEKFRAIADCTVNLEIWWGPDGKpRWINPSVDHYTGYTVAECMAMPNFARTL 401
Cdd:COG3614 325 ALLLLSLARRRRRAEALAAARAALRALRAAELRLRALLRRALLALLRNALA-LALLLAALLLLLARLLLLLAALLLLLAR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 402 IHPDDVERVAPEFQKGLQGFRGDDLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITERKKSEEKIRELAFYD 481
Cdd:COG3614 404 ALSAADLLLLQADLLLLRLLLLLRRRLLLVRDLRLGRGLGLGVVLLLDAILLDLLALAELELAAARAEVALAEALLALLV 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 482 TLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVGGDEF 561
Cdd:COG3614 484 VLLLALLLALLRLLLALAELAATAAREAAGAALLLDREAALLDAALEALLDLLGLLVLLLLAELLLRLGALLLGRALLGG 563
|
...
gi 740671249 562 VVV 564
Cdd:COG3614 564 VGA 566
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
662-899 |
5.54e-97 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 304.52 E-value: 5.54e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 662 LRSAIEENRFVLHYQAQV-VDGDHITGAEALVRWEHPVCGLIPPAEFIPLAEETGLILEIGRMVLESACAQLALWatepQ 740
Cdd:smart00052 4 LRQALENGQFLLYYQPIVsLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEW----Q 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 741 MAH---LSIAVNVSARQFREPDFVESVLGVINRKGARADRLKLELTESVLVENVEDIIEKMGALRARGVTFSLDDFGIGY 817
Cdd:smart00052 80 AQGpppLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 818 SSLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALARSFDLGVIAEGVETEAQRDFLAVAGCHAYQGFLFCKPLP 897
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
..
gi 740671249 898 VR 899
Cdd:smart00052 240 LD 241
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
466-897 |
2.06e-90 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 305.16 E-value: 2.06e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 466 ERKKSEEKIRELAFYDTLTRLPNRALLLDRLRESMAASRENnvcgALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSS 545
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 546 SVSKGDTVARVGGDEFVVVLGNLSLNKAAATAeteaagEKILAVLGRAYELNGVQFRSTASIGVTVFNGEqtSTDELFKQ 625
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVLVSLENDVSNITQIA------DELRNVVSKPIMIDDKPFPLTLSIGISYDVGK--NRDYLLST 511
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 626 ADLAMYKSKERGRNAMCFFDPAMQTTVLKRAELEVGLRSAIEENRFVLHYQAQV-VDGDHITGAEALVRWEHPVCGLIPP 704
Cdd:PRK11359 512 AHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIfAETGELYGIEALARWHDPLHGHVPP 591
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 705 AEFIPLAEETGLILEIGRMVLESACAQLALWatEPQMAHLS-IAVNVSARQFREPDFVESVLGVINRKGARADRLKLELT 783
Cdd:PRK11359 592 SRFIPLAEEIGEIENIGRWVIAEACRQLAEW--RSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEIT 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 784 ESVLVENVEDIIEKMGALRARGVTFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALARSFDL 863
Cdd:PRK11359 670 ESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNL 749
|
410 420 430
....*....|....*....|....*....|....
gi 740671249 864 GVIAEGVETEAQRDFLAVAGCHAYQGFLFCKPLP 897
Cdd:PRK11359 750 TVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLP 783
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
472-903 |
4.97e-88 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 294.70 E-value: 4.97e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 472 EKIRELAFYDTLTRLPNRALLLDRLrESMAASRENNvcgALMFIDLDhfkTLNDTLG---HDKGDLLLRHVAYRLSSSVS 548
Cdd:PRK13561 225 EEQSRNATRFPVSDLPNKALLMALL-EQVVARKQTT---ALMIITCE---TLRDTAGvlkEAQREILLLTLVEKLKSVLS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 549 KGDTVARVGGDEFVVVLgnlslNKAAATAETEAAGEKILAVLGRAYELNGVQFRSTASIGVTVFNGEQTStDELFKQADL 628
Cdd:PRK13561 298 PRMVLAQISGYDFAIIA-----NGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLTA-EQLYSRAIS 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 629 AMYKSKERGRNAMCFFDPAMQTTVLKRAELEVGLRSAIEENRFVLHYQAQV-VDGDHITGAEALVRWEHPVCGLIPPAEF 707
Cdd:PRK13561 372 AAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVeMRSGKLVSAEALLRMQQPDGSWDLPEGL 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 708 IPLAEETGLILEIGRMVLESACAQLALWatEPQMAHLSIAVNVSARQFREPDFVESVLGVINRKGARADRLKLELTESVL 787
Cdd:PRK13561 452 IDRIESCGLMVTVGHWVLEESCRLLAAW--QERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 788 VENVEDIIEKMGALRARGVTFSLDDFGIGYSSLSYL---KRLPLDQLKIDRSFVrDILedPNDADIARTIVALARSFDLG 864
Cdd:PRK13561 530 IDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLqhmKSLPIDVLKIDKMFV-DGL--PEDDSMVAAIIMLAQSLNLQ 606
|
410 420 430
....*....|....*....|....*....|....*....
gi 740671249 865 VIAEGVETEAQRDFLAVAGCHAYQGFLFCKPLPVRSFEQ 903
Cdd:PRK13561 607 VIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEE 645
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
662-895 |
3.84e-77 |
|
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: 251.47 E-value: 3.84e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 662 LRSAIEENRFVLHYQAQV-VDGDHITGAEALVRWEHPVCGLIPPAEFIPLAEETGLILEIGRMVLESACAQLALWATEPQ 740
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVdLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 741 MahlSIAVNVSARQFREPDFVESVLGVINRKGARADRLKLELTESVLVENVEDIIEKMGALRARGVTFSLDDFGIGYSSL 820
Cdd:pfam00563 84 I---KLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740671249 821 SYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALARSFDLGVIAEGVETEAQRDFLAVAGCHAYQGFLFCKP 895
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
662-906 |
2.13e-74 |
|
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: 254.07 E-value: 2.13e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 662 LRSAIEENRFVLHYQAqVVDGDH--ITGAEALVRWEHPVCGLIPPAEFIPLAEETGLILEIGRMVLESACAQL-ALWATE 738
Cdd:COG4943 276 LRRAIKRREFYVHYQP-IVDLKTgrCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLgDLLAAD 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 739 PQMaHLSIavNVSARQFREPDFVESVLGVINRKGARADRLKLELTESVLVeNVEDIIEKMGALRARGVTFSLDDFGIGYS 818
Cdd:COG4943 355 PDF-HISI--NLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDFGTGYS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 819 SLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALARSFDLGVIAEGVETEAQRDFLAVAGCHAYQGFLFCKPLPV 898
Cdd:COG4943 431 SLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPA 510
|
....*...
gi 740671249 899 RSFEQFVA 906
Cdd:COG4943 511 EEFIAWLA 518
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
458-902 |
1.51e-73 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 255.25 E-value: 1.51e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 458 RTSGRDITERKKSEEKIRELAFYDTLTRLPNRALLLDRLRESMAAS-RENNVCgaLMFIDLDHFKTLNDTLGHDKGDLLL 536
Cdd:PRK11829 212 RNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASStRTDHFH--LLVIGIETLQEVSGAMSEAQHQQLL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 537 RHVAYRLSSSVSKGDTVARVGGDEFVVVLGNLSlnkaaATAETEAAGEKILAVLGRAYELNGVQFRSTASIGVTVFNGEQ 616
Cdd:PRK11829 290 LTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTR-----RSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQ 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 617 TSTDELFKQADLAMYKSKERGRNAMCFFDPAMQTTVLKRAELEVGLRSAIEENRFVLHYQAQV-VDGDHITGAEALVRWE 695
Cdd:PRK11829 365 DTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWdMKRQQVIGAEALLRWC 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 696 HPVCGLIPPAEFIPLAEETGLILEIGRMVLESACAQLALWATEPQMAHLSiaVNVSARQFREPDFVESVLGVINRKGARA 775
Cdd:PRK11829 445 QPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPLS--VNISGLQVQNKQFLPHLKTLISHYHIDP 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 776 DRLKLELTESVLVENVEDIIEKMGALRARGVTFSLDDFGIGYSSLSYL---KRLPLDQLKIDRSFVRDIledPNDADIAR 852
Cdd:PRK11829 523 QQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL---PEDDAIAR 599
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 740671249 853 TIVALARSFDLGVIAEGVETEAQRDFLAVAGCHAYQGFLFCKPLPVRSFE 902
Cdd:PRK11829 600 IISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEFE 649
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
333-897 |
1.22e-63 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 233.80 E-value: 1.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 333 ERAIRLASGMT--RELRES--EEKFR------AIADCTVNLEIwwgpDGKPRWINPSVDHYTGYTVAECMAMPnfARTLI 402
Cdd:PRK09776 512 ERLLGINMDMTevRQLNEAlfQEKERlhitldSIGEAVVCTDM----AMKVTFMNPVAEKMTGWTQEEALGVP--LLTVL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 403 HPDDvERVAPEF---QKGLQGFRGDDLEFRCV--RKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITERKKSEEKIREL 477
Cdd:PRK09776 586 HITF-GDNGPLMeniYSCLTSRSAAYLEQDVVlhCRSGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYS 664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 478 AFYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVG 557
Cdd:PRK09776 665 ASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLG 744
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 558 GDEFVVVLGNLSLNKaaataeTEAAGEKIL-AVLGRAYELNGVQFRSTASIGVTVFNGEQTSTDELFKQADLAMYKSKER 636
Cdd:PRK09776 745 GDEFGLLLPDCNVES------ARFIATRIIsAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNA 818
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 637 GRNAMCFFDPAMQTTVLKRAELEV--GLRSAIEENRFVLHYQ-AQVVDGDHITGAEALVRWEHPVCGLIPPAEFIPLAEE 713
Cdd:PRK09776 819 GRGRVTVYEPQQAAAHSEHRALSLaeQWRMIKENQLMMLAHGvASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAED 898
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 714 TGLILEIGRMVLESACAQLAlwatePQMAH--LSIAVNVSARQFREPDFVESVLGVINRKGARADRLKLELTESVLVENV 791
Cdd:PRK09776 899 PALMHALDRRVIHEFFRQAA-----KAVASkgLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHA 973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 792 EDIIEKMGALRARGVTFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALARSFDLGVIAEGVE 871
Cdd:PRK09776 974 ESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVE 1053
|
570 580
....*....|....*....|....*.
gi 740671249 872 TEAQRDFLAVAGCHAYQGFLFCKPLP 897
Cdd:PRK09776 1054 LPLVLDTLSGIGVDLAYGYAIARPQP 1079
|
|
| CHASE |
pfam03924 |
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - ... |
73-261 |
6.83e-62 |
|
CHASE domain; This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases. This is a ligand-binding domain that binds cytokinin (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 427591 Cd Length: 184 Bit Score: 207.53 E-value: 6.83e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 73 GTIDRDRFRRYVGALNLDANfsGIHAVGVVEWVPAAQKAGHVARMREEGVPGYTILPEGQREDYAPLVQREPYVGiTQSS 152
Cdd:pfam03924 1 DSVDREEFRRYAASLLLRRP--GIQGLGWAPRVPAAERAAFEAAVRAEGFPDFTIRPAGDRDEYFPIIYIEPLAG-NNRA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 153 PGFDTWSDPVRRAAMERARDSGMAALSGTVHLLIDADSdlRPGFIMYLPIYASGeTQESVLQRRAHITGWVYASFRMHDV 232
Cdd:pfam03924 78 LGFDMASEPVRREAIERARDTGEPVLSGPVTLVQDGDG--QPGFLLYLPVYRGG-PPDTVAERRAALLGFVYAPFRIDDL 154
|
170 180 190
....*....|....*....|....*....|
gi 740671249 233 M-ASLYGEQPAGVSLAVYDGVAASDAALLY 261
Cdd:pfam03924 155 LeAALLRLGEDGLDLALYDGTSASAPELLY 184
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
437-644 |
6.75e-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: 197.51 E-value: 6.75e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 437 LLWLSLSWVPISNARGDFVGFRTSGRDITERKKSEEKIRELAFYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFID 516
Cdd:COG2199 73 ALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLID 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 517 LDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVGGDEFVVVLGNLSLNkaaataETEAAGEKILAVLGRA-YE 595
Cdd:COG2199 153 LDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLE------EAEALAERLREALEQLpFE 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740671249 596 LNGVQFRSTASIGVTVFNGEQTSTDELFKQADLAMYKSKERGRNAMCFF 644
Cdd:COG2199 227 LEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
479-639 |
3.80e-52 |
|
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: 179.67 E-value: 3.80e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 479 FYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVGG 558
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 559 DEFVVVLGNLSLnkaaatAETEAAGEKILAVLGRAYELNGVQFRSTASIGVTVFNGEQTSTDELFKQADLAMYKSKERGR 638
Cdd:cd01949 81 DEFAILLPGTDL------EEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGR 154
|
.
gi 740671249 639 N 639
Cdd:cd01949 155 N 155
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
478-639 |
1.39e-51 |
|
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: 177.83 E-value: 1.39e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 478 AFYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVG 557
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 558 GDEFVVVLGNLSLNKAAATAETEaagEKILAVLGRAYELNGVQFRSTASIGVTVFNGEQTSTDELFKQADLAMYKSKERG 637
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERI---RRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAG 157
|
..
gi 740671249 638 RN 639
Cdd:pfam00990 158 RN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
476-644 |
2.07e-48 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 168.97 E-value: 2.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 476 ELAFYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVAR 555
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 556 VGGDEFVVVLGNLSLNKaaataeTEAAGEKILAVLGRAYELNGVQFRSTASIGVTVFNGEQTSTDELFKQADLAMYKSKE 635
Cdd:smart00267 81 LGGDEFALLLPETSLEE------AIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKK 154
|
....*....
gi 740671249 636 RGRNAMCFF 644
Cdd:smart00267 155 AGRNQVAVY 163
|
|
| CHASE |
smart01079 |
This domain is found in the extracellular portion of receptor-like proteins - such as serine ... |
72-250 |
2.54e-47 |
|
This domain is found in the extracellular portion of receptor-like proteins - such as serine/threonine kinases and adenylyl cyclases; Predicted to be a ligand binding domain.
Pssm-ID: 215015 Cd Length: 176 Bit Score: 166.74 E-value: 2.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 72 NGTIDRDRFRRYVGALNLDANFSGIHAVGVVEWVPAAQKAGHVARMREEGVPGYTI--LPEGQREDYAPLVQREPYVGiT 149
Cdd:smart01079 1 SESVSRAEFRRFALELQLNRRLPGIQGLGWAPRVPPAERAAFEAALRAGGPGLFNIrlAPDGERDEYFVITYIEPLAG-N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 150 QSSPGFDTWSDPVRRAAMERARDSGMAALSGTVHLLidADSDLRPGFIMYLPIYASGETQESvlqRRAHITGWVYASFRM 229
Cdd:smart01079 80 EAALGLDLLSEPVRRAALERARDSGRPVLSGPVTLV--QGTGDGRGFLLRLPVYRGGPPTST---RREALWGFVSAVFRL 154
|
170 180
....*....|....*....|..
gi 740671249 230 HDVMASLYGE-QPAGVSLAVYD 250
Cdd:smart01079 155 DDLLEGLLGAlDLPGLDLALYD 176
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
477-640 |
1.14e-38 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 141.32 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 477 LAFYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARV 556
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 557 GGDEFVVVLGNLSLNKAAATAETEAAGEKILAVLGRAYELNGVqfrsTASIGVTVFNGEQTSTDELFKQADLAMYKSKER 636
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTV----TVSIGVACYPGHGLTLEELLKRADEALYQAKKA 156
|
....
gi 740671249 637 GRNA 640
Cdd:TIGR00254 157 GRNR 160
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
651-918 |
5.64e-38 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 149.76 E-value: 5.64e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 651 TVLKRAELEVgLRsAIEENRFVLHYQAqVVDG--DHITGAEALVRWEHPVCGLIPPAEFIPLAEETGLILEIGRMVLEsa 728
Cdd:PRK10551 259 SLRMRPGKEI-LT-GIKRGQFYVEYQP-VVDTqtLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFE-- 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 729 caqlaLWATE-PQMAHL-----SIAVNVSARQFREPDFVESVLGVINRKGARADRLKLELTESVLVENvEDIIEKMGALR 802
Cdd:PRK10551 334 -----LIARDaAELQKVlpvgaKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQE-EEATKLFAWLH 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 803 ARGVTFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVALARSFDLGVIAEGVETEAQRDFLAVA 882
Cdd:PRK10551 408 SQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRER 487
|
250 260 270
....*....|....*....|....*....|....*.
gi 740671249 883 GCHAYQGFLFCKPLPVrsfEQFVASfeCRDRMADRR 918
Cdd:PRK10551 488 GVNFLQGYWISRPLPL---EDFVRW--LKEPYTPQW 518
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
467-642 |
3.35e-27 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 116.15 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 467 RKKSEEKIR-------ELAFYDTLTRLPNR-------ALLLDRlresmAASRENNVcgALMFIDLDHFKTLNDTLGHDKG 532
Cdd:PRK09581 274 RKRYQDALRnnleqsiEMAVTDGLTGLHNRryfdmhlKNLIER-----ANERGKPL--SLMMIDIDHFKKVNDTYGHDAG 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 533 DLLLRHVAYRLSSSVSKGDTVARVGGDEFVVVLGNLSLNKaaataeTEAAGEKI-LAVLGRAYELNG--VQFRSTASIGV 609
Cdd:PRK09581 347 DEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIED------AIAVAERIrRKIAEEPFIISDgkERLNVTVSIGV 420
|
170 180 190
....*....|....*....|....*....|...
gi 740671249 610 TVFNGEQTSTDELFKQADLAMYKSKERGRNAMC 642
Cdd:PRK09581 421 AELRPSGDTIEALIKRADKALYEAKNTGRNRVV 453
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
472-647 |
4.98e-26 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 113.96 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 472 EKIRELAFYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGD 551
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 552 TVARVGGDEFVVVLGNLSLnkaaatAETEAAGEKI-LAVLGRAYEL-NGVQFRSTASIGV--TVFNGEQTsTDELFKQAD 627
Cdd:PRK15426 472 VAGRVGGEEFCVVLPGASL------AEAAQVAERIrLRINEKEILVaKSTTIRISASLGVssAEEDGDYD-FEQLQSLAD 544
|
170 180
....*....|....*....|
gi 740671249 628 LAMYKSKERGRNAMCFFDPA 647
Cdd:PRK15426 545 RRLYLAKQAGRNRVCASDNA 564
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
344-565 |
1.23e-24 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 104.34 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 344 RELRESEEKFRAIADCTVNLEIWWGPDGKPRWINPSVDHYTGYTVAECMAMPnfARTLIHPDDVERVAPEFQKGLQGFRG 423
Cdd:COG2202 4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKT--LRDLLPPEDDDEFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 424 DDLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITERKKSEEKIRELAFYDTLTRLPNRALLLDRLRESMAAS 503
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILY 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740671249 504 RENNVCGALMFIDLDHF-KTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVGGDEFVVVL 565
Cdd:COG2202 162 VNPAAEELLGYSPEELLgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVW 224
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
480-649 |
2.18e-23 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 101.68 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 480 YDTLTRLPNRALLLDRLrESMAASRENNVCgALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVGGD 559
Cdd:PRK09894 131 MDVLTGLPGRRVLDESF-DHQLRNREPQNL-YLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGE 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 560 EFVVVLgnlslnKAAATAETEAAGEKI-LAVLGRAYELNGVQFRSTASIGVTVFNGEQTsTDELFKQADLAMYKSKERGR 638
Cdd:PRK09894 209 EFIICL------KAATDEEACRAGERIrQLIANHAITHSDGRINITATFGVSRAFPEET-LDVVIGRADRAMYEGKQTGR 281
|
170
....*....|.
gi 740671249 639 NAMCFFDPAMQ 649
Cdd:PRK09894 282 NRVMFIDEQNV 292
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
474-898 |
2.45e-21 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 99.55 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 474 IRELAFYDTLTRLPNRALLLDRL------RESMAASrennvcGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSV 547
Cdd:PRK11059 224 IRSNAFQDAKTGLGNRLFFDNQLatlledQEMVGAH------GVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFV 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 548 -SKGDTV-ARVGGDEFVVVLGNLSLNKAaataeteaagEKILAVLGRAYE---LNGVQFRSTA-SIGVTVFNGEQtSTDE 621
Cdd:PRK11059 298 mRYPGALlARYSRSDFAVLLPHRSLKEA----------DSLASQLLKAVDalpPPKMLDRDDFlHIGICAYRSGQ-STEQ 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 622 LFKQADLAMYKSKERGRNAMCFFDPAMQT-----TVLKRAELEvglrSAIEENRFVLhYQAQVVDGD-HITGAEALVRWE 695
Cdd:PRK11059 367 VMEEAEMALRSAQLQGGNGWFVYDKAQLPekgrgSVRWRTLLE----QTLVRGGPRL-YQQPAVTRDgKVHHRELFCRIR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 696 HPVCGLIPPAEFIPLAEETGLILEIGRMVLESACAQLALWATEPqmahlsIAVNVSARQFREPDFV---ESVLGVINRKG 772
Cdd:PRK11059 442 DGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEEN------LSINLSVDSLLSRAFQrwlRDTLLQCPRSQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 773 ARadRLKLELTESVLVENVEDIIEKMGALRARGVTFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDI-LEDPNDADIA 851
Cdd:PRK11059 516 RK--RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIhKRTENQLFVR 593
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 740671249 852 RTIVALARSfDLGVIAEGVETEAQRDFLAVAGCHAYQGFLFCKPLPV 898
Cdd:PRK11059 594 SLVGACAGT-ETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
342-486 |
1.25e-20 |
|
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: 96.20 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 342 MTRELRESEEKFRAIADCTVNLEIWWGPDGKPRWINPSVDHYTGYTVAECMAMPNFarTLIHPDDVERVAPEFQKGLQGF 421
Cdd:COG5809 132 MEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSIL--ELIHSDDQENVAAFISQLLKDG 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740671249 422 RGDDLEFRCVRKDGSLLWLSLSWVPIsNARGDFVGFRTSGRDITERKKSEEKIRELafyDTLTRL 486
Cdd:COG5809 210 GIAQGEVRFWTKDGRWRLLEASGAPI-KKNGEVDGIVIIFRDITERKKLEELLRKS---EKLSVV 270
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
438-639 |
1.27e-17 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 85.65 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 438 LWLSLSWVPISNARGDFVGFRTSGRdITERKKseeKIRELAFYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDL 517
Cdd:PRK10245 169 WWLSLPVIVIYPLLFAWVSYQTATK-LAEHKR---RLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDI 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 518 DHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVGGDEFVVVLGNlslnkaaataeteAAGEKILAVLGRAYE-L 596
Cdd:PRK10245 245 DHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSG-------------TPAESAITAMSRVHEgL 311
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 740671249 597 NGV------QFRSTASIGVTVFNGEQTSTDELFKQADLAMYKSKERGRN 639
Cdd:PRK10245 312 NTLrlpnapQVTLRISVGVAPLNPQMSHYREWLKSADLALYKAKNAGRN 360
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
344-474 |
4.50e-17 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 81.99 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 344 RELRESEEKFRAIADCTVNLEIWWGPDGKPRWINPSVDHYTGYTVAECMAMPNFArtLIHPDDVERVAPEFQKGLQG-FR 422
Cdd:COG2202 130 EALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLD--LLHPEDRERLLELLRRLLEGgRE 207
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 740671249 423 GDDLEFRCVRKDGSLLWLSLSWVPISNaRGDFVGFRTSGRDITERKKSEEKI 474
Cdd:COG2202 208 SYELELRLKDGDGRWVWVEASAVPLRD-GGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
478-636 |
8.16e-16 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 80.82 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 478 AFYDTLTRLPNRALLLDRLRESMAASRENNvCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVG 557
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGINTLMNNSDARK-TSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLG 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 558 GDEFVVVLGNLSLNKAAataeteaagEKILAVLGRAYEL-----NGVQFRSTASIGVTVfNGEQTSTDELFKQADLAMYK 632
Cdd:PRK09966 327 GDEFAMVLYDVQSESEV---------QQICSALTQIFNLpfdlhNGHQTTMTLSIGYAM-TIEHASAEKLQELADHNMYQ 396
|
....
gi 740671249 633 SKER 636
Cdd:PRK09966 397 AKHQ 400
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
339-477 |
2.64e-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: 76.55 E-value: 2.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 339 ASGMTRELRESEEKFRAIADCTVNLEIWWGPDGKPRWINPSVDHYTGYTVAECMAMPNfaRTLIHPDDVERVAPEFQKGL 418
Cdd:COG5809 3 SSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNI--LDFLHPDDEKELREILKLLK 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 740671249 419 QGFRGDDLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITERKKSEEKIREL 477
Cdd:COG5809 81 EGESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRES 139
|
|
| CHASE |
COG3452 |
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ... |
1-856 |
4.50e-14 |
|
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442675 [Multi-domain] Cd Length: 785 Bit Score: 76.50 E-value: 4.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 1 MIRVRSVLLPLFVLTASLCVTWTVWNHERQATSKELRTQFDYTLGDAVSRIEQRMASYELMLRGVQSLFAANGTIDRDRF 80
Cdd:COG3452 8 LLRRRPLLLALLAFLLLLAVGAVLERLLREQEEQQLRAEVLQELSAIRARLEGELNARLSLLRGLAALVEANPGISQEEF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 81 RRYvgALNLDANFSGIHAVGVVewvpaaqkaghvarmreegvPGYTIlpegqREDYaPLVQREPYVGitqsspgFDTWSD 160
Cdd:COG3452 88 ERL--ARNLLEDYPGIRNIALA--------------------PDGVI-----RYVY-PLAGNEAALG-------LDLRTD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 161 PVRRAAMERARDSGMAALSGTVHLLidadsDLRPGFIMYLPIYASGETQesvlqrraHITGWVYASFRMHDVMAS--LYG 238
Cdd:COG3452 133 PEQRAAALRARESGQLVLAGPVNLV-----QGGRGLIGRLPVFLDGGDD--------RFWGFVSAVIDLDRLLDSagLDD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 239 EQPaGVSLAV--YDGVAASDAALLyrTPAANGWHAPALMSaneyLVVDGRDWMLSMDASDEFRSRLGSNAEPLIAGAGIG 316
Cdd:COG3452 200 AQD-GYQIALrgRDGDGAEGEVFY--GDAALFDQDPVTLE----VNLPGGSWQLAAAPKGGWLASPRNALPLRLAGLLIS 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 317 LSLLLALLTWLMVTGRERAIRLASGMTRELRESEEKFRAIADctvnleiwwgpdgkprwinpsVDHYTGYTVAECMAMPN 396
Cdd:COG3452 273 LLLALLVYLLRQLLLLRLLLLLLRLELIAAALLLLLLALDLL---------------------LELLLLLRLAEALLQER 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 397 FARTLIHPDDVERVAPEF-QKGLQGFRGDDLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSG---RDITERKKSEE 472
Cdd:COG3452 332 LRALALLAALEDLLLLKFdRDLLDLLLLLELEAILALLLLLRRLLRSREARGGLGGDLVRVGGVIDgrvAVILIIEALEL 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 473 KIRELAFYDTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDT 552
Cdd:COG3452 412 AEARLAALDQERDASDVALGAALVVLEALLIIALLRELALLAGALLARKSLLLALDLAAESERLRYLELLLGDALRERIR 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 553 VARVGGDEFVVVLGNLSLNKAAATAETEAAGEKILAVLGRAYELNGVQFRSTASIGVTVFNGEQTSTDELFKQADLAMYK 632
Cdd:COG3452 492 RALLRLQLLSLDLSALAAVLGAESLAGLLISVFIDARILEAERLELALVAGEVALEELLLRLLGEILLLRAELILALLDA 571
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 633 SKERGRNAMCFFDPAMQTTVLKRAELEVGLRSAIEENRFVLHyqaqVVDGDHITGAEALVRWEHPVCGLIPPAEFIPLAE 712
Cdd:COG3452 572 KSGLSALELSGLLAGRAALDSLLLLLALALRQLDESALFILE----ELLLRLIIDLRIERLLLLLLGGEILLGELALLLL 647
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 713 ETGLILEIGRMVLESACAQLAL-WATEPQMAHLSIAVNVSARQFREpdfvesvLGVINRKGARADRLKLELTESVLVENV 791
Cdd:COG3452 648 LLVLIILILLSVEEAGLILALSlLLALLLLAILDAAVSLLATLLLL-------FQLLLLLLIILEGLLAELVAEALRLAL 720
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 740671249 792 EDIIEKMGALRARGVTFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVA 856
Cdd:COG3452 721 ALAQLLLRLLLAELLQLLLLLLGLILLELLLRLDGLLVELIALRLEILILTLLILDADEILADQT 785
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
775-900 |
4.60e-14 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 75.22 E-value: 4.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 775 ADRLKLELTESVLVEnvEDIIEKMGALRARGVTFSLDDFGigySSLSYLKRLPL-DQLKIDrsfVRDIledpnDADIART 853
Cdd:COG3434 83 PERVVLEILEDVEPD--EELLEALKELKEKGYRIALDDFV---LDPEWDPLLPLaDIIKID---VLAL-----DLEELAE 149
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 740671249 854 IVALARSFDLGVIAEGVETEAQRDFLAVAGCHAYQGFLFCKPLPVRS 900
Cdd:COG3434 150 LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
349-474 |
1.83e-13 |
|
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: 67.70 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 349 SEEKFRAIADCTVNLEIWWGPDGKPRWINPSVDHYTGYTVAECMAMPnfARTLIHPDDVERVAPEFQKGLQGFRGDD-LE 427
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRN--VLELIPEEDREEVRERIERRLEGEPEPVsEE 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 740671249 428 FRCVRKDGSLLWLSLSWVPISNArGDFVGFRTSGRDITERKKSEEKI 474
Cdd:TIGR00229 79 RRVRRKDGSEIWVEVSVSPIRTN-GGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
367-464 |
2.16e-12 |
|
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: 64.19 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 367 WGPDGKPRWINPSVDHYTGYTVAECMAMPNFArtLIHPDDVERVAPEFQKGLQGFRGDDLEFRCVRKDGSLLWLSLSWVP 446
Cdd:cd00130 8 LDLDGRILYANPAAEQLLGYSPEELIGKSLLD--LIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTP 85
|
90
....*....|....*...
gi 740671249 447 ISNARGDFVGFRTSGRDI 464
Cdd:cd00130 86 IRDEGGEVIGLLGVVRDI 103
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
376-457 |
4.11e-12 |
|
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: 62.74 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 376 INPSVDHYTGYTVAECMAMPNFARTLIHPDDVERVAPEFQKGLQGFRGDDLEFRCVRKDGSLLWLSLSWVPISNARGDFV 455
Cdd:pfam08447 4 WSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENGKPV 83
|
..
gi 740671249 456 GF 457
Cdd:pfam08447 84 RV 85
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
481-565 |
8.26e-12 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 68.83 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 481 DTLTRLPNRALLLDRLRESMAASRENNVCGALMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSKGDTVARVGGDE 560
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLGGDE 423
|
....*
gi 740671249 561 FVVVL 565
Cdd:NF040885 424 FCIIL 428
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
512-566 |
1.26e-09 |
|
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: 57.37 E-value: 1.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 740671249 512 LMFIDLDHFKTLNDTLGHDKGDLLLRHVAYRLSSSVSK-GDTVARVGGDEFVVVLG 566
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRsGDLKIKTIGDEFMVVSG 59
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
345-486 |
7.52e-09 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 58.70 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 345 ELRESEEKFRAIADCTVNLEIWWGPDGKPRWINPSVDHYTGYTVAECMAMPnfARTLIHPDDveRVAPEFQKGLQ-GFRG 423
Cdd:COG3852 1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRP--LAELFPEDS--PLRELLERALAeGQPV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 740671249 424 DDLEFRCVRKDGSLLWLSLSWVPISNARGDfVGFRTSGRDITERKKSEEKIRELAFYDTLTRL 486
Cdd:COG3852 77 TEREVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGEL 138
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
345-475 |
2.77e-08 |
|
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: 57.43 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 345 ELRESEEKFRAIADCTVNLEIWWGPDGKPRWINPSVDHYTGYTVAECMAMPnfARTLIHPDDVERVAPEFQKGLQGFRGD 424
Cdd:COG5805 151 ILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKN--LLELLHPCDKEEFKERIESITEVWQEF 228
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 740671249 425 DLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITERKKSEEKIR 475
Cdd:COG5805 229 IIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMA 279
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
425-467 |
4.71e-07 |
|
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: 47.18 E-value: 4.71e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 740671249 425 DLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITER 467
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
356-476 |
1.81e-06 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 51.76 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 356 IADCTVnleiwwgPDGKPRWINPSVDHYTGYTVAEcmAMPNFARTLIHPD-DVERVApEFQKGLQGFRGDDLEFRCVRKD 434
Cdd:PRK13558 163 IADATL-------PDEPLIYINDAFERITGYSPDE--VLGRNCRFLQGEDtNEERVA-ELREAIDEERPTSVELRNYRKD 232
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 740671249 435 GSLLWLSLSWVPISNARGD---FVGFRTsgrDITERKKSEEKIRE 476
Cdd:PRK13558 233 GSTFWNQVDIAPIRDEDGTvthYVGFQT---DVTERKEAELALQR 274
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
778-908 |
3.27e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 49.61 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 778 LKLELTESVLVENvEDIIEKMgalrARGVTFSLDDFGIGYSSLSYLKRLPLDQLKIDRSFVRDILEDPNDADIARTIVAL 857
Cdd:PRK11596 130 LRFELVEHIRLPK-DSPFASM----CEFGPLWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHL 204
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 740671249 858 ARSFDLGVIAEGVETeaQRDFLAVAGCHAY--QGFLFCKPLPVRSFEQFVASF 908
Cdd:PRK11596 205 MNRYCRGVIVEGVET--PEEWRDVQRSPAFaaQGYFLSRPAPFETLETLPLAL 255
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
385-475 |
3.86e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 50.83 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 385 GYTVAECMAMPNFARTLIHPDDVERVAPEFQK-GLQGFRGDDLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSGRD 463
Cdd:PRK13560 508 GYEPDEFISGKRMFAAIIHPADLEQVAAEVAEfAAQGVDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVID 587
|
90
....*....|..
gi 740671249 464 ITERKKSEEKIR 475
Cdd:PRK13560 588 ISERKHAEEKIK 599
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
375-466 |
4.43e-06 |
|
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: 45.92 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 375 WINPSVDHYTGYTVAECMAMpNFARTLIHPDDVERVAPEFQkglQGFRGDDLEFRCVRKDGSLLWLSLSWVPISNARGDF 454
Cdd:pfam13426 6 YVNDAALRLLGYTREELLGK-SITDLFAEPEDSERLREALR---EGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDGGEL 81
|
90
....*....|..
gi 740671249 455 VGFRTSGRDITE 466
Cdd:pfam13426 82 VGIIAILRDITE 93
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
551-634 |
1.06e-05 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 46.83 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 551 DTVARVGGDEFVVVLGNLSLNkaaataETEAAGEKILAVLGRAYElngvqFRSTASIGVtvfngeqtSTDELFKQADlAM 630
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLE------GALAVAERIREAVAELPS-----LRVTVSIGV--------AGDSLLKRAD-AL 175
|
....
gi 740671249 631 YKSK 634
Cdd:COG3706 176 YQAR 179
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
328-478 |
1.75e-05 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 48.90 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 328 MVTGRERAIRlasgmtRELRESEEKFR------AIADCTVnleiwwGPDGKPRWINPSVDHYTGYTVAECMAMPnFaRTL 401
Cdd:PRK09776 266 MVMYAFRAER------KHISESETRFRnameysAIGMALV------GTEGQWLQVNKALCQFLGYSQEELRGLT-F-QQL 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 402 IHPDDVERVAPEFQKGLQG----FRgddLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITERKKSEEKIREL 477
Cdd:PRK09776 332 TWPEDLNKDLQQVEKLLSGeinsYS---MEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKRTEQVNERL 408
|
.
gi 740671249 478 A 478
Cdd:PRK09776 409 M 409
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
329-476 |
1.68e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 45.43 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 329 VTGRERAirlasgmTRELRESEEKFRAIADCTVNLEIWWGPDGKPRWI-NPSVDHYTGYTVAECMAMPNFART------- 400
Cdd:PRK13560 317 ISGRRAA-------ERELLEKEDMLRAIIEAAPIAAIGLDADGNICFVnNNAAERMLGWSAAEVMGKPLPGMDpelneef 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 401 ------LIHPDD---VERVAPEFQKGLQGFRGDDLEFRCVRKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITERKKSE 471
Cdd:PRK13560 390 wcgdfqEWYPDGrpmAFDACPMAKTIKGGKIFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVE 469
|
....*
gi 740671249 472 EKIRE 476
Cdd:PRK13560 470 EQLLL 474
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
367-464 |
2.87e-04 |
|
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: 41.25 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 367 WGPDGKPRWINPSVDHYTGYTVAECMAmPNFARTLIHPDDVERVAPEFQKGLQGFRGDDLEFRCVRKDGSLLWLSLSWVP 446
Cdd:pfam00989 17 VDEDGRILYVNAAAEELLGLSREEVIG-KSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFRVPDGRPRHVEVRASP 95
|
90
....*....|....*...
gi 740671249 447 ISNARGDFVGFRTSGRDI 464
Cdd:pfam00989 96 VRDAGGEILGFLGVLRDI 113
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
367-468 |
3.75e-04 |
|
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: 40.86 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 367 WGPDGKPRWINPSVDHYTGYTVAECMAMPnfARTLIHPDDVERVAPEFQKGLQGfrGDDLEF-RCVRKDGSLLWLSLSWV 445
Cdd:pfam08448 11 LDPDGRVRYANAAAAELFGLPPEELLGKT--LAELLPPEDAARLERALRRALEG--EEPIDFlEELLLNGEERHYELRLT 86
|
90 100
....*....|....*....|...
gi 740671249 446 PISNARGDFVGFRTSGRDITERK 468
Cdd:pfam08448 87 PLRDPDGEVIGVLVISRDITERR 109
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
351-419 |
4.59e-04 |
|
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: 39.30 E-value: 4.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 740671249 351 EKFRAIADCTVNLeIW-WGPDGKPRWINPSVDHYTGYTVAECMAMPNFArtLIHPDDVERVAPEFQKGLQ 419
Cdd:smart00091 1 ERLRAILESLPDG-IFvLDLDGRILYANPAAEELLGYSPEELIGKSLLE--LIHPEDRERVQEALQRLLS 67
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
432-476 |
2.59e-03 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 41.58 E-value: 2.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 740671249 432 RKDGSLLWLSLSWVPISNARGDFVGFRTSGRDITERKKSEEKIRE 476
Cdd:PRK13557 112 RKDGSSFWNALFVSPVYNDAGDLVYFFGSQLDVSRRRDAEDALRQ 156
|
|
| |
