|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
250-852 |
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: 616.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 250 VQIIWDGENPGQALIIYFLPLLILSVILTVSMTVILMRHIMQKARMLDENTFLLEQARLNLITSEKRFRDVSETTSDWFW 329
Cdd:COG5001 63 LALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 330 ETDLSLKITWLSGRFSTVTGYENSKWIGRRLDELFPSTTGLLQDCVRFRELTERFEFKSCPYIHAQQSTAYCTLLAKLSA 409
Cdd:COG5001 143 AALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 410 QPDGTVVLRGAATDVSLEVEATKRVEFLSRHDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGH 489
Cdd:COG5001 223 LLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 490 STGDALLGEVALRLKNCVRRGDFVARQGGDEFMLLLGNTSQKDQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALAPL 569
Cdd:COG5001 303 AAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPD 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 570 DSSSANDLLRYADIALYQAKQSGRNRWVYYRPDMSEKLTERRKLELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVR 649
Cdd:COG5001 383 DGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLR 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 650 WQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKACAETK----DKLPGLSVSVNISAIEFQASDLAERIKEILHETGLE 725
Cdd:COG5001 463 WQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAawqdAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLP 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 726 PDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRILIDDFGTGYASLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKI 805
Cdd:COG5001 543 PSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAI 622
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 544825310 806 IDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKPAAITEL 852
Cdd:COG5001 623 IALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEEL 669
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
420-846 |
6.11e-114 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 362.46 E-value: 6.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 420 AATDVSLEVEATKRVEFLSRHDELTGLPNRYHIKEFLAGQLAKEDLNHypFAMICLDLDKFKPVNDIFGHSTGDALLGEV 499
Cdd:PRK10060 219 SGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQ--VGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 500 ALRLKNCVRRGDFVARQGGDEFMLLLGNTSQkDQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALAPLDSSSANDLLR 579
Cdd:PRK10060 297 SLAILSCLEEDQTLARLGGDEFLVLASHTSQ-AALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIR 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 580 YADIALYQAKQSGRNRWVYYRPDMSEKLTERRKLELELKTAIREEQLYLVYQPRYNLRySKIEAVEALVRWQHPHRGTMM 659
Cdd:PRK10060 376 SADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIP 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 660 PDQFIPLAEETGLIINLSNWVIRKACAET---KDKLPGLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTEN 736
Cdd:PRK10060 455 PLEFISYAEESGLIVPLGRWVMLDVVRQVakwRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTES 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 737 VTLSDPEKTLQTMKALKKMGVRILIDDFGTGYASLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAV 816
Cdd:PRK10060 535 CLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQV 614
|
410 420 430
....*....|....*....|....*....|
gi 544825310 817 TAEGVETTEQLSFLKKNRCDEVQGYLLGKP 846
Cdd:PRK10060 615 IAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
616-851 |
1.69e-103 |
|
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: 319.88 E-value: 1.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 616 ELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKAC---AETKDKL 692
Cdd:cd01948 2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACrqlARWQAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 693 PGLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRILIDDFGTGYASLS 772
Cdd:cd01948 82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825310 773 YLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKPAAITE 851
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
614-846 |
9.16e-96 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 299.90 E-value: 9.16e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 614 ELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKAC---AETKD 690
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACqqlAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 691 KLP-GLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRILIDDFGTGYA 769
Cdd:smart00052 81 QGPpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825310 770 SLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKP 846
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
616-846 |
7.36e-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: 252.24 E-value: 7.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 616 ELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKACAETKDK--LP 693
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 694 GLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRILIDDFGTGYASLSY 773
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825310 774 LRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKP 846
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
437-598 |
1.27e-36 |
|
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: 135.54 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 437 LSRHDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQ 516
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 517 GGDEFMLLLGNTSQKDQIdEVCHRIVQELN-RPFSIEGND-VAIGVSMGIALAPLDSSSANDLLRYADIALYQAKQSGRN 594
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDAL-SKAERLRDAINsKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....
gi 544825310 595 RWVY 598
Cdd:TIGR00254 160 RVVV 163
|
|
| CHASE4 |
pfam05228 |
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various ... |
65-217 |
8.20e-15 |
|
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in prokaryotes. Specifically, CHASE4 domains are found in histidine kinases in Archaea and in predicted diguanylate cyclases/phosphodiesterases in Bacteria. Environmental factors that are recognized by CHASE4 domains are not known at this time.
Pssm-ID: 428380 Cd Length: 139 Bit Score: 71.97 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 65 ALDSRQESMRSHLKDNAEWGDAYKHLHlntDVHWAWDKQNLGKSLYDNFGYEGVFILSPEGTTRYSVLDGKLKLQDLGRW 144
Cdd:pfam05228 1 ALEQELDSLDRLLRDWAVWDDTYDFVQ---DGNPDYIESNLGPETFENLGLDLILFVDADGKLVYDLENGKPDSPLLSRS 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825310 145 LDKSTKERLLRevsVNNGlpvsiltlidsvPAIVSAEWITTGDDASvqPLPGkpsVMVFVDKLTAKKLLAIGQ 217
Cdd:pfam05228 78 SPDSGLSGIVL---LGGG------------PALVAARPILTSDGSG--PPRG---TLVMGRYLDEAFLDRLSE 130
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
250-852 |
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: 616.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 250 VQIIWDGENPGQALIIYFLPLLILSVILTVSMTVILMRHIMQKARMLDENTFLLEQARLNLITSEKRFRDVSETTSDWFW 329
Cdd:COG5001 63 LALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 330 ETDLSLKITWLSGRFSTVTGYENSKWIGRRLDELFPSTTGLLQDCVRFRELTERFEFKSCPYIHAQQSTAYCTLLAKLSA 409
Cdd:COG5001 143 AALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 410 QPDGTVVLRGAATDVSLEVEATKRVEFLSRHDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGH 489
Cdd:COG5001 223 LLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGH 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 490 STGDALLGEVALRLKNCVRRGDFVARQGGDEFMLLLGNTSQKDQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALAPL 569
Cdd:COG5001 303 AAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPD 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 570 DSSSANDLLRYADIALYQAKQSGRNRWVYYRPDMSEKLTERRKLELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVR 649
Cdd:COG5001 383 DGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLR 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 650 WQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKACAETK----DKLPGLSVSVNISAIEFQASDLAERIKEILHETGLE 725
Cdd:COG5001 463 WQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAawqdAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLP 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 726 PDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRILIDDFGTGYASLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKI 805
Cdd:COG5001 543 PSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAI 622
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 544825310 806 IDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKPAAITEL 852
Cdd:COG5001 623 IALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEEL 669
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
284-852 |
1.56e-116 |
|
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: 366.42 E-value: 1.56e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 284 ILMRHIMQKARMLDENTFLLEQARLNLITSEKRFRDVSETTSDWFWETDLSLKITWLSGRFSTVTGYENSKWIGRRLDEL 363
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 364 FPSTTGLLQDCVRFRELTERFEFKSCPYIHAQQSTAYCTLLAKLSAQPDGTVVLRGAATDVSLEVEATKRVEFLSRHDEL 443
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 444 TGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQGGDEFML 523
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 524 LLGNTSQKDQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALAPLDSSSANDLLRYADIALYQAKQSGRNRWVYYRPDM 603
Cdd:COG2200 241 LLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 604 sEKLTERRKLELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRK 683
Cdd:COG2200 321 -ARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLER 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 684 AC---AETKDKLPGLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRIL 760
Cdd:COG2200 400 ALrqlARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIA 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 761 IDDFGTGYASLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQG 840
Cdd:COG2200 480 LDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQG 559
|
570
....*....|..
gi 544825310 841 YLLGKPAAITEL 852
Cdd:COG2200 560 YLFGRPLPLEEL 571
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
420-846 |
6.11e-114 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 362.46 E-value: 6.11e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 420 AATDVSLEVEATKRVEFLSRHDELTGLPNRYHIKEFLAGQLAKEDLNHypFAMICLDLDKFKPVNDIFGHSTGDALLGEV 499
Cdd:PRK10060 219 SGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQ--VGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 500 ALRLKNCVRRGDFVARQGGDEFMLLLGNTSQkDQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALAPLDSSSANDLLR 579
Cdd:PRK10060 297 SLAILSCLEEDQTLARLGGDEFLVLASHTSQ-AALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIR 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 580 YADIALYQAKQSGRNRWVYYRPDMSEKLTERRKLELELKTAIREEQLYLVYQPRYNLRySKIEAVEALVRWQHPHRGTMM 659
Cdd:PRK10060 376 SADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIP 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 660 PDQFIPLAEETGLIINLSNWVIRKACAET---KDKLPGLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTEN 736
Cdd:PRK10060 455 PLEFISYAEESGLIVPLGRWVMLDVVRQVakwRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTES 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 737 VTLSDPEKTLQTMKALKKMGVRILIDDFGTGYASLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAV 816
Cdd:PRK10060 535 CLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQV 614
|
410 420 430
....*....|....*....|....*....|
gi 544825310 817 TAEGVETTEQLSFLKKNRCDEVQGYLLGKP 846
Cdd:PRK10060 615 IAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
616-851 |
1.69e-103 |
|
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: 319.88 E-value: 1.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 616 ELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKAC---AETKDKL 692
Cdd:cd01948 2 DLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACrqlARWQAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 693 PGLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRILIDDFGTGYASLS 772
Cdd:cd01948 82 PDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLS 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825310 773 YLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKPAAITE 851
Cdd:cd01948 162 YLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
614-846 |
9.16e-96 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 299.90 E-value: 9.16e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 614 ELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKAC---AETKD 690
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACqqlAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 691 KLP-GLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRILIDDFGTGYA 769
Cdd:smart00052 81 QGPpPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825310 770 SLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKP 846
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
429-852 |
1.49e-87 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 295.53 E-value: 1.49e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 429 EATKRVEFLSRHDELTGLPNRYHIKEFLAGQLAKEdlnhYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVR 508
Cdd:PRK11359 367 KSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKA----VSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLK 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 509 RGDFVARQGGDEFMLLlgntSQKDQIDEVCHrIVQEL----NRPFSIEGNDVAIGVSMGIALAPldSSSANDLLRYADIA 584
Cdd:PRK11359 443 PDQYLCRIEGTQFVLV----SLENDVSNITQ-IADELrnvvSKPIMIDDKPFPLTLSIGISYDV--GKNRDYLLSTAHNA 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 585 LYQAKQSGRNRWVYYRPDMSEKLTERRKLELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFI 664
Cdd:PRK11359 516 MDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFI 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 665 PLAEETGLIINLSNWVIRKAC---AETKDKLPGLS-VSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLS 740
Cdd:PRK11359 596 PLAEEIGEIENIGRWVIAEACrqlAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMME 675
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 741 DPEKTLQTMKALKKMGVRILIDDFGTGYASLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEG 820
Cdd:PRK11359 676 HDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEG 755
|
410 420 430
....*....|....*....|....*....|..
gi 544825310 821 VETTEQLSFLKKNRCDEVQGYLLGKPAAITEL 852
Cdd:PRK11359 756 VETKEQFEMLRKIHCRVIQGYFFSRPLPAEEI 787
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
616-846 |
7.36e-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: 252.24 E-value: 7.36e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 616 ELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKACAETKDK--LP 693
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLqlGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 694 GLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRILIDDFGTGYASLSY 773
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825310 774 LRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKP 846
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
607-852 |
7.47e-76 |
|
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: 256.77 E-value: 7.47e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 607 LTERRKLELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKACA 686
Cdd:COG4943 266 LRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 687 ETKDKL---PGLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENvTLSDPEKTLQTMKALKKMGVRILIDD 763
Cdd:COG4943 346 DLGDLLaadPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITER-GFIDPAKARAVIAALREAGHRIAIDD 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 764 FGTGYASLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLL 843
Cdd:COG4943 425 FGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLF 504
|
....*....
gi 544825310 844 GKPAAITEL 852
Cdd:COG4943 505 AKPLPAEEF 513
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
331-858 |
3.57e-71 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 254.60 E-value: 3.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 331 TDLSLKITWLSGRFSTVTGYENSKWIGRRLDELFPST---TGLLQDCVRfRELTERfefkSCPYIhaQQSTAYCTLLAKL 407
Cdd:PRK09776 552 TDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVLHITfgdNGPLMENIY-SCLTSR----SAAYL--EQDVVLHCRSGGS 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 408 -----SAQP----DGTVVlrGAA---TDVSlevEATKRVEFLSR---HDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAM 472
Cdd:PRK09776 625 ydvhySITPlstlDGENI--GSVlviQDVT---ESRKMLRQLSYsasHDALTHLANRASFEKQLRRLLQTVNSTHQRHAL 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 473 ICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQGGDEFMLLLGNTSQkDQIDEVCHRIVQELN-RPFSI 551
Cdd:PRK09776 700 VFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNV-ESARFIATRIISAINdYHFPW 778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 552 EGNDVAIGVSMGIALAPLDSSSANDLLRYADIALYQAKQSGRNRWVYYRPDMSEKLTERRKLEL-ELKTAIREEQLYLVY 630
Cdd:PRK09776 779 EGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSLaEQWRMIKENQLMMLA 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 631 -------QPRYNlryskiEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKACAETKDKL--PGLSVSVNI 701
Cdd:PRK09776 859 hgvasprIPEAR------NHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVasKGLSIALPL 932
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 702 SAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRILIDDFGTGYASLSYLRKFQFDG 781
Cdd:PRK09776 933 SVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADY 1012
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825310 782 LKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKPAAITELnLNANR 858
Cdd:PRK09776 1013 LKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL-LNSSY 1088
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
444-846 |
1.44e-65 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 232.14 E-value: 1.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 444 TGLPNRYHIKEFLAGQLAKEDlNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQGGDEFML 523
Cdd:PRK11829 238 TELPNRSLFISLLEKEIASST-RTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 524 LLGNTSQKDQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALAPLDSSSANDLLRYADIALYQAKQSGRNRWVYYRPDM 603
Cdd:PRK11829 317 LARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 604 SEKLTERRKLELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRK 683
Cdd:PRK11829 397 IEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 684 ACAETKD-KLPGLSV--SVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKTLQTMKALKKMGVRIL 760
Cdd:PRK11829 477 ACRILADwKARGVSLplSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIA 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 761 IDDFGTGYASLSYLRKFQ---FDGLKLDKSFIFTLadsPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDE 837
Cdd:PRK11829 557 LDDFGIGYSSLRYLNHLKslpIHMIKLDKSFVKNL---PEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQC 633
|
....*....
gi 544825310 838 VQGYLLGKP 846
Cdd:PRK11829 634 GQGFLFSPP 642
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
438-853 |
3.23e-64 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 228.06 E-value: 3.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 438 SRHDE---------LTGLPNRYHIKEFLAGQLAKEDlnhyPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVR 508
Cdd:PRK13561 222 RQYEEqsrnatrfpVSDLPNKALLMALLEQVVARKQ----TTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 509 RGDFVARQGGDEFMLLLGNTSQKDQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALApLDSSSANDLLRYADIALYQA 588
Cdd:PRK13561 298 PRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFTA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 589 KQSGRNRWVYYRPDMSEKLTERRKLELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAE 668
Cdd:PRK13561 377 RRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIE 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 669 ETGLIINLSNWVIRKAC---AETKDKLPGLSVSVNISAIEFQASDLAERIKEILHETGLEPDRLEIEVTENVTLSDPEKT 745
Cdd:PRK13561 457 SCGLMVTVGHWVLEESCrllAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAA 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 746 LQTMKALKKMGVRILIDDFGTGYASLSYLRKFQ---FDGLKLDKSFIFTLadsPQNQSVVEKIIDLGKAYSMAVTAEGVE 822
Cdd:PRK13561 537 VAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGL---PEDDSMVAAIIMLAQSLNLQVIAEGVE 613
|
410 420 430
....*....|....*....|....*....|.
gi 544825310 823 TTEQLSFLKKNRCDEVQGYLLGKPAAITELN 853
Cdd:PRK13561 614 TEAQRDWLLKAGVGIAQGFLFARALPIEIFE 644
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
439-597 |
2.83e-60 |
|
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: 201.63 E-value: 2.83e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 439 RHDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQGG 518
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825310 519 DEFMLLLGNTSqKDQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALAPLDSSSANDLLRYADIALYQAKQSGRNRWV 597
Cdd:cd01949 81 DEFAILLPGTD-LEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
415-599 |
8.13e-60 |
|
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: 204.83 E-value: 8.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 415 VVLRGAATDVSLEVEATKRVEFLSRHDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDA 494
Cdd:COG2199 91 LLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 495 LLGEVALRLKNCVRRGDFVARQGGDEFMLLLGNTSQkDQIDEVCHRIVQELNR-PFSIEGNDVAIGVSMGIALAPLDSSS 573
Cdd:COG2199 171 VLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDL-EEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDS 249
|
170 180
....*....|....*....|....*.
gi 544825310 574 ANDLLRYADIALYQAKQSGRNRWVYY 599
Cdd:COG2199 250 AEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
440-595 |
1.68e-56 |
|
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: 191.31 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 440 HDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQGGD 519
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544825310 520 EFMLLLGNTSQK--DQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALAPLDSSSANDLLRYADIALYQAKQSGRNR 595
Cdd:pfam00990 83 EFAILLPETSLEgaQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
437-599 |
3.51e-53 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 182.06 E-value: 3.51e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 437 LSRHDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQ 516
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLARL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 517 GGDEFMLLLGNTSQkDQIDEVCHRIVQELNRPFSIEGNDVAIGVSMGIALAPLDSSSANDLLRYADIALYQAKQSGRNRW 596
Cdd:smart00267 82 GGDEFALLLPETSL-EEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 544825310 597 VYY 599
Cdd:smart00267 161 AVY 163
|
|
| CHASE4 |
COG3322 |
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ... |
18-745 |
8.02e-49 |
|
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442551 [Multi-domain] Cd Length: 724 Bit Score: 185.14 E-value: 8.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 18 KGLINKTFTYIVTLL----ISIFIAAIISLLLIKNNVNKISDKHDEFLLRKALDSRQESMRSHLKDNAEWGDAYKHLHlN 93
Cdd:COG3322 1 MSLRRKTLLAILLLLllllALLYLVSRLILLSSFSELEEQAAERDVERVLNALDAELDQLARLVADWAVWDDTYEFVQ-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 94 TDVHWAwdKQNLGKSLYDNFGYEGVFILSPEGTTRYSVLDG--KLKLQDLGRWLDKSTKERLLREVSVNNGLPVSILTLI 171
Cdd:COG3322 80 GDPEWI--ESNLGDWTFENLGLDLVLVLDPDGRLVYSKGYDleDGELVPLPEALAPLLARARALLRHASPDSSVSGLLRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 172 DSVPAIVSAEWITTGDDAsvqplPGKPSVMVFVDKLTAKKLLAIGQDAGIK------NVRTSPNAVTSQINNQT---EFT 242
Cdd:COG3322 158 DGGPALVAARPILPSDGP-----GPPRGTLVFGRYLDEAFLARLAERTGLDltlspaDPPAPPDQVVEPLSDDTiagYVP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 243 LSTQNGDVQII--WDGENP----GQALIIYFLPLLILSVILTVSMTVILMRHImqkarmldentflleqaRLNLITSEKR 316
Cdd:COG3322 233 LRDIDGQPVLLlrWTPPRPiyqqGRALLRYLLPALLLLGLLLALLALLLLRLV-----------------LLLLLLLLRL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 317 FRDVSETTSDWFWETDLSLKITWLSGRFSTVTGYENSKWIGRRLDELFPSTTGLLQDCVRFRELTERFEFKSCPYIHAQQ 396
Cdd:COG3322 296 VLSRLLLLLLRLLLLELLRALELLLLLLRRLLLLLLLLRLLLLLLDLLAALNLLLLLRALAERLVALALLALLLLGLLGL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 397 STAYCTLLAKLSAQPDGTVVLRGAATDVSLEVEATKRVEFLSRHDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLD 476
Cdd:COG3322 376 LAALRRLGLLAILALAEEAARLLLLALAIAGELLIGIEVLLALGLELAGSAIALARAAAALALLLAAAAAARLAARAASG 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 477 LDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQGGDEFMLLLGNTSQKDQIDEVCHRIVQELNRPFSIEGNDV 556
Cdd:COG3322 456 LLRDLLEADELEDRLRRALLAEAAALLLLALLALELLLALGDAALEILLAILLLGLVLEAQLAELERLLLLGEAGGELLE 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 557 AIGVSMGIALAPLDSSSANDLLRYADIALYQAKQSGRNRWVYYRPDMSEKLTERRKLELELKTAIREEQLYLVYQPRYNL 636
Cdd:COG3322 536 EIALLAALLAGLLLAVLLSLLLRLLLLIDALVALAEAAAGLLEALLEEEVELRRALLEAEELLLIALALLSLGLALALDD 615
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 637 RYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLSNWVIRKACAETKDKLPGLSVSVNISAIEFQASDLAERIK 716
Cdd:COG3322 616 GGRGLAGLLLLFRLSGIGLLLLRRLLGDDLLGLLAALIDLILALAGSLLLLTLAAAAEATAVVLVAELLEGALLLQALAL 695
|
730 740
....*....|....*....|....*....
gi 544825310 717 EILHETGLEPDRLEIEVTENVTLSDPEKT 745
Cdd:COG3322 696 ISLLELLLLLLLLELQLLEQVLSAPAALA 724
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
607-852 |
1.17e-41 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 160.16 E-value: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 607 LTERRKLELELKTAIREEQLYLVYQPRYNLRYSKIEAVEALVRWQHPHRGTMMPDQFIPLAEETGLIINLS----NWVIR 682
Cdd:PRK10551 258 LSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTqhlfELIAR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 683 KAcAETKDKLP-GLSVSVNISAIEFQASDLAERIKEILheTGLEPDRLEI--EVTENVTLSDpEKTLQTMKALKKMGVRI 759
Cdd:PRK10551 338 DA-AELQKVLPvGAKLGINISPAHLHSDSFKADVQRLL--ASLPADHFQIvlEITERDMVQE-EEATKLFAWLHSQGIEI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 760 LIDDFGTGYASLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQ 839
Cdd:PRK10551 414 AIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQ 493
|
250
....*....|...
gi 544825310 840 GYLLGKPAAITEL 852
Cdd:PRK10551 494 GYWISRPLPLEDF 506
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
437-598 |
1.27e-36 |
|
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: 135.54 E-value: 1.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 437 LSRHDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQ 516
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 517 GGDEFMLLLGNTSQKDQIdEVCHRIVQELN-RPFSIEGND-VAIGVSMGIALAPLDSSSANDLLRYADIALYQAKQSGRN 594
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDAL-SKAERLRDAINsKPIEVAGSEtLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRN 159
|
....
gi 544825310 595 RWVY 598
Cdd:TIGR00254 160 RVVV 163
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
441-597 |
5.20e-31 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 127.32 E-value: 5.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 441 DELTGLPNRY----HIKEFLAGQLAKEDlnhyPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQ 516
Cdd:PRK09581 295 DGLTGLHNRRyfdmHLKNLIERANERGK----PLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARY 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 517 GGDEFMLLLGNTSQKDQIdEVCHRIVQEL-NRPFSIEGNDVAIGVSMGIALAPLDSS--SANDLLRYADIALYQAKQSGR 593
Cdd:PRK09581 371 GGEEFVVVMPDTDIEDAI-AVAERIRRKIaEEPFIISDGKERLNVTVSIGVAELRPSgdTIEALIKRADKALYEAKNTGR 449
|
....
gi 544825310 594 NRWV 597
Cdd:PRK09581 450 NRVV 453
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
437-602 |
4.51e-27 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 112.08 E-value: 4.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 437 LSRHDELTGLPNRYHIKEFLAGQLAkeDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQ 516
Cdd:PRK09894 128 RSNMDVLTGLPGRRVLDESFDHQLR--NREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 517 GGDEFMLLLGNTSQkDQIDEVCHRIVQEL-NRPFSIEGNDVAIGVSMGIALAPLDsSSANDLLRYADIALYQAKQSGRNR 595
Cdd:PRK09894 206 GGEEFIICLKAATD-EEACRAGERIRQLIaNHAITHSDGRINITATFGVSRAFPE-ETLDVVIGRADRAMYEGKQTGRNR 283
|
....*..
gi 544825310 596 WVYYRPD 602
Cdd:PRK09894 284 VMFIDEQ 290
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
435-595 |
7.48e-27 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 116.27 E-value: 7.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 435 EFLSRHDELTGLPNRYHIKEfLAGQLAKE-DLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFV 513
Cdd:PRK15426 395 QWQAWHDPLTRLYNRGALFE-KARALAKRcQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 514 ARQGGDEFMLLLGNTSqKDQIDEVCHRIVQELNRPFSIEGNDVAI--GVSMGIalapldSSSAND-------LLRYADIA 584
Cdd:PRK15426 474 GRVGGEEFCVVLPGAS-LAEAAQVAERIRLRINEKEILVAKSTTIriSASLGV------SSAEEDgdydfeqLQSLADRR 546
|
170
....*....|.
gi 544825310 585 LYQAKQSGRNR 595
Cdd:PRK15426 547 LYLAKQAGRNR 557
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
440-597 |
1.38e-20 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 95.07 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 440 HDELTGLPNRYHIKEFLaGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVARQGGD 519
Cdd:PRK09966 250 HDPLTGLANRAAFRSGI-NTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGD 328
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825310 520 EFMLLLGNTSQKDQIDEVCHRIVQELNRPFSIE-GNDVAIGVSMGIALApLDSSSANDLLRYADIALYQAKQSGRNRWV 597
Cdd:PRK09966 329 EFAMVLYDVQSESEVQQICSALTQIFNLPFDLHnGHQTTMTLSIGYAMT-IEHASAEKLQELADHNMYQAKHQRAEKLV 406
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
429-595 |
2.48e-19 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 90.66 E-value: 2.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 429 EATKRVEFLSRHDELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVR 508
Cdd:PRK10245 196 EHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLR 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 509 RGDFVARQGGDEFMLLLGNTSQKDQIDEVChRIVQELNRPFSIEGNDVAIGVSMGIalAPLDSSSAN--DLLRYADIALY 586
Cdd:PRK10245 276 GSDVIGRFGGDEFAVIMSGTPAESAITAMS-RVHEGLNTLRLPNAPQVTLRISVGV--APLNPQMSHyrEWLKSADLALY 352
|
....*....
gi 544825310 587 QAKQSGRNR 595
Cdd:PRK10245 353 KAKNAGRNR 361
|
|
| CHASE4 |
pfam05228 |
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various ... |
65-217 |
8.20e-15 |
|
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in prokaryotes. Specifically, CHASE4 domains are found in histidine kinases in Archaea and in predicted diguanylate cyclases/phosphodiesterases in Bacteria. Environmental factors that are recognized by CHASE4 domains are not known at this time.
Pssm-ID: 428380 Cd Length: 139 Bit Score: 71.97 E-value: 8.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 65 ALDSRQESMRSHLKDNAEWGDAYKHLHlntDVHWAWDKQNLGKSLYDNFGYEGVFILSPEGTTRYSVLDGKLKLQDLGRW 144
Cdd:pfam05228 1 ALEQELDSLDRLLRDWAVWDDTYDFVQ---DGNPDYIESNLGPETFENLGLDLILFVDADGKLVYDLENGKPDSPLLSRS 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544825310 145 LDKSTKERLLRevsVNNGlpvsiltlidsvPAIVSAEWITTGDDASvqPLPGkpsVMVFVDKLTAKKLLAIGQ 217
Cdd:pfam05228 78 SPDSGLSGIVL---LGGG------------PALVAARPILTSDGSG--PPRG---TLVMGRYLDEAFLDRLSE 130
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
441-831 |
2.43e-13 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 73.74 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 441 DELTGLPNRYHIKEFLAGQLAKEDLNHYPFAMICLDLDKFKPVNDIFGHSTGDALLGEVALRLKNCVRR--GDFVARQGG 518
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRypGALLARYSR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 519 DEFMLLLGNTSQK--DQIDEVCHRIVQELNRPFSIEGND-VAIGVSM---GialapldsSSANDLLRYADIALYQAKQSG 592
Cdd:PRK11059 311 SDFAVLLPHRSLKeaDSLASQLLKAVDALPPPKMLDRDDfLHIGICAyrsG--------QSTEQVMEEAEMALRSAQLQG 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 593 RNRW-VYYRPDMSEKltER-----RKLeleLKTAIREEQLYLVYQPRYNlRYSKIEAVEALVRWQHPHRGTMMPDQFIPL 666
Cdd:PRK11059 383 GNGWfVYDKAQLPEK--GRgsvrwRTL---LEQTLVRGGPRLYQQPAVT-RDGKVHHRELFCRIRDGQGELLSAELFMPM 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 667 AEETGLIINLSNWVIRKACAETKDKlPGLSVSVNISAIEFQASDLAERIKEILHETG-LEPDRLEIEVTENVTLSDPEKT 745
Cdd:PRK11059 457 VQQLGLSEQYDRQVIERVLPLLRYW-PEENLSINLSVDSLLSRAFQRWLRDTLLQCPrSQRKRLIFELAEADVCQHISRL 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 746 LQTMKALKKMGVRILIDDFGTGYASLSYLRKFQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTE 825
Cdd:PRK11059 536 RPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESRE 615
|
....*.
gi 544825310 826 QLSFLK 831
Cdd:PRK11059 616 EWQTLQ 621
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
724-859 |
2.74e-11 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 66.36 E-value: 2.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 724 LEPDRLEIEVTENVTLSdpEKTLQTMKALKKMGVRILIDDFGTGYASLSYLRKFQFdgLKLDksfiFTLADSPQNQSVVE 803
Cdd:COG3434 81 LPPERVVLEILEDVEPD--EELLEALKELKEKGYRIALDDFVLDPEWDPLLPLADI--IKID----VLALDLEELAELVA 152
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 544825310 804 KIidlgKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKPAAITELNLNANRI 859
Cdd:COG3434 153 RL----KRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKGKKLPPSQL 204
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
476-589 |
5.53e-10 |
|
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: 58.14 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 476 DLDKFKPVNDIFGHSTGDALLGEVALRL-KNCVRRGDFVARQGGDEFMLLLGNTSQKDQID--EVCHRIVQELNRPfsiE 552
Cdd:cd07556 8 DIVGFTSLADALGPDEGDELLNELAGRFdSLIRRSGDLKIKTIGDEFMVVSGLDHPAAAVAfaEDMREAVSALNQS---E 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 544825310 553 GNDV--AIGVSMGIALAPLDSSS-----ANDLLRYADIALYQAK 589
Cdd:cd07556 85 GNPVrvRIGIHTGPVVVGVIGSRpqydvWGALVNLASRMESQAK 128
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
630-853 |
1.29e-09 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 59.63 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 630 YQPRYnlRYS-KIEAVEALVRWQHPhrgtMMPDQF---------IPLAEETGLIINLSNWVIRKACAETKDklpGLSVSV 699
Cdd:PRK11596 34 FQPIY--RTSgRLMAIELLTAVTHP----SNPSQRlsperyfaeITVSHRLDVVKEQLDLLAQWADFFVRH---GLLASV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 700 NISAIEFQASDLAERIKEILhetglepDR---LEIEVTENVTLSdPEKTLQTMKALkkmgVRILIDDFGTGYASLSYLRK 776
Cdd:PRK11596 105 NIDGPTLIALRQQPAILRLI-------ERlpwLRFELVEHIRLP-KDSPFASMCEF----GPLWLDDFGTGMANFSALSE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544825310 777 FQFDGLKLDKSFIFTLADSPQNQSVVEKIIDLGKAYSMAVTAEGVETTEQLSFLKKNRCDEVQGYLLGKPAAITELN 853
Cdd:PRK11596 173 VRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETLE 249
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
511-589 |
5.21e-09 |
|
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: 56.46 E-value: 5.21e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544825310 511 DFVARQGGDEFMLLLGNTSQkDQIDEVCHRIVQELNRPFSIEgndvaIGVSMGIAlapldsssANDLLRYADiALYQAK 589
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDL-EGALAVAERIREAVAELPSLR-----VTVSIGVA--------GDSLLKRAD-ALYQAR 179
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
305-425 |
1.37e-05 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 47.71 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 305 QARLNLITSEKRFRDVSETTSDWFWETDLSLKITWLSGRFSTVTGYENSKWIGRRLDELFPSTTGLLQDCVRFRELTERF 384
Cdd:COG2202 127 RAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGR 206
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 544825310 385 EFKSCPYIHAQQSTAYCTLLAKLSAQPDGTVVLR--GAATDVS 425
Cdd:COG2202 207 ESYELELRLKDGDGRWVWVEASAVPLRDGGEVIGvlGIVRDIT 249
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
305-542 |
2.23e-05 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 46.94 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 305 QARLNLITSEKRFRDVSETTSDWFWETDLSLKITWLSGRFSTVTGYENSKWIGRRLDELFPSTTGLLQDCVRFRELTE-- 382
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGgg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 383 --RFEFKscpYIHAQQSTAYCTLLAKLSAQPDGTVV-LRGAATDVSLEVEATKRVEFLSRHDELTGLPNRYHIKEFLAgQ 459
Cdd:COG2202 81 vwRGELR---NRRKDGSLFWVELSISPVRDEDGEITgFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDL-D 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544825310 460 LAKEDLNHYPFAMICLDLDKF--KPVNDIFGHSTGDALLGEVALRLKNCVRRGDFVAR-QGGDEFMLLLGNTSQKDQIDE 536
Cdd:COG2202 157 GRILYVNPAAEELLGYSPEELlgKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRlKDGDGRWVWVEASAVPLRDGG 236
|
....*.
gi 544825310 537 VCHRIV 542
Cdd:COG2202 237 EVIGVL 242
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
316-365 |
4.67e-04 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 39.30 E-value: 4.67e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 544825310 316 RFRDVSETTSDWFWETDLSLKITWLSGRFSTVTGYENSKWIGRRLDELFP 365
Cdd:smart00091 2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIH 51
|
|
| |
