|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
493-729 |
6.63e-84 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 265.62 E-value: 6.63e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 493 NTIRTALDQGDLLLYAQPIRNKEGEG--YDEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLATHPCD 569
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRlvGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 570 KKGP-RFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGTGYAN 648
Cdd:smart00052 82 GPPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 649 YERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPLA 728
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
.
gi 15832527 729 D 729
Cdd:smart00052 242 D 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
493-729 |
6.32e-78 |
|
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: 249.77 E-value: 6.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 493 NTIRTALDQGDLLLYAQPI---RNKEGEGYdEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLATHPC 568
Cdd:cd01948 1 ADLRRALERGEFELYYQPIvdlRTGRIVGY-EALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 569 DKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGTGYAN 648
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 649 YERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPLA 728
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 15832527 729 D 729
Cdd:cd01948 240 E 240
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
169-729 |
1.30e-76 |
|
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: 257.41 E-value: 1.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 169 LLSLFTAVLIYNMLFYYLTRMIVSPHFAQILWRRDIAPSLGKEKRAFTLSWLAALSVLLLLLCTPYENDFIAGYLVPVFF 248
Cdd:COG2200 2 LLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 249 IIFTLGVGKLRYPFLNLTWAVSTLCLLNYNQNFLQGVETEYSLAFILAVLISFSVCLLYMVRIYHRSEWLNRRWHLQALT 328
Cdd:COG2200 82 LLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 329 DPLTLLPNFRALEQAPEQEAGKSFC-------CLRIDNLEFMSRHYGLMMRVHCIRSIYRTLLPLMQENEKLYQLPGSEL 401
Cdd:COG2200 162 LLLRRLLLLLLLLLLLLLLALALLAlllllllLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 402 LLVLSGPETEGRLQHMVNILNSRQIHWNNTGLDMGYGAAWGRFDGNQETLQPLLGQLSWLAEQSCAHHHVLALDSREEMV 481
Cdd:COG2200 242 LLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 482 sgQTTKQVLLLNTIRTALDQGDLLLYAQPI---RNKEGEGYdEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDLQVLE 557
Cdd:COG2200 322 --RARRRLALESELREALEEGELRLYYQPIvdlRTGRVVGY-EALLRWRHpDGGLISPAEFIPAAERSGLIVELDRWVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 558 SLLKWLATHPCDKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRI 637
Cdd:COG2200 399 RALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 638 AIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQ 717
Cdd:COG2200 479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558
|
570
....*....|..
gi 15832527 718 GYLIGRPQPLAD 729
Cdd:COG2200 559 GYLFGRPLPLEE 570
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
493-724 |
1.12e-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: 217.19 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 493 NTIRTALDQGDLLLYAQPI---RNKEGEGYdEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLATHPC 568
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIvdlRTGRVVGY-EALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 569 DKkGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGTGYAN 648
Cdd:pfam00563 81 GP-DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832527 649 YERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRP 724
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
478-729 |
2.23e-60 |
|
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: 215.41 E-value: 2.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 478 EEMvSGQTTKQVLLLNTIRTALDQGDLLLYAQPIRN-KEGE--GYdEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDL 553
Cdd:COG5001 414 PEM-DERARERLELEADLRRALERGELELHYQPQVDlATGRivGA-EALLRWQHpERGLVSPAEFIPLAEETGLIVPLGE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 554 QVLES----LLKWLATHPCDkkgPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQ 629
Cdd:COG5001 492 WVLREacrqLAAWQDAGLPD---LRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRA 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 630 LHKFGFRIAIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLH 709
Cdd:COG5001 569 LRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLR 648
|
250 260
....*....|....*....|
gi 15832527 710 KLGVQYLQGYLIGRPQPLAD 729
Cdd:COG5001 649 ELGCDYAQGYLFSRPLPAEE 668
|
|
| MASE1 |
pfam05231 |
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate ... |
15-311 |
9.85e-54 |
|
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate cyclases and other bacterial signaling proteins. This entry also includes members of the 8 transmembrane UhpB type (8TMR-UT) domain family.
Pssm-ID: 428383 [Multi-domain] Cd Length: 299 Bit Score: 187.24 E-value: 9.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 15 TLAFTLTVVLIQLSRFISPLAIIHSSYIFLAWMPLCVMLSILFIFGWRGVVPVLCGMFCTNL---WNFHLSFLQTAVMLG 91
Cdd:pfam05231 1 LLLLLLLLYALLAAVSLSLALALVSSGSAPIWLPTGLALAALLLFGRRGWPGILLGAVLASLmagLLSGLNLLLALAIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 92 SQTFVVLCACAILRWQLGTRWRYGLTSryvwqrlFWLGLVTPIGIKCSMYLVGSFFDFPLKISTFFGDADAIFTVVDLLS 171
Cdd:pfam05231 81 VNALEALLGAALLRRLLPGRNRLQRLR-------FWLRLVIPGAIIAALLLAIIGLALLLLLGLIPLAPFSIVWLTWWLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 172 LFTAVLIYNMLFYYLTRMIVSPHFAQILWRRDIAPSLGKEKRAFTLSWLAALSVLLLLLCTPYENDFIAG-YLVPVFFII 250
Cdd:pfam05231 154 SATGVLVVTPLLLLLRRYLRLRHRLRLWYERDLAPAAAKLLLLFALLLLLILSLLLLLLCMPEINYPLGYlLLPPLLWAA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832527 251 FTLGVGKLRYPFLnLTWAVSTLCLLNYNQNFLQGVETEYSLAFILAVLISFSVCLLYMVRI 311
Cdd:pfam05231 234 FRFGVRGGSLAAL-LLAVLLILFTLQGGGPFLQTSGDESSQAILLQLFLAILALVALLVSA 293
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
321-729 |
9.00e-36 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 144.05 E-value: 9.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 321 RWHLQALTDPLTLLPNFRA--------LEQAPEQEAGKSFccLRIDNLEFMSRHYGLMMRVHCIRSIYRTLLPLMQENEK 392
Cdd:PRK10060 232 RLRILANTDSITGLPNRNAiqelidhaINAADNNQVGIVY--LDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 393 LYQLPGSELLlVLSGPETEGRLQHMVNILNSRQIHWNNTGLDMGY-GAAWG--RFDGNQETLQPLLGQLS---WLAEQSC 466
Cdd:PRK10060 310 LARLGGDEFL-VLASHTSQAALEAMASRILTRLRLPFRIGLIEVYtGCSIGiaLAPEHGDDSESLIRSADtamYTAKEGG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 467 AHHH-VLALdsreEMvsGQTTKQVLLLNT-IRTALDQGDLLLYAQPIRNKEGEGYD-EVLAR-LKYDGGIMTPDKFLPLI 542
Cdd:PRK10060 389 RGQFcVFSP----EM--NQRVFEYLWLDTnLRKALENDQLVIHYQPKITWRGEVRSlEALVRwQSPERGLIPPLEFISYA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 543 AQFNLSARFDLQVLESLLKWLATHPCDKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAES 622
Cdd:PRK10060 463 EESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 623 SMYNIEQLHKFGFRIAIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQ 702
Cdd:PRK10060 543 ALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETA 622
|
410 420
....*....|....*....|....*..
gi 15832527 703 QQQALLHKLGVQYLQGYLIGRPQPLAD 729
Cdd:PRK10060 623 KEDAFLTKNGVNERQGFLFAKPMPAVA 649
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
324-473 |
2.08e-24 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 100.01 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 324 LQALTDPLTLLPNFRALEQAPEQEAGK--------SFCCLRIDNLEFMSRHYGLMMRVHCIRSIYRTLLPLMQENEKLYQ 395
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRaqrqgspfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 396 LPGSELLLVLSGPETEGRLQHMVNILNSRQIHWNNTG----LDMGYGAAWGRFDG-NQETLQPLLGQLSWLAEQSCAHHH 470
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGiplyLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 15832527 471 VLA 473
Cdd:smart00267 161 AVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
325-421 |
1.58e-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: 42.71 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 325 QALTDPLTLLPNFRALEQAPEQEA------GKSFCCLRI--DNLEFMSRHYGLMMRVHCIRSIYRtllpLMQENEKLYQL 396
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELkrarrfQRSFSVLMIdiDNFKKINDTLGHDVGDEVLREVAR----ILQSSVRGSDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 15832527 397 P----GSELLLVLSGPETEG------RLQHMVNIL 421
Cdd:TIGR00254 77 VgrygGEEFVVILPGTPLEDalskaeRLRDAINSK 111
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
326-434 |
3.51e-04 |
|
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: 41.85 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 326 ALTDPLTLLPNFRALEQAPEQEAGK--------SFCCLRIDNLEFMSRHYGLMMRVHCIRSIYRTLLPLMQENEKLYQLP 397
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRalregspvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15832527 398 GSELLLVLSGPETEGRLQHMVNI---LNSRQIHWNNTGLD 434
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIrrlLAKLKIPHTVSGLP 120
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
493-729 |
6.63e-84 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 265.62 E-value: 6.63e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 493 NTIRTALDQGDLLLYAQPIRNKEGEG--YDEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLATHPCD 569
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRlvGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 570 KKGP-RFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGTGYAN 648
Cdd:smart00052 82 GPPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 649 YERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPLA 728
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
.
gi 15832527 729 D 729
Cdd:smart00052 242 D 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
493-729 |
6.32e-78 |
|
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: 249.77 E-value: 6.32e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 493 NTIRTALDQGDLLLYAQPI---RNKEGEGYdEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLATHPC 568
Cdd:cd01948 1 ADLRRALERGEFELYYQPIvdlRTGRIVGY-EALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 569 DKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGTGYAN 648
Cdd:cd01948 80 GGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 649 YERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPLA 728
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 15832527 729 D 729
Cdd:cd01948 240 E 240
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
169-729 |
1.30e-76 |
|
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: 257.41 E-value: 1.30e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 169 LLSLFTAVLIYNMLFYYLTRMIVSPHFAQILWRRDIAPSLGKEKRAFTLSWLAALSVLLLLLCTPYENDFIAGYLVPVFF 248
Cdd:COG2200 2 LLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 249 IIFTLGVGKLRYPFLNLTWAVSTLCLLNYNQNFLQGVETEYSLAFILAVLISFSVCLLYMVRIYHRSEWLNRRWHLQALT 328
Cdd:COG2200 82 LLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 329 DPLTLLPNFRALEQAPEQEAGKSFC-------CLRIDNLEFMSRHYGLMMRVHCIRSIYRTLLPLMQENEKLYQLPGSEL 401
Cdd:COG2200 162 LLLRRLLLLLLLLLLLLLLALALLAlllllllLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 402 LLVLSGPETEGRLQHMVNILNSRQIHWNNTGLDMGYGAAWGRFDGNQETLQPLLGQLSWLAEQSCAHHHVLALDSREEMV 481
Cdd:COG2200 242 LLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 482 sgQTTKQVLLLNTIRTALDQGDLLLYAQPI---RNKEGEGYdEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDLQVLE 557
Cdd:COG2200 322 --RARRRLALESELREALEEGELRLYYQPIvdlRTGRVVGY-EALLRWRHpDGGLISPAEFIPAAERSGLIVELDRWVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 558 SLLKWLATHPCDKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRI 637
Cdd:COG2200 399 RALRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 638 AIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQ 717
Cdd:COG2200 479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558
|
570
....*....|..
gi 15832527 718 GYLIGRPQPLAD 729
Cdd:COG2200 559 GYLFGRPLPLEE 570
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
493-724 |
1.12e-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: 217.19 E-value: 1.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 493 NTIRTALDQGDLLLYAQPI---RNKEGEGYdEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLATHPC 568
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIvdlRTGRVVGY-EALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 569 DKkGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGTGYAN 648
Cdd:pfam00563 81 GP-DIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832527 649 YERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRP 724
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
478-729 |
2.23e-60 |
|
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: 215.41 E-value: 2.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 478 EEMvSGQTTKQVLLLNTIRTALDQGDLLLYAQPIRN-KEGE--GYdEVLARLKY-DGGIMTPDKFLPLIAQFNLSARFDL 553
Cdd:COG5001 414 PEM-DERARERLELEADLRRALERGELELHYQPQVDlATGRivGA-EALLRWQHpERGLVSPAEFIPLAEETGLIVPLGE 491
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 554 QVLES----LLKWLATHPCDkkgPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQ 629
Cdd:COG5001 492 WVLREacrqLAAWQDAGLPD---LRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRA 568
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 630 LHKFGFRIAIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLH 709
Cdd:COG5001 569 LRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLR 648
|
250 260
....*....|....*....|
gi 15832527 710 KLGVQYLQGYLIGRPQPLAD 729
Cdd:COG5001 649 ELGCDYAQGYLFSRPLPAEE 668
|
|
| MASE1 |
pfam05231 |
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate ... |
15-311 |
9.85e-54 |
|
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate cyclases and other bacterial signaling proteins. This entry also includes members of the 8 transmembrane UhpB type (8TMR-UT) domain family.
Pssm-ID: 428383 [Multi-domain] Cd Length: 299 Bit Score: 187.24 E-value: 9.85e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 15 TLAFTLTVVLIQLSRFISPLAIIHSSYIFLAWMPLCVMLSILFIFGWRGVVPVLCGMFCTNL---WNFHLSFLQTAVMLG 91
Cdd:pfam05231 1 LLLLLLLLYALLAAVSLSLALALVSSGSAPIWLPTGLALAALLLFGRRGWPGILLGAVLASLmagLLSGLNLLLALAIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 92 SQTFVVLCACAILRWQLGTRWRYGLTSryvwqrlFWLGLVTPIGIKCSMYLVGSFFDFPLKISTFFGDADAIFTVVDLLS 171
Cdd:pfam05231 81 VNALEALLGAALLRRLLPGRNRLQRLR-------FWLRLVIPGAIIAALLLAIIGLALLLLLGLIPLAPFSIVWLTWWLG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 172 LFTAVLIYNMLFYYLTRMIVSPHFAQILWRRDIAPSLGKEKRAFTLSWLAALSVLLLLLCTPYENDFIAG-YLVPVFFII 250
Cdd:pfam05231 154 SATGVLVVTPLLLLLRRYLRLRHRLRLWYERDLAPAAAKLLLLFALLLLLILSLLLLLLCMPEINYPLGYlLLPPLLWAA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832527 251 FTLGVGKLRYPFLnLTWAVSTLCLLNYNQNFLQGVETEYSLAFILAVLISFSVCLLYMVRI 311
Cdd:pfam05231 234 FRFGVRGGSLAAL-LLAVLLILFTLQGGGPFLQTSGDESSQAILLQLFLAILALVALLVSA 293
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
491-729 |
2.51e-49 |
|
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: 181.65 E-value: 2.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 491 LLNTIRTALDQGDLLLYAQPI---RNKEGEGYdEVLARLK-YDGGIMTPDKFLPLIAQFNLSARFDLQVLESLLK----W 562
Cdd:COG4943 272 PRRRLRRAIKRREFYVHYQPIvdlKTGRCVGA-EALVRWRdPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRdlgdL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 563 LATHPCdkkgprF--SVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQaFSNAESSMYNIEQLHKFGFRIAID 640
Cdd:COG4943 351 LAADPD------FhiSINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERG-FIDPAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 641 DFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYL 720
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
....*....
gi 15832527 721 IGRPQPLAD 729
Cdd:COG4943 504 FAKPLPAEE 512
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
321-729 |
9.00e-36 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 144.05 E-value: 9.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 321 RWHLQALTDPLTLLPNFRA--------LEQAPEQEAGKSFccLRIDNLEFMSRHYGLMMRVHCIRSIYRTLLPLMQENEK 392
Cdd:PRK10060 232 RLRILANTDSITGLPNRNAiqelidhaINAADNNQVGIVY--LDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 393 LYQLPGSELLlVLSGPETEGRLQHMVNILNSRQIHWNNTGLDMGY-GAAWG--RFDGNQETLQPLLGQLS---WLAEQSC 466
Cdd:PRK10060 310 LARLGGDEFL-VLASHTSQAALEAMASRILTRLRLPFRIGLIEVYtGCSIGiaLAPEHGDDSESLIRSADtamYTAKEGG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 467 AHHH-VLALdsreEMvsGQTTKQVLLLNT-IRTALDQGDLLLYAQPIRNKEGEGYD-EVLAR-LKYDGGIMTPDKFLPLI 542
Cdd:PRK10060 389 RGQFcVFSP----EM--NQRVFEYLWLDTnLRKALENDQLVIHYQPKITWRGEVRSlEALVRwQSPERGLIPPLEFISYA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 543 AQFNLSARFDLQVLESLLKWLATHPCDKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAES 622
Cdd:PRK10060 463 EESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEEL 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 623 SMYNIEQLHKFGFRIAIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQ 702
Cdd:PRK10060 543 ALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETA 622
|
410 420
....*....|....*....|....*..
gi 15832527 703 QQQALLHKLGVQYLQGYLIGRPQPLAD 729
Cdd:PRK10060 623 KEDAFLTKNGVNERQGFLFAKPMPAVA 649
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
308-729 |
1.23e-34 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 140.46 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 308 MVRIYHRSEWL--NRRWHLQALTD--PLTLLPN----FRALEQAPEQEAGKSFCCLRIDNLEFMSRHYGLM---MRVHCI 376
Cdd:PRK11829 210 LVRNYNRNQQLlaDAYADMGRISHrfPVTELPNrslfISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMseaQHQQLL 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 377 RSIYRTLLPLMQENEKLYQLPGSELLLVLSG-PETEGRLQHMVNILN--SRQIHWNNTGLDMGYGAAWGRFDGNQETLQP 453
Cdd:PRK11829 290 LTIVQRIEQCIDDSDLLAQLSKTEFAVLARGtRRSFPAMQLARRIMSqvTQPLFFDEITLRPSASIGITRYQAQQDTAES 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 454 LLGQLSwlAEQSCAHH----HVLALDSR-EEMVSGQTTKQvlllNTIRTALDQGDLLLYAQP---IRNKEGEGYDEVLAR 525
Cdd:PRK11829 370 MMRNAS--TAMMAAHHegrnQIMVFEPHlIEKTHKRLTQE----NDLLQAIENHDFTLFLQPqwdMKRQQVIGAEALLRW 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 526 LKYDGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLATHPCDKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQ 605
Cdd:PRK11829 444 CQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQ 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 606 AVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGTGYA--NYER-LKRLQADIIKIDGVFVKDIvtnTLDAMIVRS 682
Cdd:PRK11829 524 QLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSslRYLNhLKSLPIHMIKLDKSFVKNL---PEDDAIARI 600
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15832527 683 ITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPLAD 729
Cdd:PRK11829 601 ISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAE 647
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
495-728 |
2.88e-32 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 133.30 E-value: 2.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 495 IRTALDQGDLLLYAQP---IRNKEGEGYDEVLARLKYDGGIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLA------- 564
Cdd:PRK13561 405 ILNALENHQFAIWLQPqveMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAawqergi 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 565 THPcdkkgprFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQLHKFGFRIAIDDFGT 644
Cdd:PRK13561 485 MLP-------LSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGM 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 645 GYAN---YERLKRLQADIIKIDGVFVKDIVTntlDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLI 721
Cdd:PRK13561 558 GYAGlrqLQHMKSLPIDVLKIDKMFVDGLPE---DDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLF 634
|
....*..
gi 15832527 722 GRPQPLA 728
Cdd:PRK13561 635 ARALPIE 641
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
484-729 |
2.70e-26 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 115.25 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 484 QTTKQVLLLNT-IRTALDQGDLLLYAQP-IRNKEGEGYD-EVLARLkYD--GGIMTPDKFLPLIAqfnlsarfDLQVLES 558
Cdd:PRK11359 536 EMVKERLVLGAaLKEAISNNQLKLVYQPqIFAETGELYGiEALARW-HDplHGHVPPSRFIPLAE--------EIGEIEN 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 559 LLKWLATHPC------DKKG---PRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMYNIEQ 629
Cdd:PRK11359 607 IGRWVIAEACrqlaewRSQNihiPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQI 686
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 630 LHKFGFRIAIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLH 709
Cdd:PRK11359 687 LRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLR 766
|
250 260
....*....|....*....|
gi 15832527 710 KLGVQYLQGYLIGRPQPLAD 729
Cdd:PRK11359 767 KIHCRVIQGYFFSRPLPAEE 786
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
462-728 |
3.07e-26 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 115.54 E-value: 3.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 462 AEQSCAHHHVLALDSReemvsgqttkqvlllntIRTALDQGDLLLYAQPI--RNKEGEGYDEVLARL-KYDGGIMTPDKF 538
Cdd:PRK09776 830 QAAAHSEHRALSLAEQ-----------------WRMIKENQLMMLAHGVAspRIPEARNHWLISLRLwDPEGEIIDEGAF 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 539 LPLIAQFNLSARFDLQVLESLLKWLATHPCdKKGPRFSVNLMPLTLLQKNIAGRIIRLFKRYHISPQAVILEITEEQAFS 618
Cdd:PRK09776 893 RPAAEDPALMHALDRRVIHEFFRQAAKAVA-SKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLN 971
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 619 NAESSMYNIEQLHKFGFRIAIDDFGTGYANYERLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEF 698
Cdd:PRK09776 972 HAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGP 1051
|
250 260 270
....*....|....*....|....*....|
gi 15832527 699 VETQQQQALLHKLGVQYLQGYLIGRPQPLA 728
Cdd:PRK09776 1052 VELPLVLDTLSGIGVDLAYGYAIARPQPLD 1081
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
521-729 |
4.12e-25 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 110.08 E-value: 4.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 521 EVLARLKY-DGGIMTPDKFLPLI-AQ----------FNLSARfDLQVLESLLKwlathpcdkKGPRFSVNLMPLTLLQKN 588
Cdd:PRK10551 296 EALLRWRHpTAGEIPPDAFINYAeAQklivpltqhlFELIAR-DAAELQKVLP---------VGAKLGINISPAHLHSDS 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 589 IAGRIIRLFKRYHISPQAVILEITEEQAFSNAESSMyNIEQLHKFGFRIAIDDFGTGYANYERLKRLQADIIKIDGVFVK 668
Cdd:PRK10551 366 FKADVQRLLASLPADHFQIVLEITERDMVQEEEATK-LFAWLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQ 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832527 669 DIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPLAD 729
Cdd:PRK10551 445 AIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLED 505
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
324-473 |
2.08e-24 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 100.01 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 324 LQALTDPLTLLPNFRALEQAPEQEAGK--------SFCCLRIDNLEFMSRHYGLMMRVHCIRSIYRTLLPLMQENEKLYQ 395
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRaqrqgspfALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 396 LPGSELLLVLSGPETEGRLQHMVNILNSRQIHWNNTG----LDMGYGAAWGRFDG-NQETLQPLLGQLSWLAEQSCAHHH 470
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGiplyLTISIGVAAYPNPGeDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 15832527 471 VLA 473
Cdd:smart00267 161 AVY 163
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
495-727 |
6.42e-13 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 72.20 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 495 IRTALDQGDLLLYAQPIRNKEGEG-YDEVLARLkYDG--GIMTPDKFLPLIAQFNLSARFDLQVLESLLKWLAthpcDKK 571
Cdd:PRK11059 408 LEQTLVRGGPRLYQQPAVTRDGKVhHRELFCRI-RDGqgELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLR----YWP 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 572 GPRFSVNLMPLTLLQKniagRIIRLFK------RYHISPQaVILEITEEQAfsnaessMYNIEQL-------HKFGFRIA 638
Cdd:PRK11059 483 EENLSINLSVDSLLSR----AFQRWLRdtllqcPRSQRKR-LIFELAEADV-------CQHISRLrpvlrmlRGLGCRLA 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 639 IDDFG-----TGYanyerLKRLQADIIKIDGVFVKDIVTNTLDAMIVRSITDLAKAKSLSVVAEFVETQQQQALLHKLGV 713
Cdd:PRK11059 551 VDQAGltvvsTSY-----IKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVESREEWQTLQELGV 625
|
250
....*....|....
gi 15832527 714 QYLQGYLIGRPQPL 727
Cdd:PRK11059 626 SGGQGDFFAESQPL 639
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
602-727 |
9.18e-13 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 70.60 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 602 ISPQAVILEITEEQAFSNA--ESsmynIEQLHKFGFRIAIDDFgTGYANYERLKRLqADIIKIDgvfvkdivTNTLDAMI 679
Cdd:COG3434 81 LPPERVVLEILEDVEPDEEllEA----LKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID--------VLALDLEE 146
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 15832527 680 VRSITDLAKAKSLSVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPL 727
Cdd:COG3434 147 LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEIL 194
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
233-455 |
2.53e-07 |
|
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: 52.67 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 233 PYENDFIAGYLVPVFFIIFTLGVGKLRYPFLNLTWAVSTLCLLNYNQNFLQGVETEYSLAFILAVLISFSVCLLYMVRIY 312
Cdd:COG2199 21 SLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 313 HRSEWLNRRWHLQALTDPLTLLPNFRALEQAPEQE------AGKSFCCL--RIDNLEFMSRHYGLMMRVHCIRSIYRTLL 384
Cdd:COG2199 101 TELRRLEERLRRLATHDPLTGLPNRRAFEERLERElararrEGRPLALLliDLDHFKRINDTYGHAAGDEVLKEVARRLR 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832527 385 PLMQENEKLYQLPGSELLLVLSGPETEG---RLQHMVNILNSRQIHWNNTGLDMG--YGAAwgRFDGNQETLQPLL 455
Cdd:COG2199 181 ASLRESDLVARLGGDEFAVLLPGTDLEEaeaLAERLREALEQLPFELEGKELRVTvsIGVA--LYPEDGDSAEELL 254
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
535-727 |
6.97e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 48.07 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 535 PDKFLPLIAQF-NLSARFDLQVLESLLKWLAthpcdKKGPRF-------SVNLMPLTL--LQKNIAGR--IIRL-FKRYh 601
Cdd:PRK11596 59 PSQRLSPERYFaEITVSHRLDVVKEQLDLLA-----QWADFFvrhgllaSVNIDGPTLiaLRQQPAILrlIERLpWLRF- 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 602 ispqavilEITEEQAFSNAESsmynIEQLHKFGfRIAIDDFGTGYANYERLKRLQADIIKID-GVFV---KDIVTNTLDA 677
Cdd:PRK11596 133 --------ELVEHIRLPKDSP----FASMCEFG-PLWLDDFGTGMANFSALSEVRYDYIKVArELFImlrQSEEGRNLFS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15832527 678 MIVRSITDLAKAkslsVVAEFVETQQQQALLHKLGVQYLQGYLIGRPQPL 727
Cdd:PRK11596 200 QLLHLMNRYCRG----VIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPF 245
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
325-421 |
1.58e-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: 42.71 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 325 QALTDPLTLLPNFRALEQAPEQEA------GKSFCCLRI--DNLEFMSRHYGLMMRVHCIRSIYRtllpLMQENEKLYQL 396
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELkrarrfQRSFSVLMIdiDNFKKINDTLGHDVGDEVLREVAR----ILQSSVRGSDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 15832527 397 P----GSELLLVLSGPETEG------RLQHMVNIL 421
Cdd:TIGR00254 77 VgrygGEEFVVILPGTPLEDalskaeRLRDAINSK 111
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
326-434 |
3.51e-04 |
|
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: 41.85 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832527 326 ALTDPLTLLPNFRALEQAPEQEAGK--------SFCCLRIDNLEFMSRHYGLMMRVHCIRSIYRTLLPLMQENEKLYQLP 397
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRalregspvAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 15832527 398 GSELLLVLSGPETEGRLQHMVNI---LNSRQIHWNNTGLD 434
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIrrlLAKLKIPHTVSGLP 120
|
|
| |
