|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
337-766 |
6.18e-125 |
|
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: 389.13 E-value: 6.18e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 337 EREQKISFQARHDSLTGFYNRSAMLEVLDDELT----PSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGFSD 412
Cdd:COG5001 242 RAEERLRHLAYHDPLTGLPNRRLFLDRLEQALArarrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 413 ElGGFHARIGGDEFLTVFPSAAAREResgIVGLMAQLLAC----YTIKTLKINLRFSAGVVEYPMQGLASDDLMRRVLIA 488
Cdd:COG5001 322 E-GDTVARLGGDEFAVLLPDLDDPED---AEAVAERILAAlaepFELDGHELYVSASIGIALYPDDGADAEELLRNADLA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 489 VDNA-TDSQDSIHYYQNGEDEAHLDRLKMLDELKQAIsdDDGQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPEL 567
Cdd:COG5001 398 MYRAkAAGRNRYRFFDPEMDERARERLELEADLRRAL--ERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 568 FIDLAEQSGLIVELTSWVVNTVVSQVADWQAKGIE-MQAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDM 646
Cdd:COG5001 476 FIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESAL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 647 IENEEKGIKALQNLKAIGVKISLDDYGVGQTSLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVA 726
Cdd:COG5001 556 LEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVA 635
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 490726579 727 EGVENRDSLDLLKLMHCDHAQGYYLSRPLKAELLEQWLKE 766
Cdd:COG5001 636 EGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
519-758 |
3.91e-88 |
|
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: 277.50 E-value: 3.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 519 ELKQAIsdDDGQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQA 598
Cdd:cd01948 2 DLRRAL--ERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 599 KGIEMQAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQTS 678
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 679 LGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLKAE 758
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
332-767 |
4.20e-81 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 272.71 E-value: 4.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 332 GNDINER---EQKISFQARHDSLTGFYNRSAMLEVLDDELT--PSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAVANR 406
Cdd:PRK10060 220 GTDITEErraQERLRILANTDSITGLPNRNAIQELIDHAINaaDNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 407 ISGFSDElGGFHARIGGDEFLTVFPSAAARERESgivglMAQLLacytIKTLKINLRF---------SAGVVEYPMQGLA 477
Cdd:PRK10060 300 ILSCLEE-DQTLARLGGDEFLVLASHTSQAALEA-----MASRI----LTRLRLPFRIglievytgcSIGIALAPEHGDD 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 478 SDDLMRRVLIAVDNATDSQDSIHYYQNGEDEAHLDRLKMLD-ELKQAIsdDDGQLFMTYQPKLHLhTQKINKVESLIRWQ 556
Cdd:PRK10060 370 SESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDtNLRKAL--ENDQLVIHYQPKITW-RGEVRSLEALVRWQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 557 RKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQAKGIEMQAAINVSAQDIASPSFHSALVRTLKKYNVDPTL 636
Cdd:PRK10060 447 SPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 637 ITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQTSLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITL 716
Cdd:PRK10060 527 IDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAV 606
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 490726579 717 GHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLKAELLEQWLKEY 767
Cdd:PRK10060 607 AQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRY 657
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
519-759 |
6.95e-78 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 250.60 E-value: 6.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 519 ELKQAIsdDDGQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQA 598
Cdd:smart00052 3 ELRQAL--ENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 599 KGIEM-QAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQT 677
Cdd:smart00052 81 QGPPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 678 SLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLKA 757
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 490726579 758 EL 759
Cdd:smart00052 241 DD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
518-754 |
1.24e-65 |
|
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: 217.96 E-value: 1.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 518 DELKQAISDddGQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQ 597
Cdd:pfam00563 2 RALRRALEN--GEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 598 AKGiEMQAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQT 677
Cdd:pfam00563 80 LGP-DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726579 678 SLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRP 754
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
345-484 |
7.08e-18 |
|
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: 81.61 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 345 QARHDSLTGFYNRSAMLEVLDDELTPSTQY----TLVAIDIKGLRHINDKLGPRVGDECLKAVANRISG---FSDELGgf 417
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFqrsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSsvrGSDVVG-- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726579 418 haRIGGDEFLTVFPSAAARERESGIVGLMAQLLACYTI--KTLKINLRFSAGVVEYPMQGLASDDLMRR 484
Cdd:TIGR00254 79 --RYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvaGSETLTVTVSIGVACYPGHGLTLEELLKR 145
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
263-348 |
4.43e-09 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 59.21 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 263 LLFTLIIMAILTMLVGVITSSLLANNLTTPLSQLAVIARQFAQGNYAFEFNASKQStEIATLANAFDNMGNDINEREQKI 342
Cdd:COG5000 7 FLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDD-EIGELARAFNRMTDQLKEQREEL 85
|
....*.
gi 490726579 343 SFQARH 348
Cdd:COG5000 86 EERRRY 91
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
140-342 |
2.26e-05 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 47.71 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 140 SSFVVLNNQLYQVILLPVRAPRTVAYSLVGFKIDDEVALELKNLTGMDVSFIAEQDNLVRSSLLNRPEFFSPKNYFNTTT 219
Cdd:COG2972 32 IILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLILLLLLLLLLLLILLLSLLLLLALILLLAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 220 TTRLFGDYPVYKNQDIMLPSLQGDAVTILLSADLTQSYNDFENLLFTLIIMAILTMLVGVITSSLLANNLTTPLSQLAVI 299
Cdd:COG2972 112 LLLLSILLLILGLLLIILLLLSLLGWTLVSLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490726579 300 ARQFAQGNyaFEFNASKQSTEIATLANAFDNMGNDINEREQKI 342
Cdd:COG2972 192 MKKVEKGD--LVRLEVSGNDEIGILARSFNEMVERIKELIEEV 232
|
|
| dCache_3 |
pfam14827 |
Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor ... |
62-191 |
5.16e-05 |
|
Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor domains of sensor histidine kinase of E. coli DcuS. This domain forms one of the components of the two-component signalling system that allows bacteria to adapt to changing environments. The ability of bacteria to monitor and adapt to their environment is crucial to their survival, and two-component signal transduction systems mediate most of these adaptive responses. One component is a histidine kinase sensor - this domain - most commonly part of a homodimeric transmembrane sensor protein, and the second component is a cytoplasmic response regulator. The two components interact in tandem through a phospho-transfer cascade.
Pssm-ID: 464339 [Multi-domain] Cd Length: 235 Bit Score: 45.48 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 62 LLTAAKVLTADFGFKQAVATRDAGTISSVLFNHSQRIDAELMLLIDLSGKLIsANTNADLYPQNLKPLLDELLTSPEQSS 141
Cdd:pfam14827 26 LLALAELVASSPGVAEAISEGDREQLERLLDSRWQVLGLEQIVLHDADGTSI-LRLEPSTLGDDLSLFRLTIQSTLRGET 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 490726579 142 ----FVVLNNQLYQVILLPVR-APRTVAYSLVGFKIDDeVALELKNLTGMDVSFI 191
Cdd:pfam14827 105 allgLECGVAGCGFRVVIPVLsAGKHVGAVVFGVSLDD-FLREFAEATGADIAIL 158
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
290-331 |
2.69e-03 |
|
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.
Pssm-ID: 381743 [Multi-domain] Cd Length: 45 Bit Score: 36.27 E-value: 2.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490726579 290 TTPLSQLAVIARQFAQGNYAFEFNASKQStEIATLANAFDNM 331
Cdd:cd06225 1 TRPLRRLTEAARRIAEGDLDVRVPVRSKD-EIGELARAFNQM 41
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
337-766 |
6.18e-125 |
|
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: 389.13 E-value: 6.18e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 337 EREQKISFQARHDSLTGFYNRSAMLEVLDDELT----PSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGFSD 412
Cdd:COG5001 242 RAEERLRHLAYHDPLTGLPNRRLFLDRLEQALArarrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLR 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 413 ElGGFHARIGGDEFLTVFPSAAAREResgIVGLMAQLLAC----YTIKTLKINLRFSAGVVEYPMQGLASDDLMRRVLIA 488
Cdd:COG5001 322 E-GDTVARLGGDEFAVLLPDLDDPED---AEAVAERILAAlaepFELDGHELYVSASIGIALYPDDGADAEELLRNADLA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 489 VDNA-TDSQDSIHYYQNGEDEAHLDRLKMLDELKQAIsdDDGQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPEL 567
Cdd:COG5001 398 MYRAkAAGRNRYRFFDPEMDERARERLELEADLRRAL--ERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAE 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 568 FIDLAEQSGLIVELTSWVVNTVVSQVADWQAKGIE-MQAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDM 646
Cdd:COG5001 476 FIPLAEETGLIVPLGEWVLREACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESAL 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 647 IENEEKGIKALQNLKAIGVKISLDDYGVGQTSLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVA 726
Cdd:COG5001 556 LEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVA 635
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 490726579 727 EGVENRDSLDLLKLMHCDHAQGYYLSRPLKAELLEQWLKE 766
Cdd:COG5001 636 EGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
234-765 |
5.08e-98 |
|
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: 315.57 E-value: 5.08e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 234 DIMLPSLQGDAVTILLSADLTQSYNDFENLLFTLIIMAILTMLVGVITSSLLANNLTTPLSQLAVIARQFAQGNYAFEFN 313
Cdd:COG2200 41 LLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 314 ASKQSTEIATLANAFDNMGNDINEREQKISFQARHDSLTGFYNRS------AMLEVLDDELTPSTQYTLVAIDIKGLRHI 387
Cdd:COG2200 121 LLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRrlllllLLLLLLLLLALALLALLLLLLLLLLLLLD 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 388 NDKLGPRVGDECLKAVANRISGFSDELGGFHARIGGDEFLTVFPSAAARERESGIVGLMAQLLACYTIKTLKINLRFSAG 467
Cdd:COG2200 201 NDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 468 VVEYPMQGLASDDLMRRVLIAVDNATDSQDSIHYYQNGEDEAHLDRLKMLDELKQAIsdDDGQLFMTYQPKLHLHTQKIN 547
Cdd:COG2200 281 GAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRLALESELREAL--EEGELRLYYQPIVDLRTGRVV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 548 KVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQAKGIEMQAAINVSAQDIASPSFHSALVRTL 627
Cdd:COG2200 359 GYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELL 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 628 KKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQTSLGRLKMLPIDELKLDKCFILKLDESRKDQ 707
Cdd:COG2200 439 AEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQ 518
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 490726579 708 YIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLKAELLEQWLK 765
Cdd:COG2200 519 AIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALLR 576
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
519-758 |
3.91e-88 |
|
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: 277.50 E-value: 3.91e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 519 ELKQAIsdDDGQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQA 598
Cdd:cd01948 2 DLRRAL--ERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 599 KGIEMQAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQTS 678
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 679 LGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLKAE 758
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
332-767 |
4.20e-81 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 272.71 E-value: 4.20e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 332 GNDINER---EQKISFQARHDSLTGFYNRSAMLEVLDDELT--PSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAVANR 406
Cdd:PRK10060 220 GTDITEErraQERLRILANTDSITGLPNRNAIQELIDHAINaaDNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 407 ISGFSDElGGFHARIGGDEFLTVFPSAAARERESgivglMAQLLacytIKTLKINLRF---------SAGVVEYPMQGLA 477
Cdd:PRK10060 300 ILSCLEE-DQTLARLGGDEFLVLASHTSQAALEA-----MASRI----LTRLRLPFRIglievytgcSIGIALAPEHGDD 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 478 SDDLMRRVLIAVDNATDSQDSIHYYQNGEDEAHLDRLKMLD-ELKQAIsdDDGQLFMTYQPKLHLhTQKINKVESLIRWQ 556
Cdd:PRK10060 370 SESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDtNLRKAL--ENDQLVIHYQPKITW-RGEVRSLEALVRWQ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 557 RKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQAKGIEMQAAINVSAQDIASPSFHSALVRTLKKYNVDPTL 636
Cdd:PRK10060 447 SPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 637 ITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQTSLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITL 716
Cdd:PRK10060 527 IDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAV 606
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 490726579 717 GHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLKAELLEQWLKEY 767
Cdd:PRK10060 607 AQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRY 657
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
519-759 |
6.95e-78 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 250.60 E-value: 6.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 519 ELKQAIsdDDGQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQA 598
Cdd:smart00052 3 ELRQAL--ENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 599 KGIEM-QAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQT 677
Cdd:smart00052 81 QGPPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 678 SLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLKA 757
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 490726579 758 EL 759
Cdd:smart00052 241 DD 242
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
306-767 |
2.10e-66 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 235.43 E-value: 2.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 306 GNYAFEFNASKQ-STEIATLANAFDNMGNDINERE---QKISFQARHDSLTGFYNRSAMLEVLDDELTPSTQYTLVAIDI 381
Cdd:PRK11359 332 GTLQIKTSSGAEtSAFIERVADISQHLAALALEQEksrQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 382 KGLRHINDKLGPRVGDECLKAVANRISGFSDElGGFHARIGGDEFLTVFPSAAAREresgiVGLMAQLL-----ACYTIK 456
Cdd:PRK11359 412 DHFQDVIDSLGYAWADQALLEVVNRFREKLKP-DQYLCRIEGTQFVLVSLENDVSN-----ITQIADELrnvvsKPIMID 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 457 TLKINLRFSAGVvEYPMqGLASDDLMRRVLIAVDN-ATDSQDSIHYYQNGEDEAHLDRLKMLDELKQAISDddGQLFMTY 535
Cdd:PRK11359 486 DKPFPLTLSIGI-SYDV-GKNRDYLLSTAHNAMDYiRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISN--NQLKLVY 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 536 QPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQAKGIEMQA-AINVSAQDI 614
Cdd:PRK11359 562 QPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPAlSVNLSALHF 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 615 ASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQTSLGRLKMLPIDELKLDK 694
Cdd:PRK11359 642 RSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDK 721
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726579 695 CFILKLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLKAELLEQWLKEY 767
Cdd:PRK11359 722 SFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSV 794
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
518-754 |
1.24e-65 |
|
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: 217.96 E-value: 1.24e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 518 DELKQAISDddGQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQ 597
Cdd:pfam00563 2 RALRRALEN--GEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 598 AKGiEMQAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQT 677
Cdd:pfam00563 80 LGP-DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726579 678 SLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRP 754
Cdd:pfam00563 159 SLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
513-764 |
3.42e-65 |
|
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: 3.42e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 513 RLKMLDELKQAISDddGQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQ 592
Cdd:COG4943 269 RLSPRRRLRRAIKR--REFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRD 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 593 VADWQAKGIEMQAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIeNEEKGIKALQNLKAIGVKISLDDY 672
Cdd:COG4943 347 LGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDF 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 673 GVGQTSLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLS 752
Cdd:COG4943 426 GTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFA 505
|
250
....*....|..
gi 490726579 753 RPLKAELLEQWL 764
Cdd:COG4943 506 KPLPAEEFIAWL 517
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
260-763 |
1.59e-50 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 188.23 E-value: 1.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 260 FENLLFTLIIMA-ILTMLVGVITSSLLANNLTTPLSQLAVIARQfAQGNYAFEFNASKQSTEIATLANAFDNMGNDINER 338
Cdd:PRK11829 146 LSAMLSTYLLLAlVLSVSIAWCINRLIIHPLRAMAKELEDIGDH-GVLHHQLTLPAHHQDDELGVLVRNYNRNQQLLADA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 339 EQKISFQARHDSLTGFYNRSAMLEVLDDELTPSTQ---YTLVAIDIKGLRHINDKLGPRVGDECLKAVANRI-SGFSDel 414
Cdd:PRK11829 225 YADMGRISHRFPVTELPNRSLFISLLEKEIASSTRtdhFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIeQCIDD-- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 415 GGFHARIGGDEFL-----TVFPSAAARERESgivgLMAQLLACYTIKTLKINLRFSAGVVEYPMQGLASDDLMRRVLIAV 489
Cdd:PRK11829 303 SDLLAQLSKTEFAvlargTRRSFPAMQLARR----IMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAM 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 490 DNA-TDSQDSIHYYQNGEDEAHLDRLKMLDELKQAISDDDGQLFMtyQPKLHLHTQKINKVESLIRWQRKDGSWVNPELF 568
Cdd:PRK11829 379 MAAhHEGRNQIMVFEPHLIEKTHKRLTQENDLLQAIENHDFTLFL--QPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGF 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 569 IDLAEQSGLIVELTSWVVNTVVSQVADWQAKGIEMQAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIE 648
Cdd:PRK11829 457 VHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQ 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 649 NEEKGIKALQNLKAIGVKISLDDYGVGQTSLGRL---KMLPIDELKLDKCFILKLDEsrkDQYIVQSSITLGHQLGFSVV 725
Cdd:PRK11829 537 DLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLPE---DDAIARIISCVSDVLKVRVM 613
|
490 500 510
....*....|....*....|....*....|....*....
gi 490726579 726 AEGVENRDSLDLLKLMHCDHAQGYYLSRPL-KAELLEQW 763
Cdd:PRK11829 614 AEGVETEEQRQWLLEHGIQCGQGFLFSPPLpRAEFEAQY 652
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
218-766 |
8.29e-49 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 182.99 E-value: 8.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 218 TTTTRLFgDYPVyknqDIMLP--SLQGDA-----VTILLSADLTQSYNDFENLLFTLIIMAILTMLVGVITSSLLANNLT 290
Cdd:PRK13561 97 VMVTRLF-ELPV----QISLPvySLERPAnpqplAYLVLQADSFRMYKFVMSALSTLVTIYLLLSLILTVAISWCINRLI 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 291 tpLSQLAVIARQF------AQGNYAFEFNASKQSTEIATLANAFDNMGNDINEREQKISFQARHDSLTGFYNRSAMLEVL 364
Cdd:PRK13561 172 --VHPLRNIARELndippqELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDLPNKALLMALL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 365 DDELTPSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGFSDELGGFhARIGGDEFLTVFPSAAAREREsgiVG 444
Cdd:PRK13561 250 EQVVARKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLSPRMVL-AQISGYDFAIIANGVKEPWHA---IT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 445 LMAQLLACYTIKTL--KINLRFSA--GVVEYpMQGLASDDLMRRVLIAVDNATDS-QDSIHYYQNGEDEAHLDRLKMLDE 519
Cdd:PRK13561 326 LGQQVLTIINERLPiqRIQLRPSCsiGIAMF-YGDLTAEQLYSRAISAAFTARRKgKNQIQFFDPQQMEAAQKRLTEESD 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 520 LKQAISDDDGQLFMtyQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQAK 599
Cdd:PRK13561 405 ILNALENHQFAIWL--QPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQER 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 600 GIEMQAAINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQTSL 679
Cdd:PRK13561 483 GIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGL 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 680 GRL---KMLPIDELKLDKCFILKLDEsrkDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLK 756
Cdd:PRK13561 563 RQLqhmKSLPIDVLKIDKMFVDGLPE---DDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALP 639
|
570
....*....|.
gi 490726579 757 AELLE-QWLKE 766
Cdd:PRK13561 640 IEIFEeRYLEE 650
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
341-762 |
8.63e-36 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 145.97 E-value: 8.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 341 KISFQARHDSLTGFYNR----SAMLEVLDDELTPSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGF---SDE 413
Cdd:PRK09776 660 QLSYSASHDALTHLANRasfeKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMlrsSDV 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 414 LggfhARIGGDEFLTVFPS---AAARERESGIVGlmaqllacytiktlKIN-LRF-----------SAGVVEYPMQGLAS 478
Cdd:PRK09776 740 L----ARLGGDEFGLLLPDcnvESARFIATRIIS--------------AINdYHFpwegrvyrvgaSAGITLIDANNHQA 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 479 DDLMRRVLIAVDNATDSQDSIHY-YQNGEDEAHLDRlKMLDELKQAISDDDGQLFMTYQPKLH-LHTQKINKVESLIRWQ 556
Cdd:PRK09776 802 SEVMSQADIACYAAKNAGRGRVTvYEPQQAAAHSEH-RALSLAEQWRMIKENQLMMLAHGVASpRIPEARNHWLISLRLW 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 557 RKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVAD-WQAKGIEMqaAINVSAQDIASPSFHSALVRTLKKYNVDPT 635
Cdd:PRK09776 881 DPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKaVASKGLSI--ALPLSVAGLSSPTLLPFLLEQLENSPLPPR 958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 636 LITVELTERDMIENEEKGIKALQNLKAIGVKISLDDYGVGQTSLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSIT 715
Cdd:PRK09776 959 LLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQG 1038
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 490726579 716 LGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLK-AELLEQ 762
Cdd:PRK09776 1039 HAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPlDLLLNS 1086
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
529-766 |
1.23e-32 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 133.19 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 529 GQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQA---KGIEMqa 605
Cdd:PRK10551 275 GQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKvlpVGAKL-- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 606 AINVSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEkGIKALQNLKAIGVKISLDDYGVGQTSLGRLKML 685
Cdd:PRK10551 353 GINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEE-ATKLFAWLHSQGIEIAIDDFGTGHSALIYLERF 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 686 PIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRPLKAELLEQWLK 765
Cdd:PRK10551 432 TLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVRWLK 511
|
.
gi 490726579 766 E 766
Cdd:PRK10551 512 E 512
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
243-488 |
4.70e-29 |
|
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: 117.39 E-value: 4.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 243 DAVTILLSADLTQSYNDFENLLFTLIIMAILTMLVGVITSSLLANNLTTPLSQLAVIARQFAQGNYAFEFNASKQSTEIA 322
Cdd:COG2199 12 LLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 323 TLANAFDNMgNDINEREQKISFQARHDSLTGFYNRSAMLEVLDDELTPSTQY----TLVAIDIKGLRHINDKLGPRVGDE 398
Cdd:COG2199 92 LLLLALEDI-TELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREgrplALLLIDLDHFKRINDTYGHAAGDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 399 CLKAVANRISGFSDElGGFHARIGGDEFLTVFPS---AAARERESGIVGLMAQLlaCYTIKTLKINLRFSAGVVEYPMQG 475
Cdd:COG2199 171 VLKEVARRLRASLRE-SDLVARLGGDEFAVLLPGtdlEEAEALAERLREALEQL--PFELEGKELRVTVSIGVALYPEDG 247
|
250
....*....|...
gi 490726579 476 LASDDLMRRVLIA 488
Cdd:COG2199 248 DSAEELLRRADLA 260
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
347-484 |
4.88e-28 |
|
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: 110.34 E-value: 4.88e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 347 RHDSLTGFYNRSAMLEVLDDEL----TPSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGFSDElGGFHARIG 422
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLararRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRE-SDLVARLG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726579 423 GDEFLTVFPSAAARERESGIVGLMAQLLACYTIKTLKINLRFSAGVVEYPMQGLASDDLMRR 484
Cdd:cd01949 80 GDEFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRR 141
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
346-488 |
9.68e-24 |
|
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: 98.09 E-value: 9.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 346 ARHDSLTGFYNRSAMLEVLDDEL----TPSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGF---SDELggfh 418
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELqralREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSlrrSDLV---- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726579 419 ARIGGDEFLTVFP---SAAARERESGIVGLMAQLLACYTIKTLKINLRFSAGVVEYPMQGLASDDLMRRVLIA 488
Cdd:pfam00990 77 ARLGGDEFAILLPetsLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTA 149
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
345-492 |
1.79e-23 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 97.70 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 345 QARHDSLTGFYNRSAMLEVLDDEL----TPSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGFSdELGGFHAR 420
Cdd:smart00267 2 LAFRDPLTGLPNRRYFEEELEQELqraqRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCL-RPGDLLAR 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490726579 421 IGGDEFLTVFPSAAARERESGIVGLMAQLLACYTIKTLKINLRFSAGVVEYPMQGLASDDLMRRVLIAVDNA 492
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQA 152
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
345-484 |
7.08e-18 |
|
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: 81.61 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 345 QARHDSLTGFYNRSAMLEVLDDELTPSTQY----TLVAIDIKGLRHINDKLGPRVGDECLKAVANRISG---FSDELGgf 417
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFqrsfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSsvrGSDVVG-- 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726579 418 haRIGGDEFLTVFPSAAARERESGIVGLMAQLLACYTI--KTLKINLRFSAGVVEYPMQGLASDDLMRR 484
Cdd:TIGR00254 79 --RYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEvaGSETLTVTVSIGVACYPGHGLTLEELLKR 145
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
328-470 |
4.03e-10 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 63.11 E-value: 4.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 328 FDNMgndiNEREQKISFQARHDSLTGFYNRSAMLEVLDDEL----TPSTQYTLVAIDIKGLRHINDKLGPRVGDECLKAV 403
Cdd:PRK15426 384 VSNM----FVLQSSLQWQAWHDPLTRLYNRGALFEKARALAkrcqRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHA 459
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726579 404 ANRISGfSDELGGFHARIGGDEFLTVFP------SAAARERESGIVGLMAQLLACYTIktlkinLRFSA--GVVE 470
Cdd:PRK15426 460 AGLISS-SLRAQDVAGRVGGEEFCVVLPgaslaeAAQVAERIRLRINEKEILVAKSTT------IRISAslGVSS 527
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
53-671 |
1.29e-09 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 61.67 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 53 QYLSAKESLLLTAAKVLTADFGFKQAVATRDAGTISSVLFNHSQRIDAELMLLIDLSGKLISANTNADLYPQNLKPLLDE 132
Cdd:COG2770 1 LLLLLLALLLLLLLLLLLLLLAGALLVLALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 133 LLTSPEQSSFVVLNNQLYQVILLPVRAPRTVAYSLVGFKIDDEVALELKNLTGMDVSFIAEQDNLVRSSLLNRPEFFSPK 212
Cdd:COG2770 81 LLSLVALAALLLALLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 213 NYFNTTTTTRLFGDYPVYKNQDIMLPSLQGDAVTILLSADLTQSYNDFEnLLFTLIIMAILTMLVGVITSSLLANNLTTP 292
Cdd:COG2770 161 AAALALALGAGELLLLADLAAAIAALLAALLLLLLGGLLLVVLLEAALA-ALLLLLLLALLALLLALLLALLLARRITRP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 293 LSQLAVIARQFAQGNYAFEFNASKQsTEIATLANAFDNMGNDINEREQKISFQARHDSLTGFYNRSAMLEVLDDELTPST 372
Cdd:COG2770 240 LRRLAEAARRIAAGDLDVRIPVSRK-DEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 373 QYTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGFSDELGGFHARIGGDEFLTVFPS----AAARERESGIVGLMAQ 448
Cdd:COG2770 319 ALLLLAAAALLLELLLLLLLALLLLLLLAADLLLALALAALLLLLALELLLEAELLVLLAlealALEAELAAVLALLAAL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 449 LLACYTIKTLKINLRFSAGVVEYPMQGLASDDLMRRVLIAVDNATDSQDSIHYYQNGEDEAHLDRLKMLDELKQAISDDD 528
Cdd:COG2770 399 AAALLLLELALEELVLALLALALLALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAAL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 529 GQLFMTYQPKLHLHTQKINKVESLIRWQRKDGSWVNPELFIDLAEQSGLIVELTSWVVNTVVSQVADWQAKGIEMQAAIN 608
Cdd:COG2770 479 LLLAALGALELLLLEEEEEAGAAAEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLAL 558
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490726579 609 VSAQDIASPSFHSALVRTLKKYNVDPTLITVELTERDMIENEEKGIKALQNLKAIGVKISLDD 671
Cdd:COG2770 559 AAVEAAALLLAALLLAAVAALLELAALLLLLLAAAEALAALELELAAAAEAALAEAELLEVAA 621
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
607-754 |
3.41e-09 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 59.82 E-value: 3.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 607 INVSAQDIASPSFHSalvrtlkkynVDPTLITVELTERdmIENEEKGIKALQNLKAIGVKISLDDYgVGQTSLGRLkmLP 686
Cdd:COG3434 66 INFTEELLLSDLPEL----------LPPERVVLEILED--VEPDEELLEALKELKEKGYRIALDDF-VLDPEWDPL--LP 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726579 687 -IDELKLDkcfILKLDESRKDQYIvqssiTLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQGYYLSRP 754
Cdd:COG3434 131 lADIIKID---VLALDLEELAELV-----ARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
263-348 |
4.43e-09 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 59.21 E-value: 4.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 263 LLFTLIIMAILTMLVGVITSSLLANNLTTPLSQLAVIARQFAQGNYAFEFNASKQStEIATLANAFDNMGNDINEREQKI 342
Cdd:COG5000 7 FLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDD-EIGELARAFNRMTDQLKEQREEL 85
|
....*.
gi 490726579 343 SFQARH 348
Cdd:COG5000 86 EERRRY 91
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
349-484 |
7.39e-09 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 58.76 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 349 DSLTGFYNRSAM---LEVLDDELTPSTQ-YTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISG---FSDELggfhARI 421
Cdd:PRK09581 295 DGLTGLHNRRYFdmhLKNLIERANERGKpLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNnirGTDLI----ARY 370
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490726579 422 GGDEFLTVFP----SAAAR--ERESGIVGLMAQLLAcytIKTLKINLRFSAGVVEYPMQGLASDDLMRR 484
Cdd:PRK09581 371 GGEEFVVVMPdtdiEDAIAvaERIRRKIAEEPFIIS---DGKERLNVTVSIGVAELRPSGDTIEALIKR 436
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
566-754 |
6.32e-08 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 56.02 E-value: 6.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 566 ELFIDLAEQSGLIVELTSWVVNTVVSQVADWQAKGIemqaAINVSAQDIASPSFHSALVRTLKKYN-VDPTLITVELTER 644
Cdd:PRK11059 451 ELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEENL----SINLSVDSLLSRAFQRWLRDTLLQCPrSQRKRLIFELAEA 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 645 DMIENEEKGIKALQNLKAIGVKISLDDygVGQT--SLGRLKMLPIDELKLDKCFILKLDESRKDQYIVQSSITLGHQLGF 722
Cdd:PRK11059 527 DVCQHISRLRPVLRMLRGLGCRLAVDQ--AGLTvvSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTET 604
|
170 180 190
....*....|....*....|....*....|..
gi 490726579 723 SVVAEGVENRDSLDLLKLMHCDHAQGYYLSRP 754
Cdd:PRK11059 605 QVFATGVESREEWQTLQELGVSGGQGDFFAES 636
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
337-468 |
1.29e-07 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 54.45 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 337 EREQKISFQARHDSLTGFYNRSAMLEVLDDELTPSTQY----TLVAIDIKGLRHINDKLGPRVGDECLKAVANRIS---G 409
Cdd:PRK10245 196 EHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHhrdaTLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQitlR 275
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490726579 410 FSDELGgfhaRIGGDEFLTVFPSAAArerESGIV-------GLMAQLLACytikTLKINLRFSAGV 468
Cdd:PRK10245 276 GSDVIG----RFGGDEFAVIMSGTPA---ESAITamsrvheGLNTLRLPN----APQVTLRISVGV 330
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
349-485 |
1.99e-07 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 53.53 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 349 DSLTGFYNRSAMLEVLDDELTPSTQ--YTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGF---SDELggfhARIGG 423
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQLRNREPqnLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWtrdYETV----YRYGG 207
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490726579 424 DEFLTVFPsaAARERESGIVGL-MAQLLAC--YTIKTLKINLRFSAGVVEYpMQGLASDDLMRRV 485
Cdd:PRK09894 208 EEFIICLK--AATDEEACRAGErIRQLIANhaITHSDGRINITATFGVSRA-FPEETLDVVIGRA 269
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
346-430 |
2.08e-06 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 50.78 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 346 ARHDSLTGFYNRSA----MLEVLDDELTPSTQyTLVAIDIKGLRHINDKLGPRVGDECLKAVANRISgfsdELGGFHA-- 419
Cdd:PRK09966 248 ALHDPLTGLANRAAfrsgINTLMNNSDARKTS-ALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLA----EFGGLRHka 322
|
90
....*....|..
gi 490726579 420 -RIGGDEFLTVF 430
Cdd:PRK09966 323 yRLGGDEFAMVL 334
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
140-342 |
2.26e-05 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 47.71 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 140 SSFVVLNNQLYQVILLPVRAPRTVAYSLVGFKIDDEVALELKNLTGMDVSFIAEQDNLVRSSLLNRPEFFSPKNYFNTTT 219
Cdd:COG2972 32 IILLLLLLLILLLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLLILLLLLLLLLLLILLLSLLLLLALILLLAL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 220 TTRLFGDYPVYKNQDIMLPSLQGDAVTILLSADLTQSYNDFENLLFTLIIMAILTMLVGVITSSLLANNLTTPLSQLAVI 299
Cdd:COG2972 112 LLLLSILLLILGLLLIILLLLSLLGWTLVSLIPKSELFRGLFSLRRLILLIILLLLLLALLLSYLLSRSITRPIKRLKKA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490726579 300 ARQFAQGNyaFEFNASKQSTEIATLANAFDNMGNDINEREQKI 342
Cdd:COG2972 192 MKKVEKGD--LVRLEVSGNDEIGILARSFNEMVERIKELIEEV 232
|
|
| dCache_3 |
pfam14827 |
Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor ... |
62-191 |
5.16e-05 |
|
Double sensory domain of two-component sensor kinase; Cache_3 is the periplasmic sensor domains of sensor histidine kinase of E. coli DcuS. This domain forms one of the components of the two-component signalling system that allows bacteria to adapt to changing environments. The ability of bacteria to monitor and adapt to their environment is crucial to their survival, and two-component signal transduction systems mediate most of these adaptive responses. One component is a histidine kinase sensor - this domain - most commonly part of a homodimeric transmembrane sensor protein, and the second component is a cytoplasmic response regulator. The two components interact in tandem through a phospho-transfer cascade.
Pssm-ID: 464339 [Multi-domain] Cd Length: 235 Bit Score: 45.48 E-value: 5.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 62 LLTAAKVLTADFGFKQAVATRDAGTISSVLFNHSQRIDAELMLLIDLSGKLIsANTNADLYPQNLKPLLDELLTSPEQSS 141
Cdd:pfam14827 26 LLALAELVASSPGVAEAISEGDREQLERLLDSRWQVLGLEQIVLHDADGTSI-LRLEPSTLGDDLSLFRLTIQSTLRGET 104
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 490726579 142 ----FVVLNNQLYQVILLPVR-APRTVAYSLVGFKIDDeVALELKNLTGMDVSFI 191
Cdd:pfam14827 105 allgLECGVAGCGFRVVIPVLsAGKHVGAVVFGVSLDD-FLREFAEATGADIAIL 158
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
266-348 |
6.81e-05 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 46.03 E-value: 6.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 266 TLIIMAILTMLVGVITSSLLANNLTTPLSQLAVIARQFAQGNYAFEFNASkQSTEIATLANAFDNMGNDINEREQKISFQ 345
Cdd:COG3850 119 LALLRLLLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVS-GRDELGTLARAFNRMADELQELYAELEEE 197
|
...
gi 490726579 346 ARH 348
Cdd:COG3850 198 EEL 200
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
669-761 |
1.77e-04 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 43.84 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 669 LDDYGVGQTSLGRLKMLPIDELKLDK-CFILkLDESRKDQYIVQSSITLGHQLGFSVVAEGVENRDSLDLLKLMHCDHAQ 747
Cdd:PRK11596 157 LDDFGTGMANFSALSEVRYDYIKVAReLFIM-LRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQ 235
|
90
....*....|....
gi 490726579 748 GYYLSRPLKAELLE 761
Cdd:PRK11596 236 GYFLSRPAPFETLE 249
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
375-468 |
1.85e-03 |
|
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: 39.26 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 375 TLVAIDIKGLRHINDKLGPRVGDECLKAVANRISGFSDELGGFHARIGGDEFLTVFPS---AAARERESGIVGLMAQLLa 451
Cdd:cd07556 3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLKIKTIGDEFMVVSGLdhpAAAVAFAEDMREAVSALN- 81
|
90
....*....|....*..
gi 490726579 452 cytiKTLKINLRFSAGV 468
Cdd:cd07556 82 ----QSEGNPVRVRIGI 94
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
95-331 |
2.45e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 41.16 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 95 SQRIDAELMLLIDLSGKLISANTNADLYPQNLKPLLDELLTSPEQSSFVVLNNQLYQVILLPVRAPRTVAYSLVGFKIDD 174
Cdd:COG0840 12 LALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLALLLALLLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490726579 175 EVALELKNLTGMDVSFIAEQDNLVRSSLLNRPEFFSPKNYFNTTTTTRLFGDYPVYKNQDIMLPSLQGDAVTILLSADLT 254
Cdd:COG0840 92 LLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAALAALLEAAA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490726579 255 QSYNDFENLLFTLIIMAILTMLVGVITSSLLANNLTTPLSQLAVIARQFAQGNYAFEFNASKQStEIATLANAFDNM 331
Cdd:COG0840 172 LALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKD-EIGQLADAFNRM 247
|
|
| HAMP |
cd06225 |
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; ... |
290-331 |
2.69e-03 |
|
Histidine kinase, Adenylyl cyclase, Methyl-accepting protein, and Phosphatase (HAMP) domain; HAMP is a signaling domain which occurs in a wide variety of signaling proteins, many of which are bacterial. The HAMP domain consists of two alpha helices connected by an extended linker. The structure of the Af1503 HAMP dimer from Archaeoglobus fulgidus has been solved using nuclear magnetic resonance, revealing a parallel four-helix bundle; this structure has been confirmed by cross-linking analysis of HAMP domains from the Escherichia coli aerotaxis receptor Aer. It has been suggested that the four-helix arrangement can rotate between the unusually packed conformation observed in the NMR structure and a canonical coiled-coil arrangement. Such rotation may coincide with signal transduction, but a common mechanism by which HAMP domains relay a variety of input signals has yet to be established.
Pssm-ID: 381743 [Multi-domain] Cd Length: 45 Bit Score: 36.27 E-value: 2.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 490726579 290 TTPLSQLAVIARQFAQGNYAFEFNASKQStEIATLANAFDNM 331
Cdd:cd06225 1 TRPLRRLTEAARRIAEGDLDVRVPVRSKD-EIGELARAFNQM 41
|
|
| |
