|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
182-717 |
1.10e-78 |
|
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: 262.80 E-value: 1.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 182 ARTFWRRSVKPLFCHKKALFIVVWLMLLISMIAILCAPFESQFIAGYLMPIVFILFTLGIGRLSYALISLFWAASALMLL 261
Cdd:COG2200 32 LLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 262 TYNYNFLNGVESGHSLSFILSVLISFAICLLYMSRIYQKSEWLKQGWQERALTDPLTGLPNIRALEVFLQHHPEAKVCCL 341
Cdd:COG2200 112 ALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 342 RLDNLEFLSRHYGILMRVHCKKMITASLQPLLQKDEKLFQLPGSELVVVLLGPGT-----AERLQYMVDHLNSRKIVWNK 416
Cdd:COG2200 192 LLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAaaaaaAAALRLLLLLLLEPLLLGGG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 417 TELDIEFGASWGEVPDGESLHHTLGQLSWLSEQSCAGHNVLALtnSLDDVSGQTTDRVLMLARIKRALDVGGLHLYAQPI 496
Cdd:COG2200 272 LVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVV--FFAAAEARARRRLALESELREALEEGELRLYYQPI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 497 HNARGEG--YFEILSRLES-EGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPSERAGTRFSVNLMPLTLMQNE 573
Cdd:COG2200 350 VDLRTGRvvGYEALLRWRHpDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLRLSVNLSARSLLDPD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 574 IAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANFERLKRLEADIIKIDGCFVK 653
Cdd:COG2200 430 FLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVR 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578264101 654 DICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPLTALEA 717
Cdd:COG2200 510 DIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEA 573
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
478-712 |
2.74e-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: 250.54 E-value: 2.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 478 ARIKRALDVGGLHLYAQPIHNARGEG--YFEILSRLES-EGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPSE 554
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRivGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 555 RAGTRFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANF 634
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578264101 635 ERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPL 712
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
479-712 |
6.29e-73 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 236.34 E-value: 6.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 479 RIKRALDVGGLHLYAQPIHNARGEG--YFEILSRLES-EGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPSER 555
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRlvGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 556 AGT-RFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANF 634
Cdd:smart00052 83 PPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578264101 635 ERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPL 712
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
478-709 |
5.73e-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: 215.26 E-value: 5.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 478 ARIKRALDVGGLHLYAQPIHNARGEG--YFEILSRLE-SEGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPsE 554
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRvvGYEALLRWQhPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 555 RAGTRFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANF 634
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578264101 635 ERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKP 709
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
309-717 |
2.26e-34 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 139.82 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 309 QER----ALTDPLTGLPNIRALEVFLQHHPEAK------VCCLRLDNLEFLSRHYGILMRVHCKKMITASLQPLLQKDEK 378
Cdd:PRK10060 230 QERlrilANTDSITGLPNRNAIQELIDHAINAAdnnqvgIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 379 LFQLPGSELVVvLLGPGTAERLQYMvdhlnSRKIVwnkTELDIEFGASWGEVPDGESLHHTLGQLSwlseqscaGHNVLA 458
Cdd:PRK10060 310 LARLGGDEFLV-LASHTSQAALEAM-----ASRIL---TRLRLPFRIGLIEVYTGCSIGIALAPEH--------GDDSES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 459 LTNSLDDV------SGQTTDRVL---MLARI----------KRALDVGGLHLYAQPIHNARGEGY-FEILSRLES-EGEI 517
Cdd:PRK10060 373 LIRSADTAmytakeGGRGQFCVFspeMNQRVfeylwldtnlRKALENDQLVIHYQPKITWRGEVRsLEALVRWQSpERGL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 518 ITPDRFIP------LIAQfnLSHRFDLNVVEKLLMWmrshpseRA---GTRFSVNLMPLTLMQNEIAAEIIALFERYAIA 588
Cdd:PRK10060 453 IPPLEFISyaeesgLIVP--LGRWVMLDVVRQVAKW-------RDkgiNLRVAVNVSARQLADQTIFTALKQALQELNFE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 589 PQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANFERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSI 668
Cdd:PRK10060 524 YCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAI 603
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 578264101 669 CNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPLTALEA 717
Cdd:PRK10060 604 VAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFER 652
|
|
| MASE1 |
pfam05231 |
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate ... |
2-302 |
6.81e-27 |
|
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: 111.35 E-value: 6.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 2 IALALSLIAIPFSryISPRAIVSENDVYLAWLPLSAMLAIVLLFGRRAIIPLLLSFSITNIY---NLDLAPLQSAVLLCC 78
Cdd:pfam05231 4 LLLLLYALLAAVS--LSLALALVSSGSAPIWLPTGLALAALLLFGRRGWPGILLGAVLASLMaglLSGLNLLLALAIAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 79 QTFTVFAACGVIRLVLGKRWRHSIPnkyigirIFWLGFMVPVGIKLSMYLAGYLFDFPVTISSYFGEGSAIYNVIDIQSL 158
Cdd:pfam05231 82 NALEALLGAALLRRLLPGRNRLQRL-------RFWLRLVIPGAIIAALLLAIIGLALLLLLGLIPLAPFSIVWLTWWLGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 159 ICAALIFTMMFYYPLRMIINPRYARTFWRRSVKPLFCHKKALFIVVWLMLLISMIAILCAPFESqFIAGYLM--PIVFIL 236
Cdd:pfam05231 155 ATGVLVVTPLLLLLRRYLRLRHRLRLWYERDLAPAAAKLLLLFALLLLLILSLLLLLLCMPEIN-YPLGYLLlpPLLWAA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578264101 237 FTLGIGRLSYALIsLFWAASALMLLTYNYNFLNGVESGHSLSFILSVLISFAICLLY-MSRIYQKSE 302
Cdd:pfam05231 234 FRFGVRGGSLAAL-LLAVLLILFTLQGGGPFLQTSGDESSQAILLQLFLAILALVALlVSAAISEQR 299
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
182-717 |
1.10e-78 |
|
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: 262.80 E-value: 1.10e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 182 ARTFWRRSVKPLFCHKKALFIVVWLMLLISMIAILCAPFESQFIAGYLMPIVFILFTLGIGRLSYALISLFWAASALMLL 261
Cdd:COG2200 32 LLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 262 TYNYNFLNGVESGHSLSFILSVLISFAICLLYMSRIYQKSEWLKQGWQERALTDPLTGLPNIRALEVFLQHHPEAKVCCL 341
Cdd:COG2200 112 ALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 342 RLDNLEFLSRHYGILMRVHCKKMITASLQPLLQKDEKLFQLPGSELVVVLLGPGT-----AERLQYMVDHLNSRKIVWNK 416
Cdd:COG2200 192 LLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAaaaaaAAALRLLLLLLLEPLLLGGG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 417 TELDIEFGASWGEVPDGESLHHTLGQLSWLSEQSCAGHNVLALtnSLDDVSGQTTDRVLMLARIKRALDVGGLHLYAQPI 496
Cdd:COG2200 272 LVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVV--FFAAAEARARRRLALESELREALEEGELRLYYQPI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 497 HNARGEG--YFEILSRLES-EGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPSERAGTRFSVNLMPLTLMQNE 573
Cdd:COG2200 350 VDLRTGRvvGYEALLRWRHpDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDLRLSVNLSARSLLDPD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 574 IAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANFERLKRLEADIIKIDGCFVK 653
Cdd:COG2200 430 FLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVR 509
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 578264101 654 DICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPLTALEA 717
Cdd:COG2200 510 DIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEA 573
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
478-712 |
2.74e-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: 250.54 E-value: 2.74e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 478 ARIKRALDVGGLHLYAQPIHNARGEG--YFEILSRLES-EGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPSE 554
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRivGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 555 RAGTRFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANF 634
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578264101 635 ERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPL 712
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
479-712 |
6.29e-73 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 236.34 E-value: 6.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 479 RIKRALDVGGLHLYAQPIHNARGEG--YFEILSRLES-EGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPSER 555
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRlvGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 556 AGT-RFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANF 634
Cdd:smart00052 83 PPPlLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 578264101 635 ERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPL 712
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
478-709 |
5.73e-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: 215.26 E-value: 5.73e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 478 ARIKRALDVGGLHLYAQPIHNARGEG--YFEILSRLE-SEGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPsE 554
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRvvGYEALLRWQhPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 555 RAGTRFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANF 634
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 578264101 635 ERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKP 709
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
199-717 |
1.65e-64 |
|
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: 226.96 E-value: 1.65e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 199 ALFIVVWLMLLISMIAILCAPFESQFIAGYLMPIVFILFTLGIGRLSYALISLFWAASALMLLTYNYNFLNGVESGHSLS 278
Cdd:COG5001 135 ALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 279 FILSVLISFAICLLYMSRIYQKSEWLKQGWQE---RALTDPLTGLPN----IRALEVFLQHHPEAK----VCCLRLDNle 347
Cdd:COG5001 215 GLLLLGLLLLLLLVAVLAIARLITERKRAEERlrhLAYHDPLTGLPNrrlfLDRLEQALARARRSGrrlaLLFIDLDR-- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 348 F------LSRHYG--ILmrvhckKMITASLQPLLQKDEKLFQLPGSELVVVLLGPGTAERLQYMVDHLN---SRKIVWNK 416
Cdd:COG5001 293 FkeindtLGHAAGdeLL------REVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILaalAEPFELDG 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 417 TELDIefGASWGEV---PDGESLHHTLgqlswlseqSCA----------GHNVLAL-TNSLDDvsgQTTDRVLMLARIKR 482
Cdd:COG5001 367 HELYV--SASIGIAlypDDGADAEELL---------RNAdlamyrakaaGRNRYRFfDPEMDE---RARERLELEADLRR 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 483 ALDVGGLHLYAQPIHNARGE---GyFEILSRLES-EGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPSE-RAG 557
Cdd:COG5001 433 ALERGELELHYQPQVDLATGrivG-AEALLRWQHpERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAgLPD 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 558 TRFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANFERL 637
Cdd:COG5001 512 LRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYL 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 638 KRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPLTALEA 717
Cdd:COG5001 592 KRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEA 671
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
473-717 |
1.63e-52 |
|
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: 190.13 E-value: 1.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 473 RVLMLARIKRALDVGGLHLYAQPI---HNARGEGyFEILSRLE-SEGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWM 548
Cdd:COG4943 269 RLSPRRRLRRAIKRREFYVHYQPIvdlKTGRCVG-AEALVRWRdPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 549 RSHPSERAGTRFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQaFSDSGSSINNIQQLRDYGFRIAIDDFG 628
Cdd:COG4943 348 GDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERG-FIDPAKARAVIAALREAGHRIAIDDFG 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 629 TGYANFERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGK 708
Cdd:COG4943 427 TGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAK 506
|
....*....
gi 578264101 709 PLPLTALEA 717
Cdd:COG4943 507 PLPAEEFIA 515
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
309-717 |
2.26e-34 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 139.82 E-value: 2.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 309 QER----ALTDPLTGLPNIRALEVFLQHHPEAK------VCCLRLDNLEFLSRHYGILMRVHCKKMITASLQPLLQKDEK 378
Cdd:PRK10060 230 QERlrilANTDSITGLPNRNAIQELIDHAINAAdnnqvgIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLEEDQT 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 379 LFQLPGSELVVvLLGPGTAERLQYMvdhlnSRKIVwnkTELDIEFGASWGEVPDGESLHHTLGQLSwlseqscaGHNVLA 458
Cdd:PRK10060 310 LARLGGDEFLV-LASHTSQAALEAM-----ASRIL---TRLRLPFRIGLIEVYTGCSIGIALAPEH--------GDDSES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 459 LTNSLDDV------SGQTTDRVL---MLARI----------KRALDVGGLHLYAQPIHNARGEGY-FEILSRLES-EGEI 517
Cdd:PRK10060 373 LIRSADTAmytakeGGRGQFCVFspeMNQRVfeylwldtnlRKALENDQLVIHYQPKITWRGEVRsLEALVRWQSpERGL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 518 ITPDRFIP------LIAQfnLSHRFDLNVVEKLLMWmrshpseRA---GTRFSVNLMPLTLMQNEIAAEIIALFERYAIA 588
Cdd:PRK10060 453 IPPLEFISyaeesgLIVP--LGRWVMLDVVRQVAKW-------RDkgiNLRVAVNVSARQLADQTIFTALKQALQELNFE 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 589 PQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANFERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSI 668
Cdd:PRK10060 524 YCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAI 603
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 578264101 669 CNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPLTALEA 717
Cdd:PRK10060 604 VAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFER 652
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
561-717 |
5.92e-34 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 138.31 E-value: 5.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 561 SVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYAN---FERL 637
Cdd:PRK13561 489 SVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGlrqLQHM 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 638 KRLEADIIKIDGCFVKDICTDsmDAMiVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPLTALEA 717
Cdd:PRK13561 569 KSLPIDVLKIDKMFVDGLPED--DSM-VAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIFEE 645
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
315-711 |
5.71e-32 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 132.97 E-value: 5.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 315 DPLTGLPN----IRALEVFLQHHPEAKVCCLRLDNLEFLSRHYGILMRVHCKKMITASLQPLLQKDEKLFQLPGSELVVV 390
Cdd:PRK11359 379 DPLTGLPNrnnlHNYLDDLVDKAVSPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLV 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 391 LLGpGTAERLQYMVDHLnsRKIVWNKTELD---IEFGASWGEVPDGESLHHTLgqlswLSEQSCA-------GHNVLALT 460
Cdd:PRK11359 459 SLE-NDVSNITQIADEL--RNVVSKPIMIDdkpFPLTLSIGISYDVGKNRDYL-----LSTAHNAmdyirknGGNGWQFF 530
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 461 NSldDVSGQTTDRVLMLARIKRALDVGGLHLYAQP-IHNARGEGY-FEILSRL-ESEGEIITPDRFIPLIAQF----NLS 533
Cdd:PRK11359 531 SP--AMNEMVKERLVLGAALKEAISNNQLKLVYQPqIFAETGELYgIEALARWhDPLHGHVPPSRFIPLAEEIgeieNIG 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 534 HRFDLNVVEKLLMWmrshpsERAGTR---FSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSIN 610
Cdd:PRK11359 609 RWVIAEACRQLAEW------RSQNIHipaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFK 682
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 611 NIQQLRDYGFRIAIDDFGTGYANFERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQR 690
Cdd:PRK11359 683 RIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQF 762
|
410 420
....*....|....*....|.
gi 578264101 691 EMLLRFGVDYLQGYLIGKPLP 711
Cdd:PRK11359 763 EMLRKIHCRVIQGYFFSRPLP 783
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
312-715 |
6.43e-32 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 133.26 E-value: 6.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 312 ALTDPLTGLPN--------IRALEVFLQHHPEAKVCCLRLDNL------------EFLSRHYGILMRVHckkmitaslqp 371
Cdd:PRK09776 665 ASHDALTHLANrasfekqlRRLLQTVNSTHQRHALVFIDLDRFkavndsaghaagDALLRELASLMLSM----------- 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 372 lLQKDEKLFQLPGSELVVVLLG---PGTAERLQYMVDHLNSRKIVWNKTELDIefGASWGEVPDGESLHhtlgQLSWLSE 448
Cdd:PRK09776 734 -LRSSDVLARLGGDEFGLLLPDcnvESARFIATRIISAINDYHFPWEGRVYRV--GASAGITLIDANNH----QASEVMS 806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 449 QS---C-----AGHNVLALTNSlDDVSGQTTDRVLMLA-RIKRALDVGGLHLYAQPIH--NARGEGYFEILSRL-ESEGE 516
Cdd:PRK09776 807 QAdiaCyaaknAGRGRVTVYEP-QQAAAHSEHRALSLAeQWRMIKENQLMMLAHGVASprIPEARNHWLISLRLwDPEGE 885
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 517 IITPDRFIPLIAQFNLSHRFDLNVVEKLLmwmRSHPSERA--GTRFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVI 594
Cdd:PRK09776 886 IIDEGAFRPAAEDPALMHALDRRVIHEFF---RQAAKAVAskGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHL 962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 595 EITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYANFERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKT 674
Cdd:PRK09776 963 EITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQR 1042
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 578264101 675 KSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPLTAL 715
Cdd:PRK09776 1043 LGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| MASE1 |
pfam05231 |
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate ... |
2-302 |
6.81e-27 |
|
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: 111.35 E-value: 6.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 2 IALALSLIAIPFSryISPRAIVSENDVYLAWLPLSAMLAIVLLFGRRAIIPLLLSFSITNIY---NLDLAPLQSAVLLCC 78
Cdd:pfam05231 4 LLLLLYALLAAVS--LSLALALVSSGSAPIWLPTGLALAALLLFGRRGWPGILLGAVLASLMaglLSGLNLLLALAIAAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 79 QTFTVFAACGVIRLVLGKRWRHSIPnkyigirIFWLGFMVPVGIKLSMYLAGYLFDFPVTISSYFGEGSAIYNVIDIQSL 158
Cdd:pfam05231 82 NALEALLGAALLRRLLPGRNRLQRL-------RFWLRLVIPGAIIAALLLAIIGLALLLLLGLIPLAPFSIVWLTWWLGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 159 ICAALIFTMMFYYPLRMIINPRYARTFWRRSVKPLFCHKKALFIVVWLMLLISMIAILCAPFESqFIAGYLM--PIVFIL 236
Cdd:pfam05231 155 ATGVLVVTPLLLLLRRYLRLRHRLRLWYERDLAPAAAKLLLLFALLLLLILSLLLLLLCMPEIN-YPLGYLLlpPLLWAA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 578264101 237 FTLGIGRLSYALIsLFWAASALMLLTYNYNFLNGVESGHSLSFILSVLISFAICLLY-MSRIYQKSE 302
Cdd:pfam05231 234 FRFGVRGGSLAAL-LLAVLLILFTLQGGGPFLQTSGDESSQAILLQLFLAILALVALlVSAAISEQR 299
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
480-717 |
1.29e-26 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 115.42 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 480 IKRALDVGGLHLYAQPIHNARGE---GYFEILSRLESEGEIITPDRFIPLIAQFNLSHRFDLNVVEK----LLMWMRSHP 552
Cdd:PRK11829 410 LLQAIENHDFTLFLQPQWDMKRQqviGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEacriLADWKARGV 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 553 SeragTRFSVNLMPLTLMQNEIAAEIIALFERYAIAPQDIVIEITEEQAFSDSGSSINNIQQLRDYGFRIAIDDFGTGYA 632
Cdd:PRK11829 490 S----LPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYS 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 633 NFERL---KRLEADIIKIDGCFVKDICTDSMDAMIVQSIcnmAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKP 709
Cdd:PRK11829 566 SLRYLnhlKSLPIHMIKLDKSFVKNLPEDDAIARIISCV---SDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
|
....*...
gi 578264101 710 LPLTALEA 717
Cdd:PRK11829 643 LPRAEFEA 650
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
480-715 |
9.87e-25 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 108.54 E-value: 9.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 480 IKRaldvGGLHLYAQPI---HNARGEGyFEILSRLE--SEGEIiTPDRFIPLIAQFNL-----SHRFDLNVVEKLLMwMR 549
Cdd:PRK10551 272 IKR----GQFYVEYQPVvdtQTLRVTG-LEALLRWRhpTAGEI-PPDAFINYAEAQKLivpltQHLFELIARDAAEL-QK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 550 SHPserAGTRFSVNLMPLTLMQNEIAAEIIALFeryAIAPQD---IVIEITEEQAFSDSgSSINNIQQLRDYGFRIAIDD 626
Cdd:PRK10551 345 VLP---VGAKLGINISPAHLHSDSFKADVQRLL---ASLPADhfqIVLEITERDMVQEE-EATKLFAWLHSQGIEIAIDD 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 627 FGTGYANFERLKRLEADIIKIDGCFVKDICTDSMDAMIVQSICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLI 706
Cdd:PRK10551 418 FGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWI 497
|
....*....
gi 578264101 707 GKPLPLTAL 715
Cdd:PRK10551 498 SRPLPLEDF 506
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
310-458 |
4.85e-17 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 78.83 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 310 ERALTDPLTGLPNIRALEVFL----QHHPEAK----VCCLRLDNLEFLSRHYGILMRVHCKKMITASLQPLLQKDEKLFQ 381
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELeqelQRAQRQGspfaLLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 382 LPGSELVVVLLGPGTAERL---QYMVDHLNSRKIVWNKT-ELDIEFGASWG--EVPDGESLHHTLGQLSWLSEQSCAGHN 455
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIalaERILQQLREPIIIHGIPlYLTISIGVAAYpnPGEDAEDLLKRADTALYQAKKAGRNQV 160
|
...
gi 578264101 456 VLA 458
Cdd:smart00267 161 AVY 163
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
589-714 |
3.36e-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: 72.14 E-value: 3.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 589 PQDIVIEITEEQAFSDSGssINNIQQLRDYGFRIAIDDFgTGYANFERLKRLeADIIKIDgcfvkdicTDSMDAMIVQSI 668
Cdd:COG3434 83 PERVVLEILEDVEPDEEL--LEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKID--------VLALDLEELAEL 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 578264101 669 CNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPLTA 714
Cdd:COG3434 151 VARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILKG 196
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
480-712 |
1.07e-10 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 64.88 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 480 IKRALDVGGLHLYAQPIHNARGEG-YFEILSRL-ESEGEIITPDRFIPLIAQFNLSHRFDLNVVEKLLMWMRSHPSErag 557
Cdd:PRK11059 408 LEQTLVRGGPRLYQQPAVTRDGKVhHRELFCRIrDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE--- 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 558 tRFSVNLMPLTLMQNEiaaeiialFERY----------AIAPQdIVIEITEEQAfsdsgssINNIQQLRD-------YGF 620
Cdd:PRK11059 485 -NLSINLSVDSLLSRA--------FQRWlrdtllqcprSQRKR-LIFELAEADV-------CQHISRLRPvlrmlrgLGC 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 621 RIAIDDFG-----TGYanferLKRLEADIIKIDGCFVKDICTDSMDAMIVQSI---CNMAKTKslcVVAEYVESAEQREM 692
Cdd:PRK11059 548 RLAVDQAGltvvsTSY-----IKELNVELIKLHPSLVRNIHKRTENQLFVRSLvgaCAGTETQ---VFATGVESREEWQT 619
|
250 260
....*....|....*....|
gi 578264101 693 LLRFGVDYLQGYLIGKPLPL 712
Cdd:PRK11059 620 LQELGVSGGQGDFFAESQPL 639
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
199-440 |
1.37e-08 |
|
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: 56.53 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 199 ALFIVVWLMLLISMIAILCAPFESQFIAGYLMPIVFILFTLGIGRLSYALISLFWAASALMLLTYNYNFLNGVESGHSLS 278
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 279 FILSVLISFAICLLYMSRIYQKSEWLKQGWQERALTDPLTGLPNIRALEVFLQHHPEAK--------VCCLRLDNLEFLS 350
Cdd:COG2199 81 LELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARArregrplaLLLIDLDHFKRIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 351 RHYGILMRVHCKKMITASLQPLLQKDEKLFQLPGSELVVVLlgPGT--------AERLQymvDHLNSRKIVWNKTELDIe 422
Cdd:COG2199 161 DTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLL--PGTdleeaealAERLR---EALEQLPFELEGKELRV- 234
|
250 260
....*....|....*....|.
gi 578264101 423 fGASWGEV---PDGESLHHTL 440
Cdd:COG2199 235 -TVSIGVAlypEDGDSAEELL 254
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
518-717 |
4.40e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 51.93 E-value: 4.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 518 ITPDRFIpliAQFNLSHRFDLnVVEKLLMWMRSHPS-ERAGTRFSVNLMPLTLMQNEIAAEIIALFERYAIapqdIVIEI 596
Cdd:PRK11596 63 LSPERYF---AEITVSHRLDV-VKEQLDLLAQWADFfVRHGLLASVNIDGPTLIALRQQPAILRLIERLPW----LRFEL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 597 TEEQAFSDSGSsinnIQQLRDYGfRIAIDDFGTGYANFERLKRLEADIIKID-GCFVkdictdsmdaMIVQS-------- 667
Cdd:PRK11596 135 VEHIRLPKDSP----FASMCEFG-PLWLDDFGTGMANFSALSEVRYDYIKVArELFI----------MLRQSeegrnlfs 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 578264101 668 -ICNMAKTKSLCVVAEYVESAEQREMLLRFGVDYLQGYLIGKPLPLTALEA 717
Cdd:PRK11596 200 qLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETLET 250
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
312-428 |
6.90e-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: 49.56 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578264101 312 ALTDPLTGLPNIRALEVFL---------QHHPEAkVCCLRLDNLEFLSRHYGILMRVHCKKMITASLQPLLQKDEKLFQL 382
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLeqelqralrEGSPVA-VLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 578264101 383 PGSELVVVLLGPGT------AERLQYMVDHLnsrKIVWNKTELDIEFGASWG 428
Cdd:pfam00990 80 GGDEFAILLPETSLegaqelAERIRRLLAKL---KIPHTVSGLPLYVTISIG 128
|
|
| |
