|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
10-520 |
2.67e-151 |
|
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: 442.82 E-value: 2.67e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 10 QFRRKRL-----LIALSIATVVLILTLAFRYIEEKSRIEQQAMDFADKAIMRFDRMFSPLEVSASNTLGLVGAPCQDV-R 83
Cdd:COG4943 2 RMRRRRLlslatLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAhL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 84 FPLIEKISSLQTVRAILLVENDMLYCSSIyGPRNIPFSQTYPD-LAFNSQRMTLATDEYLLKGSPILLLWtpksldnRSG 162
Cdd:COG4943 82 AALRRLVFSSRYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDyVTADGYRLWLNVDNPLDPGRPMLIVG-------RGN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 163 ILQVINIEMMSNYLLEPqlPWVERAVFNVNGESLEYGNPLIEPTV------------PSDDEVSYEQGSLRYPFTLTLYG 230
Cdd:COG4943 154 YVVVIDPAAFIDVLSPQ--PGISLALLATNGGHLFASSGNPDPALlsrllrgpsswfIQGDRLYASACSPQYPICVVAAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 231 PSPTRLALATLPSQLPLAL--LLSLLMGYIIWLATANRMSLSWQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHN 308
Cdd:COG4943 232 PLAGLLALWRQLLLLLLPLglLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 309 ARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQ-LPDDSAFHIAINVAASHFRDRAILEDLQNLWWPAS-PVPQL 386
Cdd:COG4943 312 PDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDlLAADPDFHISINLSASDLLSPRFLDDLERLLARTGvAPQQI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 387 VVELTERDALPVVD-QSVIAQLHEIGVRLAIDDFGTGHSSLSYLKDLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQ 465
Cdd:COG4943 392 VLEITERGFIDPAKaRAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAK 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1750418682 466 RLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLEDFPAWLTRHQADARR 520
Cdd:COG4943 472 TLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRAPASA 526
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
11-511 |
8.81e-91 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 287.27 E-value: 8.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 11 FRRKRLLIALSIATVVLILTLAFRYIEEKSRIEQQAMDFADKAIMRFDRMFSPLEVSASNTLGLVGAPCQDVRFPLIEKI 90
Cdd:PRK10551 8 SGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVNPELTSRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 91 SSLQTVRAILLVENDMLYCSSIYGPRNIPFSQTYPDLAFNSQR-MTLATDEYLLKGSPILLLWTPKSLDNRSGILQVINI 169
Cdd:PRK10551 88 AFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVdMAILPGTPMMPNKPAIVIWYRNPLLKNSGVFATLNL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 170 EMMSnYLL----EPQLPWV-----ERAV--FN---VNGESLEyGNPLIEPTVPSddevsyeqgslrYPFTLTLYGPSPT- 234
Cdd:PRK10551 168 NLTP-YLLytsrQEDFDGIaliigNTALstFSsrlMNVNELP-DMPLRETTIPG------------YPLTIRLYADSWTa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 235 ---RLALatlpsqlPLALLLSLLMGYIIWLATANRMSLSWQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQ 311
Cdd:PRK10551 234 ndiWYAL-------LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 312 GWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQL----PDDSAFhiAINVAASHFRDRAILEDLQNlWWPASPVP--Q 385
Cdd:PRK10551 307 GEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELqkvlPVGAKL--GINISPAHLHSDSFKADVQR-LLASLPADhfQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 386 LVVELTERDalpVVDQSVIAQ----LHEIGVRLAIDDFGTGHSSLSYLKDLQPDVLKIDKIFTAAIGTDAINATVTDMVI 461
Cdd:PRK10551 384 IVLEITERD---MVQEEEATKlfawLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVL 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1750418682 462 SLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLEDFPAWL 511
Cdd:PRK10551 461 TLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVRWL 510
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
276-506 |
5.11e-89 |
|
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: 272.88 E-value: 5.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 276 GITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQLPD-DSAFH 354
Cdd:cd01948 6 ALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAgGPDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 355 IAINVAASHFRDRAILEDLQNLWwPASPVP--QLVVELTERDALPVVDQS--VIAQLHEIGVRLAIDDFGTGHSSLSYLK 430
Cdd:cd01948 86 LSVNLSARQLRDPDFLDRLLELL-AETGLPprRLVLEITESALIDDLEEAlaTLRRLRALGVRIALDDFGTGYSSLSYLK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1750418682 431 DLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLED 506
Cdd:cd01948 165 RLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
271-506 |
2.55e-86 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 266.01 E-value: 2.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 271 WQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQLPDD 350
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 351 S--AFHIAINVAASHFRDRAILEDLQNLWWPASPVP-QLVVELTERDALPVVDQSV--IAQLHEIGVRLAIDDFGTGHSS 425
Cdd:smart00052 82 GppPLLISINLSARQLISPDLVPRVLELLEETGLPPqRLELEITESVLLDDDESAVatLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 426 LSYLKDLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLE 505
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
.
gi 1750418682 506 D 506
Cdd:smart00052 242 D 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
272-501 |
2.74e-71 |
|
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: 227.20 E-value: 2.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 272 QISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQLPDDS 351
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 352 AFHIAINVAASHFRDRAILEDLQNLWWPASPVPQ-LVVELTERDALPVVD--QSVIAQLHEIGVRLAIDDFGTGHSSLSY 428
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSrLVLEITESDLLARLEalREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1750418682 429 LKDLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARP 501
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
10-520 |
2.67e-151 |
|
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: 442.82 E-value: 2.67e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 10 QFRRKRL-----LIALSIATVVLILTLAFRYIEEKSRIEQQAMDFADKAIMRFDRMFSPLEVSASNTLGLVGAPCQDV-R 83
Cdd:COG4943 2 RMRRRRLlslatLLALLAALLPLLLSLWLAQIQARRREREQLESYAQRALARAERVFDQARSALDELNALPGDPCSPAhL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 84 FPLIEKISSLQTVRAILLVENDMLYCSSIyGPRNIPFSQTYPD-LAFNSQRMTLATDEYLLKGSPILLLWtpksldnRSG 162
Cdd:COG4943 82 AALRRLVFSSRYVRDIGYVRDGRLLCSSL-GKLSKPVPLPPPDyVTADGYRLWLNVDNPLDPGRPMLIVG-------RGN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 163 ILQVINIEMMSNYLLEPqlPWVERAVFNVNGESLEYGNPLIEPTV------------PSDDEVSYEQGSLRYPFTLTLYG 230
Cdd:COG4943 154 YVVVIDPAAFIDVLSPQ--PGISLALLATNGGHLFASSGNPDPALlsrllrgpsswfIQGDRLYASACSPQYPICVVAAA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 231 PSPTRLALATLPSQLPLAL--LLSLLMGYIIWLATANRMSLSWQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHN 308
Cdd:COG4943 232 PLAGLLALWRQLLLLLLPLglLLSLLLGLLVLRLLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 309 ARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQ-LPDDSAFHIAINVAASHFRDRAILEDLQNLWWPAS-PVPQL 386
Cdd:COG4943 312 PDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDlLAADPDFHISINLSASDLLSPRFLDDLERLLARTGvAPQQI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 387 VVELTERDALPVVD-QSVIAQLHEIGVRLAIDDFGTGHSSLSYLKDLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQ 465
Cdd:COG4943 392 VLEITERGFIDPAKaRAVIAALREAGHRIAIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAK 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1750418682 466 RLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLEDFPAWLTRHQADARR 520
Cdd:COG4943 472 TLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAEEFIAWLAAQRAPASA 526
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
11-511 |
8.81e-91 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 287.27 E-value: 8.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 11 FRRKRLLIALSIATVVLILTLAFRYIEEKSRIEQQAMDFADKAIMRFDRMFSPLEVSASNTLGLVGAPCQDVRFPLIEKI 90
Cdd:PRK10551 8 SGRKILLTSIVAGVMIALLFSCLQFLLLWHKREVKYDTLITDVQKYLDTYFADLKSTTDRLQPLTLDTCQQVNPELTSRA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 91 SSLQTVRAILLVENDMLYCSSIYGPRNIPFSQTYPDLAFNSQR-MTLATDEYLLKGSPILLLWTPKSLDNRSGILQVINI 169
Cdd:PRK10551 88 AFSLNVRAFLLVKDKKAFCSSATGEMNTPLSELIPAIDINKPVdMAILPGTPMMPNKPAIVIWYRNPLLKNSGVFATLNL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 170 EMMSnYLL----EPQLPWV-----ERAV--FN---VNGESLEyGNPLIEPTVPSddevsyeqgslrYPFTLTLYGPSPT- 234
Cdd:PRK10551 168 NLTP-YLLytsrQEDFDGIaliigNTALstFSsrlMNVNELP-DMPLRETTIPG------------YPLTIRLYADSWTa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 235 ---RLALatlpsqlPLALLLSLLMGYIIWLATANRMSLSWQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQ 311
Cdd:PRK10551 234 ndiWYAL-------LLGLLSGILVGLLCYYLLSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 312 GWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQL----PDDSAFhiAINVAASHFRDRAILEDLQNlWWPASPVP--Q 385
Cdd:PRK10551 307 GEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELqkvlPVGAKL--GINISPAHLHSDSFKADVQR-LLASLPADhfQ 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 386 LVVELTERDalpVVDQSVIAQ----LHEIGVRLAIDDFGTGHSSLSYLKDLQPDVLKIDKIFTAAIGTDAINATVTDMVI 461
Cdd:PRK10551 384 IVLEITERD---MVQEEEATKlfawLHSQGIEIAIDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVL 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1750418682 462 SLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLEDFPAWL 511
Cdd:PRK10551 461 TLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDFVRWL 510
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
276-506 |
5.11e-89 |
|
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: 272.88 E-value: 5.11e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 276 GITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQLPD-DSAFH 354
Cdd:cd01948 6 ALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAgGPDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 355 IAINVAASHFRDRAILEDLQNLWwPASPVP--QLVVELTERDALPVVDQS--VIAQLHEIGVRLAIDDFGTGHSSLSYLK 430
Cdd:cd01948 86 LSVNLSARQLRDPDFLDRLLELL-AETGLPprRLVLEITESALIDDLEEAlaTLRRLRALGVRIALDDFGTGYSSLSYLK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1750418682 431 DLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLED 506
Cdd:cd01948 165 RLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
271-506 |
2.55e-86 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 266.01 E-value: 2.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 271 WQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQLPDD 350
Cdd:smart00052 2 RELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 351 S--AFHIAINVAASHFRDRAILEDLQNLWWPASPVP-QLVVELTERDALPVVDQSV--IAQLHEIGVRLAIDDFGTGHSS 425
Cdd:smart00052 82 GppPLLISINLSARQLISPDLVPRVLELLEETGLPPqRLELEITESVLLDDDESAVatLQRLRELGVRIALDDFGTGYSS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 426 LSYLKDLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLE 505
Cdd:smart00052 162 LSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLD 241
|
.
gi 1750418682 506 D 506
Cdd:smart00052 242 D 242
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
262-516 |
1.18e-84 |
|
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: 275.50 E-value: 1.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 262 ATANRMSLSWQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVV 341
Cdd:COG5001 419 RARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLREAC 498
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 342 RQLPQLPDD--SAFHIAINVAASHFRDRAILEDLQNLWWpASPVP--QLVVELTERDALPVVDQ--SVIAQLHEIGVRLA 415
Cdd:COG5001 499 RQLAAWQDAglPDLRVAVNLSARQLRDPDLVDRVRRALA-ETGLPpsRLELEITESALLEDPEEalETLRALRALGVRIA 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 416 IDDFGTGHSSLSYLKDLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQG 495
Cdd:COG5001 578 LDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQG 657
|
250 260
....*....|....*....|.
gi 1750418682 496 YYFARPMPLEDFPAWLTRHQA 516
Cdd:COG5001 658 YLFSRPLPAEELEALLRARAA 678
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
262-511 |
2.51e-82 |
|
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: 267.04 E-value: 2.51e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 262 ATANRMSLSWQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVV 341
Cdd:COG2200 322 RARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERAL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 342 RQLPQLPDDSA-FHIAINVAASHFRDRAILEDLQNLWwPASPVP--QLVVELTERDALPVVDQ--SVIAQLHEIGVRLAI 416
Cdd:COG2200 402 RQLARWPERGLdLRLSVNLSARSLLDPDFLERLLELL-AEYGLPpeRLVLEITESALLEDLEAaiELLARLRALGVRIAL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 417 DDFGTGHSSLSYLKDLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGY 496
Cdd:COG2200 481 DDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGY 560
|
250
....*....|....*
gi 1750418682 497 YFARPMPLEDFPAWL 511
Cdd:COG2200 561 LFGRPLPLEELEALL 575
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
272-501 |
2.74e-71 |
|
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: 227.20 E-value: 2.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 272 QISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQLPDDS 351
Cdd:pfam00563 3 ALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 352 AFHIAINVAASHFRDRAILEDLQNLWWPASPVPQ-LVVELTERDALPVVD--QSVIAQLHEIGVRLAIDDFGTGHSSLSY 428
Cdd:pfam00563 83 DIKLSINLSPASLADPGFLELLRALLKQAGPPPSrLVLEITESDLLARLEalREVLKRLRALGIRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1750418682 429 LKDLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARP 501
Cdd:pfam00563 163 LLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
281-516 |
1.65e-51 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 186.04 E-value: 1.65e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 281 EFMVYCQPLINSkSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQLPDDS-AFHIAINV 359
Cdd:PRK10060 421 QLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGiNLRVAVNV 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 360 AASHFRDRAILEDLQNLWWPASPVPQLV-VELTER-----DALPVvdqSVIAQLHEIGVRLAIDDFGTGHSSLSYLKDLQ 433
Cdd:PRK10060 500 SARQLADQTIFTALKQALQELNFEYCPIdVELTESclienEELAL---SVIQQFSQLGAQVHLDDFGTGYSSLSQLARFP 576
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 434 PDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLEDFPAWLTR 513
Cdd:PRK10060 577 IDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKR 656
|
...
gi 1750418682 514 HQA 516
Cdd:PRK10060 657 YLK 659
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
262-516 |
3.70e-45 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 169.56 E-value: 3.70e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 262 ATANRMSLSWQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVV 341
Cdd:PRK11359 537 MVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEAC 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 342 RQLPQLpDDSAFHI---AINVAASHFRDRAI---LEDLQNLWwpASPVPQLVVELTERDALPVVDQ--SVIAQLHEIGVR 413
Cdd:PRK11359 617 RQLAEW-RSQNIHIpalSVNLSALHFRSNQLpnqVSDAMQAW--GIDGHQLTVEITESMMMEHDTEifKRIQILRDMGVG 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 414 LAIDDFGTGHSSLSYLKDLQPDVLKIDKIFTAAIGTDA-INATVtDMVISLAQRLNISLVAEGVETAEQADYLRERGVDH 492
Cdd:PRK11359 694 LSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKrILALL-EAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRV 772
|
250 260
....*....|....*....|....
gi 1750418682 493 LQGYYFARPMPLEDFPAWLTRHQA 516
Cdd:PRK11359 773 IQGYFFSRPLPAEEIPGWMSSVLP 796
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
273-512 |
2.34e-42 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 160.26 E-value: 2.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 273 ISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLP------- 345
Cdd:PRK13561 405 ILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAawqergi 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 346 QLPddsafhIAINVAASHFRDRAILEDLQNLWWPASPVP-QLVVELTERDALPVVDQSV--IAQLHEIGVRLAIDDFGTG 422
Cdd:PRK13561 485 MLP------LSVNLSALQLMHPNMVADMLELLTRYRIQPgTLILEVTESRRIDDPHAAVaiLRPLRNAGVRVALDDFGMG 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 423 HSSLSYL---KDLQPDVLKIDKIFTAAIGTDAinaTVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFA 499
Cdd:PRK13561 559 YAGLRQLqhmKSLPIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFA 635
|
250
....*....|....
gi 1750418682 500 RPMPLEDFPA-WLT 512
Cdd:PRK13561 636 RALPIEIFEErYLE 649
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
263-509 |
3.29e-36 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 142.77 E-value: 3.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 263 TANRMSLSWQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVR 342
Cdd:PRK11829 400 THKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACR 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 343 QLPQLPDDS-AFHIAINVAASHFRDRAILEDLQNLWWPASPVPQ-LVVELTERDALPVVDQS--VIAQLHEIGVRLAIDD 418
Cdd:PRK11829 480 ILADWKARGvSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQqLLLEITETAQIQDLDEAlrLLRELQGLGLLIALDD 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 419 FGTGHSSLSYL---KDLQPDVLKIDKIFTAAIGTDainATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQG 495
Cdd:PRK11829 560 FGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNLPED---DAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQG 636
|
250
....*....|....
gi 1750418682 496 YYFARPMPLEDFPA 509
Cdd:PRK11829 637 FLFSPPLPRAEFEA 650
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
267-507 |
1.85e-23 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 104.75 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 267 MSLSWQISYGITAREFMVYCQPLINSKSGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQLPQ 346
Cdd:PRK09776 840 LSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAK 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 347 LPDDSAFHIAINVAASHFRDRAILEDLQNLWwPASPVP--QLVVELTErDAL---PVVDQSVIAQLHEIGVRLAIDDFGT 421
Cdd:PRK09776 920 AVASKGLSIALPLSVAGLSSPTLLPFLLEQL-ENSPLPprLLHLEITE-TALlnhAESASRLVQKLRLAGCRVVLSDFGR 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 422 GHSSLSYLKDLQPDVLKIDKIFTAAIGTDAINATVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARP 501
Cdd:PRK09776 998 GLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARP 1077
|
....*.
gi 1750418682 502 MPLEDF 507
Cdd:PRK09776 1078 QPLDLL 1083
|
|
| CSS-motif |
pfam12792 |
CSS motif domain associated with EAL; This family with its characteriztic highly conserved CSS ... |
43-237 |
4.16e-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: 4.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 43 EQQAMDFADKAIMRFDRMFSPLEVSASNTLGLVGAPC-QDVRFPLIEKISSLQTVRAILLVENDMLYCSSIYGPRNIPFS 121
Cdd:pfam12792 2 QEQLDAFAERALRRLESVLDQADQALDRLLPLTGQPCsPAHLAELRRIVAFSPYVRDVGLVKNGRLYCSSLWGELDTPLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 122 QTYPDL-AFNSQRMTLATDEYLLKGSPILLLWTPKSLD-NRSGILqvINIEMMSNYLLEPQlPWVERAVFNVNGES---- 195
Cdd:pfam12792 82 LLPPDLtTPPGVRLWLLRGTPLVPGRPALVLRRGGYGVvIDPGVF--IDVQYLPGLLAAVS-QPDGRLLALVVGDDallf 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1750418682 196 ---LEYGNPLIEPTVPSDDEVSYEQGSLRYPFTLTLYGPSPTRLA 237
Cdd:pfam12792 159 dgrLHSLAEPAPGTARSGGALYARARSTRYPLTVVVYAPRASLLA 203
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
382-505 |
3.43e-14 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 74.45 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 382 PVPQLVVELTERDAlpvVDQSVIA---QLHEIGVRLAIDDFgtghsslSYLKDLQP-----DVLKIDkifTAAIGTDAIN 453
Cdd:COG3434 82 PPERVVLEILEDVE---PDEELLEalkELKEKGYRIALDDF-------VLDPEWDPllplaDIIKID---VLALDLEELA 148
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1750418682 454 AtvtdmVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLE 505
Cdd:COG3434 149 E-----LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEILK 195
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
287-509 |
4.97e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 63.10 E-value: 4.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 287 QPlINSKSGECDGIELLLR-WH-NARQGWITPDVF---IPLAERqnlikpltrfvLNEVVRQLPQLPDDSAFHIAINVAA 361
Cdd:PRK11596 35 QP-IYRTSGRLMAIELLTAvTHpSNPSQRLSPERYfaeITVSHR-----------LDVVKEQLDLLAQWADFFVRHGLLA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 362 SHFRDRAILEDLQNLwwPA-----SPVPQLVVELTERDALPvvDQSVIAQLHEIGvRLAIDDFGTGHSSLSYLKDLQPDV 436
Cdd:PRK11596 103 SVNIDGPTLIALRQQ--PAilrliERLPWLRFELVEHIRLP--KDSPFASMCEFG-PLWLDDFGTGMANFSALSEVRYDY 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1750418682 437 LKIDK-IFTAAIGTDAINaTVTDMVISLAQRLNISLVAEGVETAEQADYLRERGVDHLQGYYFARPMPLEDFPA 509
Cdd:PRK11596 178 IKVAReLFIMLRQSEEGR-NLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETLET 250
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
266-504 |
9.70e-09 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 57.95 E-value: 9.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 266 RMSLSWQ--ISYGITAREFMVYCQPLINSKsGECDGIELLLRWHNARQGWITPDVFIPLAERQNLIKPLTRFVLNEVVRQ 343
Cdd:PRK11059 399 RGSVRWRtlLEQTLVRGGPRLYQQPAVTRD-GKVHHRELFCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPL 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 344 LPQLPDDSafhIAINVAASHFRDRAILEDLQN--LWWPASPVPQLVVELTERDalpVVD-----QSVIAQLHEIGVRLAI 416
Cdd:PRK11059 478 LRYWPEEN---LSINLSVDSLLSRAFQRWLRDtlLQCPRSQRKRLIFELAEAD---VCQhisrlRPVLRMLRGLGCRLAV 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750418682 417 DDFGTGHSSLSYLKDLQPDVLKIDKIFTAAIGTDAINAT-VTDMVISLAqRLNISLVAEGVETAEQADYLRERGVDHLQG 495
Cdd:PRK11059 552 DQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLfVRSLVGACA-GTETQVFATGVESREEWQTLQELGVSGGQG 630
|
....*....
gi 1750418682 496 YYFARPMPL 504
Cdd:PRK11059 631 DFFAESQPL 639
|
|
|