|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
226-644 |
4.85e-53 |
|
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: 191.54 E-value: 4.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 226 AALSIKQEAYKDVITELGNRNMFVEYYEKHIENSERSTFGSLALVRCSELQTINQSRGYQKGDDYVKGVADIIKHISGTY 305
Cdd:COG2200 147 LLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 306 TGSQVFRLNSSDFAIVLPNTPLKEAERFGENLQSRFTQY--QQNQELSSVANTGIVGYEKGKPLGELLSVVDNAMSMAQS 383
Cdd:COG2200 227 LLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPllLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 384 KQVNAWHVQRETDLvnnvSAGFGNQNWRKVINEVIESKRVHLVMQNIMPLGKSIKAYAEIQVRFKTEDNQVLPTASFLAM 463
Cdd:COG2200 307 GGGRGRVVFFAAAE----ARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 464 AEKLDMAIEIDRLIIDSSLEKIKSRNLSEK--FFGLNVTASSAHNDQFVIWLERRLLKDTHIASKLVFEVSEFGLQQNIK 541
Cdd:COG2200 383 AERSGLIVELDRWVLERALRQLARWPERGLdlRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 542 ASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVSVFAEGVES 621
Cdd:COG2200 463 AAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVET 542
|
410 420
....*....|....*....|...
gi 567931824 622 QEEKHIVETLCLDGVQGYYIEKP 644
Cdd:COG2200 543 EEQLEALRELGCDYAQGYLFGRP 565
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
418-644 |
2.19e-52 |
|
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: 180.21 E-value: 2.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 418 IESKRVHLVMQNIMPLGKSIKAYAEIQVRFKTEDNQVLPTASFLAMAEKLDMAIEIDRLIIDSSLEKIKSRNLSEKF-FG 496
Cdd:pfam00563 8 LENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPDIkLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 497 LNVTASSAHNDQFVIWLERRLLKDTHIASKLVFEVSEFGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLK 576
Cdd:pfam00563 88 INLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567931824 577 PDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVSVFAEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:pfam00563 168 PDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
414-644 |
3.73e-40 |
|
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: 146.92 E-value: 3.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 414 INEVIESKRVHLVMQNIMPL-GKSIKAYaEIQVRFKTEDNQVLPTASFLAMAEKLDMAIEIDRLIIDSSLEKIKSRNLSE 492
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLrTGRIVGY-EALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 493 K--FFGLNVTASSAHNDQFVIWLeRRLLKDTHI-ASKLVFEVSEFGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSF 569
Cdd:cd01948 82 PdlRLSVNLSARQLRDPDFLDRL-LELLAETGLpPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567931824 570 KFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVSVFAEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
230-644 |
2.12e-36 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 145.00 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 230 IKQEAYKDVITELGNRNMFVEYYEKHIENSER-STFGSLALVRCSELQTINQSRGYQKGDDYVKGVADIIKHISGTYTGS 308
Cdd:PRK11059 224 IRSNAFQDAKTGLGNRLFFDNQLATLLEDQEMvGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 309 QVFRLNSSDFAIVLPNTPLKEAErfgeNLQSRFTQYQQNQELSSVANT------GIVGYEKGKPLGELLSVVDNAMSMAQ 382
Cdd:PRK11059 304 LLARYSRSDFAVLLPHRSLKEAD----SLASQLLKAVDALPPPKMLDRddflhiGICAYRSGQSTEQVMEEAEMALRSAQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 383 SKQVNAWHVqreTDLVNNVSAGFGNQNWRKVINEVIESKRVHLVMQNIMPLGKSIKAYaEIQVRFKTEDNQVLPTASFLA 462
Cdd:PRK11059 380 LQGGNGWFV---YDKAQLPEKGRGSVRWRTLLEQTLVRGGPRLYQQPAVTRDGKVHHR-ELFCRIRDGQGELLSAELFMP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 463 MAEKLDMAIEIDRLIIDSSLEKIKSRNlsEKFFGLNVTASSAHNDQFVIWLERRLLK-DTHIASKLVFEVSEFGLQQNIK 541
Cdd:PRK11059 456 MVQQLGLSEQYDRQVIERVLPLLRYWP--EENLSINLSVDSLLSRAFQRWLRDTLLQcPRSQRKRLIFELAEADVCQHIS 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 542 ASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVSVFAEGVES 621
Cdd:PRK11059 534 RLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVES 613
|
410 420
....*....|....*....|...
gi 567931824 622 QEEKHIVETLCLDGVQGYYIEKP 644
Cdd:PRK11059 614 REEWQTLQELGVSGGQGDFFAES 636
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
440-644 |
2.58e-36 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 136.19 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 440 YAEIQVRFKTEDNQVLPTASFLAMAEKLDMAIEIDRLIIDSSLE---KIKSRNLSEKFFGLNVTASSAHNDQFVIWLeRR 516
Cdd:smart00052 30 GVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQqlaEWQAQGPPPLLISINLSARQLISPDLVPRV-LE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 517 LLKDTHI-ASKLVFEVSEFGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKN 595
Cdd:smart00052 109 LLEETGLpPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 567931824 596 NQYFMRLMVDLAHRIGVSVFAEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:smart00052 189 DEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
234-381 |
1.01e-06 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 49.26 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 234 AYKDVITELGNRNMFVEYYEKHIENSERSTFG-SLALVRCSELQTINQSRGYQKGDDYVKGVADIIKhiSGTYTGSQVFR 312
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQ--SSVRGSDVVGR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567931824 313 LNSSDFAIVLPNTPLKEA----ERFGENLQSRFTQYQQNQELSSVANTGIVGY-EKGKPLGELLSVVDNAMSMA 381
Cdd:TIGR00254 80 YGGEEFVVILPGTPLEDAlskaERLRDAINSKPIEVAGSETLTVTVSIGVACYpGHGLTLEELLKRADEALYQA 153
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
226-644 |
4.85e-53 |
|
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: 191.54 E-value: 4.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 226 AALSIKQEAYKDVITELGNRNMFVEYYEKHIENSERSTFGSLALVRCSELQTINQSRGYQKGDDYVKGVADIIKHISGTY 305
Cdd:COG2200 147 LLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 306 TGSQVFRLNSSDFAIVLPNTPLKEAERFGENLQSRFTQY--QQNQELSSVANTGIVGYEKGKPLGELLSVVDNAMSMAQS 383
Cdd:COG2200 227 LLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPllLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAA 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 384 KQVNAWHVQRETDLvnnvSAGFGNQNWRKVINEVIESKRVHLVMQNIMPLGKSIKAYAEIQVRFKTEDNQVLPTASFLAM 463
Cdd:COG2200 307 GGGRGRVVFFAAAE----ARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPA 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 464 AEKLDMAIEIDRLIIDSSLEKIKSRNLSEK--FFGLNVTASSAHNDQFVIWLERRLLKDTHIASKLVFEVSEFGLQQNIK 541
Cdd:COG2200 383 AERSGLIVELDRWVLERALRQLARWPERGLdlRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 542 ASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVSVFAEGVES 621
Cdd:COG2200 463 AAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVET 542
|
410 420
....*....|....*....|...
gi 567931824 622 QEEKHIVETLCLDGVQGYYIEKP 644
Cdd:COG2200 543 EEQLEALRELGCDYAQGYLFGRP 565
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
418-644 |
2.19e-52 |
|
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: 180.21 E-value: 2.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 418 IESKRVHLVMQNIMPLGKSIKAYAEIQVRFKTEDNQVLPTASFLAMAEKLDMAIEIDRLIIDSSLEKIKSRNLSEKF-FG 496
Cdd:pfam00563 8 LENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPDIkLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 497 LNVTASSAHNDQFVIWLERRLLKDTHIASKLVFEVSEFGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLK 576
Cdd:pfam00563 88 INLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 567931824 577 PDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVSVFAEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:pfam00563 168 PDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
414-644 |
3.73e-40 |
|
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: 146.92 E-value: 3.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 414 INEVIESKRVHLVMQNIMPL-GKSIKAYaEIQVRFKTEDNQVLPTASFLAMAEKLDMAIEIDRLIIDSSLEKIKSRNLSE 492
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLrTGRIVGY-EALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 493 K--FFGLNVTASSAHNDQFVIWLeRRLLKDTHI-ASKLVFEVSEFGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSF 569
Cdd:cd01948 82 PdlRLSVNLSARQLRDPDFLDRL-LELLAETGLpPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567931824 570 KFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVSVFAEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRP 235
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
230-644 |
5.80e-37 |
|
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: 146.84 E-value: 5.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 230 IKQEAYKDVITELGNRNMFVEYYEKHIENSERSTfGSLALV-----RcseLQTINQSRGYQKGDDYVKGVADIIKHISGT 304
Cdd:COG5001 247 LRHLAYHDPLTGLPNRRLFLDRLEQALARARRSG-RRLALLfidldR---FKEINDTLGHAAGDELLREVARRLRACLRE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 305 ytGSQVFRLNSSDFAIVLPNTP-LKEAERFGENLQSRFTQ-YQ-QNQELSSVANTGIVGY-EKGKPLGELLSVVDNAMSM 380
Cdd:COG5001 323 --GDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAALAEpFElDGHELYVSASIGIALYpDDGADAEELLRNADLAMYR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 381 AQSKQVNAWHV---QRETDLvnnvsagfgnQNWRKVINEV---IESKRVHLVMQNIMPL--GKSIKAyaEIQVRFKTEDN 452
Cdd:COG5001 401 AKAAGRNRYRFfdpEMDERA----------RERLELEADLrraLERGELELHYQPQVDLatGRIVGA--EALLRWQHPER 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 453 QVLPTASFLAMAEKLDMAIEIDRLIIDSSLEKIK---SRNLSEKFFGLNVTASSAHNDQFVIWLeRRLLKDTHI-ASKLV 528
Cdd:COG5001 469 GLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAawqDAGLPDLRVAVNLSARQLRDPDLVDRV-RRALAETGLpPSRLE 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 529 FEVSEFGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLMVDLAH 608
Cdd:COG5001 548 LEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAH 627
|
410 420 430
....*....|....*....|....*....|....*.
gi 567931824 609 RIGVSVFAEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:COG5001 628 SLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRP 663
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
230-644 |
2.12e-36 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 145.00 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 230 IKQEAYKDVITELGNRNMFVEYYEKHIENSER-STFGSLALVRCSELQTINQSRGYQKGDDYVKGVADIIKHISGTYTGS 308
Cdd:PRK11059 224 IRSNAFQDAKTGLGNRLFFDNQLATLLEDQEMvGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRYPGA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 309 QVFRLNSSDFAIVLPNTPLKEAErfgeNLQSRFTQYQQNQELSSVANT------GIVGYEKGKPLGELLSVVDNAMSMAQ 382
Cdd:PRK11059 304 LLARYSRSDFAVLLPHRSLKEAD----SLASQLLKAVDALPPPKMLDRddflhiGICAYRSGQSTEQVMEEAEMALRSAQ 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 383 SKQVNAWHVqreTDLVNNVSAGFGNQNWRKVINEVIESKRVHLVMQNIMPLGKSIKAYaEIQVRFKTEDNQVLPTASFLA 462
Cdd:PRK11059 380 LQGGNGWFV---YDKAQLPEKGRGSVRWRTLLEQTLVRGGPRLYQQPAVTRDGKVHHR-ELFCRIRDGQGELLSAELFMP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 463 MAEKLDMAIEIDRLIIDSSLEKIKSRNlsEKFFGLNVTASSAHNDQFVIWLERRLLK-DTHIASKLVFEVSEFGLQQNIK 541
Cdd:PRK11059 456 MVQQLGLSEQYDRQVIERVLPLLRYWP--EENLSINLSVDSLLSRAFQRWLRDTLLQcPRSQRKRLIFELAEADVCQHIS 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 542 ASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVSVFAEGVES 621
Cdd:PRK11059 534 RLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATGVES 613
|
410 420
....*....|....*....|...
gi 567931824 622 QEEKHIVETLCLDGVQGYYIEKP 644
Cdd:PRK11059 614 REEWQTLQELGVSGGQGDFFAES 636
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
440-644 |
2.58e-36 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 136.19 E-value: 2.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 440 YAEIQVRFKTEDNQVLPTASFLAMAEKLDMAIEIDRLIIDSSLE---KIKSRNLSEKFFGLNVTASSAHNDQFVIWLeRR 516
Cdd:smart00052 30 GVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQqlaEWQAQGPPPLLISINLSARQLISPDLVPRV-LE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 517 LLKDTHI-ASKLVFEVSEFGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKN 595
Cdd:smart00052 109 LLEETGLpPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYSSLSYLKRLPVDLLKIDKSFVRDLQTDPE 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 567931824 596 NQYFMRLMVDLAHRIGVSVFAEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:smart00052 189 DEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
234-644 |
1.59e-22 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 103.21 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 234 AYKDVITELGNRNMFVEYYEKHIENS-ERSTFGSLALVRCSELQTINQSRGYQKGDDYVKGVADIIKHIsgTYTGSQVFR 312
Cdd:PRK09776 665 ASHDALTHLANRASFEKQLRRLLQTVnSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSM--LRSSDVLAR 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 313 LNSSDFAIVLPNTPLKEAERFGENLQSRFTQYQQNQE--LSSV-ANTGIVGY-EKGKPLGELLSVVDNA----------- 377
Cdd:PRK09776 743 LGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEgrVYRVgASAGITLIdANNHQASEVMSQADIAcyaaknagrgr 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 378 MSMAQSKQVNAWHVQRETDLvnnvsagfgnqnwRKVINEVIESKRVHLVMQNIMPLGKSIKAYAEIQVRFKTEDNQVLPT 457
Cdd:PRK09776 823 VTVYEPQQAAAHSEHRALSL-------------AEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLWDPEGEIIDE 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 458 ASFLAMAEKLDMAIEIDRLIIDSSL----EKIKSRNLSekfFGLNVTASSAHNDQFVIWLERRLLKDTHIASKLVFEVSE 533
Cdd:PRK09776 890 GAFRPAAEDPALMHALDRRVIHEFFrqaaKAVASKGLS---IALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITE 966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 534 FGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVS 613
Cdd:PRK09776 967 TALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMK 1046
|
410 420 430
....*....|....*....|....*....|....
gi 567931824 614 VFAEGVESQEekhIVETLC---LDGVQGYYIEKP 644
Cdd:PRK09776 1047 TIAGPVELPL---VLDTLSgigVDLAYGYAIARP 1077
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
222-391 |
5.30e-22 |
|
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: 96.20 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 222 DIQNAALSIKQEAYKDVITELGNRNMFVEYYEKHIENSERS-TFGSLALVRCSELQTINQSRGYQKGDDYVKGVADIIKH 300
Cdd:COG2199 102 ELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREgRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 301 ISGTytGSQVFRLNSSDFAIVLPNTPLKEAERFGENLQSRFTQYQ---QNQELSSVANTGIVGY-EKGKPLGELLSVVDN 376
Cdd:COG2199 182 SLRE--SDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPfelEGKELRVTVSIGVALYpEDGDSAEELLRRADL 259
|
170
....*....|....*
gi 567931824 377 AMSMAQSKQVNAWHV 391
Cdd:COG2199 260 ALYRAKRAGRNRVVV 274
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
205-644 |
1.55e-21 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 99.25 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 205 LVPSFNRLSHFLKNKNDDIQnaalsikQEAYKDVITELGNRNMFVEYYEKHIENSERSTFGSLALVrcsELQTINQSRGY 284
Cdd:PRK11829 210 LVRNYNRNQQLLADAYADMG-------RISHRFPVTELPNRSLFISLLEKEIASSTRTDHFHLLVI---GIETLQEVSGA 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 285 QKGDDYVKGVADIIKHI-SGTYTGSQVFRLNSSDFAIVLPNTPLK-EAERFGENLQSRFTQ--YQQNQELSSVANTGIVG 360
Cdd:PRK11829 280 MSEAQHQQLLLTIVQRIeQCIDDSDLLAQLSKTEFAVLARGTRRSfPAMQLARRIMSQVTQplFFDEITLRPSASIGITR 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 361 YEKGKPLGE-LLSVVDNAMSMAQSKQVNAWHVqRETDLVNNVSAGFGNQNwrKVINeVIESKRVHLVMQNIMPLGKSIKA 439
Cdd:PRK11829 360 YQAQQDTAEsMMRNASTAMMAAHHEGRNQIMV-FEPHLIEKTHKRLTQEN--DLLQ-AIENHDFTLFLQPQWDMKRQQVI 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 440 YAEIQVRFKTEDNQVLPTASFLAMAEKLDMAIEIDRLIIDSS---LEKIKSRNLSEKfFGLNVTASSAHNDQFVIWLErR 516
Cdd:PRK11829 436 GAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEAcriLADWKARGVSLP-LSVNISGLQVQNKQFLPHLK-T 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 517 LLKDTHI-ASKLVFEVSEFGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKP---DFIKMDASYTRGLED 592
Cdd:PRK11829 514 LISHYHIdPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLNHLKSlpiHMIKLDKSFVKNLPE 593
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 567931824 593 DKNnqyFMRLMVDLAHRIGVSVFAEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:PRK11829 594 DDA---IARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPP 642
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
232-381 |
6.14e-16 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 75.75 E-value: 6.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 232 QEAYKDVITELGNRNMFVEYYEKHIENSERS-TFGSLALVRCSELQTINQSRGYQKGDDYVKGVADIIKhiSGTYTGSQV 310
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQgSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLS--SCLRPGDLL 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 567931824 311 FRLNSSDFAIVLPNTPLKEAERFGENLQSRFTQYQQNQELsSVANTGIVG----YEKGKPLGELLSVVDNAMSMA 381
Cdd:smart00267 79 ARLGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGI-PLYLTISIGvaayPNPGEDAEDLLKRADTALYQA 152
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
235-390 |
1.11e-14 |
|
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This 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. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.
Pssm-ID: 143635 [Multi-domain] Cd Length: 158 Bit Score: 71.82 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 235 YKDVITELGNRNMFVEYYEKHIENSERS-TFGSLALVRCSELQTINQSRGYQKGDDYVKGVADIIKHISGTytGSQVFRL 313
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSgRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRE--SDLVARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 314 NSSDFAIVLPNTPLKEAERFGENLQSRFTQY--QQNQELSSVANTGIVGY-EKGKPLGELLSVVDNAMSMAQSKQVNAWH 390
Cdd:cd01949 79 GGDEFAILLPGTDLEEAEALAERLREAIEEPffIDGQEIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
234-644 |
6.81e-14 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 75.10 E-value: 6.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 234 AYKDVITELGNRNMFVEYYEKHIENSERSTFGSLALvRCSELQTINQSRGYQKGDDYVKGVADIIkhiSGTYTGSQVF-R 312
Cdd:PRK10060 237 ANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYL-DLDNFKKVNDAYGHMFGDQLLQDVSLAI---LSCLEEDQTLaR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 313 LNSSDFAIVLPNTPLKEAERFGENLQSRFTQYQQNQ--ELSSVANTGIVGY-EKGKPLGELLSVVDNAMSMAQ------- 382
Cdd:PRK10060 313 LGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGliEVYTGCSIGIALApEHGDDSESLIRSADTAMYTAKeggrgqf 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 383 ---SKQVNawhvQRETDLVnnvsagFGNQNWRKVIneviESKRVHLVMQNIMPLGKSIKAyAEIQVRFKTEDNQVLPTAS 459
Cdd:PRK10060 393 cvfSPEMN----QRVFEYL------WLDTNLRKAL----ENDQLVIHYQPKITWRGEVRS-LEALVRWQSPERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 460 FLAMAEKLDMAIEIDRLIIDSSLEKI---KSRNLSEKFfGLNVTASSAhNDQFVIWLERRLLKDTHIASKLV-FEVSEFG 535
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVakwRDKGINLRV-AVNVSARQL-ADQTIFTALKQALQELNFEYCPIdVELTESC 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 536 LQQNIKASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLMVDLAHRIGVSVF 615
Cdd:PRK10060 536 LIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVI 615
|
410 420
....*....|....*....|....*....
gi 567931824 616 AEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:PRK10060 616 AEGVETAKEDAFLTKNGVNERQGFLFAKP 644
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
234-378 |
6.48e-12 |
|
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: 63.81 E-value: 6.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 234 AYKDVITELGNRNMFVEYYEKHIENSER-STFGSLALVRCSELQTINQSRGYQKGDDYVKGVADIIKhiSGTYTGSQVFR 312
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALReGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLS--SSLRRSDLVAR 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 567931824 313 LNSSDFAIVLPNTPLKEAERFGENLQSRFTQYQ-----QNQELSSVANTGIVGY-EKGKPLGELLSVVDNAM 378
Cdd:pfam00990 79 LGGDEFAILLPETSLEGAQELAERIRRLLAKLKiphtvSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTAL 150
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
226-644 |
7.40e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 65.56 E-value: 7.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 226 AALSIKQEAYK---------DVITELGNRNMFVEYYEKHIENSERSTFGSLALVRcseLQTINQSRGYQKGDDYVKGVAD 296
Cdd:PRK11359 359 AALALEQEKSRqhieqliqfDPLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDH---FQDVIDSLGYAWADQALLEVVN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 297 IIKHISGTytGSQVFRLNSSDFAIVLPNTPLKEAERFGENLQSRFTQ--YQQNQELSSVANTGIvGYEKGKPLGELLSVV 374
Cdd:PRK11359 436 RFREKLKP--DQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKpiMIDDKPFPLTLSIGI-SYDVGKNRDYLLSTA 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 375 DNAMSMAQSKQVNAWHVqretdlvnnVSAGFgNQNWRK------VINEVIESKRVHLVMQ-NIMPlgKSIKAYA-EIQVR 446
Cdd:PRK11359 513 HNAMDYIRKNGGNGWQF---------FSPAM-NEMVKErlvlgaALKEAISNNQLKLVYQpQIFA--ETGELYGiEALAR 580
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 447 FKTEDNQVLPTASFLAMAEKLDMAIEIDRLIIDSS---LEKIKSRNLSEKFFGLNVTASSAHNDQFVIWLERRLLKDTHI 523
Cdd:PRK11359 581 WHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEAcrqLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGID 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 524 ASKLVFEVSEFGLQQNIKASKRFIDMVHRVGARVTVERFGVGLTSFKFFRDLKPDFIKMDASYTRGLEDDKNNQYFMRLM 603
Cdd:PRK11359 661 GHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAI 740
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 567931824 604 VDLAHRIGVSVFAEGVESQEEKHIVETLCLDGVQGYYIEKP 644
Cdd:PRK11359 741 TSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRP 781
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
234-381 |
1.01e-06 |
|
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by many proteins carrying the domain. There is evidence that the domain has diguanylate cyclase activity. Several proteins carrying this domain also carry domains with functions relating to environmental sensing. These include PleD, a response regulator protein involved in the swarmer-to-stalked cell transition in Caulobacter crescentus, and FixL, a heme-containing oxygen sensor protein. [Regulatory functions, Small molecule interactions, Signal transduction, Other]
Pssm-ID: 272984 [Multi-domain] Cd Length: 165 Bit Score: 49.26 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 234 AYKDVITELGNRNMFVEYYEKHIENSERSTFG-SLALVRCSELQTINQSRGYQKGDDYVKGVADIIKhiSGTYTGSQVFR 312
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQ--SSVRGSDVVGR 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 567931824 313 LNSSDFAIVLPNTPLKEA----ERFGENLQSRFTQYQQNQELSSVANTGIVGY-EKGKPLGELLSVVDNAMSMA 381
Cdd:TIGR00254 80 YGGEEFVVILPGTPLEDAlskaERLRDAINSKPIEVAGSETLTVTVSIGVACYpGHGLTLEELLKRADEALYQA 153
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
229-340 |
4.08e-04 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 43.46 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 229 SIKQEAYKDVITELGNRNMFVEYYEKhiENSERSTFG---SLALVRCSELQTINQSRGYQKGDDYVKGVADIIKhiSGTY 305
Cdd:PRK15426 393 SLQWQAWHDPLTRLYNRGALFEKARA--LAKRCQRDQqpfSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLIS--SSLR 468
|
90 100 110
....*....|....*....|....*....|....*
gi 567931824 306 TGSQVFRLNSSDFAIVLPNTPLKEAERFGENLQSR 340
Cdd:PRK15426 469 AQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLR 503
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
562-644 |
9.26e-04 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 41.53 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 562 FGVGLTSFKFFRDLKPDFIKMDasytRGL-----EDDKNNQYFMRLmVDLAHRIGVSVFAEGVESQEEKHIVETLCLDGV 636
Cdd:PRK11596 160 FGTGMANFSALSEVRYDYIKVA----RELfimlrQSEEGRNLFSQL-LHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAA 234
|
....*...
gi 567931824 637 QGYYIEKP 644
Cdd:PRK11596 235 QGYFLSRP 242
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
234-378 |
4.12e-03 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 39.88 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 567931824 234 AYKDVITELGNRnmfvEYYEKHIEN-SERSTFG----SLALVRCSELQTINQSRGYQKGDDYVKGVADIIK-HISGTytg 307
Cdd:PRK09581 292 AVTDGLTGLHNR----RYFDMHLKNlIERANERgkplSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRnNIRGT--- 364
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 567931824 308 SQVFRLNSSDFAIVLPNTPLKEAERFGENL-----QSRFTQYQQNQELSSVANTGIVGYEK-GKPLGELLSVVDNAM 378
Cdd:PRK09581 365 DLIARYGGEEFVVVMPDTDIEDAIAVAERIrrkiaEEPFIISDGKERLNVTVSIGVAELRPsGDTIEALIKRADKAL 441
|
|
| |
