|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
20-1105 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 1914.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 20 VSLGLVSFIFTLFSLELSQFGTQLAPLWFPTSIMMVAFYRHAGRMWPGIALSCSLGNIAASILLFSTSSLNMTWTTINIV 99
Cdd:PRK09776 1 VSLGLVSFIFTLFSLELSRFPTTLAPLWFPTAIMMVAFYRHAGRMWPGILLSCSLGNIAANILLFSTSSLNLTWTTINLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 100 EAVVGAVLLRKLLPWYNPLQNLADWLRLALGSAIVPPLLGGVLVVLLTPGDDPLRAFLIWVLSESIGALALVPLGLLFKP 179
Cdd:PRK09776 81 EAVVGAVLLRKLLPWYNPLQNLADWLRLALGSAIVPPLLGGVLVVLLTPGDDPLRAFLIWVLSEAIGMLALVPLGLLFKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 180 HYLLRHRNPRLLFESLLTLAITLTLSWLSMLYLPWPFTFIIVLLMWSAVRLPRMEAFLIFLTTVMMVSLMMAADPSLLAT 259
Cdd:PRK09776 161 HYLLRHRNPRLLFESLLTLAITLTLSWLALLYLPWPFTFIIVLLMWSAVRLPRMEAFLIFLTTVMMVSLMMAADPSLLAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 260 PRTYLMSHMPWLPFLLILLPANIMTMVMYAFRAERKHISESETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQ 339
Cdd:PRK09776 241 PRTYLMSHMPWLPFLLILLPANIMTMVMYAFRAERKHISESETRFRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 340 EELRGLTFQQLTWPEDLNKDLQQVEKLISGEINTYSMEKRYYNRNGDVVWALLAVSLVRHTDGTPLYFIAQIEDINELKR 419
Cdd:PRK09776 321 EELRGLTFQQLTWPEDLNKDLQQVEKLLSGEINSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 420 TEQVNQQLMERITLANEAGGIGIWEWELKPNIFSWDKRMFELYEIPPHIKPNWQVWYECVLPEDRQHAEKVIRDSLQSRS 499
Cdd:PRK09776 401 TEQVNERLMERITLANEAGGIGIWEWDLKPNIISWDKRMFELYEIPPHIKPTWQVWYACLHPEDRQRVEKEIRDALQGRS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 500 PFKLEFRITVKDGIRHIRALANRVLNKEGEVERLLGINMDMTEVKQLNEALFQEKERLHITLDSIGEAVVCIDMAMKITF 579
Cdd:PRK09776 481 PFKLEFRIVVKDGVRHIRALANRVLNKDGEVERLLGINMDMTEVRQLNEALFQEKERLHITLDSIGEAVVCTDMAMKVTF 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 580 MNPVAEKMSGWTQEEALGVPLLTVLHITFGDNGPLMENIYSADTSRSA--IEQDVVLHCRSGGSYDVHYSITPLSTLDGS 657
Cdd:PRK09776 561 MNPVAEKMTGWTQEEALGVPLLTVLHITFGDNGPLMENIYSCLTSRSAayLEQDVVLHCRSGGSYDVHYSITPLSTLDGE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 658 NIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRILLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGD 737
Cdd:PRK09776 641 NIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGD 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 738 ALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAVNDYHFIWEGRVHRVGASAGITLIDDNNHQ 817
Cdd:PRK09776 721 ALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQ 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 818 AAEVMSQADIACYASKNGGRGRVTVYEPQQAAAHSERAAMSLDEQWRMIKENQLMMLAHGVASPRIPEARNLWLISLKLW 897
Cdd:PRK09776 801 ASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLW 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 898 SCEGEIIDEQTFRRSFSDPALSHALDRRVFHEFFQQAAKAVASKGISISLPLSVAGLSSATLVNDLLEQLENSPLPPRLL 977
Cdd:PRK09776 881 DPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLL 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 978 HLIIPAEAILDHAES----VQKLRLAGCRIVLSQVGRDLQIFNSLKANMADYLLLDGELCANVQGNLMDEMLITIIQGHA 1053
Cdd:PRK09776 961 HLEITETALLNHAESasrlVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHA 1040
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|..
gi 16130007 1054 QRLGMKTIAGPVVLPLVMDTLSGIGVDLIYGEVIADAQPLDLLVNSSYFAIN 1105
Cdd:PRK09776 1041 QRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLNSSYFAIN 1092
|
|
| MASE1 |
COG3447 |
Integral membrane sensor domain MASE1 [Signal transduction mechanisms]; |
4-636 |
2.96e-98 |
|
Integral membrane sensor domain MASE1 [Signal transduction mechanisms];
Pssm-ID: 442670 [Multi-domain] Cd Length: 637 Bit Score: 325.22 E-value: 2.96e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 4 QSQHVLIALPHPLLHLVSLGLVSFIFTLFSLELSQFGTQLAPLWFPTSIMMVAFYRHAGRMWPGIALSCSLGNIAASiLL 83
Cdd:COG3447 2 SSSSALGTPGRPLLRLLLLALLYFLLALLGLLLARPPGGVSPIWPPAGVALAALLRFGRRAWPGILLGALLANLLAG-LT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 84 FSTSSLNMTWTTINIVEAVVGAVLLRKLLPWYNPLQNLADWLRLALGSAIV------PPLLGGVLVVLLTPGDDPLRAFL 157
Cdd:COG3447 81 GDPLLLALLIALGNTLEALLAAWLLRRLLGFSPPLQRLRDVLRFLLAAALLaplisaLLGALALALAGLLPGSPFLSSWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 158 IWVLSESIGALALVPLGLLFKPHYLLRHRnPRLLFESLLTLAITLTLSWLSMLYLPWPFTFIIV-LLMWSAVRLPRMEAF 236
Cdd:COG3447 161 TWWLGDALGILLVTPLLLAWRRPRLRRLR-RRRLLEALALLALLLLVSWLVFGLLGYPLAFLLFpLLLWAALRFGLRGAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 237 LIFLTTVMMVSLMMAADPSLLATPRTYLMSHMPWLPFLLILLPANIMTMVMYAFRaeRKHISESETHFRNAMEYSAIGMA 316
Cdd:COG3447 240 LAVLLLALIAILATALGLGPFASLSPNQSLLLLQLFLAVLALTGLLLAAALAERR--RQRLRERELALRAALELLALGLL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 317 LVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLISGEINTYSMEKRYYNRNGDVVWALLAVSL 396
Cdd:COG3447 318 LAALDDALLLLNARGLLLLALSLAALLLLRLALLLLLLALDALLLLLADDDRGELRGDLLRRRGATRLGAVVARLLRRSG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 397 VRHTDGTPLYFIAQIEDINELKRTEQVNQQLMERITLANEAGGIGIWEWELKPNIFSWDKRMFELYEIPPHIKPNWQVWY 476
Cdd:COG3447 398 GRGEEVVVLLVIAQVEEALELALRERREERLLERLALALELLAITAALLAAALLLALADLLLLLLAEAAQLLARALLLGL 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 477 ECVLPEDRQHAEKVIRDSLQSRSPFKLEFRITVKDGIRHIRALANRVLNKEGEVERLLGINMDMTEVKQLNEALFQEKER 556
Cdd:COG3447 478 DRLLADAALAALAALADLLGALLSAGLRRRGGRRLGARLIRSLLSRVLAELGAVELLLALIADLTEVALGAEALERLLER 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 557 LHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLHITFGDNGPLMENIYSADTSRSAIEQDVVLHC 636
Cdd:COG3447 558 LLLALLGLGLAVAALLATLGLLLALLAALALSGAAALLALGAALLLAAAILGLAAALLALLRLLGERARLLETRRLVGAL 637
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
479-1094 |
1.16e-63 |
|
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: 229.66 E-value: 1.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 479 VLPEDRQHAEKVIRDSLQSRSPFKLEFRITVKDGIRHIRALANRVLNKEGEVERLLGINMDMTEVKQLNEALFQEKERLH 558
Cdd:COG5001 49 LLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALLAALLARALAALL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 559 ITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLHITFGDNGPLMENIYSADTSRSAIEQDVVLHCRS 638
Cdd:COG5001 129 LAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRLLLLLRGGRLLRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 639 GGSYDVHYSITPLSTLDGSnIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRILLQTVNSTHQRHALVF 718
Cdd:COG5001 209 ALRLLLGLLLLGLLLLLLL-VAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARARRSGRRLALLF 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 719 IDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDC-NVESARFIATRIISAVNDyHFIWEG 797
Cdd:COG5001 288 IDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLdDPEDAEAVAERILAALAE-PFELDG 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 798 RVHRVGASAGITLIDDNNHQAAEVMSQADIACYASKNGGRGRVTVYEPQQAAAHSERAAMsldEQ--WRMIKENQLMMla 875
Cdd:COG5001 367 HELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARERLEL---EAdlRRALERGELEL-- 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 876 hgVASPRIPearnlwLISLKLWSCE---------------GEIID--EQTfrrsfsdpALSHALDRRVFHEFFQQAAK-- 936
Cdd:COG5001 442 --HYQPQVD------LATGRIVGAEallrwqhperglvspAEFIPlaEET--------GLIVPLGEWVLREACRQLAAwq 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 937 AVASKGISISLPLSVAGLSSATLVNDLLEQLENSPLPPRLLHLIIPAEAILDHAESV----QKLRLAGCRIVLSQVG--- 1009
Cdd:COG5001 506 DAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDPEEAletlRALRALGVRIALDDFGtgy 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 1010 ------RDLQIfNSLKanmadyllLDGELCANVQGNLMDEMLITIIQGHAQRLGMKTIAGPVVLPLVMDTLSGIGVDLIY 1083
Cdd:COG5001 586 sslsylKRLPV-DTLK--------IDRSFVRDLAEDPDDAAIVRAIIALAHSLGLEVVAEGVETEEQLEFLRELGCDYAQ 656
|
650
....*....|.
gi 16130007 1084 GEVIADAQPLD 1094
Cdd:COG5001 657 GYLFSRPLPAE 667
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
645-843 |
8.23e-62 |
|
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: 212.15 E-value: 8.23e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 645 HYSITPLSTLDGSNIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRILLQTVNSTHQRHALVFIDLDRF 724
Cdd:COG2199 77 LSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDHF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 725 KAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAVNDYHFIWEGRVHRVGA 804
Cdd:COG2199 157 KRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVTV 236
|
170 180 190
....*....|....*....|....*....|....*....
gi 16130007 805 SAGITLIDDNNHQAAEVMSQADIACYASKNGGRGRVTVY 843
Cdd:COG2199 237 SIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
684-840 |
2.58e-57 |
|
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: 194.70 E-value: 2.58e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 684 HDALTHLANRASFEKQLRILLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGD 763
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130007 764 EFGLLLPDCNVESARFIATRIISAVNDYHFIWEGRVHrVGASAGITLIDDNNHQAAEVMSQADIACYASKNGGRGRV 840
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIR-VTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
682-839 |
1.49e-56 |
|
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: 192.47 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 682 ASHDALTHLANRASFEKQLRILLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLG 761
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 762 GDEFGLLLPDCNVESARFIATRIISAVNDYHFIWEGRVHR--VGASAGITLIDDNNHQAAEVMSQADIACYASKNGGRGR 839
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPlyVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRNR 160
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
680-843 |
2.49e-54 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 186.30 E-value: 2.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 680 YSASHDALTHLANRASFEKQLRILLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLAR 759
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 760 LGGDEFGLLLPDCNVESARFIATRIISAVNDYHFIWeGRVHRVGASAGITLIDDNNHQAAEVMSQADIACYASKNGGRGR 839
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIH-GIPLYLTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 16130007 840 VTVY 843
Cdd:smart00267 160 VAVY 163
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
860-1095 |
6.58e-54 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 188.19 E-value: 6.58e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 860 DEQWRMIKEN-QLMMLAHGVASPRipEARNLWLISLKLWSC-EGEIIDEQTFRRSFSDPALSHALDRRVFHEFFQQAAKA 937
Cdd:smart00052 1 ERELRQALENgQFLLYYQPIVSLR--TGRLVGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 938 VASK--GISISLPLSVAGLSSATLVNDLLEQLENSPLPPRLLHLIIPAEAILDHAESV----QKLRLAGCRIVLSQVGRD 1011
Cdd:smart00052 79 QAQGppPLLISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAvatlQRLRELGVRIALDDFGTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 1012 LQIFNSLKANMADYLLLDGELCANVQGNLMDEMLITIIQGHAQRLGMKTIAGPVVLPLVMDTLSGIGVDLIYGEVIADAQ 1091
Cdd:smart00052 159 YSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
....
gi 16130007 1092 PLDL 1095
Cdd:smart00052 239 PLDD 242
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
532-1098 |
3.83e-42 |
|
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: 163.80 E-value: 3.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 532 RLLGINMDMTEVKQLNEALFQEKERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLHITFGDN 611
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 612 GPLMENIYSADTSRSAIEQDVVLHCRSGGSYDVHYSITPLSTLDGSNIGSVLVIQDV---TESRKMLRQLSYSASHDALT 688
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSLLLLLVLVLLrlaLELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 689 HLANRASFEKQLRILLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLL 768
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 769 LPDCNVESARFIATRIISAVNDYHFIWEGRVHRVGASAGITLIDDNNHQAAEVMSQADIACYASKNGGRGRVTVYEPQQA 848
Cdd:COG2200 241 LLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 849 AAHSERAAMsLDEQWRMIKENQLMMLAHGVASPRIP-----EArnlwliSLKLWSCEGEIIDEQTFRRSFSDPALSHALD 923
Cdd:COG2200 321 ARARRRLAL-ESELREALEEGELRLYYQPIVDLRTGrvvgyEA------LLRWRHPDGGLISPAEFIPAAERSGLIVELD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 924 RRVFHEFFQQAAK-AVASKGISISLPLSVAGLSSATLVNDLLEQLENSPLPPRLLHLIIPAEAILDHAES----VQKLRL 998
Cdd:COG2200 394 RWVLERALRQLARwPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAaielLARLRA 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 999 AGCRIVLSQVGRDLQIFNSLKANMADYLLLDGELCANVQGNLMDEMLITIIQGHAQRLGMKTIAGPVVLPLVMDTLSGIG 1078
Cdd:COG2200 474 LGVRIALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELG 553
|
570 580
....*....|....*....|
gi 16130007 1079 VDLIYGEVIADAQPLDLLVN 1098
Cdd:COG2200 554 CDYAQGYLFGRPLPLEELEA 573
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
300-422 |
5.37e-36 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 132.41 E-value: 5.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 300 SETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLISGEINTYSMEKR 379
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 16130007 380 YYNRNGDVVWALLAVSLVRhTDGTPLYFIAQIEDINELKRTEQ 422
Cdd:TIGR00229 81 VRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAEE 122
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
292-550 |
5.05e-35 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 134.77 E-value: 5.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 292 AERKHISESETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLISGEi 371
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 372 NTYSMEKRYYNRNGDVVWALLAVSLVRHTDGTPLYFIAQIEDINELKRTEQVNQQLMERITLANEAGGIGIWEWELKPNI 451
Cdd:COG2202 80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 452 FSWDKRMFELYEIPPHIKPNwQVWYECVLPEDRQHAEKVIRDSLQ-SRSPFKLEFRITVKDGIRHIRALANRVLNKEGEV 530
Cdd:COG2202 160 LYVNPAAEELLGYSPEELLG-KSLLDLLHPEDRERLLELLRRLLEgGRESYELELRLKDGDGRWVWVEASAVPLRDGGEV 238
|
250 260
....*....|....*....|
gi 16130007 531 ERLLGINMDMTEVKQLNEAL 550
Cdd:COG2202 239 IGVLGIVRDITERKRAEEAL 258
|
|
| MASE1 |
pfam05231 |
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate ... |
18-295 |
8.11e-32 |
|
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate cyclases and other bacterial signaling proteins. This entry also includes members of the 8 transmembrane UhpB type (8TMR-UT) domain family.
Pssm-ID: 428383 [Multi-domain] Cd Length: 299 Bit Score: 126.38 E-value: 8.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 18 HLVSLGLVSFIFTLFSLELSQF--GTQLAPLWFPTSIMMVAFYRHAGRMWPGIALSCSLGNIAASILLFSTSSLNMTWTT 95
Cdd:pfam05231 1 LLLLLLLLYALLAAVSLSLALAlvSSGSAPIWLPTGLALAALLLFGRRGWPGILLGAVLASLMAGLLSGLNLLLALAIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 96 INIVEAVVGAVLLRKLLPWYNPLQNLADWLRL-----ALGSAIVPPLLGGVLVVLLTPGDDPLR-AFLIWVLSESIGALA 169
Cdd:pfam05231 81 VNALEALLGAALLRRLLPGRNRLQRLRFWLRLvipgaIIAALLLAIIGLALLLLLGLIPLAPFSiVWLTWWLGSATGVLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 170 LVPLGLLFKPHYLLRHRNP----RLLFESLLTLAITLTLSWLSMLYL-----------PWPFTFIIVLLMWSAVRLPRME 234
Cdd:pfam05231 161 VTPLLLLLRRYLRLRHRLRlwyeRDLAPAAAKLLLLFALLLLLILSLlllllcmpeinYPLGYLLLPPLLWAAFRFGVRG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130007 235 AFLI-FLTTVMMVSLMMAADPSLLATPRTYLMSHMPWLPFLLILLPANimtMVMYAFRAERK 295
Cdd:pfam05231 241 GSLAaLLLAVLLILFTLQGGGPFLQTSGDESSQAILLQLFLAILALVA---LLVSAAISEQR 299
|
|
| GGDEF |
TIGR00254 |
diguanylate cyclase (GGDEF) domain; The GGDEF domain is named for the motif GG[DE]EF shared by ... |
682-842 |
1.36e-31 |
|
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: 121.29 E-value: 1.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 682 ASHDALTHLANRASFEKQLRILLQTVNsTHQRH-ALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARL 760
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRAR-RFQRSfSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 761 GGDEFGLLLPDCNVESARFIATRIISAVNDYHFIWEGR-VHRVGASAGITLIDDNNHQAAEVMSQADIACYASKNGGRGR 839
Cdd:TIGR00254 81 GGEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSeTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNR 160
|
...
gi 16130007 840 VTV 842
Cdd:TIGR00254 161 VVV 163
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
676-850 |
9.43e-31 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 128.98 E-value: 9.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 676 RQLSYSASHDALTHLANRASFEKQLRILLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 755
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 756 VLARLGGDEFGLLLPDCNVESARFIATRIISAVNDYH-FIWEGRVHRVGASAGITLIDDNNHQAAEVM-SQADIACYASK 833
Cdd:PRK15426 472 VAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEiLVAKSTTIRISASLGVSSAEEDGDYDFEQLqSLADRRLYLAK 551
|
170
....*....|....*..
gi 16130007 834 NGGRGRVTVYEPQQAAA 850
Cdd:PRK15426 552 QAGRNRVCASDNAHERE 568
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
685-840 |
5.31e-30 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 125.01 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 685 DALTHLANRASFEKQLRILLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDE 764
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130007 765 FGLLLPDCNVESARFIATRIISAVNDYHFIWEG--RVHRVGASAGITLIDDNNHQAAEVMSQADIACYASKNGGRGRV 840
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDgkERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
419-678 |
1.12e-28 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 116.28 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 419 RTEQVNQQLMERITLANEAGGIGIWEWELKPNIFSWDKRMFELYEIPPHIKPNwQVWYECVLPEDRQHAEKVIRDSLQSR 498
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLG-KTLRDLLPPEDDDEFLELLRAALAGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 499 SPFKLEFRITVKDG-IRHIRALANRVLNKEGEVERLLGINMDMTEVKQLNEALFQEKERLHITLDSIGEAVVCIDMAMKI 577
Cdd:COG2202 80 GVWRGELRNRRKDGsLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 578 TFMNPVAEKMSGWTQEEALGVPLLTVLHITFGDNgpLMENIYSA-DTSRSAIEQDVVLHCRSGGSYDVHYSITPLSTlDG 656
Cdd:COG2202 160 LYVNPAAEELLGYSPEELLGKSLLDLLHPEDRER--LLELLRRLlEGGRESYELELRLKDGDGRWVWVEASAVPLRD-GG 236
|
250 260
....*....|....*....|..
gi 16130007 657 SNIGSVLVIQDVTESRKMLRQL 678
Cdd:COG2202 237 EVIGVLGIVRDITERKRAEEAL 258
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
682-851 |
1.47e-28 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 117.09 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 682 ASHDALTHLANR----ASFEKQLrillqtVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVL 757
Cdd:PRK09894 129 SNMDVLTGLPGRrvldESFDHQL------RNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETV 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 758 ARLGGDEFGLLLPDCNVESARFIATRIISAVNDYHFIW-EGRVHrVGASAGITLIDDNNHqAAEVMSQADIACYASKNGG 836
Cdd:PRK09894 203 YRYGGEEFIICLKAATDEEACRAGERIRQLIANHAITHsDGRIN-ITATFGVSRAFPEET-LDVVIGRADRAMYEGKQTG 280
|
170
....*....|....*
gi 16130007 837 RGRVTVYEPQQAAAH 851
Cdd:PRK09894 281 RNRVMFIDEQNVINR 295
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
667-1092 |
3.70e-28 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 121.71 E-value: 3.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 667 DVTESRKMLRQLSYSASHDALTHLANRASFEKQLRILLQTvnSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASL 746
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNRNAIQELIDHAINA--ADNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSLA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 747 MLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAVNDYHFIWEGRVHrVGASAGITLIDDNNHQAAEVMSQAD 826
Cdd:PRK10060 300 ILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILTRLRLPFRIGLIEVY-TGCSIGIALAPEHGDDSESLIRSAD 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 827 IACYASKNGGRGRVTVYEPQQaaahSERAA--MSLDEQWR-MIKENQLM------MLAHGVAspRIPEARNLWLislklw 897
Cdd:PRK10060 379 TAMYTAKEGGRGQFCVFSPEM----NQRVFeyLWLDTNLRkALENDQLVihyqpkITWRGEV--RSLEALVRWQ------ 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 898 SCEGEIIDEQTFRRSFSDPALSHALDRRVFHEFFQQAAKAVAsKGISISLPLSVAG--LSSATLVNDLLEQLENSPLPPR 975
Cdd:PRK10060 447 SPERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAKWRD-KGINLRVAVNVSArqLADQTIFTALKQALQELNFEYC 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 976 LLHLIIPAEAILDHAES----VQKLRLAGCRIVLSQVGRDLQIFNSLKANMADYLLLDGELCANVQGNLMDEMLITIIQG 1051
Cdd:PRK10060 526 PIDVELTESCLIENEELalsvIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIHKQPVSQSLVRAIVA 605
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 16130007 1052 HAQRLGMKTIAGPVVLPLVMDTLSGIGVDLIYGEVIADAQP 1092
Cdd:PRK10060 606 VAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMP 646
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
287-566 |
7.54e-24 |
|
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444511 [Multi-domain] Cd Length: 489 Bit Score: 106.60 E-value: 7.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 287 MYAFRAErKHISESETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDlNKDLQQVEKL 366
Cdd:COG5809 1 MKSSKME-LQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDD-EKELREILKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 367 ISGEINTYSMEKRYYNRNGDVVWALLAVSLVRHTDGTPLYFIAQIEDINELKRTEQVNQQLMERITLANEAGGIGIWEWE 446
Cdd:COG5809 79 LKEGESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 447 LKPNIFSWDKRMFELYEIPPHiKPNWQVWYECVLPEDRQHAEKVIRDSLQSRSPFKLEFRITVKDGIRHIRALANRVLNK 526
Cdd:COG5809 159 LDGRIIYANPAACKLLGISIE-ELIGKSILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 16130007 527 EGEVERLLGINMDMTEVKQLNEALfQEKERLHItldsIGE 566
Cdd:COG5809 238 NGEVDGIVIIFRDITERKKLEELL-RKSEKLSV----VGE 272
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
552-691 |
3.36e-20 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 93.76 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 552 QEKERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVlhitFGDNGPLMENIYSA-DTSRSAIEQ 630
Cdd:COG3852 4 ESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAEL----FPEDSPLRELLERAlAEGQPVTER 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130007 631 DVVLHCRSGGSYDVHYSITPLSTLDGsNIGSVLVIQDVTESRKMLRQLSYSASHDALTHLA 691
Cdd:COG3852 80 EVTLRRKDGEERPVDVSVSPLRDAEG-EGGVLLVLRDITERKRLERELRRAEKLAAVGELA 139
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
291-422 |
5.34e-20 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 90.85 E-value: 5.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 291 RAERKhISESETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLISGE 370
Cdd:COG2202 127 RAEEA-LRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGG 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 16130007 371 INTYSMEKRYynRNGDVVWALLAVSLVRHTDG-TPLYFIAQIEDINELKRTEQ 422
Cdd:COG2202 206 RESYELELRL--KDGDGRWVWVEASAVPLRDGgEVIGVLGIVRDITERKRAEE 256
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
918-1094 |
5.88e-19 |
|
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: 87.22 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 918 LSHALDRRVFHEFFQQAAK-AVASKGISISLPLSVAGLSSATLVNDLLEQLENSPLPPRLLHLIIPAEAILDHAES---- 992
Cdd:cd01948 58 LIVELGRWVLEEACRQLARwQAGGPDLRLSVNLSARQLRDPDFLDRLLELLAETGLPPRRLVLEITESALIDDLEEalat 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 993 VQKLRLAGCRIVLSQVGRDLQIFNSLKANMADYLLLDGELCANVQGNLMDEMLITIIQGHAQRLGMKTIAGPVVLPLVMD 1072
Cdd:cd01948 138 LRRLRALGVRIALDDFGTGYSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVRAIIALAHSLGLKVVAEGVETEEQLE 217
|
170 180
....*....|....*....|..
gi 16130007 1073 TLSGIGVDLIYGEVIADAQPLD 1094
Cdd:cd01948 218 LLRELGCDYVQGYLFSRPLPAE 239
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
900-1088 |
1.88e-17 |
|
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: 82.75 E-value: 1.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 900 EGEIIDEQTFRRSFSDPALSHALDRRVFHEFFQQAAKAVASKGISISLPLSVAGLSSATLVNDLLEQLENSPLPPRLLHL 979
Cdd:pfam00563 41 DGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPDIKLSINLSPASLADPGFLELLRALLKQAGPPPSRLVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 980 IIPAEAIL----DHAESVQKLRLAGCRIVLSQVGRDLQIFNSLKANMADYLLLDGELCANVQGNLMDEMLITIIQGHAQR 1055
Cdd:pfam00563 121 EITESDLLarleALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRALIALAHS 200
|
170 180 190
....*....|....*....|....*....|...
gi 16130007 1056 LGMKTIAGPVVLPLVMDTLSGIGVDLIYGEVIA 1088
Cdd:pfam00563 201 LGIKVVAEGVETEEQLEALRELGCDLVQGYYFS 233
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
676-842 |
2.58e-17 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 85.27 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 676 RQLSYSASHDALTHLANRASFEKQLRILLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSD 755
Cdd:PRK10245 199 RRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSD 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 756 VLARLGGDEFGLLLPDCNVESARFIATRIISAVNDYHFIWEGRVhRVGASAGITLIDDNNHQAAEVMSQADIACYASKNG 835
Cdd:PRK10245 279 VIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQV-TLRISVGVAPLNPQMSHYREWLKSADLALYKAKNA 357
|
....*..
gi 16130007 836 GRGRVTV 842
Cdd:PRK10245 358 GRNRTEV 364
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
677-789 |
2.45e-16 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 82.75 E-value: 2.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 677 QLSYSASHDALTHLANRASFEKQLRILLQTvNSTHQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDV 756
Cdd:PRK09966 243 QLLRTALHDPLTGLANRAAFRSGINTLMNN-SDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321
|
90 100 110
....*....|....*....|....*....|...
gi 16130007 757 LARLGGDEFGLLLPDCNVESArfiATRIISAVN 789
Cdd:PRK09966 322 AYRLGGDEFAMVLYDVQSESE---VQQICSALT 351
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
545-747 |
6.76e-16 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 78.91 E-value: 6.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 545 QLNEALFQEKERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLHItfGDNGPLMENIYSADTS 624
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPP--EDDDEFLELLRAALAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 625 RSAIEQDVVLHCRSGGSYDVHYSITPLSTLDGSNIGSVLVIQDVTESRKMLRQLsysashdalthlanRASfEKQLRILL 704
Cdd:COG2202 79 GGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEAL--------------RES-EERLRLLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 16130007 705 QTVNsthqrHALVFIDLD-RFKAVNDSA----GHAAGDALLRELASLM 747
Cdd:COG2202 144 ENAP-----DGIFVLDLDgRILYVNPAAeellGYSPEELLGKSLLDLL 186
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
311-414 |
1.01e-14 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 71.13 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 311 SAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLISGEINtYSMEKRYYNRNGDVVWA 390
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEP-VTLEVRLRRKDGSVIWV 79
|
90 100
....*....|....*....|....
gi 16130007 391 LLAVSLVRHTDGTPLYFIAQIEDI 414
Cdd:cd00130 80 LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
670-871 |
4.47e-14 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 77.12 E-value: 4.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 670 ESRKMLRQLsysASHDALTHLANRASFEKQLRILLQTVNSThqrhALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLS 749
Cdd:PRK11359 367 KSRQHIEQL---IQFDPLTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 750 MLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAVNDYHFIwEGRVHRVGASAGITLIDDNNHQaaEVMSQADIAC 829
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMI-DDKPFPLTLSIGISYDVGKNRD--YLLSTAHNAM 516
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 16130007 830 -YASKNGGRGrVTVYEPQQAAAHSER----AAMSldeqwRMIKENQL 871
Cdd:PRK11359 517 dYIRKNGGNG-WQFFSPAMNEMVKERlvlgAALK-----EAISNNQL 557
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
451-537 |
4.54e-13 |
|
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: 65.82 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 451 IFSWDKRMFELYEIPPH-IKPNWQVWYECVLPEDRQHAEKVIRDSLQSRSPFKLEFRITVKDG-IRHIRALANRVLNKEG 528
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEeLLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGeYRWVEARARPIRDENG 80
|
....*....
gi 16130007 529 EVERLLGIN 537
Cdd:pfam08447 81 KPVRVIGVA 89
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
550-679 |
3.83e-11 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 66.72 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 550 LFQEKERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLHitfgdNGPLMENIysaDTSRSAIE 629
Cdd:COG3829 6 LKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIP-----NSPLLEVL---KTGKPVTG 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 16130007 630 QdvvLHCRSGGSYDVHYSITPLSTlDGSNIGSVLVIQDVTESRKMLRQLS 679
Cdd:COG3829 78 V---IQKTGGKGKTVIVTAIPIFE-DGEVIGAVETFRDITELKRLERKLR 123
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
297-440 |
8.38e-11 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 64.87 E-value: 8.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 297 ISESETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDlnKDLQQVEKLISGEINTYSM 376
Cdd:COG3852 2 LRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS--PLRELLERALAEGQPVTER 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130007 377 EKRYYNRNGDVVWALLAVSLVRHTDGTPlYFIAQIEDINELKRTEQVNQQLmERITLANE-AGGI 440
Cdd:COG3852 80 EVTLRRKDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERELRRA-EKLAAVGElAAGL 142
|
|
| PRK13561 |
PRK13561 |
putative diguanylate cyclase; Provisional |
673-1094 |
1.73e-10 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 184143 [Multi-domain] Cd Length: 651 Bit Score: 65.12 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 673 KMLRQLSYSASHDALTHLANRASFekqLRILLQTVNSThQRHALVFIdldRFKAVNDSAG---HAAGDALLRELASLMLS 749
Cdd:PRK13561 222 RQYEEQSRNATRFPVSDLPNKALL---MALLEQVVARK-QTTALMII---TCETLRDTAGvlkEAQREILLLTLVEKLKS 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 750 MLRSSDVLARLGGDEFGLLLPDCNV-ESARFIATRIISAVNDYHFIWEGRVhRVGASAGITLIdDNNHQAAEVMSQADIA 828
Cdd:PRK13561 295 VLSPRMVLAQISGYDFAIIANGVKEpWHAITLGQQVLTIINERLPIQRIQL-RPSCSIGIAMF-YGDLTAEQLYSRAISA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 829 CYASKNGGRGRVTVYEPQQAaahsERAamsldeQWRMIKENQLMmlaHGVASPRIPearnLWL------ISLKLWSCEGe 902
Cdd:PRK13561 373 AFTARRKGKNQIQFFDPQQM----EAA------QKRLTEESDIL---NALENHQFA----IWLqpqvemRSGKLVSAEA- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 903 IIDEQTFRRSFSDPA----------LSHALDRRVFHEFFQQAAkAVASKGisISLPLSVaGLSS-----ATLVNDLLEQL 967
Cdd:PRK13561 435 LLRMQQPDGSWDLPEglidriescgLMVTVGHWVLEESCRLLA-AWQERG--IMLPLSV-NLSAlqlmhPNMVADMLELL 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 968 ENSPLPPRLLHLIIPAEAILDHAESV----QKLRLAGCRIVLSQVG------RDLQIFNSLKanmADYLLLDGELcanVQ 1037
Cdd:PRK13561 511 TRYRIQPGTLILEVTESRRIDDPHAAvailRPLRNAGVRVALDDFGmgyaglRQLQHMKSLP---IDVLKIDKMF---VD 584
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16130007 1038 GNLMDEMLITIIQGHAQRLGMKTIAGPVVLPLVMDTLSGIGVDLIYGEVIADAQPLD 1094
Cdd:PRK13561 585 GLPEDDSMVAAIIMLAQSLNLQVIAEGVETEAQRDWLLKAGVGIAQGFLFARALPIE 641
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
555-677 |
2.12e-10 |
|
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain occupies the central portion of the PAS domain but is more widely distributed. It is often tandemly repeated. Known prosthetic groups bound in the S-box domain include heme in the oxygen sensor FixL, FAD in the redox potential sensor NifL, and a 4-hydroxycinnamyl chromophore in photoactive yellow protein. Proteins containing the domain often contain other regulatory domains such as response regulator or sensor histidine kinase domains. Other S-box proteins include phytochromes and the aryl hydrocarbon receptor nuclear translocator. [Regulatory functions, Small molecule interactions]
Pssm-ID: 272971 [Multi-domain] Cd Length: 124 Bit Score: 59.23 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 555 ERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLHItfGDNGPLMENIYSADTSRSAI-EQDVV 633
Cdd:TIGR00229 3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPE--EDREEVRERIERRLEGEPEPvSEERR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 16130007 634 LHCRSGGSYDVHYSITPLSTlDGSNIGSVLVIQDVTEsRKMLRQ 677
Cdd:TIGR00229 81 VRRKDGSEIWVEVSVSPIRT-NGGELGVVGIVRDITE-RKEAEE 122
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
328-416 |
2.34e-10 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 58.24 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 328 NKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLISGEINTysmEKRYYNRNGDVVWALLAVSLVRHTDGTPLYF 407
Cdd:pfam13426 8 NDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVREF---EVVLYRKDGEPFPVLVSLAPIRDDGGELVGI 84
|
....*....
gi 16130007 408 IAQIEDINE 416
Cdd:pfam13426 85 IAILRDITE 93
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
564-668 |
2.34e-10 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 58.41 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 564 IGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLHItfGDNGPLMENIYSADTSRSAIEQDVVLHCRSGGSYD 643
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHP--EDREELRERLENLLSGGEPVTLEVRLRRKDGSVIW 78
|
90 100
....*....|....*....|....*
gi 16130007 644 VHYSITPLSTLDGSNIGSVLVIQDV 668
Cdd:cd00130 79 VLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
542-678 |
3.57e-10 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 63.83 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 542 EVKQLNEalfqekerlhITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVlhitFGDNGPLMENIYSA 621
Cdd:PRK11360 259 ETRSLNE----------LILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSEL----FPPNTPFASPLLDT 324
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 16130007 622 -DTSRSAIEQDVVLHcRSGGSYDVHYSITPLSTLDGSNIGSVLVIQDVTESRKMLRQL 678
Cdd:PRK11360 325 lEHGTEHVDLEISFP-GRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRV 381
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
561-672 |
9.25e-10 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 57.04 E-value: 9.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 561 LDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLhiTFGDNGPLMENI-YSADTSRSAIEQDVVLHCRSG 639
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELL--PPEDAARLERALrRALEGEEPIDFLEELLLNGEE 78
|
90 100 110
....*....|....*....|....*....|...
gi 16130007 640 GSYDVHYsiTPLSTLDGSNIGSVLVIQDVTESR 672
Cdd:pfam08448 79 RHYELRL--TPLRDPDGEVIGVLVISRDITERR 109
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
294-441 |
1.36e-09 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 62.06 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 294 RKHISESETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNkDLQQVEKLISGEINT 373
Cdd:COG5805 149 EEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKE-EFKERIESITEVWQE 227
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130007 374 YSMEKRYYNRNGDVVWALLAVSLVRHTDGTPLYFIAQIEDINELKRTEqvnqQLM---ERITLANE-AGGIG 441
Cdd:COG5805 228 FIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAE----ELMarsEKLSIAGQlAAGIA 295
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
716-813 |
1.85e-09 |
|
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: 56.98 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 716 LVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSML-RSSDVLARLGGDEFGLLLPDCNVESARFIATRI---ISAVNdy 791
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMreaVSALN-- 81
|
90 100
....*....|....*....|....*
gi 16130007 792 hfiWEGRVH---RVGASAGITLIDD 813
Cdd:cd07556 82 ---QSEGNPvrvRIGIHTGPVVVGV 103
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
303-368 |
2.12e-09 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 54.71 E-value: 2.12e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130007 303 HFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLIS 368
Cdd:smart00091 2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
302-414 |
1.93e-08 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 53.58 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 302 THFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLISGEINTYSMEKRYY 381
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|...
gi 16130007 382 NRNGDVVWALLAVSLVRHTDGTPLYFIAQIEDI 414
Cdd:pfam00989 81 VPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
755-833 |
1.06e-07 |
|
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: 52.99 E-value: 1.06e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16130007 755 DVLARLGGDEFGLLLPDCNVESARFIATRIISAVNDYHFIwegrvhRVGASAGITliddnnhqAAEVMSQADiACYASK 833
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPSL------RVTVSIGVA--------GDSLLKRAD-ALYQAR 179
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
576-670 |
1.19e-07 |
|
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor domain. It recognizes FMN, Zn(II), FAD and riboflavin (MAtilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463873 [Multi-domain] Cd Length: 93 Bit Score: 50.54 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 576 KITFMNPVAEKMSGWTQEEALGVPLlTVLHITFGDNGPLMENIysaDTSRSAIEQDVVLHCRSGGSYDVHYSITPLSTLD 655
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLGKSI-TDLFAEPEDSERLREAL---REGKAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78
|
90
....*....|....*
gi 16130007 656 GSNIGSVLVIQDVTE 670
Cdd:pfam13426 79 GELVGIIAILRDITE 93
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
539-670 |
3.42e-07 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 53.81 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 539 DMT-EVKQLNEALFQEKERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLHITFgdngpLMEN 617
Cdd:COG5000 73 RMTdQLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELD-----LAEL 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 16130007 618 IysADTSRSAIEQDVVLHcrSGGSYDVHYSITPLstldgSNIGSVLVIQDVTE 670
Cdd:COG5000 148 L--REALERGWQEEIELT--RDGRRTLLVRASPL-----RDDGYVIVFDDITE 191
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
316-419 |
3.64e-07 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain is associated to signalling systems and works as a signal sensor domain. It recognizes differently substituted aromatic hydrocarbons, oxygen, different dodecanoic acids, autoinducers, 3,5-dimethyl-pyrazin-2-ol and N-alanyl-aminoacetone (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 312075 [Multi-domain] Cd Length: 110 Bit Score: 49.72 E-value: 3.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 316 ALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLtWPEDLNKDLQ-QVEKLISGEINTYSMEkrYYNRNGDVVWALLAV 394
Cdd:pfam08448 9 AVLDPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAARLErALRRALEGEEPIDFLE--ELLLNGEERHYELRL 85
|
90 100
....*....|....*....|....*
gi 16130007 395 SLVRHTDGTPLYFIAQIEDINELKR 419
Cdd:pfam08448 86 TPLRDPDGEVIGVLVISRDITERRR 110
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
375-417 |
3.70e-07 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 47.56 E-value: 3.70e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 16130007 375 SMEKRYYNRNGDVVWALLAVSLVRHTDGTPLYFIAQIEDINEL 417
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
555-605 |
4.66e-07 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 48.16 E-value: 4.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 16130007 555 ERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLH 605
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIH 51
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
291-552 |
5.49e-07 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 53.91 E-value: 5.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 291 RAERKhISESETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTwPEDLNKDLQQV--EKLIS 368
Cdd:PRK13560 194 RAEER-IDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFA-PAQPADDYQEAdaAKFDA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 369 GEINTYSMEKRyyNRNGDVVWALLAVSLVRHTDgtPLYFIAQ----IEDINELKRTEQVNQQLMERITLANEAGGIGIWE 444
Cdd:PRK13560 272 DGSQIIEAEFQ--NKDGRTRPVDVIFNHAEFDD--KENHCAGlvgaITDISGRRAAERELLEKEDMLRAIIEAAPIAAIG 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 445 WELKPNI-FSWD---KRMFELYEIPPHIKPNW---------------QVWYECVLPE--DRQHAEKVIRdslQSRSPFKL 503
Cdd:PRK13560 348 LDADGNIcFVNNnaaERMLGWSAAEVMGKPLPgmdpelneefwcgdfQEWYPDGRPMafDACPMAKTIK---GGKIFDGQ 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 16130007 504 EFRITVKD-GIRHIRALANRVLNKEGEVERLLGINMDMTEVKQLNEALFQ 552
Cdd:PRK13560 425 EVLIEREDdGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLL 474
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
637-1062 |
9.61e-07 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 53.02 E-value: 9.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 637 RSGGSYDVHYSITPLSTLDGSNIGSVLV------IQDVTESRKMLRQLSYSASHdalTHLANRASFekqLRILLQTVNST 710
Cdd:PRK11829 184 EDIGDHGVLHHQLTLPAHHQDDELGVLVrnynrnQQLLADAYADMGRISHRFPV---TELPNRSLF---ISLLEKEIASS 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 711 --HQRHALVFIDLDRFKAVNDSAGHAAGDALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVES-ARFIATRIISA 787
Cdd:PRK11829 258 trTDHFHLLVIGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFpAMQLARRIMSQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 788 VNDYHFIWEGRVhRVGASAGITLIDDNNHQAAEVMSQADIACYASKNGGRGRVTVYEPQQAaahsERAamsldeQWRMIK 867
Cdd:PRK11829 338 VTQPLFFDEITL-RPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPHLI----EKT------HKRLTQ 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 868 ENQLM-MLAHG-----------VASPRIPEARNLwlisLKLWSCEGEIIDEQTFRRSFSDPALSHALDRRVFHEffqqAA 935
Cdd:PRK11829 407 ENDLLqAIENHdftlflqpqwdMKRQQVIGAEAL----LRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEE----AC 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 936 KAVA---SKGISISLPLSVAGL--SSATLVNDLLEQLENSPLPPRLLHLIIPAEA----ILDHAESVQKLRLAGCRIVLS 1006
Cdd:PRK11829 479 RILAdwkARGVSLPLSVNISGLqvQNKQFLPHLKTLISHYHIDPQQLLLEITETAqiqdLDEALRLLRELQGLGLLIALD 558
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 16130007 1007 QVG---RDLQIFNSLKANMADYLLLDGELCANVQgnlMDEMLITIIQGHAQRLGMKTIA 1062
Cdd:PRK11829 559 DFGigySSLRYLNHLKSLPIHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMA 614
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
555-668 |
1.15e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya. This domain can bind gases (O2, CO and NO), FAD, 4-hydroxycinnamic acid and NAD+ (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 395786 [Multi-domain] Cd Length: 113 Bit Score: 48.18 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 555 ERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLHITFGDNGP-LMENIYSADTSRSAIEQDVV 633
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAeLLRQALLQGEESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|....*
gi 16130007 634 LHCrsGGSYDVHYSITPLSTLDGSNIGSVLVIQDV 668
Cdd:pfam00989 81 VPD--GRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
441-540 |
3.07e-06 |
|
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising identification of a PAS domain was that in EAG-like K+-channels. PAS domains have been found to bind ligands, and to act as sensors for light and oxygen in signal transduction.
Pssm-ID: 238075 [Multi-domain] Cd Length: 103 Bit Score: 46.86 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 441 GIWEWELKPNIFSWDKRMFELYEIPPHIKPNwQVWYECVLPEDRQHAEKVIRDSLQSRSPFKLEFRITVKDG-IRHIRAL 519
Cdd:cd00130 4 GVIVLDLDGRILYANPAAEQLLGYSPEELIG-KSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGsVIWVLVS 82
|
90 100
....*....|....*....|.
gi 16130007 520 ANRVLNKEGEVERLLGINMDM 540
Cdd:cd00130 83 LTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
328-409 |
4.46e-06 |
|
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined as PAS and PAC motifs. The PAS fold appears in archaea, eubacteria and eukarya.
Pssm-ID: 430001 [Multi-domain] Cd Length: 89 Bit Score: 45.79 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 328 NKALCQFLGYSQEELRGL--TFQQLTWPEDLNKDLQQVEKLISGEINtYSMEKRYYNRNGDVVWALLAVSLVRHTDGTPL 405
Cdd:pfam08447 5 SPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGEP-YSGEYRIRRKDGEYRWVEARARPIRDENGKPV 83
|
....
gi 16130007 406 YFIA 409
Cdd:pfam08447 84 RVIG 87
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
665-788 |
5.63e-06 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 50.63 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 665 IQDVTESRKMLRQL--SYSAsHDALTHLANRASFEKQLRILL--QTVNSTHQrhALVFIDLDRFKAVNDSAGHAAGDALL 740
Cdd:PRK11059 210 LQDAREERSRFDTFirSNAF-QDAKTGLGNRLFFDNQLATLLedQEMVGAHG--VVMLIRLPDFDLLQEEWGESQVEELL 286
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 16130007 741 RELASlMLS--MLRSSD-VLARLGGDEFGLLLPDCNVESARFIATRIISAV 788
Cdd:PRK11059 287 FELIN-LLStfVMRYPGaLLARYSRSDFAVLLPHRSLKEADSLASQLLKAV 336
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
502-542 |
3.31e-05 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 42.17 E-value: 3.31e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 16130007 502 KLEFRITVKDG-IRHIRALANRVLNKEGEVERLLGINMDMTE 542
Cdd:smart00086 1 TVEYRLRRKDGsYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
|
|
| PAS_8 |
pfam13188 |
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ... |
555-605 |
2.59e-04 |
|
PAS domain; PAS domains are involved in many signalling proteins where they are used as a signal sensor domain. PAS domains appear in archaea, bacteria and eukaryotes. Several PAS-domain proteins are known to detect their signal by way of an associated cofactor. Heme, flavin, and a 4-hydroxycinnamyl chromophore are used in different proteins. This domain recognizes oxygen and CO (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 463802 [Multi-domain] Cd Length: 65 Bit Score: 40.23 E-value: 2.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 16130007 555 ERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWTQEEALGVPLLTVLH 605
Cdd:pfam13188 1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLD 51
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
533-690 |
1.21e-03 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 42.53 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 533 LLGINMDMTEVKQLNEALFQEKERLHITLDSIGEAVVCIDMAMKITFMNPVAEKMSGWtqeEALGVPLLTVLhitfgdng 612
Cdd:COG3290 62 LLLLLLLAALLLKLLEEIARLVEEREAVLESIREGVIAVDRDGRITLINDAARRLLGL---DAIGRPIDEVL-------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 613 plMENIYSADTSRSAIEQDVVLHCrsggsydvhySITPLsTLDGSNIGSVLVIQDVTESRKMLRQLSY---------SAS 683
Cdd:COG3290 131 --AEVLETGERDEEILLNGRVLVV----------NRVPI-RDDGRVVGAVATFRDRTELERLEEELEGvkelaealrAQR 197
|
....*..
gi 16130007 684 HDALTHL 690
Cdd:COG3290 198 HDFRNHL 204
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
289-432 |
2.87e-03 |
|
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];
Pssm-ID: 444024 [Multi-domain] Cd Length: 422 Bit Score: 41.49 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 289 AFRAERKHISESETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQV-EKLI 367
Cdd:COG5000 77 QLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREAlERGW 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130007 368 SGEINtysmekryYNRNGDVVWALLAVSLVrhTDGTPLYFiaqiEDINELKRTEQVN--QQLMERIT 432
Cdd:COG5000 157 QEEIE--------LTRDGRRTLLVRASPLR--DDGYVIVF----DDITELLRAERLAawGELARRIA 209
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
292-422 |
3.86e-03 |
|
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];
Pssm-ID: 443041 [Multi-domain] Cd Length: 448 Bit Score: 40.91 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130007 292 AERKHISESETHFRNAMEYSAIGMALVGTEGQWLQTNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLISgei 371
Cdd:COG3829 1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNSPLLEVLKTGKPVTG--- 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 16130007 372 ntysmekRYYNRNGDVVWALLAVSLVRHtDGTPLYFIAQIEDINELKRTEQ 422
Cdd:COG3829 78 -------VIQKTGGKGKTVIVTAIPIFE-DGEVIGAVETFRDITELKRLER 120
|
|
| |
