|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
3-503 |
1.30e-176 |
|
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: 512.78 E-value: 1.30e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 3 RIQPTRPQVEIVVWLAVFLLLFCLSWSFDWHEGLDAFIEKHHDYPLDHALLAMNISGFLGLIYSALRISDLSREVHRRLQ 82
Cdd:COG5001 163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKR 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 83 AEKNVDWIACHDTLTELPNRRFLDSICAQAMSD-QRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLSSLFPR 161
Cdd:COG5001 243 AEERLRHLAYHDPLTGLPNRRLFLDRLEQALARaRRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 162 E-HVFRLGGDEFVVLARRTGNP-DLAALGNRIVSVIGKPFTFNGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAK 239
Cdd:COG5001 323 GdTVARLGGDEFAVLLPDLDDPeDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 240 KQARNLVKPFVPSMQDELAKRIRVEADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEE 319
Cdd:COG5001 403 AAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 320 AGLIVELTDQLLRHACTDALSWPSE----LVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTA 395
Cdd:COG5001 483 TGLIVPLGEWVLREACRQLAAWQDAglpdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEA 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 396 RIVLDDLVNAGVRIALDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQES 475
Cdd:COG5001 563 LETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEE 642
|
490 500
....*....|....*....|....*...
gi 636787716 476 QLQRLQDLGCDIGQGYLLGRPAPAAELA 503
Cdd:COG5001 643 QLEFLRELGCDYAQGYLFSRPLPAEELE 670
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
265-501 |
1.17e-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: 302.54 E-value: 1.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 265 ADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQLLRHACTDALSWPS- 343
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 344 --ELVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNAGVRIALDDFGTGYSSL 421
Cdd:cd01948 81 gpDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 422 SQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRPAPAAE 501
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
72-502 |
2.43e-95 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 303.14 E-value: 2.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 72 DLSREvhRRLQAEKNVdwIACHDTLTELPNRRFLDSICAQAMSdQRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTV 151
Cdd:PRK10060 222 DITEE--RRAQERLRI--LANTDSITGLPNRNAIQELIDHAIN-AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 152 AQRLSSLFPREHVF-RLGGDEFVVLARRTGNPDLAALGNRIVSVIGKPFTFNGVAVDLGASVGFALYPENGDDLSQVIRH 230
Cdd:PRK10060 297 SLAILSCLEEDQTLaRLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 231 SDCAMYVAKKQARNLVKPFVPSMQDELAKRIRVEADLRAAIRKAEIVPYYQPLVDLkTNKIIGFEALARWKIASGEFIPP 310
Cdd:PRK10060 377 ADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 311 NEFIPVAEEAGLIVELTDQLLRHACTDALSWPS---ELVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESA 387
Cdd:PRK10060 456 LEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDkgiNLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESC 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 388 IIQDAVTARIVLDDLVNAGVRIALDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTIT 467
Cdd:PRK10060 536 LIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVI 615
|
410 420 430
....*....|....*....|....*....|....*
gi 636787716 468 AEGIEQESQLQRLQDLGCDIGQGYLLGRPAPAAEL 502
Cdd:PRK10060 616 AEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
264-501 |
6.34e-88 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 270.24 E-value: 6.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 264 EADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQLLRHACTDALSWPS 343
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 344 ELV----LSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNAGVRIALDDFGTGYS 419
Cdd:smart00052 81 QGPppllISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 420 SLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRPAPA 499
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 636787716 500 AE 501
Cdd:smart00052 241 DD 242
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
264-496 |
9.23e-75 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 236.06 E-value: 9.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 264 EADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQLLRHACTDALSW-- 341
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 342 PSELVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNAGVRIALDDFGTGYSSL 421
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636787716 422 SQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRP 496
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
91-247 |
3.16e-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: 123.99 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 91 ACHDTLTELPNRRFLDSIC-AQAMSDQRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRL-SSLFPREHVFRLG 168
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLdSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILqSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 169 GDEFVVLARRTGNPDLAALGNRIVSVI-GKPFTF-NGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAKKQARNLV 246
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAInSKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
.
gi 636787716 247 K 247
Cdd:TIGR00254 162 V 162
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
3-503 |
1.30e-176 |
|
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: 512.78 E-value: 1.30e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 3 RIQPTRPQVEIVVWLAVFLLLFCLSWSFDWHEGLDAFIEKHHDYPLDHALLAMNISGFLGLIYSALRISDLSREVHRRLQ 82
Cdd:COG5001 163 ALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKR 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 83 AEKNVDWIACHDTLTELPNRRFLDSICAQAMSD-QRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLSSLFPR 161
Cdd:COG5001 243 AEERLRHLAYHDPLTGLPNRRLFLDRLEQALARaRRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLRE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 162 E-HVFRLGGDEFVVLARRTGNP-DLAALGNRIVSVIGKPFTFNGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAK 239
Cdd:COG5001 323 GdTVARLGGDEFAVLLPDLDDPeDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAK 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 240 KQARNLVKPFVPSMQDELAKRIRVEADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEE 319
Cdd:COG5001 403 AAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 320 AGLIVELTDQLLRHACTDALSWPSE----LVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTA 395
Cdd:COG5001 483 TGLIVPLGEWVLREACRQLAAWQDAglpdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEA 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 396 RIVLDDLVNAGVRIALDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQES 475
Cdd:COG5001 563 LETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEE 642
|
490 500
....*....|....*....|....*...
gi 636787716 476 QLQRLQDLGCDIGQGYLLGRPAPAAELA 503
Cdd:COG5001 643 QLEFLRELGCDYAQGYLFSRPLPAEELE 670
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
13-503 |
1.17e-103 |
|
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: 322.12 E-value: 1.17e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 13 IVVWLAVFLLLFCLSWSFDWHEGLDAFIEKHHDYPLDHALLAMNISGFLGLIYSALRISDLSREVHRRLQAEKNVDWIAC 92
Cdd:COG2200 77 LLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 93 HDTLTELPNRRFLDSICAQAMSDQRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLSSLFPREHVFRLGGDE- 171
Cdd:COG2200 157 DLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGg 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 172 --FVVLARRTGNPDLAALGNRIVSVIGKPFTFNGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAKKQARNLVkPF 249
Cdd:COG2200 237 gfLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRV-VF 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 250 VPSMQDELAKRIRVEADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQ 329
Cdd:COG2200 316 FAAAEARARRRLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRW 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 330 LLRHACTDALSWPS---ELVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNAG 406
Cdd:COG2200 396 VLERALRQLARWPErglDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 407 VRIALDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCD 486
Cdd:COG2200 476 VRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCD 555
|
490
....*....|....*..
gi 636787716 487 IGQGYLLGRPAPAAELA 503
Cdd:COG2200 556 YAQGYLFGRPLPLEELE 572
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
265-501 |
1.17e-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: 302.54 E-value: 1.17e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 265 ADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQLLRHACTDALSWPS- 343
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 344 --ELVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNAGVRIALDDFGTGYSSL 421
Cdd:cd01948 81 gpDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 422 SQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRPAPAAE 501
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAEE 240
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
72-502 |
2.43e-95 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 303.14 E-value: 2.43e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 72 DLSREvhRRLQAEKNVdwIACHDTLTELPNRRFLDSICAQAMSdQRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTV 151
Cdd:PRK10060 222 DITEE--RRAQERLRI--LANTDSITGLPNRNAIQELIDHAIN-AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDV 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 152 AQRLSSLFPREHVF-RLGGDEFVVLARRTGNPDLAALGNRIVSVIGKPFTFNGVAVDLGASVGFALYPENGDDLSQVIRH 230
Cdd:PRK10060 297 SLAILSCLEEDQTLaRLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRS 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 231 SDCAMYVAKKQARNLVKPFVPSMQDELAKRIRVEADLRAAIRKAEIVPYYQPLVDLkTNKIIGFEALARWKIASGEFIPP 310
Cdd:PRK10060 377 ADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIPP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 311 NEFIPVAEEAGLIVELTDQLLRHACTDALSWPS---ELVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESA 387
Cdd:PRK10060 456 LEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDkgiNLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESC 535
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 388 IIQDAVTARIVLDDLVNAGVRIALDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTIT 467
Cdd:PRK10060 536 LIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVI 615
|
410 420 430
....*....|....*....|....*....|....*
gi 636787716 468 AEGIEQESQLQRLQDLGCDIGQGYLLGRPAPAAEL 502
Cdd:PRK10060 616 AEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
264-501 |
6.34e-88 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 270.24 E-value: 6.34e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 264 EADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQLLRHACTDALSWPS 343
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 344 ELV----LSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNAGVRIALDDFGTGYS 419
Cdd:smart00052 81 QGPppllISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 420 SLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRPAPA 499
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
..
gi 636787716 500 AE 501
Cdd:smart00052 241 DD 242
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
69-502 |
2.61e-77 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 258.55 E-value: 2.61e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 69 RISDLSreVHR---RLQAEKN---VDWIACHDTLTELPNRRFLDSICAQAMSDQRaqeSYAVFSIDLDGFKKVNDLLGHD 142
Cdd:PRK11359 350 RVADIS--QHLaalALEQEKSrqhIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAV---SPVVYLIGVDHFQDVIDSLGYA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 143 HGDAVLKTVAQRLSSLF-PREHVFRLGGDEFVVLARRTGNPDLAALGNRIVSVIGKPFTFNGVAVDLGASVGFALypENG 221
Cdd:PRK11359 425 WADQALLEVVNRFREKLkPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISY--DVG 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 222 DDLSQVIRHSDCAMYVAKKQARNLVKPFVPSMQDELAKRIRVEADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWK 301
Cdd:PRK11359 503 KNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWH 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 302 IASGEFIPPNEFIPVAEEAGLIVELTDQLLRHACTDALSWPSE----LVLSFNLSPIQLSDRLLGLRILKILGDVGLPAH 377
Cdd:PRK11359 583 DPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQnihiPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGH 662
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 378 RVELEVTESAIIqdAVTARI--VLDDLVNAGVRIALDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAI 455
Cdd:PRK11359 663 QLTVEITESMMM--EHDTEIfkRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAI 740
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 636787716 456 IALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRPAPAAEL 502
Cdd:PRK11359 741 TSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEI 787
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
264-502 |
3.74e-77 |
|
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: 251.76 E-value: 3.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 264 EADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQLLRHACTDALSW-- 341
Cdd:COG4943 273 RRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLla 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 342 -PSELVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIqDAVTARIVLDDLVNAGVRIALDDFGTGYSS 420
Cdd:COG4943 353 aDPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFI-DPAKARAVIAALREAGHRIAIDDFGTGYSS 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 421 LSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRPAPAA 500
Cdd:COG4943 432 LSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPLPAE 511
|
..
gi 636787716 501 EL 502
Cdd:COG4943 512 EF 513
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
264-496 |
9.23e-75 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 236.06 E-value: 9.23e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 264 EADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQLLRHACTDALSW-- 341
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 342 PSELVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNAGVRIALDDFGTGYSSL 421
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636787716 422 SQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRP 496
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
91-501 |
1.84e-74 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 247.70 E-value: 1.84e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 91 ACHDTLTELPNRRFLDSICAQAMSDQraqESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRL-SSLFPREHVFRLGG 169
Cdd:PRK13561 231 ATRFPVSDLPNKALLMALLEQVVARK---QTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLkSVLSPRMVLAQISG 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 170 DEFVVLARRTGNPDLA-ALGNRIVSVIGKPFTFNGVAVDLGASVGFALYpENGDDLSQVIRHSDCAMYVAKKQARNLVKP 248
Cdd:PRK13561 308 YDFAIIANGVKEPWHAiTLGQQVLTIINERLPIQRIQLRPSCSIGIAMF-YGDLTAEQLYSRAISAAFTARRKGKNQIQF 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 249 FVPSMQDELAKRIRVEADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTD 328
Cdd:PRK13561 387 FDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGH 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 329 QLLRHACTDALSWPS---ELVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNA 405
Cdd:PRK13561 467 WVLEESCRLLAAWQErgiMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 406 GVRIALDDFGTGYSSLSQLSNYR---FDKIKIDRSFVSSFETNdkqDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQD 482
Cdd:PRK13561 547 GVRVALDDFGMGYAGLRQLQHMKslpIDVLKIDKMFVDGLPED---DSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLK 623
|
410
....*....|....*....
gi 636787716 483 LGCDIGQGYLLGRPAPAAE 501
Cdd:PRK13561 624 AGVGIAQGFLFARALPIEI 642
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
97-508 |
8.48e-68 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 230.21 E-value: 8.48e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 97 TELPNRRFLDSICAQAMSDQRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRL-SSLFPREHVFRLGGDEFVVL 175
Cdd:PRK11829 238 TELPNRSLFISLLEKEIASSTRTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIeQCIDDSDLLAQLSKTEFAVL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 176 ARRTGNP-DLAALGNRIVSVIGKPFTFNGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAKKQARNLVKPFVPSMQ 254
Cdd:PRK11829 318 ARGTRRSfPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLI 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 255 DELAKRIRVEADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQLLRHA 334
Cdd:PRK11829 398 EKTHKRLTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 335 CTDALSWPSE---LVLSFNLSPIQLSDRLLGLRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNAGVRIAL 411
Cdd:PRK11829 478 CRILADWKARgvsLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIAL 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 412 DDFGTGYSSLSQLSNYR---FDKIKIDRSFVSSFETNDKQDKVIKAIIALgvgLGVTITAEGIEQESQLQRLQDLGCDIG 488
Cdd:PRK11829 558 DDFGIGYSSLRYLNHLKslpIHMIKLDKSFVKNLPEDDAIARIISCVSDV---LKVRVMAEGVETEEQRQWLLEHGIQCG 634
|
410 420
....*....|....*....|....*.
gi 636787716 489 QGYLLGRPAPAAEL------ATDHVS 508
Cdd:PRK11829 635 QGFLFSPPLPRAEFeaqyfsSAHHVS 660
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
62-503 |
2.42e-54 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 197.59 E-value: 2.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 62 GLIYSALRISDL--SREVHRRLQaeknvdWIACHDTLTELPNR----RFLDSICAQAMSdqRAQESYAVFsIDLDGFKKV 135
Cdd:PRK09776 640 ENIGSVLVIQDVteSRKMLRQLS------YSASHDALTHLANRasfeKQLRRLLQTVNS--THQRHALVF-IDLDRFKAV 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 136 NDLLGHDHGDAVLKTVAQ-RLSSLFPREHVFRLGGDEFVVLARRTGNPDLAALGNRIVSVI-GKPFTFNGVAVDLGASVG 213
Cdd:PRK09776 711 NDSAGHAAGDALLRELASlMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAInDYHFPWEGRVYRVGASAG 790
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 214 FALYPENGDDLSQVIRHSDCAMYVAKKQARNLVKPFVPsmQDELAKRIRVEADLRAAIRKAE-------IVPYYQPLVDL 286
Cdd:PRK09776 791 ITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEP--QQAAAHSEHRALSLAEQWRMIKenqlmmlAHGVASPRIPE 868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 287 KTNKIigfEALARWKIASGEFIPPNEFIPVAEEAGLIVELTD----QLLRHACTdALSWPSeLVLSFNLSPIQLSDRLLG 362
Cdd:PRK09776 869 ARNHW---LISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRrvihEFFRQAAK-AVASKG-LSIALPLSVAGLSSPTLL 943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 363 LRILKILGDVGLPAHRVELEVTESAIIQDAVTARIVLDDLVNAGVRIALDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSF 442
Cdd:PRK09776 944 PFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANL 1023
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636787716 443 ETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRPAPAAELA 503
Cdd:PRK09776 1024 HGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLL 1084
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
93-244 |
7.85e-51 |
|
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: 170.82 E-value: 7.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 93 HDTLTELPNRRFLDSICAQAMSD-QRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLSSLFPRE-HVFRLGGD 170
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARaRRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESdLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636787716 171 EFVVLARRTGNPDLAALGNRIVSVIGKPFTFNGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAKKQARN 244
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRN 155
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
17-249 |
5.42e-50 |
|
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: 172.86 E-value: 5.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 17 LAVFLLLFCLSWSFDWHEGLDAFIEKHHDYPLDHALLAMNISGFLGLIYSALRISDLSREVHRRLQAEKNVDWIACHDTL 96
Cdd:COG2199 40 LLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 97 TELPNRRFLDSICAQAMSD-QRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLSSLFPREH-VFRLGGDEFVV 174
Cdd:COG2199 120 TGLPNRRAFEERLERELARaRREGRPLALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDlVARLGGDEFAV 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636787716 175 LARRTGNPDLAALGNRIVSVIGK-PFTFNGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAKKQARNLVKPF 249
Cdd:COG2199 200 LLPGTDLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
91-244 |
1.98e-45 |
|
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: 156.64 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 91 ACHDTLTELPNRRFLDSICAQAMSD-QRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLSSLFPREH-VFRLG 168
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRaLREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDlVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 636787716 169 GDEFVVLARRTGNPDLAALGNRI---VSVIGKPFTFNGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAKKQARN 244
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIrrlLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
257-503 |
1.00e-43 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 162.08 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 257 LAKRIRVEADLRAAIRKAEIVPYYQPLVDLKTNKIIGFEALARWKIASGEFIPPNEFIPVAEEAGLIVELTDQLLRHACT 336
Cdd:PRK10551 258 LSLRMRPGKEILTGIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFELIAR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 337 DA----LSWPSELVLSFNLSPIQLSDRLLGLRILKILGDvgLPAHRVE--LEVTESAIIQDAVTARiVLDDLVNAGVRIA 410
Cdd:PRK10551 338 DAaelqKVLPVGAKLGINISPAHLHSDSFKADVQRLLAS--LPADHFQivLEITERDMVQEEEATK-LFAWLHSQGIEIA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 411 LDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQG 490
Cdd:PRK10551 415 IDDFGTGHSALIYLERFTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQG 494
|
250
....*....|...
gi 636787716 491 YLLGRPAPAAELA 503
Cdd:PRK10551 495 YWISRPLPLEDFV 507
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
93-244 |
1.20e-43 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 152.02 E-value: 1.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 93 HDTLTELPNRRFLDSICAQAMSD-QRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLSSLFPREH-VFRLGGD 170
Cdd:smart00267 5 RDPLTGLPNRRYFEEELEQELQRaQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDlLARLGGD 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 636787716 171 EFVVLARRTGNPDLAALGNRIVSVIGKPFTFNGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAKKQARN 244
Cdd:smart00267 85 EFALLLPETSLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRN 158
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
91-247 |
3.16e-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: 123.99 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 91 ACHDTLTELPNRRFLDSIC-AQAMSDQRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRL-SSLFPREHVFRLG 168
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLdSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILqSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 169 GDEFVVLARRTGNPDLAALGNRIVSVI-GKPFTF-NGVAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAKKQARNLV 246
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAInSKPIEVaGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
.
gi 636787716 247 K 247
Cdd:TIGR00254 162 V 162
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
94-246 |
1.75e-24 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 103.22 E-value: 1.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 94 DTLTELPNRRFLDSiCAQAMSDQRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLSS-LFPREHVFRLGGDEF 172
Cdd:PRK09894 132 DVLTGLPGRRVLDE-SFDHQLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASwTRDYETVYRYGGEEF 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 636787716 173 VVLARRTGNPDLAALGNRIVSVI-GKPFTFNGVAVDLGASVGFALYPEnGDDLSQVIRHSDCAMYVAKKQARNLV 246
Cdd:PRK09894 211 IICLKAATDEEACRAGERIRQLIaNHAITHSDGRINITATFGVSRAFP-EETLDVVIGRADRAMYEGKQTGRNRV 284
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
89-246 |
1.43e-22 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 101.24 E-value: 1.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 89 WIACHDTLTELPNRR-FLDSICAQAMSDQRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLSSLFpREHVF-- 165
Cdd:PRK15426 396 WQAWHDPLTRLYNRGaLFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSL-RAQDVag 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 166 RLGGDEFVVLARRTGNPDLAALGNRIVSVIGKPFTF--NGVAVDLGASVGFALYPENGD-DLSQVIRHSDCAMYVAKKQA 242
Cdd:PRK15426 475 RVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILvaKSTTIRISASLGVSSAEEDGDyDFEQLQSLADRRLYLAKQAG 554
|
....
gi 636787716 243 RNLV 246
Cdd:PRK15426 555 RNRV 558
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
94-246 |
6.61e-22 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 98.43 E-value: 6.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 94 DTLTELPNRRFLDSICAQAMSDQRAQE-SYAVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRL-SSLFPREHVFRLGGDE 171
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGkPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLrNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636787716 172 FVVLARRTGNPDLAALGNRI-VSVIGKPFTFNG--VAVDLGASVGFALYPENGDDLSQVIRHSDCAMYVAKKQARNLV 246
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIrRKIAEEPFIISDgkERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
72-247 |
1.26e-17 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 85.06 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 72 DLSREVHRRLQAeKNVDWI--ACHDTLTELPNRRFLDSICAQAMSDQRAQESYAVFSIDLDGFKKVNDLLGHDHGDAVLK 149
Cdd:PRK09966 228 DEMEEWQLRLQA-KNAQLLrtALHDPLTGLANRAAFRSGINTLMNNSDARKTSALLFLDGDNFKYINDTWGHATGDRVLI 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 150 TVAQRLSSLFPREH-VFRLGGDEF-VVLARRTGNPDLAALGNRIVSVIGKPFTF-NGVAVDLGASVGFALYPEN--GDDL 224
Cdd:PRK09966 307 EIAKRLAEFGGLRHkAYRLGGDEFaMVLYDVQSESEVQQICSALTQIFNLPFDLhNGHQTTMTLSIGYAMTIEHasAEKL 386
|
170 180
....*....|....*....|....
gi 636787716 225 SQVirhSDCAMYVAKKQ-ARNLVK 247
Cdd:PRK09966 387 QEL---ADHNMYQAKHQrAEKLVR 407
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
94-499 |
5.13e-14 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 74.51 E-value: 5.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 94 DTLTELPNRRFLDSICAQAMSDQRAQESY-AVFSIDLDGFKKVNDLLGHDHGDAVLKTVAQRLS--------SLFPREHv 164
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLEDQEMVGAHgVVMLIRLPDFDLLQEEWGESQVEELLFELINLLStfvmrypgALLARYS- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 165 frlgGDEF-VVLARRTGNpDLAALGNRIVSVIGK-PFTfngVAVD------LGASvgfalYPENGDDLSQVIRHSDCAMY 236
Cdd:PRK11059 310 ----RSDFaVLLPHRSLK-EADSLASQLLKAVDAlPPP---KMLDrddflhIGIC-----AYRSGQSTEQVMEEAEMALR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 237 VAKKQARNLVKPFVPSMQDELAK-RIRVEADLRAAIRKAEIVPYYQPLVDlKTNKIIGFEALARWKIASGEFIPPNEFIP 315
Cdd:PRK11059 377 SAQLQGGNGWFVYDKAQLPEKGRgSVRWRTLLEQTLVRGGPRLYQQPAVT-RDGKVHHRELFCRIRDGQGELLSAELFMP 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 316 VAEEAGLIVELTDQLLRHACTDALSWPSElVLSFNLSPIQLSDRllglRILKILGDVGL--PAH---RVELEVTESAIIQ 390
Cdd:PRK11059 456 MVQQLGLSEQYDRQVIERVLPLLRYWPEE-NLSINLSVDSLLSR----AFQRWLRDTLLqcPRSqrkRLIFELAEADVCQ 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 391 DAVTARIVLDDLVNAGVRIALDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIKAIIALGVGLGVTITAEG 470
Cdd:PRK11059 531 HISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFATG 610
|
410 420
....*....|....*....|....*....
gi 636787716 471 IEQESQLQRLQDLGCDIGQGYLLGRPAPA 499
Cdd:PRK11059 611 VESREEWQTLQELGVSGGQGDFFAESQPL 639
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
281-496 |
3.27e-10 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 62.13 E-value: 3.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 281 QPLVDlKTNKIIGFEALARwkiaSGEfipPNEFIPVAEEaglivELTDQLLRHACTDA-LSWPSELVLSF-NLSPIQLSD 358
Cdd:COG3434 9 QPILD-RDQRVVGYELLFR----SGL---ENSAPDVDGD-----QATARVLLNAFLEIgLDRLLGGKLAFiNFTEELLLS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 359 RLLGLrilkilgdvgLPAHRVELEVTESAIIQDAVTARivLDDLVNAGVRIALDDF--GTGYSSLSQLSNYrfdkIKIDr 436
Cdd:COG3434 76 DLPEL----------LPPERVVLEILEDVEPDEELLEA--LKELKEKGYRIALDDFvlDPEWDPLLPLADI----IKID- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 437 sfvssFETNDKQDkvIKAIIALGVGLGVTITAEGIEQESQLQRLQDLGCDIGQGYLLGRP 496
Cdd:COG3434 139 -----VLALDLEE--LAELVARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKP 191
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
76-244 |
5.25e-09 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 57.92 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 76 EVHRRLQAeknvdwIACHDTLTELPNRRFLDS-ICAQAMSDQRAQESYAVFSIDLDGFKKVNDLLGHDHGD-AVLKTVAQ 153
Cdd:PRK10245 196 EHKRRLQV------MSTRDGMTGVYNRRHWETlLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDeAIVALTRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 154 RLSSLFPREHVFRLGGDEFVVLARRTGNPDLAALGNRIVSVIGKPFTFNGVAVDLGASVGFA-LYPENGdDLSQVIRHSD 232
Cdd:PRK10245 270 LQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVTLRISVGVApLNPQMS-HYREWLKSAD 348
|
170
....*....|..
gi 636787716 233 CAMYVAKKQARN 244
Cdd:PRK10245 349 LALYKAKNAGRN 360
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
127-213 |
2.30e-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: 46.97 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 127 IDLDGFKKVNDLLGHDHGDAVLKTVAQRLSSLFPREHVF--RLGGDEFVVLARRTGNPDLAALGNRIVSVIGK--PFTFN 202
Cdd:cd07556 7 ADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLkiKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSAlnQSEGN 86
|
90
....*....|.
gi 636787716 203 GVAVDLGASVG 213
Cdd:cd07556 87 PVRVRIGIHTG 97
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
374-498 |
2.61e-06 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 48.84 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636787716 374 LPAHRVELeVTESAIIQDAVTARivlddLVNAGvRIALDDFGTGYSSLSQLSNYRFDKIKIDRSFVSSFETNDKQDKVIK 453
Cdd:PRK11596 127 LPWLRFEL-VEHIRLPKDSPFAS-----MCEFG-PLWLDDFGTGMANFSALSEVRYDYIKVARELFIMLRQSEEGRNLFS 199
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 636787716 454 AIIAL------GVglgvtiTAEGIEQESQLQRLQDLGCDIGQGYLLGRPAP 498
Cdd:PRK11596 200 QLLHLmnrycrGV------IVEGVETPEEWRDVQRSPAFAAQGYFLSRPAP 244
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
164-239 |
6.82e-03 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 37.58 E-value: 6.82e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636787716 164 VFRLGGDEFVVLARRTGNPDLAALGNRIVSVIGKPFTFNgvavdLGASVGFAlypenGDDLsqvIRHSDcAMYVAK 239
Cdd:COG3706 118 VARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSLR-----VTVSIGVA-----GDSL---LKRAD-ALYQAR 179
|
|
| |
