|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
97-695 |
2.38e-174 |
|
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: 513.94 E-value: 2.38e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 97 VLDEHYRILWGAFQSQVMPRTDLSFLGAGLTSLIHTHAQALREGKNAFAGITRTEAGIAFVGIGLIRPTTARLQVFDATR 176
Cdd:COG5001 67 LLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 177 RYLVITRHINPQLLERLGDTFQISHLHLAEGPGAYRIPLRTQAGEVLGYLAWQPRLPGAEAAQASSGSMRLIAGVAASLI 256
Cdd:COG5001 147 AALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 257 LLFILFSSLGMYKLARGERQAREIAMIDWLSRLPNRRALLLRLSQVCETGKHDIQC--VVFIDLDGFKDVNDNYGHDVGD 334
Cdd:COG5001 227 LVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRlaLLFIDLDRFKEINDTLGHAAGD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 335 ALIRHIASALQTRVPAGAMLARMGGDEFAMAVSGAKAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIASGAPAECS 414
Cdd:COG5001 307 ELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGAD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 415 STELFRRADIAMYHAKKSGKGRTAWYDDALDAVRRHQMTIENGIRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRR 494
Cdd:COG5001 387 AEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHP 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 495 PQGALAPDAFISIAESSGLIDALGQFVLQRACSDL-----QPMDDLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRL 569
Cdd:COG5001 467 ERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLaawqdAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRL 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 570 QVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIA 649
Cdd:COG5001 547 ELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALA 626
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2119197963 650 RALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPIADLLQR 695
Cdd:COG5001 627 HSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEAL 672
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
458-691 |
1.71e-100 |
|
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: 307.94 E-value: 1.71e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 458 IRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACSDL----QPMD 533
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLarwqAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 534 DLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGY 613
Cdd:cd01948 83 DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119197963 614 LRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPIAD 691
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
274-698 |
6.29e-90 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 294.67 E-value: 6.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 274 ERQA----REIAMIDWLSRLPNRRALLLRLSQVCETGKHDIQCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVP 349
Cdd:PRK10060 226 ERRAqerlRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 350 AGAMLARMGGDEF-AMAVSGAKAIdrAAAFAWAALELLKAPVTLSKRKIYIGASIGIASgAPAECSSTE-LFRRADIAMY 427
Cdd:PRK10060 306 EDQTLARLGGDEFlVLASHTSQAA--LEAMASRILTRLRLPFRIGLIEVYTGCSIGIAL-APEHGDDSEsLIRSADTAMY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 428 HAKKSGKGRTAWYDDALDAVRRHQMTIENGIRQGLEEEEFEVWYQPVVDAdTLAMIGVEALLRWPRRPQGALAPDAFISI 507
Cdd:PRK10060 383 TAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 508 AESSGLIDALGQFVLQRACSDLQPMDD----LLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPE 583
Cdd:PRK10060 462 AEESGLIVPLGRWVMLDVVRQVAKWRDkginLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 584 RSLAVVENLKAQGIAVALDDFGTGYSSIGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVED 663
Cdd:PRK10060 542 LALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVET 621
|
410 420 430
....*....|....*....|....*....|....*...
gi 2119197963 664 PQQLALLRRAGCDRLQGYYFSKPMPIADL---LQRRQP 698
Cdd:PRK10060 622 AKEDAFLTKNGVNERQGFLFAKPMPAVAFerwYKRYLK 659
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
455-691 |
1.58e-88 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 276.79 E-value: 1.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 455 ENGIRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACSDL----- 529
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLaewqa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 530 QPMDDLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYS 609
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 610 SIGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPI 689
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 2119197963 690 AD 691
Cdd:smart00052 241 DD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
458-686 |
3.38e-77 |
|
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: 247.23 E-value: 3.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 458 IRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACSDLQPMD---D 534
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQlgpD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 535 LLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGYL 614
Cdd:pfam00563 84 IKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119197963 615 RRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKP 686
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
281-437 |
1.18e-33 |
|
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: 126.68 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 281 AMIDWLSRLPNRRAL---LLRLSQVCETGKHDIqCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARM 357
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLeemLDSELKRARRFQRSF-SVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 358 GGDEFAMAVSGAKAIDRAAAFAWAALELLKAPVTLSKR-KIYIGASIGIASGAPAECSSTELFRRADIAMYHAKKSGKGR 436
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSeTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 2119197963 437 T 437
Cdd:TIGR00254 161 V 161
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
97-695 |
2.38e-174 |
|
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: 513.94 E-value: 2.38e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 97 VLDEHYRILWGAFQSQVMPRTDLSFLGAGLTSLIHTHAQALREGKNAFAGITRTEAGIAFVGIGLIRPTTARLQVFDATR 176
Cdd:COG5001 67 LLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 177 RYLVITRHINPQLLERLGDTFQISHLHLAEGPGAYRIPLRTQAGEVLGYLAWQPRLPGAEAAQASSGSMRLIAGVAASLI 256
Cdd:COG5001 147 AALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 257 LLFILFSSLGMYKLARGERQAREIAMIDWLSRLPNRRALLLRLSQVCETGKHDIQC--VVFIDLDGFKDVNDNYGHDVGD 334
Cdd:COG5001 227 LVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRlaLLFIDLDRFKEINDTLGHAAGD 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 335 ALIRHIASALQTRVPAGAMLARMGGDEFAMAVSGAKAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIASGAPAECS 414
Cdd:COG5001 307 ELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGAD 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 415 STELFRRADIAMYHAKKSGKGRTAWYDDALDAVRRHQMTIENGIRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRR 494
Cdd:COG5001 387 AEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHP 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 495 PQGALAPDAFISIAESSGLIDALGQFVLQRACSDL-----QPMDDLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRL 569
Cdd:COG5001 467 ERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLaawqdAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRL 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 570 QVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIA 649
Cdd:COG5001 547 ELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALA 626
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 2119197963 650 RALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPIADLLQR 695
Cdd:COG5001 627 HSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEAL 672
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
161-695 |
1.49e-104 |
|
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: 330.59 E-value: 1.49e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 161 LIRPTTARLQVFDATRRYLVITRHINPQLLERLGDTFQISHLHLAEGPGAYRIPLRTQAGEVLGYLAWQPRLPGAEAAQA 240
Cdd:COG2200 35 LALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 241 SSGSMRLIAGVAASLILLFILFSSLGMYKLARGERQAREIAMIDWLSRLPNRRALLLRLSQVCET--GKHDIQCVVFIDL 318
Cdd:COG2200 115 LLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLlaLALLALLLLLLLL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 319 DGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARMGGDEFAMAVSGAKAIDRAAAFAWAALELLKAPVTLSKRKIY 398
Cdd:COG2200 195 LLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 399 IGASIGIASgAPAECSSTELFRRADIAMYHAKKSGKGRTAWYDDALDAVRRHQMTIENGIRQGLEEEEFEVWYQPVVDAD 478
Cdd:COG2200 275 VASSGGGAA-APDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARRRLALESELREALEEGELRLYYQPIVDLR 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 479 TLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACSDL----QPMDDLLLSVNISPAQFRDPAFENR 554
Cdd:COG2200 354 TGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLarwpERGLDLRLSVNLSARSLLDPDFLER 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 555 VMKTVAACRFPPSRLQVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGYLRRFRFDSLKIDKSLAGRVER 634
Cdd:COG2200 434 LLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIAR 513
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119197963 635 DEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPIADLLQR 695
Cdd:COG2200 514 DPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEAL 574
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
458-691 |
1.71e-100 |
|
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: 307.94 E-value: 1.71e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 458 IRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACSDL----QPMD 533
Cdd:cd01948 3 LRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLarwqAGGP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 534 DLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGY 613
Cdd:cd01948 83 DLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119197963 614 LRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPIAD 691
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
274-698 |
6.29e-90 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 294.67 E-value: 6.29e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 274 ERQA----REIAMIDWLSRLPNRRALLLRLSQVCETGKHDIQCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVP 349
Cdd:PRK10060 226 ERRAqerlRILANTDSITGLPNRNAIQELIDHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSCLE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 350 AGAMLARMGGDEF-AMAVSGAKAIdrAAAFAWAALELLKAPVTLSKRKIYIGASIGIASgAPAECSSTE-LFRRADIAMY 427
Cdd:PRK10060 306 EDQTLARLGGDEFlVLASHTSQAA--LEAMASRILTRLRLPFRIGLIEVYTGCSIGIAL-APEHGDDSEsLIRSADTAMY 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 428 HAKKSGKGRTAWYDDALDAVRRHQMTIENGIRQGLEEEEFEVWYQPVVDAdTLAMIGVEALLRWPRRPQGALAPDAFISI 507
Cdd:PRK10060 383 TAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPPLEFISY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 508 AESSGLIDALGQFVLQRACSDLQPMDD----LLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPE 583
Cdd:PRK10060 462 AEESGLIVPLGRWVMLDVVRQVAKWRDkginLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 584 RSLAVVENLKAQGIAVALDDFGTGYSSIGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVED 663
Cdd:PRK10060 542 LALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVET 621
|
410 420 430
....*....|....*....|....*....|....*...
gi 2119197963 664 PQQLALLRRAGCDRLQGYYFSKPMPIADL---LQRRQP 698
Cdd:PRK10060 622 AKEDAFLTKNGVNERQGFLFAKPMPAVAFerwYKRYLK 659
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
455-691 |
1.58e-88 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 276.79 E-value: 1.58e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 455 ENGIRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACSDL----- 529
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLaewqa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 530 QPMDDLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYS 609
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 610 SIGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPI 689
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 2119197963 690 AD 691
Cdd:smart00052 241 DD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
458-686 |
3.38e-77 |
|
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: 247.23 E-value: 3.38e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 458 IRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACSDLQPMD---D 534
Cdd:pfam00563 4 LRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQlgpD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 535 LLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGYL 614
Cdd:pfam00563 84 IKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119197963 615 RRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKP 686
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
447-699 |
1.38e-71 |
|
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: 241.74 E-value: 1.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 447 VRRHQMTIENGIRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRAC 526
Cdd:COG4943 265 LLRRRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVF 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 527 SDLQPM----DDLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYvLENPERSLAVVENLKAQGIAVALD 602
Cdd:COG4943 345 RDLGDLlaadPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERG-FIDPAKARAVIAALREAGHRIAID 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 603 DFGTGYSSIGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYY 682
Cdd:COG4943 424 DFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWL 503
|
250
....*....|....*..
gi 2119197963 683 FSKPMPIADLLQRRQPQ 699
Cdd:COG4943 504 FAKPLPAEEFIAWLAAQ 520
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
200-692 |
1.32e-69 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 242.75 E-value: 1.32e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 200 SHLHLAEGPGA-YRIPLRTQAGEVLGYLAWQPRlpgaeAAQASSGSMRLIAGVAASLILLFIlfsslgmyKLARGERQAR 278
Cdd:PRK11359 307 SSHGAEYQNAQsWSATIRQRDGAPAGTLQIKTS-----SGAETSAFIERVADISQHLAALAL--------EQEKSRQHIE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 279 EIAMIDWLSRLPNRRALLLRLSQVCETgkhDIQCVVF-IDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARM 357
Cdd:PRK11359 374 QLIQFDPLTGLPNRNNLHNYLDDLVDK---AVSPVVYlIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRI 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 358 GGDEFAMaVSGAKAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIA--SGAPAEcsstELFRRADIAMYHAKKSGKG 435
Cdd:PRK11359 451 EGTQFVL-VSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISydVGKNRD----YLLSTAHNAMDYIRKNGGN 525
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 436 RTAWYDDALDAVRRHQMTIENGIRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWpRRPQ-GALAPDAFISIAESSGLI 514
Cdd:PRK11359 526 GWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARW-HDPLhGHVPPSRFIPLAEEIGEI 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 515 DALGQFVLQRACSDLQPMDDL-----LLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPERSLAVV 589
Cdd:PRK11359 605 ENIGRWVIAEACRQLAEWRSQnihipALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRI 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 590 ENLKAQGIAVALDDFGTGYSSIGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLAL 669
Cdd:PRK11359 685 QILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEM 764
|
490 500
....*....|....*....|...
gi 2119197963 670 LRRAGCDRLQGYYFSKPMPIADL 692
Cdd:PRK11359 765 LRKIHCRVIQGYFFSRPLPAEEI 787
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
270-695 |
1.06e-66 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 231.91 E-value: 1.06e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 270 LARGERQAREIAMIDWLSRLPNRRALLLRLSQVCETGkhDIQCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVP 349
Cdd:PRK13561 220 LQRQYEEQSRNATRFPVSDLPNKALLMALLEQVVARK--QTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVLS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 350 AGAMLARMGGDEFAMAVSGAKAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIASgAPAECSSTELFRRADIAMYHA 429
Cdd:PRK13561 298 PRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAM-FYGDLTAEQLYSRAISAAFTA 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 430 KKSGKGRTAWYDDALDAVRRHQMTIENGIRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWpRRPQGALA-PDAFISIA 508
Cdd:PRK13561 377 RRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRM-QQPDGSWDlPEGLIDRI 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 509 ESSGLIDALGQFVLQRACSDLQPMD----DLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPER 584
Cdd:PRK13561 456 ESCGLMVTVGHWVLEESCRLLAAWQergiMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHA 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 585 SLAVVENLKAQGIAVALDDFGTGYSSIGYLRRFR---FDSLKIDKSLAGRVERDEQaaeMVRGTVRIARALGMTVVAEGV 661
Cdd:PRK13561 536 AVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGLPEDDS---MVAAIIMLAQSLNLQVIAEGV 612
|
410 420 430
....*....|....*....|....*....|....
gi 2119197963 662 EDPQQLALLRRAGCDRLQGYYFSKPMPIADLLQR 695
Cdd:PRK13561 613 ETEAQRDWLLKAGVGIAQGFLFARALPIEIFEER 646
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
287-693 |
2.64e-57 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 206.33 E-value: 2.64e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 287 SRLPNRrALLLRL--SQVCETGKHDIQCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARMGGDEFAM 364
Cdd:PRK11829 238 TELPNR-SLFISLleKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 365 AVSGAKAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIASGAPAECSSTELFRRADIAMYHAKKSGKGRTAWYDDAL 444
Cdd:PRK11829 317 LARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 445 DAVRRHQMTIENGIRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQR 524
Cdd:PRK11829 397 IEKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 525 ACSDLQPMD----DLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPERSLAVVENLKAQGIAVA 600
Cdd:PRK11829 477 ACRILADWKargvSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIA 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 601 LDDFGTGYSSIGYLRRFR---FDSLKIDKSLAGRVERDEQAAEMVRGtvrIARALGMTVVAEGVEDPQQLALLRRAGCDR 677
Cdd:PRK11829 557 LDDFGIGYSSLRYLNHLKslpIHMIKLDKSFVKNLPEDDAIARIISC---VSDVLKVRVMAEGVETEEQRQWLLEHGIQC 633
|
410
....*....|....*.
gi 2119197963 678 LQGYYFSKPMPIADLL 693
Cdd:PRK11829 634 GQGFLFSPPLPRAEFE 649
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
275-693 |
3.98e-55 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 204.14 E-value: 3.98e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 275 RQAREIAMIDWLSRLPNRRALLLRLSQVCETGK--HDIQCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGA 352
Cdd:PRK09776 659 RQLSYSASHDALTHLANRASFEKQLRRLLQTVNstHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 353 MLARMGGDEFAM-----AVSGAKAIDRaaafawaalELLKA----PVTLSKRKIYIGASIGIASGAPAECSSTELFRRAD 423
Cdd:PRK09776 739 VLARLGGDEFGLllpdcNVESARFIAT---------RIISAindyHFPWEGRVYRVGASAGITLIDANNHQASEVMSQAD 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 424 IAMYHAKKSGKGRTAWYD-DALDAVR-RHQMTIENGIRQGLEEEEFEVWYQPVVDADTLAMIGVEALLR-WprRPQGAL- 499
Cdd:PRK09776 810 IACYAAKNAGRGRVTVYEpQQAAAHSeHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRlW--DPEGEIi 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 500 APDAFISIAESSGLIDALGQFVLQRACSDLQP---MDDLLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTES 576
Cdd:PRK09776 888 DEGAFRPAAEDPALMHALDRRVIHEFFRQAAKavaSKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLLHLEITET 967
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 577 YVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTV 656
Cdd:PRK09776 968 ALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHAQRLGMKT 1047
|
410 420 430
....*....|....*....|....*....|....*..
gi 2119197963 657 VAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPIADLL 693
Cdd:PRK09776 1048 IAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLL 1084
|
|
| CHASE4 |
COG3322 |
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction ... |
1-700 |
6.82e-54 |
|
Extracellular (periplasmic) sensor domain CHASE (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 442551 [Multi-domain] Cd Length: 724 Bit Score: 197.86 E-value: 6.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 1 MIFLAGLGLTASVISLLYLSQHLI----ASKSNEIDQQRSVLSVEGAVQTSVNRVLSLVLDNAIWDDAVTQTYAPslDQK 76
Cdd:COG3322 6 KTLLAILLLLLLLLALLYLVSRLIllssFSELEEQAAERDVERVLNALDAELDQLARLVADWAVWDDTYEFVQDG--DPE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 77 WLYDSWGSGFKINNLYDGTFVLDEHYRILWGAFQSQVmpRTDLSFLGAGLTSLIHTHAQALREG--KNAFAGITRTEAGI 154
Cdd:COG3322 84 WIESNLGDWTFENLGLDLVLVLDPDGRLVYSKGYDLE--DGELVPLPEALAPLLARARALLRHAspDSSVSGLLRLDGGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 155 AFVGIGLIRPTTARlqvfDATRRYLVITRHINPQLLERLGDTFQIS-HLHLAEGPG--------------AYRIPLRTQA 219
Cdd:COG3322 162 ALVAARPILPSDGP----GPPRGTLVFGRYLDEAFLARLAERTGLDlTLSPADPPAppdqvveplsddtiAGYVPLRDID 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 220 GEVLGYLAWQPRLP----GAEAAQASSGSMRLIAGVAASLILLFILFSSLGMYKLARGERQAREIamidwLSRLPNRRAL 295
Cdd:COG3322 238 GQPVLLLRWTPPRPiyqqGRALLRYLLPALLLLGLLLALLALLLLRLVLLLLLLLLRLVLSRLLL-----LLLRLLLLEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 296 LLRLSQVCETGkhdiqcVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARMGGDEFAMAVSGAKAIDRA 375
Cdd:COG3322 313 LRALELLLLLL------RRLLLLLLLLRLLLLLLDLLAALNLLLLLRALAERLVALALLALLLLGLLGLLAALRRLGLLA 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 376 AAFAWAALELLKAPVTLSKRKIYIGASIGIASGAPAECSSTELFRRADIAMYHAKKSGKGRTAWYDDALDAVRRHQMTIE 455
Cdd:COG3322 387 ILALAEEAARLLLLALAIAGELLIGIEVLLALGLELAGSAIALARAAAALALLLAAAAAARLAARAASGLLRDLLEADEL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 456 NGIRQGLEEEEFEVWYQPVVDAD-TLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACSDLQPMDD 534
Cdd:COG3322 467 EDRLRRALLAEAAALLLLALLALeLLLALGDAALEILLAILLLGLVLEAQLAELERLLLLGEAGGELLEEIALLAALLAG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 535 LLLSVNISPAQFRDPAFENRVMKTVAACRFPPSRLQVEVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGYL 614
Cdd:COG3322 547 LLLAVLLSLLLRLLLLIDALVALAEAAAGLLEALLEEEVELRRALLEAEELLLIALALLSLGLALALDDGGRGLAGLLLL 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 615 RRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPIADLLQ 694
Cdd:COG3322 627 FRLSGIGLLLLRRLLGDDLLGLLAALIDLILALAGSLLLLTLAAAAEATAVVLVAELLEGALLLQALALISLLELLLLLL 706
|
....*.
gi 2119197963 695 RRQPQG 700
Cdd:COG3322 707 LLELQL 712
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
458-694 |
5.67e-51 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 185.58 E-value: 5.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 458 IRQGLEEEEFEVWYQPVVDADTLAMIGVEALLRWPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACSDLQPMDDLL- 536
Cdd:PRK10551 268 ILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIARDAAELQKVLp 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 537 ----LSVNISPAQFRDPAFENRVMKTVAAcrFPPSRLQV--EVTESYVLENpERSLAVVENLKAQGIAVALDDFGTGYSS 610
Cdd:PRK10551 348 vgakLGINISPAHLHSDSFKADVQRLLAS--LPADHFQIvlEITERDMVQE-EEATKLFAWLHSQGIEIAIDDFGTGHSA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 611 IGYLRRFRFDSLKIDKSLAGRVERDEQAAEMVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPIA 690
Cdd:PRK10551 425 LIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLE 504
|
....
gi 2119197963 691 DLLQ 694
Cdd:PRK10551 505 DFVR 508
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
282-436 |
1.90e-45 |
|
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: 159.26 E-value: 1.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 282 MIDWLSRLPNRRALLLRLSQVCETGKHDIQ--CVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARMGG 359
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRplALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119197963 360 DEFAMAVSGAkAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIASGAPAECSSTELFRRADIAMYHAKKSGKGR 436
Cdd:cd01949 81 DEFAILLPGT-DLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
167-440 |
5.94e-45 |
|
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: 162.07 E-value: 5.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 167 ARLQVFDATRRYLVITRHINPQLLERLGDTFQISHLHLAEGPGAYRIPLRTQAGEVLGYLAWQPRLPGAEAAQASSGSMR 246
Cdd:COG2199 1 VLLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 247 LIAgVAASLILLFILFSSLGMYKLARGERQAREIAMIDWLSRLPNRRALLLRLSQVCETGKHDIQ--CVVFIDLDGFKDV 324
Cdd:COG2199 81 LEL-LLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRplALLLIDLDHFKRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 325 NDNYGHDVGDALIRHIASALQTRVPAGAMLARMGGDEFAMAVSGAKAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIG 404
Cdd:COG2199 160 NDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 2119197963 405 IASGAPAECSSTELFRRADIAMYHAKKSGKGRTAWY 440
Cdd:COG2199 240 VALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
281-436 |
1.24e-38 |
|
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: 140.47 E-value: 1.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 281 AMIDWLSRLPNRRALLLRLSQVCETGKHDIQC--VVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARMG 358
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPvaVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 359 GDEFAMAVSGA--KAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIASGAPAECSSTELFRRADIAMYHAKKSGKGR 436
Cdd:pfam00990 81 GDEFAILLPETslEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
279-440 |
9.39e-38 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 138.15 E-value: 9.39e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 279 EIAMIDWLSRLPNRRALLLRLSQV---CETGKHDIqCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLA 355
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQElqrAQRQGSPF-ALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 356 RMGGDEFAMAVSGAkAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIASGAPAECSSTELFRRADIAMYHAKKSGKG 435
Cdd:smart00267 80 RLGGDEFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRN 158
|
....*
gi 2119197963 436 RTAWY 440
Cdd:smart00267 159 QVAVY 163
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
281-437 |
1.18e-33 |
|
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: 126.68 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 281 AMIDWLSRLPNRRAL---LLRLSQVCETGKHDIqCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARM 357
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLeemLDSELKRARRFQRSF-SVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 358 GGDEFAMAVSGAKAIDRAAAFAWAALELLKAPVTLSKR-KIYIGASIGIASGAPAECSSTELFRRADIAMYHAKKSGKGR 436
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSeTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 2119197963 437 T 437
Cdd:TIGR00254 161 V 161
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
283-448 |
8.57e-20 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 90.51 E-value: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 283 IDWLSRLPNRRALLLRL-SQVCETGKHDIqCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARMGGDE 361
Cdd:PRK09894 131 MDVLTGLPGRRVLDESFdHQLRNREPQNL-YLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 362 FAMAVSGAKAIDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIASGAPAEcSSTELFRRADIAMYHAKKSGKGRTAWYD 441
Cdd:PRK09894 210 FIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFPEE-TLDVVIGRADRAMYEGKQTGRNRVMFID 288
|
....*..
gi 2119197963 442 DALDAVR 448
Cdd:PRK09894 289 EQNVINR 295
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
236-449 |
9.43e-20 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 93.54 E-value: 9.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 236 EAAQASSGSMRLIAGVAASLILLFILFSSL---GMYK--LARGErQAREIAMIDWLSRLPNRRALLLRLSQVCETGKHDI 310
Cdd:PRK15426 349 EGVRGDFGSISIALTLLWALFTAMLLISWYvirRMVSnmFVLQS-SLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQ 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 311 Q--CVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLARMGGDEFAMAVSGAKAIDRAAAFAWAALELLKA 388
Cdd:PRK15426 428 QpfSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEK 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119197963 389 PVTLSK-RKIYIGASIGIASGAPAECSSTE-LFRRADIAMYHAKKSGKGRTAWYDDALDAVRR 449
Cdd:PRK15426 508 EILVAKsTTIRISASLGVSSAEEDGDYDFEqLQSLADRRLYLAKQAGRNRVCASDNAHEREVK 570
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
257-437 |
2.06e-19 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 90.66 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 257 LLFILFSSLGMYKLARGERQAREIAMIDWLSRLPNRR--ALLLRLS-QVCETGKHDiQCVVFIDLDGFKDVNDNYGHDVG 333
Cdd:PRK10245 181 LLFAWVSYQTATKLAEHKRRLQVMSTRDGMTGVYNRRhwETLLRNEfDNCRRHHRD-ATLLIIDIDHFKSINDTWGHDVG 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 334 DALIRHIASALQTRVPAGAMLARMGGDEFAMAVSGAKAiDRAAAFAWAALELLKAPVTLSKRKIYIGASIGIASGAPAEC 413
Cdd:PRK10245 260 DEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPA-ESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVAPLNPQMS 338
|
170 180
....*....|....*....|....
gi 2119197963 414 SSTELFRRADIAMYHAKKSGKGRT 437
Cdd:PRK10245 339 HYREWLKSADLALYKAKNAGRNRT 362
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
279-436 |
1.25e-18 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 89.19 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 279 EIAMIDWLSRLPNRRALLLRLSQVCE--TGKHDIQCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAMLAR 356
Cdd:PRK09581 290 EMAVTDGLTGLHNRRYFDMHLKNLIEraNERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 357 MGGDEF---------AMAVSGAKAIDRAAAfawaalellKAPVTLSK--RKIYIGASIGIASGAPAECSSTELFRRADIA 425
Cdd:PRK09581 370 YGGEEFvvvmpdtdiEDAIAVAERIRRKIA---------EEPFIISDgkERLNVTVSIGVAELRPSGDTIEALIKRADKA 440
|
170
....*....|.
gi 2119197963 426 MYHAKKSGKGR 436
Cdd:PRK09581 441 LYEAKNTGRNR 451
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
472-689 |
1.25e-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: 76.38 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 472 QPVVDADtLAMIGVEaLLrwPRRPQGALAPDAFISIAESSGLIDALGQFVLQRACsdlqpmDDLLLSVNISPAQFRDPAF 551
Cdd:COG3434 9 QPILDRD-QRVVGYE-LL--FRSGLENSAPDVDGDQATARVLLNAFLEIGLDRLL------GGKLAFINFTEELLLSDLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 552 EnrvmktvaacRFPPSRLQVEVTESyVLENPERsLAVVENLKAQGIAVALDDFGTGYSSIGYLRRFRFdsLKIDkslAGR 631
Cdd:COG3434 79 E----------LLPPERVVLEILED-VEPDEEL-LEALKELKEKGYRIALDDFVLDPEWDPLLPLADI--IKID---VLA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119197963 632 VERDEQAAemvrgTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPI 689
Cdd:COG3434 142 LDLEELAE-----LVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEIL 194
|
|
| CHASE4 |
pfam05228 |
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various ... |
43-204 |
1.79e-08 |
|
CHASE4 domain; CHASE4. This is an extracellular sensory domain, which is present in various classes of transmembrane receptors that are parts of signal transduction pathways in prokaryotes. Specifically, CHASE4 domains are found in histidine kinases in Archaea and in predicted diguanylate cyclases/phosphodiesterases in Bacteria. Environmental factors that are recognized by CHASE4 domains are not known at this time.
Pssm-ID: 428380 Cd Length: 139 Bit Score: 53.48 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 43 AVQTSVNRVLSLVLDNAIWDDAVTQTYAPslDQKWLYDSWGSGFKINNLYDGTFVLDEHYRILWGAFQSQVMPRTDLSfl 122
Cdd:pfam05228 1 ALEQELDSLDRLLRDWAVWDDTYDFVQDG--NPDYIESNLGPETFENLGLDLILFVDADGKLVYDLENGKPDSPLLSR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 123 gagltslihthaqalREGKNAFAGITRTEAGIAFVGIGLIRPTTARLQVfdatRRYLVITRHINPQLLERLGDTFQIShL 202
Cdd:pfam05228 77 ---------------SSPDSGLSGIVLLGGGPALVAARPILTSDGSGPP----RGTLVMGRYLDEAFLDRLSELTLLD-L 136
|
..
gi 2119197963 203 HL 204
Cdd:pfam05228 137 TL 138
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
276-430 |
5.30e-07 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 52.70 E-value: 5.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 276 QAREIAMIDWLSRLPNRRALLLRLSQVC-ETGKHDIQCVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRVPAGAML 354
Cdd:PRK09966 243 QLLRTALHDPLTGLANRAAFRSGINTLMnNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKA 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 355 ARMGGDEFAMAVSGAKAIDRAAAFAWAALELLKAPVTL-SKRKIYIGASIGIA---SGAPAEcsstELFRRADIAMYHAK 430
Cdd:PRK09966 323 YRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGYAmtiEHASAE----KLQELADHNMYQAK 398
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
278-689 |
5.66e-07 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 52.94 E-value: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 278 REIAMIDWLSRLPNRraLLL--RL-SQVCETGKHDIQCVVF-IDLDGFKDVNDNYGHDVGDALIRHIASALQTRVP--AG 351
Cdd:PRK11059 225 RSNAFQDAKTGLGNR--LFFdnQLaTLLEDQEMVGAHGVVMlIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMryPG 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 352 AMLARMGGDEFAMAV--SGAKAIDRAAAFAWAALELLKAPVTLSKRKIYigaSIGIA---SGAPAEcsstELFRRADIAM 426
Cdd:PRK11059 303 ALLARYSRSDFAVLLphRSLKEADSLASQLLKAVDALPPPKMLDRDDFL---HIGICayrSGQSTE----QVMEEAEMAL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 427 YHAKKSGKgrTAW--YDDALDA------VR-RhqmTIengIRQGLEEEEFEVWYQPVVDADtlamiGV----EALLRWpR 493
Cdd:PRK11059 376 RSAQLQGG--NGWfvYDKAQLPekgrgsVRwR---TL---LEQTLVRGGPRLYQQPAVTRD-----GKvhhrELFCRI-R 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 494 RPQGAL-APDAFISIAESSGLIDALGQFVLQRACSDLQPMDDLLLSVNISPAQFRDPAFENRVMKTVAACRFP-PSRLQV 571
Cdd:PRK11059 442 DGQGELlSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEENLSINLSVDSLLSRAFQRWLRDTLLQCPRSqRKRLIF 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 572 EVTESYVLENPERSLAVVENLKAQGIAVALDDFGTGYSSIGYLRRFRFDSLKIDKSLagrVERDEQAAE---MVRGTVRI 648
Cdd:PRK11059 522 ELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSL---VRNIHKRTEnqlFVRSLVGA 598
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2119197963 649 ARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPI 689
Cdd:PRK11059 599 CAGTETQVFATGVESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
492-692 |
1.74e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 50.00 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 492 PRRPQGALAPD---AFISIAESSGLIDALGQFVLQRAcsDLQPMDDLLLSVNISP----AQFRDPAfenrVMKTVAACRF 564
Cdd:PRK11596 56 PSNPSQRLSPEryfAEITVSHRLDVVKEQLDLLAQWA--DFFVRHGLLASVNIDGptliALRQQPA----ILRLIERLPW 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 565 ppsrLQVEVTESYVLEnPERSLAvvenlkaqGIAVA----LDDFGTGYSSIGYLRRFRFDSLKIDKSLAGRVERDEQAAE 640
Cdd:PRK11596 130 ----LRFELVEHIRLP-KDSPFA--------SMCEFgplwLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRN 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2119197963 641 MVRGTVRIARALGMTVVAEGVEDPQQLALLRRAGCDRLQGYYFSKPMPIADL 692
Cdd:PRK11596 197 LFSQLLHLMNRYCRGVIVEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETL 248
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
312-410 |
1.88e-06 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 47.74 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119197963 312 CVVFIDLDGFKDVNDNYGHDVGDALIRHIASALQTRV-PAGAMLARMGGDEFaMAVSGAKAIDRAAAFAWAALELLKA-- 388
Cdd:cd07556 3 TILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEF-MVVSGLDHPAAAVAFAEDMREAVSAln 81
|
90 100
....*....|....*....|....*..
gi 2119197963 389 -----PVTLskrkiyigaSIGIASGAP 410
Cdd:cd07556 82 qsegnPVRV---------RIGIHTGPV 99
|
|
| |
