|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
20-1109 |
0e+00 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 1879.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 20 VSLGLVTFIFTLFSLELTRFGTFLAPLWFPTSIMMVAFYRHAGKMWPGIALACSVGNIFATWLIFSWDAINLWYTGINVL 99
Cdd:PRK09776 1 VSLGLVSFIFTLFSLELSRFPTTLAPLWFPTAIMMVAFYRHAGRMWPGILLSCSLGNIAANILLFSTSSLNLTWTTINLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 100 EAIVGALLLRKLLPGYNPLQNLGDWIRLALGSALIPPLLGGVLVWQLVPSDEPLRSFMVWVLSESVGALALVPLGLLFKP 179
Cdd:PRK09776 81 EAVVGAVLLRKLLPWYNPLQNLADWLRLALGSAIVPPLLGGVLVVLLTPGDDPLRAFLIWVLSEAIGMLALVPLGLLFKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 180 HYLLRHRNPRLLFETLLTMVVTLLLSWIALHFLPWPFTAIIVLLMWSAVRLPRLEAFLVFLVTVMMVSLMIAKNPVPLTT 259
Cdd:PRK09776 161 HYLLRHRNPRLLFESLLTLAITLTLSWLALLYLPWPFTFIIVLLMWSAVRLPRMEAFLIFLTTVMMVSLMMAADPSLLAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 260 QNFGAMTNAPWLPFLMMLLPANVMTMVMYAFRAERKHITESEERFRNAMEYSVIGMALVSTDGQWLQANKALCQFLGYSQ 339
Cdd:PRK09776 241 PRTYLMSHMPWLPFLLILLPANIMTMVMYAFRAERKHISESETRFRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 340 AELRSLSFQQLTWPEDLESDLEQLDQLLQGKINSYSLEKRYYTRSGEVVWALLAVSLVRHADGTPLYFIAQVEDINDLKH 419
Cdd:PRK09776 321 EELRGLTFQQLTWPEDLNKDLQQVEKLLSGEINSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKR 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 420 TEWVNKRLMERITLANEAGGIGIWEWDVKPNVISWDKRMFELYEVPPHVKPTWQLWHESMLPEDRAMAEQVVRDSLAARV 499
Cdd:PRK09776 401 TEQVNERLMERITLANEAGGIGIWEWDLKPNIISWDKRMFELYEIPPHIKPTWQVWYACLHPEDRQRVEKEIRDALQGRS 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 500 PFKLEFRIRVKDGVRHIRALANRVLNKQGEVERLLGINMDMTEVKELNEALFQEKERLHITLDSIGEAVLCTDVNMNVTF 579
Cdd:PRK09776 481 PFKLEFRIVVKDGVRHIRALANRVLNKDGEVERLLGINMDMTEVRQLNEALFQEKERLHITLDSIGEAVVCTDMAMKVTF 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 580 MNPVAEKMSGWLQEEALSQPILSVLHITFGDNGPLMENIHSGDMSRSD--IEQDVVLHNRNGGSYDIHYSITPLSTLDGQ 657
Cdd:PRK09776 561 MNPVAEKMTGWTQEEALGVPLLTVLHITFGDNGPLMENIYSCLTSRSAayLEQDVVLHCRSGGSYDVHYSITPLSTLDGE 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 658 NIGSVLVIQDVTESRKMLRELSYNASHDALTHLANRVSFEASLKRMLHTVQETRQRHALVFIDLDRFKAVNDTAGHAAGD 737
Cdd:PRK09776 641 NIGSVLVIQDVTESRKMLRQLSYSASHDALTHLANRASFEKQLRRLLQTVNSTHQRHALVFIDLDRFKAVNDSAGHAAGD 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 738 ALLRELSSLMLSMLRSTDMLARLGGDEFGLLLPDCNTESARYIAGRIIDAINGYHFMWEGRLHRIGASAGITQIDERNNQ 817
Cdd:PRK09776 721 ALLRELASLMLSMLRSSDVLARLGGDEFGLLLPDCNVESARFIATRIISAINDYHFPWEGRVYRVGASAGITLIDANNHQ 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 818 ASEVMSQADIACYSSKNSGRGVVTVYEPQQERMLNAPGAISLDEQWHMIKDNHLLMIARSVASPRTPESSTFWMLALRLW 897
Cdd:PRK09776 801 ASEVMSQADIACYAAKNAGRGRVTVYEPQQAAAHSEHRALSLAEQWRMIKENQLMMLAHGVASPRIPEARNHWLISLRLW 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 898 TNDGEMLEEQAFRAGLAEPELIHALDRRILQEFFRNFATPLTNKGTGVALPLSMAGLASATLVDELLEMLHACPLQTRLL 977
Cdd:PRK09776 881 DPEGEIIDEGAFRPAAEDPALMHALDRRVIHEFFRQAAKAVASKGLSIALPLSVAGLSSPTLLPFLLEQLENSPLPPRLL 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 978 HLIVNVSVLTQEDDNTHHNLQKLREAGCRIILSHVGRDMEVFNHLSAQMADYLLLDPELVANVHGNLMDEMLVTIIQGHA 1057
Cdd:PRK09776 961 HLEITETALLNHAESASRLVQKLRLAGCRVVLSDFGRGLSSFNYLKAFMADYLKLDGELVANLHGNLMDEMLISIIQGHA 1040
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|..
gi 1782164966 1058 QRLGIKTIAGPSNQPIMMDTLSGIGIDYIYGNTIGEPQPLELLLNTSYFGIN 1109
Cdd:PRK09776 1041 QRLGMKTIAGPVELPLVLDTLSGIGVDLAYGYAIARPQPLDLLLNSSYFAIN 1092
|
|
| MASE1 |
COG3447 |
Integral membrane sensor domain MASE1 [Signal transduction mechanisms]; |
6-635 |
2.40e-109 |
|
Integral membrane sensor domain MASE1 [Signal transduction mechanisms];
Pssm-ID: 442670 [Multi-domain] Cd Length: 637 Bit Score: 355.27 E-value: 2.40e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 6 QRVLVTTPHPLLRLVSLGLVTFIFTLFSLELTRFGTFLAPLWFPTSIMMVAFYRHAGKMWPGIALACSVGNIFATWLIFS 85
Cdd:COG3447 4 SSALGTPGRPLLRLLLLALLYFLLALLGLLLARPPGGVSPIWPPAGVALAALLRFGRRAWPGILLGALLANLLAGLTGDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 86 WdAINLWYTGINVLEAIVGALLLRKLLPGYNPLQNLGDWIRLALGSALIPPLLGGVLVW------QLVPSDEPLRSFMVW 159
Cdd:COG3447 84 L-LLALLIALGNTLEALLAAWLLRRLLGFSPPLQRLRDVLRFLLAAALLAPLISALLGAlalalaGLLPGSPFLSSWLTW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 160 VLSESVGALALVPLGLLFKPHYLLRHRnPRLLFETLLTMVVTLLLSWIALHFLPWPFTAIIV-LLMWSAVRLPRLEAFLV 238
Cdd:COG3447 163 WLGDALGILLVTPLLLAWRRPRLRRLR-RRRLLEALALLALLLLVSWLVFGLLGYPLAFLLFpLLLWAALRFGLRGAALA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 239 FLVTVMMVSLMIAKNPVPLTTQNFGAMTNAPWLPFLMMLLPANVMTMVMYAFRaeRKHITESEERFRNAMEYSVIGMALV 318
Cdd:COG3447 242 VLLLALIAILATALGLGPFASLSPNQSLLLLQLFLAVLALTGLLLAAALAERR--RQRLRERELALRAALELLALGLLLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 319 STDGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDLESDLEQLDQLLQGKINSYSLEKRYYTRSGEVVWALLAVSLVR 398
Cdd:COG3447 320 ALDDALLLLNARGLLLLALSLAALLLLRLALLLLLLALDALLLLLADDDRGELRGDLLRRRGATRLGAVVARLLRRSGGR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 399 HADGTPLYFIAQVEDINDLKHTEWVNKRLMERITLANEAGGIGIWEWDVKPNVISWDKRMFELYEVPPHVKPTWQLWHES 478
Cdd:COG3447 400 GEEVVVLLVIAQVEEALELALRERREERLLERLALALELLAITAALLAAALLLALADLLLLLLAEAAQLLARALLLGLDR 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 479 MLPEDRAMAEQVVRDSLAARVPFKLEFRIRVKDGVRHIRALANRVLNKQGEVERLLGINMDMTEVKELNEALFQEKERLH 558
Cdd:COG3447 480 LLADAALAALAALADLLGALLSAGLRRRGGRRLGARLIRSLLSRVLAELGAVELLLALIADLTEVALGAEALERLLERLL 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1782164966 559 ITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHITFGDNGPLMENIHSGDMSRSDIEQDVVLH 635
Cdd:COG3447 560 LALLGLGLAVAALLATLGLLLALLAALALSGAAALLALGAALLLAAAILGLAAALLALLRLLGERARLLETRRLVGA 636
|
|
| COG5001 |
COG5001 |
Cyclic di-GMP metabolism protein, combines GGDEF and EAL domains with a 6TM membrane domain ... |
472-1098 |
8.05e-62 |
|
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: 224.27 E-value: 8.05e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 472 WQLWHESMLPEDRAMAEQVVRDSLAARVPFKLEFRIRVKDGVRHIRALANRVLNKQGEVERLLGINMDMTEVKELNEALF 551
Cdd:COG5001 37 ALLLLLLLLLLALLLAALLLLALLALLALLLLAAALLALALAALLLAALLAALLLLLLLLLALLVLLLLLLLLLALLALL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 552 QEKERLHITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHITFGDNGPLMENIHSGDMSRSDIEQD 631
Cdd:COG5001 117 AALLARALAALLLAAASAALLAAALGAALLAALALALLLALARALLALLLLLLLALLLLLLLLLLLALLLLLLLALLLRL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 632 VVLHNRNGGSYDIHYSITPLSTLDGQN----IGSVLVIQDVTESRKMLRELSYNASHDALTHLANRVSFEASLKRMLHTV 707
Cdd:COG5001 197 LLLLRGGRLLRLALRLLLGLLLLGLLLllllVAVLAIARLITERKRAEERLRHLAYHDPLTGLPNRRLFLDRLEQALARA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 708 QETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLGGDEFGLLLPDC-NTESARYIAGRIID 786
Cdd:COG5001 277 RRSGRRLALLFIDLDRFKEINDTLGHAAGDELLREVARRLRACLREGDTVARLGGDEFAVLLPDLdDPEDAEAVAERILA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 787 AINGyHFMWEGRLHRIGASAGITQIDERNNQASEVMSQADIACYSSKNSGRGVVTVYEPQQERMLNA--------PGAIS 858
Cdd:COG5001 357 ALAE-PFELDGHELYVSASIGIALYPDDGADAEELLRNADLAMYRAKAAGRNRYRFFDPEMDERARErleleadlRRALE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 859 LDEqwhmikdnhllmiarsvasprtpesstfwmlaLRLW------TNDGEMLeeqAFRA------------------GLA 914
Cdd:COG5001 436 RGE--------------------------------LELHyqpqvdLATGRIV---GAEAllrwqhperglvspaefiPLA 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 915 EpE--LIHALDRRILQEFFRNFAT--PLTNKGTGVALPLSMAGLASATLVDELLEMLHACPLQTRLLHLIVNVSVLTQED 990
Cdd:COG5001 481 E-EtgLIVPLGEWVLREACRQLAAwqDAGLPDLRVAVNLSARQLRDPDLVDRVRRALAETGLPPSRLELEITESALLEDP 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 991 DNTHHNLQKLREAGCRI-I---------LSHVgRDMEVfnhlsaqmaDYLLLDPELVANVHGNLMDEMLVTIIQGHAQRL 1060
Cdd:COG5001 560 EEALETLRALRALGVRIaLddfgtgyssLSYL-KRLPV---------DTLKIDRSFVRDLAEDPDDAAIVRAIIALAHSL 629
|
650 660 670
....*....|....*....|....*....|....*....
gi 1782164966 1061 GIKTIA-GPSNQPImMDTLSGIGIDYIYGNTIGEPQPLE 1098
Cdd:COG5001 630 GLEVVAeGVETEEQ-LEFLRELGCDYAQGYLFSRPLPAE 667
|
|
| GGDEF |
COG2199 |
GGDEF domain, diguanylate cyclase (c-di-GMP synthetase) or its enzymatically inactive variants ... |
644-843 |
1.40e-59 |
|
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: 205.98 E-value: 1.40e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 644 IHYSITPLSTLDGQNIGSVLVIQDVTESRKMLRELSYNASHDALTHLANRVSFEASLKRMLHTVQETRQRHALVFIDLDR 723
Cdd:COG2199 76 LLSLVLELLLLLLALLLLLLALEDITELRRLEERLRRLATHDPLTGLPNRRAFEERLERELARARREGRPLALLLIDLDH 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 724 FKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLGGDEFGLLLPDCNTESARYIAGRIIDAINGYHFMWEGRLHRIG 803
Cdd:COG2199 156 FKRINDTYGHAAGDEVLKEVARRLRASLRESDLVARLGGDEFAVLLPGTDLEEAEALAERLREALEQLPFELEGKELRVT 235
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1782164966 804 ASAGITQIDERNNQASEVMSQADIACYSSKNSGRGVVTVY 843
Cdd:COG2199 236 VSIGVALYPEDGDSAEELLRRADLALYRAKRAGRNRVVVY 275
|
|
| GGDEF |
cd01949 |
Diguanylate-cyclase (DGC) or GGDEF domain; Diguanylate-cyclase (DGC) or GGDEF domain: ... |
684-840 |
3.13e-54 |
|
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: 185.84 E-value: 3.13e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 684 HDALTHLANRVSFEASLKRMLHTVQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLGGD 763
Cdd:cd01949 2 TDPLTGLPNRRAFEERLERLLARARRSGRPLALLLIDIDHFKQINDTYGHAAGDEVLKEVAERLRSSLRESDLVARLGGD 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1782164966 764 EFGLLLPDCNTESARYIAGRIIDAINGYHFMWEGRLHrIGASAGITQIDERNNQASEVMSQADIACYSSKNSGRGVV 840
Cdd:cd01949 82 EFAILLPGTDLEEAEALAERLREAIEEPFFIDGQEIR-VTASIGIATYPEDGEDAEELLRRADEALYRAKRSGRNRV 157
|
|
| GGDEF |
pfam00990 |
Diguanylate cyclase, GGDEF domain; This domain is found linked to a wide range of ... |
682-838 |
1.03e-47 |
|
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: 167.43 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 682 ASHDALTHLANRVSFEASLKRMLHTVQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLG 761
Cdd:pfam00990 1 AAHDPLTGLPNRRYFEEQLEQELQRALREGSPVAVLLIDLDNFKRINDTYGHSVGDEVLQEVAQRLSSSLRRSDLVARLG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1782164966 762 GDEFGLLLPDCNTESARYIAGRIIDAINGYHFMWEGRLHR--IGASAGITQIDERNNQASEVMSQADIACYSSKNSGRG 838
Cdd:pfam00990 81 GDEFAILLPETSLEGAQELAERIRRLLAKLKIPHTVSGLPlyVTISIGIAAYPNDGEDPEDLLKRADTALYQAKQAGRN 159
|
|
| GGDEF |
smart00267 |
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria. |
680-843 |
3.05e-47 |
|
diguanylate cyclase; Diguanylate cyclase, present in a variety of bacteria.
Pssm-ID: 128563 [Multi-domain] Cd Length: 163 Bit Score: 166.27 E-value: 3.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 680 YNASHDALTHLANRVSFEASLKRMLHTVQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLAR 759
Cdd:smart00267 1 RLAFRDPLTGLPNRRYFEEELEQELQRAQRQGSPFALLLIDLDNFKDINDTYGHAVGDELLQEVAQRLSSCLRPGDLLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 760 LGGDEFGLLLPDCNTESARYIAGRIIDAINGYHFMWEGRLHrIGASAGITQIDERNNQASEVMSQADIACYSSKNSGRGV 839
Cdd:smart00267 81 LGGDEFALLLPETSLEEAIALAERILQQLREPIIIHGIPLY-LTISIGVAAYPNPGEDAEDLLKRADTALYQAKKAGRNQ 159
|
....
gi 1782164966 840 VTVY 843
Cdd:smart00267 160 VAVY 163
|
|
| EAL |
COG2200 |
EAL domain, c-di-GMP-specific phosphodiesterase class I (or its enzymatically inactive variant) ... |
532-1102 |
4.18e-47 |
|
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: 178.44 E-value: 4.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 532 RLLGINMDMTEVKELNEALFQEKERLHITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHITFGDN 611
Cdd:COG2200 1 LLLLLALLRERLLLLLLALLAEALALLLLLALLLLALASALLLAVAALLAALLAALLLLLALALLLLLLLLLLLLLLLLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 612 GPLMENIHSGDMSRSDIEQDVVLHNRNGGSYDIHYSITPLSTLDGQN--IGSVLVIQDVTESRKMLRELSYNASHDALTH 689
Cdd:COG2200 81 LLLALLLLLLLLLLLLLLLLLLLALLLAALLALLLLLLLLLLLLLLSllLLLVLVLLRLALELLLALLLLALLALLDLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 690 LANRVSFEASLKRMLHTVQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLGGDEFGLLL 769
Cdd:COG2200 161 LLLLRRLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLDNDGLGGAGLLLLLLLALLLLLLLARLLLALLGGGGGGFLL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 770 PDCNTESARYIAGRIIDAINGYHFMWEGRLHRIGASAGITQIDERNNQASEVMSQADIACYSSKNSGRGVVTVYEPQQER 849
Cdd:COG2200 241 LLLLLAAAAAAAAALRLLLLLLLEPLLLGGGLVVVASSGGGAAAPDDGADAALLLAAAAAAAAAAAGGGRGRVVFFAAAE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 850 MLNAPGAISLDEQWHMIKDNHLLMIARSVASPRTPEssTFWMLAL-RLWTNDGEMLEEQAFRAGLAEPELIHALDRRILQ 928
Cdd:COG2200 321 ARARRRLALESELREALEEGELRLYYQPIVDLRTGR--VVGYEALlRWRHPDGGLISPAEFIPAAERSGLIVELDRWVLE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 929 EFFRNFAT-PLTNKGTGVALPLSMAGLASATLVDELLEMLHACPLQTRLLHLIVNVSVLTQEDDNTHHNLQKLREAGCRI 1007
Cdd:COG2200 399 RALRQLARwPERGLDLRLSVNLSARSLLDPDFLERLLELLAEYGLPPERLVLEITESALLEDLEAAIELLARLRALGVRI 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 1008 ILSHVGRDMEVFNHLSAQMADYLLLDPELVANVHGNLMDEMLVTIIQGHAQRLGIKTIAGPSNQPIMMDTLSGIGIDYIY 1087
Cdd:COG2200 479 ALDDFGTGYSSLSYLKRLPPDYLKIDRSFVRDIARDPRDQAIVRAIVALAHRLGLKVVAEGVETEEQLEALRELGCDYAQ 558
|
570
....*....|....*
gi 1782164966 1088 GNTIGEPQPLELLLN 1102
Cdd:COG2200 559 GYLFGRPLPLEELEA 573
|
|
| EAL |
smart00052 |
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a ... |
860-1099 |
2.87e-35 |
|
Putative diguanylate phosphodiesterase; Putative diguanylate phosphodiesterase, present in a variety of bacteria.
Pssm-ID: 214491 [Multi-domain] Cd Length: 242 Bit Score: 134.65 E-value: 2.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 860 DEQWHMIKDNHLLMI-ARSVASPRTPEssTFWMLALRLWTN-DGEMLEEQAFRAGLAEPELIHALDRRILQEFFRNFATP 937
Cdd:smart00052 1 ERELRQALENGQFLLyYQPIVSLRTGR--LVGVEALIRWQHpEGGIISPDEFIPLAEETGLIVPLGRWVLEQACQQLAEW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 938 LTNKGTG--VALPLSMAGLASATLVDELLEMLHACPLQTRLLHLIVNVSVLTQEDDNTHHNLQKLREAGCRIILSHVGRD 1015
Cdd:smart00052 79 QAQGPPPllISINLSARQLISPDLVPRVLELLEETGLPPQRLELEITESVLLDDDESAVATLQRLRELGVRIALDDFGTG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 1016 MEVFNHLSAQMADYLLLDPELVANVHGNLMDEMLVTIIQGHAQRLGIKTIAGPSNQPIMMDTLSGIGIDYIYGNTIGEPQ 1095
Cdd:smart00052 159 YSSLSYLKRLPVDLLKIDKSFVRDLQTDPEDEAIVQSIIELAQKLGLQVVAEGVETPEQLDLLRSLGCDYGQGYLFSRPL 238
|
....
gi 1782164966 1096 PLEL 1099
Cdd:smart00052 239 PLDD 242
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
292-550 |
9.80e-34 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 130.92 E-value: 9.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 292 AERKHITESEERFRNAMEYSVIGMALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDLESDLEQLDQLLQGKi 371
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 372 NSYSLEKRYYTRSGEVVWALLAVSLVRHADGTPLYFIAQVEDINDLKHTEwvnKRL---MERITLANEAGGIGIWEWDVK 448
Cdd:COG2202 80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAE---EALresEERLRLLVENAPDGIFVLDLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 449 PNVISWDKRMFELYEVPPH---VKPTWQLWHESMLPEDRAMAEQVVRDSlaaRVPFKLEFRIRVKDGVRHIRALANRVLN 525
Cdd:COG2202 157 GRILYVNPAAEELLGYSPEellGKSLLDLLHPEDRERLLELLRRLLEGG---RESYELELRLKDGDGRWVWVEASAVPLR 233
|
250 260
....*....|....*....|....*
gi 1782164966 526 KQGEVERLLGINMDMTEVKELNEAL 550
Cdd:COG2202 234 DGGEVIGVLGIVRDITERKRAEEAL 258
|
|
| MASE1 |
pfam05231 |
MASE1; Predicted integral membrane sensory domain found in histidine kinases, diguanylate ... |
16-295 |
1.09e-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: 129.07 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 16 LLRLVSLGLVTFIFTLFSLELTRFGTFLAPLWFPTSIMMVAFYRHAGKMWPGIALACSVGNIFATWLIFSWDAINLWYTG 95
Cdd:pfam05231 1 LLLLLLLLYALLAAVSLSLALALVSSGSAPIWLPTGLALAALLLFGRRGWPGILLGAVLASLMAGLLSGLNLLLALAIAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 96 INVLEAIVGALLLRKLLPGYNPLQNLGDWIRLALGSALIPPLLG-----GVLVWQLVPSDEPLRSFMV-WVLSESVGALA 169
Cdd:pfam05231 81 VNALEALLGAALLRRLLPGRNRLQRLRFWLRLVIPGAIIAALLLaiiglALLLLLGLIPLAPFSIVWLtWWLGSATGVLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 170 LVPLGLLFKPHYLLRHRNP----RLLFETLLTMVVTLLLSWIALH-----------FLPWPFTAIIVLLMWSAVRLPRLE 234
Cdd:pfam05231 161 VTPLLLLLRRYLRLRHRLRlwyeRDLAPAAAKLLLLFALLLLLILsllllllcmpeINYPLGYLLLPPLLWAAFRFGVRG 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1782164966 235 AFL-VFLVTVMMVSLMIAKNPVPLTTQNFGAMTNAPWLPFLMMLLPANvmtMVMYAFRAERK 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 |
1.98e-30 |
|
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: 118.21 E-value: 1.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 682 ASHDALTHLANRVSFEASLKRMLHTVQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLG 761
Cdd:TIGR00254 2 AVRDPLTGLYNRRYLEEMLDSELKRARRFQRSFSVLMIDIDNFKKINDTLGHDVGDEVLREVARILQSSVRGSDVVGRYG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 762 GDEFGLLLPDCNTESARYIAGRIIDAINGYHFMWEGR-LHRIGASAGITQIDERNNQASEVMSQADIACYSSKNSGRGVV 840
Cdd:TIGR00254 82 GEEFVVILPGTPLEDALSKAERLRDAINSKPIEVAGSeTLTVTVSIGVACYPGHGLTLEELLKRADEALYQAKKAGRNRV 161
|
..
gi 1782164966 841 TV 842
Cdd:TIGR00254 162 VV 163
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
300-421 |
4.17e-30 |
|
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: 115.47 E-value: 4.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 300 SEERFRNAMEYSVIGMALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDLESDLEQLDQLLQGKINSYSLEKR 379
Cdd:TIGR00229 1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEERR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1782164966 380 YYTRSGEVVWALLAVSLVRhADGTPLYFIAQVEDINDLKHTE 421
Cdd:TIGR00229 81 VRRKDGSEIWVEVSVSPIR-TNGGELGVVGIVRDITERKEAE 121
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
685-840 |
2.48e-29 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 122.70 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 685 DALTHLANRVSFEASLKRMLHTVQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLGGDE 764
Cdd:PRK09581 295 DGLTGLHNRRYFDMHLKNLIERANERGKPLSLMMIDIDHFKKVNDTYGHDAGDEVLREFAKRLRNNIRGTDLIARYGGEE 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1782164966 765 FGLLLPDCNTESARYIAGRIIDAINGYHFMWEG--RLHRIGASAGITQIDERNNQASEVMSQADIACYSSKNSGRGVV 840
Cdd:PRK09581 375 FVVVMPDTDIEDAIAVAERIRRKIAEEPFIISDgkERLNVTVSIGVAELRPSGDTIEALIKRADKALYEAKNTGRNRV 452
|
|
| PRK15426 |
PRK15426 |
cellulose biosynthesis regulator YedQ; |
676-850 |
3.59e-29 |
|
cellulose biosynthesis regulator YedQ;
Pssm-ID: 237964 [Multi-domain] Cd Length: 570 Bit Score: 123.97 E-value: 3.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 676 RELSYNASHDALTHLANRVSFEASLKRMLHTVQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTD 755
Cdd:PRK15426 392 SSLQWQAWHDPLTRLYNRGALFEKARALAKRCQRDQQPFSVIQLDLDHFKSINDRFGHQAGDRVLSHAAGLISSSLRAQD 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 756 MLARLGGDEFGLLLPDCNTESARYIAGRIIDAINGYH-FMWEGRLHRIGASAGITQIDERNNQASEVM-SQADIACYSSK 833
Cdd:PRK15426 472 VAGRVGGEEFCVVLPGASLAEAAQVAERIRLRINEKEiLVAKSTTIRISASLGVSSAEEDGDYDFEQLqSLADRRLYLAK 551
|
170
....*....|....*..
gi 1782164966 834 NSGRGVVTVYEPQQERM 850
Cdd:PRK15426 552 QAGRNRVCASDNAHERE 568
|
|
| PRK10060 |
PRK10060 |
cyclic di-GMP phosphodiesterase; |
667-1096 |
9.43e-29 |
|
cyclic di-GMP phosphodiesterase;
Pssm-ID: 236645 [Multi-domain] Cd Length: 663 Bit Score: 123.64 E-value: 9.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 667 DVTESRKMLRELSYNASHDALTHLANRvsfEASLKRMLHTVQE-TRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSS 745
Cdd:PRK10060 222 DITEERRAQERLRILANTDSITGLPNR---NAIQELIDHAINAaDNNQVGIVYLDLDNFKKVNDAYGHMFGDQLLQDVSL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 746 LMLSMLRSTDMLARLGGDEFGLLLPDCNTESARYIAGRIIDaingyhfmwegRLH---RIG-------ASAGITQIDERN 815
Cdd:PRK10060 299 AILSCLEEDQTLARLGGDEFLVLASHTSQAALEAMASRILT-----------RLRlpfRIGlievytgCSIGIALAPEHG 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 816 NQASEVMSQADIACYSSKNSGRGVVTVYEPQQERMLNApgAISLDEQWHMIKDNHLLMI-----------ARSVAsprtp 884
Cdd:PRK10060 368 DDSESLIRSADTAMYTAKEGGRGQFCVFSPEMNQRVFE--YLWLDTNLRKALENDQLVIhyqpkitwrgeVRSLE----- 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 885 esstfwmlALRLWTN-DGEMLEEQAFRAGLAEPELIHALDRRILQEFFRNFATpLTNKGTG--VALPLSMAGLASATLVD 961
Cdd:PRK10060 441 --------ALVRWQSpERGLIPPLEFISYAEESGLIVPLGRWVMLDVVRQVAK-WRDKGINlrVAVNVSARQLADQTIFT 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 962 ELLEMLHACPLQTRLLHLIVNVSVLTQEDDNTHHNLQKLREAGCRIILSHVGRDMEVFNHLSAQMADYLLLDPELVANVH 1041
Cdd:PRK10060 512 ALKQALQELNFEYCPIDVELTESCLIENEELALSVIQQFSQLGAQVHLDDFGTGYSSLSQLARFPIDAIKLDQSFVRDIH 591
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1782164966 1042 GNLMDEMLVTIIQGHAQRLGIKTIAGPSNQPIMMDTLSGIGIDYIYGNTIGEPQP 1096
Cdd:PRK10060 592 KQPVSQSLVRAIVAVAQALNLQVIAEGVETAKEDAFLTKNGVNERQGFLFAKPMP 646
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
425-678 |
3.43e-28 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 114.74 E-value: 3.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 425 KRLMERITLANEAGGIGIWEWDVKPNVISWDKRMFELYEVPPH---VKPTWQLWHesmlPEDRAMAEQVVRDSLAARVPF 501
Cdd:COG2202 7 EESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEellGKTLRDLLP----PEDDDEFLELLRAALAGGGVW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 502 KLEFRIRVKDG-VRHIRALANRVLNKQGEVERLLGINMDMTEVKELNEALFQEKERLHITLDSIGEAVLCTDVNMNVTFM 580
Cdd:COG2202 83 RGELRNRRKDGsLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 581 NPVAEKMSGWLQEEALSQPILSVLHITFGDNG-PLMENIHSGDMSRSDIEqdVVLHNRNGGSYDIHYSITPLSTlDGQNI 659
Cdd:COG2202 163 NPAAEELLGYSPEELLGKSLLDLLHPEDRERLlELLRRLLEGGRESYELE--LRLKDGDGRWVWVEASAVPLRD-GGEVI 239
|
250
....*....|....*....
gi 1782164966 660 GSVLVIQDVTESRKMLREL 678
Cdd:COG2202 240 GVLGIVRDITERKRAEEAL 258
|
|
| PRK09894 |
PRK09894 |
diguanylate cyclase; Provisional |
682-847 |
3.92e-28 |
|
diguanylate cyclase; Provisional
Pssm-ID: 182133 [Multi-domain] Cd Length: 296 Bit Score: 115.55 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 682 ASHDALTHLANRVSFEASLKRMLhtVQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLG 761
Cdd:PRK09894 129 SNMDVLTGLPGRRVLDESFDHQL--RNREPQNLYLALLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYG 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 762 GDEFGLLLPDCNTESARYIAGRIIDAINGYHFMW-EGRLHrIGASAGITQIDeRNNQASEVMSQADIACYSSKNSGRGVV 840
Cdd:PRK09894 207 GEEFIICLKAATDEEACRAGERIRQLIANHAITHsDGRIN-ITATFGVSRAF-PEETLDVVIGRADRAMYEGKQTGRNRV 284
|
....*..
gi 1782164966 841 TVYEPQQ 847
Cdd:PRK09894 285 MFIDEQN 291
|
|
| EAL |
cd01948 |
EAL domain. This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
894-1098 |
5.44e-26 |
|
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: 107.63 E-value: 5.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 894 LRLWTNDGEMLEEQAFrAGLAE-PELIHALDRRILQEFFRNFAT-PLTNKGTGVALPLSMAGLASATLVDELLEMLHACP 971
Cdd:cd01948 34 LRWRHPEGGLISPAEF-IPLAEeTGLIVELGRWVLEEACRQLARwQAGGPDLRLSVNLSARQLRDPDFLDRLLELLAETG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 972 LQTRLLHLIVNVSVLTQEDDNTHHNLQKLREAGCRIILSHVGRDMEVFNHLSAQMADYLLLDPELVANVHGNLMDEMLVT 1051
Cdd:cd01948 113 LPPRRLVLEITESALIDDLEEALATLRRLRALGVRIALDDFGTGYSSLSYLKRLPVDYLKIDRSFVRDIETDPEDRAIVR 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1782164966 1052 IIQGHAQRLGIKTIAGPSNQPIMMDTLSGIGIDYIYGNTIGEPQPLE 1098
Cdd:cd01948 193 AIIALAHSLGLKVVAEGVETEEQLELLRELGCDYVQGYLFSRPLPAE 239
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
287-566 |
3.25e-22 |
|
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: 101.59 E-value: 3.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 287 MYAFRAErKHITESEERFRNAMEYSVIGMALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDlESDLEQLDQL 366
Cdd:COG5809 1 MKSSKME-LQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDD-EKELREILKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 367 LQGKINSYSLEKRYYTRSGEVVWALLAVSLVRHADGTPLYFIAQVEDINDLKHTEWVNKRLMERITLANEAGGIGIWEWD 446
Cdd:COG5809 79 LKEGESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 447 VKPNVI---SWDKRMFELYEVPPHVKPTWQLWHesmlPEDRAMAEQVVRDSLAARVPFKLEFRIRVKDGVRHIRALANRV 523
Cdd:COG5809 159 LDGRIIyanPAACKLLGISIEELIGKSILELIH----SDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAP 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1782164966 524 LNKQGEVERLLGINMDMTEVKELNEALfQEKERLHItldsIGE 566
Cdd:COG5809 235 IKKNGEVDGIVIIFRDITERKKLEELL-RKSEKLSV----VGE 272
|
|
| EAL |
pfam00563 |
EAL domain; This domain is found in diverse bacterial signaling proteins. It is called EAL ... |
894-1094 |
6.33e-21 |
|
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: 93.15 E-value: 6.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 894 LRLWTNDGEMLEEQAFRAGLAEPELIHALDRRILQEFFRNFATPLTNKGTGVALPLSMAGLASATLVDELLEMLHACPLQ 973
Cdd:pfam00563 35 LRWQHPDGGLISPARFLPLAEELGLIAELDRWVLEQALADLAQLQLGPDIKLSINLSPASLADPGFLELLRALLKQAGPP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 974 TRLLHLIVNVSVLTQEDDNTHHNLQKLREAGCRIILSHVGRDMEVFNHLSAQMADYLLLDPELVANVHGNLMDEMLVTII 1053
Cdd:pfam00563 115 PSRLVLEITESDLLARLEALREVLKRLRALGIRIALDDFGTGYSSLSYLLRLPPDFVKIDRSLIADIDKDGEARAIVRAL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1782164966 1054 QGHAQRLGIKTIAGPSNQPIMMDTLSGIGIDYIYGNTIGEP 1094
Cdd:pfam00563 195 IALAHSLGIKVVAEGVETEEQLEALRELGCDLVQGYYFSKP 235
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
291-421 |
5.31e-20 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 90.85 E-value: 5.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 291 RAERKhITESEERFRNAMEYSVIGMALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDLESDLEQLDQLLQGK 370
Cdd:COG2202 127 RAEEA-LRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGG 205
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1782164966 371 INSYSLEKRYYTRSGEVVWaLLAVSLVRHADGTPLYFIAQVEDINDLKHTE 421
Cdd:COG2202 206 RESYELELRLKDGDGRWVW-VEASAVPLRDGGEVIGVLGIVRDITERKRAE 255
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
552-691 |
7.37e-19 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 89.52 E-value: 7.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 552 QEKERLHITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHITFGDNGPLMENIHSGdmsRSDIEQD 631
Cdd:COG3852 4 ESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLERALAEG---QPVTERE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 632 VVLHNRNGGSYDIHYSITPLSTLDGQnIGSVLVIQDVTESRKMLRELSYNASHDALTHLA 691
Cdd:COG3852 81 VTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKLAAVGELA 139
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
314-414 |
1.29e-15 |
|
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: 73.44 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 314 GMALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDLESDLEQLDQLLQGkINSYSLEKRYYTRSGEVVWALLA 393
Cdd:cd00130 4 GVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSG-GEPVTLEVRLRRKDGSVIWVLVS 82
|
90 100
....*....|....*....|.
gi 1782164966 394 VSLVRHADGTPLYFIAQVEDI 414
Cdd:cd00130 83 LTPIRDEGGEVIGLLGVVRDI 103
|
|
| PRK09966 |
PRK09966 |
diguanylate cyclase DgcN; |
677-776 |
1.57e-15 |
|
diguanylate cyclase DgcN;
Pssm-ID: 182171 [Multi-domain] Cd Length: 407 Bit Score: 80.05 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 677 ELSYNASHDALTHLANRVSFEASLKRMLHTvQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDM 756
Cdd:PRK09966 243 QLLRTALHDPLTGLANRAAFRSGINTLMNN-SDARKTSALLFLDGDNFKYINDTWGHATGDRVLIEIAKRLAEFGGLRHK 321
|
90 100
....*....|....*....|
gi 1782164966 757 LARLGGDEFGLLLPDCNTES 776
Cdd:PRK09966 322 AYRLGGDEFAMVLYDVQSES 341
|
|
| adrA |
PRK10245 |
diguanylate cyclase AdrA; Provisional |
676-842 |
2.84e-14 |
|
diguanylate cyclase AdrA; Provisional
Pssm-ID: 182329 [Multi-domain] Cd Length: 366 Bit Score: 75.64 E-value: 2.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 676 RELSYNASHDALTHLANRVSFEASLKRMLHTVQETRQRHALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTD 755
Cdd:PRK10245 199 RRLQVMSTRDGMTGVYNRRHWETLLRNEFDNCRRHHRDATLLIIDIDHFKSINDTWGHDVGDEAIVALTRQLQITLRGSD 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 756 MLARLGGDEFGLLLPDCNTESARYIAGRIIDAINGYHFMWEGRLhRIGASAGITQIDERNNQASEVMSQADIACYSSKNS 835
Cdd:PRK10245 279 VIGRFGGDEFAVIMSGTPAESAITAMSRVHEGLNTLRLPNAPQV-TLRISVGVAPLNPQMSHYREWLKSADLALYKAKNA 357
|
....*..
gi 1782164966 836 GRGVVTV 842
Cdd:PRK10245 358 GRNRTEV 364
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
293-441 |
3.58e-14 |
|
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: 76.55 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 293 ERKHIT----ESEERFRNAMEYSVIGMALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDLESDLEQLDQLLQ 368
Cdd:COG5809 128 ERKRMEealrESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLK 207
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1782164966 369 GKINSYsLEKRYYTRSGEVVWaLLAVSLVRHADGTPLYFIAQVEDINDLKHTEwVNKRLMERITLANE-AGGIG 441
Cdd:COG5809 208 DGGIAQ-GEVRFWTKDGRWRL-LEASGAPIKKNGEVDGIVIIFRDITERKKLE-ELLRKSEKLSVVGElAAGIA 278
|
|
| RocR |
COG3829 |
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ... |
550-679 |
1.18e-13 |
|
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: 74.42 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 550 LFQEKERLHITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHitfgdNGPLMENIHSGDMSRSDIe 629
Cdd:COG3829 6 LKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIP-----NSPLLEVLKTGKPVTGVI- 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1782164966 630 qdvvlHNRNGGSYDIHYSITPLSTlDGQNIGSVLVIQDVTESRKMLRELS 679
Cdd:COG3829 80 -----QKTGGKGKTVIVTAIPIFE-DGEVIGAVETFRDITELKRLERKLR 123
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
548-786 |
9.99e-13 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 69.67 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 548 EALFQEKERLHITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHItfGDNGPLMENIHSGDMSRSD 627
Cdd:COG2202 4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPP--EDDDEFLELLRAALAGGGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 628 IEQDVVLHNRNGGSYDIHYSITPLSTLDGQNIGSVLVIQDVTESRKMLRELsyNASHDALTHLANRVSFEASLKRMLHTV 707
Cdd:COG2202 82 WRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEAL--RESEERLRLLVENAPDGIFVLDLDGRI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 708 QETRQRHALVF---IDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLGGDEFGL------LLPDCNTESAR 778
Cdd:COG2202 160 LYVNPAAEELLgysPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWvwveasAVPLRDGGEVI 239
|
....*...
gi 1782164966 779 YIAGRIID 786
Cdd:COG2202 240 GVLGIVRD 247
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
451-537 |
1.11e-12 |
|
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: 64.67 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 451 VISWDKRMFELYEVPPH-VKPTWQLWHESMLPEDRAMAEQVVRDSLAARVPFKLEFRIRVKDG-VRHIRALANRVLNKQG 528
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEeLLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGeYRWVEARARPIRDENG 80
|
....*....
gi 1782164966 529 EVERLLGIN 537
Cdd:pfam08447 81 KPVRVIGVA 89
|
|
| PRK11359 |
PRK11359 |
cyclic-di-GMP phosphodiesterase; Provisional |
670-850 |
1.31e-12 |
|
cyclic-di-GMP phosphodiesterase; Provisional
Pssm-ID: 183097 [Multi-domain] Cd Length: 799 Bit Score: 72.11 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 670 ESRKMLRELsynASHDALTHLANRVSFEASLKRMLHTVQETrqrhALVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLS 749
Cdd:PRK11359 367 KSRQHIEQL---IQFDPLTGLPNRNNLHNYLDDLVDKAVSP----VVYLIGVDHFQDVIDSLGYAWADQALLEVVNRFRE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 750 MLRSTDMLARLGGDEFGLLLPDCNTESARYIAGRIIdAINGYHFMWEGRLHRIGASAGITQIDERNNQasEVMSQADIAC 829
Cdd:PRK11359 440 KLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELR-NVVSKPIMIDDKPFPLTLSIGISYDVGKNRD--YLLSTAHNAM 516
|
170 180
....*....|....*....|.
gi 1782164966 830 YSSKNSGRGVVTVYEPQQERM 850
Cdd:PRK11359 517 DYIRKNGGNGWQFFSPAMNEM 537
|
|
| diguan_DgcJ |
NF040885 |
diguanylate cyclase DgcJ; |
685-795 |
2.86e-12 |
|
diguanylate cyclase DgcJ;
Pssm-ID: 468821 [Multi-domain] Cd Length: 490 Bit Score: 70.37 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 685 DALTHLANR----VSFEASLKRMlhtvqeTRQRHALVFI--DLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLA 758
Cdd:NF040885 344 DSMTGLYNRkiltPTLEQRLQRL------TEKGIPVTFIalDCDKLKHINDTLGHHEGDRAITLLAQAISASIRKSDYGI 417
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1782164966 759 RLGGDEFGLLLPDCNTESARYIAGRI------IDAINGYHFMW 795
Cdd:NF040885 418 RLGGDEFCIILIDYEEAEAQNLIERIrqhlrtIDPDKRVSFSW 460
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
302-414 |
1.79e-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 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: 59.35 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 302 ERFRNAMEYSVIGMALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDLESDLEQLDQLLQGKINSYSLEKRYY 381
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|...
gi 1782164966 382 TRSGEVVWALLAVSLVRHADGTPLYFIAQVEDI 414
Cdd:pfam00989 81 VPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
302-368 |
4.03e-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.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 56.64 E-value: 4.03e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1782164966 302 ERFRNAMEYSVIGMALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDLESDLEQLDQLLQ 368
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
297-421 |
4.15e-10 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 62.94 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 297 ITESEERFRNAMEYSVIGMALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLtWPEDlESDLEQLDQLLQGKINSYSL 376
Cdd:COG3852 2 LRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAEL-FPED-SPLRELLERALAEGQPVTER 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1782164966 377 EKRYYTRSGEVVWALLAVSLVRHADGTPlYFIAQVEDINDLKHTE 421
Cdd:COG3852 80 EVTLRRKDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLE 123
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
321-416 |
1.26e-09 |
|
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: 56.32 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 321 DGQWLQANKALCQFLGYSQAELRSLSFQQLTWPEDLESDLEQLDQLLQGKINsysLEKRYYTRSGEVVWALLAVSLVRHA 400
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVRE---FEVVLYRKDGEPFPVLVSLAPIRDD 77
|
90
....*....|....*.
gi 1782164966 401 DGTPLYFIAQVEDIND 416
Cdd:pfam13426 78 GGELVGIIAILRDITE 93
|
|
| PRK11829 |
PRK11829 |
biofilm formation regulator HmsP; Provisional |
637-1096 |
2.68e-09 |
|
biofilm formation regulator HmsP; Provisional
Pssm-ID: 183329 [Multi-domain] Cd Length: 660 Bit Score: 61.11 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 637 RNGGSYDIHYSITPLSTLDGQNIGSVLV------IQDVTESRKMLRELSYNASHdalTHLANRVSFEASLKRMLHTVQET 710
Cdd:PRK11829 184 EDIGDHGVLHHQLTLPAHHQDDELGVLVrnynrnQQLLADAYADMGRISHRFPV---TELPNRSLFISLLEKEIASSTRT 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 711 RQRHALVfIDLDRFKAVNDTAGHAAGDALLRELSSLMLSMLRSTDMLARLGGDEFGLLLPDCNTES-ARYIAGRIIDAIN 789
Cdd:PRK11829 261 DHFHLLV-IGIETLQEVSGAMSEAQHQQLLLTIVQRIEQCIDDSDLLAQLSKTEFAVLARGTRRSFpAMQLARRIMSQVT 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 790 GYHFMWEGRLhRIGASAGITQIDERNNQASEVMSQADIACYSSKNSGRGVVTVYEP-----------QQERMLNA----P 854
Cdd:PRK11829 340 QPLFFDEITL-RPSASIGITRYQAQQDTAESMMRNASTAMMAAHHEGRNQIMVFEPhliekthkrltQENDLLQAienhD 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 855 GAISLDEQWHMIKDNhlLMIARSVasprtpesstfwmlaLRLWTNDGEMLEEQAFRAGLAEPELIHALDRRILQEFFRNF 934
Cdd:PRK11829 419 FTLFLQPQWDMKRQQ--VIGAEAL---------------LRWCQPDGSYVLPSGFVHFAEEEGMMVPLGNWVLEEACRIL 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 935 ATPltnKGTGVALPLSM----AGLASATLVDELLEMLHACPLQTRLLHLIVNVSVLTQEDDNTHHNLQKLREAGCRIILS 1010
Cdd:PRK11829 482 ADW---KARGVSLPLSVnisgLQVQNKQFLPHLKTLISHYHIDPQQLLLEITETAQIQDLDEALRLLRELQGLGLLIALD 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 1011 HVG---RDMEVFNHLSAQMADYLLLDPELVANVHgnlMDEMLVTIIQGHAQRLGIKTIAGPSNQPIMMDTLSGIGIDYIY 1087
Cdd:PRK11829 559 DFGigySSLRYLNHLKSLPIHMIKLDKSFVKNLP---EDDAIARIISCVSDVLKVRVMAEGVETEEQRQWLLEHGIQCGQ 635
|
....*....
gi 1782164966 1088 GNTIGEPQP 1096
Cdd:PRK11829 636 GFLFSPPLP 644
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
564-668 |
3.48e-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. 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: 55.33 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 564 IGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHItfGDNGPLMENIHSGDMSRSDIEQDVVLHNRNGGSYD 643
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHP--EDREELRERLENLLSGGEPVTLEVRLRRKDGSVIW 78
|
90 100
....*....|....*....|....*
gi 1782164966 644 IHYSITPLSTLDGQNIGSVLVIQDV 668
Cdd:cd00130 79 VLVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| Nucleotidyl_cyc_III |
cd07556 |
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
716-808 |
5.37e-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: 55.44 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 716 LVFIDLDRFKAVNDTAGHAAGDALLRELSSLMLSML-RSTDMLARLGGDEFGLLLPDCNTESARYIAGRIIDAINGYHFM 794
Cdd:cd07556 4 ILFADIVGFTSLADALGPDEGDELLNELAGRFDSLIrRSGDLKIKTIGDEFMVVSGLDHPAAAVAFAEDMREAVSALNQS 83
|
90
....*....|....*
gi 1782164966 795 -WEGRLHRIGASAGI 808
Cdd:cd07556 84 eGNPVRVRIGIHTGP 98
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
548-688 |
1.00e-08 |
|
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: 59.22 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 548 EALFQEKERLHITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHITF-GDNGPLMENIHSGDmSRS 626
Cdd:COG5809 8 LQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDeKELREILKLLKEGE-SRD 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1782164966 627 DIEQDvvLHNRNGGSYDIHYSITPLSTLDGQNIGSVLVIQDVTESRKMLRELS---------YNASHDALT 688
Cdd:COG5809 87 ELEFE--LRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALReseekfrliFNHSPDGII 155
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
555-677 |
6.33e-08 |
|
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: 52.29 E-value: 6.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 555 ERLHITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHitfgdngPLMENIHSGDMSR------SDI 628
Cdd:TIGR00229 3 ERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIP-------EEDREEVRERIERrlegepEPV 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1782164966 629 EQDVVLHNRNGGSYDIHYSITPLSTlDGQNIGSVLVIQDVTEsRKMLRE 677
Cdd:TIGR00229 76 SEERRVRRKDGSEIWVEVSVSPIRT-NGGELGVVGIVRDITE-RKEAEE 122
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
555-668 |
9.79e-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: 51.26 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 555 ERLHITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLHIT--FGDNGPLMENIHSGDMSRSdieQDV 632
Cdd:pfam00989 1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEddAEVAELLRQALLQGEESRG---FEV 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 1782164966 633 VLHNRNGGSYDIHYSITPLSTLDGQNIGSVLVIQDV 668
Cdd:pfam00989 78 SFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
441-540 |
2.04e-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. 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: 50.32 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 441 GIWEWDVKPNVISWDKRMFELYEVPPHV---KPTWQLWHesmlPEDRAMAEQVVRDSLAARVPFKLEFRIRVKDG-VRHI 516
Cdd:cd00130 4 GVIVLDLDGRILYANPAAEQLLGYSPEEligKSLLDLIH----PEDREELRERLENLLSGGEPVTLEVRLRRKDGsVIWV 79
|
90 100
....*....|....*....|....
gi 1782164966 517 RALANRVLNKQGEVERLLGINMDM 540
Cdd:cd00130 80 LVSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
561-672 |
2.84e-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: 50.11 E-value: 2.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 561 LDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLhitfgdNGPLMENIHSGD---MS--RSDIEQDVVLH 635
Cdd:pfam08448 1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELL------PPEDAARLERALrraLEgeEPIDFLEELLL 74
|
90 100 110
....*....|....*....|....*....|....*..
gi 1782164966 636 NRNGGSYDIHYsiTPLSTLDGQNIGSVLVIQDVTESR 672
Cdd:pfam08448 75 NGEERHYELRL--TPLRDPDGEVIGVLVISRDITERR 109
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
755-833 |
4.38e-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: 51.06 E-value: 4.38e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1782164966 755 DMLARLGGDEFGLLLPDCNTESARYIAGRIIDAINGYHFmwegrlHRIGASAGITQIDernnqaseVMSQADiACYSSK 833
Cdd:COG3706 116 DLVARYGGEEFAILLPGTDLEGALAVAERIREAVAELPS------LRVTVSIGVAGDS--------LLKRAD-ALYQAR 179
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
508-670 |
1.42e-06 |
|
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: 51.89 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 508 RVKDGVRHIRA--LANRV-LNKQGEVERL-LGINmDMT-EVKELNEALFQEKERLHITLDSIGEAVLCTDVNMNVTFMNP 582
Cdd:COG5000 39 RLAEATRAVAAgdLSVRLpVTGDDEIGELaRAFN-RMTdQLKEQREELEERRRYLETILENLPAGVIVLDADGRITLANP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 583 VAEKMSGWLQEEALSQPILSVLHITFgdngpLMENIHsgDMSRSDIEQDVVLHnrNGGSYDIHYSITPLstldgQNIGSV 662
Cdd:COG5000 118 AAERLLGIPLEELIGKPLEELLPELD-----LAELLR--EALERGWQEEIELT--RDGRRTLLVRASPL-----RDDGYV 183
|
....*...
gi 1782164966 663 LVIQDVTE 670
Cdd:COG5000 184 IVFDDITE 191
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
375-417 |
1.82e-06 |
|
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: 45.64 E-value: 1.82e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1782164966 375 SLEKRYYTRSGEVVWALLAVSLVRHADGTPLYFIAQVEDINDL 417
Cdd:smart00086 1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
576-670 |
1.96e-06 |
|
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: 47.07 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 576 NVTFMNPVAEKMSGWLQEEALSQPIlSVLHITFGDNGPLMENIHSGdmsRSDIEQDVVLHNRNGGSYDIHYSITPLSTLD 655
Cdd:pfam13426 3 RIIYVNDAALRLLGYTREELLGKSI-TDLFAEPEDSERLREALREG---KAVREFEVVLYRKDGEPFPVLVSLAPIRDDG 78
|
90
....*....|....*
gi 1782164966 656 GQNIGSVLVIQDVTE 670
Cdd:pfam13426 79 GELVGIIAILRDITE 93
|
|
| PRK11059 |
PRK11059 |
regulatory protein CsrD; Provisional |
681-788 |
3.30e-06 |
|
regulatory protein CsrD; Provisional
Pssm-ID: 236833 [Multi-domain] Cd Length: 640 Bit Score: 51.40 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 681 NASHDALTHLANRVSFEASLKRMLHTvQETRQRHALVF-IDLDRFKAVNDTAGHAAGDALLRELSSlMLS--MLRSTD-M 756
Cdd:PRK11059 227 NAFQDAKTGLGNRLFFDNQLATLLED-QEMVGAHGVVMlIRLPDFDLLQEEWGESQVEELLFELIN-LLStfVMRYPGaL 304
|
90 100 110
....*....|....*....|....*....|..
gi 1782164966 757 LARLGGDEFGLLLPDCNTESARYIAGRIIDAI 788
Cdd:PRK11059 305 LARYSRSDFAVLLPHRSLKEADSLASQLLKAV 336
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
327-409 |
4.35e-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: 4.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 327 ANKALCQFLGYSQAELRSL--SFQQLTWPEDLESDLEQLDQLLQGKInSYSLEKRYYTRSGEVVWALLAVSLVRHADGTP 404
Cdd:pfam08447 4 WSPRFEEILGYTPEELLGKgeSWLDLVHPDDRERVREALWEALKGGE-PYSGEYRIRRKDGEYRWVEARARPIRDENGKP 82
|
....*
gi 1782164966 405 LYFIA 409
Cdd:pfam08447 83 VRVIG 87
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
316-414 |
6.74e-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 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: 46.25 E-value: 6.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 316 ALVSTDGQWLQANKALCQFLGYSQAELRSLSFQQLtWPEDLESDLE-QLDQLLQGKINSYSLEkrYYTRSGEVVWALLAV 394
Cdd:pfam08448 9 AVLDPDGRVRYANAAAAELFGLPPEELLGKTLAEL-LPPEDAARLErALRRALEGEEPIDFLE--ELLLNGEERHYELRL 85
|
90 100
....*....|....*....|
gi 1782164966 395 SLVRHADGTPLYFIAQVEDI 414
Cdd:pfam08448 86 TPLRDPDGEVIGVLVISRDI 105
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
555-605 |
7.88e-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.
Pssm-ID: 214512 Cd Length: 67 Bit Score: 44.70 E-value: 7.88e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1782164966 555 ERLHITLDSIGEAVLCTDVNMNVTFMNPVAEKMSGWLQEEALSQPILSVLH 605
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIH 51
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
502-542 |
8.57e-06 |
|
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: 43.71 E-value: 8.57e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1782164966 502 KLEFRIRVKDG-VRHIRALANRVLNKQGEVERLLGINMDMTE 542
Cdd:smart00086 1 TVEYRLRRKDGsYIWVLVSASPIRDEDGEVEGILGVVRDITE 42
|
|
| COG5373 |
COG5373 |
Uncharacterized membrane protein [Function unknown]; |
14-397 |
5.26e-05 |
|
Uncharacterized membrane protein [Function unknown];
Pssm-ID: 444140 [Multi-domain] Cd Length: 854 Bit Score: 47.30 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 14 HPLLRLVSLGLVTFIFTLFSLELTRFGTFLAPLWFPTSIMMVAFYRHAGKMW-PGIALACSVGNIFATWLIFSWDAINLW 92
Cdd:COG5373 431 RLLLRWWALLLQLAPLAALLAAYWPVANLAGSYLWALLALALAALFAALALRlARRRSAGLRLWGAAWWALAALAAIALA 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 93 YTGinVLEAIVGALLLRKLLPGYNPLQNLGDWIRLALGSALIPPLLGGVLVWQLVPSDEPLRSFMvWVLSESVGALALVP 172
Cdd:COG5373 511 LTL--LLEEAALTLALALLVLSLAWLARRLDWPLLRWLAALLLPLVLLRLLWDPGLVGGPLAGFN-WLLWGYGGPLLALA 587
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 173 LGLlfkphYLLRHRNPRLLFETLLTMVVTLLLSWIALHFLP--------------------WPFTAIIVLLMWSAVRLPR 232
Cdd:COG5373 588 AAA-----WLLRRRRLRRWLEAAALWLLVLLLALELRYLLWggdlfasewslaeagllallWLALALALLRRWLRRAGRV 662
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 233 LEAFLVFLVTVMMVSLMIAknpVPLTTQNFGAMTNAPWLPFLMMLLPANVMTMVMYAFRAERKHItesEERFRNAMEYSV 312
Cdd:COG5373 663 YRLAALALGPLAALSYLLL---LLLLLNPLWSGAPVGYLPLLNPLLLAYLLPALLLALWARLLLL---APRLRRAAAGLA 736
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 313 IGMALVSTDGQWlqankalcqflgysqaeLRSLSFQQLTWPeDLESDLEQLdqllqgkinSYSlekryytrsgeVVWALL 392
Cdd:COG5373 737 GLLGFLWLNLEI-----------------RRLWHGGDLALW-LGVSDLEQY---------SYS-----------IVWLLL 778
|
....*
gi 1782164966 393 AVSLV 397
Cdd:COG5373 779 ALALL 783
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
293-552 |
1.03e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 46.59 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 293 ERKhitESEERFRNAM---EYSVIGMAL----VSTDGQWLQANKALCQFLGYSQAELRSLSFQQLTwPEDLESDLEQLDQ 365
Cdd:PRK13560 191 ERK---RAEERIDEALhflQQLLDNIADpafwKDEDAKVFGCNDAACLACGFRREEIIGMSIHDFA-PAQPADDYQEADA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 366 LLQGKINSYSLEKRYYTRSGEVVWALLAVSLVRHADgtPLYFIAQ----VEDINDLKHTEWVNKRLMERITLANEAGGIG 441
Cdd:PRK13560 267 AKFDADGSQIIEAEFQNKDGRTRPVDVIFNHAEFDD--KENHCAGlvgaITDISGRRAAERELLEKEDMLRAIIEAAPIA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 442 IWEWDVKPNVISWDK----RMFELYEVPPHVKPTW--------QLWHESM---LPEDRAMAEQVVRDSLAARVPFKL--- 503
Cdd:PRK13560 345 AIGLDADGNICFVNNnaaeRMLGWSAAEVMGKPLPgmdpelneEFWCGDFqewYPDGRPMAFDACPMAKTIKGGKIFdgq 424
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1782164966 504 EFRI-RVKDGVRHIRALANRVLNKQGEVERLLGINMDMTEVKELNEALFQ 552
Cdd:PRK13560 425 EVLIeREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLL 474
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
530-690 |
1.63e-03 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 42.14 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 530 VERLLGINMDMTEVKELNEALFQEKErlhITLDSIGEAVLCTDVNMNVTFMNPVAEKMsgwLQEEALSQPILSVLhitfg 609
Cdd:COG3290 62 LLLLLLLAALLLKLLEEIARLVEERE---AVLESIREGVIAVDRDGRITLINDAARRL---LGLDAIGRPIDEVL----- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 610 dngplMENIHSGDMSRsdieqdvvLHNRNGGSYDIhySITPLsTLDGQNIGSVLVIQDVTESRKMLRELS-----YNA-- 682
Cdd:COG3290 131 -----AEVLETGERDE--------EILLNGRVLVV--NRVPI-RDDGRVVGAVATFRDRTELERLEEELEgvkelAEAlr 194
|
170
....*....|
gi 1782164966 683 --SHDALTHL 690
Cdd:COG3290 195 aqRHDFRNHL 204
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
441-540 |
3.46e-03 |
|
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: 38.55 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1782164966 441 GIWEWDVKPNVISWDKRMFELYEVPPHV---KPTWQLWHEsmlPEDRAMAEQVVRDSLAARVPFKLEFRIRVKDG-VRHI 516
Cdd:pfam00989 13 GIFVVDEDGRILYVNAAAEELLGLSREEvigKSLLDLIPE---EDDAEVAELLRQALLQGEESRGFEVSFRVPDGrPRHV 89
|
90 100
....*....|....*....|....
gi 1782164966 517 RALANRVLNKQGEVERLLGINMDM 540
Cdd:pfam00989 90 EVRASPVRDAGGEILGFLGVLRDI 113
|
|
| |
