|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
384-867 |
4.35e-117 |
|
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: 371.80 E-value: 4.35e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 384 DLELLTFVSQHIATAIERKLATEALKRSNEELEEKILERTRELATTNQELQKEISQRRKAEQQLLHDAKHDALTGLPNRL 463
Cdd:COG5001 184 LLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRR 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 464 MFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGGDEFVILLDGLR 543
Cdd:COG5001 264 LFLDRLEQALARARRS-GRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLD 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 544 TADDAKEVAERILKELSRPYELADKQFNSGASIGIAVSGHHrDDTSESILRDADTAMYMAKTRGKGCYVVFDEKSHQQLM 623
Cdd:COG5001 343 DPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDD-GADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERAR 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 624 QDVSLENELRNALDTQQIRLSYFPVQDLKTGQLQALDVRLYWPHPQHGKIKQQQLANLAEQANLQLELDRYAI-EALnSE 702
Cdd:COG5001 422 ERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLrEAC-RQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 703 LPKLQLAAGTKLHLAI--CSQHLKHKHALRSLKNCLRNCRFPLNDLCLFFNEQSLSRDLENHINGFEVLKRLQVTLGITG 780
Cdd:COG5001 501 LAAWQDAGLPDLRVAVnlSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 781 YGSGYSPLISLSFLPVNVLRLDASLVSHL-QSPHHRRLLKAI-RLsAGALELELVLDGVNTQEQKQQLAQMGFNSGQGQA 858
Cdd:COG5001 581 FGTGYSSLSYLKRLPVDTLKIDRSFVRDLaEDPDDAAIVRAIiAL-AHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYL 659
|
....*....
gi 765523125 859 LGSRLSAAD 867
Cdd:COG5001 660 FSRPLPAEE 668
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
436-856 |
1.19e-62 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 224.18 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 436 EISQRRKAEQQLLHDAKHDALTGLPNRLMFMERLSQAVKHNRRHmqdKFALLFVDLDRFKLINDTLGHLEGDKFLVETAI 515
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNN---QVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 516 RLKFCIRDNDTLARLGGDEFVILL-DGLRTADDAkeVAERILKELSRPYELADKQFNSGASIGIAVSGHHRDDtSESILR 594
Cdd:PRK10060 299 AILSCLEEDQTLARLGGDEFLVLAsHTSQAALEA--MASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDD-SESLIR 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 595 DADTAMYMAKTRGKGCYVVFDEKSHQQLMQDVSLENELRNALDTQQIRLSYFPVQDLkTGQLQALDVRLYWPHPQHGKIK 674
Cdd:PRK10060 376 SADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIP 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 675 QQQLANLAEQANLQLELDRYAIEALNSELPKLQlAAGTKLHLAI--CSQHLKHKHALRSLKNCLRNCRFplnDLCLFFNE 752
Cdd:PRK10060 455 PLEFISYAEESGLIVPLGRWVMLDVVRQVAKWR-DKGINLRVAVnvSARQLADQTIFTALKQALQELNF---EYCPIDVE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 753 QSLSRDLENHINGFEVLKRLQvTLG----ITGYGSGYSPLISLSFLPVNVLRLDASLVSHL-QSPHHRRLLKAIRLSAGA 827
Cdd:PRK10060 531 LTESCLIENEELALSVIQQFS-QLGaqvhLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIhKQPVSQSLVRAIVAVAQA 609
|
410 420
....*....|....*....|....*....
gi 765523125 828 LELELVLDGVNTQEQKQQLAQMGFNSGQG 856
Cdd:PRK10060 610 LNLQVIAEGVETAKEDAFLTKNGVNERQG 638
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
453-612 |
1.42e-58 |
|
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: 197.01 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 453 HDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGG 532
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRS-GRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 533 DEFVILLDGlRTADDAKEVAERILKELSRPYELADKQFNSGASIGIAVSGHHrDDTSESILRDADTAMYMAKTRGKGCYV 612
Cdd:cd01949 81 DEFAILLPG-TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPED-GEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
449-614 |
3.66e-51 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 176.67 E-value: 3.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 449 HDAKHDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLA 528
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQ-GSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 529 RLGGDEFVILLDGLrTADDAKEVAERILKELSRPYELADKQFNSGASIGIAVSGHHrDDTSESILRDADTAMYMAKTRGK 608
Cdd:smart00267 80 RLGGDEFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKAGR 157
|
....*.
gi 765523125 609 GCYVVF 614
Cdd:smart00267 158 NQVAVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
451-610 |
8.24e-51 |
|
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: 175.52 E-value: 8.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 451 AKHDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARL 530
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALRE-GSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 531 GGDEFVILLDG--LRTADDAKEVAERILKELSRPYELADKQFNSGASIGIAVSGHHRDDTsESILRDADTAMYMAKTRGK 608
Cdd:pfam00990 80 GGDEFAILLPEtsLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDP-EDLLKRADTALYQAKQAGR 158
|
..
gi 765523125 609 GC 610
Cdd:pfam00990 159 NR 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
451-615 |
1.28e-39 |
|
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: 144.02 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 451 AKHDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARL 530
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRF-QRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 531 GGDEFVILLDGLRTAdDAKEVAERI-LKELSRPYELADKQFNS-GASIGIAVSGHHrDDTSESILRDADTAMYMAKTRGK 608
Cdd:TIGR00254 81 GGEEFVVILPGTPLE-DALSKAERLrDAINSKPIEVAGSETLTvTVSIGVACYPGH-GLTLEELLKRADEALYQAKKAGR 158
|
....*..
gi 765523125 609 GCYVVFD 615
Cdd:TIGR00254 159 NRVVVAD 165
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
5-559 |
2.81e-14 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 77.16 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 5 ETLHQHSAQEVSSLEKRVARLRRLAAKYKRAEATQNALLEISNIANKATSMESFYQGMHLHLQQLIPADNFYISLLDAQR 84
Cdd:COG2203 158 RVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 85 QHLELPFFSDEKDSHPSELYPEQelseilmqGLTGYVLRTAKPLLCDERKAEELAAAGEIMSLGSP-CHQWLGVPIMQND 163
Cdd:COG2203 238 GELELVAAPGLPEEELGRLPLGE--------GLAGRALRTGEPVVVNDASTDPRFAPSLRELLLALgIRSLLCVPLLVDG 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 164 RAIGVLVVQSYNPASsYGEMEFELMAFISHHIAGAMERLRHHEQLEQAITQRTQELSQAYDKLKQEVYERRRAERLQKSL 243
Cdd:COG2203 310 RLIGVLALYSKEPRA-FTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 244 FEIAELSSSNLDDSEFYTELHRVLSHLLPAnncyIALLDDTATELHFPFYVSQLSDQPPKCRPLMDGLVEYLLRLKRPVL 323
Cdd:COG2203 389 LALLLLLSLLGAELLLLLLDAADLSGLLAL----EGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELEL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 324 LDQSDIQSLVCAKEIYSKAPELNHTQSMHQWIGVPLFIQDRIAGALTIYSFSMHQNYQFKDLELLTFVSQHIATAIERKL 403
Cdd:COG2203 465 LEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALL 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 404 ATEALKRSNEELEEKILERTRELATTNQELQKEISQRRKAEQQLLHDAKHDALTGLPNRLMFMERLSQAVKHNRRHMQDK 483
Cdd:COG2203 545 EDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVV 624
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765523125 484 FALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGGDEFVILLDGLRTADDAKEVAERILKEL 559
Cdd:COG2203 625 TLELTVLVVLAAVEDSALLLRLALALASLVLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLG 700
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
454-608 |
3.94e-14 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 75.77 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 454 DALTGLPNRLMFMERLSQAVKhnrRHMQDKFALLFV--DLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLG 531
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQ---RLTEKGIPVTFIalDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLG 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765523125 532 GDEF-VILLDGlrTADDAKEVAERILKELSRPYELADKQFNSGASigiavsgHHRD-DTSESILRDADTAMYMAKTRGK 608
Cdd:NF040885 421 GDEFcIILIDY--EEAEAQNLIERIRQHLRTIDPDKRVSFSWGAY-------QMQPgDTLDDAYKAADERLYLNKKQKH 490
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
265-409 |
3.81e-09 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 56.24 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 265 RVLSHLLPANNCYIALLDDTATELHFPFYVSQLSDQP-PKCRPLMDGLVEYLLRLKRPVLLDQsdiqslvCAKEIYSKAP 343
Cdd:smart00065 11 EELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTlGIRFPLDEGLAGRVAETGRPLNIPD-------VEADPLFAED 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765523125 344 ELNHTQSMHQWIGVPLFIQDRIAGALTIYsfSMHQNYQF--KDLELLTFVSQHIATAIERKLATEALK 409
Cdd:smart00065 84 LLGRYQGVRSFLAVPLVADGELVGVLALH--NKKSPRPFteEDEELLQALANQLAIALANAQLYEELR 149
|
|
| GAF_2 |
pfam13185 |
GAF domain; The GAF domain is named after some of the proteins it is found in, including ... |
258-400 |
1.42e-08 |
|
GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433019 [Multi-domain] Cd Length: 137 Bit Score: 54.39 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 258 EFYTELHRVLSHLLPANNCYIALLDDTATELHFPFYVSQLSDQPPkcRPLMDGLVEYLLRLKRPVLLDqsDIQSLVCAKE 337
Cdd:pfam13185 6 ELLDAVLEAAVELGASAVGFILLVDDDGRLAAWGGAADELSAALD--DPPGEGLVGEALRTGRPVIVN--DLAADPAKKG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 765523125 338 IYSKAPELNHtqsmhqWIGVPLFIQDRIAGALTIYSFSMHQnYQFKDLELLTFVSQHIATAIE 400
Cdd:pfam13185 82 LPAGHAGLRS------FLSVPLVSGGRVVGVLALGSNRPGA-FDEEDLELLELLAEQAAIAIE 137
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
384-867 |
4.35e-117 |
|
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: 371.80 E-value: 4.35e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 384 DLELLTFVSQHIATAIERKLATEALKRSNEELEEKILERTRELATTNQELQKEISQRRKAEQQLLHDAKHDALTGLPNRL 463
Cdd:COG5001 184 LLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRR 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 464 MFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGGDEFVILLDGLR 543
Cdd:COG5001 264 LFLDRLEQALARARRS-GRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLD 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 544 TADDAKEVAERILKELSRPYELADKQFNSGASIGIAVSGHHrDDTSESILRDADTAMYMAKTRGKGCYVVFDEKSHQQLM 623
Cdd:COG5001 343 DPEDAEAVAERILAALAEPFELDGHELYVSASIGIALYPDD-GADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERAR 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 624 QDVSLENELRNALDTQQIRLSYFPVQDLKTGQLQALDVRLYWPHPQHGKIKQQQLANLAEQANLQLELDRYAI-EALnSE 702
Cdd:COG5001 422 ERLELEADLRRALERGELELHYQPQVDLATGRIVGAEALLRWQHPERGLVSPAEFIPLAEETGLIVPLGEWVLrEAC-RQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 703 LPKLQLAAGTKLHLAI--CSQHLKHKHALRSLKNCLRNCRFPLNDLCLFFNEQSLSRDLENHINGFEVLKRLQVTLGITG 780
Cdd:COG5001 501 LAAWQDAGLPDLRVAVnlSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 781 YGSGYSPLISLSFLPVNVLRLDASLVSHL-QSPHHRRLLKAI-RLsAGALELELVLDGVNTQEQKQQLAQMGFNSGQGQA 858
Cdd:COG5001 581 FGTGYSSLSYLKRLPVDTLKIDRSFVRDLaEDPDDAAIVRAIiAL-AHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYL 659
|
....*....
gi 765523125 859 LGSRLSAAD 867
Cdd:COG5001 660 FSRPLPAEE 668
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
436-856 |
1.19e-62 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 224.18 E-value: 1.19e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 436 EISQRRKAEQQLLHDAKHDALTGLPNRLMFMERLSQAVKHNRRHmqdKFALLFVDLDRFKLINDTLGHLEGDKFLVETAI 515
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNN---QVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 516 RLKFCIRDNDTLARLGGDEFVILL-DGLRTADDAkeVAERILKELSRPYELADKQFNSGASIGIAVSGHHRDDtSESILR 594
Cdd:PRK10060 299 AILSCLEEDQTLARLGGDEFLVLAsHTSQAALEA--MASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDD-SESLIR 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 595 DADTAMYMAKTRGKGCYVVFDEKSHQQLMQDVSLENELRNALDTQQIRLSYFPVQDLkTGQLQALDVRLYWPHPQHGKIK 674
Cdd:PRK10060 376 SADTAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSPERGLIP 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 675 QQQLANLAEQANLQLELDRYAIEALNSELPKLQlAAGTKLHLAI--CSQHLKHKHALRSLKNCLRNCRFplnDLCLFFNE 752
Cdd:PRK10060 455 PLEFISYAEESGLIVPLGRWVMLDVVRQVAKWR-DKGINLRVAVnvSARQLADQTIFTALKQALQELNF---EYCPIDVE 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 753 QSLSRDLENHINGFEVLKRLQvTLG----ITGYGSGYSPLISLSFLPVNVLRLDASLVSHL-QSPHHRRLLKAIRLSAGA 827
Cdd:PRK10060 531 LTESCLIENEELALSVIQQFS-QLGaqvhLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIhKQPVSQSLVRAIVAVAQA 609
|
410 420
....*....|....*....|....*....
gi 765523125 828 LELELVLDGVNTQEQKQQLAQMGFNSGQG 856
Cdd:PRK10060 610 LNLQVIAEGVETAKEDAFLTKNGVNERQG 638
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
453-612 |
1.42e-58 |
|
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: 197.01 E-value: 1.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 453 HDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGG 532
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRS-GRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 533 DEFVILLDGlRTADDAKEVAERILKELSRPYELADKQFNSGASIGIAVSGHHrDDTSESILRDADTAMYMAKTRGKGCYV 612
Cdd:cd01949 81 DEFAILLPG-TDLEEAEALAERLREAIEEPFFIDGQEIRVTASIGIATYPED-GEDAEELLRRADEALYRAKRSGRNRVV 158
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
345-614 |
3.20e-58 |
|
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: 200.59 E-value: 3.20e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 345 LNHTQSMHQWIGVPLFIQDRIAGALTIYSFSMHQNYQFKDLELLTFVSQHIATAIERKLATEALKRSNEELEEKILERTR 424
Cdd:COG2199 6 LLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 425 ELATTNQELQK--EISQRRKAEQQLLHDAKHDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLG 502
Cdd:COG2199 86 LLLALLLLLLAleDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARRE-GRPLALLLIDLDHFKRINDTYG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 503 HLEGDKFLVETAIRLKFCIRDNDTLARLGGDEFVILLDGLrTADDAKEVAERILKELSR-PYELADKQFNSGASIGIAVS 581
Cdd:COG2199 165 HAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGT-DLEEAEALAERLREALEQlPFELEGKELRVTVSIGVALY 243
|
250 260 270
....*....|....*....|....*....|...
gi 765523125 582 GHHrDDTSESILRDADTAMYMAKTRGKGCYVVF 614
Cdd:COG2199 244 PED-GDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
385-860 |
1.92e-53 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 196.16 E-value: 1.92e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 385 LELLTFVSQHIATAIERKLATEALKRSNEELEEKILERTRELATTNQELQKEISQRRKAEQQLLHDAKHDALTGLPNRLM 464
Cdd:COG2200 88 LLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 465 FMERLSQAVKHNRRHMQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGGDEFVILLDGLRT 544
Cdd:COG2200 168 LLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 545 ADDAKEVAERILKELSRPYELADKQFNSGASIGIAVsgHHRDDTSESILRDADTAMYMAKTRGKGCYVVFDEKSHQQLMQ 624
Cdd:COG2200 248 AAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAA--APDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAEARARR 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 625 DVSLENELRNALDTQQIRLSYFPVQDLKTGQLQALDVRLYWPHPQHGKIKQQQLANLAEQANLQLELDRYAIEALNSELP 704
Cdd:COG2200 326 RLALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLA 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 705 KLQlAAGTKLHLAI--CSQHLKHKHALRSLKNCLRNCRFPLNDLCLFFNEQSLSRDLENHINGFEVLKRLQVTLGITGYG 782
Cdd:COG2200 406 RWP-ERGLDLRLSVnlSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFG 484
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765523125 783 SGYSPLISLSFLPVNVLRLDASLVSHL-QSPHHRRLLKAIRLSAGALELELVLDGVNTQEQKQQLAQMGFNSGQGQALG 860
Cdd:COG2200 485 TGYSSLSYLKRLPPDYLKIDRSFVRDIaRDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFG 563
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
449-614 |
3.66e-51 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 176.67 E-value: 3.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 449 HDAKHDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLA 528
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQ-GSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 529 RLGGDEFVILLDGLrTADDAKEVAERILKELSRPYELADKQFNSGASIGIAVSGHHrDDTSESILRDADTAMYMAKTRGK 608
Cdd:smart00267 80 RLGGDEFALLLPET-SLEEAIALAERILQQLREPIIIHGIPLYLTISIGVAAYPNP-GEDAEDLLKRADTALYQAKKAGR 157
|
....*.
gi 765523125 609 GCYVVF 614
Cdd:smart00267 158 NQVAVY 163
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
451-610 |
8.24e-51 |
|
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: 175.52 E-value: 8.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 451 AKHDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARL 530
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALRE-GSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 531 GGDEFVILLDG--LRTADDAKEVAERILKELSRPYELADKQFNSGASIGIAVSGHHRDDTsESILRDADTAMYMAKTRGK 608
Cdd:pfam00990 80 GGDEFAILLPEtsLEGAQELAERIRRLLAKLKIPHTVSGLPLYVTISIGIAAYPNDGEDP-EDLLKRADTALYQAKQAGR 158
|
..
gi 765523125 609 GC 610
Cdd:pfam00990 159 NR 160
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
436-860 |
2.97e-44 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 173.71 E-value: 2.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 436 EISQRRKAEQQLLHDAKHDALTGLPNRLMFMERL----SQAVKHNRRHmqdkfALLFVDLDRFKLINDTLGHLEGDKFLV 511
Cdd:PRK09776 650 DVTESRKMLRQLSYSASHDALTHLANRASFEKQLrrllQTVNSTHQRH-----ALVFIDLDRFKAVNDSAGHAAGDALLR 724
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 512 ETAIRLKFCIRDNDTLARLGGDEFVILLDGLrTADDAKEVAERILKEL-SRPYELADKQFNSGASIGIAVSGHHRDDTSE 590
Cdd:PRK09776 725 ELASLMLSMLRSSDVLARLGGDEFGLLLPDC-NVESARFIATRIISAInDYHFPWEGRVYRVGASAGITLIDANNHQASE 803
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 591 sILRDADTAMYMAKTRGKGCYVVFdEKSHQQLM---QDVSLENELRNALDTQQIRLSY---FPVQDLKTGQLQALdVRLY 664
Cdd:PRK09776 804 -VMSQADIACYAAKNAGRGRVTVY-EPQQAAAHsehRALSLAEQWRMIKENQLMMLAHgvaSPRIPEARNHWLIS-LRLW 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 665 WPHPQhgKIKQQQLANLAEQANLQLELDRYAIEALNSELPKLQLAAGTKLHLAICSQHLKHKHALRSLKNCLRNCRFPLN 744
Cdd:PRK09776 881 DPEGE--IIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPR 958
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 745 DLCLFFNEQSLSRDLENHINGFEVLKRLQVTLGITGYGSGYSPLISLSFLPVNVLRLDASLVSHL-------------QS 811
Cdd:PRK09776 959 LLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLhgnlmdemlisiiQG 1038
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 765523125 812 PHHRRllkAIRLSAGALELELVLDgvntqeqkqQLAQMGFNSGQGQALG 860
Cdd:PRK09776 1039 HAQRL---GMKTIAGPVELPLVLD---------TLSGIGVDLAYGYAIA 1075
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
439-867 |
6.17e-41 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 161.86 E-value: 6.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 439 QRRKAEQQLLHDAKHDALTGLPNRLMFMERLSQAVKHNRrhmqdKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLK 518
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLVDKAV-----SPVVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 519 FCIRDNDTLARLGGDEFVILLDGLRtADDAKEVAERILKELSRPYELADKQFNSGASIGIAVS-GHHRDDtsesILRDAD 597
Cdd:PRK11359 439 EKLKPDQYLCRIEGTQFVLVSLEND-VSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDvGKNRDY----LLSTAH 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 598 TAMYMAKTRGKGCYVVFDEKSHQQLMQDVSLENELRNALDTQQIRLSYFPVQDLKTGQLQALDVRLYWPHPQHGKIKQQQ 677
Cdd:PRK11359 514 NAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSR 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 678 LANLAEQANLQLELDRYAIEALNSELPKLQLAAgtkLHLAICSQHLKHKHALRS-----LKNCLRNCRFPLNDLCLFFNE 752
Cdd:PRK11359 594 FIPLAEEIGEIENIGRWVIAEACRQLAEWRSQN---IHIPALSVNLSALHFRSNqlpnqVSDAMQAWGIDGHQLTVEITE 670
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 753 QSLSRDLENHINGFEVLKRLQVTLGITGYGSGYSPLISLSFLPVNVLRLDASLVSHLQSPHH-RRLLKAIRLSAGALELE 831
Cdd:PRK11359 671 SMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRiLALLEAITSIGQSLNLT 750
|
410 420 430
....*....|....*....|....*....|....*.
gi 765523125 832 LVLDGVNTQEQKQQLAQMGFNSGQGQALGSRLSAAD 867
Cdd:PRK11359 751 VVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEE 786
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
451-615 |
1.28e-39 |
|
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: 144.02 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 451 AKHDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARL 530
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRF-QRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 531 GGDEFVILLDGLRTAdDAKEVAERI-LKELSRPYELADKQFNS-GASIGIAVSGHHrDDTSESILRDADTAMYMAKTRGK 608
Cdd:TIGR00254 81 GGEEFVVILPGTPLE-DALSKAERLrDAINSKPIEVAGSETLTvTVSIGVACYPGH-GLTLEELLKRADEALYQAKKAGR 158
|
....*..
gi 765523125 609 GCYVVFD 615
Cdd:TIGR00254 159 NRVVVAD 165
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
445-867 |
2.59e-38 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 152.79 E-value: 2.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 445 QQLLHDAKHD--------ALTGLPNRLMFMERLSQAVKHNRRHmqDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIR 516
Cdd:PRK11829 218 QQLLADAYADmgrishrfPVTELPNRSLFISLLEKEIASSTRT--DHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQR 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 517 LKFCIRDNDTLARLGGDEFVILLDGLRTADDAKEVAERILKELSRPYELADKQFNSGASIGIAVSgHHRDDTSESILRDA 596
Cdd:PRK11829 296 IEQCIDDSDLLAQLSKTEFAVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRY-QAQQDTAESMMRNA 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 597 DTAMYMAKTRGKGCYVVFD----EKSHQQLMQdvslENELRNALDTQQIRLSYFPVQDLKTGQLQALDVRLYWPHPQHGK 672
Cdd:PRK11829 375 STAMMAAHHEGRNQIMVFEphliEKTHKRLTQ----ENDLLQAIENHDFTLFLQPQWDMKRQQVIGAEALLRWCQPDGSY 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 673 IKQQQLANLAEQANLQLELDRYAIEALNSELPKLQLAAGT-KLHLAICSQHLKHKHALRSLKNCLRNCRFPLNDLCLFFN 751
Cdd:PRK11829 451 VLPSGFVHFAEEEGMMVPLGNWVLEEACRILADWKARGVSlPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEIT 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 752 EQSLSRDLENHINGFEVLKRLQVTLGITGYGSGYSPLISL---SFLPVNVLRLDASLVSHLqsPHHRRLLKAIRLSAGAL 828
Cdd:PRK11829 531 ETAQIQDLDEALRLLRELQGLGLLIALDDFGIGYSSLRYLnhlKSLPIHMIKLDKSFVKNL--PEDDAIARIISCVSDVL 608
|
410 420 430
....*....|....*....|....*....|....*....
gi 765523125 829 ELELVLDGVNTQEQKQQLAQMGFNSGQGQALGSRLSAAD 867
Cdd:PRK11829 609 KVRVMAEGVETEEQRQWLLEHGIQCGQGFLFSPPLPRAE 647
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
629-856 |
2.25e-35 |
|
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: 134.37 E-value: 2.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 629 ENELRNALDTQQIRLSYFPVQDLKTGQLQALDVRLYWPHPQHGKIKQQQLANLAEQANLQLELDRYAIEALNSELPKLQL 708
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 709 AAGTKLHLAICSQHLKHKHALRSLKNCLRNCRFPLNDLCLFFNEQSLSRDLENHINGFEVLKRLQVTLGITGYGSGYSPL 788
Cdd:pfam00563 81 GPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765523125 789 ISLSFLPVNVLRLDASLVSHL-QSPHHRRLLKAIRLSAGALELELVLDGVNTQEQKQQLAQMGFNSGQG 856
Cdd:pfam00563 161 SYLLRLPPDFVKIDRSLIADIdKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQG 229
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
630-867 |
1.36e-33 |
|
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: 129.59 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 630 NELRNALDTQQIRLSYFPVQDLKTGQLQALDVRLYWPHPQHGKIKQQQLANLAEQANLQLELDRYAIEALNSELPKLQlA 709
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHPEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQ-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 710 AGTKLHLAI--CSQHLKHKHALRSLKNCLRNCRFPLNDLCLFFNEQSLSRDLENHINGFEVLKRLQVTLGITGYGSGYSP 787
Cdd:cd01948 80 GGPDLRLSVnlSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 788 LISLSFLPVNVLRLDASLVSHL-QSPHHRRLLKAIRLSAGALELELVLDGVNTQEQKQQLAQMGFNSGQGQALGSRLSAA 866
Cdd:cd01948 160 LSYLKRLPVDYLKIDRSFVRDIeTDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
.
gi 765523125 867 D 867
Cdd:cd01948 240 E 240
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
445-856 |
4.11e-32 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 133.30 E-value: 4.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 445 QQLL---HD-----AKHDALTGLPNRLMFMERLSQAVKHnrrhmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIR 516
Cdd:PRK13561 217 QQLLqrqYEeqsrnATRFPVSDLPNKALLMALLEQVVAR-----KQTTALMIITCETLRDTAGVLKEAQREILLLTLVEK 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 517 LKFCIRDNDTLARLGGDEFVILLDGLRTADDAKEVAERILKELSRPYELADKQFNSGASIGIAVsgHHRDDTSESILRDA 596
Cdd:PRK13561 292 LKSVLSPRMVLAQISGYDFAIIANGVKEPWHAITLGQQVLTIINERLPIQRIQLRPSCSIGIAM--FYGDLTAEQLYSRA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 597 DTAMYMAKTRGKGCYVVFD----EKSHQQLMQdvslENELRNALDTQQIRLSYFPVQDLKTGQLQALDVRLYWPHPQHGK 672
Cdd:PRK13561 370 ISAAFTARRKGKNQIQFFDpqqmEAAQKRLTE----ESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMQQPDGSW 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 673 IKQQQLANLAEQANLQLELDRYAIEALNSELPKLQlAAGTKLHLAI--CSQHLKHKHALRSLKNCLRNCRFPLNDLCLFF 750
Cdd:PRK13561 446 DLPEGLIDRIESCGLMVTVGHWVLEESCRLLAAWQ-ERGIMLPLSVnlSALQLMHPNMVADMLELLTRYRIQPGTLILEV 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 751 NEQSLSRDLENHINGFEVLKRLQVTLGITGYGSGYSPLISLS---FLPVNVLRLDASLVSHLqsPHHRRLLKAIRLSAGA 827
Cdd:PRK13561 525 TESRRIDDPHAAVAILRPLRNAGVRVALDDFGMGYAGLRQLQhmkSLPIDVLKIDKMFVDGL--PEDDSMVAAIIMLAQS 602
|
410 420
....*....|....*....|....*....
gi 765523125 828 LELELVLDGVNTQEQKQQLAQMGFNSGQG 856
Cdd:PRK13561 603 LNLQVIAEGVETEAQRDWLLKAGVGIAQG 631
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
454-617 |
1.09e-31 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 125.56 E-value: 1.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 454 DALTGLPNRLMFMERLsqavKHNRRHMQD-KFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGG 532
Cdd:PRK09894 132 DVLTGLPGRRVLDESF----DHQLRNREPqNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGG 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 533 DEFVILLDGlRTADDAKEVAERILKELSR-PYELADKQFNSGASIGIAVSghHRDDTSESILRDADTAMYMAKTRGKGCY 611
Cdd:PRK09894 208 EEFIICLKA-ATDEEACRAGERIRQLIANhAITHSDGRINITATFGVSRA--FPEETLDVVIGRADRAMYEGKQTGRNRV 284
|
....*.
gi 765523125 612 VVFDEK 617
Cdd:PRK09894 285 MFIDEQ 290
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
397-608 |
2.19e-30 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 125.40 E-value: 2.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 397 TAIERKLATEALkRSNeeleekiLERTRELATTnqelqkeisqrrkaeqqllhdakhDALTGLPNRLMFMERLSQAVkhN 476
Cdd:PRK09581 270 TQIRRKRYQDAL-RNN-------LEQSIEMAVT------------------------DGLTGLHNRRYFDMHLKNLI--E 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 477 RRHMQDK-FALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGGDEFVILLDGLrTADDAKEVAERI 555
Cdd:PRK09581 316 RANERGKpLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDT-DIEDAIAVAERI 394
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 765523125 556 LKELS-RPYELAD--KQFNSGASIGIAVSGHHrDDTSESILRDADTAMYMAKTRGK 608
Cdd:PRK09581 395 RRKIAeEPFIISDgkERLNVTVSIGVAELRPS-GDTIEALIKRADKALYEAKNTGR 449
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
629-856 |
2.27e-27 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 111.54 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 629 ENELRNALDTQQIRLSYFPVQDLKTGQLQALDVRLYWPHPQHGKIKQQQLANLAEQANLQLELDRYAIEALNSELPKLQL 708
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHPEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 709 AAGTKLHLAI--CSQHLKHKHALRSLKNCLRNCRFPLNDLCLFFNEQSLSRDLENHINGFEVLKRLQVTLGITGYGSGYS 786
Cdd:smart00052 81 QGPPPLLISInlSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 765523125 787 PLISLSFLPVNVLRLDASLVSHLQ-SPHHRRLLKAIRLSAGALELELVLDGVNTQEQKQQLAQMGFNSGQG 856
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQtDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQG 231
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
451-619 |
2.30e-27 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 117.81 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 451 AKHDALTGLPNRLMFMERLSQAVKHNRRHmQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARL 530
Cdd:PRK15426 398 AWHDPLTRLYNRGALFEKARALAKRCQRD-QQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVAGRV 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 531 GGDEFVILLDGLrTADDAKEVAERILKELSRPYELADK----QFNsgASIGIAVSGHHRDDTSESILRDADTAMYMAKTR 606
Cdd:PRK15426 477 GGEEFCVVLPGA-SLAEAAQVAERIRLRINEKEILVAKsttiRIS--ASLGVSSAEEDGDYDFEQLQSLADRRLYLAKQA 553
|
170
....*....|...
gi 765523125 607 GKGcYVVFDEKSH 619
Cdd:PRK15426 554 GRN-RVCASDNAH 565
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
416-606 |
3.23e-23 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 103.16 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 416 EEKILERTRELATTNQELQK--EISQRRKAEQ-QLLHDAKHDALTGLPNRLMFMERLSQAVKHNRrhMQDKFALLFVDLD 492
Cdd:PRK09966 210 EERIAEFHRFALDFNSLLDEmeEWQLRLQAKNaQLLRTALHDPLTGLANRAAFRSGINTLMNNSD--ARKTSALLFLDGD 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 493 RFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGGDEFVILLDGLRTADDAKEVAERILKELSRPYELADKQFNS 572
Cdd:PRK09966 288 NFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLPFDLHNGHQTT 367
|
170 180 190
....*....|....*....|....*....|....*
gi 765523125 573 GA-SIGIAVSGHHRddTSESILRDADTAMYMAKTR 606
Cdd:PRK09966 368 MTlSIGYAMTIEHA--SAEKLQELADHNMYQAKHQ 400
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
454-609 |
1.21e-16 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 82.57 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 454 DALTGLPNRLMFMERLSQAVKHNRRHMQDKfALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGGD 533
Cdd:PRK10245 208 DGMTGVYNRRHWETLLRNEFDNCRRHHRDA-TLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGD 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 534 EFVILLDGlRTADDAKEVAERI---LKELSRPyelADKQFNSGASIGIA----VSGHHRDdtsesILRDADTAMYMAKTR 606
Cdd:PRK10245 287 EFAVIMSG-TPAESAITAMSRVhegLNTLRLP---NAPQVTLRISVGVAplnpQMSHYRE-----WLKSADLALYKAKNA 357
|
...
gi 765523125 607 GKG 609
Cdd:PRK10245 358 GRN 360
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
5-559 |
2.81e-14 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 77.16 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 5 ETLHQHSAQEVSSLEKRVARLRRLAAKYKRAEATQNALLEISNIANKATSMESFYQGMHLHLQQLIPADNFYISLLDAQR 84
Cdd:COG2203 158 RVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDEDG 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 85 QHLELPFFSDEKDSHPSELYPEQelseilmqGLTGYVLRTAKPLLCDERKAEELAAAGEIMSLGSP-CHQWLGVPIMQND 163
Cdd:COG2203 238 GELELVAAPGLPEEELGRLPLGE--------GLAGRALRTGEPVVVNDASTDPRFAPSLRELLLALgIRSLLCVPLLVDG 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 164 RAIGVLVVQSYNPASsYGEMEFELMAFISHHIAGAMERLRHHEQLEQAITQRTQELSQAYDKLKQEVYERRRAERLQKSL 243
Cdd:COG2203 310 RLIGVLALYSKEPRA-FTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLLRLRQLLLELL 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 244 FEIAELSSSNLDDSEFYTELHRVLSHLLPAnncyIALLDDTATELHFPFYVSQLSDQPPKCRPLMDGLVEYLLRLKRPVL 323
Cdd:COG2203 389 LALLLLLSLLGAELLLLLLDAADLSGLLAL----EGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELEL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 324 LDQSDIQSLVCAKEIYSKAPELNHTQSMHQWIGVPLFIQDRIAGALTIYSFSMHQNYQFKDLELLTFVSQHIATAIERKL 403
Cdd:COG2203 465 LEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLLLGLLAALAADLLLLAAALL 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 404 ATEALKRSNEELEEKILERTRELATTNQELQKEISQRRKAEQQLLHDAKHDALTGLPNRLMFMERLSQAVKHNRRHMQDK 483
Cdd:COG2203 545 EDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALALLELLLVAVGDLLLLERDLLLLLVLLVRLLLELLVV 624
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 765523125 484 FALLFVDLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLGGDEFVILLDGLRTADDAKEVAERILKEL 559
Cdd:COG2203 625 TLELTVLVVLAAVEDSALLLRLALALASLVLLRALLATELDLILDSSLLLGLLLLGALLLLGGGLALLLSIGLGLG 700
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
454-608 |
3.94e-14 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 75.77 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 454 DALTGLPNRLMFMERLSQAVKhnrRHMQDKFALLFV--DLDRFKLINDTLGHLEGDKFLVETAIRLKFCIRDNDTLARLG 531
Cdd:NF040885 344 DSMTGLYNRKILTPTLEQRLQ---RLTEKGIPVTFIalDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGIRLG 420
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765523125 532 GDEF-VILLDGlrTADDAKEVAERILKELSRPYELADKQFNSGASigiavsgHHRD-DTSESILRDADTAMYMAKTRGK 608
Cdd:NF040885 421 GDEFcIILIDY--EEAEAQNLIERIRQHLRTIDPDKRVSFSWGAY-------QMQPgDTLDDAYKAADERLYLNKKQKH 490
|
|
| PtsP |
COG3605 |
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms]; |
41-223 |
9.30e-14 |
|
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
Pssm-ID: 442824 [Multi-domain] Cd Length: 188 Bit Score: 70.70 E-value: 9.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 41 ALLEISNIANKATSMESFYQGMHLHLQQLIPADNFYISLLDAQRQHLELpffsdekdsHPSELYPEQELSEILM---QGL 117
Cdd:COG3605 5 ALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLEL---------RATEGLNPEAVGKVRLplgEGL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 118 TGYVLRTAKPLLCDERKAEE----LAAAGE--IMSLgspchqwLGVPIMQNDRAIGVLVVQSYNPaSSYGEMEFELMAFI 191
Cdd:COG3605 76 VGLVAERGEPLNLADAASHPrfkyFPETGEegFRSF-------LGVPIIRRGRVLGVLVVQSREP-REFTEEEVEFLVTL 147
|
170 180 190
....*....|....*....|....*....|..
gi 765523125 192 SHHIAGAMERLRHHEQLEQAITQRTQELSQAY 223
Cdd:COG3605 148 AAQLAEAIANAELLGELRAALAELSLAREEER 179
|
|
| GAF |
COG2203 |
GAF domain [Signal transduction mechanisms]; |
182-607 |
5.12e-13 |
|
GAF domain [Signal transduction mechanisms];
Pssm-ID: 441805 [Multi-domain] Cd Length: 712 Bit Score: 72.92 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 182 EMEFELMAFISHHIAGAMERLRHHEQLEQAITQRTQELSQAYDKLKQEVYERRRAERLQKSLFEIAELSSSNLDDSEFYT 261
Cdd:COG2203 134 LLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELLQ 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 262 ELHRVLSHLLPANNCYIALLDDTATELHFpFYVSQLSDQPPKCRPLMDGLVEYLLRLKRPVLLDqsDIQSLVCAKEIYSK 341
Cdd:COG2203 214 RILELAGELLGADRGAILLVDEDGGELEL-VAAPGLPEEELGRLPLGEGLAGRALRTGEPVVVN--DASTDPRFAPSLRE 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 342 APELNHTQSmhqWIGVPLFIQDRIAGALTIYSFSMHQnYQFKDLELLTFVSQHIATAIERKLATEALKRSNEELEEkILE 421
Cdd:COG2203 291 LLLALGIRS---LLCVPLLVDGRLIGVLALYSKEPRA-FTEEDLELLEALADQAAIAIERARLYEALEAALAALLQ-ELA 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 422 RTRELATTNQELQKEISQRRKAEQQLLHDAKHDALTGLPNRLMFMERLSQAVKHNRRHMQDKFALLFVDLDRFKLINDTL 501
Cdd:COG2203 366 LLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 502 GHLEGDKFLVETAIRLKFCIRDNDTLARLGGDEFVILLDGLRTADDAKEVAERILKELSRPYELADKQFNSGASIGIAVS 581
Cdd:COG2203 446 LLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLLLLL 525
|
410 420
....*....|....*....|....*.
gi 765523125 582 GHHRDDTSESILRDADTAMYMAKTRG 607
Cdd:COG2203 526 LGLLAALAADLLLLAAALLEDLLILL 551
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
486-604 |
2.02e-10 |
|
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: 59.29 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 486 LLFVDLDRFKLINDTLGHLEGDKFLVETAIRL-KFCIRDNDTLARLGGDEFVILLdGLRTADDAKEVAERILKELSRpye 564
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFdSLIRRSGDLKIKTIGDEFMVVS-GLDHPAAAVAFAEDMREAVSA--- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 765523125 565 LADKQFNS-----GASIGIAVSG----HHRDDTSESILRDADTAMYMAK 604
Cdd:cd07556 80 LNQSEGNPvrvriGIHTGPVVVGvigsRPQYDVWGALVNLASRMESQAK 128
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
454-856 |
5.15e-10 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 62.96 E-value: 5.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 454 DALTGLPNRLMFMERLsQAVKHNRRHMQDKFALLFVDLDRFKLINDTLGHLEGDKFLVETAIRL-KFCIRDNDT-LARLG 531
Cdd:PRK11059 231 DAKTGLGNRLFFDNQL-ATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLsTFVMRYPGAlLARYS 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 532 GDEFVILLDGlRTADDAKEVAERILKELSR--PYELADKQfnsgASIGIAVSGHHRDDTSESILRDADTAMYMAKTRGKG 609
Cdd:PRK11059 310 RSDFAVLLPH-RSLKEADSLASQLLKAVDAlpPPKMLDRD----DFLHIGICAYRSGQSTEQVMEEAEMALRSAQLQGGN 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 610 CYVVFDEKSHQQLMQ-DVSLENELRNALDTQQIRLSYFPVQDlKTGQLQALDV--RLYwpHPQHGKIKQQQLANLAEQAN 686
Cdd:PRK11059 385 GWFVYDKAQLPEKGRgSVRWRTLLEQTLVRGGPRLYQQPAVT-RDGKVHHRELfcRIR--DGQGELLSAELFMPMVQQLG 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 687 LQLELDRYAIEALnseLPKLQLAAGTKLHLAICSQHLKHKHALRSLKNCLRNCRFPLNDLCLF-FNEQSLSRDLE----- 760
Cdd:PRK11059 462 LSEQYDRQVIERV---LPLLRYWPEENLSINLSVDSLLSRAFQRWLRDTLLQCPRSQRKRLIFeLAEADVCQHISrlrpv 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 761 -NHINGFEVlkRLQVT-LGITGYGSGYsplisLSFLPVNVLRLDASLVSHLQSPHHRRLLkaIRLSAGAL---ELELVLD 835
Cdd:PRK11059 539 lRMLRGLGC--RLAVDqAGLTVVSTSY-----IKELNVELIKLHPSLVRNIHKRTENQLF--VRSLVGACagtETQVFAT 609
|
410 420
....*....|....*....|.
gi 765523125 836 GVNTQEQKQQLAQMGFNSGQG 856
Cdd:PRK11059 610 GVESREEWQTLQELGVSGGQG 630
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
525-604 |
8.61e-10 |
|
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: 58.77 E-value: 8.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 525 DTLARLGGDEFVILLDGLrTADDAKEVAERILKELSRPYEladkqFNSGASIGIAvsghhrddtSESILRDADtAMYMAK 604
Cdd:COG3706 116 DLVARYGGEEFAILLPGT-DLEGALAVAERIREAVAELPS-----LRVTVSIGVA---------GDSLLKRAD-ALYQAR 179
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
265-409 |
3.81e-09 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 56.24 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 265 RVLSHLLPANNCYIALLDDTATELHFPFYVSQLSDQP-PKCRPLMDGLVEYLLRLKRPVLLDQsdiqslvCAKEIYSKAP 343
Cdd:smart00065 11 EELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTlGIRFPLDEGLAGRVAETGRPLNIPD-------VEADPLFAED 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 765523125 344 ELNHTQSMHQWIGVPLFIQDRIAGALTIYsfSMHQNYQF--KDLELLTFVSQHIATAIERKLATEALK 409
Cdd:smart00065 84 LLGRYQGVRSFLAVPLVADGELVGVLALH--NKKSPRPFteEDEELLQALANQLAIALANAQLYEELR 149
|
|
| GAF_2 |
pfam13185 |
GAF domain; The GAF domain is named after some of the proteins it is found in, including ... |
258-400 |
1.42e-08 |
|
GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433019 [Multi-domain] Cd Length: 137 Bit Score: 54.39 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 258 EFYTELHRVLSHLLPANNCYIALLDDTATELHFPFYVSQLSDQPPkcRPLMDGLVEYLLRLKRPVLLDqsDIQSLVCAKE 337
Cdd:pfam13185 6 ELLDAVLEAAVELGASAVGFILLVDDDGRLAAWGGAADELSAALD--DPPGEGLVGEALRTGRPVIVN--DLAADPAKKG 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 765523125 338 IYSKAPELNHtqsmhqWIGVPLFIQDRIAGALTIYSFSMHQnYQFKDLELLTFVSQHIATAIE 400
Cdd:pfam13185 82 LPAGHAGLRS------FLSVPLVSGGRVVGVLALGSNRPGA-FDEEDLELLELLAEQAAIAIE 137
|
|
| GAF |
smart00065 |
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ... |
65-210 |
1.49e-08 |
|
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.
Pssm-ID: 214500 [Multi-domain] Cd Length: 149 Bit Score: 54.31 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 65 HLQQLIPADNFYISLLDA-QRQHLELPFFSDEKDSHPSELYPeqelseiLMQGLTGYVLRTAKPLLCDERKAEELAAAGE 143
Cdd:smart00065 12 ELRQLLGADRVLIYLVDEnDRGELVLVAADGLTLPTLGIRFP-------LDEGLAGRVAETGRPLNIPDVEADPLFAEDL 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 765523125 144 IMSLGSPCHqWLGVPIMQNDRAIGVLVVQSYNPASSYGEMEFELMAFISHHIAGAmerLRHHEQLEQ 210
Cdd:smart00065 85 LGRYQGVRS-FLAVPLVADGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIA---LANAQLYEE 147
|
|
| GAF_2 |
pfam13185 |
GAF domain; The GAF domain is named after some of the proteins it is found in, including ... |
52-200 |
1.22e-07 |
|
GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433019 [Multi-domain] Cd Length: 137 Bit Score: 51.70 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 52 ATSMESFYQGMHLHLQQLIPADNFYISLLDAQRQhLELPFFSDEKDSHPSELYPEQelseilmqGLTGYVLRTAKPLLCD 131
Cdd:pfam13185 1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGR-LAAWGGAADELSAALDDPPGE--------GLVGEALRTGRPVIVN 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 765523125 132 ERKAEELAAAGEimSLGSPCHQWLGVPIMQNDRAIGVLVVQSYNPAsSYGEMEFELMAFISHHIAGAME 200
Cdd:pfam13185 72 DLAADPAKKGLP--AGHAGLRSFLSVPLVSGGRVVGVLALGSNRPG-AFDEEDLELLELLAEQAAIAIE 137
|
|
| PtsP |
COG3605 |
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms]; |
241-421 |
6.09e-07 |
|
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
Pssm-ID: 442824 [Multi-domain] Cd Length: 188 Bit Score: 50.66 E-value: 6.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 241 KSLFEIAELSSSNLDDSEFYTELHRVLSHLLPANNCYIALLDDTATELHF-------PFYVSQLSdqppkcRPLMDGLVE 313
Cdd:COG3605 4 KALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELrateglnPEAVGKVR------LPLGEGLVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 314 YLLRLKRPVLLDqsDIQSlvcaKEIYSKAPELNH--TQSMhqwIGVPLFIQDRIAGALTIYSFSMHQnYQFKDLELLTFV 391
Cdd:COG3605 78 LVAERGEPLNLA--DAAS----HPRFKYFPETGEegFRSF---LGVPIIRRGRVLGVLVVQSREPRE-FTEEEVEFLVTL 147
|
170 180 190
....*....|....*....|....*....|
gi 765523125 392 SQHIATAIERKLATEALKRSNEELEEKILE 421
Cdd:COG3605 148 AAQLAEAIANAELLGELRAALAELSLAREE 177
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
66-199 |
2.65e-06 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 47.47 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 66 LQQLIPADNFYISLLDAQRQHLelpffsdekdsHPSELYPEQELSEILMQGLTGYVLRTAKPLLCDERKAEELAAAGEIM 145
Cdd:pfam01590 13 LRELLGADRCALYLPDADGLEY-----------LPPGARWLKAAGLEIPPGTGVTVLRTGRPLVVPDAAGDPRFLDPLLL 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 765523125 146 SLGSPCHQWLGVPIMQNDRAIGVLVVqsYNPASSYGEMEFELMAFISHHIAGAM 199
Cdd:pfam01590 82 LRNFGIRSLLAVPIIDDGELLGVLVL--HHPRPPFTEEELELLEVLADQVAIAL 133
|
|
| GAF |
pfam01590 |
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ... |
258-399 |
3.09e-06 |
|
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 460259 [Multi-domain] Cd Length: 133 Bit Score: 47.47 E-value: 3.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 258 EFYTELHRVLSHLLPANNCYIALLDDTATElhfpFYVSQLSDQPPKCRPLMDGLVEYLLRLKRPVLLDQsdiqslVCAKE 337
Cdd:pfam01590 4 EILQTILEELRELLGADRCALYLPDADGLE----YLPPGARWLKAAGLEIPPGTGVTVLRTGRPLVVPD------AAGDP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 765523125 338 IYSKAPELNHTQSMHQWIGVPLFIQDRIAGALTIYsfSMHQNYQFKDLELLTFVSQHIATAI 399
Cdd:pfam01590 74 RFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLH--HPRPPFTEEELELLEVLADQVAIAL 133
|
|
| FhlA |
COG3604 |
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ... |
353-441 |
8.56e-04 |
|
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 442823 [Multi-domain] Cd Length: 338 Bit Score: 42.53 E-value: 8.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 765523125 353 QWIGVPLFIQDRIAGALTIYSfSMHQNYQFKDLELLTFVSQHIATAIERKLAT----------EALKRSN---------- 412
Cdd:COG3604 75 LFLGVPLRVGGEVLGVLTLDS-RRPGAFSEEDLRLLETLASLAAVAILGETGTgkelvanaihELSPRADkpfvkvncaa 153
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 765523125 413 ------EELEEKILER----------TRELATTNQELQKEISQRR 441
Cdd:COG3604 154 lpesllESLQEGEFERvggdetikvdVRIIAATNRDLEEEVAEGR 198
|
|
| |
