|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
5-513 |
0e+00 |
|
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: 520.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 5 FDRRWFLAIMTIVLVAAGAL---CGTWISRLVVISSDRGQMQIFADQLLNRAVEVFAEADKMLAVVNASPHPFCSDKEIM 81
Cdd:COG4943 3 MRRRRLLSLATLLALLAALLpllLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 82 FLRDMLFGTKYLKDMGRVRDGFFHCSAVfGNGKKPMPLIKHDLETPDGKLIYANSRLAISK-STAPIIGIGNANVVLDPA 160
Cdd:COG4943 83 ALRRLVFSSRYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPgRPMLIVGRGNYVVVIDPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 161 AFETLKNPAYTFGVMYNPQGVSSTVGMFGTLDIGKTGMEL--PAGAGRIGDTVYRNVC--RNTACVTVHAEVGRLESSAE 236
Cdd:COG4943 162 AFIDVLSPQPGISLALLATNGGHLFASSGNPDPALLSRLLrgPSSWFIQGDRLYASACspQYPICVVAAAPLAGLLALWR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 237 PITSIITTFGAALGGAAAVILILLQRNNLSLKARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDV 315
Cdd:COG4943 242 QLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRdPDGSVISPDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 316 FIPVAEKAGLINRLTICVIDHVLSDMAASLDANPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERSTA 395
Cdd:COG4943 322 FIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 396 NAADAKEAIERLRSRGHKIYIDDFGTGYSSLAYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEG 475
Cdd:COG4943 402 DPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEG 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 1277281641 476 IETTAQRDYFAALKPKVdGQGWLFGRPASAITIKKALE 513
Cdd:COG4943 482 VETEEQADYLRARGVQY-GQGWLFAKPLPAEEFIAWLA 518
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
269-505 |
1.19e-92 |
|
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: 282.13 E-value: 1.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 269 ARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLSDMAASLDA 347
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRhPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 348 NPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERST-ANAADAKEAIERLRSRGHKIYIDDFGTGYSSL 426
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALiDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 427 AYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALkpKVD-GQGWLFGRPASA 505
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLREL--GCDyVQGYLFSRPLPA 238
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
269-502 |
1.48e-75 |
|
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: 237.99 E-value: 1.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 269 ARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLSDMAaSLDA 347
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQhPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA-QLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 348 NPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERS-TANAADAKEAIERLRSRGHKIYIDDFGTGYSSL 426
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDlLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277281641 427 AYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALkpKVD-GQGWLFGRP 502
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALREL--GCDlVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
270-502 |
3.41e-75 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 237.50 E-value: 3.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 270 RLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLSDMAASLDA- 347
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQhPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 348 NPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITER-STANAADAKEAIERLRSRGHKIYIDDFGTGYSSL 426
Cdd:smart00052 83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESvLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277281641 427 AYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALKPKVdGQGWLFGRP 502
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDY-GQGYLFSRP 237
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
267-505 |
3.90e-44 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 165.24 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 267 LKARLQHALSQNRLTVEYQPIVDvATGRPVAAEALVRWR--ENGEwIPPDVFIPVAEKAGLINRLTICVIDHVLSDMAAS 344
Cdd:PRK10060 409 LDTNLRKALENDQLVIHYQPKIT-WRGEVRSLEALVRWQspERGL-IPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKW 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 345 LDANPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERS-TANAADAKEAIERLRSRGHKIYIDDFGTGY 423
Cdd:PRK10060 487 RDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESClIENEELALSVIQQFSQLGAQVHLDDFGTGY 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 424 SSLAYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFaaLKPKVDG-QGWLFGRP 502
Cdd:PRK10060 567 SSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFL--TKNGVNErQGFLFAKP 644
|
...
gi 1277281641 503 ASA 505
Cdd:PRK10060 645 MPA 647
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
5-513 |
0e+00 |
|
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: 520.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 5 FDRRWFLAIMTIVLVAAGAL---CGTWISRLVVISSDRGQMQIFADQLLNRAVEVFAEADKMLAVVNASPHPFCSDKEIM 81
Cdd:COG4943 3 MRRRRLLSLATLLALLAALLpllLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAHLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 82 FLRDMLFGTKYLKDMGRVRDGFFHCSAVfGNGKKPMPLIKHDLETPDGKLIYANSRLAISK-STAPIIGIGNANVVLDPA 160
Cdd:COG4943 83 ALRRLVFSSRYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDYVTADGYRLWLNVDNPLDPgRPMLIVGRGNYVVVIDPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 161 AFETLKNPAYTFGVMYNPQGVSSTVGMFGTLDIGKTGMEL--PAGAGRIGDTVYRNVC--RNTACVTVHAEVGRLESSAE 236
Cdd:COG4943 162 AFIDVLSPQPGISLALLATNGGHLFASSGNPDPALLSRLLrgPSSWFIQGDRLYASACspQYPICVVAAAPLAGLLALWR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 237 PITSIITTFGAALGGAAAVILILLQRNNLSLKARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDV 315
Cdd:COG4943 242 QLLLLLLPLGLLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRdPDGSVISPDI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 316 FIPVAEKAGLINRLTICVIDHVLSDMAASLDANPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERSTA 395
Cdd:COG4943 322 FIPLAEQSGLISPLTRQVIEQVFRDLGDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 396 NAADAKEAIERLRSRGHKIYIDDFGTGYSSLAYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEG 475
Cdd:COG4943 402 DPAKARAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEG 481
|
490 500 510
....*....|....*....|....*....|....*...
gi 1277281641 476 IETTAQRDYFAALKPKVdGQGWLFGRPASAITIKKALE 513
Cdd:COG4943 482 VETEEQADYLRARGVQY-GQGWLFAKPLPAEEFIAWLA 518
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
269-505 |
1.19e-92 |
|
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: 282.13 E-value: 1.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 269 ARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLSDMAASLDA 347
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRhPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 348 NPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERST-ANAADAKEAIERLRSRGHKIYIDDFGTGYSSL 426
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALiDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 427 AYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALkpKVD-GQGWLFGRPASA 505
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLREL--GCDyVQGYLFSRPLPA 238
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
262-513 |
9.12e-83 |
|
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: 267.81 E-value: 9.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 262 RNNLSLKARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLSD 340
Cdd:COG2200 324 RRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRhPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 341 MAASLDANPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERS-TANAADAKEAIERLRSRGHKIYIDDF 419
Cdd:COG2200 404 LARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESAlLEDLEAAIELLARLRALGVRIALDDF 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 420 GTGYSSLAYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALkpKVD-GQGWL 498
Cdd:COG2200 484 GTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALREL--GCDyAQGYL 561
|
250
....*....|....*
gi 1277281641 499 FGRPASAITIKKALE 513
Cdd:COG2200 562 FGRPLPLEELEALLR 576
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
262-505 |
1.38e-79 |
|
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: 262.02 E-value: 1.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 262 RNNLSLKARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLSD 340
Cdd:COG5001 421 RERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQhPERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQ 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 341 MAASLDA-NPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERS-TANAADAKEAIERLRSRGHKIYIDD 418
Cdd:COG5001 501 LAAWQDAgLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESAlLEDPEEALETLRALRALGVRIALDD 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 419 FGTGYSSLAYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALkpKVD-GQGW 497
Cdd:COG5001 581 FGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLREL--GCDyAQGY 658
|
....*...
gi 1277281641 498 LFGRPASA 505
Cdd:COG5001 659 LFSRPLPA 666
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
269-502 |
1.48e-75 |
|
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: 237.99 E-value: 1.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 269 ARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLSDMAaSLDA 347
Cdd:pfam00563 2 RALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQhPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA-QLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 348 NPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERS-TANAADAKEAIERLRSRGHKIYIDDFGTGYSSL 426
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDlLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277281641 427 AYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALkpKVD-GQGWLFGRP 502
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALREL--GCDlVQGYYFSKP 235
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
270-502 |
3.41e-75 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 237.50 E-value: 3.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 270 RLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR-ENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLSDMAASLDA- 347
Cdd:smart00052 3 ELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQhPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 348 NPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITER-STANAADAKEAIERLRSRGHKIYIDDFGTGYSSL 426
Cdd:smart00052 83 PPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESvLLDDDESAVATLQRLRELGVRIALDDFGTGYSSL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277281641 427 AYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALKPKVdGQGWLFGRP 502
Cdd:smart00052 163 SYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDY-GQGYLFSRP 237
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
267-505 |
3.90e-44 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 165.24 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 267 LKARLQHALSQNRLTVEYQPIVDvATGRPVAAEALVRWR--ENGEwIPPDVFIPVAEKAGLINRLTICVIDHVLSDMAAS 344
Cdd:PRK10060 409 LDTNLRKALENDQLVIHYQPKIT-WRGEVRSLEALVRWQspERGL-IPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKW 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 345 LDANPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERS-TANAADAKEAIERLRSRGHKIYIDDFGTGY 423
Cdd:PRK10060 487 RDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESClIENEELALSVIQQFSQLGAQVHLDDFGTGY 566
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 424 SSLAYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFaaLKPKVDG-QGWLFGRP 502
Cdd:PRK10060 567 SSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFL--TKNGVNErQGFLFAKP 644
|
...
gi 1277281641 503 ASA 505
Cdd:PRK10060 645 MPA 647
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
274-504 |
1.35e-39 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 150.53 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 274 ALSQNRLTVEYQPIVDVATGRPVAAEALVRWRE--NGEwIPPDVFIPVAEKAGLINRLTICVIDHVLSD---MAASLDAN 348
Cdd:PRK10551 271 GIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHptAGE-IPPDAFINYAEAQKLIVPLTQHLFELIARDaaeLQKVLPVG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 349 PDFhiSINISAADLFDRHFGALLALRLKEANVANNQIALEITERSTANAADAKEAIERLRSRGHKIYIDDFGTGYSSLAY 428
Cdd:PRK10551 350 AKL--GINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEATKLFAWLHSQGIEIAIDDFGTGHSALIY 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 429 LGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAAlkpkvDG----QGWLFGRPAS 504
Cdd:PRK10551 428 LERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRE-----RGvnflQGYWISRPLP 502
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
271-502 |
1.39e-38 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 149.48 E-value: 1.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 271 LQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWREN-GEWIPPDVFIPVAEKAGLINRLTICVIDHVLSDMAASLDANP 349
Cdd:PRK13561 405 ILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPdGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQERGI 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 350 DFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITErsTANAADAKEAIERLR---SRGHKIYIDDFGTGYSSL 426
Cdd:PRK13561 485 MLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTE--SRRIDDPHAAVAILRplrNAGVRVALDDFGMGYAGL 562
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277281641 427 AYLGE---LNVDGIKIDKSFTQTIGTSSvsvSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALKPKVdGQGWLFGRP 502
Cdd:PRK13561 563 RQLQHmksLPIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGI-AQGFLFARA 637
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
262-508 |
5.11e-33 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 133.74 E-value: 5.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 262 RNNLSLKARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVRWR--ENGEwIPPDVFIPVAEKAGLINRLTICVIDHVLS 339
Cdd:PRK11359 539 KERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHdpLHGH-VPPSRFIPLAEEIGEIENIGRWVIAEACR 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 340 DMAASLDANPDFH-ISINISAADLFDRHFGALLALRLKEANVANNQIALEITErSTANAADAK--EAIERLRSRGHKIYI 416
Cdd:PRK11359 618 QLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITE-SMMMEHDTEifKRIQILRDMGVGLSV 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 417 DDFGTGYSSLAYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALKPKVdGQG 496
Cdd:PRK11359 697 DDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRV-IQG 775
|
250
....*....|..
gi 1277281641 497 WLFGRPASAITI 508
Cdd:PRK11359 776 YFFSRPLPAEEI 787
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
268-504 |
4.32e-32 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 130.45 E-value: 4.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 268 KARLQ------HALSQNRLTVEYQPIVDVATGRPVAAEALVRW-RENGEWIPPDVFIPVAEKAGLINRLTICVIDH---V 337
Cdd:PRK11829 401 HKRLTqendllQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWcQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEacrI 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 338 LSDMAASLDANPdfhISINISAADLFDRHFGALLALRLKEANVANNQIALEITErsTANAADAKEA---IERLRSRGHKI 414
Cdd:PRK11829 481 LADWKARGVSLP---LSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITE--TAQIQDLDEAlrlLRELQGLGLLI 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 415 YIDDFGTGYSSLAYL---GELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARahgLAIVVEGIETTAQRDYFAALKPK 491
Cdd:PRK11829 556 ALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDVLK---VRVMAEGVETEEQRQWLLEHGIQ 632
|
250
....*....|...
gi 1277281641 492 VdGQGWLFGRPAS 504
Cdd:PRK11829 633 C-GQGFLFSPPLP 644
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
261-502 |
1.12e-23 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 105.52 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 261 QRNNLSLKARLQHALSQNRLTVEYQPIVDVATGRPVAAEALVR-WRENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLS 339
Cdd:PRK09776 836 EHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRlWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFR 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 340 DMAASLdANPDFHISINISAADLFDRHFGALLALRLKEANVANNQIALEITERSTANAAD-AKEAIERLRSRGHKIYIDD 418
Cdd:PRK09776 916 QAAKAV-ASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAEsASRLVQKLRLAGCRVVLSD 994
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 419 FGTGYSSLAYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIETTAQRDYFAALkpKVDG-QGW 497
Cdd:PRK09776 995 FGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGI--GVDLaYGY 1072
|
....*
gi 1277281641 498 LFGRP 502
Cdd:PRK09776 1073 AIARP 1077
|
|
| CSS-motif |
pfam12792 |
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ... |
38-233 |
5.18e-17 |
|
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS sequence motif is found N-terminal to the EAL, pfam00563, domain in many cyclic diguanylate phosphodiesterases.
Pssm-ID: 463709 Cd Length: 209 Bit Score: 79.88 E-value: 5.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 38 DRGQMQIFADQLLNRAVEVFAEADKMLAVVNASPHPFCSDKEIMFLRDMLFGTKYLKDMGRVRDGFFHCSAVFGNGKKPM 117
Cdd:pfam12792 1 EQEQLDAFAERALRRLESVLDQADQALDRLLPLTGQPCSPAHLAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGELDTPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 118 PLIKHDLETPDG-KLIYANSRLAISKSTAPIIGIGNANVVLDPAAFetlKNPAYTFGVMY-----NPQGVSSTVGMFGTL 191
Cdd:pfam12792 81 PLLPPDLTTPPGvRLWLLRGTPLVPGRPALVLRRGGYGVVIDPGVF---IDVQYLPGLLAavsqpDGRLLALVVGDDALL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1277281641 192 DIGK--TGMELPAGAGRIGDTVYRNVCRNTA--CVTVHAEVGRLES 233
Cdd:pfam12792 158 FDGRlhSLAEPAPGTARSGGALYARARSTRYplTVVVYAPRASLLA 203
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
271-447 |
2.58e-06 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 50.25 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 271 LQHALSQNRLTVEYQPIVDVaTGRPVAAEALVRWR-ENGEWIPPDVFIPVAEKAGLINRLTICVIDHVLSDmaasLDANP 349
Cdd:PRK11059 408 LEQTLVRGGPRLYQQPAVTR-DGKVHHRELFCRIRdGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPL----LRYWP 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 350 DFHISINISAADLFDRHFGALLALRLKEANVA-NNQIALEITErstanaADAKEAIERLRSR-------GHKIYIDDFGT 421
Cdd:PRK11059 483 EENLSINLSVDSLLSRAFQRWLRDTLLQCPRSqRKRLIFELAE------ADVCQHISRLRPVlrmlrglGCRLAVDQAGL 556
|
170 180
....*....|....*....|....*.
gi 1277281641 422 GYSSLAYLGELNVDGIKIDKSFTQTI 447
Cdd:PRK11059 557 TVVSTSYIKELNVELIKLHPSLVRNI 582
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
412-504 |
1.82e-05 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 46.15 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 412 HKIYIDDFGTGYSSLAYLGELNVDGIKIDKSFTQTIGTSSVSVSIVPQIIDMARAHGLAIVVEGIET------TAQRDYF 485
Cdd:PRK11596 153 GPLWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETpeewrdVQRSPAF 232
|
90
....*....|....*....
gi 1277281641 486 AAlkpkvdgQGWLFGRPAS 504
Cdd:PRK11596 233 AA-------QGYFLSRPAP 244
|
|
| Hydrolase_3 |
pfam08282 |
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like ... |
388-479 |
5.49e-03 |
|
haloacid dehalogenase-like hydrolase; This family contains haloacid dehalogenase-like hydrolase enzymes.
Pssm-ID: 429897 [Multi-domain] Cd Length: 255 Bit Score: 38.76 E-value: 5.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277281641 388 EITERStanaadaKEAIERLRSRGHKIYIddfGTG---YSSLAYLGELNVDGIKI--------DKSFtQTIGTSSVSVSI 456
Cdd:pfam08282 15 KISEKT-------KEAIKKLKEKGIKFVI---ATGrpyRAILPVIKELGLDDPVIcyngaliyDENG-KILYSNPISKEA 83
|
90 100
....*....|....*....|...
gi 1277281641 457 VPQIIDMARAHGLAIVVEGIETT 479
Cdd:pfam08282 84 VKEIIEYLKENNLEILLYTDDGV 106
|
|
| |
