|
Name |
Accession |
Description |
Interval |
E-value |
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
2-539 |
2.78e-60 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 223.33 E-value: 2.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 2 MRFLLVCVLMLCAMPSwASITDYVVKQWNIKDGLPSQSLKSVVQDQQGYMWVGTQFGLSRFDGTTFTNY--NTQNSPFLP 79
Cdd:COG3292 1 KRLLLLLLLLLLSLFA-QAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFrhDPGDPNSLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 80 SNGINKLLIDSNGYLWVGTKSGLVVINPQT-----LAAQEFNIKGPVRDILEDAKGSIWIA-ANGLYYVDRNQVDLRDKA 153
Cdd:COG3292 80 SNYIRALLEDSDGRLWIGTDGGLSRYDPKTdkftrYPLDPGLPNNSIRSIAEDSDGNIWVGtSNGLYRYDPKTGKFKRFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 154 NELVPIVNATVITQivGSVSQMALSPEG-IWLVNDRH-LLRLTKSASDFSKLRLELTAKvSLPERLAQTIVHDlsfLNGN 231
Cdd:COG3292 160 LDGLPSNTITSLAE--DADGNLWVDSDGnLWIGTDGNgLYRLDPNTGKFEHITHDPDPN-SLSSNSIYSLFED---REGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 232 LYLASEL-GAYFLDLDDE----LRPFPLPNANNSAVYKFMSDTNGG----LWVSTYGRLLFR--AKSGEWQWVEPSQLDQ 300
Cdd:COG3292 234 LWVGTYGgGLNYLDPNNSkfksYRHNDPNGLSGNSVRSIAEDSDGNlwirLWIGTYGGGLFRldPKTGKFKRYNPNGLPS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 301 SIWFAdIYRDSQNNIWLASFSEGLWL--AHEGRIERHSALSQMTEA-VMAISQAPDGNLWVANKSGIGYFDLN----KNF 373
Cdd:COG3292 314 NSVYS-ILEDSDGNLWIGTSGGGLYRydPKTGKFTKFSEDNGLSNNfIRSILEDSDGNLWVGTNGGLYRLDPKtgkfTNF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 374 VNKIPSAQFGRATVHDLQFDGS-RLYIAT-GRGLFFF--EQDKLYSFPGR-ALRDNPVFAISPSSKGGFWIGTGRGLYRL 448
Cdd:COG3292 393 THDPDKNGLSSNYINSIFEDSDgRLWIGTdGGGLYRYdpKTGKFKHFTTKdGLPSNTIYSILEDDNGNLWNFNSASNLGL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 449 SYGGLTPFAYNAFLGSKFITYVLDKANFGVIGTSKGAYYFTDRGIEKIGDQTSLESAYITSVLYIDGVGILIGSLNDGLF 528
Cdd:COG3292 473 LSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLTLLLLALLLLLSLLLLLLLLLLLLLLLLLLLLL 552
|
570
....*....|.
gi 1677595700 529 YRSLQGHWRQL 539
Cdd:COG3292 553 LLLLILLLLLL 563
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
697-989 |
6.94e-39 |
|
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: 146.28 E-value: 6.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 697 LSGLDSDWRYANARREAIYTNLPAGSFLFELEAKRQGEDWDRAQTVEYAFVVPQRFDETIYFRLLIVSGFILLFYFIFWV 776
Cdd:COG2199 2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 777 fRAQERRKQEVLEALVTERTLELRQANDklgqvnsQLKLVSHSDELTGLRSRRFLFDQLPKDIEHFQRNaqslqaqGKSL 856
Cdd:COG2199 82 -ELLLLLLALLLLLLALEDITELRRLEE-------RLRRLATHDPLTGLPNRRAFEERLERELARARRE-------GRPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 857 VLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDYVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFQ 936
Cdd:COG2199 147 ALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1677595700 937 LpNGKTTNITASLGWSFYPlpllgGQVISWETSINLADIALHQVKKRGGDGVA 989
Cdd:COG2199 227 L-EGKELRVTVSIGVALYP-----EDGDSAEELLRRADLALYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
818-989 |
1.80e-37 |
|
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: 138.07 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 818 HSDELTGLRSRRFLFDQLPKDIEHFQRnaqslqaQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSD 897
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARR-------SGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 898 YVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFqlPNGKTTNITASLGWSFYPlpllgGQVISWETSINLADIAL 977
Cdd:cd01949 74 LVARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFF--IDGQEIRVTASIGIATYP-----EDGEDAEELLRRADEAL 146
|
170
....*....|..
gi 1677595700 978 HQVKKRGGDGVA 989
Cdd:cd01949 147 YRAKRSGRNRVV 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
817-989 |
6.68e-32 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 121.97 E-value: 6.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 817 SHSDELTGLRSRRFLFDQLPKDIEHFQRnaqslqaQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGS 896
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRAQR-------QGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 897 DYVARWSGDEFLLLLRDfkCNmiDSYASDLCQAI--ALNSFQLPNGKTTNITASLGWSFYPLPllggqVISWETSINLAD 974
Cdd:smart00267 76 DLLARLGGDEFALLLPE--TS--LEEAIALAERIlqQLREPIIIHGIPLYLTISIGVAAYPNP-----GEDAEDLLKRAD 146
|
170
....*....|....*
gi 1677595700 975 IALHQVKKRGGDGVA 989
Cdd:smart00267 147 TALYQAKKAGRNQVA 161
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
817-986 |
1.48e-31 |
|
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: 121.21 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 817 SHSDELTGLRSRRFLFDQLPKDIEHFQRnaqslqaQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGS 896
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALR-------EGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 897 DYVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFQLP-NGKTTNITASLGWSFYPLPllgGQviSWETSINLADI 975
Cdd:pfam00990 74 DLVARLGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTvSGLPLYVTISIGIAAYPND---GE--DPEDLLKRADT 148
|
170
....*....|.
gi 1677595700 976 ALHQVKKRGGD 986
Cdd:pfam00990 149 ALYQAKQAGRN 159
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
820-988 |
8.77e-28 |
|
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: 110.50 E-value: 8.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 820 DELTGLRSRRFLFDQLPKDIEHFQRNaqslqaqGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDYV 899
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARRF-------QRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 900 ARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFQLPNGKTTNITASLGWSFYPlpllgGQVISWETSINLADIALHQ 979
Cdd:TIGR00254 78 GRYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYP-----GHGLTLEELLKRADEALYQ 152
|
....*....
gi 1677595700 980 VKKRGGDGV 988
Cdd:TIGR00254 153 AKKAGRNRV 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
778-984 |
1.19e-19 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 93.04 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 778 RAQERRK--QEVLEALVtERTLELrqandklgqvnsqlklvSHSDELTGLRSRRFlFDQlpkdieHFQRNAQSLQAQGKS 855
Cdd:PRK09581 269 RTQIRRKryQDALRNNL-EQSIEM-----------------AVTDGLTGLHNRRY-FDM------HLKNLIERANERGKP 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 856 LVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDYVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSF 935
Cdd:PRK09581 324 LSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPF 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1677595700 936 QLPNGKTT-NITASLGWSFYplpllGGQVISWETSINLADIALHQVKKRG 984
Cdd:PRK09581 404 IISDGKERlNVTVSIGVAEL-----RPSGDTIEALIKRADKALYEAKNTG 448
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
819-914 |
1.36e-07 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 55.35 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 819 SDELTGLRSRRFLFDQLPKDIehfqrnaQSLQAQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDY 898
Cdd:NF040885 343 SDSMTGLYNRKILTPTLEQRL-------QRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDY 415
|
90
....*....|....*.
gi 1677595700 899 VARWSGDEFLLLLRDF 914
Cdd:NF040885 416 GIRLGGDEFCIILIDY 431
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
2-539 |
2.78e-60 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 223.33 E-value: 2.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 2 MRFLLVCVLMLCAMPSwASITDYVVKQWNIKDGLPSQSLKSVVQDQQGYMWVGTQFGLSRFDGTTFTNY--NTQNSPFLP 79
Cdd:COG3292 1 KRLLLLLLLLLLSLFA-QAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFrhDPGDPNSLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 80 SNGINKLLIDSNGYLWVGTKSGLVVINPQT-----LAAQEFNIKGPVRDILEDAKGSIWIA-ANGLYYVDRNQVDLRDKA 153
Cdd:COG3292 80 SNYIRALLEDSDGRLWIGTDGGLSRYDPKTdkftrYPLDPGLPNNSIRSIAEDSDGNIWVGtSNGLYRYDPKTGKFKRFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 154 NELVPIVNATVITQivGSVSQMALSPEG-IWLVNDRH-LLRLTKSASDFSKLRLELTAKvSLPERLAQTIVHDlsfLNGN 231
Cdd:COG3292 160 LDGLPSNTITSLAE--DADGNLWVDSDGnLWIGTDGNgLYRLDPNTGKFEHITHDPDPN-SLSSNSIYSLFED---REGN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 232 LYLASEL-GAYFLDLDDE----LRPFPLPNANNSAVYKFMSDTNGG----LWVSTYGRLLFR--AKSGEWQWVEPSQLDQ 300
Cdd:COG3292 234 LWVGTYGgGLNYLDPNNSkfksYRHNDPNGLSGNSVRSIAEDSDGNlwirLWIGTYGGGLFRldPKTGKFKRYNPNGLPS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 301 SIWFAdIYRDSQNNIWLASFSEGLWL--AHEGRIERHSALSQMTEA-VMAISQAPDGNLWVANKSGIGYFDLN----KNF 373
Cdd:COG3292 314 NSVYS-ILEDSDGNLWIGTSGGGLYRydPKTGKFTKFSEDNGLSNNfIRSILEDSDGNLWVGTNGGLYRLDPKtgkfTNF 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 374 VNKIPSAQFGRATVHDLQFDGS-RLYIAT-GRGLFFF--EQDKLYSFPGR-ALRDNPVFAISPSSKGGFWIGTGRGLYRL 448
Cdd:COG3292 393 THDPDKNGLSSNYINSIFEDSDgRLWIGTdGGGLYRYdpKTGKFKHFTTKdGLPSNTIYSILEDDNGNLWNFNSASNLGL 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 449 SYGGLTPFAYNAFLGSKFITYVLDKANFGVIGTSKGAYYFTDRGIEKIGDQTSLESAYITSVLYIDGVGILIGSLNDGLF 528
Cdd:COG3292 473 LSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLTLLLLALLLLLSLLLLLLLLLLLLLLLLLLLLL 552
|
570
....*....|.
gi 1677595700 529 YRSLQGHWRQL 539
Cdd:COG3292 553 LLLLILLLLLL 563
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
697-989 |
6.94e-39 |
|
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: 146.28 E-value: 6.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 697 LSGLDSDWRYANARREAIYTNLPAGSFLFELEAKRQGEDWDRAQTVEYAFVVPQRFDETIYFRLLIVSGFILLFYFIFWV 776
Cdd:COG2199 2 LLLLLLLLALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 777 fRAQERRKQEVLEALVTERTLELRQANDklgqvnsQLKLVSHSDELTGLRSRRFLFDQLPKDIEHFQRNaqslqaqGKSL 856
Cdd:COG2199 82 -ELLLLLLALLLLLLALEDITELRRLEE-------RLRRLATHDPLTGLPNRRAFEERLERELARARRE-------GRPL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 857 VLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDYVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFQ 936
Cdd:COG2199 147 ALLLIDLDHFKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFE 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1677595700 937 LpNGKTTNITASLGWSFYPlpllgGQVISWETSINLADIALHQVKKRGGDGVA 989
Cdd:COG2199 227 L-EGKELRVTVSIGVALYP-----EDGDSAEELLRRADLALYRAKRAGRNRVV 273
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
818-989 |
1.80e-37 |
|
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: 138.07 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 818 HSDELTGLRSRRFLFDQLPKDIEHFQRnaqslqaQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSD 897
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARR-------SGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 898 YVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFqlPNGKTTNITASLGWSFYPlpllgGQVISWETSINLADIAL 977
Cdd:cd01949 74 LVARLGGDEFAILLPGTDLEEAEALAERLREAIEEPFF--IDGQEIRVTASIGIATYP-----EDGEDAEELLRRADEAL 146
|
170
....*....|..
gi 1677595700 978 HQVKKRGGDGVA 989
Cdd:cd01949 147 YRAKRSGRNRVV 158
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
817-989 |
6.68e-32 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 121.97 E-value: 6.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 817 SHSDELTGLRSRRFLFDQLPKDIEHFQRnaqslqaQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGS 896
Cdd:smart00267 3 AFRDPLTGLPNRRYFEEELEQELQRAQR-------QGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 897 DYVARWSGDEFLLLLRDfkCNmiDSYASDLCQAI--ALNSFQLPNGKTTNITASLGWSFYPLPllggqVISWETSINLAD 974
Cdd:smart00267 76 DLLARLGGDEFALLLPE--TS--LEEAIALAERIlqQLREPIIIHGIPLYLTISIGVAAYPNP-----GEDAEDLLKRAD 146
|
170
....*....|....*
gi 1677595700 975 IALHQVKKRGGDGVA 989
Cdd:smart00267 147 TALYQAKKAGRNQVA 161
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
817-986 |
1.48e-31 |
|
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: 121.21 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 817 SHSDELTGLRSRRFLFDQLPKDIEHFQRnaqslqaQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGS 896
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALR-------EGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 897 DYVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFQLP-NGKTTNITASLGWSFYPLPllgGQviSWETSINLADI 975
Cdd:pfam00990 74 DLVARLGGDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTvSGLPLYVTISIGIAAYPND---GE--DPEDLLKRADT 148
|
170
....*....|.
gi 1677595700 976 ALHQVKKRGGD 986
Cdd:pfam00990 149 ALYQAKQAGRN 159
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
700-999 |
3.70e-29 |
|
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: 124.89 E-value: 3.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 700 LDSDWRYANARREAIYTNLPAGSFLFELEAKRQGEDWDRAQTVEYAFVVPQRFDETIYFRLLIVSGFILLFYFIFWVFRA 779
Cdd:COG5001 134 AALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLL 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 780 QERRKQEVLEALVTERTLELRQANDKLGQVNSQLKLVSHSDELTGLRSRRFLFDQLPKDIEHFQRNaqslqaqGKSLVLL 859
Cdd:COG5001 214 LGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRS-------GRRLALL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 860 IINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDYVARWSGDEFLLLLRDFKCnmiDSYASDLCQAIaLNSFQLP- 938
Cdd:COG5001 287 FIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDD---PEDAEAVAERI-LAALAEPf 362
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1677595700 939 --NGKTTNITASLGWSFYPlpllgGQVISWETSINLADIALHQVKKRGGDGVAniTFDKQLDA 999
Cdd:COG5001 363 elDGHELYVSASIGIALYP-----DDGADAEELLRNADLAMYRAKAAGRNRYR--FFDPEMDE 418
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
820-988 |
8.77e-28 |
|
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: 110.50 E-value: 8.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 820 DELTGLRSRRFLFDQLPKDIEHFQRNaqslqaqGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDYV 899
Cdd:TIGR00254 5 DPLTGLYNRRYLEEMLDSELKRARRF-------QRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 900 ARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFQLPNGKTTNITASLGWSFYPlpllgGQVISWETSINLADIALHQ 979
Cdd:TIGR00254 78 GRYGGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSETLTVTVSIGVACYP-----GHGLTLEELLKRADEALYQ 152
|
....*....
gi 1677595700 980 VKKRGGDGV 988
Cdd:TIGR00254 153 AKKAGRNRV 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
778-984 |
1.19e-19 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 93.04 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 778 RAQERRK--QEVLEALVtERTLELrqandklgqvnsqlklvSHSDELTGLRSRRFlFDQlpkdieHFQRNAQSLQAQGKS 855
Cdd:PRK09581 269 RTQIRRKryQDALRNNL-EQSIEM-----------------AVTDGLTGLHNRRY-FDM------HLKNLIERANERGKP 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 856 LVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDYVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSF 935
Cdd:PRK09581 324 LSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEEFVVVMPDTDIEDAIAVAERIRRKIAEEPF 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1677595700 936 QLPNGKTT-NITASLGWSFYplpllGGQVISWETSINLADIALHQVKKRG 984
Cdd:PRK09581 404 IISDGKERlNVTVSIGVAEL-----RPSGDTIEALIKRADKALYEAKNTG 448
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
813-998 |
1.42e-19 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 90.51 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 813 LKLVSHSDELTGLRSRRFLFdqlpkdiEHFQRnaQSLQAQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSR 892
Cdd:PRK09894 125 LTIRSNMDVLTGLPGRRVLD-------ESFDH--QLRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASW 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 893 TQGSDYVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFQLPNGKtTNITASLGWSfyplplLGGQVISWETSINL 972
Cdd:PRK09894 196 TRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGR-INITATFGVS------RAFPEETLDVVIGR 268
|
170 180
....*....|....*....|....*.
gi 1677595700 973 ADIALHQVKKRGGDGVANItfDKQLD 998
Cdd:PRK09894 269 ADRAMYEGKQTGRNRVMFI--DEQNV 292
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
813-950 |
2.07e-14 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 78.18 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 813 LKLVSHS---DELTGLRSRRFlFDqlpkdiEHFQRNAQSLQAQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALL 889
Cdd:PRK09776 658 LRQLSYSashDALTHLANRAS-FE------KQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLM 730
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1677595700 890 NSRTQGSDYVARWSGDEFLLLLRDfkCNmIDSyASDLCQAI--ALNSFQLP-NGKTTNITASLG 950
Cdd:PRK09776 731 LSMLRSSDVLARLGGDEFGLLLPD--CN-VES-ARFIATRIisAINDYHFPwEGRVYRVGASAG 790
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
820-952 |
2.27e-12 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 70.81 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 820 DELTGLRSRRFLFDQlpkdiehFQRNAQSLQAQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDYV 899
Cdd:PRK15426 401 DPLTRLYNRGALFEK-------ARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQDVA 473
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1677595700 900 ARWSGDEFLLLLRDFKCNMIDSYASDLCQAIALNSFQLPNGKTTNITASLGWS 952
Cdd:PRK15426 474 GRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEILVAKSTTIRISASLGVS 526
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
801-984 |
7.31e-11 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 65.24 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 801 QANDKLGQVNSQLKLVSHSDELTGLRSRRFLFDQLPKDIEHFQRnaqslqaQGKSLVLLIINFDNFSRINDAYGPIAGDS 880
Cdd:PRK10245 189 QTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRR-------HHRDATLLIIDIDHFKSINDTWGHDVGDE 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 881 CLQQMAALLNSRTQGSDYVARWSGDEFLLLlrdfkcnMIDSYASDLCQAIA-----LNSFQLPNGKTTNITASLGWSfyP 955
Cdd:PRK10245 262 AIVALTRQLQITLRGSDVIGRFGGDEFAVI-------MSGTPAESAITAMSrvhegLNTLRLPNAPQVTLRISVGVA--P 332
|
170 180
....*....|....*....|....*....
gi 1677595700 956 LPLLGGQVISWETSinlADIALHQVKKRG 984
Cdd:PRK10245 333 LNPQMSHYREWLKS---ADLALYKAKNAG 358
|
|
| Y_Y_Y |
pfam07495 |
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a ... |
684-742 |
3.76e-10 |
|
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a family of two component regulators. However they are also found tandemly repeated in Swiss:Q891H4 without other signal conduction domains being present. It's named after the conserved tyrosines found in the alignment. The exact function is not known.
Pssm-ID: 400051 [Multi-domain] Cd Length: 65 Bit Score: 56.59 E-value: 3.76e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1677595700 684 DYYAPNSIEFRYKLSGLDSDWRYANARREAIYTNLPAGSFLFELEAKRQGEDWDRAQTV 742
Cdd:pfam07495 1 NYDGPENLLYRYRLEGFDGEWVELGDYSEASYTNLPPGKYTLKVKAKDNDGNWSYDDAS 59
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
798-983 |
9.06e-10 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 61.95 E-value: 9.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 798 ELRQANDKLGQVNSQLKLVSHSDELTGLRSR---RFLFDQLPKDiehfqRNAQSLQAqgkslvLLIINFDNFSRINDAYG 874
Cdd:PRK09966 229 EMEEWQLRLQAKNAQLLRTALHDPLTGLANRaafRSGINTLMNN-----SDARKTSA------LLFLDGDNFKYINDTWG 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 875 PIAGDSCLQQMAALLnSRTQGSDYVA-RWSGDEFLLLLRDFKCnmiDSYASDLCQAI--ALN-SFQLPNGKTTNITASLG 950
Cdd:PRK09966 298 HATGDRVLIEIAKRL-AEFGGLRHKAyRLGGDEFAMVLYDVQS---ESEVQQICSALtqIFNlPFDLHNGHQTTMTLSIG 373
|
170 180 190
....*....|....*....|....*....|....*...
gi 1677595700 951 WSfyplpllggqvISWETSI-----NLADIALHQVKKR 983
Cdd:PRK09966 374 YA-----------MTIEHASaeklqELADHNMYQAKHQ 400
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
813-910 |
9.83e-09 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 59.31 E-value: 9.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 813 LKLVSHSDELTGLRSRRFLFDQLPKDIEhfqrnaqslQAQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSR 892
Cdd:PRK10060 233 LRILANTDSITGLPNRNAIQELIDHAIN---------AADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLAILSC 303
|
90
....*....|....*...
gi 1677595700 893 TQGSDYVARWSGDEFLLL 910
Cdd:PRK10060 304 LEEDQTLARLGGDEFLVL 321
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
819-914 |
1.36e-07 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 55.35 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 819 SDELTGLRSRRFLFDQLPKDIehfqrnaQSLQAQGKSLVLLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSRTQGSDY 898
Cdd:NF040885 343 SDSMTGLYNRKILTPTLEQRL-------QRLTEKGIPVTFIALDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDY 415
|
90
....*....|....*.
gi 1677595700 899 VARWSGDEFLLLLRDF 914
Cdd:NF040885 416 GIRLGGDEFCIILIDY 431
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
788-987 |
3.17e-07 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 54.39 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 788 LEALVTERTlELRQANDKLGQVnsqlklvshsDELTGLRSRRFLFDQLPKdiehfqrnaqSLQAQgKSLVLLIINFDNFS 867
Cdd:PRK11359 358 LAALALEQE-KSRQHIEQLIQF----------DPLTGLPNRNNLHNYLDD----------LVDKA-VSPVVYLIGVDHFQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 868 RINDAYGPIAGDSCLQQMAALLNSRTQGSDYVARWSGDEFLLLLRDFKCNMIdSYASDLCQAIAlNSFQLPNGKTTNITA 947
Cdd:PRK11359 416 DVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNI-TQIADELRNVV-SKPIMIDDKPFPLTL 493
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1677595700 948 SLGWSFYplpllGGQviSWETSINLADIALHQVKKRGGDG 987
Cdd:PRK11359 494 SIGISYD-----VGK--NRDYLLSTAHNAMDYIRKNGGNG 526
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
86-321 |
5.80e-06 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 49.25 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 86 LLIDSNGYLWV-GTKSG-LVVINPQTLAAQEFNIKGP--VRDILEDAKGSIWIAANGLYYVDRnqVDLRDKANELVPivn 161
Cdd:COG4257 22 VAVDPDGAVWFtDQGGGrIGRLDPATGEFTEYPLGGGsgPHGIAVDPDGNLWFTDNGNNRIGR--IDPKTGEITTFA--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 162 atvITQIVGSVSQMALSPEG-IWlVNDRH---LLRLTKSASDFSklrleltaKVSLPERLAQTivHDLSF-LNGNLYLAs 236
Cdd:COG4257 97 ---LPGGGSNPHGIAFDPDGnLW-FTDQGgnrIGRLDPATGEVT--------EFPLPTGGAGP--YGIAVdPDGNLWVT- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 237 ELGA---YFLDLDD-ELRPFPLPNANNSAVYkFMSDTNGGLWVSTY--GRLL-FRAKSGEW-QWVEPSQLDQSIWfadIY 308
Cdd:COG4257 162 DFGAnaiGRIDPDTgTLTEYALPTPGAGPRG-LAVDPDGNLWVADTgsGRIGrFDPKTGTVtEYPLPGGGARPYG---VA 237
|
250
....*....|...
gi 1677595700 309 RDSQNNIWLASFS 321
Cdd:COG4257 238 VDGDGRVWFAESG 250
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
122-368 |
3.33e-05 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 46.94 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 122 RDILEDAKGSIWIAANGLYYVDRnqVDLRDKANELVPIVNATVITQIvgsvsqmALSPEG-IWLV--NDRHLLRLTKSAS 198
Cdd:COG4257 20 RDVAVDPDGAVWFTDQGGGRIGR--LDPATGEFTEYPLGGGSGPHGI-------AVDPDGnLWFTdnGNNRIGRIDPKTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 199 DFSklRLELTAKVSLPERLAqtiVHDlsflNGNLYLASELGAY--FLDLDD---ELRPFPLPNANNSAVykfMSDTNGGL 273
Cdd:COG4257 91 EIT--TFALPGGGSNPHGIA---FDP----DGNLWFTDQGGNRigRLDPATgevTEFPLPTGGAGPYGI---AVDPDGNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 274 WVSTYG--RLL-FRAKSGEWQWVE-PSQLDQ--SIWFadiyrDSQNNIWLASFSEGlWLAH----EGRIERHsALSQMTE 343
Cdd:COG4257 159 WVTDFGanAIGrIDPDTGTLTEYAlPTPGAGprGLAV-----DPDGNLWVADTGSG-RIGRfdpkTGTVTEY-PLPGGGA 231
|
250 260
....*....|....*....|....*..
gi 1677595700 344 AVMAISQAPDGNLWVANKSG--IGYFD 368
Cdd:COG4257 232 RPYGVAVDGDGRVWFAESGAnrIVRFD 258
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
43-143 |
2.16e-04 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 44.24 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 43 VVQDQQGYMWVGTQFG--LSRFDGTT--FTNYNTQNSPFLPsngiNKLLIDSNGYLWV--GTKSGLVVINPQTLAAQEFN 116
Cdd:COG4257 64 IAVDPDGNLWFTDNGNnrIGRIDPKTgeITTFALPGGGSNP----HGIAFDPDGNLWFtdQGGNRIGRLDPATGEVTEFP 139
|
90 100 110
....*....|....*....|....*....|...
gi 1677595700 117 IKGPV---RDILEDAKGSIWIA---ANGLYYVD 143
Cdd:COG4257 140 LPTGGagpYGIAVDPDGNLWVTdfgANAIGRID 172
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
897-979 |
1.30e-03 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 41.05 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 897 DYVARWSGDEFLLLLRDFKCNMIDSYASDLCQAIA-LNSFQlpngkttnITASLGwsfyplpllggqvISWETSINLADi 975
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAeLPSLR--------VTVSIG-------------VAGDSLLKRAD- 173
|
....
gi 1677595700 976 ALHQ 979
Cdd:COG3706 174 ALYQ 177
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
46-135 |
1.92e-03 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 41.16 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 46 DQQGYMWVgTQFGLS---RFDGTTftNYNTQNSPFLPSNGINKLLIDSNGYLWVG--TKSGLVVINPQTLAAQEFNIKGP 120
Cdd:COG4257 153 DPDGNLWV-TDFGANaigRIDPDT--GTLTEYALPTPGAGPRGLAVDPDGNLWVAdtGSGRIGRFDPKTGTVTEYPLPGG 229
|
90
....*....|....*...
gi 1677595700 121 VR---DILEDAKGSIWIA 135
Cdd:COG4257 230 GArpyGVAVDGDGRVWFA 247
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
858-911 |
2.83e-03 |
|
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: 38.88 E-value: 2.83e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1677595700 858 LLIINFDNFSRINDAYGPIAGDSCLQQMAALLNSR-TQGSDYVARWSGDEFLLLL 911
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLiRRSGDLKIKTIGDEFMVVS 58
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
247-440 |
4.35e-03 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 40.39 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 247 DELRPFPLPNANnSAVYKFMSDTNGGLWVSTY--GRLL-FRAKSGEWQWVEPSQL----------DQSIWFAD-----IY 308
Cdd:COG4257 5 VDITEYPVPAPG-SGPRDVAVDPDGAVWFTDQggGRIGrLDPATGEFTEYPLGGGsgphgiavdpDGNLWFTDngnnrIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 309 R-------------------------DSQNNIWLASFseglwlaHEGRIERHSALSQMTEAV---------MAISQAPDG 354
Cdd:COG4257 84 RidpktgeittfalpgggsnphgiafDPDGNLWFTDQ-------GGNRIGRLDPATGEVTEFplptggagpYGIAVDPDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1677595700 355 NLWVAN--KSGIGYFDLNKNFVNKIPS-AQFGRATVHDLQFDGsRLYIA-TGRGLFF-----FEQDKLYSFPGRALRdnP 425
Cdd:COG4257 157 NLWVTDfgANAIGRIDPDTGTLTEYALpTPGAGPRGLAVDPDG-NLWVAdTGSGRIGrfdpkTGTVTEYPLPGGGAR--P 233
|
250
....*....|....*
gi 1677595700 426 vFAISPSSKGGFWIG 440
Cdd:COG4257 234 -YGVAVDGDGRVWFA 247
|
|
| |
