|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
877-1498 |
0e+00 |
|
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: 573.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 877 ALIHPDDKRQLSLDWAAFLEQKNQQQWQATYRLKHALGHWLWYQDIGEVIETDENKKPIRVSGIYTNITESRATAQQAAV 956
Cdd:COG5001 47 LALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 957 LGEAFSQINDWLLILDHQLLPFSVNNSFADAFSVDSSPATLNLKGFLAALGKQQYADYIKILNSLKPRQNWRGDAYIKTR 1036
Cdd:COG5001 127 LLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1037 TNPSHPIHISITAVAKDSDFVSYYVVVISDLTEQKRAENELRYLANYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALL 1116
Cdd:COG5001 207 RLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1117 FIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQSGDEFLLLVNNLNSPQALSAQVKALTIELAKRVVIDD 1196
Cdd:COG5001 287 FIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1197 FAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNGFKFFTEQMNDQITQKLLLENALKDAFKDDLLFNNYQPI 1276
Cdd:COG5001 367 HELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQ 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1277 VNVKSKKIKGVELLMRWQH-EGQFISPAKFIPIAEETGLIDVLTEQALSRALKELAPLLRA-NPRFYLSLNLSPVHILKS 1354
Cdd:COG5001 447 VDLATGRIVGAEALLRWQHpERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAgLPDLRVAVNLSARQLRDP 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1355 NLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTGYSSLTYLNQFPIDVIKIDQSFV 1434
Cdd:COG5001 527 DLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFV 606
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2741887859 1435 RKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARPITADKLL 1498
Cdd:COG5001 607 RDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELE 670
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
1066-1497 |
5.08e-102 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 341.66 E-value: 5.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1066 DLTEQKRAENELRYLANYDPLTKLPNRTLMYQKINRAIKDADKRQTlsALLFIDLDKFKPVNDSFGHAVGDQLLCDITQR 1145
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQV--GIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1146 VNAMLDSDGVLGRQSGDEFLLLVNNlNSPQALSAQVKALTIELAKRVVIDDFAINISASIGVALYPFDAKTADQLIRHAD 1225
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASH-TSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1226 IAMMHAKQSGRNGFKFFTEQMNDQITQKLLLENALKDAFKDDLLFNNYQPIVNVkSKKIKGVELLMRWQH-EGQFISPAK 1304
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSpERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1305 FIPIAEETGLIDVLTEQALSRALKELAPLLRANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLL 1384
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLI 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1385 DDKNKAAKQLQTLRNAGFKLLLDDFGTGYSSLTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAE 1464
Cdd:PRK10060 538 ENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAE 617
|
410 420 430
....*....|....*....|....*....|...
gi 2741887859 1465 GVETIEQIRFLNRIGCYDLQGYYFARPITADKL 1497
Cdd:PRK10060 618 GVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
1258-1495 |
3.06e-94 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 304.08 E-value: 3.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1258 NALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRWQH-EGQFISPAKFIPIAEETGLIDVLTEQALSRALKELAPLLRA 1336
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1337 NPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTGYSSL 1416
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741887859 1417 TYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARPITAD 1495
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
1257-1495 |
2.94e-81 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 267.16 E-value: 2.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1257 ENALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRWQH-EGQFISPAKFIPIAEETGLIDVLTEQALSRALKELAPLL- 1334
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1335 RANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTGYS 1414
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1415 SLTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARPITA 1494
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
.
gi 2741887859 1495 D 1495
Cdd:smart00052 241 D 241
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
1257-1491 |
6.90e-69 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 231.44 E-value: 6.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1257 ENALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRWQH-EGQFISPAKFIPIAEETGLIDVLTEQALSRALKELApLLR 1335
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA-QLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1336 ANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTGYSS 1415
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741887859 1416 LTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARP 1491
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
8-637 |
2.07e-44 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 175.56 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 8 FILFALLCILYSTTSHAQNYalQLQRLSPDEGLSQGYVTNTLQDHLGFVWIGTKQGLNRFDGYQVKTFT----GEQGLDQ 83
Cdd:COG3292 3 LLLLLLLLLLSLFAQAAQQY--RFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRhdpgDPNSLPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 84 ASILFLFATESDEIFVSTeysgaflinpvtlvtrkvysgklseedkryspinavkqrgtlfyyaiNDHVYTFDSKHSTFT 163
Cdd:COG3292 81 NYIRALLEDSDGRLWIGT-----------------------------------------------DGGLSRYDPKTDKFT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 164 H-TFSINKPEHLVRALTI-HNNFIYIATSNGLYSKSLIDDHITKIPLLSKdklneDNNNIKFLHVDPQLGLMVgtvegfy 241
Cdd:COG3292 114 RyPLDPGLPNNSIRSIAEdSDGNIWVGTSNGLYRYDPKTGKFKRFTLDGL-----PSNTITSLAEDADGNLWV------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 242 sislDKNsqfdfaniktliphHNIWdyINTpfgefvvTQDGLYQYDRHTNQsLFILRFDQSKFNMTDNTILDVMVDKTGL 321
Cdd:COG3292 182 ----DSD--------------GNLW--IGT-------DGNGLYRLDPNTGK-FEHITHDPDPNSLSSNSIYSLFEDREGN 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 322 MWLASRSQGVFTWSTFARRFNNIEITSRDKLHSNVVLSVFQDDTN----ALWLGT-NNGLTRINEKAGITKTYlatadTK 396
Cdd:COG3292 234 LWVGTYGGGLNYLDPNNSKFKSYRHNDPNGLSGNSVRSIAEDSDGnlwiRLWIGTyGGGLFRLDPKTGKFKRY-----NP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 397 AFYGQYSVYGIAPAELNEpnrfLWL-LLYNGLALFDKQTEQLLP-TPMQGITQNILTegptygyyqiqtdtfaffsekdf 474
Cdd:COG3292 309 NGLPSNSVYSILEDSDGN----LWIgTSGGGLYRYDPKTGKFTKfSEDNGLSNNFIR----------------------- 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 475 YIYDGKTGNTrpirglkeqldpinvhrflkplntypddhLISVSGALYRYNEKRERLTLLYEVKNYNPLSYITIDDWVLD 554
Cdd:COG3292 362 SILEDSDGNL-----------------------------WVGTNGGLYRLDPKTGKFTNFTHDPDKNGLSSNYINSIFED 412
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 555 YNNILWLASSQEGLIGLDANTyEEKYRVNLASGLKTKSIFALQIDPFGFLWVSSQNGLYRLNLSSMQIDTYTVSDGLTVN 634
Cdd:COG3292 413 SDGRLWIGTDGGGLYRYDPKT-GKFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSASNLGLLSLLGGLLGGLNLGNAIKL 491
|
...
gi 2741887859 635 EFN 637
Cdd:COG3292 492 PLS 494
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
1080-1243 |
2.06e-34 |
|
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: 129.76 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1080 LANYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQ 1159
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1160 SGDEFLLLVNNLNSPQALSAQVKALTIELAKRV-VIDDFAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNG 1238
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIeVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 2741887859 1239 FKFFT 1243
Cdd:TIGR00254 161 VVVAD 165
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
877-1498 |
0e+00 |
|
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: 573.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 877 ALIHPDDKRQLSLDWAAFLEQKNQQQWQATYRLKHALGHWLWYQDIGEVIETDENKKPIRVSGIYTNITESRATAQQAAV 956
Cdd:COG5001 47 LALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 957 LGEAFSQINDWLLILDHQLLPFSVNNSFADAFSVDSSPATLNLKGFLAALGKQQYADYIKILNSLKPRQNWRGDAYIKTR 1036
Cdd:COG5001 127 LLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1037 TNPSHPIHISITAVAKDSDFVSYYVVVISDLTEQKRAENELRYLANYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALL 1116
Cdd:COG5001 207 RLALRLLLGLLLLGLLLLLLLVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1117 FIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQSGDEFLLLVNNLNSPQALSAQVKALTIELAKRVVIDD 1196
Cdd:COG5001 287 FIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLDDPEDAEAVAERILAALAEPFELDG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1197 FAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNGFKFFTEQMNDQITQKLLLENALKDAFKDDLLFNNYQPI 1276
Cdd:COG5001 367 HELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLELEADLRRALERGELELHYQPQ 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1277 VNVKSKKIKGVELLMRWQH-EGQFISPAKFIPIAEETGLIDVLTEQALSRALKELAPLLRA-NPRFYLSLNLSPVHILKS 1354
Cdd:COG5001 447 VDLATGRIVGAEALLRWQHpERGLVSPAEFIPLAEETGLIVPLGEWVLREACRQLAAWQDAgLPDLRVAVNLSARQLRDP 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1355 NLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTGYSSLTYLNQFPIDVIKIDQSFV 1434
Cdd:COG5001 527 DLVDRVRRALAETGLPPSRLELEITESALLEDPEEALETLRALRALGVRIALDDFGTGYSSLSYLKRLPVDTLKIDRSFV 606
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2741887859 1435 RKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARPITADKLL 1498
Cdd:COG5001 607 RDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQGYLFSRPLPAEELE 670
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
935-1499 |
2.12e-111 |
|
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) [Signal transduction mechanisms];
Pssm-ID: 441802 [Multi-domain] Cd Length: 576 Bit Score: 364.88 E-value: 2.12e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 935 IRVSGIYTNITESRATAQQAAVLGEAFSQINDWLLILDHQLLPFSVNNSFADAFSVDSSPATLNLKGFLAALGKQQYADY 1014
Cdd:COG2200 8 LRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLLLLLALLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1015 IKILNSLKPRQNWRGDAYIKTRTNPSHPIHISITAVAKDSDFVSYYVVVISDLTEQKRAENELRYLANYDPLTKLPNRTL 1094
Cdd:COG2200 88 LLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLRLALELLLALLLLALLALLDLLLLLLLRRL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1095 M-YQKINRAIKDADKRQTLSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQSGDEFLLLVNNLNS 1173
Cdd:COG2200 168 LlLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLLLLLLLAA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1174 PQALSAQVKALTIELAKRVVIDDFAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNGFKFFTEQMnDQITQK 1253
Cdd:COG2200 248 AAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE-ARARRR 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1254 LLLENALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRWQH-EGQFISPAKFIPIAEETGLIDVLTEQALSRALKELAP 1332
Cdd:COG2200 327 LALESELREALEEGELRLYYQPIVDLRTGRVVGYEALLRWRHpDGGLISPAEFIPAAERSGLIVELDRWVLERALRQLAR 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1333 LLRANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTG 1412
Cdd:COG2200 407 WPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRIALDDFGTG 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1413 YSSLTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARPI 1492
Cdd:COG2200 487 YSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQGYLFGRPL 566
|
....*..
gi 2741887859 1493 TADKLLS 1499
Cdd:COG2200 567 PLEELEA 573
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
1066-1497 |
5.08e-102 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 341.66 E-value: 5.08e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1066 DLTEQKRAENELRYLANYDPLTKLPNRTLMYQKINRAIKDADKRQTlsALLFIDLDKFKPVNDSFGHAVGDQLLCDITQR 1145
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINAADNNQV--GIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1146 VNAMLDSDGVLGRQSGDEFLLLVNNlNSPQALSAQVKALTIELAKRVVIDDFAINISASIGVALYPFDAKTADQLIRHAD 1225
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASH-TSQAALEAMASRILTRLRLPFRIGLIEVYTGCSIGIALAPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1226 IAMMHAKQSGRNGFKFFTEQMNDQITQKLLLENALKDAFKDDLLFNNYQPIVNVkSKKIKGVELLMRWQH-EGQFISPAK 1304
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEMNQRVFEYLWLDTNLRKALENDQLVIHYQPKITW-RGEVRSLEALVRWQSpERGLIPPLE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1305 FIPIAEETGLIDVLTEQALSRALKELAPLLRANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLL 1384
Cdd:PRK10060 458 FISYAEESGLIVPLGRWVMLDVVRQVAKWRDKGINLRVAVNVSARQLADQTIFTALKQALQELNFEYCPIDVELTESCLI 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1385 DDKNKAAKQLQTLRNAGFKLLLDDFGTGYSSLTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAE 1464
Cdd:PRK10060 538 ENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVAVAQALNLQVIAE 617
|
410 420 430
....*....|....*....|....*....|...
gi 2741887859 1465 GVETIEQIRFLNRIGCYDLQGYYFARPITADKL 1497
Cdd:PRK10060 618 GVETAKEDAFLTKNGVNERQGFLFAKPMPAVAF 650
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
1258-1495 |
3.06e-94 |
|
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues and is also known as domain of unknown function 2 (DUF2). The EAL domain has been shown to stimulate degradation of a second messenger, cyclic di-GMP, and is a good candidate for a diguanylate phosphodiesterase function. Together with the GGDEF domain, EAL might be involved in regulating cell surface adhesiveness in bacteria.
Pssm-ID: 238923 [Multi-domain] Cd Length: 240 Bit Score: 304.08 E-value: 3.06e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1258 NALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRWQH-EGQFISPAKFIPIAEETGLIDVLTEQALSRALKELAPLLRA 1336
Cdd:cd01948 1 ADLRRALERGEFELYYQPIVDLRTGRIVGYEALLRWRHpEGGLISPAEFIPLAEETGLIVELGRWVLEEACRQLARWQAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1337 NPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTGYSSL 1416
Cdd:cd01948 81 GPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741887859 1417 TYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARPITAD 1495
Cdd:cd01948 161 SYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
1069-1497 |
3.59e-83 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 291.67 E-value: 3.59e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1069 EQKRAENELRYLANYDPLTKLPNRTLMYQKINRAIkdaDKRQTLsALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNA 1148
Cdd:PRK11359 364 EQEKSRQHIEQLIQFDPLTGLPNRNNLHNYLDDLV---DKAVSP-VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1149 MLDSDGVLGRQSGDEFLLLVNNLNSPQAlsAQVKALTIELA-KRVVIDDFAINISASIGVAlypFDA-KTADQLIRHADI 1226
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVLVSLENDVSNI--TQIADELRNVVsKPIMIDDKPFPLTLSIGIS---YDVgKNRDYLLSTAHN 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1227 AMMHAKQSGRNGFKFFTEQMNDQITQKLLLENALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRWqHEGQF--ISPAK 1304
Cdd:PRK11359 515 AMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARW-HDPLHghVPPSR 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1305 FIPIAEETGLIDVLTEQALSRALKELAPLLRANPRF-YLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTL 1383
Cdd:PRK11359 594 FIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIpALSVNLSALHFRSNQLPNQVSDAMQAWGIDGHQLTVEITESMM 673
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1384 LDDKNKAAKQLQTLRNAGFKLLLDDFGTGYSSLTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIA 1463
Cdd:PRK11359 674 MEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVA 753
|
410 420 430
....*....|....*....|....*....|....
gi 2741887859 1464 EGVETIEQIRFLNRIGCYDLQGYYFARPITADKL 1497
Cdd:PRK11359 754 EGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEI 787
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
1257-1495 |
2.94e-81 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 267.16 E-value: 2.94e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1257 ENALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRWQH-EGQFISPAKFIPIAEETGLIDVLTEQALSRALKELAPLL- 1334
Cdd:smart00052 1 ERELRQALENGQFLLYYQPIVSLRTGRLVGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEWQa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1335 RANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTGYS 1414
Cdd:smart00052 81 QGPPPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTGYS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1415 SLTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARPITA 1494
Cdd:smart00052 161 SLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPLPL 240
|
.
gi 2741887859 1495 D 1495
Cdd:smart00052 241 D 241
|
|
| YjcC |
COG4943 |
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal ... |
1252-1498 |
1.24e-78 |
|
Redox-sensing c-di-GMP phosphodiesterase, contains CSS-motif and EAL domains [Signal transduction mechanisms];
Pssm-ID: 443970 [Multi-domain] Cd Length: 528 Bit Score: 270.25 E-value: 1.24e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1252 QKLLLENALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRWQHE-GQFISPAKFIPIAEETGLIDVLTEQALSRALKEL 1330
Cdd:COG4943 268 RRLSPRRRLRRAIKRREFYVHYQPIVDLKTGRCVGAEALVRWRDPdGSVISPDIFIPLAEQSGLISPLTRQVIEQVFRDL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1331 APLLRANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKnKAAKQLQTLRNAGFKLLLDDFG 1410
Cdd:COG4943 348 GDLLAADPDFHISINLSASDLLSPRFLDDLERLLARTGVAPQQIVLEITERGFIDPA-KARAVIAALREAGHRIAIDDFG 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1411 TGYSSLTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFAR 1490
Cdd:COG4943 427 TGYSSLSYLQTLPVDILKIDKSFVDAIGTDSANSAVVPHIIEMAKTLNLDVVAEGVETEEQADYLRARGVQYGQGWLFAK 506
|
....*...
gi 2741887859 1491 PITADKLL 1498
Cdd:COG4943 507 PLPAEEFI 514
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
1071-1495 |
3.28e-72 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 255.41 E-value: 3.28e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1071 KRAENELRYLANYDPLTKLPNRTLMYQKINRAIKdadkRQTLSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAML 1150
Cdd:PRK13561 221 QRQYEEQSRNATRFPVSDLPNKALLMALLEQVVA----RKQTTALMIITCETLRDTAGVLKEAQREILLLTLVEKLKSVL 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1151 DSDGVLGRQSGDEFLLLVNNLNSP-QALSAQVKALTIeLAKRVVIDDFAINISASIGVALYPFDaKTADQLIRHADIAMM 1229
Cdd:PRK13561 297 SPRMVLAQISGYDFAIIANGVKEPwHAITLGQQVLTI-INERLPIQRIQLRPSCSIGIAMFYGD-LTAEQLYSRAISAAF 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1230 HAKQSGRNGFKFFTEQMNDQITQKLLLENALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRW-QHEGQFISPAKFIPI 1308
Cdd:PRK13561 375 TARRKGKNQIQFFDPQQMEAAQKRLTEESDILNALENHQFAIWLQPQVEMRSGKLVSAEALLRMqQPDGSWDLPEGLIDR 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1309 AEETGLIDVLTEQALSRALKELAPLLRANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKN 1388
Cdd:PRK13561 455 IESCGLMVTVGHWVLEESCRLLAAWQERGIMLPLSVNLSALQLMHPNMVADMLELLTRYRIQPGTLILEVTESRRIDDPH 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1389 KAAKQLQTLRNAGFKLLLDDFGTGYSSLTYLNQF---PIDVIKIDQSFVRKIGQDSgneSILKTIHTLAENLNLYCIAEG 1465
Cdd:PRK13561 535 AAVAILRPLRNAGVRVALDDFGMGYAGLRQLQHMkslPIDVLKIDKMFVDGLPEDD---SMVAAIIMLAQSLNLQVIAEG 611
|
410 420 430
....*....|....*....|....*....|
gi 2741887859 1466 VETIEQIRFLNRIGCYDLQGYYFARPITAD 1495
Cdd:PRK13561 612 VETEAQRDWLLKAGVGIAQGFLFARALPIE 641
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
1085-1499 |
9.31e-71 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 251.40 E-value: 9.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1085 PLTKLPNRTLMYQKINRAIKDADKRQTLsALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQSGDEF 1164
Cdd:PRK11829 236 PVTELPNRSLFISLLEKEIASSTRTDHF-HLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEF 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1165 LLLVNNLNSPQALSAQVKALTIELAKRVVIDDFAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNGFKFFTE 1244
Cdd:PRK11829 315 AVLARGTRRSFPAMQLARRIMSQVTQPLFFDEITLRPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1245 QMNDQITQKLLLENALKDAFK--DDLLFnnYQPIVNVKSKKIKGVELLMRW-QHEGQFISPAKFIPIAEETGLIDVLTEQ 1321
Cdd:PRK11829 395 HLIEKTHKRLTQENDLLQAIEnhDFTLF--LQPQWDMKRQQVIGAEALLRWcQPDGSYVLPSGFVHFAEEEGMMVPLGNW 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1322 ALSRALKELAPLLRANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAG 1401
Cdd:PRK11829 473 VLEEACRILADWKARGVSLPLSVNISGLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLG 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1402 FKLLLDDFGTGYSSLTYLNQ---FPIDVIKIDQSFVRKIGQDsgnESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRI 1478
Cdd:PRK11829 553 LLIALDDFGIGYSSLRYLNHlksLPIHMIKLDKSFVKNLPED---DAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEH 629
|
410 420
....*....|....*....|.
gi 2741887859 1479 GCYDLQGYYFARPITADKLLS 1499
Cdd:PRK11829 630 GIQCGQGFLFSPPLPRAEFEA 650
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
829-1502 |
1.47e-70 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 258.83 E-value: 1.47e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 829 QQTELALSSSKSGVWEVNFLTRSASQHRVKHELgYETLPHTH-SFEQFTALIHPDDKRQLSLDWAAFLEQKnqQQWQATY 907
Cdd:PRK09776 410 ERITLANEAGGIGIWEWDLKPNIISWDKRMFEL-YEIPPHIKpTWQVWYACLHPEDRQRVEKEIRDALQGR--SPFKLEF 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 908 RLKHALG-HWLwyQDIGEVIeTDENKKPIRVSGIYTNITESRAtaqqaavLGEAFSQINDWLLI-LDhqllpfsvnnSFA 985
Cdd:PRK09776 487 RIVVKDGvRHI--RALANRV-LNKDGEVERLLGINMDMTEVRQ-------LNEALFQEKERLHItLD----------SIG 546
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 986 DA-FSVDS-------SPATLNLKGFL--AALGkQQYADYIKILNSLK--PRQNW------RGDAYIK------TRTNPSH 1041
Cdd:PRK09776 547 EAvVCTDMamkvtfmNPVAEKMTGWTqeEALG-VPLLTVLHITFGDNgpLMENIyscltsRSAAYLEqdvvlhCRSGGSY 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1042 PIHISITAVAKDSDFVSYYVVVISDLTEQKRAENELRYLANYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALLFIDLD 1121
Cdd:PRK09776 626 DVHYSITPLSTLDGENIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLD 705
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1122 KFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQSGDEFLLLVNNLNSPQAlsAQVKALTIEL--AKRVVIDDFAI 1199
Cdd:PRK09776 706 RFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESA--RFIATRIISAinDYHFPWEGRVY 783
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1200 NISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNGFKFFTEQMNDQITQK--LLLENALKDAFKDDLLFNNYQPIV 1277
Cdd:PRK09776 784 RVGASAGITLIDANNHQASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHraLSLAEQWRMIKENQLMMLAHGVAS 863
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1278 NVKSKKIKGVELLMR-WQHEGQFISPAKFIPIAEETGLIDVLTEQALSRALKELAPLLRAnPRFYLSLNLSPVHILKSNL 1356
Cdd:PRK09776 864 PRIPEARNHWLISLRlWDPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVAS-KGLSIALPLSVAGLSSPTL 942
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1357 TERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTGYSSLTYLNQFPIDVIKIDQSFVRK 1436
Cdd:PRK09776 943 LPFLLEQLENSPLPPRLLHLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVAN 1022
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741887859 1437 IGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARPITADKLLSDDY 1502
Cdd:PRK09776 1023 LHGNLMDEMLISIIQGHAQRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLNSSY 1088
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
1257-1491 |
6.90e-69 |
|
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL after its conserved residues. The EAL domain is a good candidate for a diguanylate phosphodiesterase function. The domain contains many conserved acidic residues that could participate in metal binding and might form the phosphodiesterase active site.
Pssm-ID: 425752 [Multi-domain] Cd Length: 235 Bit Score: 231.44 E-value: 6.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1257 ENALKDAFKDDLLFNNYQPIVNVKSKKIKGVELLMRWQH-EGQFISPAKFIPIAEETGLIDVLTEQALSRALKELApLLR 1335
Cdd:pfam00563 1 ARALRRALENGEFVLYYQPIVDLRTGRVVGYEALLRWQHpDGGLISPARFLPLAEELGLIAELDRWVLEQALADLA-QLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1336 ANPRFYLSLNLSPVHILKSNLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAKQLQTLRNAGFKLLLDDFGTGYSS 1415
Cdd:pfam00563 80 LGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741887859 1416 LTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARP 1491
Cdd:pfam00563 160 LSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
1043-1242 |
6.24e-57 |
|
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: 198.66 E-value: 6.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1043 IHISITAVAKDSDFVSYYVVVISDLTEQKRAENELRYLANYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALLFIDLDK 1122
Cdd:COG2199 76 LLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDH 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1123 FKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQSGDEFLLLVNNLNSPQALsAQVKALTIELAK-RVVIDDFAINI 1201
Cdd:COG2199 156 FKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAE-ALAERLREALEQlPFELEGKELRV 234
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2741887859 1202 SASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNGFKFF 1242
Cdd:COG2199 235 TVSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
1082-1239 |
1.42e-52 |
|
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: 181.60 E-value: 1.42e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1082 NYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQSG 1161
Cdd:cd01949 1 YTDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2741887859 1162 DEFLLLVNNLNSPQALsAQVKALTIELAKRVVIDDFAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNGF 1239
Cdd:cd01949 81 DEFAILLPGTDLEEAE-ALAERLREAIEEPFFIDGQEIRVTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| PRK10551 |
PRK10551 |
cyclic di-GMP phosphodiesterase; |
1273-1497 |
5.77e-50 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 182541 [Multi-domain] Cd Length: 518 Bit Score: 186.35 E-value: 5.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1273 YQPIVNVKSKKIKGVELLMRWQH--EGQfISPAKFIPIAEETGLIdvlteQALSRALKEL----APLLR-ANPR-FYLSL 1344
Cdd:PRK10551 281 YQPVVDTQTLRVTGLEALLRWRHptAGE-IPPDAFINYAEAQKLI-----VPLTQHLFELiardAAELQkVLPVgAKLGI 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1345 NLSPVHILKSNLTE---RLLFILTQHHIKPVqlrLEITENTLLDdKNKAAKQLQTLRNAGFKLLLDDFGTGYSSLTYLNQ 1421
Cdd:PRK10551 355 NISPAHLHSDSFKAdvqRLLASLPADHFQIV---LEITERDMVQ-EEEATKLFAWLHSQGIEIAIDDFGTGHSALIYLER 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2741887859 1422 FPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIAEGVETIEQIRFLNRIGCYDLQGYYFARPITADKL 1497
Cdd:PRK10551 431 FTLDYLKIDRGFIQAIGTETVTSPVLDAVLTLAKRLNMLTVAEGVETPEQARWLRERGVNFLQGYWISRPLPLEDF 506
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
1081-1237 |
1.26e-48 |
|
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of non-homologous domains in a variety of bacteria. It has been shown to be homologous to the adenylyl cyclase catalytic domain and has diguanylate cyclase activity. This observation correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. In the WspR protein of Pseudomonas aeruginosa, the GGDEF domain acts as a diguanylate cyclase, PDB:3bre, when the whole molecule appears to form a tetramer consisting of two symmetrically-related dimers representing a biological unit. The active site is the GGD/EF motif, buried in the structure, and the cyclic dimeric guanosine monophosphate (c-di-GMP) bind to the inhibitory-motif RxxD on the surface. The enzyme thus catalyzes the cyclization of two guanosine triphosphate (GTP) molecules to one c-di-GMP molecule.
Pssm-ID: 425976 [Multi-domain] Cd Length: 160 Bit Score: 170.51 E-value: 1.26e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1081 ANYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQS 1160
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2741887859 1161 GDEFLLLVNNLNSPQALSAQVKALTI--ELAKRVVIDDFAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRN 1237
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLlaKLKIPHTVSGLPLYVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
1079-1242 |
3.26e-47 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 166.65 E-value: 3.26e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1079 YLANYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGR 1158
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1159 QSGDEFLLLVNNLNSPQALSAqVKALTIELAKRVVIDDFAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNG 1238
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIAL-AERILQQLREPIIIHGIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 2741887859 1239 FKFF 1242
Cdd:smart00267 160 VAVY 163
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
8-637 |
2.07e-44 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 175.56 E-value: 2.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 8 FILFALLCILYSTTSHAQNYalQLQRLSPDEGLSQGYVTNTLQDHLGFVWIGTKQGLNRFDGYQVKTFT----GEQGLDQ 83
Cdd:COG3292 3 LLLLLLLLLLSLFAQAAQQY--RFRHLTVEDGLPQNSVNSIAQDSDGFLWIGTEDGLNRYDGYEFKVFRhdpgDPNSLPS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 84 ASILFLFATESDEIFVSTeysgaflinpvtlvtrkvysgklseedkryspinavkqrgtlfyyaiNDHVYTFDSKHSTFT 163
Cdd:COG3292 81 NYIRALLEDSDGRLWIGT-----------------------------------------------DGGLSRYDPKTDKFT 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 164 H-TFSINKPEHLVRALTI-HNNFIYIATSNGLYSKSLIDDHITKIPLLSKdklneDNNNIKFLHVDPQLGLMVgtvegfy 241
Cdd:COG3292 114 RyPLDPGLPNNSIRSIAEdSDGNIWVGTSNGLYRYDPKTGKFKRFTLDGL-----PSNTITSLAEDADGNLWV------- 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 242 sislDKNsqfdfaniktliphHNIWdyINTpfgefvvTQDGLYQYDRHTNQsLFILRFDQSKFNMTDNTILDVMVDKTGL 321
Cdd:COG3292 182 ----DSD--------------GNLW--IGT-------DGNGLYRLDPNTGK-FEHITHDPDPNSLSSNSIYSLFEDREGN 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 322 MWLASRSQGVFTWSTFARRFNNIEITSRDKLHSNVVLSVFQDDTN----ALWLGT-NNGLTRINEKAGITKTYlatadTK 396
Cdd:COG3292 234 LWVGTYGGGLNYLDPNNSKFKSYRHNDPNGLSGNSVRSIAEDSDGnlwiRLWIGTyGGGLFRLDPKTGKFKRY-----NP 308
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 397 AFYGQYSVYGIAPAELNEpnrfLWL-LLYNGLALFDKQTEQLLP-TPMQGITQNILTegptygyyqiqtdtfaffsekdf 474
Cdd:COG3292 309 NGLPSNSVYSILEDSDGN----LWIgTSGGGLYRYDPKTGKFTKfSEDNGLSNNFIR----------------------- 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 475 YIYDGKTGNTrpirglkeqldpinvhrflkplntypddhLISVSGALYRYNEKRERLTLLYEVKNYNPLSYITIDDWVLD 554
Cdd:COG3292 362 SILEDSDGNL-----------------------------WVGTNGGLYRLDPKTGKFTNFTHDPDKNGLSSNYINSIFED 412
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 555 YNNILWLASSQEGLIGLDANTyEEKYRVNLASGLKTKSIFALQIDPFGFLWVSSQNGLYRLNLSSMQIDTYTVSDGLTVN 634
Cdd:COG3292 413 SDGRLWIGTDGGGLYRYDPKT-GKFKHFTTKDGLPSNTIYSILEDDNGNLWNFNSASNLGLLSLLGGLLGGLNLGNAIKL 491
|
...
gi 2741887859 635 EFN 637
Cdd:COG3292 492 PLS 494
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
1080-1243 |
2.06e-34 |
|
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: 129.76 E-value: 2.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1080 LANYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQ 1159
Cdd:TIGR00254 1 QAVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1160 SGDEFLLLVNNLNSPQALSAQVKALTIELAKRV-VIDDFAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGRNG 1238
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIeVAGSETLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
....*
gi 2741887859 1239 FKFFT 1243
Cdd:TIGR00254 161 VVVAD 165
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
1053-1237 |
4.85e-25 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 107.07 E-value: 4.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1053 DSDFVSYYVVVISDLTEQKRAENEL-RYLANYDPLTKLPNRTLMYQKINRAIKDADKrQTLsALLFIDLDKFKPVNDSFG 1131
Cdd:PRK09894 100 DAHFDAFQEGLLSFTAALTDYKIYLlTIRSNMDVLTGLPGRRVLDESFDHQLRNREP-QNL-YLALLDIDRFKLVNDTYG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1132 HAVGDQLLCDITQRVNAMLDSDGVLGRQSGDEFLLLVNNLNSPQALSAQVKALTIELAKRVVIDDFAINISASIGVALYp 1211
Cdd:PRK09894 178 HLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHSDGRINITATFGVSRA- 256
|
170 180
....*....|....*....|....*.
gi 2741887859 1212 FDAKTADQLIRHADIAMMHAKQSGRN 1237
Cdd:PRK09894 257 FPEETLDVVIGRADRAMYEGKQTGRN 282
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
1075-1237 |
2.01e-21 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 100.47 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1075 NELRYLANYDPLTKLPNRTLMYQKINRAIKDADKRQTLSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDG 1154
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1155 VLGRQSGDEFLLLVNNLNSPQAL-SAQVKALTIELAKRVVIDDFAINISASIGVA-LYPFDAKTADQLIRHADIAMMHAK 1232
Cdd:PRK15426 472 VAGRVGGEEFCVVLPGASLAEAAqVAERIRLRINEKEILVAKSTTIRISASLGVSsAEEDGDYDFEQLQSLADRRLYLAK 551
|
....*
gi 2741887859 1233 QSGRN 1237
Cdd:PRK15426 552 QAGRN 556
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
1080-1237 |
2.60e-18 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 89.96 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1080 LANYDPLTKLPNRTLMYQKINRAIKDA-DKRQTLSaLLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGR 1158
Cdd:PRK09581 291 MAVTDGLTGLHNRRYFDMHLKNLIERAnERGKPLS-LMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIAR 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1159 QSGDEFLLLVNNLNSPQALSA--QVKALTIELAKRVVIDDFAINISASIGVALYPFDAKTADQLIRHADIAMMHAKQSGR 1236
Cdd:PRK09581 370 YGGEEFVVVMPDTDIEDAIAVaeRIRRKIAEEPFIISDGKERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGR 449
|
.
gi 2741887859 1237 N 1237
Cdd:PRK09581 450 N 450
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
1036-1233 |
2.56e-17 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 86.21 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1036 RTNPSHPIHISITAVAKDSDFVSYYVVVISDLTEQK---RAEN-ELRYLANYDPLTKLPNRTLMYQKINRAIKDADKRQT 1111
Cdd:PRK09966 199 RSNRNFSRRVSEERIAEFHRFALDFNSLLDEMEEWQlrlQAKNaQLLRTALHDPLTGLANRAAFRSGINTLMNNSDARKT 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1112 lSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVLGRQSGDEFLLLVNNLNSPQALSAQVKALTIELAKR 1191
Cdd:PRK09966 279 -SALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHKAYRLGGDEFAMVLYDVQSESEVQQICSALTQIFNLP 357
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2741887859 1192 VVIDD-FAINISASIGVALyPFDAKTADQLIRHADIAMMHAKQ 1233
Cdd:PRK09966 358 FDLHNgHQTTMTLSIGYAM-TIEHASAEKLQELADHNMYQAKH 399
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
1084-1492 |
2.84e-16 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 84.53 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1084 DPLTKLPNRTLMYQKINRAIKDADKRQTLSALLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDS--DGVLGRQSG 1161
Cdd:PRK11059 231 DAKTGLGNRLFFDNQLATLLEDQEMVGAHGVVMLIRLPDFDLLQEEWGESQVEELLFELINLLSTFVMRypGALLARYSR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1162 DEFLLLVNNLNSPQA--LSAQ-VKALTIELAKRVVI-DDFAinisaSIGVALYPfDAKTADQLIRHADIAMMHAKQSGRN 1237
Cdd:PRK11059 311 SDFAVLLPHRSLKEAdsLASQlLKAVDALPPPKMLDrDDFL-----HIGICAYR-SGQSTEQVMEEAEMALRSAQLQGGN 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1238 GFKFFTEQMNDQITQ-----KLLLENALkdAFKDDLLFNnyQPIVNVKsKKIKGVELLMRWQHEGQFISPA-KFIPIAEE 1311
Cdd:PRK11059 385 GWFVYDKAQLPEKGRgsvrwRTLLEQTL--VRGGPRLYQ--QPAVTRD-GKVHHRELFCRIRDGQGELLSAeLFMPMVQQ 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1312 TGLIDVLTEQALSRALkelaPLLRANPRFYLSLNLSpvhiLKSnLTER--------LLFILTQHHIKpvQLRLEITENTL 1383
Cdd:PRK11059 460 LGLSEQYDRQVIERVL----PLLRYWPEENLSINLS----VDS-LLSRafqrwlrdTLLQCPRSQRK--RLIFELAEADV 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1384 LDDKNKAAKQLQTLRNAGFKLLLDDFGTGYSSLTYLNQFPIDVIKIDQSFVRKIGQDSGNESILKTIHTLAENLNLYCIA 1463
Cdd:PRK11059 529 CQHISRLRPVLRMLRGLGCRLAVDQAGLTVVSTSYIKELNVELIKLHPSLVRNIHKRTENQLFVRSLVGACAGTETQVFA 608
|
410 420
....*....|....*....|....*....
gi 2741887859 1464 EGVETIEQIRFLNRIGCYDLQGYYFARPI 1492
Cdd:PRK11059 609 TGVESREEWQTLQELGVSGGQGDFFAESQ 637
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
1056-1237 |
2.56e-14 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 76.41 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1056 FVSYYVVVisDLTEQKRaenELRYLANYDPLTKLPNR----TLM---YQKINRAIKDAdkrqtlsALLFIDLDKFKPVND 1128
Cdd:PRK10245 185 WVSYQTAT--KLAEHKR---RLQVMSTRDGMTGVYNRrhweTLLrneFDNCRRHHRDA-------TLLIIDIDHFKSIND 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1129 SFGHAVGDQLLCDITQRVNAMLDSDGVLGRQSGDEFLLLVNNLNSPQALSA------QVKALTIELAKRVViddfainIS 1202
Cdd:PRK10245 253 TWGHDVGDEAIVALTRQLQITLRGSDVIGRFGGDEFAVIMSGTPAESAITAmsrvheGLNTLRLPNAPQVT-------LR 325
|
170 180 190
....*....|....*....|....*....|....*..
gi 2741887859 1203 ASIGVAlyPFDAKTAD--QLIRHADIAMMHAKQSGRN 1237
Cdd:PRK10245 326 ISVGVA--PLNPQMSHyrEWLKSADLALYKAKNAGRN 360
|
|
| YuxH |
COG3434 |
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction ... |
1274-1493 |
9.28e-14 |
|
c-di-GMP phosphodiesterase YuxH/PdeH, contains EAL and HDOD domains [Signal transduction mechanisms];
Pssm-ID: 442660 [Multi-domain] Cd Length: 407 Bit Score: 75.22 E-value: 9.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1274 QPIVNvKSKKIKGVELLMRWQHEGQFISpakfipIAEETGLIDVLTEQALSRALKELapllranprfylsLNLSPVHIlk 1353
Cdd:COG3434 9 QPILD-RDQRVVGYELLFRSGLENSAPD------VDGDQATARVLLNAFLEIGLDRL-------------LGGKLAFI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1354 sNLTERLLFILTQHHIKPVQLRLEITENTLLDDKNKAAkqLQTLRNAGFKLLLDDFGTGYSSLTYLNQfpIDVIKIDQsf 1433
Cdd:COG3434 67 -NFTEELLLSDLPELLPPERVVLEILEDVEPDEELLEA--LKELKEKGYRIALDDFVLDPEWDPLLPL--ADIIKIDV-- 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2741887859 1434 vrkigQDSGNESILKTIHTLAeNLNLYCIAEGVETIEQIRFLNRIGCyDL-QGYYFARPIT 1493
Cdd:COG3434 140 -----LALDLEELAELVARLK-RYGIKLLAEKVETREEFELCKELGF-DLfQGYFFSKPEI 193
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
875-1077 |
2.17e-13 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 71.98 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 875 FTALIHPDDKRQLSLDWAAFLEQknQQQWQATYRLKHALGHWLWYQDIGEVIeTDENKKPIRVSGIYTNITESRAT---- 950
Cdd:COG2202 56 LRDLLPPEDDDEFLELLRAALAG--GGVWRGELRNRRKDGSLFWVELSISPV-RDEDGEITGFVGIARDITERKRAeeal 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 951 AQQAAVLGEAFSQINDWLLILDHQLLPFSVNNSFADAFSVdsSPATLNLKGFLAALGKQQYADYIKILNSLKPRQNWRGD 1030
Cdd:COG2202 133 RESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGY--SPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYE 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2741887859 1031 AYIKTRTNPSHPIHISITAVA-KDSDFVSYYVVVISDLTEQKRAENEL 1077
Cdd:COG2202 211 LELRLKDGDGRWVWVEASAVPlRDGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK11596 |
PRK11596 |
cyclic-di-GMP phosphodiesterase; Provisional |
1246-1497 |
3.92e-11 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183222 [Multi-domain] Cd Length: 255 Bit Score: 65.02 E-value: 3.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1246 MNDQITQKLLLENALKDAFKDDLLFNN------YQPIVNVkSKKIKGVELLMRWQHE---GQFISPAKF---IPIAEEtg 1313
Cdd:PRK11596 1 MIRQVIQRISLPEASIESLQERRYWLQceraytFQPIYRT-SGRLMAIELLTAVTHPsnpSQRLSPERYfaeITVSHR-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1314 lIDVLTEQAlsRALKELAPLLRANprfylslnlspvHILKSNLTERLLFILTQHHIKPVQL-------RLEITENTLLDD 1386
Cdd:PRK11596 78 -LDVVKEQL--DLLAQWADFFVRH------------GLLASVNIDGPTLIALRQQPAILRLierlpwlRFELVEHIRLPK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1387 KNKAAKqlqtLRNAGfKLLLDDFGTGYSSLTYLNQFPIDVIKIDQS-FVRKIGQDSGNESILKTIHTLaenlNLYC---I 1462
Cdd:PRK11596 143 DSPFAS----MCEFG-PLWLDDFGTGMANFSALSEVRYDYIKVARElFIMLRQSEEGRNLFSQLLHLM----NRYCrgvI 213
|
250 260 270
....*....|....*....|....*....|....*
gi 2741887859 1463 AEGVETIEQIRFLNRIGCYDLQGYYFARPITADKL 1497
Cdd:PRK11596 214 VEGVETPEEWRDVQRSPAFAAQGYFLSRPAPFETL 248
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
856-940 |
5.85e-11 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 60.05 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 856 RVKHELGYETLPHTHSFEQFTALIHPDDKRQLSLDWAAFLeqKNQQQWQATYRLKHALGHWLWYQDIGEVIEtDENKKPI 935
Cdd:pfam08447 7 RFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEAL--KGGEPYSGEYRIRRKDGEYRWVEARARPIR-DENGKPV 83
|
....*
gi 2741887859 936 RVSGI 940
Cdd:pfam08447 84 RVIGV 88
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
945-1078 |
6.06e-07 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 52.72 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 945 TESRATAQQAAVLGEAFSQINDWLLILDHQLLPFSVNNSFADAFSVDSSPAtLNLKGFLAALGKQQYADYIKILNSLKPR 1024
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEEL-LGKTLRDLLPPEDDDEFLELLRAALAGG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2741887859 1025 QNWRGDAYIKTRTNPSHPIHISITAVAKDSDFVSYYVVVISDLTEQKRAENELR 1078
Cdd:COG2202 80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALR 133
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
521-653 |
1.36e-05 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 49.99 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 521 LYRYNEKRERlTLLYEVKNYNPLSYITIDDWVLDYNNILWLASSQeGLIGLDANTyEEKYRVNLASGLKTKSIFALQIDP 600
Cdd:COG3292 57 LNRYDGYEFK-VFRHDPGDPNSLPSNYIRALLEDSDGRLWIGTDG-GLSRYDPKT-DKFTRYPLDPGLPNNSIRSIAEDS 133
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2741887859 601 FGFLWVSSQNGLYRLNLSSMQIDTYTVS--DGLTVNEFNVDSHTQL---SDGRLAFGT 653
Cdd:COG3292 134 DGNIWVGTSNGLYRYDPKTGKFKRFTLDglPSNTITSLAEDADGNLwvdSDGNLWIGT 191
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
1115-1208 |
7.65e-05 |
|
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: 43.88 E-value: 7.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1115 LLFIDLDKFKPVNDSFGHAVGDQLLCDITQRVNAMLDSDGVL-GRQSGDEFlLLVNNLNSPQALSAQVKALTIELAKrvV 1193
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIRRSGDLkIKTIGDEF-MVVSGLDHPAAAVAFAEDMREAVSA--L 80
|
90
....*....|....*
gi 2741887859 1194 IDDFAINISASIGVA 1208
Cdd:cd07556 81 NQSEGNPVRVRIGIH 95
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
818-953 |
1.39e-04 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 45.40 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 818 KLAHDKILDSQQQTELALSSSKSGVWEVNFLTR-SASQHRVKHELGY---ETLPHThsfeqFTALIHPDDKRQLSLDWAA 893
Cdd:COG2202 126 KRAEEALRESEERLRLLVENAPDGIFVLDLDGRiLYVNPAAEELLGYspeELLGKS-----LLDLLHPEDRERLLELLRR 200
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 894 FLEQKnQQQWQATYRLKHALGHWLWYQdiGEVIETDENKKPIRVSGIYTNITESRATAQQ 953
Cdd:COG2202 201 LLEGG-RESYELELRLKDGDGRWVWVE--ASAVPLRDGGEVIGVLGIVRDITERKRAEEA 257
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
951-1078 |
1.47e-04 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 45.99 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 951 AQQAAVLGEAFSQINDWLLILDHQLLPFSVNNSFADAFSVDSSpatlNLKG-FLAALGKQQYADYIKILNSLKPRQN-WR 1028
Cdd:COG3852 3 RESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAE----ELLGrPLAELFPEDSPLRELLERALAEGQPvTE 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1029 GDAYIKTRTNPSHPIHISITAVaKDSDFVSYYVVVISDLTEQKRAENELR 1078
Cdd:COG3852 79 REVTLRRKDGEERPVDVSVSPL-RDAEGEGGVLLVLRDITERKRLERELR 127
|
|
| COG3292 |
COG3292 |
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms]; |
535-664 |
1.60e-04 |
|
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
Pssm-ID: 442521 [Multi-domain] Cd Length: 924 Bit Score: 46.52 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 535 YEVKNYNP---LSYITIDDWVLDYNNILWLASsQEGLIGLDANTYEE-KYRVNLASGLKTKSIFALQIDPFGFLWVSSQN 610
Cdd:COG3292 22 YRFRHLTVedgLPQNSVNSIAQDSDGFLWIGT-EDGLNRYDGYEFKVfRHDPGDPNSLPSNYIRALLEDSDGRLWIGTDG 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2741887859 611 GLYRLNLSSMQIDTYTVSDGLTVNefNVDSHTQLSDGRLAFGTTLGLLTLAPQD 664
Cdd:COG3292 101 GLSRYDPKTDKFTRYPLDPGLPNN--SIRSIAEDSDGNIWVGTSNGLYRYDPKT 152
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
843-948 |
2.96e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 45.43 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 843 WEVNFLTRSASQhrvkheLGYETLPHTHSFEQFTALIHPDDKRQLSLDWAAFLEQkNQQQWQATYRLKHALGHWLWYQDI 922
Cdd:PRK13560 495 WPVELVSKNITQ------FGYEPDEFISGKRMFAAIIHPADLEQVAAEVAEFAAQ-GVDRFEQEYRILGKGGAVCWIDDQ 567
|
90 100
....*....|....*....|....*.
gi 2741887859 923 GEViETDENKKPIRVSGIYTNITESR 948
Cdd:PRK13560 568 SAA-ERDEEGQISHFEGIVIDISERK 592
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
1148-1232 |
2.05e-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: 40.66 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2741887859 1148 AMLDsdgVLGRQSGDEFLLLVNNLNSPQALSAqvkaltIELAKRVVIDDFAINISASIGVAlypfdaktADQLIRHADiA 1227
Cdd:COG3706 113 ARVD---LVARYGGEEFAILLPGTDLEGALAV------AERIREAVAELPSLRVTVSIGVA--------GDSLLKRAD-A 174
|
....*
gi 2741887859 1228 MMHAK 1232
Cdd:COG3706 175 LYQAR 179
|
|
| |
