|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
12-652 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 1128.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 12 MAMVSAVSVFFLFIFSVVLLFHFVQSHRYHTAMQMESIARSVRQPLSAAILKANIPEAEAILREIKPAGVISRADVVLPN 91
Cdd:PRK13561 1 MAMVAAVVLVFVFIFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRADVVLPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 92 QFQALRMRFTPERPIPVTLARVFELPVQISLPLYSLERPANPQPLAYLVLQADSWRLYRFIINAISTLLTTFLLLALILS 171
Cdd:PRK13561 81 QFQALRKSFIPERPVPVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSFRMYKFVMSALSTLVTIYLLLSLILT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 172 VAITWCINRLILHPLRDITRTLNALDAHELAHHQLTIPRLHQDDEIGMLVRTYNRNQQALARQVDEARTSGTRFPLTGLP 251
Cdd:PRK13561 161 VAISWCINRLIVHPLRNIARELNDIPPQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 252 NQALLTALLEQAVAGGGATALLYVACEPLRESN----ESQRDALQHARVDKLRSVLTPRMVLAQISQDDFAIIAHGVKTP 327
Cdd:PRK13561 241 NKALLMALLEQVVARKQTTALMIITCETLRDTAgvlkEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 328 EHAVTLTQQLLAALNEPLESPTAAQTGGASIGVAMFDGRQSASTLYQSAISAALDARRSGINQVAFFGEASVNA------ 401
Cdd:PRK13561 321 WHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAaqkrlt 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 402 QESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQ 481
Cdd:PRK13561 401 EESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 482 AHGITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFGMGYS 561
Cdd:PRK13561 481 ERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 562 SLSQLQKMKALPVDSLKIDKSFIDNLPDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKATTP 641
Cdd:PRK13561 561 GLRQLQHMKSLPIDVLKIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPI 640
|
650
....*....|.
gi 1126561684 642 AAFEDAWLPTP 652
Cdd:PRK13561 641 EIFEERYLEEK 651
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
12-649 |
8.33e-115 |
|
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: 358.70 E-value: 8.33e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 12 MAMVSAVSVFFLFIFSVVLLFHFVQSHRYHTAMQMESIARSVRQPLSAAILKANIPEAEAILREIKPAGVISRADVVLPN 91
Cdd:COG5001 28 LLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 92 QFQALRMRFTPERPIPVTLARVFELPVQISLPLYSLERPANPQPLAYLVLQADSWRLYRFIINAISTLLTTFLLLALILS 171
Cdd:COG5001 108 LLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 172 VAITWCINRLILHPLRDITRTLNALDAHELAHHQLTIPRLHQDDEIGMLVRTYNRNQQALARQvdeARTSgtrfPLTGLP 251
Cdd:COG5001 188 LLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHL---AYHD----PLTGLP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 252 NQALLTALLEQAVA----GGGATALLYVACEPLRESNesqrDALQHARVDK--------LRSVLTPRMVLAQISQDDFAI 319
Cdd:COG5001 261 NRRLFLDRLEQALArarrSGRRLALLFIDLDRFKEIN----DTLGHAAGDEllrevarrLRACLREGDTVARLGGDEFAV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 320 IAHGVKTPEHAVTLTQQLLAALNEPLESPTAAQTGGASIGVAMF-DGRQSASTLYQSAISAALDARRSGINQVAFFgEAS 398
Cdd:COG5001 337 LLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYpDDGADAEELLRNADLAMYRAKAAGRNRYRFF-DPE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 399 VNAQ-------ESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLE 471
Cdd:COG5001 416 MDERarerlelEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLR 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 472 EACQLLARWQAHGIT-LPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVR 550
Cdd:COG5001 496 EACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVR 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 551 IALDDFGMGYSSLSQLQKmkaLPVDSLKIDKSFIDNL---PDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGV 627
Cdd:COG5001 576 IALDDFGTGYSSLSYLKR---LPVDTLKIDRSFVRDLaedPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGC 652
|
650 660
....*....|....*....|..
gi 1126561684 628 TVGQGYLFGKATTPAAFEdAWL 649
Cdd:COG5001 653 DYAQGYLFSRPLPAEELE-ALL 673
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
404-643 |
5.88e-90 |
|
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: 279.43 E-value: 5.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 404 SAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQAH 483
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 484 GITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFGMGYSSL 563
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 564 SQLQKmkaLPVDSLKIDKSFIDNL---PDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKATT 640
Cdd:cd01948 161 SYLKR---LPVDYLKIDRSFVRDIetdPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 1126561684 641 PAA 643
Cdd:cd01948 238 AEE 240
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
403-638 |
3.75e-86 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 269.47 E-value: 3.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 403 ESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQA 482
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 483 HGIT-LPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFGMGYS 561
Cdd:smart00052 81 QGPPpLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 562 SLSQLqkmKALPVDSLKIDKSFIDNL---PDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKA 638
Cdd:smart00052 161 SLSYL---KRLPVDLLKIDKSFVRDLqtdPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
403-638 |
2.81e-67 |
|
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: 219.88 E-value: 2.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 403 ESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQa 482
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 483 HGITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFGMGYSS 562
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126561684 563 LSQLQKmkaLPVDSLKIDKSFIDNLPDDDS---VVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKA 638
Cdd:pfam00563 160 LSYLLR---LPPDFVKIDRSLIADIDKDGEaraIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
243-391 |
3.55e-03 |
|
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: 38.86 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 243 TRFPLTGLPNQALLTALLEQAVA----GGGATALLYVACEPLRESNesqrDALQHARVDK--------LRSVLTPRMVLA 310
Cdd:TIGR00254 3 VRDPLTGLYNRRYLEEMLDSELKrarrFQRSFSVLMIDIDNFKKIN----DTLGHDVGDEvlrevariLQSSVRGSDVVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 311 QISQDDFAIIAHGVKTpEHAVTLTQQLLAALN-EPLESPTAAQ-TGGASIGVAMF--DGRQSAStLYQSAISAALDARRS 386
Cdd:TIGR00254 79 RYGGEEFVVILPGTPL-EDALSKAERLRDAINsKPIEVAGSETlTVTVSIGVACYpgHGLTLEE-LLKRADEALYQAKKA 156
|
....*
gi 1126561684 387 GINQV 391
Cdd:TIGR00254 157 GRNRV 161
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
12-652 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 1128.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 12 MAMVSAVSVFFLFIFSVVLLFHFVQSHRYHTAMQMESIARSVRQPLSAAILKANIPEAEAILREIKPAGVISRADVVLPN 91
Cdd:PRK13561 1 MAMVAAVVLVFVFIFCTVLLFHLVQQNRYNTATQLESIARSVREPLSSAILKADIPEAEAILASIKPAGVVSRADVVLPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 92 QFQALRMRFTPERPIPVTLARVFELPVQISLPLYSLERPANPQPLAYLVLQADSWRLYRFIINAISTLLTTFLLLALILS 171
Cdd:PRK13561 81 QFQALRKSFIPERPVPVMVTRLFELPVQISLPVYSLERPANPQPLAYLVLQADSFRMYKFVMSALSTLVTIYLLLSLILT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 172 VAITWCINRLILHPLRDITRTLNALDAHELAHHQLTIPRLHQDDEIGMLVRTYNRNQQALARQVDEARTSGTRFPLTGLP 251
Cdd:PRK13561 161 VAISWCINRLIVHPLRNIARELNDIPPQELVGHQLALPRLHQDDEIGMLVRSYNLNQQLLQRQYEEQSRNATRFPVSDLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 252 NQALLTALLEQAVAGGGATALLYVACEPLRESN----ESQRDALQHARVDKLRSVLTPRMVLAQISQDDFAIIAHGVKTP 327
Cdd:PRK13561 241 NKALLMALLEQVVARKQTTALMIITCETLRDTAgvlkEAQREILLLTLVEKLKSVLSPRMVLAQISGYDFAIIANGVKEP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 328 EHAVTLTQQLLAALNEPLESPTAAQTGGASIGVAMFDGRQSASTLYQSAISAALDARRSGINQVAFFGEASVNA------ 401
Cdd:PRK13561 321 WHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTARRKGKNQIQFFDPQQMEAaqkrlt 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 402 QESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQ 481
Cdd:PRK13561 401 EESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQ 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 482 AHGITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFGMGYS 561
Cdd:PRK13561 481 ERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 562 SLSQLQKMKALPVDSLKIDKSFIDNLPDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKATTP 641
Cdd:PRK13561 561 GLRQLQHMKSLPIDVLKIDKMFVDGLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPI 640
|
650
....*....|.
gi 1126561684 642 AAFEDAWLPTP 652
Cdd:PRK13561 641 EIFEERYLEEK 651
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
12-645 |
0e+00 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 588.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 12 MAMVSAVSVFFLFIFSVVLLFHFVQSHRYHTAMQMESIARSVRQPLSAAILKANIPEAEAILREIKPAGVISRADVVLPN 91
Cdd:PRK11829 1 MAAVAVVALVTICIFIILQLFHFVQQRKDDYANQLESIAYSVRQPLSEAILSVDIPQAKKILNSLLPIGILSRAEVILPN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 92 QFQALRMRFTPERPIPVTLARVFELPVQISLPLYSLER-PANPQPLAYLVLQADSWRLYRFIINAISTLLTTFLLLALIL 170
Cdd:PRK11829 81 QIQVLHANFPTERPIPHWAKRVFSLPVQITVPLYALERvPANPQPLAHLVLRADSFRMYQFILSALSAMLSTYLLLALVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 171 SVAITWCINRLILHPLRDITRTLNALDAHELAHHQLTIPRLHQDDEIGMLVRTYNRNQQALARQVDEARTSGTRFPLTGL 250
Cdd:PRK11829 161 SVSIAWCINRLIIHPLRAMAKELEDIGDHGVLHHQLTLPAHHQDDELGVLVRNYNRNQQLLADAYADMGRISHRFPVTEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 251 PNQALLTALLEQAVAGGGAT---ALLYVACEPLRES----NESQRDALQHARVDKLRSVLTPRMVLAQISQDDFAIIAHG 323
Cdd:PRK11829 241 PNRSLFISLLEKEIASSTRTdhfHLLVIGIETLQEVsgamSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 324 VKTPEHAVTLTQQLLAALNEPLESPTAAQTGGASIGVAMFDGRQ-SASTLYQSAISAALDARRSGINQVAFFGEASVN-- 400
Cdd:PRK11829 321 TRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQdTAESMMRNASTAMMAAHHEGRNQIMVFEPHLIEkt 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 401 ----AQESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQL 476
Cdd:PRK11829 401 hkrlTQENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRI 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 477 LARWQAHGITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDF 556
Cdd:PRK11829 481 LADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALDDF 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 557 GMGYSSLSQLQKMKALPVDSLKIDKSFIDNLPDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFG 636
Cdd:PRK11829 561 GIGYSSLRYLNHLKSLPIHMIKLDKSFVKNLPEDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFS 640
|
....*....
gi 1126561684 637 KATTPAAFE 645
Cdd:PRK11829 641 PPLPRAEFE 649
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
12-649 |
8.33e-115 |
|
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: 358.70 E-value: 8.33e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 12 MAMVSAVSVFFLFIFSVVLLFHFVQSHRYHTAMQMESIARSVRQPLSAAILKANIPEAEAILREIKPAGVISRADVVLPN 91
Cdd:COG5001 28 LLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 92 QFQALRMRFTPERPIPVTLARVFELPVQISLPLYSLERPANPQPLAYLVLQADSWRLYRFIINAISTLLTTFLLLALILS 171
Cdd:COG5001 108 LLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 172 VAITWCINRLILHPLRDITRTLNALDAHELAHHQLTIPRLHQDDEIGMLVRTYNRNQQALARQvdeARTSgtrfPLTGLP 251
Cdd:COG5001 188 LLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHL---AYHD----PLTGLP 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 252 NQALLTALLEQAVA----GGGATALLYVACEPLRESNesqrDALQHARVDK--------LRSVLTPRMVLAQISQDDFAI 319
Cdd:COG5001 261 NRRLFLDRLEQALArarrSGRRLALLFIDLDRFKEIN----DTLGHAAGDEllrevarrLRACLREGDTVARLGGDEFAV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 320 IAHGVKTPEHAVTLTQQLLAALNEPLESPTAAQTGGASIGVAMF-DGRQSASTLYQSAISAALDARRSGINQVAFFgEAS 398
Cdd:COG5001 337 LLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYpDDGADAEELLRNADLAMYRAKAAGRNRYRFF-DPE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 399 VNAQ-------ESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLE 471
Cdd:COG5001 416 MDERarerlelEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLR 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 472 EACQLLARWQAHGIT-LPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVR 550
Cdd:COG5001 496 EACRQLAAWQDAGLPdLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVR 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 551 IALDDFGMGYSSLSQLQKmkaLPVDSLKIDKSFIDNL---PDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGV 627
Cdd:COG5001 576 IALDDFGTGYSSLSYLKR---LPVDTLKIDRSFVRDLaedPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGC 652
|
650 660
....*....|....*....|..
gi 1126561684 628 TVGQGYLFGKATTPAAFEdAWL 649
Cdd:COG5001 653 DYAQGYLFSRPLPAEELE-ALL 673
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
404-643 |
5.88e-90 |
|
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: 279.43 E-value: 5.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 404 SAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQAH 483
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 484 GITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFGMGYSSL 563
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 564 SQLQKmkaLPVDSLKIDKSFIDNL---PDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKATT 640
Cdd:cd01948 161 SYLKR---LPVDYLKIDRSFVRDIetdPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLP 237
|
...
gi 1126561684 641 PAA 643
Cdd:cd01948 238 AEE 240
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
82-646 |
1.20e-89 |
|
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: 290.15 E-value: 1.20e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 82 ISRADVVLPNQFQALRMRFTPERPIPVTLARVFELPVQISLPLYSLERPANPQPLAYLVLQADSWRLYRFIINAISTLLT 161
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 162 TFLLLALILSVAITWCINRLILHPLRDITRTLNALDAHELAHHQLTIPRLHQDDEIGMLVRTYNRNQQALARQVDEARTS 241
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 242 GTRFPLTGLPNQALLTALLEQAVAGGGATALLYVACEPLRESNESQRDALQHARVDKLRSVLTPR--MVLAQISQDDFAI 319
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARllLALLGGGGGGFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 320 IAHGVKTPEHAVTLTQQLLAALNEPLESPTAAQTGGASIGVAMF-DGRQSASTLYQSAISAALDARRSGINQVAFFGEAS 398
Cdd:COG2200 241 LLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAApDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 399 VNAQ-----ESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEA 473
Cdd:COG2200 321 ARARrrlalESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 474 CQLLARWQAHGITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIAL 553
Cdd:COG2200 401 LRQLARWPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIAL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 554 DDFGMGYSSLSQLQKmkaLPVDSLKIDKSFIDNL---PDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVG 630
Cdd:COG2200 481 DDFGTGYSSLSYLKR---LPPDYLKIDRSFVRDIardPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYA 557
|
570
....*....|....*.
gi 1126561684 631 QGYLFGKATTPAAFED 646
Cdd:COG2200 558 QGYLFGRPLPLEELEA 573
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
403-638 |
3.75e-86 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 269.47 E-value: 3.75e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 403 ESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQA 482
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 483 HGIT-LPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFGMGYS 561
Cdd:smart00052 81 QGPPpLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 562 SLSQLqkmKALPVDSLKIDKSFIDNL---PDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKA 638
Cdd:smart00052 161 SLSYL---KRLPVDLLKIDKSFVRDLqtdPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRP 237
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
403-649 |
2.05e-69 |
|
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: 234.81 E-value: 2.05e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 403 ESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQA 482
Cdd:COG4943 273 RRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDLGDLLA 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 483 HGITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAiAILRPLREAGVRIALDDFGMGYSS 562
Cdd:COG4943 353 ADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPAKAR-AVIAALREAGHRIAIDDFGTGYSS 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 563 LSQLQKmkaLPVDSLKIDKSFIDNLPDDD---SVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKAT 639
Cdd:COG4943 432 LSYLQT---LPVDILKIDKSFVDAIGTDSansAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAKPL 508
|
250
....*....|
gi 1126561684 640 TPAAFEdAWL 649
Cdd:COG4943 509 PAEEFI-AWL 517
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
403-638 |
2.81e-67 |
|
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: 219.88 E-value: 2.81e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 403 ESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQa 482
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 483 HGITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFGMGYSS 562
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126561684 563 LSQLQKmkaLPVDSLKIDKSFIDNLPDDDS---VVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKA 638
Cdd:pfam00563 160 LSYLLR---LPPDFVKIDRSLIADIDKDGEaraIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
246-649 |
3.30e-64 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 224.18 E-value: 3.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 246 PLTGLPNQALLTALLEQAV--AGGGATALLYVACEPLRESNesqrDALQHARVDKL--------RSVLTPRMVLAQISQD 315
Cdd:PRK10060 241 SITGLPNRNAIQELIDHAInaADNNQVGIVYLDLDNFKKVN----DAYGHMFGDQLlqdvslaiLSCLEEDQTLARLGGD 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 316 DFAIIAHgvKTPEHAV-TLTQQLLAALNEPLESPTAAQTGGASIGVAMFDGR-QSASTLYQSAISAALDARRSGINQVAF 393
Cdd:PRK10060 317 EFLVLAS--HTSQAALeAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHgDDSESLIRSADTAMYTAKEGGRGQFCV 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 394 FGEaSVNAQ-------ESAMQNALARRQYAIWLQPQVDMRnGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVG 466
Cdd:PRK10060 395 FSP-EMNQRvfeylwlDTNLRKALENDQLVIHYQPKITWR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLG 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 467 DWVLEEACQLLARWQAHGITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLRE 546
Cdd:PRK10060 473 RWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQ 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 547 AGVRIALDDFGMGYSSLSQLQKmkaLPVDSLKIDKSFIDNL---PDDDSVVSAIISMAKKLNLELVAEGIQNESQRDWLL 623
Cdd:PRK10060 553 LGAQVHLDDFGTGYSSLSQLAR---FPIDAIKLDQSFVRDIhkqPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLT 629
|
410 420
....*....|....*....|....*.
gi 1126561684 624 NAGVTVGQGYLFGKATTPAAFEdAWL 649
Cdd:PRK10060 630 KNGVNERQGFLFAKPMPAVAFE-RWY 654
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
246-651 |
9.79e-57 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 205.77 E-value: 9.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 246 PLTGLPNQALLTALLEQAVAGGGATALLYVACEPLRESNESqrdaLQHARVD--------KLRSVLTPRMVLAQISQDDF 317
Cdd:PRK11359 380 PLTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHFQDVIDS----LGYAWADqallevvnRFREKLKPDQYLCRIEGTQF 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 318 AIIAHGVKTPEhAVTLTQQLLAALNEPLESPTAAQTGGASIGVAmFDGRQSASTLYQSAISAALDARRSGINQVAFFGEA 397
Cdd:PRK11359 456 VLVSLENDVSN-ITQIADELRNVVSKPIMIDDKPFPLTLSIGIS-YDVGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPA 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 398 -SVNAQE-----SAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLE 471
Cdd:PRK11359 534 mNEMVKErlvlgAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIA 613
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 472 EACQLLARWQAHGITLP-LSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIAILRPLREAGVR 550
Cdd:PRK11359 614 EACRQLAEWRSQNIHIPaLSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVG 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 551 IALDDFGMGYSSLSQLqkmKALPVDSLKIDKSFIDNLPDDD---SVVSAIISMAKKLNLELVAEGIQNESQRDWLLNAGV 627
Cdd:PRK11359 694 LSVDDFGTGFSGLSRL---VSLPVTEIKIDKSFVDRCLTEKrilALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHC 770
|
410 420
....*....|....*....|....
gi 1126561684 628 TVGQGYLFGKAtTPAAFEDAWLPT 651
Cdd:PRK11359 771 RVIQGYFFSRP-LPAEEIPGWMSS 793
|
|
| GAPES3 |
pfam17154 |
Gammaproteobacterial periplasmic sensor domain; GAPES3 (GAmmaproteobacterial PEriplasmic ... |
36-155 |
4.83e-51 |
|
Gammaproteobacterial periplasmic sensor domain; GAPES3 (GAmmaproteobacterial PEriplasmic Sensor) domain is a periplasmic sensor domain found in diguanylate cyclases/phosphodiesterases, including the c-di-GMP phosphodiesterases PdeK (YhjK) of Escherichia coli and HmsP of Yersinia pestis.
Pssm-ID: 435753 [Multi-domain] Cd Length: 121 Bit Score: 172.62 E-value: 4.83e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 36 QSHRYHTAMQMESIARSVRQPLSAAILKANIPEAEAILREIKPAGVISRADVVLPNQFQALRMRFTPERPIPVTLARVFE 115
Cdd:pfam17154 1 QQRKDDYANQLENIAVSVRAPLTEALLSSDLNEAKSILITLRPSGILGRADVVLPNQIQVLHLNFATERPIPELAKRVFG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1126561684 116 LPVQISLPLYSLER-PANPQPLAYLVLQADSWRLYRFIINA 155
Cdd:pfam17154 81 LPVEISVPLYSYGVsPTNPQPLAHLVLQADSNRMYRFIIST 121
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
247-638 |
1.20e-35 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 144.43 E-value: 1.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 247 LTGLPNQAL----LTALLEQAVAGGGATALLYVACEPLRESNESQR----DALQHARVDKLRSVLTPRMVLAQISQDDFA 318
Cdd:PRK09776 670 LTHLANRASfekqLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGhaagDALLRELASLMLSMLRSSDVLARLGGDEFG 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 319 IIAHGVkTPEHAVTLTQQLLAALNE---PLESptAAQTGGASIGVAMFDG--RQSASTLYQSAIsAALDARRSGINQVAF 393
Cdd:PRK09776 750 LLLPDC-NVESARFIATRIISAINDyhfPWEG--RVYRVGASAGITLIDAnnHQASEVMSQADI-ACYAAKNAGRGRVTV 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 394 F-----------GEASVNAQESAMQNALARRQYAIWLQPQVDMRNGNIvgaEALLRERQPDGDWTLPVGFIDNIESSGLI 462
Cdd:PRK09776 826 YepqqaaahsehRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHW---LISLRLWDPEGEIIDEGAFRPAAEDPALM 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 463 VTVGDWVLEEAC-QLLARWQAHGIT--LPLSVNvsslQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAIA 539
Cdd:PRK09776 903 HALDRRVIHEFFrQAAKAVASKGLSiaLPLSVA----GLSSPTLLPFLLEQLENSPLPPRLLHLEITETALLNHAESASR 978
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 540 ILRPLREAGVRIALDDFGMGYSSLSQLqkmKALPVDSLKIDKSFIDNLPD---DDSVVSAIISMAKKLNLELVAEGIQNE 616
Cdd:PRK09776 979 LVQKLRLAGCRVVLSDFGRGLSSFNYL---KAFMADYLKLDGELVANLHGnlmDEMLISIIQGHAQRLGMKTIAGPVELP 1055
|
410 420
....*....|....*....|..
gi 1126561684 617 SQRDWLLNAGVTVGQGYLFGKA 638
Cdd:PRK09776 1056 LVLDTLSGIGVDLAYGYAIARP 1077
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
409-652 |
6.61e-31 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 127.03 E-value: 6.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 409 ALARRQYAIWLQPQVDMRNGNIVGAEALLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEeacqLLARwQAHGI--T 486
Cdd:PRK10551 271 GIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTAGEIPPDAFINYAEAQKLIVPLTQHLFE----LIAR-DAAELqkV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 487 LP----LSVNVSSLQLLTRDLVQTMLQRLERYAIAPGTLVLEMTESQRIDDTEAAiAILRPLREAGVRIALDDFGMGYSS 562
Cdd:PRK10551 346 LPvgakLGINISPAHLHSDSFKADVQRLLASLPADHFQIVLEITERDMVQEEEAT-KLFAWLHSQGIEIAIDDFGTGHSA 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 563 LSQLQKMKalpVDSLKIDKSFIDNLpDDDSVVS----AIISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKA 638
Cdd:PRK10551 425 LIYLERFT---LDYLKIDRGFIQAI-GTETVTSpvldAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRP 500
|
250
....*....|....
gi 1126561684 639 TTPAAFEdAWLPTP 652
Cdd:PRK10551 501 LPLEDFV-RWLKEP 513
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
244-394 |
1.07e-18 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 83.45 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 244 RFPLTGLPNQALLTALLEQAVA----GGGATALLYVACEPLRESN----ESQRDALQHARVDKLRSVLTPRMVLAQISQD 315
Cdd:smart00267 5 RDPLTGLPNRRYFEEELEQELQraqrQGSPFALLLIDLDNFKDINdtygHAVGDELLQEVAQRLSSCLRPGDLLARLGGD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 316 DFAIIAHGVkTPEHAVTLTQQLLAALNEPLESPTAAQTGGASIGVAMF-DGRQSASTLYQSAISAALDARRSGINQVAFF 394
Cdd:smart00267 85 EFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYpNPGEDAEDLLKRADTALYQAKKAGRNQVAVY 163
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
134-394 |
3.05e-16 |
|
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: 79.25 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 134 QPLAYLVLQADSWRLYRFIINAISTLLTTFLLLALILSVAITWCINRLILHPLRDITRTLNALDAHELAHHQLTIPRLHQ 213
Cdd:COG2199 7 LLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 214 DDEIGMLVRTYnRNQQALARQVDEARTSGTRFPLTGLPNQALLTALLEQAVA----GGGATALLYVACEPLRESNESQ-- 287
Cdd:COG2199 87 LLALLLLLLAL-EDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELArarrEGRPLALLLIDLDHFKRINDTYgh 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 288 ---RDALQHArVDKLRSVLTPRMVLAQISQDDFAIIAHGVkTPEHAVTLTQQLLAALNE-PLESPTAAQTGGASIGVAMF 363
Cdd:COG2199 166 aagDEVLKEV-ARRLRASLRESDLVARLGGDEFAVLLPGT-DLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALY 243
|
250 260 270
....*....|....*....|....*....|..
gi 1126561684 364 DGR-QSASTLYQSAISAALDARRSGINQVAFF 394
Cdd:COG2199 244 PEDgDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
246-392 |
8.25e-12 |
|
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: 63.73 E-value: 8.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 246 PLTGLPN----QALLTALLEQAVAGGGATALLYVACEPLRESNesqrDALQHARVDK--------LRSVLTPRMVLAQIS 313
Cdd:cd01949 4 PLTGLPNrrafEERLERLLARARRSGRPLALLLIDIDHFKQIN----DTYGHAAGDEvlkevaerLRSSLRESDLVARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 314 QDDFAIIAHGVkTPEHAVTLTQQLLAALNEPLESPTAAQTGGASIGVAMF-DGRQSASTLYQSAISAALDARRSGINQVA 392
Cdd:cd01949 80 GDEFAILLPGT-DLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYpEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
231-636 |
8.15e-11 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 64.88 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 231 LARQVDEARTSGTRF-----------PLTGLPNQAL----LTALLE--QAVAGGGATALLYVA-CEPLRES-NESQRDAL 291
Cdd:PRK11059 206 LLSELQDAREERSRFdtfirsnafqdAKTGLGNRLFfdnqLATLLEdqEMVGAHGVVMLIRLPdFDLLQEEwGESQVEEL 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 292 QHARVDKLRSVLT--PRMVLAQISQDDFAI-IAHgvKTPEHAVTLTQQLLAAL-----NEPLESPTAAQtggasIGVAMF 363
Cdd:PRK11059 286 LFELINLLSTFVMryPGALLARYSRSDFAVlLPH--RSLKEADSLASQLLKAVdalppPKMLDRDDFLH-----IGICAY 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 364 DGRQSASTLYQSAISAALDARRSGIN--------QVAFFGEASVNAQeSAMQNALARRQYAIWLQPQVDmRNGNIVGAEA 435
Cdd:PRK11059 359 RSGQSTEQVMEEAEMALRSAQLQGGNgwfvydkaQLPEKGRGSVRWR-TLLEQTLVRGGPRLYQQPAVT-RDGKVHHREL 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 436 LLRERQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQAHgitlPLSVNVSSLQLLTRDLVQ----TMLQ-- 509
Cdd:PRK11059 437 FCRIRDGQGELLSAELFMPMVQQLGLSEQYDRQVIERVLPLLRYWPEE----NLSINLSVDSLLSRAFQRwlrdTLLQcp 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 510 RLERYAIapgtlVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFGMGYSSLSQLqkmKALPVDSLKIDKSF---IDN 586
Cdd:PRK11059 513 RSQRKRL-----IFELAEADVCQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYI---KELNVELIKLHPSLvrnIHK 584
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1126561684 587 LPDDDSVVSAIISMAKKLNLELVAEGIqnESQRDW--LLNAGVTVGQGYLFG 636
Cdd:PRK11059 585 RTENQLFVRSLVGACAGTETQVFATGV--ESREEWqtLQELGVSGGQGDFFA 634
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
518-640 |
2.29e-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: 62.90 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 518 PGTLVLEMTESqrIDDTEAAIAILRPLREAGVRIALDDFGMGYSSLSQLQKmkalpVDSLKIDksfIDNLPDDDsvVSAI 597
Cdd:COG3434 83 PERVVLEILED--VEPDEELLEALKELKEKGYRIALDDFVLDPEWDPLLPL-----ADIIKID---VLALDLEE--LAEL 150
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1126561684 598 ISMAKKLNLELVAEGIQNESQRDWLLNAGVTVGQGYLFGKATT 640
Cdd:COG3434 151 VARLKRYGIKLLAEKVETREEFELCKELGFDLFQGYFFSKPEI 193
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
246-390 |
1.20e-07 |
|
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: 51.48 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 246 PLTGLPNQAL----LTALLEQAVAGGGATALLYVACEPLRESNesqrDALQHARVDK--------LRSVLTPRMVLAQIS 313
Cdd:pfam00990 5 PLTGLPNRRYfeeqLEQELQRALREGSPVAVLLIDLDNFKRIN----DTYGHSVGDEvlqevaqrLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 314 QDDFAIIAHGVKTPE--HAVTLTQQLLAALNEPLESPTAAQTGGASIGVAMF-DGRQSASTLYQSAISAALDARRSGINQ 390
Cdd:pfam00990 81 GDEFAILLPETSLEGaqELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYpNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
120-557 |
8.63e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 42.55 E-value: 8.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 120 ISLPLYSLERPANPQPLAYLVLQADSWRLYRFIINAISTLLTTFLLLALILSVAITWCINRLILHPLRDITRTLNALDAH 199
Cdd:COG3321 861 VPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAA 940
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 200 ELAHHQLTIPRLHQDDEIGmLVRTYNRNQQALARQVDEARTSGTRFPLTGLPNQALLTALLEQAVAGGGATALLYVACEP 279
Cdd:COG3321 941 ALLALAAAAAAAAAALAAA-EAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAA 1019
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 280 LRESNESQRDALQHARVDklrSVLTPRMVLAQISQDDFAIIAHGVKTPEHAVTLTQQLLAALNEPLESPTAAQTGGASIG 359
Cdd:COG3321 1020 ALLALAALLAAAAAALAA---AAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAALA 1096
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 360 VAMFDGRQSASTLYQSAISAALDARRSGINQVAFFGEASVNAQESAMQNALARRQYAIWLQPQVDMRNGNIVGAEALLRE 439
Cdd:COG3321 1097 LALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLA 1176
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 440 RQPDGDWTLPVGFIDNIESSGLIVTVGDWVLEEACQLLARWQAHGITLPLSVNVSSLQLLTRDLVQTMLQRLERYAIAPG 519
Cdd:COG3321 1177 LALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALL 1256
|
410 420 430
....*....|....*....|....*....|....*...
gi 1126561684 520 TLVLEMTESQRIDDTEAAIAILRPLREAGVRIALDDFG 557
Cdd:COG3321 1257 AALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAA 1294
|
|
| HAMP |
pfam00672 |
HAMP domain; |
178-231 |
9.17e-04 |
|
HAMP domain;
Pssm-ID: 459898 [Multi-domain] Cd Length: 53 Bit Score: 37.60 E-value: 9.17e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1126561684 178 INRLILHPLRDITRTLNALDAHELAHHqltiPRLHQDDEIGMLVRTYNRNQQAL 231
Cdd:pfam00672 2 LARRILRPLRRLAEAARRIASGDLDVR----LPVSGRDEIGELARAFNQMAERL 51
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
243-391 |
3.55e-03 |
|
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: 38.86 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 243 TRFPLTGLPNQALLTALLEQAVA----GGGATALLYVACEPLRESNesqrDALQHARVDK--------LRSVLTPRMVLA 310
Cdd:TIGR00254 3 VRDPLTGLYNRRYLEEMLDSELKrarrFQRSFSVLMIDIDNFKKIN----DTLGHDVGDEvlrevariLQSSVRGSDVVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126561684 311 QISQDDFAIIAHGVKTpEHAVTLTQQLLAALN-EPLESPTAAQ-TGGASIGVAMF--DGRQSAStLYQSAISAALDARRS 386
Cdd:TIGR00254 79 RYGGEEFVVILPGTPL-EDALSKAERLRDAINsKPIEVAGSETlTVTVSIGVACYpgHGLTLEE-LLKRADEALYQAKKA 156
|
....*
gi 1126561684 387 GINQV 391
Cdd:TIGR00254 157 GRNRV 161
|
|
| |
