|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
27-662 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 1272.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 27 CTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADLPGAETILESIKPAGVVSRADVVLPNQFQALRKRFIPERPV 106
Cdd:PRK13561 16 CTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRADVVLPNQFQALRKSFIPERPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 107 PVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSYRMYKFVMSALSTLVTIYLLLSLILTVAIAWCVNRLIVHPL 186
Cdd:PRK13561 96 PVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSFRMYKFVMSALSTLVTIYLLLSLILTVAISWCINRLIVHPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 187 RKIARELNDIPQQELIGHQLALPRLHQDDEIGMLVRSYNLNQQLMQRQREEQTDNAMRFPVSELPNKAFLMALLEQVITR 266
Cdd:PRK13561 176 RNIARELNDIPPQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 267 QQTTALIIVTCETLRDTAGVLQETQREILLLTLVEKLKSVLAPRMVLTQVSGYDFAIIAHGVKEPWHAITLGQQILTIIN 346
Cdd:PRK13561 256 KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIIN 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 347 ERLPIQGIQLRPSCSIGIAMYYGDLTAEALYGRAVSAAFTARRKGKNQIQFFDPAQMEAAQQRLTEESDILTALDNHQFA 426
Cdd:PRK13561 336 ERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 427 IWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQERGVTLPLSVNLSAL 506
Cdd:PRK13561 416 IWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSAL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 507 QLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHMKSLPVDI 586
Cdd:PRK13561 496 QLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSLPIDV 575
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447189083 587 LKIDKMFVDGLPDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARPVPADIFEERYLSHE 662
Cdd:PRK13561 576 LKIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEERYLEEK 651
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
250-661 |
1.15e-118 |
|
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: 369.49 E-value: 1.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 250 LPNKAFLMALLEQVITR----QQTTALIIVTCE---TLRDTAGvlqetqREI---LLLTLVEKLKSVLAPRMVLTQVSGY 319
Cdd:COG5001 259 LPNRRLFLDRLEQALARarrsGRRLALLFIDLDrfkEINDTLG------HAAgdeLLREVARRLRACLREGDTVARLGGD 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 320 DFAIIAHGVKEPWHAITLGQQILTIINERLPIQGIQLRPSCSIGIAMYYGD-LTAEALYGRAVSAAFTARRKGKNQIQFF 398
Cdd:COG5001 333 EFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDgADAEELLRNADLAMYRAKAAGRNRYRFF 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 399 DPAQMEAAQQRLTEESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYW 478
Cdd:COG5001 413 DPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEW 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 479 VLEESCRQLAAWQERGVT-LPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNA 557
Cdd:COG5001 493 VLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRAL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 558 GVRIALDDFGMGYAGLRQLqhmKSLPVDILKIDKMFVDGL---PDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQ 634
Cdd:COG5001 573 GVRIALDDFGTGYSSLSYL---KRLPVDTLKIDRSFVRDLaedPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRE 649
|
410 420
....*....|....*....|....*..
gi 447189083 635 AGVNVAQGFLFARPVPADIFEERYLSH 661
Cdd:COG5001 650 LGCDYAQGYLFSRPLPAEELEALLRAR 676
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
413-653 |
5.85e-94 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 290.27 E-value: 5.85e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 413 ESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQE 492
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 493 RG-VTLPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYA 571
Cdd:smart00052 81 QGpPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 572 GlrqLQHMKSLPVDILKIDKMFVDGL---PDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARP 648
Cdd:smart00052 161 S---LSYLKRLPVDLLKIDKSFVRDLqtdPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
....*
gi 447189083 649 VPADI 653
Cdd:smart00052 238 LPLDD 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
414-652 |
9.47e-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: 287.13 E-value: 9.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 414 SDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQER 493
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 494 GVTLPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGL 573
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 574 RQLqhmKSLPVDILKIDKMFVDGL---PDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARPVP 650
Cdd:cd01948 161 SYL---KRLPVDYLKIDRSFVRDIetdPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
..
gi 447189083 651 AD 652
Cdd:cd01948 238 AE 239
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
413-648 |
2.66e-71 |
|
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: 231.05 E-value: 2.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 413 ESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQe 492
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 493 RGVTLPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAG 572
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447189083 573 LRQLQHmksLPVDILKIDKMFVDGLPDDHS---MVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARP 648
Cdd:pfam00563 160 LSYLLR---LPPDFVKIDRSLIADIDKDGEaraIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
27-662 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 1272.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 27 CTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADLPGAETILESIKPAGVVSRADVVLPNQFQALRKRFIPERPV 106
Cdd:PRK13561 16 CTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRADVVLPNQFQALRKSFIPERPV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 107 PVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSYRMYKFVMSALSTLVTIYLLLSLILTVAIAWCVNRLIVHPL 186
Cdd:PRK13561 96 PVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSFRMYKFVMSALSTLVTIYLLLSLILTVAISWCINRLIVHPL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 187 RKIARELNDIPQQELIGHQLALPRLHQDDEIGMLVRSYNLNQQLMQRQREEQTDNAMRFPVSELPNKAFLMALLEQVITR 266
Cdd:PRK13561 176 RNIARELNDIPPQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVAR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 267 QQTTALIIVTCETLRDTAGVLQETQREILLLTLVEKLKSVLAPRMVLTQVSGYDFAIIAHGVKEPWHAITLGQQILTIIN 346
Cdd:PRK13561 256 KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIIN 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 347 ERLPIQGIQLRPSCSIGIAMYYGDLTAEALYGRAVSAAFTARRKGKNQIQFFDPAQMEAAQQRLTEESDILTALDNHQFA 426
Cdd:PRK13561 336 ERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFA 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 427 IWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQERGVTLPLSVNLSAL 506
Cdd:PRK13561 416 IWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSAL 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 507 QLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHMKSLPVDI 586
Cdd:PRK13561 496 QLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKSLPIDV 575
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447189083 587 LKIDKMFVDGLPDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARPVPADIFEERYLSHE 662
Cdd:PRK13561 576 LKIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEERYLEEK 651
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
31-660 |
0e+00 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 655.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 31 LFHLVQQNRYNTATQLESIARSVREPLSSAILKADLPGAETILESIKPAGVVSRADVVLPNQFQALRKRFIPERPVPVMV 110
Cdd:PRK11829 20 LFHFVQQRKDDYANQLESIAYSVRQPLSEAILSVDIPQAKKILNSLLPIGILSRAEVILPNQIQVLHANFPTERPIPHWA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 111 TRLFELPVQISLPVYSLER-PANPQPLAYLVLQADSYRMYKFVMSALSTLVTIYLLLSLILTVAIAWCVNRLIVHPLRKI 189
Cdd:PRK11829 100 KRVFSLPVQITVPLYALERvPANPQPLAHLVLRADSFRMYQFILSALSAMLSTYLLLALVLSVSIAWCINRLIIHPLRAM 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 190 ARELNDIPQQELIGHQLALPRLHQDDEIGMLVRSYNLNQQLMQRQREEQTDNAMRFPVSELPNKAFLMALLEQVI---TR 266
Cdd:PRK11829 180 AKELEDIGDHGVLHHQLTLPAHHQDDELGVLVRNYNRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIassTR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 267 QQTTALIIVTCETLRDTAGVLQETQREILLLTLVEKLKSVLAPRMVLTQVSGYDFAIIAHGVKEPWHAITLGQQILTIIN 346
Cdd:PRK11829 260 TDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 347 ERLPIQGIQLRPSCSIGIAMYYGDL-TAEALYGRAVSAAFTARRKGKNQIQFFDPAQMEAAQQRLTEESDILTALDNHQF 425
Cdd:PRK11829 340 QPLFFDEITLRPSASIGITRYQAQQdTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDF 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 426 AIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQERGVTLPLSVNLSA 505
Cdd:PRK11829 420 TLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPLSVNISG 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 506 LQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHMKSLPVD 585
Cdd:PRK11829 500 LQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHLKSLPIH 579
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447189083 586 ILKIDKMFVDGLPDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARPVPADIFEERYLS 660
Cdd:PRK11829 580 MIKLDKSFVKNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAEFEAQYFS 654
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
250-661 |
1.15e-118 |
|
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: 369.49 E-value: 1.15e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 250 LPNKAFLMALLEQVITR----QQTTALIIVTCE---TLRDTAGvlqetqREI---LLLTLVEKLKSVLAPRMVLTQVSGY 319
Cdd:COG5001 259 LPNRRLFLDRLEQALARarrsGRRLALLFIDLDrfkEINDTLG------HAAgdeLLREVARRLRACLREGDTVARLGGD 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 320 DFAIIAHGVKEPWHAITLGQQILTIINERLPIQGIQLRPSCSIGIAMYYGD-LTAEALYGRAVSAAFTARRKGKNQIQFF 398
Cdd:COG5001 333 EFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDgADAEELLRNADLAMYRAKAAGRNRYRFF 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 399 DPAQMEAAQQRLTEESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYW 478
Cdd:COG5001 413 DPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEW 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 479 VLEESCRQLAAWQERGVT-LPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNA 557
Cdd:COG5001 493 VLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRAL 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 558 GVRIALDDFGMGYAGLRQLqhmKSLPVDILKIDKMFVDGL---PDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQ 634
Cdd:COG5001 573 GVRIALDDFGTGYSSLSYL---KRLPVDTLKIDRSFVRDLaedPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRE 649
|
410 420
....*....|....*....|....*..
gi 447189083 635 AGVNVAQGFLFARPVPADIFEERYLSH 661
Cdd:COG5001 650 LGCDYAQGYLFSRPLPAEELEALLRAR 676
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
82-657 |
5.71e-100 |
|
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: 317.50 E-value: 5.71e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 82 VSRADVVLPNQFQALRKRFIPERPVPVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSYRMYKFVMSALSTLVT 161
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 162 IYLLLSLILTVAIAWCVNRLIVHPLRKIARELNDIPQQELIGHQLALPRLHQDDEIGMLVRSYNLNQQLMQRQREEQTDN 241
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 242 AMRFPVSELPNKAFLMALLEQVITRQQTTALIIVTCETLRDTAGVLQEtqREILLLTLVEKLKSVLAPRMVLTQVSGYDF 321
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAG--LLLLLLLALLLLLLLARLLLALLGGGGGGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 322 AIIAHGVKEPWHAITLGQQILTIINERLPIQGIQLRPSCSIGIAMYYGDLTAEALYGRAVSAAFTARRKGKNQIQFFDPA 401
Cdd:COG2200 239 LLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 402 QMEAAQQRLTEESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLE 481
Cdd:COG2200 319 AEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 482 ESCRQLAAWQERGVTLPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRI 561
Cdd:COG2200 399 RALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 562 ALDDFGMGYAGLRQLQHmksLPVDILKIDKMFVDGL---PDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVN 638
Cdd:COG2200 479 ALDDFGTGYSSLSYLKR---LPPDYLKIDRSFVRDIardPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCD 555
|
570
....*....|....*....
gi 447189083 639 VAQGFLFARPVPADIFEER 657
Cdd:COG2200 556 YAQGYLFGRPLPLEELEAL 574
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
413-653 |
5.85e-94 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 290.27 E-value: 5.85e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 413 ESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQE 492
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 493 RG-VTLPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYA 571
Cdd:smart00052 81 QGpPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 572 GlrqLQHMKSLPVDILKIDKMFVDGL---PDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARP 648
Cdd:smart00052 161 S---LSYLKRLPVDLLKIDKSFVRDLqtdPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
....*
gi 447189083 649 VPADI 653
Cdd:smart00052 238 LPLDD 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
414-652 |
9.47e-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: 287.13 E-value: 9.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 414 SDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQER 493
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 494 GVTLPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGL 573
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 574 RQLqhmKSLPVDILKIDKMFVDGL---PDDHSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARPVP 650
Cdd:cd01948 161 SYL---KRLPVDYLKIDRSFVRDIetdPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
..
gi 447189083 651 AD 652
Cdd:cd01948 238 AE 239
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
305-664 |
1.01e-72 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 247.67 E-value: 1.01e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 305 SVLAPRMVLTQVSGYDFAIIA-HGVKEPWHAITlgQQILTIINERLPIQGIQLRPSCSIGIAMY--YGDlTAEALYGRAV 381
Cdd:PRK10060 302 SCLEEDQTLARLGGDEFLVLAsHTSQAALEAMA--SRILTRLRLPFRIGLIEVYTGCSIGIALApeHGD-DSESLIRSAD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 382 SAAFTARRKGKNQIQFFDPaQMeaaQQRLTE----ESDILTALDNHQFAIWLQPQVEMRsGNVLSAEALLRMQQPDGSWE 457
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSP-EM---NQRVFEylwlDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLI 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 458 LPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQERGVTLPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTE 537
Cdd:PRK10060 454 PPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 538 SRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHmksLPVDILKIDKMFVDGL---PDDHSMVTAIILMARSL 614
Cdd:PRK10060 534 SCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLAR---FPIDAIKLDQSFVRDIhkqPVSQSLVRAIVAVAQAL 610
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 447189083 615 NLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARPVPADIFEERYLSHENP 664
Cdd:PRK10060 611 NLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYLKR 660
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
413-648 |
2.66e-71 |
|
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: 231.05 E-value: 2.66e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 413 ESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLAAWQe 492
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 493 RGVTLPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRIALDDFGMGYAG 572
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447189083 573 LRQLQHmksLPVDILKIDKMFVDGLPDDHS---MVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARP 648
Cdd:pfam00563 160 LSYLLR---LPPDFVKIDRSLIADIDKDGEaraIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
407-664 |
1.25e-69 |
|
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: 235.97 E-value: 1.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 407 QQRLTEESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQ 486
Cdd:COG4943 267 RRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRD 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 487 LAAW--QERGVTLplSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTEsRRIDDPHAAVAILRPLRNAGVRIALD 564
Cdd:COG4943 347 LGDLlaADPDFHI--SINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITE-RGFIDPAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 565 DFGMGYAGLRQLQhmkSLPVDILKIDKMFVDGLPDD---HSMVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQ 641
Cdd:COG4943 424 DFGTGYSSLSYLQ---TLPVDILKIDKSFVDAIGTDsanSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQ 500
|
250 260
....*....|....*....|...
gi 447189083 642 GFLFARPVPADIFEERYLSHENP 664
Cdd:COG4943 501 GWLFAKPLPAEEFIAWLAAQRAP 523
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
230-651 |
2.30e-65 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 230.43 E-value: 2.30e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 230 LMQRQREEQTDNAMRF-PVSELPNKAFLMALLEQVITRQQTTALIIVTCETLRDTAGVLQETQREILLLTLVEKLKSVLA 308
Cdd:PRK11359 363 LEQEKSRQHIEQLIQFdPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 309 PRMVLTQVSGYDFAIIAHGVKEpwHAITL-GQQILTIINERLPIQGIQLRPSCSIGIAmYYGDLTAEALYGRAVSAAFTA 387
Cdd:PRK11359 443 PDQYLCRIEGTQFVLVSLENDV--SNITQiADELRNVVSKPIMIDDKPFPLTLSIGIS-YDVGKNRDYLLSTAHNAMDYI 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 388 RRKGKNQIQFFDPAQMEAAQQRLTEESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIE 467
Cdd:PRK11359 520 RKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAE 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 468 SCGLMVTVGYWVLEESCRQLAAWQERGVTLP-LSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTESRRIDDPHA 546
Cdd:PRK11359 600 EIGEIENIGRWVIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTE 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 547 AVAILRPLRNAGVRIALDDFGMGYAGLRQLQhmkSLPVDILKIDKMFVDGLPDD---HSMVTAIILMARSLNLQLIAEGV 623
Cdd:PRK11359 680 IFKRIQILRDMGVGLSVDDFGTGFSGLSRLV---SLPVTEIKIDKSFVDRCLTEkriLALLEAITSIGQSLNLTVVAEGV 756
|
410 420
....*....|....*....|....*...
gi 447189083 624 ENEAQRAWLEQAGVNVAQGFLFARPVPA 651
Cdd:PRK11359 757 ETKEQFEMLRKIHCRVIQGYFFSRPLPA 784
|
|
| GAPES3 |
pfam17154 |
Gammaproteobacterial periplasmic sensor domain; GAPES3 (GAmmaproteobacterial PEriplasmic ... |
36-155 |
7.51e-51 |
|
Gammaproteobacterial periplasmic sensor domain; GAPES3 (GAmmaproteobacterial PEriplasmic Sensor) domain is a periplasmic sensor domain found in diguanylate cyclases/phosphodiesterases, including the c-di-GMP phosphodiesterases PdeK (YhjK) of Escherichia coli and HmsP of Yersinia pestis.
Pssm-ID: 435753 [Multi-domain] Cd Length: 121 Bit Score: 172.23 E-value: 7.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 36 QQNRYNTATQLESIARSVREPLSSAILKADLPGAETILESIKPAGVVSRADVVLPNQFQALRKRFIPERPVPVMVTRLFE 115
Cdd:pfam17154 1 QQRKDDYANQLENIAVSVRAPLTEALLSSDLNEAKSILITLRPSGILGRADVVLPNQIQVLHLNFATERPIPELAKRVFG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 447189083 116 LPVQISLPVYSLER-PANPQPLAYLVLQADSYRMYKFVMSA 155
Cdd:pfam17154 81 LPVEISVPLYSYGVsPTNPQPLAHLVLQADSNRMYRFIIST 121
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
231-654 |
1.39e-36 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 147.51 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 231 MQRQReeqTDNAMRFPVSELPNKAF----LMALLEQVITRQQTTALIIVTCETLR---DTAGvlqETQREILLLTLVEKL 303
Cdd:PRK09776 657 MLRQL---SYSASHDALTHLANRASfekqLRRLLQTVNSTHQRHALVFIDLDRFKavnDSAG---HAAGDALLRELASLM 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 304 KSVLAPRMVLTQVSGYDFAIIAHGVKEPwHAITLGQQILTIINE-RLPIQGIQLRPSCSIGIAMYYGD--LTAEaLYGRA 380
Cdd:PRK09776 731 LSMLRSSDVLARLGGDEFGLLLPDCNVE-SARFIATRIISAINDyHFPWEGRVYRVGASAGITLIDANnhQASE-VMSQA 808
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 381 VSAAFTARRKGKNQIQFFDPAQMEAAQQR--LTEESDILTALDNHQFAIWLQ---PQVEMRSGNVlsaEALLRMQQPDGS 455
Cdd:PRK09776 809 DIACYAAKNAGRGRVTVYEPQQAAAHSEHraLSLAEQWRMIKENQLMMLAHGvasPRIPEARNHW---LISLRLWDPEGE 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 456 WELPEGLIERIESCGLMVTVGYWVLEESCRQLAAwQERGVTLPLSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEV 535
Cdd:PRK09776 886 IIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAK-AVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEI 964
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 536 TESRRIDDPHAAVAILRPLRNAGVRIALDDFGmgyAGLRQLQHMKSLPVDILKIDKMFVDGLPD---DHSMVTAIILMAR 612
Cdd:PRK09776 965 TETALLNHAESASRLVQKLRLAGCRVVLSDFG---RGLSSFNYLKAFMADYLKLDGELVANLHGnlmDEMLISIIQGHAQ 1041
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 447189083 613 SLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARPVPADIF 654
Cdd:PRK09776 1042 RLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
409-654 |
1.57e-28 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 120.10 E-value: 1.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 409 RLTEESDILTALDNHQFAIWLQPQVEMRSGNVLSAEALLRMQQPDGSWELPEGLIERIESCGLMVTVGYWVLEESCRQLA 488
Cdd:PRK10551 261 RMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 489 AWQErgvTLP----LSVNLSALQLMHPGMVSDLLELLNRYRIQPGTLILEVTEsRRIDDPHAAVAILRPLRNAGVRIALD 564
Cdd:PRK10551 341 ELQK---VLPvgakLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITE-RDMVQEEEATKLFAWLHSQGIEIAID 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 565 DFGMGYAGLRQLQHMKslpVDILKIDKMFVDGLPDDhsMVT-----AIILMARSLNLQLIAEGVENEAQRAWLEQAGVNV 639
Cdd:PRK10551 417 DFGTGHSALIYLERFT---LDYLKIDRGFIQAIGTE--TVTspvldAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNF 491
|
250
....*....|....*
gi 447189083 640 AQGFLFARPVPADIF 654
Cdd:PRK10551 492 LQGYWISRPLPLEDF 506
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
242-398 |
8.14e-27 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 106.95 E-value: 8.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 242 AMRFPVSELPNKAFLMALLEQVITR----QQTTALIIVTCETLRDTAGVLQETQREILLLTLVEKLKSVLAPRMVLTQVS 317
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRaqrqGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 318 GYDFAIIAHGVkEPWHAITLGQQILTIINERLPIQGIQLRPSCSIGIAMY-YGDLTAEALYGRAVSAAFTARRKGKNQIQ 396
Cdd:smart00267 83 GDEFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQVA 161
|
..
gi 447189083 397 FF 398
Cdd:smart00267 162 VY 163
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
134-398 |
6.07e-19 |
|
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: 87.34 E-value: 6.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 134 QPLAYLVLQADSYRMYKFVMSALSTLVTIYLLLSLILTVAIAWCVNRLIVHPLRKIARELNDIPQQELIGHQLALPRLHQ 213
Cdd:COG2199 7 LLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 214 DDEIGMLVRSYNLNQQLmQRQREEQTDNAMRFPVSELPNKAFLMALLEQVITR----QQTTALIIVTC---ETLRDTAGV 286
Cdd:COG2199 87 LLALLLLLLALEDITEL-RRLEERLRRLATHDPLTGLPNRRAFEERLERELARarreGRPLALLLIDLdhfKRINDTYGH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 287 LqetQREILLLTLVEKLKSVLAPRMVLTQVSGYDFAIIAHGVKEPwHAITLGQQILTIINE-RLPIQGIQLRPSCSIGIA 365
Cdd:COG2199 166 A---AGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLE-EAEALAERLREALEQlPFELEGKELRVTVSIGVA 241
|
250 260 270
....*....|....*....|....*....|....
gi 447189083 366 MYYGD-LTAEALYGRAVSAAFTARRKGKNQIQFF 398
Cdd:COG2199 242 LYPEDgDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
501-650 |
1.16e-14 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 76.38 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 501 VNLSALQLMhpgmvSDLLELLNryriqPGTLILEVTESRRIDDphAAVAILRPLRNAGVRIALDDFGMGYAGLRQLQHmk 580
Cdd:COG3434 66 INFTEELLL-----SDLPELLP-----PERVVLEILEDVEPDE--ELLEALKELKEKGYRIALDDFVLDPEWDPLLPL-- 131
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 581 slpVDILKIDkmfVDGLPDDHsmVTAIILMARSLNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFARPVP 650
Cdd:COG3434 132 ---ADIIKID---VLALDLEE--LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
278-652 |
7.87e-12 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 68.35 E-value: 7.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 278 ETLRDTAGvlqETQREILLLTLVEKLKSVLA--PRMVLTQVSGYDFAI-IAH-GVKEpwhAITLGQQILTIInERLPIQG 353
Cdd:PRK11059 271 DLLQEEWG---ESQVEELLFELINLLSTFVMryPGALLARYSRSDFAVlLPHrSLKE---ADSLASQLLKAV-DALPPPK 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 354 IQLRPS-CSIGIAMYYGDLTAEALYGRAVSAAFTARRKGKNQIQFFDPAQM-EAAQQRLTEESDILTALDNHQFAIWLQP 431
Cdd:PRK11059 344 MLDRDDfLHIGICAYRSGQSTEQVMEEAEMALRSAQLQGGNGWFVYDKAQLpEKGRGSVRWRTLLEQTLVRGGPRLYQQP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 432 QVEmRSGNVLSAEALLRMQqpDGSWELP--EGLIERIESCGLMVTVGYWVLEESCRQLAAWQERgvtlPLSVNLSALQLM 509
Cdd:PRK11059 424 AVT-RDGKVHHRELFCRIR--DGQGELLsaELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE----NLSINLSVDSLL 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 510 HPGMV----SDLLELLNRYRIQpgtLILEVTES---RRIDdphAAVAILRPLRNAGVRIALDDFGmgyaglRQL---QHM 579
Cdd:PRK11059 497 SRAFQrwlrDTLLQCPRSQRKR---LIFELAEAdvcQHIS---RLRPVLRMLRGLGCRLAVDQAG------LTVvstSYI 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 580 KSLPVDILK--------IDK-----MFVdglpddHSMVTAiilMARSlNLQLIAEGVENEAQRAWLEQAGVNVAQGFLFA 646
Cdd:PRK11059 565 KELNVELIKlhpslvrnIHKrtenqLFV------RSLVGA---CAGT-ETQVFATGVESREEWQTLQELGVSGGQGDFFA 634
|
....*.
gi 447189083 647 RPVPAD 652
Cdd:PRK11059 635 ESQPLD 640
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
246-396 |
9.62e-12 |
|
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: 63.34 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 246 PVSELPNKAFLMALLEQVITR----QQTTALIIVtcetlrD-------------TAG--VLQEtqreillltLVEKLKSV 306
Cdd:cd01949 4 PLTGLPNRRAFEERLERLLARarrsGRPLALLLI------DidhfkqindtyghAAGdeVLKE---------VAERLRSS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 307 LAPRMVLTQVSGYDFAIIAHGVKEPwHAITLGQQILTIINERLPIQGIQLRPSCSIGIAMY-YGDLTAEALYGRAVSAAF 385
Cdd:cd01949 69 LRESDLVARLGGDEFAILLPGTDLE-EAEALAERLREAIEEPFFIDGQEIRVTASIGIATYpEDGEDAEELLRRADEALY 147
|
170
....*....|.
gi 447189083 386 TARRKGKNQIQ 396
Cdd:cd01949 148 RAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
246-394 |
1.31e-08 |
|
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: 54.57 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 246 PVSELPNKAFLMALLEQVI----TRQQTTALIIVTCE---TLRDTAGvLQETqrEILLLTLVEKLKSVLAPRMVLTQVSG 318
Cdd:pfam00990 5 PLTGLPNRRYFEEQLEQELqralREGSPVAVLLIDLDnfkRINDTYG-HSVG--DEVLQEVAQRLSSSLRRSDLVARLGG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447189083 319 YDFAIIAHGVKEPW--HAITLGQQILTIINERLPIQGIQLRPSCSIGIAMYYGD-LTAEALYGRAVSAAFTARRKGKNQ 394
Cdd:pfam00990 82 DEFAILLPETSLEGaqELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDgEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
159-275 |
5.56e-06 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 49.19 E-value: 5.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 159 LVTIYLLLSLILTVAIAWCVNRLIVHPLRKIARELNDIPQQELiGHQLALPRlhqDDEIGMLVRSYN-LNQQLmQRQREE 237
Cdd:COG5000 10 LLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDL-SVRLPVTG---DDEIGELARAFNrMTDQL-KEQREE 84
|
90 100 110
....*....|....*....|....*....|....*...
gi 447189083 238 QTDnamrfpvselpNKAFLMALLEQVitrqqTTALIIV 275
Cdd:COG5000 85 LEE-----------RRRYLETILENL-----PAGVIVL 106
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
145-238 |
2.86e-03 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 40.77 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 145 SYRMYKFVMSALSTLVTIYLLLSLILTVAIAWCVNRLIVHPLRKIARELNDIPQQELIghqlaLPRLHQDDEIGMLVRSY 224
Cdd:COG2972 144 PKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKAMKKVEKGDLV-----RLEVSGNDEIGILARSF 218
|
90
....*....|....*...
gi 447189083 225 NL----NQQLMQRQREEQ 238
Cdd:COG2972 219 NEmverIKELIEEVYELE 236
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
479-656 |
3.86e-03 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 39.60 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 479 VLEESCRQLAAWQERGVT--LPLSVN-----LSALQLMHpgmvsDLLELLNRYriqPgTLILEVTESRRI--DDPHAAVA 549
Cdd:PRK11596 80 VVKEQLDLLAQWADFFVRhgLLASVNidgptLIALRQQP-----AILRLIERL---P-WLRFELVEHIRLpkDSPFASMC 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447189083 550 ILRPLrnagvriALDDFGMGYAGLRQLQHMKslpVDILKIDK-MFV--DGLPDDHSMVTAII-LMARSLNlQLIAEGVEN 625
Cdd:PRK11596 151 EFGPL-------WLDDFGTGMANFSALSEVR---YDYIKVAReLFImlRQSEEGRNLFSQLLhLMNRYCR-GVIVEGVET 219
|
170 180 190
....*....|....*....|....*....|.
gi 447189083 626 EAQRAWLEQAGVNVAQGFLFARPVPADIFEE 656
Cdd:PRK11596 220 PEEWRDVQRSPAFAAQGYFLSRPAPFETLET 250
|
|
| |
