|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
113-768 |
2.91e-168 |
|
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: 502.00 E-value: 2.91e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 113 IRTIMWPIGGLTLLWMLPAFLWFDHVSPAAQVALILILFGMASGASVTMSTVPPAALLFVAMVAISSLIAMLKLEQSSAL 192
Cdd:COG5001 5 AALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 193 FLTPIYTGLLTYAILWNVRHFAGHLAATLELEEKGELINLLREFDASGSEWLWELAPNLTVAHLSDGLAAAIGERPQDLI 272
Cdd:COG5001 85 LLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 273 GRPIIDLLDPDHSVSAVSAGMRNILDSLRSSRSFRDLAIPAKGGRAWWLLSGKPQFDAAGRLTCWRGVGSDITLSRLTGH 352
Cdd:COG5001 165 LLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 353 DSIT-AARHDPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPAHQ 431
Cdd:COG5001 245 ERLRhLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 432 -VGRLGGDEFALVLTGATDRETLSNLAEAVIVVLSAPYRISGAELNIGATIGIAIAPLDGITQEGLTRSADLALYSAKKA 510
Cdd:COG5001 325 tVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 511 GRGSFLFFEGAMAEEAAANRALESDLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAG 590
Cdd:COG5001 405 GRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 591 LIGQVGNWVLREACREAAGWVD----GARVAVNVSSAQLAAgPALVGHVIHALAASGLEARRLELEVTESIFLAGDATTR 666
Cdd:COG5001 485 LIVPLGEWVLREACRQLAAWQDaglpDLRVAVNLSARQLRD-PDLVDRVRRALAETGLPPSRLELEITESALLEDPEEAL 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 667 TTLDQLRAVGVRLVLDDFGMGYSSYACLTNGEFNTLKIDRSFTvaAAAPGRPAERAIVESILTLARGLDLDVTAEGIETG 746
Cdd:COG5001 564 ETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFV--RDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETE 641
|
650 660
....*....|....*....|..
gi 2730583529 747 EQAALMVALGCGQLQGFLFGRP 768
Cdd:COG5001 642 EQLEFLRELGCDYAQGYLFSRP 663
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
265-768 |
8.57e-97 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 315.47 E-value: 8.57e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 265 GERPQDLIGRPIIDLLdpdHSVSAVSAGMRNILDSLRSSRSFR-DLAIPAKGGRAWWLLSGKPQFDAAGR----LTCwrg 339
Cdd:PRK10060 145 GLKEHDVIGQSVFKLF---MSRREAAASRRNIRGFFRSGNAYEvERWIKTRKGQRLFLFRNKFVHSGSGKneifLIC--- 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 340 VGSDITLSRLTGHDSITAARHDPMTGLANRLLVRELLEEAlIRGRPmGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEV 419
Cdd:PRK10060 219 SGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHA-INAAD-NNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 420 ARRLERIAPAHQV-GRLGGDEFaLVLTGATDRETLSNLAEAVIVVLSAPYRISGAELNIGATIGIAIAPLDGITQEGLTR 498
Cdd:PRK10060 297 SLAILSCLEEDQTlARLGGDEF-LVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIR 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 499 SADLALYSAKKAGRGSFLFFEGAMAEEAAANRALESDLRSALKLGELSLAYQPIVHARShEVIAREALLRWTHPVRGEVA 578
Cdd:PRK10060 376 SADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWRG-EVRSLEALVRWQSPERGLIP 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 579 PDLFVPVIEDAGLIGQVGNWVLREACREAAGWVD---GARVAVNVSSAQLaAGPALVGHVIHALAASGLEARRLELEVTE 655
Cdd:PRK10060 455 PLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDkgiNLRVAVNVSARQL-ADQTIFTALKQALQELNFEYCPIDVELTE 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 656 SIFLAGDATTRTTLDQLRAVGVRLVLDDFGMGYSSYACLTNGEFNTLKIDRSFTVAAAApgRPAERAIVESILTLARGLD 735
Cdd:PRK10060 534 SCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHK--QPVSQSLVRAIVAVAQALN 611
|
490 500 510
....*....|....*....|....*....|...
gi 2730583529 736 LDVTAEGIETGEQAALMVALGCGQLQGFLFGRP 768
Cdd:PRK10060 612 LQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
534-768 |
1.85e-89 |
|
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: 281.74 E-value: 1.85e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 534 SDLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAGLIGQVGNWVLREACREAAGWVDG 613
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 614 A---RVAVNVSSAQLAAgPALVGHVIHALAASGLEARRLELEVTESIFLAGDATTRTTLDQLRAVGVRLVLDDFGMGYSS 690
Cdd:cd01948 81 GpdlRLSVNLSARQLRD-PDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2730583529 691 YACLTNGEFNTLKIDRSFTvaAAAPGRPAERAIVESILTLARGLDLDVTAEGIETGEQAALMVALGCGQLQGFLFGRP 768
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFV--RDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
206-768 |
6.76e-88 |
|
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: 289.38 E-value: 6.76e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 206 ILWNVRHFAGHLAATLELEEKGELINLLREFDASGSEWLWELAPNLTVAHLSDGLAAAIGERPQDLIGRPIIDLLDPDHS 285
Cdd:COG2200 3 LLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 286 VSAVSAGMRNILDSLRSSRSFRDLAIPAKGGRAWWLLSGKPQFDAAGRLTCWRGVGSDITLSRLTGHDSITAARHDPMTG 365
Cdd:COG2200 83 LALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 366 LANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPAHQVGRLGGDEFALVLT 445
Cdd:COG2200 163 LLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 446 GATDRETLSNLAEAVIVVLSAPYRISGAELNIGATIGIAIAPLDGITQEGLTRSADLALYSAKKAGRGSFLFFEGAMAEE 525
Cdd:COG2200 243 LLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEAR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 526 AAANRALESDLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAGLIGQVGNWVLREACR 605
Cdd:COG2200 323 ARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 606 EAAGWVD---GARVAVNVSSAQLAAgPALVGHVIHALAASGLEARRLELEVTESIFLAGDATTRTTLDQLRAVGVRLVLD 682
Cdd:COG2200 403 QLARWPErglDLRLSVNLSARSLLD-PDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALD 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 683 DFGMGYSSYACLTNGEFNTLKIDRSFTvaAAAPGRPAERAIVESILTLARGLDLDVTAEGIETGEQAALMVALGCGQLQG 762
Cdd:COG2200 482 DFGTGYSSLSYLKRLPPDYLKIDRSFV--RDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQG 559
|
....*.
gi 2730583529 763 FLFGRP 768
Cdd:COG2200 560 YLFGRP 565
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
535-774 |
4.75e-82 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 262.15 E-value: 4.75e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 535 DLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAGLIGQVGNWVLREACREAAGWVDGA 614
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 615 ----RVAVNVSSAQLAAgPALVGHVIHALAASGLEARRLELEVTESIFLAGDATTRTTLDQLRAVGVRLVLDDFGMGYSS 690
Cdd:smart00052 83 ppplLISINLSARQLIS-PDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 691 YACLTNGEFNTLKIDRSFTvaAAAPGRPAERAIVESILTLARGLDLDVTAEGIETGEQAALMVALGCGQLQGFLFGRPeI 770
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFV--RDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP-L 238
|
....
gi 2730583529 771 PFDA 774
Cdd:smart00052 239 PLDD 242
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
359-771 |
3.58e-76 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 263.17 E-value: 3.58e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 359 RHDPMTGLANRLLVRELLEEALIRGRPMgggcALMLVDLDRFKLVNDTLGHEVGDELLCEVARRL-ERIAPAHQVGRLGG 437
Cdd:PRK11359 377 QFDPLTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFrEKLKPDQYLCRIEG 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 438 DEFALVlTGATDRETLSNLAEAVIVVLSAPYRISGAELNIGATIGIAIAPldGITQEGLTRSADLALYSAKKAGRGSFLF 517
Cdd:PRK11359 453 TQFVLV-SLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDV--GKNRDYLLSTAHNAMDYIRKNGGNGWQF 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 518 FEGAMAEEAAANRALESDLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAGLIGQVGN 597
Cdd:PRK11359 530 FSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGR 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 598 WVLREACREAAGWVD-GARV-AVNVS-SAQLAAGPALVGHVIHALAASGLEARRLELEVTESIFLAGDATTRTTLDQLRA 674
Cdd:PRK11359 610 WVIAEACRQLAEWRSqNIHIpALSVNlSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRD 689
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 675 VGVRLVLDDFGMGYSSYACLTNGEFNTLKIDRSFTVAAAAPGRPaeRAIVESILTLARGLDLDVTAEGIETGEQAALMVA 754
Cdd:PRK11359 690 MGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRI--LALLEAITSIGQSLNLTVVAEGVETKEQFEMLRK 767
|
410 420
....*....|....*....|.
gi 2730583529 755 LGCGQLQGFLFGRP----EIP 771
Cdd:PRK11359 768 IHCRVIQGYFFSRPlpaeEIP 788
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
535-768 |
7.24e-67 |
|
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: 221.42 E-value: 7.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 535 DLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAGLIGQVGNWVLREACREAAGWVDGA 614
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 615 --RVAVNVSSAQLaAGPALVGHVIHALAASGLEARRLELEVTESIFLAGDATTRTTLDQLRAVGVRLVLDDFGMGYSSYA 692
Cdd:pfam00563 83 diKLSINLSPASL-ADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2730583529 693 CLTNGEFNTLKIDRSFTvaAAAPGRPAERAIVESILTLARGLDLDVTAEGIETGEQAALMVALGCGQLQGFLFGRP 768
Cdd:pfam00563 162 YLLRLPPDFVKIDRSLI--ADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
354-768 |
4.55e-59 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 212.65 E-value: 4.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 354 SITAARHdPMTGLANRLLVRELLEEALIRGRPMgggcALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPAHQV- 432
Cdd:PRK13561 228 SRNATRF-PVSDLPNKALLMALLEQVVARKQTT----ALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVl 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 433 GRLGGDEFALVLTGATDRETLSNLAEAVIVVLSAPYRISGAELNIGATIGIAIApLDGITQEGLTRSADLALYSAKKAGR 512
Cdd:PRK13561 303 AQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFTARRKGK 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 513 GSFLFFEGAMAEEAAANRALESDLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAGLI 592
Cdd:PRK13561 382 NQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLM 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 593 GQVGNWVLREACREAAGWvdGAR-----VAVNVSSAQLAAgPALVGHVIHALAASGLEARRLELEVTESIFLAGDATTRT 667
Cdd:PRK13561 462 VTVGHWVLEESCRLLAAW--QERgimlpLSVNLSALQLMH-PNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVA 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 668 TLDQLRAVGVRLVLDDFGMGYSSYACLTNGE---FNTLKIDRSFTvaaaaPGRPAERAIVESILTLARGLDLDVTAEGIE 744
Cdd:PRK13561 539 ILRPLRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMFV-----DGLPEDDSMVAAIIMLAQSLNLQVIAEGVE 613
|
410 420
....*....|....*....|....
gi 2730583529 745 TGEQAALMVALGCGQLQGFLFGRP 768
Cdd:PRK13561 614 TEAQRDWLLKAGVGIAQGFLFARA 637
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
534-768 |
1.88e-52 |
|
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: 191.28 E-value: 1.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 534 SDLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPvRGE-VAPDLFVPVIEDAGLIGQVGNWVLREACREAAGWV- 611
Cdd:COG4943 274 RRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDP-DGSvISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLa 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 612 --DGARVAVNVSSAQLAAgPALVGHVIHALAASGLEARRLELEVTESIFLAGDATtRTTLDQLRAVGVRLVLDDFGMGYS 689
Cdd:COG4943 353 adPDFHISINLSASDLLS-PRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKA-RAVIAALREAGHRIAIDDFGTGYS 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 690 SYACLTNGEFNTLKIDRSFTvaaAAPGRP-AERAIVESILTLARGLDLDVTAEGIETGEQAALMVALGCGQLQGFLFGRP 768
Cdd:COG4943 431 SLSYLQTLPVDILKIDKSFV---DAIGTDsANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKP 507
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
359-515 |
2.64e-51 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 176.21 E-value: 2.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 359 RHDPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPAHQ-VGRLGG 437
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDlVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2730583529 438 DEFALVLTGaTDRETLSNLAEAVIVVLSAPYRISGAELNIGATIGIAIAPLDGITQEGLTRSADLALYSAKKAGRGSF 515
Cdd:cd01949 81 DEFAILLPG-TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
362-768 |
9.53e-51 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 189.00 E-value: 9.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 362 PMTGLANRLLVRELLEEALIRGRPMGGGCaLMLVDLDRFKLVNDTLGHEVGDELLCEVARRLER-IAPAHQVGRLGGDEF 440
Cdd:PRK11829 236 PVTELPNRSLFISLLEKEIASSTRTDHFH-LLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQcIDDSDLLAQLSKTEF 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 441 ALVLTGATDRETLSNLAEAVIVVLSAPYRISGAELNIGATIGIAIAPLDGITQEGLTRSADLALYSAKKAGRGSFLFFEG 520
Cdd:PRK11829 315 AVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 521 AMAEEAAANRALESDLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAGLIGQVGNWVL 600
Cdd:PRK11829 395 HLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 601 REACREAAGWvdGAR-----VAVNVSSAQLaAGPALVGHVIHALAASGLEARRLELEVTESIFLAGDATTRTTLDQLRAV 675
Cdd:PRK11829 475 EEACRILADW--KARgvslpLSVNISGLQV-QNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGL 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 676 GVRLVLDDFGMGYSSYACLTNGE---FNTLKIDRSFTvaaaaPGRPAERAIVESILTLARGLDLDVTAEGIETGEQAALM 752
Cdd:PRK11829 552 GLLIALDDFGIGYSSLRYLNHLKslpIHMIKLDKSFV-----KNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWL 626
|
410
....*....|....*.
gi 2730583529 753 VALGCGQLQGFLFGRP 768
Cdd:PRK11829 627 LEHGIQCGQGFLFSPP 642
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
343-774 |
2.48e-48 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 185.26 E-value: 2.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 343 DITLSRLTGHDSITAARHDPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVAR- 421
Cdd:PRK09776 650 DVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASl 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 422 RLERIAPAHQVGRLGGDEFALVL---TGATDRETLSNLAEAvivVLSAPYRISGAELNIGATIGIAIAPLDGITQEGLTR 498
Cdd:PRK09776 730 MLSMLRSSDVLARLGGDEFGLLLpdcNVESARFIATRIISA---INDYHFPWEGRVYRVGASAGITLIDANNHQASEVMS 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 499 SADLALYSAKKAGRG--SFLFFEGAMAEEAAANRALESDLRSALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGE 576
Cdd:PRK09776 807 QADIACYAAKNAGRGrvTVYEPQQAAAHSEHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEI 886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 577 VAPDLFVPVIEDAGLIGQVGNWVLREACREAAGWV--DGARVAVNVSSAQLAAgPALVGHVIHALAASGLEARRLELEVT 654
Cdd:PRK09776 887 IDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVasKGLSIALPLSVAGLSS-PTLLPFLLEQLENSPLPPRLLHLEIT 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 655 ESIFLAGDATTRTTLDQLRAVGVRLVLDDFGMGYSSYACLTNGEFNTLKIDRSFtVAAAApGRPAERAIVESILTLARGL 734
Cdd:PRK09776 966 ETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGEL-VANLH-GNLMDEMLISIIQGHAQRL 1043
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2730583529 735 DLDVTAEGIETGEQAALMVALGCGQLQGFLFGRPEiPFDA 774
Cdd:PRK09776 1044 GMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQ-PLDL 1082
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
357-518 |
2.16e-45 |
|
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: 164.00 E-value: 2.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 357 AARHDPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPAH-QVGRL 435
Cdd:COG2199 113 LATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESdLVARL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 436 GGDEFALVLTGaTDRETLSNLAEAVIVVLSA-PYRISGAELNIGATIGIAIAPLDGITQEGLTRSADLALYSAKKAGRGS 514
Cdd:COG2199 193 GGDEFAVLLPG-TDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNR 271
|
....
gi 2730583529 515 FLFF 518
Cdd:COG2199 272 VVVY 275
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
358-518 |
8.47e-44 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 155.48 E-value: 8.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 358 ARHDPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPAHQ-VGRLG 436
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDlLARLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 437 GDEFALVLTGaTDRETLSNLAEAVIVVLSAPYRISGAELNIGATIGIAIAPLDGITQEGLTRSADLALYSAKKAGRGSFL 516
Cdd:smart00267 83 GDEFALLLPE-TSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 2730583529 517 FF 518
Cdd:smart00267 162 VY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
358-514 |
1.56e-43 |
|
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: 154.72 E-value: 1.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 358 ARHDPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIA-PAHQVGRLG 436
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLrRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 437 GDEFALVLTGaTDRETLSNLAEAVIVVLSA---PYRISGAELNIGATIGIAIAPLDGITQEGLTRSADLALYSAKKAGRG 513
Cdd:pfam00990 81 GDEFAILLPE-TSLEGAQELAERIRRLLAKlkiPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
.
gi 2730583529 514 S 514
Cdd:pfam00990 160 R 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
358-513 |
1.03e-34 |
|
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: 129.76 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 358 ARHDPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRL-ERIAPAHQVGRLG 436
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILqSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2730583529 437 GDEFALVLTGaTDRETLSNLAEAV-IVVLSAPYRISGAE-LNIGATIGIAIAPLDGITQEGLTRSADLALYSAKKAGRG 513
Cdd:TIGR00254 82 GEEFVVILPG-TPLEDALSKAERLrDAINSKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
538-768 |
6.95e-29 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 121.64 E-value: 6.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 538 SALKLGELSLAYQPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAGLIGQVGNWVLREACREAAGWVD----G 613
Cdd:PRK10551 270 TGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKvlpvG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 614 ARVAVNVSSAQLAAgPALVGHVIHALAASGLEARRLELEVTEsiflagdattRTTLDQ---------LRAVGVRLVLDDF 684
Cdd:PRK10551 350 AKLGINISPAHLHS-DSFKADVQRLLASLPADHFQIVLEITE----------RDMVQEeeatklfawLHSQGIEIAIDDF 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 685 GMGYSSYACLTNGEFNTLKIDRSF-------TVAAaapgrpaerAIVESILTLARGLDLDVTAEGIETGEQAALMVALGC 757
Cdd:PRK10551 419 GTGHSALIYLERFTLDYLKIDRGFiqaigteTVTS---------PVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGV 489
|
250
....*....|.
gi 2730583529 758 GQLQGFLFGRP 768
Cdd:PRK10551 490 NFLQGYWISRP 500
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
353-512 |
9.83e-29 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 120.39 E-value: 9.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 353 DSITAARHDPMTGLANR----LLVRELLEEALIRGRPMgggcALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLER-IA 427
Cdd:PRK09581 287 QSIEMAVTDGLTGLHNRryfdMHLKNLIERANERGKPL----SLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNnIR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 428 PAHQVGRLGGDEFALVLTGaTDRETLSNLAEAV-IVVLSAPYRISGAELNIGATIGIAIAPLD--GITQEGLTRSADLAL 504
Cdd:PRK09581 363 GTDLIARYGGEEFVVVMPD-TDIEDAIAVAERIrRKIAEEPFIISDGKERLNVTVSIGVAELRpsGDTIEALIKRADKAL 441
|
....*...
gi 2730583529 505 YSAKKAGR 512
Cdd:PRK09581 442 YEAKNTGR 449
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
356-512 |
4.11e-25 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 106.30 E-value: 4.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 356 TAARHDPMTGLANRLLVRELLEEALIRGRPMGggCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLER-IAPAHQVGR 434
Cdd:PRK09894 127 IRSNMDVLTGLPGRRVLDESFDHQLRNREPQN--LYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASwTRDYETVYR 204
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2730583529 435 LGGDEFALVLTGATDRETLSNLAEAVIVVLSAPYRISGAELNIGATIGIAIAPLDGITQEGLTRsADLALYSAKKAGR 512
Cdd:PRK09894 205 YGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEETLDVVIGR-ADRAMYEGKQTGR 281
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
358-508 |
6.55e-22 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 98.93 E-value: 6.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 358 ARHDPMTGLANRLLVRELLEeALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPA-HQVGRLG 436
Cdd:PRK09966 248 ALHDPLTGLANRAAFRSGIN-TLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLrHKAYRLG 326
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2730583529 437 GDEFALVLTGATDRETLSNLAEAVIVVLSAPYRI-SGAELNIGATIGIAIApLDGITQEGLTRSADLALYSAK 508
Cdd:PRK09966 327 GDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGYAMT-IEHASAEKLQELADHNMYQAK 398
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
358-512 |
1.36e-19 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 93.16 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 358 ARHDPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPAHQV-GRLG 436
Cdd:PRK15426 398 AWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVaGRVG 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 437 GDEFALVLTGATDRETLsNLAE---------AVIVVLSAPYRISgaelnigATIGIAIAPLDG-ITQEGLTRSADLALYS 506
Cdd:PRK15426 478 GEEFCVVLPGASLAEAA-QVAErirlrinekEILVAKSTTIRIS-------ASLGVSSAEEDGdYDFEQLQSLADRRLYL 549
|
....*.
gi 2730583529 507 AKKAGR 512
Cdd:PRK15426 550 AKQAGR 555
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
361-513 |
4.81e-18 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 86.81 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 361 DPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPAHQV-GRLGGDE 439
Cdd:PRK10245 208 DGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDViGRFGGDE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 440 FALVLTGATdretlsnlAEAVIVVLS------APYRISGAElNIGATIGIAIAPLDgiTQEGLTR----SADLALYSAKK 509
Cdd:PRK10245 288 FAVIMSGTP--------AESAITAMSrvheglNTLRLPNAP-QVTLRISVGVAPLN--PQMSHYRewlkSADLALYKAKN 356
|
....
gi 2730583529 510 AGRG 513
Cdd:PRK10245 357 AGRN 360
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
392-492 |
3.77e-08 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 52.74 E-value: 3.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 392 LMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIAPAHQ--VGRLGGDEFaLVLTGATDRETLSNLAEAVIVVLSA--P 467
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdlKIKTIGDEF-MVVSGLDHPAAAVAFAEDMREAVSAlnQ 82
|
90 100
....*....|....*....|....*
gi 2730583529 468 YRISGAELNIGATIGIAIAPLDGIT 492
Cdd:cd07556 83 SEGNPVRVRIGIHTGPVVVGVIGSR 107
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
547-770 |
1.01e-07 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 55.19 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 547 LAYQPIVHaRSHEVIAREALLRwthpvrgeVAPDLFVPVIEDAGLIGQVgnwvLREACREAA-GWVDGARVA-VNVSSAQ 624
Cdd:COG3434 6 VARQPILD-RDQRVVGYELLFR--------SGLENSAPDVDGDQATARV----LLNAFLEIGlDRLLGGKLAfINFTEEL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 625 LAAGPALVghvihalaasgLEARRLELEVTESIflAGDATTRTTLDQLRAVGVRLVLDDFGMGYSSYACLTNGEFntLKI 704
Cdd:COG3434 73 LLSDLPEL-----------LPPERVVLEILEDV--EPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADI--IKI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2730583529 705 DrsftVAAAAPGRpaeraiVESILTLARGLDLDVTAEGIETGEQAALMVALGCGQLQGFLFGRPEI 770
Cdd:COG3434 138 D----VLALDLEE------LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
222-345 |
3.63e-06 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 49.25 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 222 ELEEKGELINLLREFDASGSEWLWELAPNLTVAHLSDGLAAAIGERPQDLIGRPIIDLLDPDHSVSAVsagmRNILDSLR 301
Cdd:COG2202 2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFL----ELLRAALA 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2730583529 302 SSRSFRD--LAIPAKGGRAWWLLSGKPQFDAAGRLTCWRGVGSDIT 345
Cdd:COG2202 78 GGGVWRGelRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDIT 123
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
361-769 |
2.39e-05 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 47.93 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 361 DPMTGLANRLLVRELLEEALIRGRPMGGGCALMLVDLDRFKLVNDTLGHEVGDELLCEVARRLERIA---PAHQVGRLGG 437
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmryPGALLARYSR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 438 DEFALVLTGATDRETLSNLAEAVIVVLS-APYRISGAE--LNIGATigiaiAPLDGITQEGLTRSADLALYSA------- 507
Cdd:PRK11059 311 SDFAVLLPHRSLKEADSLASQLLKAVDAlPPPKMLDRDdfLHIGIC-----AYRSGQSTEQVMEEAEMALRSAqlqggng 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 508 ----KKA-----GRGSFLFfegamaeeaaanralESDLRSALKLGELSLAYQPIVhARSHEVIAREALLRWTHPVRGEVA 578
Cdd:PRK11059 386 wfvyDKAqlpekGRGSVRW---------------RTLLEQTLVRGGPRLYQQPAV-TRDGKVHHRELFCRIRDGQGELLS 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 579 PDLFVPVIEDAGLIGQVGNWVLREACREAAGWVDgARVAVNVSSAQLAAGPalvghVIHALAASGLE-----ARRLELEV 653
Cdd:PRK11059 450 AELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPE-ENLSINLSVDSLLSRA-----FQRWLRDTLLQcprsqRKRLIFEL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 654 TESIFLAGDATTRTTLDQLRAVGVRLVLDDFGMGYSSYACLTNGEFNTLKIDRSFTvaaaapgrpaeRAI---------V 724
Cdd:PRK11059 524 AEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLV-----------RNIhkrtenqlfV 592
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2730583529 725 ESILTLARGLDLDVTAEGIETGEQAALMVALGCGQLQGFLFGRPE 769
Cdd:PRK11059 593 RSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQ 637
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
241-344 |
1.74e-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. 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: 41.46 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 241 SEWLWELAPNLTVAHLSDGLAAAIGERPQDLIGRPIIDLLDPDHsvsavSAGMRNILDSLRSSRSFRDL---AIPAKGGR 317
Cdd:cd00130 2 PDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPED-----REELRERLENLLSGGEPVTLevrLRRKDGSV 76
|
90 100
....*....|....*....|....*..
gi 2730583529 318 AWWLLSGKPQFDAAGRLTCWRGVGSDI 344
Cdd:cd00130 77 IWVLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
432-508 |
4.65e-04 |
|
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: 41.82 E-value: 4.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2730583529 432 VGRLGGDEFALVLTGaTDRETLSNLAEAVIVVLSAPYrisgaELNIGATIGIAIapldgitqEGLTRSADlALYSAK 508
Cdd:COG3706 118 VARYGGEEFAILLPG-TDLEGALAVAERIREAVAELP-----SLRVTVSIGVAG--------DSLLKRAD-ALYQAR 179
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
250-345 |
1.83e-03 |
|
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: 38.21 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 250 NLTVAHLSDGLAAAIGERPQDLIGRPIIDLLDPDHSVSAvsagMRNILDSLRSSRSFRDLAIPAKGGRAWWLLSGKPQFD 329
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSER----LREALREGKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76
|
90
....*....|....*.
gi 2730583529 330 AAGRLTCWRGVGSDIT 345
Cdd:pfam13426 77 DGGELVGIIAILRDIT 92
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
228-345 |
3.13e-03 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 40.39 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 228 ELINLLREFDASGSEWLWELAPNLTVAHLSDGLAAAIGERPQDLIGRPIIDLLDPDHsVSAVSAGMRNILDSLRSSRSFR 307
Cdd:COG2202 134 ESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPED-RERLLELLRRLLEGGRESYELE 212
|
90 100 110
....*....|....*....|....*....|....*...
gi 2730583529 308 dLAIPAKGGRAWWLLSGKPQFDAAGRLTCWRGVGSDIT 345
Cdd:COG2202 213 -LRLKDGDGRWVWVEASAVPLRDGGEVIGVLGIVRDIT 249
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
236-345 |
4.34e-03 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 37.78 E-value: 4.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 236 FDASgSEWLWELAPNLTVAHLSDGLAAAIGERPQDLIGRPIIDLLdPDHSVSAVSAGMRNILDSLRSSRSFRDLAIPakG 315
Cdd:pfam08448 1 LDSL-PDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELL-PPEDAARLERALRRALEGEEPIDFLEELLLN--G 76
|
90 100 110
....*....|....*....|....*....|
gi 2730583529 316 GRAWWLLSGKPQFDAAGRLTCWRGVGSDIT 345
Cdd:pfam08448 77 EERHYELRLTPLRDPDGEVIGVLVISRDIT 106
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
150-679 |
5.98e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 40.24 E-value: 5.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 150 LFGMASGASVTMSTVPPAALLFVAMVAISSLIAMLKLEQSSALFLTPIYTGLLTYAILWNVRHFAGHLAATLELEEKGEL 229
Cdd:COG3321 852 LYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLA 931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 230 INLLREFDASGSEWLWELAPNLTVAHLSDGLAAAIGERPQDLIGRPIIDLLDPDHSVSAVSAGMRNILDSLRSSRSFRDL 309
Cdd:COG3321 932 LVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALL 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 310 AIPAKGGRAWWLLSGKPQFDAAGRLTCWRGVGSDITLSRLTGHDSITAARHDPMTGLANRLLVRELLEEALIRGRPMGGG 389
Cdd:COG3321 1012 LAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALA 1091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 390 CALMLVDLDRFklvndtLGHEVGDELLCEVARRLERIAPAHQVGRLGGDEFALVLTGATDRETLSNLAEAVIVVLSAPYR 469
Cdd:COG3321 1092 AAALALALAAL------AAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAA 1165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 470 ISGAELNIGATIGIAIAPLDGITQEGLTRSADLALYSAKKAGRGSFLFFEGAMAEEAAANRALESDLRSALKLGELSLAY 549
Cdd:COG3321 1166 ALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAV 1245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2730583529 550 QPIVHARSHEVIAREALLRWTHPVRGEVAPDLFVPVIEDAGLIGQVGNWVLREACREAAGWVDGARVAVNVSSAQLAAGP 629
Cdd:COG3321 1246 AALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAAL 1325
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2730583529 630 ALVGHVIHALAASGLEARRLELEVTESIFLAGDATTRTTLDQLRAVGVRL 679
Cdd:COG3321 1326 LAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAA 1375
|
|
| |
