|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
42-698 |
5.49e-137 |
|
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: 418.02 E-value: 5.49e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 42 WCFFEQERSAMANAYWQQAMALLPAEQSDNWMNWLHPEDRAQTRDAWQKAILQHNVFRHNLRLAVKEGDYRWFVAYSYTV 121
Cdd:COG5001 16 LALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 122 PGVGCRMVTFFEADQLQEDNVKAYAnwQTSKSMLDASIDCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLLPPE 201
Cdd:COG5001 96 LLALLVLLLLLLLLLALLALLAALL--ARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 202 IEGP------GREALKQAVDGHNARFFGKSESGSGQTLFWDNILTPVKTASGDVSSILCVSRDITDLHLAEQRFKYISEH 275
Cdd:COG5001 174 LLLLlllllaLLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 276 DELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGDE 355
Cdd:COG5001 254 DPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 356 FAAVLPGIETTQALLAVGKQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGRGGICCYE 435
Cdd:COG5001 334 FAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 436 PAMGGQVdklHSQMELAKEI---ISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGHIWAAFENYVLVERIG 512
Cdd:COG5001 414 PEMDERA---RERLELEADLrraLERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLG 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 513 YLIRDKVFADIRQWINQSLDVVPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEHMFDGRGAcYVFRALNLL 592
Cdd:COG5001 491 EWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPE-EALETLRAL 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 593 KSEGVRISLDDFGTGYSALANIRDYPVDVIKVDRTFVDSLSKGKE---------------GlavvkallllateleLDVV 657
Cdd:COG5001 570 RALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDdaaivraiialahslG---------------LEVV 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1770577378 658 AEGVEYTEQRESLLNEGYQLGQGFLFSAAVPAVTISRFLNN 698
Cdd:COG5001 635 AEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
242-705 |
1.26e-61 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 218.40 E-value: 1.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 242 VKTASG-DVSSILCVSRDITDLHLAEQRFKYISEHDELTGLPNRRMFNATLKHYLQPATPAAPGlaVIVIDLDYFKLVND 320
Cdd:PRK10060 205 VHSGSGkNEIFLICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVG--IVYLDLDNFKKVND 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 321 TLGHPAGDFLLETVAQRLQRAMPENAFIARIGGDEFAAVLPgiETTQALLAVGKQLIadttvpLSYQSQAIHISL----- 395
Cdd:PRK10060 283 AYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLAS--HTSQAALEAMASRI------LTRLRLPFRIGLievyt 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 396 --SIGGALWPLQATDSTSMIKAADIALNELKRSGRGGICCYEPAMGGQVDK---LHSQMELAKEiisEDAIFPYYQPKVR 470
Cdd:PRK10060 355 gcSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEylwLDTNLRKALE---NDQLVIHYQPKIT 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 471 LSdGKIMGMEALMRFFNRKGELCFPGHIWAAFENYVLVERIGYLIRDKVFADIRQWINQSLDVvPVSVNASPvefmRDNY 550
Cdd:PRK10060 432 WR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINL-RVAVNVSA----RQLA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 551 GETVLRQIRQ----YNLPPELVEIEITEHMF--DGRGACYVFRALNLLkseGVRISLDDFGTGYSALANIRDYPVDVIKV 624
Cdd:PRK10060 506 DQTIFTALKQalqeLNFEYCPIDVELTESCLieNEELALSVIQQFSQL---GAQVHLDDFGTGYSSLSQLARFPIDAIKL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 625 DRTFVDSLSKGKEGLAVVKALLLLATELELDVVAEGVEYTEQRESLLNEGYQLGQGFLFSAAVPAVTISRFLNNLERHKL 704
Cdd:PRK10060 583 DQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYLKRKL 662
|
.
gi 1770577378 705 L 705
Cdd:PRK10060 663 I 663
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
454-689 |
2.36e-60 |
|
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: 202.78 E-value: 2.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 454 EIISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGHIWAAFENYVLVERIGYLIRDKVFADIRQWINQSLDV 533
Cdd:cd01948 5 RALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGPDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 534 vPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEHMFDGRGAcYVFRALNLLKSEGVRISLDDFGTGYSALAN 613
Cdd:cd01948 85 -RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLE-EALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770577378 614 IRDYPVDVIKVDRTFVDSLSKGKEGLAVVKALLLLATELELDVVAEGVEYTEQRESLLNEGYQLGQGFLFSAAVPA 689
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
449-689 |
9.87e-51 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 176.64 E-value: 9.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 449 MELAKEIISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGHIWAAFENYVLVERIGYLIRDKVFADIRQWIN 528
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 529 QSLDVVPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEHMFDGRgACYVFRALNLLKSEGVRISLDDFGTGY 608
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDD-DESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 609 SALANIRDYPVDVIKVDRTFVDSLSKGKEGLAVVKALLLLATELELDVVAEGVEYTEQRESLLNEGYQLGQGFLFSAAVP 688
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
.
gi 1770577378 689 A 689
Cdd:smart00052 240 L 240
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
275-429 |
8.30e-48 |
|
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: 165.89 E-value: 8.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 275 HDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGD 354
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770577378 355 EFAAVLPGI--ETTQALLAVGKQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGRG 429
Cdd:pfam00990 83 EFAILLPETslEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
275-431 |
3.27e-36 |
|
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: 134.00 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 275 HDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGD 354
Cdd:TIGR00254 4 RDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770577378 355 EFAAVLPGIETTQALLAVG--KQLIADTTVPLSyQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGRGGI 431
Cdd:TIGR00254 84 EFVVILPGTPLEDALSKAErlRDAINSKPIEVA-GSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
262-428 |
6.11e-14 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 74.99 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 262 LHLAEQRF-KYIS---EH--DELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVA 335
Cdd:NF040885 324 LHLVRMHFrLYHNvsrENisDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 336 QRLQRAMPENAFIARIGGDEFAAVLpgIETTQALLAVGKQLIAdttvplsyQSQAIH-----ISLSIGGalWPLQATDS- 409
Cdd:NF040885 404 QAISASIRKSDYGIRLGGDEFCIIL--IDYEEAEAQNLIERIR--------QHLRTIdpdkrVSFSWGA--YQMQPGDTl 471
|
170
....*....|....*....
gi 1770577378 410 TSMIKAADIALNELKRSGR 428
Cdd:NF040885 472 DDAYKAADERLYLNKKQKH 490
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
42-698 |
5.49e-137 |
|
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: 418.02 E-value: 5.49e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 42 WCFFEQERSAMANAYWQQAMALLPAEQSDNWMNWLHPEDRAQTRDAWQKAILQHNVFRHNLRLAVKEGDYRWFVAYSYTV 121
Cdd:COG5001 16 LALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 122 PGVGCRMVTFFEADQLQEDNVKAYAnwQTSKSMLDASIDCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLLPPE 201
Cdd:COG5001 96 LLALLVLLLLLLLLLALLALLAALL--ARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 202 IEGP------GREALKQAVDGHNARFFGKSESGSGQTLFWDNILTPVKTASGDVSSILCVSRDITDLHLAEQRFKYISEH 275
Cdd:COG5001 174 LLLLlllllaLLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 276 DELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGDE 355
Cdd:COG5001 254 DPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 356 FAAVLPGIETTQALLAVGKQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGRGGICCYE 435
Cdd:COG5001 334 FAVLLPDLDDPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 436 PAMGGQVdklHSQMELAKEI---ISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGHIWAAFENYVLVERIG 512
Cdd:COG5001 414 PEMDERA---RERLELEADLrraLERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLG 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 513 YLIRDKVFADIRQWINQSLDVVPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEHMFDGRGAcYVFRALNLL 592
Cdd:COG5001 491 EWVLREACRQLAAWQDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPE-EALETLRAL 569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 593 KSEGVRISLDDFGTGYSALANIRDYPVDVIKVDRTFVDSLSKGKE---------------GlavvkallllateleLDVV 657
Cdd:COG5001 570 RALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFVRDLAEDPDdaaivraiialahslG---------------LEVV 634
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1770577378 658 AEGVEYTEQRESLLNEGYQLGQGFLFSAAVPAVTISRFLNN 698
Cdd:COG5001 635 AEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELEALLRA 675
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
180-697 |
2.25e-77 |
|
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: 258.95 E-value: 2.25e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 180 QALGVSAASGFGMEWLKLLPPEIEGPGREALKQAVDGHNARFFGKSESGSGQTLFWDNILTPVKTASGDVSSILCVSRDI 259
Cdd:COG2200 61 ALALLLLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 260 TDLHLAEQRFKYISEHDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQ 339
Cdd:COG2200 141 LELLLALLLLALLALLDLLLLLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 340 RAMPENAFIARIGG-DEFAAVLPGIETTQALLAVGKQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADI 418
Cdd:COG2200 221 LLLARLLLALLGGGgGGFLLLLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAA 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 419 ALNELKRSGRGGICCYEPAMggqvDKLHSQMELAKEI---ISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFP 495
Cdd:COG2200 301 AAAAAAGGGRGRVVFFAAAE----ARARRRLALESELreaLEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISP 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 496 GHIWAAFENYVLVERIGYLIRDKVFADIRQWINQSLDVvPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEH 575
Cdd:COG2200 377 AEFIPAAERSGLIVELDRWVLERALRQLARWPERGLDL-RLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITES 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 576 MFDGRGAcYVFRALNLLKSEGVRISLDDFGTGYSALANIRDYPVDVIKVDRTFVDSLSKGKEGLAVVKALLLLATELELD 655
Cdd:COG2200 456 ALLEDLE-AAIELLARLRALGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLK 534
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1770577378 656 VVAEGVEYTEQRESLLNEGYQLGQGFLFSAAVPAVTISRFLN 697
Cdd:COG2200 535 VVAEGVETEEQLEALRELGCDYAQGYLFGRPLPLEELEALLR 576
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
242-705 |
1.26e-61 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 218.40 E-value: 1.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 242 VKTASG-DVSSILCVSRDITDLHLAEQRFKYISEHDELTGLPNRRMFNATLKHYLQPATPAAPGlaVIVIDLDYFKLVND 320
Cdd:PRK10060 205 VHSGSGkNEIFLICSGTDITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQVG--IVYLDLDNFKKVND 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 321 TLGHPAGDFLLETVAQRLQRAMPENAFIARIGGDEFAAVLPgiETTQALLAVGKQLIadttvpLSYQSQAIHISL----- 395
Cdd:PRK10060 283 AYGHMFGDQLLQDVSLAILSCLEEDQTLARLGGDEFLVLAS--HTSQAALEAMASRI------LTRLRLPFRIGLievyt 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 396 --SIGGALWPLQATDSTSMIKAADIALNELKRSGRGGICCYEPAMGGQVDK---LHSQMELAKEiisEDAIFPYYQPKVR 470
Cdd:PRK10060 355 gcSIGIALAPEHGDDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFEylwLDTNLRKALE---NDQLVIHYQPKIT 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 471 LSdGKIMGMEALMRFFNRKGELCFPGHIWAAFENYVLVERIGYLIRDKVFADIRQWINQSLDVvPVSVNASPvefmRDNY 550
Cdd:PRK10060 432 WR-GEVRSLEALVRWQSPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINL-RVAVNVSA----RQLA 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 551 GETVLRQIRQ----YNLPPELVEIEITEHMF--DGRGACYVFRALNLLkseGVRISLDDFGTGYSALANIRDYPVDVIKV 624
Cdd:PRK10060 506 DQTIFTALKQalqeLNFEYCPIDVELTESCLieNEELALSVIQQFSQL---GAQVHLDDFGTGYSSLSQLARFPIDAIKL 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 625 DRTFVDSLSKGKEGLAVVKALLLLATELELDVVAEGVEYTEQRESLLNEGYQLGQGFLFSAAVPAVTISRFLNNLERHKL 704
Cdd:PRK10060 583 DQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMPAVAFERWYKRYLKRKL 662
|
.
gi 1770577378 705 L 705
Cdd:PRK10060 663 I 663
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
454-689 |
2.36e-60 |
|
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: 202.78 E-value: 2.36e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 454 EIISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGHIWAAFENYVLVERIGYLIRDKVFADIRQWINQSLDV 533
Cdd:cd01948 5 RALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAGGPDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 534 vPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEHMFDGRGAcYVFRALNLLKSEGVRISLDDFGTGYSALAN 613
Cdd:cd01948 85 -RLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLE-EALATLRRLRALGVRIALDDFGTGYSSLSY 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770577378 614 IRDYPVDVIKVDRTFVDSLSKGKEGLAVVKALLLLATELELDVVAEGVEYTEQRESLLNEGYQLGQGFLFSAAVPA 689
Cdd:cd01948 163 LKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPA 238
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
267-697 |
1.62e-59 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 214.63 E-value: 1.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 267 QRFKYISEHDELTGLPNRRMFNATLKHYLQPATPaapgLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENA 346
Cdd:PRK11359 370 QHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAVS----PVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFREKLKPDQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 347 FIARIGGDEFAAVLPGIETTQA------LLAVGKQ--LIADTTVPLSYqsqAIHISLSIGGalwplqatDSTSMIKAADI 418
Cdd:PRK11359 446 YLCRIEGTQFVLVSLENDVSNItqiadeLRNVVSKpiMIDDKPFPLTL---SIGISYDVGK--------NRDYLLSTAHN 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 419 ALNELKRSGRGGICCYEPAMGGQV-DKLHSQMELaKEIISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGH 497
Cdd:PRK11359 515 AMDYIRKNGGNGWQFFSPAMNEMVkERLVLGAAL-KEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSR 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 498 IWAAFENYVLVERIGYLIRDKVFADIRQWINQSLDVVPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEHMF 577
Cdd:PRK11359 594 FIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMM 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 578 DGRGAcYVFRALNLLKSEGVRISLDDFGTGYSALANIRDYPVDVIKVDRTFVDSLSKGKEGLAVVKALLLLATELELDVV 657
Cdd:PRK11359 674 MEHDT-EIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVV 752
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1770577378 658 AEGVEYTEQRESLLNEGYQLGQGFLFSAAVPAVTISRFLN 697
Cdd:PRK11359 753 AEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMS 792
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
252-434 |
1.44e-56 |
|
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: 194.04 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 252 ILCVSRDITDLHLAEQRFKYISEHDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLL 331
Cdd:COG2199 93 LLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAGDEVL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 332 ETVAQRLQRAMPENAFIARIGGDEFAAVLPGIETTQAlLAVGKQLIAD-TTVPLSYQSQAIHISLSIGGALWPLQATDST 410
Cdd:COG2199 173 KEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEA-EALAERLREAlEQLPFELEGKELRVTVSIGVALYPEDGDSAE 251
|
170 180
....*....|....*....|....
gi 1770577378 411 SMIKAADIALNELKRSGRGGICCY 434
Cdd:COG2199 252 ELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
275-432 |
6.33e-54 |
|
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: 182.37 E-value: 6.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 275 HDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGD 354
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770577378 355 EFAAVLPGIETTQAlLAVGKQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGRGGIC 432
Cdd:cd01949 82 EFAILLPGTDLEEA-EALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
449-689 |
9.87e-51 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 176.64 E-value: 9.87e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 449 MELAKEIISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGHIWAAFENYVLVERIGYLIRDKVFADIRQWIN 528
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 529 QSLDVVPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEHMFDGRgACYVFRALNLLKSEGVRISLDDFGTGY 608
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDD-DESAVATLQRLRELGVRIALDDFGTGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 609 SALANIRDYPVDVIKVDRTFVDSLSKGKEGLAVVKALLLLATELELDVVAEGVEYTEQRESLLNEGYQLGQGFLFSAAVP 688
Cdd:smart00052 160 SSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLP 239
|
.
gi 1770577378 689 A 689
Cdd:smart00052 240 L 240
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
275-429 |
8.30e-48 |
|
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: 165.89 E-value: 8.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 275 HDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGD 354
Cdd:pfam00990 3 HDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770577378 355 EFAAVLPGI--ETTQALLAVGKQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGRG 429
Cdd:pfam00990 83 EFAILLPETslEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
72-634 |
1.43e-47 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 181.79 E-value: 1.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 72 WMNWLHPEDRAQTRDAWQKAILQHNVFRHNLRLAVKEGdYRWFVAYSYTVPG--------VGCRM-VTffEADQLQEdnv 142
Cdd:PRK09776 456 WYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNkdgeverlLGINMdMT--EVRQLNE--- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 143 kayANWQTSKSM---LDASIDCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLL--PPEIEGPGREALKQAVDGH 217
Cdd:PRK09776 530 ---ALFQEKERLhitLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALGVPLLTVLhiTFGDNGPLMENIYSCLTSR 606
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 218 NARFFGKS---ESGSGQTLFWDNILTPVKTASGDVSSILCVSRDITDLHLAEQRFKYISEHDELTGLPNRRMFNATLKHY 294
Cdd:PRK09776 607 SAAYLEQDvvlHCRSGGSYDVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRL 686
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 295 LQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAqRLQRAMPENA-FIARIGGDEFAAVLPGIETTQALLAVG 373
Cdd:PRK09776 687 LQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELA-SLMLSMLRSSdVLARLGGDEFGLLLPDCNVESARFIAT 765
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 374 KQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGRGGICCYEPAMgGQVDKLHSQMELAK 453
Cdd:PRK09776 766 RIISAINDYHFPWEGRVYRVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQ-AAAHSEHRALSLAE 844
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 454 EI--ISEDAIF----PYYQPKVRLSDGKImgmEALMRFFNRKGELCFPGHIWAAFENYVLVERIGYLIRDKVFADIRQWI 527
Cdd:PRK09776 845 QWrmIKENQLMmlahGVASPRIPEARNHW---LISLRLWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAV 921
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 528 NQ-SLDV-VPVSVNASPVEFMRDNygetVLRQIRQYNLPPELVEIEITEH--MFDGRGACyvfRALNLLKSEGVRISLDD 603
Cdd:PRK09776 922 ASkGLSIaLPLSVAGLSSPTLLPF----LLEQLENSPLPPRLLHLEITETalLNHAESAS---RLVQKLRLAGCRVVLSD 994
|
570 580 590
....*....|....*....|....*....|.
gi 1770577378 604 FGTGYSALANIRDYPVDVIKVDRTFVDSLSK 634
Cdd:PRK09776 995 FGRGLSSFNYLKAFMADYLKLDGELVANLHG 1025
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
271-434 |
3.34e-46 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 161.65 E-value: 3.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 271 YISEHDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIAR 350
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 351 IGGDEFAAVLPGIeTTQALLAVGKQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGRGG 430
Cdd:smart00267 81 LGGDEFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 1770577378 431 ICCY 434
Cdd:smart00267 160 VAVY 163
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
278-689 |
1.47e-44 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 169.89 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 278 LTGLPNRRMFNATLKHYLqpATPAAPGLAVIVID--LDYFKLVNDTlghpAGDFLLETVAQRLQRAMPENAFIARIGGDE 355
Cdd:PRK13561 236 VSDLPNKALLMALLEQVV--ARKQTTALMIITCEtlRDTAGVLKEA----QREILLLTLVEKLKSVLSPRMVLAQISGYD 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 356 FAAVLPGIETTQALLAVGKQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNElKRSGRGGICCYE 435
Cdd:PRK13561 310 FAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAMFYGDLTAEQLYSRAISAAFTA-RRKGKNQIQFFD 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 436 PAmggqvdklhsQMELA-KEIISEDAIFP---------YYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGHIWAAFENY 505
Cdd:PRK13561 389 PQ----------QMEAAqKRLTEESDILNalenhqfaiWLQPQVEMRSGKLVSAEALLRMQQPDGSWDLPEGLIDRIESC 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 506 VLVERIGYLIRDKVFADIRQWINQSLDVvPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITE--HMFDGRGAC 583
Cdd:PRK13561 459 GLMVTVGHWVLEESCRLLAAWQERGIML-PLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTEsrRIDDPHAAV 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 584 YVFRALnllKSEGVRISLDDFGTGYSALANIRDY---PVDVIKVDRTFVDSLSkgkEGLAVVKALLLLATELELDVVAEG 660
Cdd:PRK13561 538 AILRPL---RNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGLP---EDDSMVAAIIMLAQSLNLQVIAEG 611
|
410 420
....*....|....*....|....*....
gi 1770577378 661 VEYTEQRESLLNEGYQLGQGFLFSAAVPA 689
Cdd:PRK13561 612 VETEAQRDWLLKAGVGIAQGFLFARALPI 640
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
256-688 |
5.43e-44 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 168.20 E-value: 5.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 256 SRDITDLHLAEQRFKYISEHDELTGLPNRRMFNATLKHYLQPATpAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVA 335
Cdd:PRK11829 215 NRNQQLLADAYADMGRISHRFPVTELPNRSLFISLLEKEIASST-RTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 336 QRLQRAMPENAFIARIGGDEFAAVLPGIETTQALLAVGKQLIADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKA 415
Cdd:PRK11829 294 QRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRN 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 416 ADIALNELKRSGRGGICCYEPAMGGQVDK-LHSQMELAKEIISEDAIFpYYQPKVRLSDGKIMGMEALMRFFNRKGELCF 494
Cdd:PRK11829 374 ASTAMMAAHHEGRNQIMVFEPHLIEKTHKrLTQENDLLQAIENHDFTL-FLQPQWDMKRQQVIGAEALLRWCQPDGSYVL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 495 P-GHIWAAFENYVLVERIGYLIRD--KVFADirqWINQSLdVVPVSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIE 571
Cdd:PRK11829 453 PsGFVHFAEEEGMMVPLGNWVLEEacRILAD---WKARGV-SLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLE 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 572 ITE--HMFDGRGACyvfRALNLLKSEGVRISLDDFGTGYSALANIR---DYPVDVIKVDRTFVDSLSkgkEGLAVVKALL 646
Cdd:PRK11829 529 ITEtaQIQDLDEAL---RLLRELQGLGLLIALDDFGIGYSSLRYLNhlkSLPIHMIKLDKSFVKNLP---EDDAIARIIS 602
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1770577378 647 LLATELELDVVAEGVEYTEQRESLLNEGYQLGQGFLFSAAVP 688
Cdd:PRK11829 603 CVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLP 644
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
456-686 |
1.30e-43 |
|
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: 157.09 E-value: 1.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 456 ISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGHIWAAFENYVLVERIGYLIRDKVFADIRQWinQSLDVVP 535
Cdd:pfam00563 8 LENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQL--QLGPDIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 536 VSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEH-MFDGRGACYvfRALNLLKSEGVRISLDDFGTGYSALANI 614
Cdd:pfam00563 86 LSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESdLLARLEALR--EVLKRLRALGIRIALDDFGTGYSSLSYL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1770577378 615 RDYPVDVIKVDRTFVDSLSKGKEGLAVVKALLLLATELELDVVAEGVEYTEQRESLLNEGYQLGQGFLFSAA 686
Cdd:pfam00563 164 LRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
445-703 |
6.47e-41 |
|
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: 157.00 E-value: 6.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 445 LHSQMELAkeiISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGELCFPGH-IWAAfENYVLVERIGYLIRDKVFADI 523
Cdd:COG4943 272 PRRRLRRA---IKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPDGSVISPDIfIPLA-EQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 524 RQWinqsLDVVP---VSVNASPVEFMRDNYGETVLRQIRQYNLPPELVEIEITEHMF-DGRGACyvfRALNLLKSEGVRI 599
Cdd:COG4943 348 GDL----LAADPdfhISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFiDPAKAR---AVIAALREAGHRI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 600 SLDDFGTGYSALANIRDYPVDVIKVDRTFVDSLSKGKEGLAVVKALLLLATELELDVVAEGVEYTEQRESLLNEGYQLGQ 679
Cdd:COG4943 421 AIDDFGTGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQ 500
|
250 260
....*....|....*....|....
gi 1770577378 680 GFLFSAAVPAvtiSRFLNNLERHK 703
Cdd:COG4943 501 GWLFAKPLPA---EEFIAWLAAQR 521
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
275-431 |
3.27e-36 |
|
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: 134.00 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 275 HDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGD 354
Cdd:TIGR00254 4 RDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYGGE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770577378 355 EFAAVLPGIETTQALLAVG--KQLIADTTVPLSyQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGRGGI 431
Cdd:TIGR00254 84 EFVVILPGTPLEDALSKAErlRDAINSKPIEVA-GSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
276-428 |
1.73e-24 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 107.29 E-value: 1.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 276 DELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGDE 355
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1770577378 356 FAAVLPGIETTQAlLAVGKQL---IADTTVPLSYQSQAIHISLSIGGALWPLQATDSTSMIKAADIALNELKRSGR 428
Cdd:PRK09581 375 FVVVMPDTDIEDA-IAVAERIrrkIAEEPFIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGR 449
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
253-437 |
1.92e-21 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 98.93 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 253 LCVS----RDITDLHLAEQR-FKYISEHDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAG 327
Cdd:PRK15426 373 LLISwyviRRMVSNMFVLQSsLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAG 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 328 DFLLETVAQRLQRAMPENAFIARIGGDEFAAVLPGIETTQALLAVGK--QLIADTTVpLSYQSQAIHISLSIGGA-LWPL 404
Cdd:PRK15426 453 DRVLSHAAGLISSSLRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERirLRINEKEI-LVAKSTTIRISASLGVSsAEED 531
|
170 180 190
....*....|....*....|....*....|...
gi 1770577378 405 QATDSTSMIKAADIALNELKRSGRGGICCYEPA 437
Cdd:PRK15426 532 GDYDFEQLQSLADRRLYLAKQAGRNRVCASDNA 564
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
273-428 |
6.24e-20 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 90.90 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 273 SEHDELTGLPNRRMFNATLKHYLQPATPAapGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIG 352
Cdd:PRK09894 129 SNMDVLTGLPGRRVLDESFDHQLRNREPQ--NLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYG 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1770577378 353 GDEFAAVLPGIETTQALLAVGK--QLIADTtvPLSYQSQAIHISLSIGgaLWPLQATDSTS-MIKAADIALNELKRSGR 428
Cdd:PRK09894 207 GEEFIICLKAATDEEACRAGERirQLIANH--AITHSDGRINITATFG--VSRAFPEETLDvVIGRADRAMYEGKQTGR 281
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
453-698 |
1.16e-18 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 89.67 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 453 KEI---ISEDAIFPYYQPKVRLSDGKIMGMEALMRFFNRKGelcfpGHIWA-AFENYVLVER-IGYLIRdKVFADIRQWI 527
Cdd:PRK10551 266 KEIltgIKRGQFYVEYQPVVDTQTLRVTGLEALLRWRHPTA-----GEIPPdAFINYAEAQKlIVPLTQ-HLFELIARDA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 528 NQSLDVVPV----SVNASPVEFMRDNYGETVlRQIRQyNLPPELVEI--EITEH-MFDGRGACYVFralNLLKSEGVRIS 600
Cdd:PRK10551 340 AELQKVLPVgaklGINISPAHLHSDSFKADV-QRLLA-SLPADHFQIvlEITERdMVQEEEATKLF---AWLHSQGIEIA 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 601 LDDFGTGYSALANIRDYPVDVIKVDRTFVDS--------------LSKGKEglavvkallllateLELDVVAEGVEYTEQ 666
Cdd:PRK10551 415 IDDFGTGHSALIYLERFTLDYLKIDRGFIQAigtetvtspvldavLTLAKR--------------LNMLTVAEGVETPEQ 480
|
250 260 270
....*....|....*....|....*....|..
gi 1770577378 667 RESLLNEGYQLGQGFLFSAAVPAVTISRFLNN 698
Cdd:PRK10551 481 ARWLRERGVNFLQGYWISRPLPLEDFVRWLKE 512
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
260-429 |
9.39e-18 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 85.65 E-value: 9.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 260 TDLHLAE--QRFKYISEHDELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQR 337
Cdd:PRK10245 190 TATKLAEhkRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 338 LQRAMPENAFIARIGGDEFAAVLPGIETTQALLAVGKQLIADTTVPLSYQSQAIhISLSIGGALWPLQATDSTSMIKAAD 417
Cdd:PRK10245 270 LQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQVT-LRISVGVAPLNPQMSHYREWLKSAD 348
|
170
....*....|..
gi 1770577378 418 IALNELKRSGRG 429
Cdd:PRK10245 349 LALYKAKNAGRN 360
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
275-401 |
2.44e-14 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 75.43 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 275 HDELTGLPNRRMFNATLKHYLQPATpAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGD 354
Cdd:PRK09966 250 HDPLTGLANRAAFRSGINTLMNNSD-ARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGD 328
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1770577378 355 EFAAVLPGIETTQALLAVGKQLIADTTVPLS-YQSQAIHISLSIGGAL 401
Cdd:PRK09966 329 EFAMVLYDVQSESEVQQICSALTQIFNLPFDlHNGHQTTMTLSIGYAM 376
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
262-428 |
6.11e-14 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 74.99 E-value: 6.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 262 LHLAEQRF-KYIS---EH--DELTGLPNRRMFNATLKHYLQPATPAAPGLAVIVIDLDYFKLVNDTLGHPAGDFLLETVA 335
Cdd:NF040885 324 LHLVRMHFrLYHNvsrENisDSMTGLYNRKILTPTLEQRLQRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLA 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 336 QRLQRAMPENAFIARIGGDEFAAVLpgIETTQALLAVGKQLIAdttvplsyQSQAIH-----ISLSIGGalWPLQATDS- 409
Cdd:NF040885 404 QAISASIRKSDYGIRLGGDEFCIIL--IDYEEAEAQNLIERIR--------QHLRTIdpdkrVSFSWGA--YQMQPGDTl 471
|
170
....*....|....*....
gi 1770577378 410 TSMIKAADIALNELKRSGR 428
Cdd:NF040885 472 DDAYKAADERLYLNKKQKH 490
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
276-690 |
4.22e-13 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 72.59 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 276 DELTGLPNRRMFNATLKHYLQ-PATPAAPGlAVIVIDLDYFKLVNDTLGHPAGD-FLLETVA---QRLQRAmpENAFIAR 350
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLEdQEMVGAHG-VVMLIRLPDFDLLQEEWGESQVEeLLFELINllsTFVMRY--PGALLAR 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 351 IGGDEFAAVLPGIETTQA------LLavgKQLIADTTVPLSYQSQAIHIslsiGGALWplQATDSTS-MIKAADIALNEL 423
Cdd:PRK11059 308 YSRSDFAVLLPHRSLKEAdslasqLL---KAVDALPPPKMLDRDDFLHI----GICAY--RSGQSTEqVMEEAEMALRSA 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 424 KRSGRGGICCYEPAmggqvdklhSQMELAK----------EIISEDAIFPYYQPKVrLSDGKIMGMEALMRFFNRKGELc 493
Cdd:PRK11059 379 QLQGGNGWFVYDKA---------QLPEKGRgsvrwrtlleQTLVRGGPRLYQQPAV-TRDGKVHHRELFCRIRDGQGEL- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 494 fpghIWAafENYV-LVERIGYLIR------DKVFADIRQWINQSLdVVPVSVNA--SPvEFMRdnYGETVLRQIRQYNLP 564
Cdd:PRK11059 448 ----LSA--ELFMpMVQQLGLSEQydrqviERVLPLLRYWPEENL-SINLSVDSllSR-AFQR--WLRDTLLQCPRSQRK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 565 P---ELVEIEITEHMfdgrgaCYVFRALNLLKSEGVRISLDDFG-----TGYsalanIRDYPVDVIKVDRT--------- 627
Cdd:PRK11059 518 RlifELAEADVCQHI------SRLRPVLRMLRGLGCRLAVDQAGltvvsTSY-----IKELNVELIKLHPSlvrnihkrt 586
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1770577378 628 ----FVDSLSKGKEGLAVVkallllateleldVVAEGVEYTEQRESLLNEGYQLGQGFLFSAAVPAV 690
Cdd:PRK11059 587 enqlFVRSLVGACAGTETQ-------------VFATGVESREEWQTLQELGVSGGQGDFFAESQPLD 640
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
155-263 |
1.12e-12 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 64.74 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 155 LDASIDCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLLPPEIEGPGREALKQAVDGHNARFFGKSESGSGQTLF 234
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEERH 80
|
90 100
....*....|....*....|....*....
gi 1770577378 235 WDNILTPVKTASGDVSSILCVSRDITDLH 263
Cdd:pfam08448 81 YELRLTPLRDPDGEVIGVLVISRDITERR 109
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
153-378 |
4.09e-10 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 60.81 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 153 SMLDASIDCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLLPPEIEGPGREALKQAV-DGHNARFFGKSESGSGQ 231
Cdd:COG2202 15 ALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALaGGGVWRGELRNRRKDGS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 232 TLFWDNILTPVKTASGDVSSILCVSRDITDLHLAEQRFKYISEHDELTGLPNRR-MFNATLKHYLQPATPAAPGLAVIVI 310
Cdd:COG2202 95 LFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDgIFVLDLDGRILYVNPAAEELLGYSP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770577378 311 DLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENAFIARIGGDEFAAVLpgIETTQALLAVGKQLIA 378
Cdd:COG2202 175 EELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVW--VEASAVPLRDGGEVIG 240
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
71-268 |
1.54e-09 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 59.27 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 71 NWMNWLHPEDRAQTRDAWQKAILQHNVFRHNLRLAVKEGDYRWFVAYSYTVP---GVGCRMVTFFE--------ADQLQE 139
Cdd:COG2202 55 TLRDLLPPEDDDEFLELLRAALAGGGVWRGELRNRRKDGSLFWVELSISPVRdedGEITGFVGIARditerkraEEALRE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 140 DNVKAyanwqtsKSMLDASIDCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLLPPEIEGPGREALKQAVDGHNA 219
Cdd:COG2202 135 SEERL-------RLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRE 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1770577378 220 RFFGKSESGSGQTLFWD-NILTPVKTASGDVSSILCVSRDITDLHLAEQR 268
Cdd:COG2202 208 SYELELRLKDGDGRWVWvEASAVPLRDGGEVIGVLGIVRDITERKRAEEA 257
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
307-398 |
1.78e-08 |
|
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: 53.51 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 307 VIVIDLDYFKLVNDTLGHPAGDFLLETVAQRLQRAMPENA-FIARIGGDEFAAVLPGIEtTQALLAVGKQLIadTTVPLS 385
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGdLKIKTIGDEFMVVSGLDH-PAAAVAFAEDMR--EAVSAL 80
|
90
....*....|...
gi 1770577378 386 YQSQAIHISLSIG 398
Cdd:cd07556 81 NQSEGNPVRVRIG 93
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
152-268 |
1.08e-06 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 51.39 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 152 KSMLDASIDCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLLPPeiEGPGREALKQAVDGHNARFFG--KSESGS 229
Cdd:COG3852 10 RAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPE--DSPLRELLERALAEGQPVTERevTLRRKD 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 1770577378 230 GQTLFWDNILTPVKTASGDVsSILCVSRDITDLHLAEQR 268
Cdd:COG3852 88 GEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERE 125
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
563-684 |
1.10e-06 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 51.34 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 563 LPPELVEIEITEHM-FDGRgacyVFRALNLLKSEGVRISLDDFgTGYSALANIRDYpVDVIKVD---------RTFVDSL 632
Cdd:COG3434 81 LPPERVVLEILEDVePDEE----LLEALKELKEKGYRIALDDF-VLDPEWDPLLPL-ADIIKIDvlaldleelAELVARL 154
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1770577378 633 SKGKeglavvkallllateleLDVVAEGVEYTEQRESLLNEGYQLGQGFLFS 684
Cdd:COG3434 155 KRYG-----------------IKLLAEKVETREEFELCKELGFDLFQGYFFS 189
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
33-267 |
3.98e-06 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 50.12 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 33 FFDPMPLPGWCFFEQERSAmanaYWQQAMALLPAEQSDNWM-----NWLHPEDRAQTRDAWQKAILQHNVFRHNLRLAVK 107
Cdd:COG5805 39 ILENLPDAIIAVNREGKVI----YINPAMEKLLGYTSEEIIgktifDFLEKEYHYRVKTRIERLQKGYDVVMIEQIYCKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 108 -EGDYRWFVAYSYTVPGVGCRMVTFFEADQLQEDNVKAYANWQTSKSMLDASIDCIKLINTKGELIDMNSSGCQALGVSA 186
Cdd:COG5805 115 gELIYVEVKLFPIYNQNGQAAILALRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 187 ASGFGMEWLKLLPPEIEGPGREALKQAVDGHNARFFGKSESG-SGQTLFWDNILTPVKTASGDVSSILCVSRDITDLHLA 265
Cdd:COG5805 195 EELIGKNLLELLHPCDKEEFKERIESITEVWQEFIIEREIITkDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEA 274
|
..
gi 1770577378 266 EQ 267
Cdd:COG5805 275 EE 276
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
160-275 |
4.83e-06 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 49.59 E-value: 4.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 160 DCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLLPPEIEGPGREALKQAVDGHNARFFGKS-ESGSGQTLFWDNI 238
Cdd:COG5809 26 DAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKEGESRDELEFElRHKNGKRLEFSSK 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1770577378 239 LTPVKTASGDVSSILCVSRDITD-------LHLAEQRFKYISEH 275
Cdd:COG5809 106 LSPIFDQNGDIEGMLAISRDITErkrmeeaLRESEEKFRLIFNH 149
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
70-131 |
7.86e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 44.64 E-value: 7.86e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1770577378 70 DNWMNWLHPEDRAQTRDAWQKAILQHNVFRHNLRLAVKEGDYRWFVAYSYTVP---GVGCRMVTF 131
Cdd:pfam08447 24 ESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRdenGKPVRVIGV 88
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
347-422 |
1.26e-05 |
|
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: 46.44 E-value: 1.26e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1770577378 347 FIARIGGDEFAAVLPGIETTQALLAVGK--QLIAdttvplsyQSQAIHISLSIGGAlwplqatdSTSMIKAADiALNE 422
Cdd:COG3706 117 LVARYGGEEFAILLPGTDLEGALAVAERirEAVA--------ELPSLRVTVSIGVA--------GDSLLKRAD-ALYQ 177
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
152-269 |
2.48e-04 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 41.51 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 152 KSMLDASIDCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLLPPEIEGPGREALKQAVDGHNARFFG----KSES 227
Cdd:TIGR00229 6 RAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEerrvRRKD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1770577378 228 GSgqtLFWDNI-LTPVkTASGDVSSILCVSRDITDLHLAEQRF 269
Cdd:TIGR00229 86 GS---EIWVEVsVSPI-RTNGGELGVVGIVRDITERKEAEEAL 124
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
152-259 |
4.75e-04 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 40.09 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 152 KSMLDASIDCIKLINTKGELIDMNSSGCQALGVSAASGFGMEWLKLLPPEIEGPGREALKQA-VDGHNARFFGKS-ESGS 229
Cdd:pfam00989 4 RAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQAlLQGEESRGFEVSfRVPD 83
|
90 100 110
....*....|....*....|....*....|
gi 1770577378 230 GQTLFWDNILTPVKTASGDVSSILCVSRDI 259
Cdd:pfam00989 84 GRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
595-688 |
9.50e-04 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 41.53 E-value: 9.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1770577378 595 EGVRISLDDFGTG---YSALANIRdYpvDVIKVDRTFVDSLSKGKEGLAVVKALLLLATELELDVVAEGVEYTEQRESLL 671
Cdd:PRK11596 151 EFGPLWLDDFGTGmanFSALSEVR-Y--DYIKVARELFIMLRQSEEGRNLFSQLLHLMNRYCRGVIVEGVETPEEWRDVQ 227
|
90
....*....|....*..
gi 1770577378 672 NEGYQLGQGFLFSAAVP 688
Cdd:PRK11596 228 RSPAFAAQGYFLSRPAP 244
|
|
| |
