|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
59-716 |
4.98e-180 |
|
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: 530.12 E-value: 4.98e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 59 SSIAHDQESATVWDDAVTNSLARNPDWMETNLGVWMNTYFGHDAAIVLTADLDPIYQFLVDHNDASTADGLRTAYLPLAT 138
Cdd:COG5001 8 LLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 139 KLKERLIAGDQDGTSSKVLSIGEADIVYVGSRPAIVSIKPIVSDTGDIEQQPGRENLHVAVRFLDGDLAATVGQEYQFEN 218
Cdd:COG5001 88 ALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 219 LRFALHQPTDPRFSYLALHSTSGQVVGYFEWQPFRPGQQVLEATIPAIAFAFFAIFSAASVGGNALWRRSNRLKANQEQL 298
Cdd:COG5001 168 LLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 299 QYQAAHDILTGLANRSEFNARVATA-AQNAREDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLPDS-LVA 376
Cdd:COG5001 248 RHLAYHDPLTGLPNRRLFLDRLEQAlARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGdTVA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 377 RIGGDEFTVLVTS-NDLLKPEHVAKAIVDDLRLPFEIEETQVTIGASVGVAV--KNGAfDANEAIRQADIALYHAKAAGR 453
Cdd:COG5001 328 RLGGDEFAVLLPDlDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALypDDGA-DAEELLRNADLAMYRAKAAGR 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 454 NTYAIFGEHMDELLRKRRAMEADLRKAVNgRAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGL 533
Cdd:COG5001 407 NRYRFFDPEMDERARERLELEADLRRALE-RGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 534 IHEIGAIVLEDACSMLAH-----FPDIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERT 608
Cdd:COG5001 486 IVPLGEWVLREACRQLAAwqdagLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALET 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 609 IAALRAAGVRFAIDDFGTGYSSFSRVQKIEVDRIKIDRSFIEEIHRS-DNRALVTAMINVARAKGLKITAEGVETTEQRD 687
Cdd:COG5001 566 LRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDpDDAAIVRAIIALAHSLGLEVVAEGVETEEQLE 645
|
650 660
....*....|....*....|....*....
gi 1424287064 688 ALESLGCHHLQGFLLARPLSPNAARALLS 716
Cdd:COG5001 646 FLRELGCDYAQGYLFSRPLPAEELEALLR 674
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
475-708 |
6.06e-93 |
|
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: 289.45 E-value: 6.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 475 ADLRKAVNgRAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGLIHEIGAIVLEDACSMLAH--- 551
Cdd:cd01948 1 ADLRRALE-RGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARwqa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 552 -FPDIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERTIAALRAAGVRFAIDDFGTGYSS 630
Cdd:cd01948 80 gGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424287064 631 FSRVQKIEVDRIKIDRSFIEEIHRS-DNRALVTAMINVARAKGLKITAEGVETTEQRDALESLGCHHLQGFLLARPLSP 708
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDpEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
295-710 |
3.51e-92 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 301.60 E-value: 3.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 295 QEQLQYQAAHDILTGLANRSEFNARVATAAQNaREDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLP-DS 373
Cdd:PRK10060 230 QERLRILANTDSITGLPNRNAIQELIDHAINA-ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEeDQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 374 LVARIGGDEFTVLVTSNDLLKPEHVAKAIVDDLRLPFEIEETQVTIGASVGVAVKNGAFDANEA-IRQADIALYHAKAAG 452
Cdd:PRK10060 309 TLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESlIRSADTAMYTAKEGG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 453 RNTYAIFGEHMDELLRKRRAMEADLRKAVNgRAEIEIFYQPVFSARdGMLCSLEALARWNHPTLGYVSPGEFIPLAEECG 532
Cdd:PRK10060 389 RGQFCVFSPEMNQRVFEYLWLDTNLRKALE-NDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESG 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 533 LIHEIGAIVLEDACSMLAHFPD----IDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERT 608
Cdd:PRK10060 467 LIVPLGRWVMLDVVRQVAKWRDkginLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSV 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 609 IAALRAAGVRFAIDDFGTGYSSFSRVQKIEVDRIKIDRSFIEEIHR-SDNRALVTAMINVARAKGLKITAEGVETTEQRD 687
Cdd:PRK10060 547 IQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKqPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDA 626
|
410 420
....*....|....*....|...
gi 1424287064 688 ALESLGCHHLQGFLLARPLSPNA 710
Cdd:PRK10060 627 FLTKNGVNERQGFLFAKPMPAVA 649
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
474-710 |
1.57e-83 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 264.85 E-value: 1.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 474 EADLRKAVNgRAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGLIHEIGAIVLEDACSMLAHFP 553
Cdd:smart00052 1 ERELRQALE-NGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 554 -----DIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERTIAALRAAGVRFAIDDFGTGY 628
Cdd:smart00052 80 aqgppPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 629 SSFSRVQKIEVDRIKIDRSFIEEI-HRSDNRALVTAMINVARAKGLKITAEGVETTEQRDALESLGCHHLQGFLLARPLS 707
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLqTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
...
gi 1424287064 708 PNA 710
Cdd:smart00052 240 LDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
474-705 |
3.42e-73 |
|
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: 237.60 E-value: 3.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 474 EADLRKAVNGRaEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGLIHEIGAIVLEDACSMLA--- 550
Cdd:pfam00563 1 ARALRRALENG-EFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAqlq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 551 HFPDIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERTIAALRAAGVRFAIDDFGTGYSS 630
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424287064 631 FSRVQKIEVDRIKIDRSFIEEIHRSD-NRALVTAMINVARAKGLKITAEGVETTEQRDALESLGCHHLQGFLLARP 705
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGeARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
301-456 |
5.40e-32 |
|
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: 122.06 E-value: 5.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 301 QAAHDILTGLANRSEFNARVATAAQNA-REDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLPDS-LVARI 378
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRArRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSdVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 379 GGDEFTVLVTSNDLlkpeHVAKAIVDDLR-----LPFEIEE-TQVTIGASVGVA-VKNGAFDANEAIRQADIALYHAKAA 451
Cdd:TIGR00254 81 GGEEFVVILPGTPL----EDALSKAERLRdainsKPIEVAGsETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKA 156
|
....*
gi 1424287064 452 GRNTY 456
Cdd:TIGR00254 157 GRNRV 161
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
59-716 |
4.98e-180 |
|
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: 530.12 E-value: 4.98e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 59 SSIAHDQESATVWDDAVTNSLARNPDWMETNLGVWMNTYFGHDAAIVLTADLDPIYQFLVDHNDASTADGLRTAYLPLAT 138
Cdd:COG5001 8 LLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 139 KLKERLIAGDQDGTSSKVLSIGEADIVYVGSRPAIVSIKPIVSDTGDIEQQPGRENLHVAVRFLDGDLAATVGQEYQFEN 218
Cdd:COG5001 88 ALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 219 LRFALHQPTDPRFSYLALHSTSGQVVGYFEWQPFRPGQQVLEATIPAIAFAFFAIFSAASVGGNALWRRSNRLKANQEQL 298
Cdd:COG5001 168 LLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 299 QYQAAHDILTGLANRSEFNARVATA-AQNAREDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLPDS-LVA 376
Cdd:COG5001 248 RHLAYHDPLTGLPNRRLFLDRLEQAlARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGdTVA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 377 RIGGDEFTVLVTS-NDLLKPEHVAKAIVDDLRLPFEIEETQVTIGASVGVAV--KNGAfDANEAIRQADIALYHAKAAGR 453
Cdd:COG5001 328 RLGGDEFAVLLPDlDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALypDDGA-DAEELLRNADLAMYRAKAAGR 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 454 NTYAIFGEHMDELLRKRRAMEADLRKAVNgRAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGL 533
Cdd:COG5001 407 NRYRFFDPEMDERARERLELEADLRRALE-RGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 534 IHEIGAIVLEDACSMLAH-----FPDIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERT 608
Cdd:COG5001 486 IVPLGEWVLREACRQLAAwqdagLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALET 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 609 IAALRAAGVRFAIDDFGTGYSSFSRVQKIEVDRIKIDRSFIEEIHRS-DNRALVTAMINVARAKGLKITAEGVETTEQRD 687
Cdd:COG5001 566 LRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDpDDAAIVRAIIALAHSLGLEVVAEGVETEEQLE 645
|
650 660
....*....|....*....|....*....
gi 1424287064 688 ALESLGCHHLQGFLLARPLSPNAARALLS 716
Cdd:COG5001 646 FLRELGCDYAQGYLFSRPLPAEELEALLR 674
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
286-715 |
2.81e-101 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 323.27 E-value: 2.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 286 RRSNRLKANQEQLQYQAAHDILTGLANRSEFNARVATAAQNAREDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGAR 365
Cdd:COG2200 139 LALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALL 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 366 LTSLLPDSLVARIGGDEFTVLVTSNDLLKPEHVAKAIVDDLRL---PFEIEETQVTIGASVGVAVKNGAFDANEAIRQAD 442
Cdd:COG2200 219 LLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLllePLLLGGGLVVVASSGGGAAAPDDGADAALLLAAA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 443 IALYHAKAAGRNTYAIFGEHMDELLRKRRAMEADLRKAVNgRAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPG 522
Cdd:COG2200 299 AAAAAAAAGGGRGRVVFFAAAEARARRRLALESELREALE-EGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPA 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 523 EFIPLAEECGLIHEIGAIVLEDACSMLAHFP----DIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAA 598
Cdd:COG2200 378 EFIPAAERSGLIVELDRWVLERALRQLARWPerglDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESAL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 599 TGEDGRSERTIAALRAAGVRFAIDDFGTGYSSFSRVQKIEVDRIKIDRSFIEEIHRS-DNRALVTAMINVARAKGLKITA 677
Cdd:COG2200 458 LEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDpRDQAIVRAIVALAHRLGLKVVA 537
|
410 420 430
....*....|....*....|....*....|....*...
gi 1424287064 678 EGVETTEQRDALESLGCHHLQGFLLARPLSPNAARALL 715
Cdd:COG2200 538 EGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALL 575
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
475-708 |
6.06e-93 |
|
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: 289.45 E-value: 6.06e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 475 ADLRKAVNgRAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGLIHEIGAIVLEDACSMLAH--- 551
Cdd:cd01948 1 ADLRRALE-RGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARwqa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 552 -FPDIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERTIAALRAAGVRFAIDDFGTGYSS 630
Cdd:cd01948 80 gGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424287064 631 FSRVQKIEVDRIKIDRSFIEEIHRS-DNRALVTAMINVARAKGLKITAEGVETTEQRDALESLGCHHLQGFLLARPLSP 708
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDpEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
295-710 |
3.51e-92 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 301.60 E-value: 3.51e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 295 QEQLQYQAAHDILTGLANRSEFNARVATAAQNaREDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLP-DS 373
Cdd:PRK10060 230 QERLRILANTDSITGLPNRNAIQELIDHAINA-ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEeDQ 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 374 LVARIGGDEFTVLVTSNDLLKPEHVAKAIVDDLRLPFEIEETQVTIGASVGVAVKNGAFDANEA-IRQADIALYHAKAAG 452
Cdd:PRK10060 309 TLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESlIRSADTAMYTAKEGG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 453 RNTYAIFGEHMDELLRKRRAMEADLRKAVNgRAEIEIFYQPVFSARdGMLCSLEALARWNHPTLGYVSPGEFIPLAEECG 532
Cdd:PRK10060 389 RGQFCVFSPEMNQRVFEYLWLDTNLRKALE-NDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESG 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 533 LIHEIGAIVLEDACSMLAHFPD----IDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERT 608
Cdd:PRK10060 467 LIVPLGRWVMLDVVRQVAKWRDkginLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSV 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 609 IAALRAAGVRFAIDDFGTGYSSFSRVQKIEVDRIKIDRSFIEEIHR-SDNRALVTAMINVARAKGLKITAEGVETTEQRD 687
Cdd:PRK10060 547 IQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKqPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDA 626
|
410 420
....*....|....*....|...
gi 1424287064 688 ALESLGCHHLQGFLLARPLSPNA 710
Cdd:PRK10060 627 FLTKNGVNERQGFLFAKPMPAVA 649
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
474-710 |
1.57e-83 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 264.85 E-value: 1.57e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 474 EADLRKAVNgRAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGLIHEIGAIVLEDACSMLAHFP 553
Cdd:smart00052 1 ERELRQALE-NGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 554 -----DIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERTIAALRAAGVRFAIDDFGTGY 628
Cdd:smart00052 80 aqgppPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 629 SSFSRVQKIEVDRIKIDRSFIEEI-HRSDNRALVTAMINVARAKGLKITAEGVETTEQRDALESLGCHHLQGFLLARPLS 707
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLqTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
...
gi 1424287064 708 PNA 710
Cdd:smart00052 240 LDD 242
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
294-720 |
1.58e-83 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 281.66 E-value: 1.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 294 NQEQLQYQAAHDILTGLANRSEFNARVATAAQNAREDeahAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLL-PD 372
Cdd:PRK11359 368 SRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSP---VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLkPD 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 373 SLVARIGGDEFTVLVTSNDLLKPEHVAKAIVDDLRLPFEIEETQVTIGASVGVAVKNGAfDANEAIRQADIALYHAKAAG 452
Cdd:PRK11359 445 QYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDVGK-NRDYLLSTAHNAMDYIRKNG 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 453 RNTYAIFGEHMDELLRKRRAMEADLRKAVNGrAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECG 532
Cdd:PRK11359 524 GNGWQFFSPAMNEMVKERLVLGAALKEAISN-NQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIG 602
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 533 LIHEIGAIVLEDACSMLAHFPDIDI-----ALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSER 607
Cdd:PRK11359 603 EIENIGRWVIAEACRQLAEWRSQNIhipalSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFK 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 608 TIAALRAAGVRFAIDDFGTGYSSFSRVQKIEVDRIKIDRSFIEEIHRSDN-RALVTAMINVARAKGLKITAEGVETTEQR 686
Cdd:PRK11359 683 RIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRiLALLEAITSIGQSLNLTVVAEGVETKEQF 762
|
410 420 430
....*....|....*....|....*....|....
gi 1424287064 687 DALESLGCHHLQGFLLARPLSPNAARALLSTPDP 720
Cdd:PRK11359 763 EMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLP 796
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
474-705 |
3.42e-73 |
|
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: 237.60 E-value: 3.42e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 474 EADLRKAVNGRaEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGLIHEIGAIVLEDACSMLA--- 550
Cdd:pfam00563 1 ARALRRALENG-EFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAqlq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 551 HFPDIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDGRSERTIAALRAAGVRFAIDDFGTGYSS 630
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424287064 631 FSRVQKIEVDRIKIDRSFIEEIHRSD-NRALVTAMINVARAKGLKITAEGVETTEQRDALESLGCHHLQGFLLARP 705
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGeARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
466-725 |
2.82e-71 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 242.13 E-value: 2.82e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 466 LLRKRRAMEADLRKAVNGRaEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGLIHEIG----AIV 541
Cdd:COG4943 265 LLRRRLSPRRRLRRAIKRR-EFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTrqviEQV 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 542 LEDACSMLAHFPDIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITE-SAATGEDGRseRTIAALRAAGVRFA 620
Cdd:COG4943 344 FRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITErGFIDPAKAR--AVIAALREAGHRIA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 621 IDDFGTGYSSFSRVQKIEVDRIKIDRSFIEEI-HRSDNRALVTAMINVARAKGLKITAEGVETTEQRDALESLGCHHLQG 699
Cdd:COG4943 422 IDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIgTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQG 501
|
250 260
....*....|....*....|....*.
gi 1424287064 700 FLLARPLSPNAARALLSTPDPVSTLP 725
Cdd:COG4943 502 WLFAKPLPAEEFIAWLAAQRAPASAP 527
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
292-705 |
7.91e-66 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 236.49 E-value: 7.91e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 292 KANQEQLQYQAAHDILTGLANRSEFNARVATAAQNARE-DEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLL 370
Cdd:PRK09776 655 RKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNStHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSML 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 371 -PDSLVARIGGDEFTVLVTSNDLLKPEHVAKAIVDDLR-LPFEIEETQVTIGASVGV-AVKNGAFDANEAIRQADIALYH 447
Cdd:PRK09776 735 rSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINdYHFPWEGRVYRVGASAGItLIDANNHQASEVMSQADIACYA 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 448 AKAAGRNTYAIFGEHMDELLRKRRAMEADLRKAVNGRAEIEIFYQPVFSARDGMLCSL-EALARWNHPTLGYVSPGEFIP 526
Cdd:PRK09776 815 AKNAGRGRVTVYEPQQAAAHSEHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHwLISLRLWDPEGEIIDEGAFRP 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 527 LAEECGLIHEIGAIVLEDACSMLA---HFPDIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATGEDG 603
Cdd:PRK09776 895 AAEDPALMHALDRRVIHEFFRQAAkavASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAE 974
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 604 RSERTIAALRAAGVRFAIDDFGTGYSSFSRVQKIEVDRIKIDRSFIEEIHRSD-NRALVTAMINVARAKGLKITAEGVET 682
Cdd:PRK09776 975 SASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLmDEMLISIIQGHAQRLGMKTIAGPVEL 1054
|
410 420
....*....|....*....|...
gi 1424287064 683 TEQRDALESLGCHHLQGFLLARP 705
Cdd:PRK09776 1055 PLVLDTLSGIGVDLAYGYAIARP 1077
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
286-718 |
6.99e-65 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 227.67 E-value: 6.99e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 286 RRSNRLKANQEQLQYQAAHDILTGLANRSEFnarVATAAQNAREDEAHAVLFIDLDRFKEVNDSLGHPAGDRLI-SLVGA 364
Cdd:PRK13561 215 LNQQLLQRQYEEQSRNATRFPVSDLPNKALL---MALLEQVVARKQTTALMIITCETLRDTAGVLKEAQREILLlTLVEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 365 RLTSLLPDSLVARIGGDEFTVLVtsNDLLKPEH---VAKAIVDDLRLPFEIEETQVTIGASVGVAVKNGAFDANEAIRQA 441
Cdd:PRK13561 292 LKSVLSPRMVLAQISGYDFAIIA--NGVKEPWHaitLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 442 DIALYHAKAAGRNTYAIFGEHMDELLRKRRAMEADLRKAVNGRaEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSP 521
Cdd:PRK13561 370 ISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENH-QFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLP 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 522 GEFIPLAEECGLIHEIGAIVLEDACSMLAHFPDIDIAL----NASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESA 597
Cdd:PRK13561 449 EGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLplsvNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESR 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 598 ATGEDGRSERTIAALRAAGVRFAIDDFGTGYSSFSRVQKIE---VDRIKIDRSFIEEIhrSDNRALVTAMINVARAKGLK 674
Cdd:PRK13561 529 RIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGL--PEDDSMVAAIIMLAQSLNLQ 606
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1424287064 675 ITAEGVETTEQRDALESLGCHHLQGFLLARPLSPNA-ARALLSTP 718
Cdd:PRK13561 607 VIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIfEERYLEEK 651
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
285-707 |
6.23e-57 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 205.95 E-value: 6.23e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 285 WRRSNRLKANQEQLQYQAAHDI-LTGLANRSEFNARVATAAQNAREDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVG 363
Cdd:PRK11829 214 YNRNQQLLADAYADMGRISHRFpVTELPNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 364 ARLTSLL-PDSLVARIGGDEFTVLvtSNDLLKPE---HVAKAIVDDLRLPFEIEETQVTIGASVGVAVKNGAFDANEAI- 438
Cdd:PRK11829 294 QRIEQCIdDSDLLAQLSKTEFAVL--ARGTRRSFpamQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMm 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 439 RQADIALYHAKAAGRNTYAIFGEHMDELLRKRRAMEADLRKAVNgRAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGY 518
Cdd:PRK11829 372 RNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIE-NHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSY 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 519 VSPGEFIPLAEECGLIHEIGAIVLEDACSMLAHFP----DIDIALNASLLELCSPAYPLNVIAALEKWKVSANRLEIEIT 594
Cdd:PRK11829 451 VLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKargvSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEIT 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 595 ESAATGEDGRSERTIAALRAAGVRFAIDDFGTGYSSFS---RVQKIEVDRIKIDRSFIEEIHRSDnrALVTAMINVARAK 671
Cdd:PRK11829 531 ETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRylnHLKSLPIHMIKLDKSFVKNLPEDD--AIARIISCVSDVL 608
|
410 420 430
....*....|....*....|....*....|....*.
gi 1424287064 672 GLKITAEGVETTEQRDALESLGCHHLQGFLLARPLS 707
Cdd:PRK11829 609 KVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
194-459 |
1.83e-51 |
|
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: 180.56 E-value: 1.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 194 NLHVAVRFLDGDLAATVGQEYQFENLRFALHQPTDPRFSYLALHSTSGQVVGYFEWQPFRPGQQVLEATIPAIAFAFFAI 273
Cdd:COG2199 6 LLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 274 FSAASVGGNALWRRSNRLKANQEQLQYQAAHDILTGLANRSEFNARVATAAQNA-REDEAHAVLFIDLDRFKEVNDSLGH 352
Cdd:COG2199 86 LLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARArREGRPLALLLIDLDHFKRINDTYGH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 353 PAGDRLISLVGARLTSLLPDS-LVARIGGDEFTVLVTSNDLLKPEHVAKAIVDDL-RLPFEIEETQVTIGASVGVAV-KN 429
Cdd:COG2199 166 AAGDEVLKEVARRLRASLRESdLVARLGGDEFAVLLPGTDLEEAEALAERLREALeQLPFELEGKELRVTVSIGVALyPE 245
|
250 260 270
....*....|....*....|....*....|
gi 1424287064 430 GAFDANEAIRQADIALYHAKAAGRNTYAIF 459
Cdd:COG2199 246 DGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
304-457 |
1.87e-49 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 170.82 E-value: 1.87e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 304 HDILTGLANRSEFNARVATAAQNA-REDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLPDS-LVARIGGD 381
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARArRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESdLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424287064 382 EFTVLVTSNDLLKPEHVAKAIVDDLRLPFEIEETQVTIGASVGVAV-KNGAFDANEAIRQADIALYHAKAAGRNTYA 457
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATyPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
302-454 |
1.61e-45 |
|
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: 159.73 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 302 AAHDILTGLANRSEFNARVATAAQNA-REDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLPDS-LVARIG 379
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRAlREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSdLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1424287064 380 GDEFTVLVTSNDLLKPEHVAKAI---VDDLRLPFEIEETQVTIGASVGVAV-KNGAFDANEAIRQADIALYHAKAAGRN 454
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIrrlLAKLKIPHTVSGLPLYVTISIGIAAyPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
300-459 |
1.62e-45 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 160.11 E-value: 1.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 300 YQAAHDILTGLANRSEFNARVATAAQNA-REDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLPDS-LVAR 377
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGdLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 378 IGGDEFTVLVTSNDLLKPEHVAKAIVDDLRLPFEIEETQVTIGASVGVAVK-NGAFDANEAIRQADIALYHAKAAGRNTY 456
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 1424287064 457 AIF 459
Cdd:smart00267 161 AVY 163
|
|
| CHASE4 |
COG3322 |
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ... |
11-724 |
1.52e-38 |
|
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442551 [Multi-domain] Cd Length: 724 Bit Score: 153.17 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 11 WRFSLPVMASFAICGLLLL-----SLYFAAIASDGIAVARQRDVVALTVSKLKSSIAHDQESATVWDDAVTNSLARNPDW 85
Cdd:COG3322 5 RKTLLAILLLLLLLLALLYlvsrlILLSSFSELEEQAAERDVERVLNALDAELDQLARLVADWAVWDDTYEFVQDGDPEW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 86 METNLGVWMNTYFGHDAAIVLTADLDPIYQFLVDHNDASTADgLRTAYLPLATKLKERLIAGDQDgtsskvlsIGEADIV 165
Cdd:COG3322 85 IESNLGDWTFENLGLDLVLVLDPDGRLVYSKGYDLEDGELVP-LPEALAPLLARARALLRHASPD--------SSVSGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 166 YVGSRPAIVSIKPIVSDTGdieqQPGRENLHVAVRFLDGDLAATVGQEYQFeNLRFALHQPTDPRF------------SY 233
Cdd:COG3322 156 RLDGGPALVAARPILPSDG----PGPPRGTLVFGRYLDEAFLARLAERTGL-DLTLSPADPPAPPDqvveplsddtiaGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 234 LALHSTSGQVVGYFEWQPFRP----GQQVLEATIPAIAFAFFAIFSAASVGGNALWRRSNRLKANQEQLQYQAAHDILTG 309
Cdd:COG3322 231 VPLRDIDGQPVLLLRWTPPRPiyqqGRALLRYLLPALLLLGLLLALLALLLLRLVLLLLLLLLRLVLSRLLLLLLRLLLL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 310 LANRSEFNARVATAAQNAREDEAhAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLPDSLVARIGGDEFTVLVTs 389
Cdd:COG3322 311 ELLRALELLLLLLRRLLLLLLLL-RLLLLLLDLLAALNLLLLLRALAERLVALALLALLLLGLLGLLAALRRLGLLAIL- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 390 ndllkpehVAKAIVDDLRLPFEIEETQVTIGASVGVAVKNGAFDANEAIRQADIALYHAKAAGRNTYAIFGEHMDELLRK 469
Cdd:COG3322 389 --------ALAEEAARLLLLALAIAGELLIGIEVLLALGLELAGSAIALARAAAALALLLAAAAAARLAARAASGLLRDL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 470 RRAMEADLRKAVNGRAEIEIFYQPVFSARDG--MLCSLEALARWNHPTLGYVSPGEFIPLAEECGLIHEIGAIVLEDACS 547
Cdd:COG3322 461 LEADELEDRLRRALLAEAAALLLLALLALELllALGDAALEILLAILLLGLVLEAQLAELERLLLLGEAGGELLEEIALL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 548 MLAHFPDIDIALNASLLELCSPAYPLNVIAALEKWKVSAnRLEIEITESAATGEDGRSERTIAALRAAGVRFAIDDFGTG 627
Cdd:COG3322 541 AALLAGLLLAVLLSLLLRLLLLIDALVALAEAAAGLLEA-LLEEEVELRRALLEAEELLLIALALLSLGLALALDDGGRG 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 628 YSSFSRVQKIEVDRIKIDRSFIEEI-HRSDNRALVTAMINVARAKGLKITAEGVETTEQRDALESLGCHHLQGFLLARPL 706
Cdd:COG3322 620 LAGLLLLFRLSGIGLLLLRRLLGDDlLGLLAALIDLILALAGSLLLLTLAAAAEATAVVLVAELLEGALLLQALALISLL 699
|
730
....*....|....*...
gi 1424287064 707 SPNAARALLSTPDPVSTL 724
Cdd:COG3322 700 ELLLLLLLLELQLLEQVL 717
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
484-719 |
1.40e-35 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 141.67 E-value: 1.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 484 RAEIEIFYQPVFSARDGMLCSLEALARWNHPTLGYVSPGEFIPLAEECGLI----HEIGAIVLEDACSMLAHFP-DIDIA 558
Cdd:PRK10551 274 RGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIvpltQHLFELIARDAAELQKVLPvGAKLG 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 559 LNASLLELCSPAYPLNVIAALEKWKVSANRLEIEITESAATgEDGRSERTIAALRAAGVRFAIDDFGTGYSSFSRVQKIE 638
Cdd:PRK10551 354 INISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMV-QEEEATKLFAWLHSQGIEIAIDDFGTGHSALIYLERFT 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 639 VDRIKIDRSFIEEIhrsdNRALVT-----AMINVARAKGLKITAEGVETTEQRDALESLGCHHLQGFLLARPLSPNAARA 713
Cdd:PRK10551 433 LDYLKIDRGFIQAI----GTETVTspvldAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVR 508
|
....*.
gi 1424287064 714 LLSTPD 719
Cdd:PRK10551 509 WLKEPY 514
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
301-456 |
5.40e-32 |
|
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: 122.06 E-value: 5.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 301 QAAHDILTGLANRSEFNARVATAAQNA-REDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLPDS-LVARI 378
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRArRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSdVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 379 GGDEFTVLVTSNDLlkpeHVAKAIVDDLR-----LPFEIEE-TQVTIGASVGVA-VKNGAFDANEAIRQADIALYHAKAA 451
Cdd:TIGR00254 81 GGEEFVVILPGTPL----EDALSKAERLRdainsKPIEVAGsETLTVTVSIGVAcYPGHGLTLEELLKRADEALYQAKKA 156
|
....*
gi 1424287064 452 GRNTY 456
Cdd:TIGR00254 157 GRNRV 161
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
301-705 |
4.80e-26 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 113.80 E-value: 4.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 301 QAAHDILTGLANRSEFNARVATAAQNAREDEAHAVLF-IDLDRFKEVNDSLGHPAGDRLISLVGARLTSLL---PDSLVA 376
Cdd:PRK11059 227 NAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMlIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmryPGALLA 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 377 RIGGDEFTVLVTSNDLLKPEHVA----KAIvddLRLPF---EIEETQVTIGASvgvAVKNGAfDANEAIRQADIALYHAK 449
Cdd:PRK11059 307 RYSRSDFAVLLPHRSLKEADSLAsqllKAV---DALPPpkmLDRDDFLHIGIC---AYRSGQ-STEQVMEEAEMALRSAQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 450 AAGRNTYAIFGEHMDELL-----RKRRAMEADLrkaVNGRaeIEIFYQPVFSaRDGMLCSLEALARWNHPTLGYVSPGEF 524
Cdd:PRK11059 380 LQGGNGWFVYDKAQLPEKgrgsvRWRTLLEQTL---VRGG--PRLYQQPAVT-RDGKVHHRELFCRIRDGQGELLSAELF 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 525 IPLAEECGLIHEIGAIVLEDACSMLAHFPDIDIALNASLLELCSPAYplnviaalEKW---------KVSANRLEIEITE 595
Cdd:PRK11059 454 MPMVQQLGLSEQYDRQVIERVLPLLRYWPEENLSINLSVDSLLSRAF--------QRWlrdtllqcpRSQRKRLIFELAE 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 596 SAATGEDGRSERTIAALRAAGVRFAIDDFGTGYSSFSRVQKIEVDRIKIDRSFIEEIH-RSDNRALVTAMINVARAKGLK 674
Cdd:PRK11059 526 ADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHkRTENQLFVRSLVGACAGTETQ 605
|
410 420 430
....*....|....*....|....*....|.
gi 1424287064 675 ITAEGVETTEQRDALESLGCHHLQGFLLARP 705
Cdd:PRK11059 606 VFATGVESREEWQTLQELGVSGGQGDFFAES 636
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
295-454 |
2.41e-25 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 111.26 E-value: 2.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 295 QEQLQYQAAHDILTGLANRSEFNARVATAAQNAREDEA-HAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTS-LLPD 372
Cdd:PRK15426 391 QSSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQpFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSsLRAQ 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 373 SLVARIGGDEFTVLV---TSNDllkpehvAKAIVDDLRLPFEIEE------TQVTIGASVGVAVK----NGAFDANEAIr 439
Cdd:PRK15426 471 DVAGRVGGEEFCVVLpgaSLAE-------AAQVAERIRLRINEKEilvaksTTIRISASLGVSSAeedgDYDFEQLQSL- 542
|
170
....*....|....*
gi 1424287064 440 qADIALYHAKAAGRN 454
Cdd:PRK15426 543 -ADRRLYLAKQAGRN 556
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
286-454 |
2.45e-24 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 106.91 E-value: 2.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 286 RRSNRLKANQEQLQYQAAHDILTGLANRSEFNARVATAAQNARE-DEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGA 364
Cdd:PRK09581 276 RYQDALRNNLEQSIEMAVTDGLTGLHNRRYFDMHLKNLIERANErGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAK 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 365 RL-TSLLPDSLVARIGGDEFTVLVTSNDLlkpeHVAKAIVDDLRL-----PFEIE--ETQVTIGASVGVAVKNGAFDANE 436
Cdd:PRK09581 356 RLrNNIRGTDLIARYGGEEFVVVMPDTDI----EDAIAVAERIRRkiaeePFIISdgKERLNVTVSIGVAELRPSGDTIE 431
|
170
....*....|....*....
gi 1424287064 437 A-IRQADIALYHAKAAGRN 454
Cdd:PRK09581 432 AlIKRADKALYEAKNTGRN 450
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
290-449 |
2.18e-19 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 91.22 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 290 RLKANQEQLQYQAAHDILTGLANRSEFNARVATAAQNAREDEAHAVLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSL 369
Cdd:PRK09966 236 RLQAKNAQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEF 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 370 LPDSLVA-RIGGDEFT-VLVTSNDLLKPEHVAKAIVDDLRLPFEIEETQ-VTIGASVGVAVKNGAFDANEAIRQADIALY 446
Cdd:PRK09966 316 GGLRHKAyRLGGDEFAmVLYDVQSESEVQQICSALTQIFNLPFDLHNGHqTTMTLSIGYAMTIEHASAEKLQELADHNMY 395
|
...
gi 1424287064 447 HAK 449
Cdd:PRK09966 396 QAK 398
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
305-454 |
2.37e-19 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 89.36 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 305 DILTGLANR----SEF-NARVAtaaqnaREDEAHAVLFIDLDRFKEVNDSLGHPAGDR-LISLVGARLTSLLPDSLVARI 378
Cdd:PRK09894 132 DVLTGLPGRrvldESFdHQLRN------REPQNLYLALLDIDRFKLVNDTYGHLIGDVvLRTLATYLASWTRDYETVYRY 205
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1424287064 379 GGDEFTVLVTSNDLLKPEHVAKAIVDDL-RLPFEIEETQVTIGASVGVAVKNGAFDANEAIRQADIALYHAKAAGRN 454
Cdd:PRK09894 206 GGEEFIICLKAATDEEACRAGERIRQLIaNHAITHSDGRINITATFGVSRAFPEETLDVVIGRADRAMYEGKQTGRN 282
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
290-454 |
1.27e-17 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 85.27 E-value: 1.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 290 RLKANQEQLQYQAAHDILTGLANRSEFNARVATAAQNAREDEAHA-VLFIDLDRFKEVNDSLGHPAGDRLISLVGARL-T 367
Cdd:PRK10245 193 KLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDAtLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLqI 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 368 SLLPDSLVARIGGDEFTVLVTSNdllkPEHVAKAI-------VDDLRLPFeieETQVTIGASVGVAVKNGAFDA-NEAIR 439
Cdd:PRK10245 273 TLRGSDVIGRFGGDEFAVIMSGT----PAESAITAmsrvhegLNTLRLPN---APQVTLRISVGVAPLNPQMSHyREWLK 345
|
170
....*....|....*
gi 1424287064 440 QADIALYHAKAAGRN 454
Cdd:PRK10245 346 SADLALYKAKNAGRN 360
|
|
| CHASE4 |
pfam05228 |
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various ... |
59-221 |
7.21e-16 |
|
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in prokaryotes. Specifically, CHASE4 domains are found in histidine kinases in Archaea and in predicted diguanylate cyclases/phosphodiesterases in Bacteria. Environmental factors that are recognized by CHASE4 domains are not known at this time.
Pssm-ID: 428380 Cd Length: 139 Bit Score: 75.06 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 59 SSIAHDQESATVWDDAVTNSLARNPDWMETNLGVWMNTYFGHDAAIVLTADLDPIYQFLVDHndastadglrtaylplat 138
Cdd:pfam05228 7 DSLDRLLRDWAVWDDTYDFVQDGNPDYIESNLGPETFENLGLDLILFVDADGKLVYDLENGK------------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 139 klkerliaGDQDGTSSKVLSIGEADIVYVGSRPAIVSIKPIvSDTGDIEQQPGrenLHVAVRFLDGDLAATVGqEYQFEN 218
Cdd:pfam05228 69 --------PDSPLLSRSSPDSGLSGIVLLGGGPALVAARPI-LTSDGSGPPRG---TLVMGRYLDEAFLDRLS-ELTLLD 135
|
...
gi 1424287064 219 LRF 221
Cdd:pfam05228 136 LTL 138
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
591-720 |
1.85e-11 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 66.75 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 591 IEITESAATGEDGRseRTIAALRAAGVRFAIDDFgTGYSSFSRVQKIeVDRIKIDrsfieeiHRSDNRALVTAMINVARA 670
Cdd:COG3434 88 LEILEDVEPDEELL--EALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID-------VLALDLEELAELVARLKR 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1424287064 671 KGLKITAEGVETTEQRDALESLGCHHLQGFLLARP-------LSPNAAR-----ALLSTPDP 720
Cdd:COG3434 157 YGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPeilkgkkLPPSQLTllqllNELNKPDA 218
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
335-450 |
4.14e-08 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 52.36 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 335 VLFIDLDRFKEVNDSLGHPAGDRLISLVGARLTSLLPDS--LVARIGGDEFTVLVTSNDLlkpeHVAKAIVDDLRLPFEI 412
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSgdLKIKTIGDEFMVVSGLDHP----AAAVAFAEDMREAVSA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1424287064 413 EETQ------VTIGASVGVAVKNGA-----FDA-NEAIRQADIALYHAKA 450
Cdd:cd07556 80 LNQSegnpvrVRIGIHTGPVVVGVIgsrpqYDVwGALVNLASRMESQAKA 129
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
374-449 |
5.28e-06 |
|
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: 47.60 E-value: 5.28e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1424287064 374 LVARIGGDEFTVLVTSNDLLKPEHVAKAIVDDLRLPFEIeetQVTIgaSVGVAVKNgafdaneAIRQADiALYHAK 449
Cdd:COG3706 117 LVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSL---RVTV--SIGVAGDS-------LLKRAD-ALYQAR 179
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
589-707 |
2.46e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 46.53 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1424287064 589 LEIEITESAATGEDGrserTIAALRAAGvRFAIDDFGTGYSSFSRVQKIEVDRIKIDRS-FIEEIHRSDNRALVTAMINV 667
Cdd:PRK11596 130 LRFELVEHIRLPKDS----PFASMCEFG-PLWLDDFGTGMANFSALSEVRYDYIKVARElFIMLRQSEEGRNLFSQLLHL 204
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1424287064 668 AR--AKGLKItaEGVETTEQ-RDALESLGChHLQGFLLARPLS 707
Cdd:PRK11596 205 MNryCRGVIV--EGVETPEEwRDVQRSPAF-AAQGYFLSRPAP 244
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