|
Name |
Accession |
Description |
Interval |
E-value |
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
43-584 |
2.66e-84 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 292.28 E-value: 2.66e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 43 APPLRDYAIDVWTSRNGLPHNSLRDIAQTPEGHLWFATWEGLVRYNGLDFTVFDRSTR--PGLRDNGIGALLVDRQGGLW 120
Cdd:COG3292 16 AQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGdpNSLPSNYIRALLEDSDGRLW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 121 ISDSRGNVSHRGNDGQWRVWEHQADTPQVLIQSMQMDSQGRLWLLYEGkGIGYLTPDKGIVYQAPAADLPMAmSFTKLVV 200
Cdd:COG3292 96 IGTDGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDGNIWVGTSN-GLYRYDPKTGKFKRFTLDGLPSN-TITSLAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 201 DAQDRVWVgtldglvlrdndgvlkrapaawglgagtglswpyrapdgalwivagerlyrveddqlvlvhrlpgqlhmtsm 280
Cdd:COG3292 174 DADGNLWV------------------------------------------------------------------------ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 281 lqDRHGDLWLGTENQGLLRIS--AHGLERLPAGLN---LPGGRVVSLREDAEGSIWVG-ANGGLYRLRE--TLFSSY--T 350
Cdd:COG3292 182 --DSDGNLWIGTDGNGLYRLDpnTGKFEHITHDPDpnsLSSNSIYSLFEDREGNLWVGtYGGGLNYLDPnnSKFKSYrhN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 351 ERDGLSGDYVRTVLEDRDRQLWV-----GSASGLD-LQTPDGRFRavPLHNRGGKAPSVLSLAQGPDGDLWVGTFGDGVY 424
Cdd:COG3292 260 DPNGLSGNSVRSIAEDSDGNLWIrlwigTYGGGLFrLDPKTGKFK--RYNPNGLPSNSVYSILEDSDGNLWIGTSGGGLY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 425 RLDRDGSLRHNYAAADGMPGGNIRAISVDPQGRVWAGTQKGVVRIDGDRVQVST------APGMPGGLITALEHDHQGNL 498
Cdd:COG3292 338 RYDPKTGKFTKFSEDNGLSNNFIRSILEDSDGNLWVGTNGGLYRLDPKTGKFTNfthdpdKNGLSSNYINSIFEDSDGRL 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 499 WIGTiegirvlrgdhvqsidlapmgggrsvfgfhqlgeamwisSDRGLYRWR--DGKLARVGLEQGMPVDAVFQLVPDRL 576
Cdd:COG3292 418 WIGT---------------------------------------DGGGLYRYDpkTGKFKHFTTKDGLPSNTIYSILEDDN 458
|
....*...
gi 501456184 577 GNVWISSN 584
Cdd:COG3292 459 GNLWNFNS 466
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
742-1007 |
3.30e-63 |
|
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: 215.61 E-value: 3.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 742 LHVSAAHPGGAWGQQEAVWSFTVEPFWWQRRSVQLLGGLLLLAGLVVLYRLLLQQLKASNLRLARRVDEATFDLQAKTVH 821
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 822 LQALNQEKTELAERLARQAEAFERQAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIG 901
Cdd:COG2199 89 ALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 902 DAVLVQVARLIAAACRDSDLPARTGGEEFALLLNDTRLEEAAQLCARLRGLFHDHPDWAGVAGLRVTFSAGLVELDADDR 981
Cdd:COG2199 169 DEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGD 248
|
250 260
....*....|....*....|....*.
gi 501456184 982 TPALLYQRADRALYRAKSDGRDRTSI 1007
Cdd:COG2199 249 SAEELLRRADLALYRAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
850-1004 |
8.48e-60 |
|
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: 201.25 E-value: 8.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 850 DALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPARTGGEE 929
Cdd:cd01949 3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501456184 930 FALLLNDTRLEEAAQLCARLRGLFHDHPDWAGVaGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:cd01949 83 FAILLPGTDLEEAEALAERLREAIEEPFFIDGQ-EIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
845-1007 |
7.08e-49 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 170.51 E-value: 7.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 845 RQAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPAR 924
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 925 TGGEEFALLLNDTRLEEAAQLCARLRGLFHDHPDWAGVAgLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP-LYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 501456184 1005 TSI 1007
Cdd:smart00267 160 VAV 162
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
841-1004 |
2.27e-46 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 166.70 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 841 EAFERQAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSD 920
Cdd:NF038266 88 EALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 921 LPARTGGEEFALLLNDTRLEEAAQLCARLRGLFHDHPDWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSD 1000
Cdd:NF038266 168 LCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRA 247
|
....
gi 501456184 1001 GRDR 1004
Cdd:NF038266 248 GRDR 251
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
850-1004 |
4.13e-45 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 159.73 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 850 DALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPARTGGEE 929
Cdd:pfam00990 4 DPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGDE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501456184 930 FALLLNDTRLEEAAQLCARLRGLfHDH---PDWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:pfam00990 84 FAILLPETSLEGAQELAERIRRL-LAKlkiPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
846-1005 |
2.79e-42 |
|
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: 152.11 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 846 QAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPART 925
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 926 GGEEFALLLNDTRLEEAAQLCARLRGLFHDHP-DWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPiEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 501456184 1005 T 1005
Cdd:TIGR00254 161 V 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
850-1004 |
1.94e-39 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 152.75 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 850 DALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPARTGGEE 929
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501456184 930 FALLLNDTRLEEAAQLCARLRGLFHDHP--DWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIRRKIAEEPfiISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNR 451
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
434-672 |
1.39e-23 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 107.77 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 434 HNYAAADGMPGGNIRAISVDPQGRVWAGTQKGVVRIDGDRVQV-----STAPGMPGGLITALEHDHQGNLWIGTIEGIRV 508
Cdd:COG3292 25 RHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVfrhdpGDPNSLPSNYIRALLEDSDGRLWIGTDGGLSR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 509 L--RGDHVQSIDLAPMGGGRSVFGFHQLGE-AMWISSDRGLYRW--RDGKLARVGLEqGMPVDAVFQLVPDRLGNVWISS 583
Cdd:COG3292 105 YdpKTDKFTRYPLDPGLPNNSIRSIAEDSDgNIWVGTSNGLYRYdpKTGKFKRFTLD-GLPSNTITSLAEDADGNLWVDS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 584 N---------RGVLRTDMATLNavadgraprvvVERYNEIDgmaNAQANGSSGPSAILR-QDGTFWVVT-AGGLSTVDPQ 652
Cdd:COG3292 184 DgnlwigtdgNGLYRLDPNTGK-----------FEHITHDP---DPNSLSSNSIYSLFEdREGNLWVGTyGGGLNYLDPN 249
|
250 260
....*....|....*....|
gi 501456184 653 RLQRFRERPSPPAAIESVQV 672
Cdd:COG3292 250 NSKFKSYRHNDPNGLSGNSV 269
|
|
| Y_Y_Y |
pfam07495 |
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a ... |
701-765 |
4.75e-16 |
|
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: 73.16 E-value: 4.75e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501456184 701 SYLMSDRIRYRTRLEGLDAGWVERGPQRSVEFVGLPPGDYTLHVSAAHPGGAWGQQEAVWSFTVE 765
Cdd:pfam07495 1 NYDGPENLLYRYRLEGFDGEWVELGDYSEASYTNLPPGKYTLKVKAKDNDGNWSYDDASLNFTIL 65
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
309-476 |
3.84e-04 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 43.43 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 309 PAGLNLPGGRVVslreDAEGSIWVGANGGlYRLRE-----TLFSSYTERDGLSG--DYVRTVLEDRDRQLWVGSASGLDL 381
Cdd:cd14956 103 PGQFNAPRGVAV----DADGNLYVADFGN-QRIQKfdpdgSFLRQWGGTGIEPGsfNYPRGVAVDPDGTLYVADTYNDRI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 382 Q--TPDGRF-RAVPLHNRG-GKAPSVLSLAQGPDGDLWVGTFGDG-VYRLDRDGSLRHNYAAADGMPG--GNIRAISVDP 454
Cdd:cd14956 178 QvfDNDGAFlRKWGGRGTGpGQFNYPYGIAIDPDGNVFVADFGNNrIQKFTADGTFLTSWGSPGTGPGqfKNPWGVVVDA 257
|
170 180
....*....|....*....|..
gi 501456184 455 QGRVWagtqkgVVRIDGDRVQV 476
Cdd:cd14956 258 DGTVY------VADSNNNRVQR 273
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
43-584 |
2.66e-84 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 292.28 E-value: 2.66e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 43 APPLRDYAIDVWTSRNGLPHNSLRDIAQTPEGHLWFATWEGLVRYNGLDFTVFDRSTR--PGLRDNGIGALLVDRQGGLW 120
Cdd:COG3292 16 AQAAQQYRFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRHDPGdpNSLPSNYIRALLEDSDGRLW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 121 ISDSRGNVSHRGNDGQWRVWEHQADTPQVLIQSMQMDSQGRLWLLYEGkGIGYLTPDKGIVYQAPAADLPMAmSFTKLVV 200
Cdd:COG3292 96 IGTDGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDGNIWVGTSN-GLYRYDPKTGKFKRFTLDGLPSN-TITSLAE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 201 DAQDRVWVgtldglvlrdndgvlkrapaawglgagtglswpyrapdgalwivagerlyrveddqlvlvhrlpgqlhmtsm 280
Cdd:COG3292 174 DADGNLWV------------------------------------------------------------------------ 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 281 lqDRHGDLWLGTENQGLLRIS--AHGLERLPAGLN---LPGGRVVSLREDAEGSIWVG-ANGGLYRLRE--TLFSSY--T 350
Cdd:COG3292 182 --DSDGNLWIGTDGNGLYRLDpnTGKFEHITHDPDpnsLSSNSIYSLFEDREGNLWVGtYGGGLNYLDPnnSKFKSYrhN 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 351 ERDGLSGDYVRTVLEDRDRQLWV-----GSASGLD-LQTPDGRFRavPLHNRGGKAPSVLSLAQGPDGDLWVGTFGDGVY 424
Cdd:COG3292 260 DPNGLSGNSVRSIAEDSDGNLWIrlwigTYGGGLFrLDPKTGKFK--RYNPNGLPSNSVYSILEDSDGNLWIGTSGGGLY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 425 RLDRDGSLRHNYAAADGMPGGNIRAISVDPQGRVWAGTQKGVVRIDGDRVQVST------APGMPGGLITALEHDHQGNL 498
Cdd:COG3292 338 RYDPKTGKFTKFSEDNGLSNNFIRSILEDSDGNLWVGTNGGLYRLDPKTGKFTNfthdpdKNGLSSNYINSIFEDSDGRL 417
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 499 WIGTiegirvlrgdhvqsidlapmgggrsvfgfhqlgeamwisSDRGLYRWR--DGKLARVGLEQGMPVDAVFQLVPDRL 576
Cdd:COG3292 418 WIGT---------------------------------------DGGGLYRYDpkTGKFKHFTTKDGLPSNTIYSILEDDN 458
|
....*...
gi 501456184 577 GNVWISSN 584
Cdd:COG3292 459 GNLWNFNS 466
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
742-1007 |
3.30e-63 |
|
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: 215.61 E-value: 3.30e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 742 LHVSAAHPGGAWGQQEAVWSFTVEPFWWQRRSVQLLGGLLLLAGLVVLYRLLLQQLKASNLRLARRVDEATFDLQAKTVH 821
Cdd:COG2199 9 LALLLLLLLLLLSLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLVLLLLALGLLLLALLLLSLVLELLLLLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 822 LQALNQEKTELAERLARQAEAFERQAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIG 901
Cdd:COG2199 89 ALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHFKRINDTYGHAAG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 902 DAVLVQVARLIAAACRDSDLPARTGGEEFALLLNDTRLEEAAQLCARLRGLFHDHPDWAGVAGLRVTFSAGLVELDADDR 981
Cdd:COG2199 169 DEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTVSIGVALYPEDGD 248
|
250 260
....*....|....*....|....*.
gi 501456184 982 TPALLYQRADRALYRAKSDGRDRTSI 1007
Cdd:COG2199 249 SAEELLRRADLALYRAKRAGRNRVVV 274
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
850-1004 |
8.48e-60 |
|
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: 201.25 E-value: 8.48e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 850 DALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPARTGGEE 929
Cdd:cd01949 3 DPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGDE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501456184 930 FALLLNDTRLEEAAQLCARLRGLFHDHPDWAGVaGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:cd01949 83 FAILLPGTDLEEAEALAERLREAIEEPFFIDGQ-EIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNR 156
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
845-1007 |
7.08e-49 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 170.51 E-value: 7.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 845 RQAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPAR 924
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 925 TGGEEFALLLNDTRLEEAAQLCARLRGLFHDHPDWAGVAgLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIP-LYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
...
gi 501456184 1005 TSI 1007
Cdd:smart00267 160 VAV 162
|
|
| diguan_SiaD |
NF038266 |
biofilm regulation diguanylate cyclase SiaD; |
841-1004 |
2.27e-46 |
|
biofilm regulation diguanylate cyclase SiaD;
Pssm-ID: 468439 [Multi-domain] Cd Length: 252 Bit Score: 166.70 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 841 EAFERQAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSD 920
Cdd:NF038266 88 EALREASTRDPLTGLPNRRLLMERLREEVERARRSGRPFTLAMLDVDHFKRINDRYGHEVGDRVLVEIARTLRAELREYD 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 921 LPARTGGEEFALLLNDTRLEEAAQLCARLRGLFHDHPDWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSD 1000
Cdd:NF038266 168 LCGRWGGEEFLLLLPETGLEEAQVVLERLREAVRALAVRVGDDVLSVTASAGLAEHRPPEEGLSATLSRADQALYQAKRA 247
|
....
gi 501456184 1001 GRDR 1004
Cdd:NF038266 248 GRDR 251
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
850-1004 |
4.13e-45 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 159.73 E-value: 4.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 850 DALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPARTGGEE 929
Cdd:pfam00990 4 DPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLGGDE 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501456184 930 FALLLNDTRLEEAAQLCARLRGLfHDH---PDWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:pfam00990 84 FAILLPETSLEGAQELAERIRRL-LAKlkiPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
597-1004 |
4.30e-45 |
|
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: 173.81 E-value: 4.30e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 597 AVADGRAPRVVVERYNEIDGMANAQANGSSGPSAILRQDGTFWVVTAGGLSTVDPQRLQRFRERPSPPAAIESVQVDGAP 676
Cdd:COG5001 1 LLALAALLLLLLALLLALLLLALLLLALLLAALLALALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 677 VHWEGPDRNYIPGGRRLAVSYVGLSYLMSDRIRYRTRLEGLDAGWVERGPQRSVEFVGLPPGDYTLHVSAAHPGGAWGQQ 756
Cdd:COG5001 81 LLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALLLAAASAALLAAALGAALLAALALALLLALARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 757 EAVWSFTVEPFWWQRRSVQLLGGLLLLAGLVVLYRLLLQQLKASNLRLARRVDEATFDLQAKTVHLQALNQEKTELAERL 836
Cdd:COG5001 161 LLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRLALRLLLGLLLLGLLLLLLLVAVLAIARLITER 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 837 ARQAEAFERQAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAAC 916
Cdd:COG5001 241 KRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 917 RDSDLPARTGGEEFALLLNDTR-LEEAAQLCARLRGLFhDHPDWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRALY 995
Cdd:COG5001 321 REGDTVARLGGDEFAVLLPDLDdPEDAEAVAERILAAL-AEPFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMY 399
|
....*....
gi 501456184 996 RAKSDGRDR 1004
Cdd:COG5001 400 RAKAAGRNR 408
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
846-1005 |
2.79e-42 |
|
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: 152.11 E-value: 2.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 846 QAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPART 925
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 926 GGEEFALLLNDTRLEEAAQLCARLRGLFHDHP-DWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPiEVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
.
gi 501456184 1005 T 1005
Cdd:TIGR00254 161 V 161
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
850-1004 |
1.94e-39 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 152.75 E-value: 1.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 850 DALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPARTGGEE 929
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501456184 930 FALLLNDTRLEEAAQLCARLRGLFHDHP--DWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRALYRAKSDGRDR 1004
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIRRKIAEEPfiISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNR 451
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
850-1005 |
5.19e-38 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 144.44 E-value: 5.19e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 850 DALTGLANRRAFDETLARDfaRSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPARTGGEE 929
Cdd:PRK09894 132 DVLTGLPGRRVLDESFDHQ--LRNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEE 209
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 501456184 930 FALLLNDTRLEEAAQLCARLRGLFHDHPDWAGVAGLRVTFSAGLVELDAdDRTPALLYQRADRALYRAKSDGRDRT 1005
Cdd:PRK09894 210 FIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRAFP-EETLDVVIGRADRAMYEGKQTGRNRV 284
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
836-1004 |
2.77e-37 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 148.62 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 836 LARQaEAFERQAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAA 915
Cdd:PRK15426 388 FVLQ-SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSS 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 916 CRDSDLPARTGGEEFALLLNDTRLEEAAQLCARLRGLFHDHP-DWAGVAGLRVTFSAGLVELDAD-DRTPALLYQRADRA 993
Cdd:PRK15426 467 LRAQDVAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEiLVAKSTTIRISASLGVSSAEEDgDYDFEQLQSLADRR 546
|
170
....*....|.
gi 501456184 994 LYRAKSDGRDR 1004
Cdd:PRK15426 547 LYLAKQAGRNR 557
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
839-1007 |
4.77e-28 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 122.47 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 839 QAEAFERQ----AREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAA 914
Cdd:PRK09776 653 ESRKMLRQlsysASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLS 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 915 ACRDSDLPARTGGEEFALLLNDTRLEEAAQLCARLRGLFHDHP-DWAGVAgLRVTFSAGLVELDADDRTPALLYQRADRA 993
Cdd:PRK09776 733 MLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHfPWEGRV-YRVGASAGITLIDANNHQASEVMSQADIA 811
|
170
....*....|....
gi 501456184 994 LYRAKSDGRDRTSI 1007
Cdd:PRK09776 812 CYAAKNAGRGRVTV 825
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
434-672 |
1.39e-23 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 107.77 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 434 HNYAAADGMPGGNIRAISVDPQGRVWAGTQKGVVRIDGDRVQV-----STAPGMPGGLITALEHDHQGNLWIGTIEGIRV 508
Cdd:COG3292 25 RHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVfrhdpGDPNSLPSNYIRALLEDSDGRLWIGTDGGLSR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 509 L--RGDHVQSIDLAPMGGGRSVFGFHQLGE-AMWISSDRGLYRW--RDGKLARVGLEqGMPVDAVFQLVPDRLGNVWISS 583
Cdd:COG3292 105 YdpKTDKFTRYPLDPGLPNNSIRSIAEDSDgNIWVGTSNGLYRYdpKTGKFKRFTLD-GLPSNTITSLAEDADGNLWVDS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 584 N---------RGVLRTDMATLNavadgraprvvVERYNEIDgmaNAQANGSSGPSAILR-QDGTFWVVT-AGGLSTVDPQ 652
Cdd:COG3292 184 DgnlwigtdgNGLYRLDPNTGK-----------FEHITHDP---DPNSLSSNSIYSLFEdREGNLWVGTyGGGLNYLDPN 249
|
250 260
....*....|....*....|
gi 501456184 653 RLQRFRERPSPPAAIESVQV 672
Cdd:COG3292 250 NSKFKSYRHNDPNGLSGNSV 269
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
800-1005 |
1.78e-19 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 91.99 E-value: 1.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 800 SNLRLARRVDE---ATFDLQAKTvhLQALNQEKTELAERLARQAEAFERQAREDALTGLANRRAF----DETLARDFARS 872
Cdd:PRK09966 200 SNRNFSRRVSEeriAEFHRFALD--FNSLLDEMEEWQLRLQAKNAQLLRTALHDPLTGLANRAAFrsgiNTLMNNSDARK 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 873 QRSghplcLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAACRDSDLPARTGGEEFALLLNDTRLE-EAAQLCARLRG 951
Cdd:PRK09966 278 TSA-----LLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSEsEVQQICSALTQ 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 501456184 952 LFHDHPDWAGVAGLRVTFSAGLVeLDADDRTPALLYQRADRALYRAKSDGRDRT 1005
Cdd:PRK09966 353 IFNLPFDLHNGHQTTMTLSIGYA-MTIEHASAEKLQELADHNMYQAKHQRAEKL 405
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
831-1007 |
1.88e-19 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 91.43 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 831 ELAERLARQAEAFERQAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVAR 910
Cdd:PRK10245 189 QTATKLAEHKRRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 911 LIAAACRDSDLPARTGGEEFALLLNDTRLEEAAQLCARL-RGLfhDHPDWAGVAGLRVTFSAGLVELdaddrTPALLYQR 989
Cdd:PRK10245 269 QLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAMSRVhEGL--NTLRLPNAPQVTLRISVGVAPL-----NPQMSHYR 341
|
170 180
....*....|....*....|...
gi 501456184 990 -----ADRALYRAKSDGRDRTSI 1007
Cdd:PRK10245 342 ewlksADLALYKAKNAGRNRTEV 364
|
|
| Y_Y_Y |
pfam07495 |
Y_Y_Y domain; This domain is mostly found at the end of the beta propellers (pfam07494) in a ... |
701-765 |
4.75e-16 |
|
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: 73.16 E-value: 4.75e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 501456184 701 SYLMSDRIRYRTRLEGLDAGWVERGPQRSVEFVGLPPGDYTLHVSAAHPGGAWGQQEAVWSFTVE 765
Cdd:pfam07495 1 NYDGPENLLYRYRLEGFDGEWVELGDYSEASYTNLPPGKYTLKVKAKDNDGNWSYDDASLNFTIL 65
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
830-1002 |
5.14e-15 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 79.73 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 830 TElaERLARqaEAFERQAREDALTGLANRRAFDETLarDFARSQRSGHPLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVA 909
Cdd:PRK10060 224 TE--ERRAQ--ERLRILANTDSITGLPNRNAIQELI--DHAINAADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVS 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 910 RLIAAACRDSDLPARTGGEEFALLLNDTR---LEEAAQ-LCARLRglfhdHPdwagvaglrvtFSAGLVEL--------- 976
Cdd:PRK10060 298 LAILSCLEEDQTLARLGGDEFLVLASHTSqaaLEAMASrILTRLR-----LP-----------FRIGLIEVytgcsigia 361
|
170 180 190
....*....|....*....|....*....|
gi 501456184 977 ----DADDRTPalLYQRADRALYRAKSDGR 1002
Cdd:PRK10060 362 lapeHGDDSES--LIRSADTAMYTAKEGGR 389
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
233-472 |
1.36e-14 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 75.06 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 233 GAGTGLSWPYRAPDGALWIV--AGERLYRVE-DDQLVLVHRLPGQLHMTSMLQDRHGDLWLGTENQG-LLRISAHGLE-- 306
Cdd:COG4257 14 APGSGPRDVAVDPDGAVWFTdqGGGRIGRLDpATGEFTEYPLGGGSGPHGIAVDPDGNLWFTDNGNNrIGRIDPKTGEit 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 307 --RLPAGLNLPGGRVVslreDAEGSIWV--GANGGLYRLRE-----TLFSSYTERDGLSGdyvrtVLEDRDRQLWVGSAS 377
Cdd:COG4257 94 tfALPGGGSNPHGIAF----DPDGNLWFtdQGGNRIGRLDPatgevTEFPLPTGGAGPYG-----IAVDPDGNLWVTDFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 378 G-----LDLQTpdGRFRAVPLHNRGGkAPSvlSLAQGPDGDLWVGTFGDG-VYRLD-RDGSLRHnYAaadgMPGGNIR-- 448
Cdd:COG4257 165 AnaigrIDPDT--GTLTEYALPTPGA-GPR--GLAVDPDGNLWVADTGSGrIGRFDpKTGTVTE-YP----LPGGGARpy 234
|
250 260
....*....|....*....|....*.
gi 501456184 449 AISVDPQGRVWAGTQKG--VVRIDGD 472
Cdd:COG4257 235 GVAVDGDGRVWFAESGAnrIVRFDPD 260
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
51-182 |
3.11e-13 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 74.26 E-value: 3.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 51 IDVWTSRNGLPHNSLRDIAQTPEGHLWFATWEGLVRYNGLD--FTVFDRSTRP-GLRDNGIGALLVDRQGGLWISDSRGN 127
Cdd:COG3292 346 FTKFSEDNGLSNNFIRSILEDSDGNLWVGTNGGLYRLDPKTgkFTNFTHDPDKnGLSSNYINSIFEDSDGRLWIGTDGGG 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 501456184 128 VSH-RGNDGQWRVWEHQADTPQVLIQSMQMDSQGRLWLLYEGKGIGYLTPDKGIVY 182
Cdd:COG3292 426 LYRyDPKTGKFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSASNLGLLSLLGGLLG 481
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
819-1001 |
2.35e-12 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 71.34 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 819 TVHLQALNQEKTELAERLarqaeafERQAREDALTGLANR----RAFDETLARDfarsqrsgHPLCLVVLDIDHFKDVND 894
Cdd:PRK11359 355 SQHLAALALEQEKSRQHI-------EQLIQFDPLTGLPNRnnlhNYLDDLVDKA--------VSPVVYLIGVDHFQDVID 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 895 RHSHSIGDAVLVQVARLIAAACRDSDLPARTGGEEFALLLNDTRLEEAAQLCARLRG------LFHDHPdwagvagLRVT 968
Cdd:PRK11359 420 SLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNvvskpiMIDDKP-------FPLT 492
|
170 180 190
....*....|....*....|....*....|....
gi 501456184 969 FSAGLVELDADDRTpaLLYQRADRAL-YRAKSDG 1001
Cdd:PRK11359 493 LSIGISYDVGKNRD--YLLSTAHNAMdYIRKNGG 524
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
920-998 |
3.56e-12 |
|
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: 66.09 E-value: 3.56e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 501456184 920 DLPARTGGEEFALLLNDTRLEEAAQLCARLRGLFHDHPDwagvagLRVTFSAGLVELDaddrtpalLYQRADrALYRAK 998
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPS------LRVTVSIGVAGDS--------LLKRAD-ALYQAR 179
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
308-510 |
3.58e-11 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 65.04 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 308 LPAGLNLPGGRVVslreDAEGSIWVGANGGLYRLRETLFS-SYTERDGLSGDYVRTVLEDRDRQLWVGSASG-----LDl 381
Cdd:COG4257 12 VPAPGSGPRDVAV----DPDGAVWFTDQGGGRIGRLDPATgEFTEYPLGGGSGPHGIAVDPDGNLWFTDNGNnrigrID- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 382 qTPDGRFRAVPLhNRGGKAPSvlSLAQGPDGDLWV-GTFGDGVYRLD-RDGSLR-HNYAAADGMPGGniraISVDPQGRV 458
Cdd:COG4257 87 -PKTGEITTFAL-PGGGSNPH--GIAFDPDGNLWFtDQGGNRIGRLDpATGEVTeFPLPTGGAGPYG----IAVDPDGNL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 501456184 459 WAGTQKG--VVRIDGDRVQVSTAPGM-PGGLITALEHDHQGNLWIGTIEGIRVLR 510
Cdd:COG4257 159 WVTDFGAnaIGRIDPDTGTLTEYALPtPGAGPRGLAVDPDGNLWVADTGSGRIGR 213
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
66-291 |
2.48e-10 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 62.34 E-value: 2.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 66 RDIAQTPEGHLWFA-TWEGLVRyngldftVFDRST-----RPGLRDNGIGALLVDRQGGLWISDSRGNVSHRGNDGQWRV 139
Cdd:COG4257 20 RDVAVDPDGAVWFTdQGGGRIG-------RLDPATgefteYPLGGGSGPHGIAVDPDGNLWFTDNGNNRIGRIDPKTGEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 140 WEHQADTPQVLIQSMQMDSQGRLWL-LYEGKGIGYLTPDKGIV--YQAPAAD-LPMAMsftklVVDAQDRVWVGTLDGLV 215
Cdd:COG4257 93 TTFALPGGGSNPHGIAFDPDGNLWFtDQGGNRIGRLDPATGEVteFPLPTGGaGPYGI-----AVDPDGNLWVTDFGANA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 216 LR---DNDGVLKRAPAAWGLGAGTGLSWpyrAPDGALWIV--AGERLYRVE-DDQLVLVHRLPGQLHM-TSMLQDRHGDL 288
Cdd:COG4257 168 IGridPDTGTLTEYALPTPGAGPRGLAV---DPDGNLWVAdtGSGRIGRFDpKTGTVTEYPLPGGGARpYGVAVDGDGRV 244
|
...
gi 501456184 289 WLG 291
Cdd:COG4257 245 WFA 247
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
57-141 |
1.16e-09 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 62.70 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 57 RNGLPHNSLRDIAQTPEGHLWFATWE-GLVRYNGLD--FTVFdrSTRPGLRDNGIGALLVDRQGGLWISDSRGNVSHRGN 133
Cdd:COG3292 398 KNGLSSNYINSIFEDSDGRLWIGTDGgGLYRYDPKTgkFKHF--TTKDGLPSNTIYSILEDDNGNLWNFNSASNLGLLSL 475
|
....*...
gi 501456184 134 DGQWRVWE 141
Cdd:COG3292 476 LGGLLGGL 483
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
325-519 |
2.78e-09 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 59.14 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 325 DAEGSIWVG--ANGGLYRLRET--LFSSYTERDGLSGdyvrTVLEDRDRQLWVGSASG--LDLQTPDGRFRavPLHNRGG 398
Cdd:COG3386 16 DPDGRLYWVdiPGGRIHRYDPDggAVEVFAEPSGRPN----GLAFDPDGRLLVADHGRglVRFDPADGEVT--VLADEYG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 399 KAPSVLS-LAQGPDGDLWVGTFGD-----GVYRLDRDGSLRhnyAAADGMPGGNirAISVDPQGRV--WAGTQKGVVR-- 468
Cdd:COG3386 90 KPLNRPNdGVVDPDGRLYFTDMGEylptgALYRVDPDGSLR---VLADGLTFPN--GIAFSPDGRTlyVADTGAGRIYrf 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 501456184 469 -IDGDR--------VQVSTAPGMPGGLITalehDHQGNLWIGTIEGIRVLR----GDHVQSIDL 519
Cdd:COG3386 165 dLDADGtlgnrrvfADLPDGPGGPDGLAV----DADGNLWVALWGGGGVVRfdpdGELLGRIEL 224
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
878-998 |
1.01e-08 |
|
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways.
Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 54.67 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 878 PLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAAC-RDSDLPARTGGEEFALLLNDTRLEEAAQLCARLRGLFH-- 954
Cdd:cd07556 1 PVTILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSal 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 501456184 955 DHPDWAGVAgLRVTFSAGLVELDADDRTPAL-----LYQRADRALYRAK 998
Cdd:cd07556 81 NQSEGNPVR-VRIGIHTGPVVVGVIGSRPQYdvwgaLVNLASRMESQAK 128
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
404-662 |
2.71e-08 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 56.18 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 404 LSLAQGPDGDLWV-GTFGDGVYRLD-RDGSLRHNYAAADGMPggniRAISVDPQGRVWAGTQKG--VVRIDGDRVQVSTA 479
Cdd:COG4257 20 RDVAVDPDGAVWFtDQGGGRIGRLDpATGEFTEYPLGGGSGP----HGIAVDPDGNLWFTDNGNnrIGRIDPKTGEITTF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 480 PgMPGG--LITALEHDHQGNLWIGTIEGIRVLRgdhvqsIDLApmGGGRSVFGfhqlgeamwissdrglyrwrdgklarV 557
Cdd:COG4257 96 A-LPGGgsNPHGIAFDPDGNLWFTDQGGNRIGR------LDPA--TGEVTEFP--------------------------L 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 558 GLEQGMPvdavFQLVPDRLGNVWISSNRG--VLRTDMATLNAV-----ADGRAPR----------VVVE-------RYNE 613
Cdd:COG4257 141 PTGGAGP----YGIAVDPDGNLWVTDFGAnaIGRIDPDTGTLTeyalpTPGAGPRglavdpdgnlWVADtgsgrigRFDP 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 501456184 614 IDGMAN--AQANGSSGPSAI-LRQDGTFWVVTAGG--LSTVDPQRLQRFRERPS 662
Cdd:COG4257 217 KTGTVTeyPLPGGGARPYGVaVDGDGRVWFAESGAnrIVRFDPDTELTEYVLPS 270
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
228-490 |
7.43e-08 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 54.90 E-value: 7.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 228 AAWGLGAGTGLSWpyrAPDGALWIV--AGERLYRV-EDDQLVLVHRLPGQLHmTSMLQDRHGDLWLGTENQGLLRISAHG 304
Cdd:COG3386 3 ADAGFRLGEGPVW---DPDGRLYWVdiPGGRIHRYdPDGGAVEVFAEPSGRP-NGLAFDPDGRLLVADHGRGLVRFDPAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 305 --LERLPAGLNLPGGRVVSLREDAEGSIWVG------ANGGLYRLRetlfssyteRDGLsgdyVRTVLEDrdrqlwVGSA 376
Cdd:COG3386 79 geVTVLADEYGKPLNRPNDGVVDPDGRLYFTdmgeylPTGALYRVD---------PDGS----LRVLADG------LTFP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 377 SGLDLqTPDGRfravplhnrggkapsVLSLAQGPDGDLWvgtfgdgVYRLDRDGSLRHNYAAADGMPG-GNIRAISVDPQ 455
Cdd:COG3386 140 NGIAF-SPDGR---------------TLYVADTGAGRIY-------RFDLDADGTLGNRRVFADLPDGpGGPDGLAVDAD 196
|
250 260 270
....*....|....*....|....*....|....*..
gi 501456184 456 GRVWAGT--QKGVVRIDGDRVQVSTAPgMPGGLITAL 490
Cdd:COG3386 197 GNLWVALwgGGGVVRFDPDGELLGRIE-LPERRPTNV 232
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
112-342 |
3.10e-07 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 52.97 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 112 LVDRQGGLWISDSRGN--VSHRGNDGQWRVWehqaDTPQVLIQSMQMDSQGRLWLLYEGKGIGYLTPDKG-IVYQAPAAD 188
Cdd:COG3386 14 VWDPDGRLYWVDIPGGriHRYDPDGGAVEVF----AEPSGRPNGLAFDPDGRLLVADHGRGLVRFDPADGeVTVLADEYG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 189 LPMaMSFTKLVVDAQDRVWVGTLD------GLVLRDNDGVLKRapAAWGLGAGTGLSWpyrAPDGALWIVA---GERLYR 259
Cdd:COG3386 90 KPL-NRPNDGVVDPDGRLYFTDMGeylptgALYRVDPDGSLRV--LADGLTFPNGIAF---SPDGRTLYVAdtgAGRIYR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 260 V---EDDQL----VLVHRLPGQLHMTSMLQDRHGDLWLGT-ENQGLLRISAHG--LERLPaglnLPGGRVVSLREDAEG- 328
Cdd:COG3386 164 FdldADGTLgnrrVFADLPDGPGGPDGLAVDADGNLWVALwGGGGVVRFDPDGelLGRIE----LPERRPTNVAFGGPDl 239
|
250 260
....*....|....*....|.
gi 501456184 329 -SIWVGAN------GGLYRLR 342
Cdd:COG3386 240 rTLYVTTArslplaGALFRVR 260
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
836-1004 |
7.93e-05 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 46.47 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 836 LARQAEAFERQAREDALTGLANRRAFDETLARDFARSQRSGHpLCLVVLDIDHFKDVNDRHSHSIGDAVLVQVARLIAAA 915
Cdd:PRK11829 221 LADAYADMGRISHRFPVTELPNRSLFISLLEKEIASSTRTDH-FHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQC 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 916 CRDSDLPARTGGEEFALLLNDT-RLEEAAQLCARLRGLFhDHPDWAGVAGLRVTFSAGLVELDADDRTPALLYQRADRAL 994
Cdd:PRK11829 300 IDDSDLLAQLSKTEFAVLARGTrRSFPAMQLARRIMSQV-TQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAM 378
|
170
....*....|
gi 501456184 995 YRAKSDGRDR 1004
Cdd:PRK11829 379 MAAHHEGRNQ 388
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
823-949 |
3.70e-04 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 44.47 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 823 QALNQEKTELAErlARQAEA----FER-QAREDALTGLANRRAFDETLARDFARSQRSGHPLCLVVLDIDHFKDVNDRHS 897
Cdd:PRK11059 201 RALDHLLSELQD--AREERSrfdtFIRsNAFQDAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWG 278
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 501456184 898 HSIGDAVLVQVARLIAAACRD--SDLPARTGGEEFALLLNDTRLEEAAQLCARL 949
Cdd:PRK11059 279 ESQVEELLFELINLLSTFVMRypGALLARYSRSDFAVLLPHRSLKEADSLASQL 332
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
309-476 |
3.84e-04 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 43.43 E-value: 3.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 309 PAGLNLPGGRVVslreDAEGSIWVGANGGlYRLRE-----TLFSSYTERDGLSG--DYVRTVLEDRDRQLWVGSASGLDL 381
Cdd:cd14956 103 PGQFNAPRGVAV----DADGNLYVADFGN-QRIQKfdpdgSFLRQWGGTGIEPGsfNYPRGVAVDPDGTLYVADTYNDRI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 382 Q--TPDGRF-RAVPLHNRG-GKAPSVLSLAQGPDGDLWVGTFGDG-VYRLDRDGSLRHNYAAADGMPG--GNIRAISVDP 454
Cdd:cd14956 178 QvfDNDGAFlRKWGGRGTGpGQFNYPYGIAIDPDGNVFVADFGNNrIQKFTADGTFLTSWGSPGTGPGqfKNPWGVVVDA 257
|
170 180
....*....|....*....|..
gi 501456184 455 QGRVWagtqkgVVRIDGDRVQV 476
Cdd:cd14956 258 DGTVY------VADSNNNRVQR 273
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
94-252 |
5.69e-04 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 43.04 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 94 VFDRSTRPGLRDNGIGA----------LLVDRQGGLWISDSRGNVSHR-GNDGQW-RVWEHQADTPQVL--IQSMQMDSQ 159
Cdd:cd14956 38 VFDKDGTFLRRFGTTGDgpgqfgrprgLAVDKDGWLYVADYWGDRIQVfTLTGELqTIGGSSGSGPGQFnaPRGVAVDAD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 160 GRLWLL-YEGKGIGYLTPDKGIVYQAPAADLPmAMSF---TKLVVDAQDRVWV--GTLDGLVLRDNDGVLKRapaAWG-L 232
Cdd:cd14956 118 GNLYVAdFGNQRIQKFDPDGSFLRQWGGTGIE-PGSFnypRGVAVDPDGTLYVadTYNDRIQVFDNDGAFLR---KWGgR 193
|
170 180
....*....|....*....|....
gi 501456184 233 GAGTG-LSWPYR---APDGALWIV 252
Cdd:cd14956 194 GTGPGqFNYPYGiaiDPDGNVFVA 217
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
59-181 |
1.10e-03 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 41.93 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501456184 59 GLPHNSLRDIAQTPEGHLWFATWEG--LVRYN--GLDFTVFDRSTrPGLRDNGIGallVDRQGGLWISDSRGNVSHR--G 132
Cdd:COG4257 141 PTGGAGPYGIAVDPDGNLWVTDFGAnaIGRIDpdTGTLTEYALPT-PGAGPRGLA---VDPDGNLWVADTGSGRIGRfdP 216
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501456184 133 NDGQWRVWEhqADTPQVLIQSMQMDSQGRLWLLYEGKG-IGYLTPDKGIV 181
Cdd:COG4257 217 KTGTVTEYP--LPGGGARPYGVAVDGDGRVWFAESGANrIVRFDPDTELT 264
|
|
| |
