|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
19-245 |
2.16e-31 |
|
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: 115.88 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 19 DVTPFLQPVINTYDNCIVGAEILCRVKTK-KGYILNQLHIEELEVPERADFYARELLLKTAELLRKNDGAGEIPsgfvFS 97
Cdd:pfam00563 12 EFVLYYQPIVDLRTGRVVGYEALLRWQHPdGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPDIK----LS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 98 LNITCGQISSQTIRNAVVRFKSYFKTDVVIL-LEIVERNINDATSDILNAITFYNSIGVKFAIDDAGINTAAMKFFGVSN 176
Cdd:pfam00563 88 INLSPASLADPGFLELLRALLKQAGPPPSRLvLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550714287 177 VSILKLDRSVTQIKENFELiYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRP 245
Cdd:pfam00563 168 PDFVKIDRSLIADIDKDGE-ARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
19-256 |
2.31e-29 |
|
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: 116.04 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 19 DVTPFLQPVINTYDNCIVGAEILCRVKTKKGYILNQLHIeeLEVPERADFYA---RELLLKTAELLRKNDGAGEipsGFV 95
Cdd:COG2200 341 ELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEF--IPAAERSGLIVeldRWVLERALRQLARWPERGL---DLR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 96 FSLNITCGQISSQTIRNAVVRF--KSYFKTDVVILlEIVERNINDATSDILNAITFYNSIGVKFAIDDAGI---NTAAMK 170
Cdd:COG2200 416 LSVNLSARSLLDPDFLERLLELlaEYGLPPERLVL-EITESALLEDLEAAIELLARLRALGVRIALDDFGTgysSLSYLK 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 171 FFGVSnvsILKLDRS-VTQIKENFEliYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVA 249
Cdd:COG2200 495 RLPPD---YLKIDRSfVRDIARDPR--DQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLE 569
|
....*..
gi 550714287 250 AFCDFIK 256
Cdd:COG2200 570 ELEALLR 576
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
19-250 |
9.02e-29 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 109.23 E-value: 9.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 19 DVTPFLQPVINTYDNCIVGAEILCRVKT-KKGYILNQLHIEELEVPERADFYARELLLKTAELLRKNDGAGeiPSGFVFS 97
Cdd:smart00052 12 QFLLYYQPIVSLRTGRLVGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG--PPPLLIS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 98 LNITCGQISSQTIRNAVVR-FKSYFKTDVVILLEIVERNINDATSDILNAITFYNSIGVKFAIDDAGI---NTAAMKFFg 173
Cdd:smart00052 90 INLSARQLISPDLVPRVLElLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTgysSLSYLKRL- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550714287 174 vsNVSILKLDRS-VTQIKENfeLIYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVAA 250
Cdd:smart00052 169 --PVDLLKIDKSfVRDLQTD--PEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
21-250 |
1.41e-27 |
|
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: 106.09 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 21 TPFLQPVINTYDNCIVGAEILCRVKTKKGyilNQLHIEE-LEVPERADFYAR--ELLLKTAelLRKNDGAGEIPSGFVFS 97
Cdd:cd01948 13 ELYYQPIVDLRTGRIVGYEALLRWRHPEG---GLISPAEfIPLAEETGLIVElgRWVLEEA--CRQLARWQAGGPDLRLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 98 LNITCGQISSQTIRNAVVR-FKSY-FKTDVVILlEIVERNINDATSDILNAITFYNSIGVKFAIDDAGINTAAMKFFGVS 175
Cdd:cd01948 88 VNLSARQLRDPDFLDRLLElLAETgLPPRRLVL-EITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550714287 176 NVSILKLDRS-VTQIKENFEliYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVAA 250
Cdd:cd01948 167 PVDYLKIDRSfVRDIETDPE--DRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
25-256 |
6.99e-19 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 85.43 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 25 QPVINTYDNCIVGAEILCRVKtkkgyilnqlHIEELEVPERAdF--YAR-------------ELLLKTAELLRKndgagE 89
Cdd:PRK10551 282 QPVVDTQTLRVTGLEALLRWR----------HPTAGEIPPDA-FinYAEaqklivpltqhlfELIARDAAELQK-----V 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 90 IPSGFVFSLNITCGQISSQTIRNAVVRFKSYFKTDVV-ILLEIVERN-INDATSDILNAitFYNSIGVKFAIDDAGINTA 167
Cdd:PRK10551 346 LPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFqIVLEITERDmVQEEEATKLFA--WLHSQGIEIAIDDFGTGHS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 168 AMKFFGVSNVSILKLDRS-VTQIKEnfELIYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPL 246
Cdd:PRK10551 424 ALIYLERFTLDYLKIDRGfIQAIGT--ETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPL 501
|
250
....*....|
gi 550714287 247 SVAAFCDFIK 256
Cdd:PRK10551 502 PLEDFVRWLK 511
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
19-245 |
2.16e-31 |
|
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: 115.88 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 19 DVTPFLQPVINTYDNCIVGAEILCRVKTK-KGYILNQLHIEELEVPERADFYARELLLKTAELLRKNDGAGEIPsgfvFS 97
Cdd:pfam00563 12 EFVLYYQPIVDLRTGRVVGYEALLRWQHPdGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPDIK----LS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 98 LNITCGQISSQTIRNAVVRFKSYFKTDVVIL-LEIVERNINDATSDILNAITFYNSIGVKFAIDDAGINTAAMKFFGVSN 176
Cdd:pfam00563 88 INLSPASLADPGFLELLRALLKQAGPPPSRLvLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 550714287 177 VSILKLDRSVTQIKENFELiYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRP 245
Cdd:pfam00563 168 PDFVKIDRSLIADIDKDGE-ARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
19-256 |
2.31e-29 |
|
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: 116.04 E-value: 2.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 19 DVTPFLQPVINTYDNCIVGAEILCRVKTKKGYILNQLHIeeLEVPERADFYA---RELLLKTAELLRKNDGAGEipsGFV 95
Cdd:COG2200 341 ELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEF--IPAAERSGLIVeldRWVLERALRQLARWPERGL---DLR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 96 FSLNITCGQISSQTIRNAVVRF--KSYFKTDVVILlEIVERNINDATSDILNAITFYNSIGVKFAIDDAGI---NTAAMK 170
Cdd:COG2200 416 LSVNLSARSLLDPDFLERLLELlaEYGLPPERLVL-EITESALLEDLEAAIELLARLRALGVRIALDDFGTgysSLSYLK 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 171 FFGVSnvsILKLDRS-VTQIKENFEliYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVA 249
Cdd:COG2200 495 RLPPD---YLKIDRSfVRDIARDPR--DQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLE 569
|
....*..
gi 550714287 250 AFCDFIK 256
Cdd:COG2200 570 ELEALLR 576
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
19-250 |
9.02e-29 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 109.23 E-value: 9.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 19 DVTPFLQPVINTYDNCIVGAEILCRVKT-KKGYILNQLHIEELEVPERADFYARELLLKTAELLRKNDGAGeiPSGFVFS 97
Cdd:smart00052 12 QFLLYYQPIVSLRTGRLVGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQAQG--PPPLLIS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 98 LNITCGQISSQTIRNAVVR-FKSYFKTDVVILLEIVERNINDATSDILNAITFYNSIGVKFAIDDAGI---NTAAMKFFg 173
Cdd:smart00052 90 INLSARQLISPDLVPRVLElLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTgysSLSYLKRL- 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 550714287 174 vsNVSILKLDRS-VTQIKENfeLIYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVAA 250
Cdd:smart00052 169 --PVDLLKIDKSfVRDLQTD--PEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPLDD 242
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
21-250 |
1.41e-27 |
|
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: 106.09 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 21 TPFLQPVINTYDNCIVGAEILCRVKTKKGyilNQLHIEE-LEVPERADFYAR--ELLLKTAelLRKNDGAGEIPSGFVFS 97
Cdd:cd01948 13 ELYYQPIVDLRTGRIVGYEALLRWRHPEG---GLISPAEfIPLAEETGLIVElgRWVLEEA--CRQLARWQAGGPDLRLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 98 LNITCGQISSQTIRNAVVR-FKSY-FKTDVVILlEIVERNINDATSDILNAITFYNSIGVKFAIDDAGINTAAMKFFGVS 175
Cdd:cd01948 88 VNLSARQLRDPDFLDRLLElLAETgLPPRRLVL-EITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 550714287 176 NVSILKLDRS-VTQIKENFEliYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVAA 250
Cdd:cd01948 167 PVDYLKIDRSfVRDIETDPE--DRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
21-254 |
3.79e-22 |
|
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: 94.98 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 21 TPFLQPVINTYDNCIVGAEILCRVKTKKGYILN---------QLH-IEEL--EVPERAdfyARELllktAELLRKNdgag 88
Cdd:COG4943 286 YVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISpdifiplaeQSGlISPLtrQVIEQV---FRDL----GDLLAAD---- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 89 eipSGFVFSLNITCGQISSQTIRNAVVRFksYFKTDVV---ILLEIVERNINDAtSDILNAITFYNSIGVKFAIDDAGin 165
Cdd:COG4943 355 ---PDFHISINLSASDLLSPRFLDDLERL--LARTGVApqqIVLEITERGFIDP-AKARAVIAALREAGHRIAIDDFG-- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 166 TaamkffGVSNVS--------ILKLDRSVTQ-IKENfeLIYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIH 236
Cdd:COG4943 427 T------GYSSLSylqtlpvdILKIDKSFVDaIGTD--SANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQY 498
|
250
....*....|....*...
gi 550714287 237 MQGYFFSRPLSVAAFCDF 254
Cdd:COG4943 499 GQGWLFAKPLPAEEFIAW 516
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
21-259 |
2.78e-21 |
|
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: 92.53 E-value: 2.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 21 TPFLQPVINTYDNCIVGAEILCRVKtkkgyilnqlHieelevPER-----ADF--YARE----------LLLKTAELLRK 83
Cdd:COG5001 440 ELHYQPQVDLATGRIVGAEALLRWQ----------H------PERglvspAEFipLAEEtglivplgewVLREACRQLAA 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 84 NDGAGEIPsgFVFSLNITCGQISS----QTIRNAVVRfksyfkTDV---VILLEIVE----RNInDATSDILNAItfyNS 152
Cdd:COG5001 504 WQDAGLPD--LRVAVNLSARQLRDpdlvDRVRRALAE------TGLppsRLELEITEsallEDP-EEALETLRAL---RA 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 153 IGVKFAIDDagintaamkfFGV--SN--------VSILKLDRS-VTQIKENFEliYRKLIDGIVKVSSLCGVHIVAEGVE 221
Cdd:COG5001 572 LGVRIALDD----------FGTgySSlsylkrlpVDTLKIDRSfVRDLAEDPD--DAAIVRAIIALAHSLGLEVVAEGVE 639
|
250 260 270
....*....|....*....|....*....|....*...
gi 550714287 222 NQHQKEALEKAGIIHMQGYFFSRPLSVAAFCDFIKHYR 259
Cdd:COG5001 640 TEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRARA 677
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
25-256 |
6.99e-19 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 85.43 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 25 QPVINTYDNCIVGAEILCRVKtkkgyilnqlHIEELEVPERAdF--YAR-------------ELLLKTAELLRKndgagE 89
Cdd:PRK10551 282 QPVVDTQTLRVTGLEALLRWR----------HPTAGEIPPDA-FinYAEaqklivpltqhlfELIARDAAELQK-----V 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 90 IPSGFVFSLNITCGQISSQTIRNAVVRFKSYFKTDVV-ILLEIVERN-INDATSDILNAitFYNSIGVKFAIDDAGINTA 167
Cdd:PRK10551 346 LPVGAKLGINISPAHLHSDSFKADVQRLLASLPADHFqIVLEITERDmVQEEEATKLFA--WLHSQGIEIAIDDFGTGHS 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 168 AMKFFGVSNVSILKLDRS-VTQIKEnfELIYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPL 246
Cdd:PRK10551 424 ALIYLERFTLDYLKIDRGfIQAIGT--ETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPL 501
|
250
....*....|
gi 550714287 247 SVAAFCDFIK 256
Cdd:PRK10551 502 PLEDFVRWLK 511
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
19-258 |
1.79e-13 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 69.59 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 19 DVTPFLQPVINTYDNCIVGAEILCR-VKTKKGYILNQLHIEELEvpERADFYAR-ELLLKTA-ELLRKNDGAG-EIPsgf 94
Cdd:PRK11829 418 DFTLFLQPQWDMKRQQVIGAEALLRwCQPDGSYVLPSGFVHFAE--EEGMMVPLgNWVLEEAcRILADWKARGvSLP--- 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 95 vFSLNITCGQISSQtirnavvRFKSYFKTDVV--------ILLEIVERNINDATSDILNAITFYNSIGVKFAIDDAGINT 166
Cdd:PRK11829 493 -LSVNISGLQVQNK-------QFLPHLKTLIShyhidpqqLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGY 564
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 167 AAMKFFGVSN---VSILKLDRS-VTQIKENFELIyrKLIDGIVKVSSLcgvHIVAEGVENQHQKEALEKAGIIHMQGYFF 242
Cdd:PRK11829 565 SSLRYLNHLKslpIHMIKLDKSfVKNLPEDDAIA--RIISCVSDVLKV---RVMAEGVETEEQRQWLLEHGIQCGQGFLF 639
|
250
....*....|....*.
gi 550714287 243 SRPLSVAafcDFIKHY 258
Cdd:PRK11829 640 SPPLPRA---EFEAQY 652
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
129-249 |
1.43e-12 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 67.10 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 129 LEIVERNINDATSDILNAITFYNSIGVKFAIDDAGINtaamkFFGVSN-----VSILKLDRSVTQIKENFELIyRKLIDG 203
Cdd:PRK11359 666 VEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTG-----FSGLSRlvslpVTEIKIDKSFVDRCLTEKRI-LALLEA 739
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 550714287 204 IVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVA 249
Cdd:PRK11359 740 ITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAE 785
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
127-251 |
6.83e-11 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 62.04 E-value: 6.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 127 ILLEIVE-RNINDaTSDILNAITFYNSIGVKFAIDDAGINTAAMKF---FGVSNVSILKLDRS-VTQIKENfeliyRKLI 201
Cdd:PRK13561 520 LILEVTEsRRIDD-PHAAVAILRPLRNAGVRVALDDFGMGYAGLRQlqhMKSLPIDVLKIDKMfVDGLPED-----DSMV 593
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 550714287 202 DGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVAAF 251
Cdd:PRK13561 594 AAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIEIF 643
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
99-259 |
1.56e-09 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 57.77 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 99 NITCGQISSQTIrnaVVRFKSYFK----TDVVILLEIVERNINDATSDILNAITFYNSIGVKFAIDDAGINTAAMKFFGV 174
Cdd:PRK10060 498 NVSARQLADQTI---FTALKQALQelnfEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLAR 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 175 SNVSILKLDRS-VTQIKENfeLIYRKLIDGIVKVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVAAFCD 253
Cdd:PRK10060 575 FPIDAIKLDQSfVRDIHKQ--PVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFER 652
|
....*.
gi 550714287 254 FIKHYR 259
Cdd:PRK10060 653 WYKRYL 658
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
125-245 |
2.89e-09 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 56.73 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 125 VVILLEIVErnindATSDILNAITFYNSIGVKFAIDDAGINTAAMKFFGVsnVSILKLDrsVTQI-KENFELIYRKLIDg 203
Cdd:COG3434 87 VLEILEDVE-----PDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKID--VLALdLEELAELVARLKR- 156
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 550714287 204 ivkvsslCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRP 245
Cdd:COG3434 157 -------YGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
22-248 |
1.25e-05 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 46.01 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 22 PFLQPVINTyDNCIVGAEILCRVKTKKGYIL---------NQLHIEELevperadfYARELLLKTAELLRKNDGAgeips 92
Cdd:PRK11059 419 LYQQPAVTR-DGKVHHRELFCRIRDGQGELLsaelfmpmvQQLGLSEQ--------YDRQVIERVLPLLRYWPEE----- 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 93 gfVFSLNITcgqISSQTIRnavvRFKSYFKTDVV---------ILLEIVE----RNInDATSDILNAItfyNSIGVKFAI 159
Cdd:PRK11059 485 --NLSINLS---VDSLLSR----AFQRWLRDTLLqcprsqrkrLIFELAEadvcQHI-SRLRPVLRML---RGLGCRLAV 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 160 DDAG---INTAAMKFFgvsNVSILKLDRS-VTQIK---ENfELIYRKLIDGivkvsslC---GVHIVAEGVENQHQKEAL 229
Cdd:PRK11059 552 DQAGltvVSTSYIKEL---NVELIKLHPSlVRNIHkrtEN-QLFVRSLVGA-------CagtETQVFATGVESREEWQTL 620
|
250
....*....|....*....
gi 550714287 230 EKAGIIHMQGYFFSRPLSV 248
Cdd:PRK11059 621 QELGVSGGQGDFFAESQPL 639
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
127-251 |
4.79e-04 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 41.20 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550714287 127 ILLEIVERNINDATSDILNAITFYNSIGVKFAIDDAGINTAAMKFFGVSNVSILKLDRS-VTQIKENfeLIYRKLIDGIV 205
Cdd:PRK09776 960 LHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGElVANLHGN--LMDEMLISIIQ 1037
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 550714287 206 KVSSLCGVHIVAEGVENQHQKEALEKAGIIHMQGYFFSRPLSVAAF 251
Cdd:PRK09776 1038 GHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLL 1083
|
|
| |
