|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
55-672 |
0e+00 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 584.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 55 LIIIAISVFRIITSRRYLLNKTNLPAHLYSHVFLTFVTGTLWGYVAYMQMYTNDDVLRNLIFLINFGLIAASIATLSAWV 134
Cdd:COG5001 54 LLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAAS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 135 YAYLAYMFPQSLAIFYVFLKLDNEYSLQMAGAFVIFTGVMIITSIRYSYRIKKEAELIHDLNNEIGMREEAQLQLQNSKQ 214
Cdd:COG5001 134 AALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 215 GLEDKVNERTKELVDMNSHLESVIDKKEQAEKSLHYLAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRF 294
Cdd:COG5001 214 LGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 295 KTINDSLGHTIGDILIKKASARLHKILRSRDTLARNGGDEFVIVLDRMENTDDAIHVAKKVINSLTETFEIQAHKIHIGA 374
Cdd:COG5001 294 KEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 375 SVGISIYPTDGKTSSILIRNADTAMYKAKKSGGNQLQFYNESMSNQLRDRLVLENELHSALEKDEFYLMYQPQVNCLTGE 454
Cdd:COG5001 374 SIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGR 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 455 TTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRT---QPANHVTYSINLSVLQFNNYKFIDFVR 531
Cdd:COG5001 454 IVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAwqdAGLPDLRVAVNLSARQLRDPDLVDRVR 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 532 NEIDKAGIDPAQIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSMSYLARLPIDVIKIDKSLVRNINEHK 611
Cdd:COG5001 534 RALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDP 613
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490347179 612 NLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKPIMPDDIDHWLS 672
Cdd:COG5001 614 DDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLR 674
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
238-671 |
7.80e-109 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 343.97 E-value: 7.80e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 238 IDKKEQAEKSLHYLAYHDELTGLPNKNLLVDRINQSIktSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARL 317
Cdd:PRK10060 223 ITEERRAQERLRILANTDSITGLPNRNAIQELIDHAI--NAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 318 HKILRSRDTLARNGGDEFvIVLdrMENTDDAI--HVAKKVINSLTETFEIQAHKIHIGASVGISIYPTDGKTSSILIRNA 395
Cdd:PRK10060 301 LSCLEEDQTLARLGGDEF-LVL--ASHTSQAAleAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 396 DTAMYKAKKSGGNQLQFYNESMSNQLRDRLVLENELHSALEKDEFYLMYQPQVNcLTGETTGFEILLRWSNTTYGEIGPD 475
Cdd:PRK10060 378 DTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKIT-WRGEVRSLEALVRWQSPERGLIPPL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 476 RFVPLLEETGLIYATGDWV----VTQVIDFiRTQPANhVTYSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITES 551
Cdd:PRK10060 457 EFISYAEESGLIVPLGRWVmldvVRQVAKW-RDKGIN-LRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTES 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 552 LLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSMSYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTN 631
Cdd:PRK10060 535 CLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQV 614
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1490347179 632 IFEGVETKEELAVIQSMKGNIIQGYLFSKPIMPDDIDHWL 671
Cdd:PRK10060 615 IAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWY 654
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
429-666 |
2.80e-94 |
|
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: 291.37 E-value: 2.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 429 NELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRT--QP 506
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARwqAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 507 ANHVTYSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSM 586
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 587 SYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKPIMPDD 666
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
428-667 |
6.33e-85 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 267.16 E-value: 6.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 428 ENELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRTQPA 507
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 508 NHVTY---SINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYT 584
Cdd:smart00052 81 QGPPPlliSINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 585 SMSYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKPiMP 664
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP-LP 239
|
...
gi 1490347179 665 DDI 667
Cdd:smart00052 240 LDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
428-661 |
4.17e-78 |
|
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: 249.16 E-value: 4.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 428 ENELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRTQPA 507
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 508 NHVT-YSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSM 586
Cdd:pfam00563 81 GPDIkLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490347179 587 SYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKP 661
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
251-408 |
1.16e-40 |
|
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: 145.94 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 251 LAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDTLARN 330
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 331 GGDEFVIVLDRmENTDDAIHVA---KKVINSLTETFEIQAhKIHIGASVGISIYPTDGKTSSILIRNADTAMYKAKKSGG 407
Cdd:TIGR00254 81 GGEEFVVILPG-TPLEDALSKAerlRDAINSKPIEVAGSE-TLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGR 158
|
.
gi 1490347179 408 N 408
Cdd:TIGR00254 159 N 159
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
55-672 |
0e+00 |
|
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain [Signal transduction mechanisms];
Pssm-ID: 444025 [Multi-domain] Cd Length: 678 Bit Score: 584.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 55 LIIIAISVFRIITSRRYLLNKTNLPAHLYSHVFLTFVTGTLWGYVAYMQMYTNDDVLRNLIFLINFGLIAASIATLSAWV 134
Cdd:COG5001 54 LLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAAS 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 135 YAYLAYMFPQSLAIFYVFLKLDNEYSLQMAGAFVIFTGVMIITSIRYSYRIKKEAELIHDLNNEIGMREEAQLQLQNSKQ 214
Cdd:COG5001 134 AALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 215 GLEDKVNERTKELVDMNSHLESVIDKKEQAEKSLHYLAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRF 294
Cdd:COG5001 214 LGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRF 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 295 KTINDSLGHTIGDILIKKASARLHKILRSRDTLARNGGDEFVIVLDRMENTDDAIHVAKKVINSLTETFEIQAHKIHIGA 374
Cdd:COG5001 294 KEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 375 SVGISIYPTDGKTSSILIRNADTAMYKAKKSGGNQLQFYNESMSNQLRDRLVLENELHSALEKDEFYLMYQPQVNCLTGE 454
Cdd:COG5001 374 SIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGR 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 455 TTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRT---QPANHVTYSINLSVLQFNNYKFIDFVR 531
Cdd:COG5001 454 IVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAwqdAGLPDLRVAVNLSARQLRDPDLVDRVR 533
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 532 NEIDKAGIDPAQIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSMSYLARLPIDVIKIDKSLVRNINEHK 611
Cdd:COG5001 534 RALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDP 613
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1490347179 612 NLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKPIMPDDIDHWLS 672
Cdd:COG5001 614 DDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLR 674
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
109-671 |
5.34e-113 |
|
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: 352.16 E-value: 5.34e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 109 DVLRNLIFLINFGLIAASIATLSAWVYAYLAYMFPQSLAIFYVFLKLDNEYSLQMAGAFVIFTGVMIITSIRYSYRIKKE 188
Cdd:COG2200 12 LLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 189 AELIHDLNNEIGMREEAQLQLQNSKQGLEDKVNERTKELVDMNSHLESVIDKKEQAEKSLHYLAYHDELTGLPNKNLLVD 268
Cdd:COG2200 92 LLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 269 RINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDTLARNGGDEFVIVLDRMENTDDA 348
Cdd:COG2200 172 LLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 349 IHVAKKVINSLTETFEIQAHKIHIGASVGISIYPTDGKTSSILIRNADTAMYKAKKSGGNQLQFYNESMSnQLRDRLVLE 428
Cdd:COG2200 252 AAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEA-RARRRLALE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 429 NELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRTQPAN 508
Cdd:COG2200 331 SELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPER 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 509 H--VTYSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSM 586
Cdd:COG2200 411 GldLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSL 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 587 SYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKPIMPDD 666
Cdd:COG2200 491 SYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEE 570
|
....*
gi 1490347179 667 IDHWL 671
Cdd:COG2200 571 LEALL 575
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
238-671 |
7.80e-109 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 343.97 E-value: 7.80e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 238 IDKKEQAEKSLHYLAYHDELTGLPNKNLLVDRINQSIktSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARL 317
Cdd:PRK10060 223 ITEERRAQERLRILANTDSITGLPNRNAIQELIDHAI--NAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 318 HKILRSRDTLARNGGDEFvIVLdrMENTDDAI--HVAKKVINSLTETFEIQAHKIHIGASVGISIYPTDGKTSSILIRNA 395
Cdd:PRK10060 301 LSCLEEDQTLARLGGDEF-LVL--ASHTSQAAleAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 396 DTAMYKAKKSGGNQLQFYNESMSNQLRDRLVLENELHSALEKDEFYLMYQPQVNcLTGETTGFEILLRWSNTTYGEIGPD 475
Cdd:PRK10060 378 DTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKIT-WRGEVRSLEALVRWQSPERGLIPPL 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 476 RFVPLLEETGLIYATGDWV----VTQVIDFiRTQPANhVTYSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITES 551
Cdd:PRK10060 457 EFISYAEESGLIVPLGRWVmldvVRQVAKW-RDKGIN-LRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTES 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 552 LLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSMSYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTN 631
Cdd:PRK10060 535 CLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQV 614
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1490347179 632 IFEGVETKEELAVIQSMKGNIIQGYLFSKPIMPDDIDHWL 671
Cdd:PRK10060 615 IAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWY 654
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
207-676 |
4.54e-95 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 311.32 E-value: 4.54e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 207 LQLQNSKQGLEDKVNERtkeLVDMNSHLESVIDKKEQAEKSLHYLAYHDELTGLPNKNLLVDRINQSIKTSsrdnQKIAI 286
Cdd:PRK11359 334 LQIKTSSGAETSAFIER---VADISQHLAALALEQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKA----VSPVV 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 287 LFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDTLARNGGDEFVIVLDRMEnTDDAIHVAKKVINSLTETFEIQ 366
Cdd:PRK11359 407 YLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLEND-VSNITQIADELRNVVSKPIMID 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 367 AHKIHIGASVGISIypTDGKTSSILIRNADTAMYKAKKSGGNQLQFYNESMSNQLRDRLVLENELHSALEKDEFYLMYQP 446
Cdd:PRK11359 486 DKPFPLTLSIGISY--DVGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQP 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 447 QVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQV---IDFIRTQPANHVTYSINLSVLQFNN 523
Cdd:PRK11359 564 QIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEAcrqLAEWRSQNIHIPALSVNLSALHFRS 643
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 524 YKFIDFVRNEIDKAGIDPAQIEFEITESLLIndfEKTHDFLSELH---SLGCSIALDDFGTGYTSMSYLARLPIDVIKID 600
Cdd:PRK11359 644 NQLPNQVSDAMQAWGIDGHQLTVEITESMMM---EHDTEIFKRIQilrDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKID 720
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1490347179 601 KSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKPIMPDDIDHWLSLAQD 676
Cdd:PRK11359 721 KSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLP 796
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
429-666 |
2.80e-94 |
|
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: 291.37 E-value: 2.80e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 429 NELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRT--QP 506
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARwqAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 507 ANHVTYSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSM 586
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 587 SYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKPIMPDD 666
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
428-667 |
6.33e-85 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 267.16 E-value: 6.33e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 428 ENELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRTQPA 507
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 508 NHVTY---SINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYT 584
Cdd:smart00052 81 QGPPPlliSINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 585 SMSYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKPiMP 664
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP-LP 239
|
...
gi 1490347179 665 DDI 667
Cdd:smart00052 240 LDD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
428-661 |
4.17e-78 |
|
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: 249.16 E-value: 4.17e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 428 ENELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRTQPA 507
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 508 NHVT-YSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSM 586
Cdd:pfam00563 81 GPDIkLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1490347179 587 SYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKP 661
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
246-667 |
1.85e-68 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 243.04 E-value: 1.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 246 KSLHYLAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRD 325
Cdd:PRK09776 659 RQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 326 TLARNGGDEFVIVLDRMeNTDDAIHVAKKVINSLTE---TFEIQAHKihIGASVGISIYPTDGKTSSILIRNADTAMYKA 402
Cdd:PRK09776 739 VLARLGGDEFGLLLPDC-NVESARFIATRIISAINDyhfPWEGRVYR--VGASAGITLIDANNHQASEVMSQADIACYAA 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 403 KKSGGNQLQFYNESMSNQLRDR--LVLENELHSALEKDEFyLMYQPQVNCLTGETTGF-EILLR-WsnTTYGE-IGPDRF 477
Cdd:PRK09776 816 KNAGRGRVTVYEPQQAAAHSEHraLSLAEQWRMIKENQLM-MLAHGVASPRIPEARNHwLISLRlW--DPEGEiIDEGAF 892
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 478 VPLLEETGLIYATGDWVVTQV-IDFIRTQPANHVTYSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLIND 556
Cdd:PRK09776 893 RPAAEDPALMHALDRRVIHEFfRQAAKAVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNH 972
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 557 FEKTHDFLSELHSLGCSIALDDFGTGYTSMSYLARLPIDVIKIDKSLVRNIneHKNL--KSIVKAIVTMSESLGMTNIFE 634
Cdd:PRK09776 973 AESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANL--HGNLmdEMLISIIQGHAQRLGMKTIAG 1050
|
410 420 430
....*....|....*....|....*....|...
gi 1490347179 635 GVETKEELAVIQSMKGNIIQGYLFSKPiMPDDI 667
Cdd:PRK09776 1051 PVELPLVLDTLSGIGVDLAYGYAIARP-QPLDL 1082
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
242-674 |
9.74e-68 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 234.22 E-value: 9.74e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 242 EQAEKSLHYlayhdELTGLPNKNLLVDRINQSIktssRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKIL 321
Cdd:PRK13561 226 EQSRNATRF-----PVSDLPNKALLMALLEQVV----ARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 322 RSRDTLARNGGDEFVIVLDRMENTDDAIHVAKKVINSLTETFEIQAHKIHIGASVGISIYPTDgKTSSILIRNADTAMYK 401
Cdd:PRK13561 297 SPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGD-LTAEQLYSRAISAAFT 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 402 AKKSGGNQLQFYNESMSNQLRDRLVLENELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLL 481
Cdd:PRK13561 376 ARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 482 EETGLIYATGDWVVTQVIDFIRTQPANHVT--YSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEK 559
Cdd:PRK13561 456 ESCGLMVTVGHWVLEESCRLLAAWQERGIMlpLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 560 THDFLSELHSLGCSIALDDFGTGYTSMSYLAR---LPIDVIKIDKSLVRNINEHknlKSIVKAIVTMSESLGMTNIFEGV 636
Cdd:PRK13561 536 AVAILRPLRNAGVRVALDDFGMGYAGLRQLQHmksLPIDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGV 612
|
410 420 430
....*....|....*....|....*....|....*....
gi 1490347179 637 ETKEELAVIQSMKGNIIQGYLFSKPIMPDDI-DHWLSLA 674
Cdd:PRK13561 613 ETEAQRDWLLKAGVGIAQGFLFARALPIEIFeERYLEEK 651
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
421-671 |
9.54e-66 |
|
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: 225.95 E-value: 9.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 421 LRDRLVLENELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVI- 499
Cdd:COG4943 266 LRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 500 ---DFIRTQPANHVtySINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLInDFEKTHDFLSELHSLGCSIAL 576
Cdd:COG4943 346 dlgDLLAADPDFHI--SINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAI 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 577 DDFGTGYTSMSYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGY 656
Cdd:COG4943 423 DDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGW 502
|
250
....*....|....*
gi 1490347179 657 LFSKPIMPDDIDHWL 671
Cdd:COG4943 503 LFAKPLPAEEFIAWL 517
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
242-662 |
5.49e-65 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 227.13 E-value: 5.49e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 242 EQAEKSLHYLAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKiAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKIL 321
Cdd:PRK11829 222 ADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDHF-HLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCI 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 322 RSRDTLARNGGDEFVIVLDRMENTDDAIHVAKKVINSLTETFEIQAHKIHIGASVGISIYPTDGKTSSILIRNADTAMYK 401
Cdd:PRK11829 301 DDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMA 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 402 AKKSGGNQLQFYNESMSNQLRDRLVLENELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLL 481
Cdd:PRK11829 381 AHHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFA 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 482 EETGLIYATGDWVVTQVIDFIRTQPANHVT--YSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEK 559
Cdd:PRK11829 461 EEEGMMVPLGNWVLEEACRILADWKARGVSlpLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDE 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 560 THDFLSELHSLGCSIALDDFGTGYTSMSYL---ARLPIDVIKIDKSLVRNINEHKNLKSIVKAIvtmSESLGMTNIFEGV 636
Cdd:PRK11829 541 ALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLPEDDAIARIISCV---SDVLKVRVMAEGV 617
|
410 420
....*....|....*....|....*.
gi 1490347179 637 ETKEELAVIQSMKGNIIQGYLFSKPI 662
Cdd:PRK11829 618 ETEEQRQWLLEHGIQCGQGFLFSPPL 643
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
238-413 |
3.81e-59 |
|
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: 200.59 E-value: 3.81e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 238 IDKKEQAEKSLHYLAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARL 317
Cdd:COG2199 100 ITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRL 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 318 HKILRSRDTLARNGGDEFVIVLDRMeNTDDAIHVAKKVINSLTET-FEIQAHKIHIGASVGISIYPTDGKTSSILIRNAD 396
Cdd:COG2199 180 RASLRESDLVARLGGDEFAVLLPGT-DLEEAEALAERLREALEQLpFELEGKELRVTVSIGVALYPEDGDSAEELLRRAD 258
|
170
....*....|....*..
gi 1490347179 397 TAMYKAKKSGGNQLQFY 413
Cdd:COG2199 259 LALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
253-411 |
5.51e-59 |
|
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: 195.85 E-value: 5.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 253 YHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDTLARNGG 332
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1490347179 333 DEFVIVLDRMeNTDDAIHVAKKVINSLTETFEIQAHKIHIGASVGISIYPTDGKTSSILIRNADTAMYKAKKSGGNQLQ 411
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
252-409 |
9.13e-53 |
|
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: 178.99 E-value: 9.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 252 AYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDTLARNG 331
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 332 GDEFVIVLDR--MENTDDAIHVAKKVINSLTETFEIQAHKIHIGASVGISIYPTDGKTSSILIRNADTAMYKAKKSGGNQ 409
Cdd:pfam00990 81 GDEFAILLPEtsLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
250-413 |
1.05e-50 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 173.59 E-value: 1.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 250 YLAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDTLAR 329
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 330 NGGDEFVIVLDRmENTDDAIHVAKKVINSLTETFEIQAHKIHIGASVGISIYPTDGKTSSILIRNADTAMYKAKKSGGNQ 409
Cdd:smart00267 81 LGGDEFALLLPE-TSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 1490347179 410 LQFY 413
Cdd:smart00267 160 VAVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
251-408 |
1.16e-40 |
|
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: 145.94 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 251 LAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDTLARN 330
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 331 GGDEFVIVLDRmENTDDAIHVA---KKVINSLTETFEIQAhKIHIGASVGISIYPTDGKTSSILIRNADTAMYKAKKSGG 407
Cdd:TIGR00254 81 GGEEFVVILPG-TPLEDALSKAerlRDAINSKPIEVAGSE-TLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGR 158
|
.
gi 1490347179 408 N 408
Cdd:TIGR00254 159 N 159
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
421-672 |
1.11e-35 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 141.67 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 421 LRDRLVLENELHSALEKDEFYLMYQPQVNCLTGETTGFEILLRWSNTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVID 500
Cdd:PRK10551 258 LSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIAR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 501 ----FIRTQPANhVTYSINLSVLQFNNYKFIDFVRNEIDKAGIDPAQIEFEITESLLINDFEKTHDFlSELHSLGCSIAL 576
Cdd:PRK10551 338 daaeLQKVLPVG-AKLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEATKLF-AWLHSQGIEIAI 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 577 DDFGTGYTSMSYLARLPIDVIKIDKSLVRNINEHKNLKSIVKAIVTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGY 656
Cdd:PRK10551 416 DDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGY 495
|
250
....*....|....*.
gi 1490347179 657 LFSKPIMPDDIDHWLS 672
Cdd:PRK10551 496 WISRPLPLEDFVRWLK 511
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
251-409 |
7.50e-28 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 117.31 E-value: 7.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 251 LAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDTLARN 330
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 331 GGDEFVIVldrMENTD--DAIHVA---KKVINSLTETFEIQAHKIHIGASVGISIYPTDGKTSSILIRNADTAMYKAKKS 405
Cdd:PRK09581 371 GGEEFVVV---MPDTDieDAIAVAeriRRKIAEEPFIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNT 447
|
....
gi 1490347179 406 GGNQ 409
Cdd:PRK09581 448 GRNR 451
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
255-416 |
8.85e-27 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 110.93 E-value: 8.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 255 DELTGLPNKNLLVDRINQSIKtsSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDTLARNGGDE 334
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQLR--NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 335 FVIVLDRmeNTDDAIHVAKKVINSLTETFEIQA--HKIHIGASVGISIYpTDGKTSSILIRNADTAMYKAKKSGGNQLQF 412
Cdd:PRK09894 210 FIICLKA--ATDEEACRAGERIRQLIANHAITHsdGRINITATFGVSRA-FPEETLDVVIGRADRAMYEGKQTGRNRVMF 286
|
....
gi 1490347179 413 YNES 416
Cdd:PRK09894 287 IDEQ 290
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
247-409 |
5.16e-23 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 103.56 E-value: 5.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 247 SLHYLAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSRDT 326
Cdd:PRK15426 393 SLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDV 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 327 LARNGGDEFVIVLDRMeNTDDAIHVAKKVINSLTETfEIQAHK---IHIGASVGISIYPTDGK-TSSILIRNADTAMYKA 402
Cdd:PRK15426 473 AGRVGGEEFCVVLPGA-SLAEAAQVAERIRLRINEK-EILVAKsttIRISASLGVSSAEEDGDyDFEQLQSLADRRLYLA 550
|
....*..
gi 1490347179 403 KKSGGNQ 409
Cdd:PRK15426 551 KQAGRNR 557
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
252-662 |
1.43e-19 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 93.00 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 252 AYHDELTGLPNKnLLVDriNQsIKTSSRDNQKIA----ILFLDLDRFKTINDSLGHTIGDILIKKASARLHKIL-RSRDT 326
Cdd:PRK11059 228 AFQDAKTGLGNR-LFFD--NQ-LATLLEDQEMVGahgvVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVmRYPGA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 327 -LARNGGDEFVIVLDRMeNTDDAIHVAKKVINSL----------TETFeiqahkIHIGASvgisiYPTDGKTSSILIRNA 395
Cdd:PRK11059 304 lLARYSRSDFAVLLPHR-SLKEADSLASQLLKAVdalpppkmldRDDF------LHIGIC-----AYRSGQSTEQVMEEA 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 396 DTAMYKAKKSGGNqlqfyNESMSNQLRD----------RLVLENelhsALEKDEFYLMYQPQVNCLtGETTGFEILLRWS 465
Cdd:PRK11059 372 EMALRSAQLQGGN-----GWFVYDKAQLpekgrgsvrwRTLLEQ----TLVRGGPRLYQQPAVTRD-GKVHHRELFCRIR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 466 NTTYGEIGPDRFVPLLEETGLIYATGDWVVTQVIDFIRTQPanHVTYSINLSVLQFNNYKFIDFVRNEI---DKAgiDPA 542
Cdd:PRK11059 442 DGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWP--EENLSINLSVDSLLSRAFQRWLRDTLlqcPRS--QRK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 543 QIEFEITESLLINDFEKTHDFLSELHSLGCSIALDDFGTGYTSMSYLARLPIDVIKIDKSLVRNINE-HKN---LKSIVk 618
Cdd:PRK11059 518 RLIFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKrTENqlfVRSLV- 596
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1490347179 619 aivtmsESLGMTN---IFEGVETKEELaviQSMKGNII---QGYLFSKPI 662
Cdd:PRK11059 597 ------GACAGTEtqvFATGVESREEW---QTLQELGVsggQGDFFAESQ 637
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
221-403 |
4.39e-16 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 80.82 E-value: 4.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 221 NERTKELVDMNSHLESVIDKKE------QAEKS-LHYLAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKiAILFLDLDR 293
Cdd:PRK09966 210 EERIAEFHRFALDFNSLLDEMEewqlrlQAKNAqLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKTS-ALLFLDGDN 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 294 FKTINDSLGHTIGDILIKKASARLHKILRSRDTLARNGGDEFVIVLDRMENTDDAIHVAKKVINSLTETFEIQ-AHKIHI 372
Cdd:PRK09966 289 FKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHnGHQTTM 368
|
170 180 190
....*....|....*....|....*....|.
gi 1490347179 373 GASVGISIyPTDGKTSSILIRNADTAMYKAK 403
Cdd:PRK09966 369 TLSIGYAM-TIEHASAEKLQELADHNMYQAK 398
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
245-409 |
1.04e-15 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 79.49 E-value: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 245 EKSLHYLAYHDELTGLPNKNLLVDRINQSIKTSSRDNQKIAILFLDLDRFKTINDSLGHTIGDILIKKASARLHKILRSR 324
Cdd:PRK10245 198 KRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGS 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 325 DTLARNGGDEFVIVldrMENT--DDAIHVAKKVINSLTETFEIQAHKIHIGASVGISIYPTDGKTSSILIRNADTAMYKA 402
Cdd:PRK10245 278 DVIGRFGGDEFAVI---MSGTpaESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMSHYREWLKSADLALYKA 354
|
....*..
gi 1490347179 403 KKSGGNQ 409
Cdd:PRK10245 355 KNAGRNR 361
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
544-661 |
3.47e-08 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 55.01 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 544 IEFEITESLLINDFEKTHDfLSELHSLGcsiaLDDFGTGYTSMSYLARLPIDVIKIDKSL---VRNINEHKNLKSivkAI 620
Cdd:PRK11596 130 LRFELVEHIRLPKDSPFAS-MCEFGPLW----LDDFGTGMANFSALSEVRYDYIKVARELfimLRQSEEGRNLFS---QL 201
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1490347179 621 VTMSESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKP 661
Cdd:PRK11596 202 LHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRP 242
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
319-403 |
5.05e-08 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 53.37 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 319 KILRSR-DTLARNGGDEFVIVLDRMeNTDDAIHVAKKVINSLTETFEiqahkIHIGASVGISIyptdgktsSILIRNADt 397
Cdd:COG3706 109 EELLARvDLVARYGGEEFAILLPGT-DLEGALAVAERIREAVAELPS-----LRVTVSIGVAG--------DSLLKRAD- 173
|
....*.
gi 1490347179 398 AMYKAK 403
Cdd:COG3706 174 ALYQAR 179
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
438-663 |
1.04e-07 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 54.81 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 438 DEFYLMYQPQVNcLTGETTGFEILLRWSNT-TYGEIGPDRfvplleetgliyATGDWVVTQVIDfirtqpanhvtysINL 516
Cdd:COG3434 2 MDVFVARQPILD-RDQRVVGYELLFRSGLEnSAPDVDGDQ------------ATARVLLNAFLE-------------IGL 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 517 SVLQFNNYKFIDFVRNEIDK---AGIDPAQIEFEITESLLINdfEKTHDFLSELHSLGCSIALDDFGTGYTSMSYLARlp 593
Cdd:COG3434 56 DRLLGGKLAFINFTEELLLSdlpELLPPERVVLEILEDVEPD--EELLEALKELKEKGYRIALDDFVLDPEWDPLLPL-- 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 594 IDVIKIDkslVRNINEHKnLKSIVKAIvtmsESLGMTNIFEGVETKEELAVIQSMKGNIIQGYLFSKPIM 663
Cdd:COG3434 132 ADIIKID---VLALDLEE-LAELVARL----KRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
284-379 |
2.54e-06 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 47.35 E-value: 2.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1490347179 284 IAILFLDLDRFKTINDSLGHTIGDILIKKASARL-HKILRSRDTLARNGGDEFVIVLDRMEnTDDAIHVAKKVINSLTet 362
Cdd:cd07556 2 VTILFADIVGFTSLADALGPDEGDELLNELAGRFdSLIRRSGDLKIKTIGDEFMVVSGLDH-PAAAVAFAEDMREAVS-- 78
|
90
....*....|....*...
gi 1490347179 363 fEIQAHKI-HIGASVGIS 379
Cdd:cd07556 79 -ALNQSEGnPVRVRIGIH 95
|
|
|