|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
12-667 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 1069.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 12 MATVSGVALVTICIFIVIQLFHFVQQRRDDYAQQLENIAHSVRQPLAEAVLRMDVPEAKKVLNTLLPVGILSRADIVLPN 91
Cdd:PRK13561 1 MAMVAAVVLVFVFIFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRADVVLPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 92 EFQALHANFPPERPVPTLIARLFELPIQISVPLYSLERvPANQQPLAYLVLQADSFRMYQFILSILSTMLSTYLLLALIL 171
Cdd:PRK13561 81 QFQALRKSFIPERPVPVMVTRLFELPVQISLPVYSLER-PANPQPLAYLVLQADSFRMYKFVMSALSTLVTIYLLLSLIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 172 SVAITWCMNRLMVHPLRAMAKELENISQDEAPYHQLMLPALHQDDELGLLVRNYNRNQQTLAKAHADMSRLSTRHPVTEL 251
Cdd:PRK13561 160 TVAISWCINRLIVHPLRNIARELNDIPPQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 252 PNPALLNALLEQHIAsslRPERFNLLVIGIETLHEASGVMSPAMREALLLALAKKLRGCIDENGVLAQLSNTEFAILAKG 331
Cdd:PRK13561 240 PNKALLMALLEQVVA---RKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 332 TERPFHAMQLARRIMAEINAPLTLEGLALRPNASIGIAHYLNqGESAEQLLRSATSAMMSAHREGKNQILFFEPSLTERT 411
Cdd:PRK13561 317 VKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYG-DLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 412 QKRLTQESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRI 491
Cdd:PRK13561 396 QKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 492 LADWQQRGIELPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDF 571
Cdd:PRK13561 476 LAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 572 GMGYSSLEYLNRLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEVLALPVMAEGVENAEQRDWLLKHGIRSGQGFLFA 651
Cdd:PRK13561 556 GMGYAGLRQLQHMKSLPIDVLKIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFA 635
|
650
....*....|....*.
gi 742394920 652 RPLPREAFEAEFCRAA 667
Cdd:PRK13561 636 RALPIEIFEERYLEEK 651
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
1-668 |
9.39e-135 |
|
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: 411.09 E-value: 9.39e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 1 MRVRRSLTIKQMATVSGVALVTICIFIVIQLFHFVQQRRDDYAQQLENIAHSVRQPLAEAVLRMDVPEAKKVLNTLLPVG 80
Cdd:COG5001 7 LLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 81 ILSRADIVLPNEFQALHANFPPERPVPTLIARLFELPIQISVPLYSLERVPANQQPLAYLVLQADSFRMYQFILSILSTM 160
Cdd:COG5001 87 AALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 161 LSTYLLLALILSVAITWCMNRLMVHPLRAMAKELENISQDEAPYHQLMLPALHQDDELGLLVRNYNRNQQT--LAKAHAD 238
Cdd:COG5001 167 LLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLIteRKRAEER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 239 MSRLSTRHPVTELPNPALLNALLEQHIASSLRP-ERFNLLVIGI-------ETL-HEAsG------VmspAMRealllal 303
Cdd:COG5001 247 LRHLAYHDPLTGLPNRRLFLDRLEQALARARRSgRRLALLFIDLdrfkeinDTLgHAA-GdellreV---ARR------- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 304 akkLRGCIDENGVLAQLSNTEFAILAKGTERPFHAMQLARRIMAEINAPLTLEGLALRPNASIGIAHYLNQGESAEQLLR 383
Cdd:COG5001 316 ---LRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 384 SATSAMMSAHREGKNQILFFEPSLTERTQKRLTQESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTL 463
Cdd:COG5001 393 NADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 464 PADVIPLAEELGVIVPLGNWVLEESCRILADWQQRGIE-LPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITE 542
Cdd:COG5001 473 PAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITE 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 543 TVRIDDLDRALALLRELHDLGLSIALDDFGMGYSSLEYlnrLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEV---L 619
Cdd:COG5001 553 SALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSY---LKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALahsL 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 742394920 620 ALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARPLPREAFEAEFCRAAP 668
Cdd:COG5001 630 GLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
419-658 |
2.68e-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: 288.29 E-value: 2.68e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 419 SEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRILADWQQR 498
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 499 GIELPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDFGMGYSSL 578
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 579 EYlnrLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEV---LALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARPLP 655
Cdd:cd01948 161 SY---LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALahsLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 742394920 656 REA 658
Cdd:cd01948 238 AEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
418-658 |
1.56e-82 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 260.61 E-value: 1.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 418 ESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRILADWQQ 497
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 498 RGIE-LPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDFGMGYS 576
Cdd:smart00052 81 QGPPpLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 577 SLEYlnrLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEV---LALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARP 653
Cdd:smart00052 161 SLSY---LKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELaqkLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
....*
gi 742394920 654 LPREA 658
Cdd:smart00052 238 LPLDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
418-653 |
1.87e-68 |
|
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: 223.35 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 418 ESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRILADWQQ 497
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 498 rGIELPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDFGMGYSS 577
Cdd:pfam00563 81 -GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742394920 578 LEYLNRlksLPIDLIKIDRSFIQGLPADDAMVRIVSSISEV---LALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARP 653
Cdd:pfam00563 160 LSYLLR---LPPDFVKIDRSLIADIDKDGEARAIVRALIALahsLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
324-400 |
3.58e-08 |
|
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: 53.49 E-value: 3.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742394920 324 EFAILAKGTERPfHAMQLARRIMAEINA-PLTLEGLA-LRPNASIGIAHYLNQGESAEQLLRSATSAMMSAHREGKNQI 400
Cdd:TIGR00254 84 EFVVILPGTPLE-DALSKAERLRDAINSkPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
12-667 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 1069.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 12 MATVSGVALVTICIFIVIQLFHFVQQRRDDYAQQLENIAHSVRQPLAEAVLRMDVPEAKKVLNTLLPVGILSRADIVLPN 91
Cdd:PRK13561 1 MAMVAAVVLVFVFIFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRADVVLPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 92 EFQALHANFPPERPVPTLIARLFELPIQISVPLYSLERvPANQQPLAYLVLQADSFRMYQFILSILSTMLSTYLLLALIL 171
Cdd:PRK13561 81 QFQALRKSFIPERPVPVMVTRLFELPVQISLPVYSLER-PANPQPLAYLVLQADSFRMYKFVMSALSTLVTIYLLLSLIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 172 SVAITWCMNRLMVHPLRAMAKELENISQDEAPYHQLMLPALHQDDELGLLVRNYNRNQQTLAKAHADMSRLSTRHPVTEL 251
Cdd:PRK13561 160 TVAISWCINRLIVHPLRNIARELNDIPPQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 252 PNPALLNALLEQHIAsslRPERFNLLVIGIETLHEASGVMSPAMREALLLALAKKLRGCIDENGVLAQLSNTEFAILAKG 331
Cdd:PRK13561 240 PNKALLMALLEQVVA---RKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 332 TERPFHAMQLARRIMAEINAPLTLEGLALRPNASIGIAHYLNqGESAEQLLRSATSAMMSAHREGKNQILFFEPSLTERT 411
Cdd:PRK13561 317 VKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYG-DLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 412 QKRLTQESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRI 491
Cdd:PRK13561 396 QKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRL 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 492 LADWQQRGIELPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDF 571
Cdd:PRK13561 476 LAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDF 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 572 GMGYSSLEYLNRLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEVLALPVMAEGVENAEQRDWLLKHGIRSGQGFLFA 651
Cdd:PRK13561 556 GMGYAGLRQLQHMKSLPIDVLKIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFA 635
|
650
....*....|....*.
gi 742394920 652 RPLPREAFEAEFCRAA 667
Cdd:PRK13561 636 RALPIEIFEERYLEEK 651
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
12-667 |
0e+00 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 923.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 12 MATVSGVALVTICIFIVIQLFHFVQQRRDDYAQQLENIAHSVRQPLAEAVLRMDVPEAKKVLNTLLPVGILSRADIVLPN 91
Cdd:PRK11829 1 MAAVAVVALVTICIFIILQLFHFVQQRKDDYANQLESIAYSVRQPLSEAILSVDIPQAKKILNSLLPIGILSRAEVILPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 92 EFQALHANFPPERPVPTLIARLFELPIQISVPLYSLERVPANQQPLAYLVLQADSFRMYQFILSILSTMLSTYLLLALIL 171
Cdd:PRK11829 81 QIQVLHANFPTERPIPHWAKRVFSLPVQITVPLYALERVPANPQPLAHLVLRADSFRMYQFILSALSAMLSTYLLLALVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 172 SVAITWCMNRLMVHPLRAMAKELENISQDEAPYHQLMLPALHQDDELGLLVRNYNRNQQTLAKAHADMSRLSTRHPVTEL 251
Cdd:PRK11829 161 SVSIAWCINRLIIHPLRAMAKELEDIGDHGVLHHQLTLPAHHQDDELGVLVRNYNRNQQLLADAYADMGRISHRFPVTEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 252 PNPALLNALLEQHIASSLRPERFNLLVIGIETLHEASGVMSPAMREALLLALAKKLRGCIDENGVLAQLSNTEFAILAKG 331
Cdd:PRK11829 241 PNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 332 TERPFHAMQLARRIMAEINAPLTLEGLALRPNASIGIAHYLNQGESAEQLLRSATSAMMSAHREGKNQILFFEPSLTERT 411
Cdd:PRK11829 321 TRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEKT 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 412 QKRLTQESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRI 491
Cdd:PRK11829 401 HKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 492 LADWQQRGIELPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDF 571
Cdd:PRK11829 481 LADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDF 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 572 GMGYSSLEYLNRLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEVLALPVMAEGVENAEQRDWLLKHGIRSGQGFLFA 651
Cdd:PRK11829 561 GIGYSSLRYLNHLKSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFS 640
|
650
....*....|....*.
gi 742394920 652 RPLPREAFEAEFCRAA 667
Cdd:PRK11829 641 PPLPRAEFEAQYFSSA 656
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
1-668 |
9.39e-135 |
|
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: 411.09 E-value: 9.39e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 1 MRVRRSLTIKQMATVSGVALVTICIFIVIQLFHFVQQRRDDYAQQLENIAHSVRQPLAEAVLRMDVPEAKKVLNTLLPVG 80
Cdd:COG5001 7 LLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 81 ILSRADIVLPNEFQALHANFPPERPVPTLIARLFELPIQISVPLYSLERVPANQQPLAYLVLQADSFRMYQFILSILSTM 160
Cdd:COG5001 87 AALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 161 LSTYLLLALILSVAITWCMNRLMVHPLRAMAKELENISQDEAPYHQLMLPALHQDDELGLLVRNYNRNQQT--LAKAHAD 238
Cdd:COG5001 167 LLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLIteRKRAEER 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 239 MSRLSTRHPVTELPNPALLNALLEQHIASSLRP-ERFNLLVIGI-------ETL-HEAsG------VmspAMRealllal 303
Cdd:COG5001 247 LRHLAYHDPLTGLPNRRLFLDRLEQALARARRSgRRLALLFIDLdrfkeinDTLgHAA-GdellreV---ARR------- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 304 akkLRGCIDENGVLAQLSNTEFAILAKGTERPFHAMQLARRIMAEINAPLTLEGLALRPNASIGIAHYLNQGESAEQLLR 383
Cdd:COG5001 316 ---LRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 384 SATSAMMSAHREGKNQILFFEPSLTERTQKRLTQESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTL 463
Cdd:COG5001 393 NADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVS 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 464 PADVIPLAEELGVIVPLGNWVLEESCRILADWQQRGIE-LPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITE 542
Cdd:COG5001 473 PAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITE 552
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 543 TVRIDDLDRALALLRELHDLGLSIALDDFGMGYSSLEYlnrLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEV---L 619
Cdd:COG5001 553 SALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSY---LKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALahsL 629
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 742394920 620 ALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARPLPREAFEAEFCRAAP 668
Cdd:COG5001 630 GLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARAA 678
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
419-658 |
2.68e-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: 288.29 E-value: 2.68e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 419 SEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRILADWQQR 498
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 499 GIELPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDFGMGYSSL 578
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 579 EYlnrLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEV---LALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARPLP 655
Cdd:cd01948 161 SY---LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALahsLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 742394920 656 REA 658
Cdd:cd01948 238 AEE 240
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
109-661 |
3.23e-92 |
|
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: 297.47 E-value: 3.23e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 109 LIARLFELPIQISVPLYSLERVPANQQPLAYLVLQADSFRMYQFILSILSTMLSTYLLLALILSVAITWCMNRLMVHPLR 188
Cdd:COG2200 27 LLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 189 AMAKELENISQDEAPYHQLMLPALHQDDELGLLVRNYNRNQQtlaKAHADMSRLSTRHPVTELPNPALLNALLEQHIASS 268
Cdd:COG2200 107 LAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALL---LLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 269 LRPERFNLLVIGIETLHEASGVMspAMREALLLALAKKLRGCIDENGVLAQLSNTEFAILAKGTERPFHAMQLARRIMAE 348
Cdd:COG2200 184 LLALLLLLLLLLLLLLDNDGLGG--AGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 349 INAPLTLEGLALRPNASIGIAHYLNQGESAEQLLRSATSAMMSAHREGKNQILFFEPSLtERTQKRLTQESEILHGIEQR 428
Cdd:COG2200 262 LLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE-ARARRRLALESELREALEEG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 429 HFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRILADWQQRGIELPLAVNV 508
Cdd:COG2200 341 ELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLRLSVNL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 509 SGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDFGMGYSSLEYlnrLKSLP 588
Cdd:COG2200 421 SARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSY---LKRLP 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742394920 589 IDLIKIDRSFIQGL---PADDAMVRIVSSISEVLALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARPLPREAFEA 661
Cdd:COG2200 498 PDYLKIDRSFVRDIardPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEA 573
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
308-661 |
5.98e-87 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 285.81 E-value: 5.98e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 308 RGCIDENGVLAQLSNTEFAILAKGTERP-FHAMqlARRIMAEINAPLTLEGLALRPNASIGIAHYLNQGESAEQLLRSAT 386
Cdd:PRK10060 301 LSCLEEDQTLARLGGDEFLVLASHTSQAaLEAM--ASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 387 SAMMSAHREGKNQILFFEPSLTERTQKRLTQESEILHGIEQRHFTLFLQPQIDMqSNEVIGAEALLRWQQYDGSYTLPAD 466
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 467 VIPLAEELGVIVPLGNWVLEESCRILADWQQRGIELPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRI 546
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLI 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 547 DDLDRALALLRELHDLGLSIALDDFGMGYSSLEYLNRlksLPIDLIKIDRSFIQGL---PADDAMVRIVSSISEVLALPV 623
Cdd:PRK10060 538 ENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLAR---FPIDAIKLDQSFVRDIhkqPVSQSLVRAIVAVAQALNLQV 614
|
330 340 350
....*....|....*....|....*....|....*...
gi 742394920 624 MAEGVENAEQRDWLLKHGIRSGQGFLFARPLPREAFEA 661
Cdd:PRK10060 615 IAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFER 652
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
418-658 |
1.56e-82 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 260.61 E-value: 1.56e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 418 ESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRILADWQQ 497
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 498 RGIE-LPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDFGMGYS 576
Cdd:smart00052 81 QGPPpLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 577 SLEYlnrLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEV---LALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARP 653
Cdd:smart00052 161 SLSY---LKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELaqkLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
....*
gi 742394920 654 LPREA 658
Cdd:smart00052 238 LPLDD 242
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
410-661 |
3.11e-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: 234.81 E-value: 3.11e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 410 RTQKRLTQESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESC 489
Cdd:COG4943 265 LLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 490 RILADWQQRGIELPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIdDLDRALALLRELHDLGLSIALD 569
Cdd:COG4943 345 RDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 570 DFGMGYSSLEYlnrLKSLPIDLIKIDRSFIQGLPADDAMVRIVSSISEV---LALPVMAEGVENAEQRDWLLKHGIRSGQ 646
Cdd:COG4943 424 DFGTGYSSLSY---LQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMaktLNLDVVAEGVETEEQADYLRARGVQYGQ 500
|
250
....*....|....*
gi 742394920 647 GFLFARPLPREAFEA 661
Cdd:COG4943 501 GWLFAKPLPAEEFIA 515
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
418-653 |
1.87e-68 |
|
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: 223.35 E-value: 1.87e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 418 ESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVIVPLGNWVLEESCRILADWQQ 497
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 498 rGIELPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDFGMGYSS 577
Cdd:pfam00563 81 -GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742394920 578 LEYLNRlksLPIDLIKIDRSFIQGLPADDAMVRIVSSISEV---LALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARP 653
Cdd:pfam00563 160 LSYLLR---LPPDFVKIDRSLIADIDKDGEARAIVRALIALahsLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GAPES3 |
pfam17154 |
Gammaproteobacterial periplasmic sensor domain; GAPES3 (GAmmaproteobacterial PEriplasmic ... |
36-156 |
1.01e-63 |
|
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: 206.51 E-value: 1.01e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 36 QQRRDDYAQQLENIAHSVRQPLAEAVLRMDVPEAKKVLNTLLPVGILSRADIVLPNEFQALHANFPPERPVPTLIARLFE 115
Cdd:pfam17154 1 QQRKDDYANQLENIAVSVRAPLTEALLSSDLNEAKSILITLRPSGILGRADVVLPNQIQVLHLNFATERPIPELAKRVFG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 742394920 116 LPIQISVPLYSLERVPANQQPLAYLVLQADSFRMYQFILSI 156
Cdd:pfam17154 81 LPVEISVPLYSYGVSPTNPQPLAHLVLQADSNRMYRFIIST 121
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
239-657 |
1.80e-63 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 225.03 E-value: 1.80e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 239 MSRLSTRHPVTELPNpallNALLEQHIASSLRPER-FNLLVIGIETLHEASGVMSPAMREALLLALAKKLRGCIDENGVL 317
Cdd:PRK11359 372 IEQLIQFDPLTGLPN----RNNLHNYLDDLVDKAVsPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYL 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 318 AQLSNTEFAILAKGTERPfHAMQLARRIMAEINAPLTLEGLALRPNASIGIAHylNQGESAEQLLRSATSAMMSAHREGK 397
Cdd:PRK11359 448 CRIEGTQFVLVSLENDVS-NITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIRKNGG 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 398 NQILFFEPSLTERTQKRLTQESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSYTLPADVIPLAEELGVI 477
Cdd:PRK11359 525 NGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEI 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 478 VPLGNWVLEESCRILADWQQRGIELP-LAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDRALALL 556
Cdd:PRK11359 605 ENIGRWVIAEACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRI 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 557 RELHDLGLSIALDDFGMGYSSleyLNRLKSLPIDLIKIDRSFIQGLPADD---AMVRIVSSISEVLALPVMAEGVENAEQ 633
Cdd:PRK11359 685 QILRDMGVGLSVDDFGTGFSG---LSRLVSLPVTEIKIDKSFVDRCLTEKrilALLEAITSIGQSLNLTVVAEGVETKEQ 761
|
410 420
....*....|....*....|....
gi 742394920 634 RDWLLKHGIRSGQGFLFARPLPRE 657
Cdd:PRK11359 762 FEMLRKIHCRVIQGYFFSRPLPAE 785
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
414-668 |
5.92e-38 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 148.22 E-value: 5.92e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 414 RLTQESEILHGIEQRHFTLFLQPQIDMQSNEVIGAEALLRWQQYDGSyTLPADV-IPLAEELGVIVPLGNWVLEescRIL 492
Cdd:PRK10551 261 RMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAG-EIPPDAfINYAEAQKLIVPLTQHLFE---LIA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 493 ADWQQRGIELP----LAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDLDrALALLRELHDLGLSIAL 568
Cdd:PRK10551 337 RDAAELQKVLPvgakLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEE-ATKLFAWLHSQGIEIAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 569 DDFGMGYSSLEYLNRLKslpIDLIKIDRSFIQGL-------PADDAmvriVSSISEVLALPVMAEGVENAEQRDWLLKHG 641
Cdd:PRK10551 416 DDFGTGHSALIYLERFT---LDYLKIDRGFIQAIgtetvtsPVLDA----VLTLAKRLNMLTVAEGVETPEQARWLRERG 488
|
250 260
....*....|....*....|....*..
gi 742394920 642 IRSGQGFLFARPLPREAFeAEFCRAAP 668
Cdd:PRK10551 489 VNFLQGYWISRPLPLEDF-VRWLKEPY 514
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
316-659 |
2.04e-31 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 131.33 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 316 VLAQLSNTEFAILAKGTERPfHAMQLARRIMAEINA-PLTLEGLALRPNASIGIAHYLNQGESAEQLLRSATSAMMSAHR 394
Cdd:PRK09776 739 VLARLGGDEFGLLLPDCNVE-SARFIATRIISAINDyHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKN 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 395 EGKNQILFFEPSLTE-RTQKRLTQESEILHGI-EQRHFTLFLQ--PQIDMQSNEVIgaEALLRWQQYDGSYTLPADVIPL 470
Cdd:PRK09776 818 AGRGRVTVYEPQQAAaHSEHRALSLAEQWRMIkENQLMMLAHGvaSPRIPEARNHW--LISLRLWDPEGEIIDEGAFRPA 895
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 471 AEELGVIVPLGNWVLEESCRILAD-WQQRGieLPLAVNVSGIQMQDEAFVPHLKNLLAQYRIDPRKLLLEITETVRIDDL 549
Cdd:PRK09776 896 AEDPALMHALDRRVIHEFFRQAAKaVASKG--LSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHA 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 550 DRALALLRELHDLGLSIALDDFGMGYSSLEYlnrLKSLPIDLIKIDRSFIQGL---PADDAMVRIVSSISEVLALPVMAE 626
Cdd:PRK09776 974 ESASRLVQKLRLAGCRVVLSDFGRGLSSFNY---LKAFMADYLKLDGELVANLhgnLMDEMLISIIQGHAQRLGMKTIAG 1050
|
330 340 350
....*....|....*....|....*....|...
gi 742394920 627 GVENAEQRDWLLKHGIRSGQGFLFARPLPREAF 659
Cdd:PRK09776 1051 PVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
132-403 |
1.82e-24 |
|
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: 103.52 E-value: 1.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 132 ANQQPLAYLVLQADSFRMYQFILSILSTMLSTYLLLALILSVAITWCMNRLMVHPLRAMAKELENISQDEAPYHQLMLPA 211
Cdd:COG2199 4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 212 LHQDDELGLLVRnYNRNQQTLAKAHADMSRLSTRHPVTELPNPALLNALLEQHIASSLRPER-FNLLVIGI--------- 281
Cdd:COG2199 84 LLLLLALLLLLL-ALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRpLALLLIDLdhfkrindt 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 282 -------ETLHEASGVMspamrealllalakklRGCIDENGVLAQLSNTEFAILAKGTERPfHAMQLARRIMAEINA-PL 353
Cdd:COG2199 163 yghaagdEVLKEVARRL----------------RASLRESDLVARLGGDEFAVLLPGTDLE-EAEALAERLREALEQlPF 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 742394920 354 TLEGLALRPNASIGIAHYLNQGESAEQLLRSATSAMMSAHREGKNQILFF 403
Cdd:COG2199 226 ELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
247-400 |
3.02e-19 |
|
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: 84.92 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 247 PVTELPNPALLNALLEQHIASSLRPER-FNLLVIGI----------------ETLHEASGVMspamrealllalakklRG 309
Cdd:cd01949 4 PLTGLPNRRAFEERLERLLARARRSGRpLALLLIDIdhfkqindtyghaagdEVLKEVAERL----------------RS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 310 CIDENGVLAQLSNTEFAILAKGTERPfHAMQLARRIMAEINAPLTLEGLALRPNASIGIAHYLNQGESAEQLLRSATSAM 389
Cdd:cd01949 68 SLRESDLVARLGGDEFAILLPGTDLE-EAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEAL 146
|
170
....*....|.
gi 742394920 390 MSAHREGKNQI 400
Cdd:cd01949 147 YRAKRSGRNRV 157
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
241-403 |
3.27e-18 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 82.30 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 241 RLSTRHPVTELPNPALLNALLEQHIASSLR-PERFNLLVI----------------GIETLHEASGVMSPAMREalllal 303
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRqGSPFALLLIdldnfkdindtyghavGDELLQEVAQRLSSCLRP------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 304 akklrgcideNGVLAQLSNTEFAILAKGTErPFHAMQLARRIMAEINAPLTLEGLALRPNASIGIAHYLNQGESAEQLLR 383
Cdd:smart00267 75 ----------GDLLARLGGDEFALLLPETS-LEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLK 143
|
170 180
....*....|....*....|
gi 742394920 384 SATSAMMSAHREGKNQILFF 403
Cdd:smart00267 144 RADTALYQAKKAGRNQVAVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
247-399 |
8.70e-15 |
|
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: 72.29 E-value: 8.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 247 PVTELPNPALLNALLEQHIASSLR-PERFNLLVIGI----------------ETLHEASGVMSPAMREalllalakklrg 309
Cdd:pfam00990 5 PLTGLPNRRYFEEQLEQELQRALReGSPVAVLLIDLdnfkrindtyghsvgdEVLQEVAQRLSSSLRR------------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 310 cideNGVLAQLSNTEFAILAKGTERPF--HAMQLARRIMAEINAPLTLEGLALRPNASIGIAHYLNQGESAEQLLRSATS 387
Cdd:pfam00990 73 ----SDLVARLGGDEFAILLPETSLEGaqELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADT 148
|
170
....*....|..
gi 742394920 388 AMMSAHREGKNQ 399
Cdd:pfam00990 149 ALYQAKQAGRNR 160
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
517-653 |
1.85e-12 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 69.45 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 517 AFVPHLKNLLAQ---YRIDPRKLLLEITETVRIDDldRALALLRELHDLGLSIALDDFGMGYSSLEYLNRlkslpIDLIK 593
Cdd:COG3434 64 AFINFTEELLLSdlpELLPPERVVLEILEDVEPDE--ELLEALKELKEKGYRIALDDFVLDPEWDPLLPL-----ADIIK 136
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 594 IDrsfIQGLPADDaMVRIVSSISEvLALPVMAEGVENAEQRDWLLKHGIRSGQGFLFARP 653
Cdd:COG3434 137 ID---VLALDLEE-LAELVARLKR-YGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
366-655 |
1.19e-11 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 67.97 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 366 IGIAHYlNQGESAEQLLRSATSAMMSAHREGKNQILFFE-PSLTERTQKRLTQESEILHGIEQRHFTLFLQPQIDMQSN- 443
Cdd:PRK11059 353 IGICAY-RSGQSTEQVMEEAEMALRSAQLQGGNGWFVYDkAQLPEKGRGSVRWRTLLEQTLVRGGPRLYQQPAVTRDGKv 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 444 ---EVI-----GAEALLRWQQYdgsytlpadvIPLAEELGVIVPLGNWVLEESCRILADWQqrgiELPLAVNVSGIQMQD 515
Cdd:PRK11059 432 hhrELFcrirdGQGELLSAELF----------MPMVQQLGLSEQYDRQVIERVLPLLRYWP----EENLSINLSVDSLLS 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 516 EAFVPHLKNLLAQY-RIDPRKLLLEITETVRIDDLDRALALLRELHDLGLSIALDDFGMGYSSLEYLnrlKSLPIDLIKI 594
Cdd:PRK11059 498 RAFQRWLRDTLLQCpRSQRKRLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYI---KELNVELIKL 574
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 742394920 595 DRSfiqglpaddaMVR----------IVSSISEVLA---LPVMAEGVENAEQRDWLLKHGIRSGQGFLFARPLP 655
Cdd:PRK11059 575 HPS----------LVRnihkrtenqlFVRSLVGACAgteTQVFATGVESREEWQTLQELGVSGGQGDFFAESQP 638
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
324-400 |
3.58e-08 |
|
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: 53.49 E-value: 3.58e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742394920 324 EFAILAKGTERPfHAMQLARRIMAEINA-PLTLEGLA-LRPNASIGIAHYLNQGESAEQLLRSATSAMMSAHREGKNQI 400
Cdd:TIGR00254 84 EFVVILPGTPLE-DALSKAERLRDAINSkPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
338-400 |
2.47e-04 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 44.12 E-value: 2.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742394920 338 AMQLARRIMAEI-NAPLTLEGLALRPN--ASIGIAHYLNQGESAEQLLRSATSAMMSAHREGKNQI 400
Cdd:PRK09581 387 AIAVAERIRRKIaEEPFIISDGKERLNvtVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
484-661 |
7.98e-04 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 41.53 E-value: 7.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 484 VLEESCRILADWQQRGIE--LPLAVNVSG---IQMQDEafvPHLKNLLAQYridPRkLLLEITETVRIDdLDRALALLRE 558
Cdd:PRK11596 80 VVKEQLDLLAQWADFFVRhgLLASVNIDGptlIALRQQ---PAILRLIERL---PW-LRFELVEHIRLP-KDSPFASMCE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 559 LHDLGLsialDDFGMGYSSLEYLNRLKslpIDLIKIDRS-FI------QGLPADDAMVRIVSSISEvlalPVMAEGVENA 631
Cdd:PRK11596 152 FGPLWL----DDFGTGMANFSALSEVR---YDYIKVARElFImlrqseEGRNLFSQLLHLMNRYCR----GVIVEGVETP 220
|
170 180 190
....*....|....*....|....*....|....
gi 742394920 632 EqrDWLLKHgiRSG----QGFLFARPLPREAFEA 661
Cdd:PRK11596 221 E--EWRDVQ--RSPafaaQGYFLSRPAPFETLET 250
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
153-242 |
1.33e-03 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 41.49 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742394920 153 ILSILSTMLSTYLLLALILSVAITWCMNRLMVHPLRAMAKELENISQDEapYHQLMlpALHQDDELGLLVRNYNRNQQTL 232
Cdd:COG5000 3 LQILFLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGD--LSVRL--PVTGDDEIGELARAFNRMTDQL 78
|
90
....*....|
gi 742394920 233 AKAHADMSRL 242
Cdd:COG5000 79 KEQREELEER 88
|
|
| |
