|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
165-642 |
1.07e-48 |
|
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: 179.98 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 165 FLILIASLAVAFLILREVFKPLKAVEHQAHLVTRKRFTLNEEIPIARELRTVTKAINNMVINLQSTFDSLTKQTQALTEE 244
Cdd:COG2200 75 LLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 245 VYIDSLTGLGNRKLFENHFSSVVDTITTDAPLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKIIGNLTNSKIFRL 324
Cdd:COG2200 155 LLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 325 NGSTFIALIPYDTQFLNRTRLEITDAFSKQKNSLHVNGFANFAILEVNKGSSIGSVLSALDTGSTI---------GDTID 395
Cdd:COG2200 235 GGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAaaaaaagggRGRVV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 396 TNKIDKDTLFSVNQWRTLIQSIIDSGEVSFSVQPVKRANSqNKQCYFEAFAHFTH-EGEKVNNGHLFAMAEKLNLTEELD 474
Cdd:COG2200 315 FFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRT-GRVVGYEALLRWRHpDGGLISPAEFIPAAERSGLIVELD 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 475 ----KKIIRNFVNIKEQYPDDVFALNVSKASLYSADFIQWLTLYAHTKPVIKTNLIFELHEISLLYNVHIASKHIDAIKD 550
Cdd:COG2200 394 rwvlERALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 551 IGINVCIEHFGTSLTSFRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLG 630
Cdd:COG2200 474 LGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELG 553
|
490
....*....|..
gi 1778737331 631 CDGVQGNLIMEP 642
Cdd:COG2200 554 CDYAQGYLFGRP 565
|
|
| LapD_MoxY_N |
pfam16448 |
LapD/MoxY periplasmic domain; This domain is the N-terminal periplasmic domain of the LapD and ... |
35-154 |
2.06e-48 |
|
LapD/MoxY periplasmic domain; This domain is the N-terminal periplasmic domain of the LapD and MoxY receptor proteins.
Pssm-ID: 465117 Cd Length: 124 Bit Score: 165.88 E-value: 2.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 35 VETTRDYLQTQMGSHAQDTATSLGLSISPYLEPENLVIAETMATAIFDSGYYKEIKFTNSQSQVVFDLENPKRVESVPNW 114
Cdd:pfam16448 5 VNNARSYLEQQLQSHAQDTATSLGLSLSPYLENEDPVTAETMINAIFDSGYYRSIRLTDPDGKVLVERQNPVLIEGVPQW 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1778737331 115 FIALSSLKAPTMQSELNNGWIMAGILEVTSHTGQSYVTLW 154
Cdd:pfam16448 85 FIRLVPLEPPPGEAEISSGWLQLGTLEVESHPGYAYQELW 124
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
418-642 |
5.47e-46 |
|
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: 163.26 E-value: 5.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 418 IDSGEVSFSVQPVKRANSqNKQCYFEAFAHFTH-EGEKVNNGHLFAMAEKLNLTEELDKKIIRNFVNI---KEQYPDDVF 493
Cdd:pfam00563 8 LENGEFVLYYQPIVDLRT-GRVVGYEALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADlaqLQLGPDIKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 494 ALNVSKASLYSADFIQWLTLYAHTKPVIKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTSFRYLQGL 573
Cdd:pfam00563 87 SINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1778737331 574 DIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:pfam00563 167 PPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
414-639 |
3.67e-39 |
|
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: 144.61 E-value: 3.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 414 IQSIIDSGEVSFSVQPVKRANSQnKQCYFEAFAHFTH-EGEKVNNGHLFAMAEKLNLTEELDKKIIRN----FVNIKEQY 488
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTG-RIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEacrqLARWQAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 489 PDDVFALNVSKASLYSADFIQWL--TLYAHtkPVIKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTS 566
Cdd:cd01948 82 PDLRLSVNLSARQLRDPDFLDRLleLLAET--GLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778737331 567 FRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLI 639
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLF 232
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
412-642 |
1.83e-36 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 136.96 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 412 TLIQSIIDSGEVSFSVQPVkrANSQNKQC-YFEAFAHFTH-EGEKVNNGHLFAMAEKLNLTEELDKKIIRNFVN----IK 485
Cdd:smart00052 2 RELRQALENGQFLLYYQPI--VSLRTGRLvGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQqlaeWQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 486 EQYPDDV-FALNVSKASLYSADFIQWLTLYAHTKPVIKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSL 564
Cdd:smart00052 80 AQGPPPLlISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778737331 565 TSFRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
448-642 |
1.74e-24 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 109.38 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 448 FTHEGEKVNNGHLFAMAEKLNLTEELDKKIIRNFVnikEQY------PDDVFALNVSKASLYSADFIQWL-TLYAHTkPV 520
Cdd:PRK09776 880 WDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFF---RQAakavasKGLSIALPLSVAGLSSPTLLPFLlEQLENS-PL 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 521 IKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTSFRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQT 600
Cdd:PRK09776 956 PPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISI 1035
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1778737331 601 VNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:PRK09776 1036 IQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
246-334 |
9.90e-04 |
|
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: 40.40 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 246 YIDSLTGLGNRKLFENHFSSVVDTITTDA-PLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKiigNLTNSKIF-R 323
Cdd:TIGR00254 3 VRDPLTGLYNRRYLEEMLDSELKRARRFQrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQS---SVRGSDVVgR 79
|
90
....*....|.
gi 1778737331 324 LNGSTFIALIP 334
Cdd:TIGR00254 80 YGGEEFVVILP 90
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
165-642 |
1.07e-48 |
|
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: 179.98 E-value: 1.07e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 165 FLILIASLAVAFLILREVFKPLKAVEHQAHLVTRKRFTLNEEIPIARELRTVTKAINNMVINLQSTFDSLTKQTQALTEE 244
Cdd:COG2200 75 LLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 245 VYIDSLTGLGNRKLFENHFSSVVDTITTDAPLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKIIGNLTNSKIFRL 324
Cdd:COG2200 155 LLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGG 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 325 NGSTFIALIPYDTQFLNRTRLEITDAFSKQKNSLHVNGFANFAILEVNKGSSIGSVLSALDTGSTI---------GDTID 395
Cdd:COG2200 235 GGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAaaaaaagggRGRVV 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 396 TNKIDKDTLFSVNQWRTLIQSIIDSGEVSFSVQPVKRANSqNKQCYFEAFAHFTH-EGEKVNNGHLFAMAEKLNLTEELD 474
Cdd:COG2200 315 FFAAAEARARRRLALESELREALEEGELRLYYQPIVDLRT-GRVVGYEALLRWRHpDGGLISPAEFIPAAERSGLIVELD 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 475 ----KKIIRNFVNIKEQYPDDVFALNVSKASLYSADFIQWLTLYAHTKPVIKTNLIFELHEISLLYNVHIASKHIDAIKD 550
Cdd:COG2200 394 rwvlERALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRA 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 551 IGINVCIEHFGTSLTSFRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLG 630
Cdd:COG2200 474 LGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELG 553
|
490
....*....|..
gi 1778737331 631 CDGVQGNLIMEP 642
Cdd:COG2200 554 CDYAQGYLFGRP 565
|
|
| LapD_MoxY_N |
pfam16448 |
LapD/MoxY periplasmic domain; This domain is the N-terminal periplasmic domain of the LapD and ... |
35-154 |
2.06e-48 |
|
LapD/MoxY periplasmic domain; This domain is the N-terminal periplasmic domain of the LapD and MoxY receptor proteins.
Pssm-ID: 465117 Cd Length: 124 Bit Score: 165.88 E-value: 2.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 35 VETTRDYLQTQMGSHAQDTATSLGLSISPYLEPENLVIAETMATAIFDSGYYKEIKFTNSQSQVVFDLENPKRVESVPNW 114
Cdd:pfam16448 5 VNNARSYLEQQLQSHAQDTATSLGLSLSPYLENEDPVTAETMINAIFDSGYYRSIRLTDPDGKVLVERQNPVLIEGVPQW 84
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1778737331 115 FIALSSLKAPTMQSELNNGWIMAGILEVTSHTGQSYVTLW 154
Cdd:pfam16448 85 FIRLVPLEPPPGEAEISSGWLQLGTLEVESHPGYAYQELW 124
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
418-642 |
5.47e-46 |
|
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: 163.26 E-value: 5.47e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 418 IDSGEVSFSVQPVKRANSqNKQCYFEAFAHFTH-EGEKVNNGHLFAMAEKLNLTEELDKKIIRNFVNI---KEQYPDDVF 493
Cdd:pfam00563 8 LENGEFVLYYQPIVDLRT-GRVVGYEALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADlaqLQLGPDIKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 494 ALNVSKASLYSADFIQWLTLYAHTKPVIKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTSFRYLQGL 573
Cdd:pfam00563 87 SINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1778737331 574 DIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:pfam00563 167 PPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
414-639 |
3.67e-39 |
|
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: 144.61 E-value: 3.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 414 IQSIIDSGEVSFSVQPVKRANSQnKQCYFEAFAHFTH-EGEKVNNGHLFAMAEKLNLTEELDKKIIRN----FVNIKEQY 488
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTG-RIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEacrqLARWQAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 489 PDDVFALNVSKASLYSADFIQWL--TLYAHtkPVIKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTS 566
Cdd:cd01948 82 PDLRLSVNLSARQLRDPDFLDRLleLLAET--GLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778737331 567 FRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLI 639
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLF 232
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
412-642 |
1.83e-36 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 136.96 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 412 TLIQSIIDSGEVSFSVQPVkrANSQNKQC-YFEAFAHFTH-EGEKVNNGHLFAMAEKLNLTEELDKKIIRNFVN----IK 485
Cdd:smart00052 2 RELRQALENGQFLLYYQPI--VSLRTGRLvGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQqlaeWQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 486 EQYPDDV-FALNVSKASLYSADFIQWLTLYAHTKPVIKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSL 564
Cdd:smart00052 80 AQGPPPLlISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778737331 565 TSFRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
161-639 |
1.31e-24 |
|
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: 109.09 E-value: 1.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 161 FYGSFLILIASLAVAFLILREVFKPLKAVEHQAHLVTRKRFTLNEEIPIARELRTVTKAINNMVINLQSTFDSLTKQTQA 240
Cdd:COG5001 163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKR 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 241 LTEEV----YIDSLTGLGNRKLFENHFSSVVDTIT-TDAPLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKIIGN 315
Cdd:COG5001 243 AEERLrhlaYHDPLTGLPNRRLFLDRLEQALARARrSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 316 ltNSKIFRLNGSTFIALIPYDT------QFLNRtrleITDAFSKqknSLHVNGfanfaiLEVNKGSSIGSVLSALDtgst 389
Cdd:COG5001 323 --GDTVARLGGDEFAVLLPDLDdpedaeAVAER----ILAALAE---PFELDG------HELYVSASIGIALYPDD---- 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 390 iGDTIDT-----------------NKI---DKDTLFSVNQWRTLIQSI---IDSGEvsFSV--QPVKRANSqNKQCYFEA 444
Cdd:COG5001 384 -GADAEEllrnadlamyrakaagrNRYrffDPEMDERARERLELEADLrraLERGE--LELhyQPQVDLAT-GRIVGAEA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 445 FAHFTH-EGEKVNNGHLFAMAEKLNLTEELDKKIIRN----FVNIKEQYPDDVF-ALNVSKASLYSADFIQWLT------ 512
Cdd:COG5001 460 LLRWQHpERGLVSPAEFIPLAEETGLIVPLGEWVLREacrqLAAWQDAGLPDLRvAVNLSARQLRDPDLVDRVRralaet 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 513 -LYAHtkpviktNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTSFRYLQGLDIEYVKIDGSYIQDLLDN 591
Cdd:COG5001 540 gLPPS-------RLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAED 612
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1778737331 592 SQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLI 639
Cdd:COG5001 613 PDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLF 660
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
448-642 |
1.74e-24 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 109.38 E-value: 1.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 448 FTHEGEKVNNGHLFAMAEKLNLTEELDKKIIRNFVnikEQY------PDDVFALNVSKASLYSADFIQWL-TLYAHTkPV 520
Cdd:PRK09776 880 WDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFF---RQAakavasKGLSIALPLSVAGLSSPTLLPFLlEQLENS-PL 955
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 521 IKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTSFRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQT 600
Cdd:PRK09776 956 PPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISI 1035
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1778737331 601 VNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:PRK09776 1036 IQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
159-646 |
9.96e-24 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 106.10 E-value: 9.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 159 RSFYGSFLILIASLAVAFLILREV--FKplKAVEHQAHLVTRKRFTLNEEipiaREL----------RTVTKAINNMVIN 226
Cdd:PRK11059 136 YSLYATASLTLAIGFIVLMLFLGVrwLR--RQLAGQELLEERARRILNGE----REQavagsgyewpRTASRALDHLLSE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 227 LQ------STFDSLTKQTQALteevyiDSLTGLGNRKLFENHFSSVV-DTITTDAPLTAMMITLPSLTNINQSVSYQDGD 299
Cdd:PRK11059 210 LQdareerSRFDTFIRSNAFQ------DAKTGLGNRLFFDNQLATLLeDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVE 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 300 AHVKDVSVILTKIIGNLTNSKIFRLNGSTFIALIPYDTQ---------------FLNRTRLEITDAFskqknsLHVnGFA 364
Cdd:PRK11059 284 ELLFELINLLSTFVMRYPGALLARYSRSDFAVLLPHRSLkeadslasqllkavdALPPPKMLDRDDF------LHI-GIC 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 365 NFailevNKGSSIGSVL--------SALDTGST---IGDTIDTNKIDKDtlfSVnQWRTLIQSIIDSGEVSFSVQPVkrA 433
Cdd:PRK11059 357 AY-----RSGQSTEQVMeeaemalrSAQLQGGNgwfVYDKAQLPEKGRG---SV-RWRTLLEQTLVRGGPRLYQQPA--V 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 434 NSQNKQCYFEAFAH-FTHEGEKVNNGHLFAMAEKLNLTEELDKKIIRNFVNIKEQYPDDVFALNVSKASLYSADFIQWL- 511
Cdd:PRK11059 426 TRDGKVHHRELFCRiRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEENLSINLSVDSLLSRAFQRWLr 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 512 -TLYAHTKPViKTNLIFELHEISLLynvhiasKHIDAIKDI-------GINVCIEHFGTSLTSFRYLQGLDIEYVKIDGS 583
Cdd:PRK11059 506 dTLLQCPRSQ-RKRLIFELAEADVC-------QHISRLRPVlrmlrglGCRLAVDQAGLTVVSTSYIKELNVELIKLHPS 577
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1778737331 584 YIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEPSKVL 646
Cdd:PRK11059 578 LVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPLD 640
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
410-636 |
1.58e-11 |
|
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: 67.25 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 410 WRTLIQSIIDSGEvsFSV--QPVkrANSQNKQCY-FEAFAHFTHE-GEKVNNGHLFAMAEKLNL----TEELDKKIIRNF 481
Cdd:COG4943 272 PRRRLRRAIKRRE--FYVhyQPI--VDLKTGRCVgAEALVRWRDPdGSVISPDIFIPLAEQSGLisplTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 482 VNIKEQYPDDVFALNVSKASLYSADFIQWLTLYAHTKPVIKTNLIFELHEISLLyNVHIASKHIDAIKDIGINVCIEHFG 561
Cdd:COG4943 348 GDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDFG 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778737331 562 TSLTSFRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQG 636
Cdd:COG4943 427 TGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQG 501
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
134-334 |
9.94e-11 |
|
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: 63.07 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 134 WIMAGILEVTSHTGQSYVTLWEHTKRSFYGSFLILIASLAVAFLILREVFKPLKAVEHQAHLVTRKRFTLNEEIPIAREL 213
Cdd:COG2199 4 LLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 214 RTVTKAINNMVINLQSTFDsLTKQTQALTEEVYIDSLTGLGNRKLFENHFSSVVDTIT-TDAPLTAMMITLPSLTNINQS 292
Cdd:COG2199 84 LLLLLALLLLLLALEDITE-LRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARrEGRPLALLLIDLDHFKRINDT 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1778737331 293 VSYQDGDAHVKDVSVILTKIIGNltNSKIFRLNGSTFIALIP 334
Cdd:COG2199 163 YGHAAGDEVLKEVARRLRASLRE--SDLVARLGGDEFAVLLP 202
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
246-360 |
4.10e-08 |
|
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: 52.94 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 246 YIDSLTGLGNRKLFENHFSSVVD-TITTDAPLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKIIGNltNSKIFRL 324
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLArARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRE--SDLVARL 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1778737331 325 NGSTFIALIPYDT-----QFLNRTRLEITDAFSKQKNSLHV 360
Cdd:cd01949 79 GGDEFAILLPGTDleeaeALAERLREAIEEPFFIDGQEIRV 119
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
239-642 |
1.49e-07 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 54.69 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 239 QALTEEVYIDSLTGLGNRklfeNHFSSVVDTITTDAPLTAMMITLPSLTN---INQSVSYQDGDAHVKDVSVIltkIIGN 315
Cdd:PRK10060 231 ERLRILANTDSITGLPNR----NAIQELIDHAINAADNNQVGIVYLDLDNfkkVNDAYGHMFGDQLLQDVSLA---ILSC 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 316 LTNSKIF-RLNGSTFIALIPYDTQFLnrtrLEITDA--FSKQKNSLHVngfanfAILEVNKGSSIGSVLSALDtgstiGD 392
Cdd:PRK10060 304 LEEDQTLaRLGGDEFLVLASHTSQAA----LEAMASriLTRLRLPFRI------GLIEVYTGCSIGIALAPEH-----GD 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 393 TIDTNKIDKDT--------------LFS--VNQ------W-RTLIQSIIDSGEVSFSVQPVKRANSqnKQCYFEAFAHF- 448
Cdd:PRK10060 369 DSESLIRSADTamytakeggrgqfcVFSpeMNQrvfeylWlDTNLRKALENDQLVIHYQPKITWRG--EVRSLEALVRWq 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 449 THEGEKVNNGHLFAMAEKLNLTEELDKKIIRNFVNIKEQYPDDvfALNVSKASLYSADFIQWLTLYAHTKPVIKTN---- 524
Cdd:PRK10060 447 SPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDK--GINLRVAVNVSARQLADQTIFTALKQALQELnfey 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 525 -LI-FELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTSFRYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQTVN 602
Cdd:PRK10060 525 cPIdVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIV 604
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1778737331 603 NICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:PRK10060 605 AVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
236-642 |
1.67e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 54.78 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 236 KQTQALTEEVYIDSLTGLGNRKLFENHFSSVVDTittDAPLTAMMITLPSLTNINQSVSYQDGDahvkdvSVILTkiign 315
Cdd:PRK11359 367 KSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDK---AVSPVVYLIGVDHFQDVIDSLGYAWAD------QALLE----- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 316 LTNSKIFRLNGSTFIALIPyDTQFLnrtrleitdaFSKQKNSLH-VNGFANFAILEVNKGSSIGSvlSALDTGSTIGDTI 394
Cdd:PRK11359 433 VVNRFREKLKPDQYLCRIE-GTQFV----------LVSLENDVSnITQIADELRNVVSKPIMIDD--KPFPLTLSIGISY 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 395 DTNKiDKDTLFSV-------------NQWR-----------------TLIQSIIDSGEVSFSVQPVKRANSqnKQCY-FE 443
Cdd:PRK11359 500 DVGK-NRDYLLSTahnamdyirknggNGWQffspamnemvkerlvlgAALKEAISNNQLKLVYQPQIFAET--GELYgIE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 444 AFA--HFTHEGEkVNNGHLFAMAEKLNLTEELDKKIIRN-----FVNIKEQYPDDVFALNVSKASLYSADFIQWLTLYAH 516
Cdd:PRK11359 577 ALArwHDPLHGH-VPPSRFIPLAEEIGEIENIGRWVIAEacrqlAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQ 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 517 TKPVIKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTSFRYLQGLDIEYVKIDGSYIQDLLDNSQSQF 596
Cdd:PRK11359 656 AWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILA 735
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1778737331 597 FIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:PRK11359 736 LLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
|
|
| NarQ |
COG3850 |
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ... |
165-400 |
1.92e-07 |
|
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];
Pssm-ID: 443059 [Multi-domain] Cd Length: 448 Bit Score: 54.12 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 165 FLILIASLAVAFLILREVFKPLKAVEHQAHLVTRKRFTLNEEIPIARELRTVTKAINNMVINLQSTFDSLTKQTQALTEE 244
Cdd:COG3850 125 LLALLLALLLAYLLRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELYAELEEEEELEAEL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 245 VYIDSLTGLGNRKLFENHFSSVVDTITTDAPLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKIIGNLTNSKIFRL 324
Cdd:COG3850 205 ELLALLDELLLLAALLLLLALLLALLLAALLAALLLLLLLQDALAESELLALNILAGLLELLLALLLLLLASALLLLELE 284
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1778737331 325 NGSTFIALIPYDTQFLNRTRLEITDAFSKQKNSLHVNGFANFAILEVNKGSSIGSVLSALDTGSTIGDTIDTNKID 400
Cdd:COG3850 285 LLALLLELVELLALAAAEEALLLLVELAALLLLLLLQAIANASLLLIALASVVAALLELASILALQAALEAAAAGA 360
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
245-334 |
3.81e-07 |
|
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: 50.33 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 245 VYIDSLTGLGNRKLFENHFSSVVDT-ITTDAPLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKIIGNltNSKIFR 323
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRaLREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRR--SDLVAR 78
|
90
....*....|.
gi 1778737331 324 LNGSTFIALIP 334
Cdd:pfam00990 79 LGGDEFAILLP 89
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
414-642 |
4.05e-07 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 53.07 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 414 IQSIIDSGEVSFSVQPVKRANSQnKQCYFEAFAHFTH--EGEKVNNGHL-FAMAEKL--NLTEELDKKIIRNFVNIKEQY 488
Cdd:PRK10551 268 ILTGIKRGQFYVEYQPVVDTQTL-RVTGLEALLRWRHptAGEIPPDAFInYAEAQKLivPLTQHLFELIARDAAELQKVL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 489 PDDV-FALNVSKASLYSADFIQWLTLYAHTKPVIKTNLIFELHEISLLyNVHIASKHIDAIKDIGINVCIEHFGTSLTSF 567
Cdd:PRK10551 347 PVGAkLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMV-QEEEATKLFAWLHSQGIEIAIDDFGTGHSAL 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778737331 568 RYLQGLDIEYVKIDGSYIQDLLDNSQSQFFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:PRK10551 426 IYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRP 500
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
493-642 |
4.63e-06 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 49.94 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 493 FALNVSKASLYSADFIQWL-TLYAHTKpVIKTNLIFELHEISLLYNVHIASKHIDAIKDIGINVCIEHFGTSLTSFRYL- 570
Cdd:PRK11829 493 LSVNISGLQVQNKQFLPHLkTLISHYH-IDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLn 571
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1778737331 571 --QGLDIEYVKIDGSYIQDL-LDNSqsqfFIQTVNNICHGFGIKVLACLIEKPETLKMLENLGCDGVQGNLIMEP 642
Cdd:PRK11829 572 hlKSLPIHMIKLDKSFVKNLpEDDA----IARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
243-334 |
4.65e-06 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 47.24 E-value: 4.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 243 EEVYIDSLTGLGNRKLFENHFSSVVDT-ITTDAPLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKIIGNltNSKI 321
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRaQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRP--GDLL 78
|
90
....*....|...
gi 1778737331 322 FRLNGSTFIALIP 334
Cdd:smart00267 79 ARLGGDEFALLLP 91
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
164-251 |
9.80e-04 |
|
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: 42.26 E-value: 9.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 164 SFLILIASLAVAFLILREVFKPLKAVEHQAHLVTRKRFtlNEEIPIAR--ELRTVTKAINNMVINLQSTFDSLTKQtQAL 241
Cdd:COG5000 15 ALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDL--SVRLPVTGddEIGELARAFNRMTDQLKEQREELEER-RRY 91
|
90
....*....|
gi 1778737331 242 TEEVyIDSLT 251
Cdd:COG5000 92 LETI-LENLP 100
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
246-334 |
9.90e-04 |
|
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: 40.40 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1778737331 246 YIDSLTGLGNRKLFENHFSSVVDTITTDA-PLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKiigNLTNSKIF-R 323
Cdd:TIGR00254 3 VRDPLTGLYNRRYLEEMLDSELKRARRFQrSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQS---SVRGSDVVgR 79
|
90
....*....|.
gi 1778737331 324 LNGSTFIALIP 334
Cdd:TIGR00254 80 YGGEEFVVILP 90
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
247-313 |
1.04e-03 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 42.20 E-value: 1.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1778737331 247 IDSLTGLGNRKLFENHFSSVVDTITT-DAPLTAMMITLPSLTNINQSVSYQDGDAHVKDVSVILTKII 313
Cdd:PRK09581 294 TDGLTGLHNRRYFDMHLKNLIERANErGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNI 361
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
167-243 |
5.90e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 39.62 E-value: 5.90e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1778737331 167 ILIASLAVAFLILREVFKPLKAVEHQAHLVTRKRFTLNEEIPIARELRTVTKAINNMVINLQSTFDSLTKQTQALTE 243
Cdd:COG0840 191 LVALAIILALLLSRSITRPLRELLEVLERIAEGDLTVRIDVDSKDEIGQLADAFNRMIENLRELVGQVRESAEQVAS 267
|
|
| |
