NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1085344563|gb|OGV17264|]
View 

MAG: hypothetical protein A2237_07720 [Stygiobacter sp. RIFOXYA2_FULL_38_8]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
2301-2537 2.80e-78

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


:

Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 259.45  E-value: 2.80e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2301 LQHSLEKEKELSELKSRFISTTSHEFRTPLTTVRVSAEMIQRyRKRWTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSE 2380
Cdd:COG2205      2 LEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLD-EEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2381 SGKIVLNREEIDLHEFCLDVIEEAKISATEA-HKLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQ 2459
Cdd:COG2205     81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKgIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARR 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 2460 LRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:COG2205    161 EGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
1638-1896 2.38e-41

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 154.03  E-value: 2.38e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1638 AEEALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDPAWHFYREdgtvlplEEYPVNYV 1717
Cdd:COG2202      2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-------EFLELLRA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1718 LATRKELRNYVVGVHRTNyKNDVWVLVNADPVWSNENELTQVIVTFSDITMRKNAEVALKLSEERYRTLVEQAMDGIFIA 1797
Cdd:COG2202     75 ALAGGGVWRGELRNRRKD-GSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1798 DSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTALAERNLIRNDGSLLPVEISGIMLPD- 1876
Cdd:COG2202    154 DLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLr 233
                          250       260
                   ....*....|....*....|....*
gi 1085344563 1877 -----KRFLGIVRDITERKKNEAAL 1896
Cdd:COG2202    234 dggevIGVLGIVRDITERKRAEEAL 258
PAS COG2202
PAS domain [Signal transduction mechanisms];
415-675 2.15e-40

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 151.33  E-value: 2.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  415 AENALYLSEERFRRLAENAPDVIYRMSLaDGKYEYISPAALTIFGYSPDDYYDNPLLFKqsIHSDWIKYFEEHWANLQKG 494
Cdd:COG2202      2 AEEALEESERRLRALVESSPDAIIITDL-DGRILYVNPAFERLTGYSAEELLGKTLRDL--LPPEDDDEFLELLRAALAG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  495 ILPQTYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQALQKAAEEIRDLYNNAPCGYHSLDKEGT 574
Cdd:COG2202     79 GGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  575 FVRINNTELKWLGYTLEEVIGKmKFTDIITPKSLKTFNENFPGFKEKGwIKNLEFELIRKDGSILPILASATAIKDSDGN 654
Cdd:COG2202    159 ILYVNPAAEELLGYSPEELLGK-SLLDLLHPEDRERLLELLRRLLEGG-RESYELELRLKDGDGRWVWVEASAVPLRDGG 236
                          250       260
                   ....*....|....*....|..
gi 1085344563  655 -YLMSRSTVNDIAELKLAELQL 675
Cdd:COG2202    237 eVIGVLGIVRDITERKRAEEAL 258
PAS COG2202
PAS domain [Signal transduction mechanisms];
1383-1642 6.99e-37

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 141.32  E-value: 6.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1383 RSDRILRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGE 1462
Cdd:COG2202      1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1463 NSELEILVPNPNNEQIVHQIRIIAERDEQNKVTSVLAIGRDITERKRAEETIKKSEAQLNEAQRIAQIGSWELDIANNIL 1542
Cdd:COG2202     81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRIL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1543 RWSDEIFRIFEIDPKEFGSSYeaFLNAIHPDDREVVNTAYSNSLVN-RTPYAIDHRLRFDDGRIKFVHEQCETIYNeENK 1621
Cdd:COG2202    161 YVNPAAEELLGYSPEELLGKS--LLDLLHPEDRERLLELLRRLLEGgRESYELELRLKDGDGRWVWVEASAVPLRD-GGE 237
                          250       260
                   ....*....|....*....|.
gi 1085344563 1622 PLRSIGTVQDITDRKLAEEAL 1642
Cdd:COG2202    238 VIGVLGIVRDITERKRAEEAL 258
PAS COG2202
PAS domain [Signal transduction mechanisms];
974-1233 3.24e-34

PAS domain [Signal transduction mechanisms];


:

Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 133.61  E-value: 3.24e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  974 RNLSESERRLTEAQRIANVGYWERDFVNNKIILSDESCRIFGLQQEnyhkelDEWHKQWLQLILPEDKERAEKTAIDAVQ 1053
Cdd:COG2202      4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAE------ELLGKTLRDLLPPEDDDEFLELLRAALA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1054 KDIPYNLDYRIIRHNGELRYIHSEANVRRDSSGKPIFMLGMMQDITVRKRAEESLLESETKLRIMFENSRDALGV-SKKG 1132
Cdd:COG2202     78 GGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVlDLDG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1133 VHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIPSFYETRGRKRDGSEFDFEINISTYELNG 1212
Cdd:COG2202    158 RILYVNPAAEELLGYSP-EELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGG 236
                          250       260
                   ....*....|....*....|..
gi 1085344563 1213 EI-YTLANIRDITSRKLLEKSL 1233
Cdd:COG2202    237 EViGVLGIVRDITERKRAEEAL 258
GAF COG2203
GAF domain [Signal transduction mechanisms];
180-558 1.88e-20

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 99.11  E-value: 1.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  180 RAYNQLEEENNLRKEAEKELRTINDELEDRVEERTIELHHANVQLEDELAVRQRAESQIRKLNRIYAVLSNINQAIVRIR 259
Cdd:COG2203    127 ARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSAL 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  260 NTKEVFDEACRIATEYGKFTMVWIGIINAKNNKVDVAASSGVESSYLDNLvidlndvQRSSGPTGIAIRTGKHKISNNII 339
Cdd:COG2203    207 DLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRL-------PLGEGLAGRALRTGEPVVVNDAS 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  340 DDDSML-LWKNEAIQYGYKSTASFPLIVFGKVVGAFCIYSDELNFFEDDDVVLLDEMVKDISFAMEFIESEAERRDAENA 418
Cdd:COG2203    280 TDPRFApSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  419 LylsEERFRRLAENAPDVIYRMSLADGKYEYISPAALTIFGYSPDDYYDNPLLFKQSIHSDWIKYFEEHWANLQKGILPQ 498
Cdd:COG2203    360 L---LQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRI 436
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  499 TYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQALQKAAEEIRDL 558
Cdd:COG2203    437 LLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLA 496
GAF COG2203
GAF domain [Signal transduction mechanisms];
1895-2280 3.84e-20

GAF domain [Signal transduction mechanisms];


:

Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 97.96  E-value: 3.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1895 ALNERIKHSQSLLRLSKNLEFAQTYSQALTAALNEIKNILGYKTVWVYLLSEDKKYFNALVARGDFEDIVMSPEGTLILP 1974
Cdd:COG2203      1 LLSVLALALAREVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1975 IEGDRMLEEIAEAKEIVIVEDARADERTNKKIVETLGNRTIINVPIYLLDKHLGTVGTGTFSDEGVRIPTRSEKEFLLAM 2054
Cdd:COG2203     81 IDALVLLSLVATAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2055 ASHLAVTLDRLHLLVERQEAEKALLRLN-RELKAISNCNQSLLRAEDEQSLLNEICRIICEEAGYDFAWVGYTEHsDANT 2133
Cdd:COG2203    161 TDLVGQLAALAGLILDIARLLTQRARLElERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDE-DGGE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2134 IHPVAWAGIDIDLKAKEKFDWSeeiecglrPAQKVIQTGDIIYVQDFSSDASLESWCQKAL-QRGYRSGMALPLKNENsQ 2212
Cdd:COG2203    240 LELVAAPGLPEEELGRLPLGEG--------LAGRALRTGEPVVVNDASTDPRFAPSLRELLlALGIRSLLCVPLLVDG-R 310
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 2213 VFGVILIYSTNRNVITQDEIRLIEELANDLAFGIITLQTRAERKRVEKELELHRDHLQELVNVRTEEL 2280
Cdd:COG2203    311 LIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLL 378
KinA super family cl47424
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
553-801 1.71e-19

Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG5805:

Pssm-ID: 444507 [Multi-domain]  Cd Length: 496  Bit Score: 94.80  E-value: 1.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  553 EEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKMkFTDIITPKSLKTFNENFPGFKEKGWIKNLEFELi 632
Cdd:COG5805     34 EELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKT-IFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIY- 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  633 RKDGSILPILASATAIkdSDGNYLMSRSTVNDIAELKLAELQLRNSEREFRTLAENLPDHIIRYDIDCRVIYLNHVVAA- 711
Cdd:COG5805    112 CKDGELIYVEVKLFPI--YNQNGQAAILALRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERl 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  712 TNYTNSSLVGKLSAEiqFNEAKGLEEYNEKLRRVIKTGTEDEMEIMLRDIEGNLHIHEVHFLAERDIEGKIVGALAIGHD 791
Cdd:COG5805    190 FGAPREELIGKNLLE--LLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRD 267
                          250
                   ....*....|
gi 1085344563  792 ISERKQAEEE 801
Cdd:COG5805    268 ITEKKEAEEL 277
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
1246-1379 9.21e-06

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


:

Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 47.47  E-value: 9.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1246 ENFFDSLAQFLGENLDMDYVVVDKLDDNPEIAETIALYAKGSIVPNIRYalkGTPCENVM-GRQLCFYPKEVQKLFPDDK 1324
Cdd:pfam01590    3 EEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIPP---GTGVTVLRtGRPLVVPDAAGDPRFLDPL 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 1325 LLLE-MGVDSYMGIPLWDSfGKPIGLIALmSSKSHPEDSIAIQVLQLVATRAAAEL 1379
Cdd:pfam01590   80 LLLRnFGIRSLLAVPIIDD-GELLGVLVL-HHPRPPFTEEELELLEVLADQVAIAL 133
 
Name Accession Description Interval E-value
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
2301-2537 2.80e-78

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 259.45  E-value: 2.80e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2301 LQHSLEKEKELSELKSRFISTTSHEFRTPLTTVRVSAEMIQRyRKRWTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSE 2380
Cdd:COG2205      2 LEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLD-EEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2381 SGKIVLNREEIDLHEFCLDVIEEAKISATEA-HKLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQ 2459
Cdd:COG2205     81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKgIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARR 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 2460 LRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:COG2205    161 EGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238
PAS COG2202
PAS domain [Signal transduction mechanisms];
1638-1896 2.38e-41

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 154.03  E-value: 2.38e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1638 AEEALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDPAWHFYREdgtvlplEEYPVNYV 1717
Cdd:COG2202      2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-------EFLELLRA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1718 LATRKELRNYVVGVHRTNyKNDVWVLVNADPVWSNENELTQVIVTFSDITMRKNAEVALKLSEERYRTLVEQAMDGIFIA 1797
Cdd:COG2202     75 ALAGGGVWRGELRNRRKD-GSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1798 DSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTALAERNLIRNDGSLLPVEISGIMLPD- 1876
Cdd:COG2202    154 DLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLr 233
                          250       260
                   ....*....|....*....|....*
gi 1085344563 1877 -----KRFLGIVRDITERKKNEAAL 1896
Cdd:COG2202    234 dggevIGVLGIVRDITERKRAEEAL 258
PAS COG2202
PAS domain [Signal transduction mechanisms];
415-675 2.15e-40

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 151.33  E-value: 2.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  415 AENALYLSEERFRRLAENAPDVIYRMSLaDGKYEYISPAALTIFGYSPDDYYDNPLLFKqsIHSDWIKYFEEHWANLQKG 494
Cdd:COG2202      2 AEEALEESERRLRALVESSPDAIIITDL-DGRILYVNPAFERLTGYSAEELLGKTLRDL--LPPEDDDEFLELLRAALAG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  495 ILPQTYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQALQKAAEEIRDLYNNAPCGYHSLDKEGT 574
Cdd:COG2202     79 GGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  575 FVRINNTELKWLGYTLEEVIGKmKFTDIITPKSLKTFNENFPGFKEKGwIKNLEFELIRKDGSILPILASATAIKDSDGN 654
Cdd:COG2202    159 ILYVNPAAEELLGYSPEELLGK-SLLDLLHPEDRERLLELLRRLLEGG-RESYELELRLKDGDGRWVWVEASAVPLRDGG 236
                          250       260
                   ....*....|....*....|..
gi 1085344563  655 -YLMSRSTVNDIAELKLAELQL 675
Cdd:COG2202    237 eVIGVLGIVRDITERKRAEEAL 258
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
2249-2537 1.47e-39

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 161.48  E-value: 1.47e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2249 LQTRAERKRVEKELELHRDHLQELVNVRTEELDKVNKKLIIEfekekeferMLQHSLEKE--KELSELKSRFISTTSHEF 2326
Cdd:TIGR02956  405 LKLQADERQVAQELQEHKESLEQLVAQRTQELAETNERLNAE---------VKNHAKARAeaEEANRAKSAFLATMSHEI 475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2327 RTPLTTVRVSAEMIQryRKRWTEDKLDvFLDKIKNSVDYLTKLLDDVLTISRSESGKIVLNREEIDLHEFCLDVIEEAKI 2406
Cdd:TIGR02956  476 RTPLNGILGTLELLG--DTGLTSQQQQ-YLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVS 552
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2407 SATEAH-KLIFNFTLKKIHYRL-DPKLMKFILLNLLSNAIKYSPKgGKIELTIK-QLRGKMVISVKDKGIGIPTDDLKHL 2483
Cdd:TIGR02956  553 RAQLKGiQLRLNIPEQLPNWWQgDGPRIRQVLINLVGNAIKFTDR-GSVVLRVSlNDDSSLLFEVEDTGCGIAEEEQATL 631
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1085344563 2484 FEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:TIGR02956  632 FDAFTQADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR 685
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
2428-2536 9.78e-39

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 140.86  E-value: 9.78e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTT-DISGTGLGLSIV 2506
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSrKIGGTGLGLSIV 81
                            90       100       110
                    ....*....|....*....|....*....|
gi 1085344563  2507 KRAVDLHNGIITVKSELNAGTTFTVKIPLE 2536
Cdd:smart00387   82 KKLVELHGGEISVESEPGGGTTFTITLPLE 111
PAS COG2202
PAS domain [Signal transduction mechanisms];
1383-1642 6.99e-37

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 141.32  E-value: 6.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1383 RSDRILRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGE 1462
Cdd:COG2202      1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1463 NSELEILVPNPNNEQIVHQIRIIAERDEQNKVTSVLAIGRDITERKRAEETIKKSEAQLNEAQRIAQIGSWELDIANNIL 1542
Cdd:COG2202     81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRIL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1543 RWSDEIFRIFEIDPKEFGSSYeaFLNAIHPDDREVVNTAYSNSLVN-RTPYAIDHRLRFDDGRIKFVHEQCETIYNeENK 1621
Cdd:COG2202    161 YVNPAAEELLGYSPEELLGKS--LLDLLHPEDRERLLELLRRLLEGgRESYELELRLKDGDGRWVWVEASAVPLRD-GGE 237
                          250       260
                   ....*....|....*....|.
gi 1085344563 1622 PLRSIGTVQDITDRKLAEEAL 1642
Cdd:COG2202    238 VIGVLGIVRDITERKRAEEAL 258
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
2435-2533 1.02e-36

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 134.65  E-value: 1.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHN 2514
Cdd:cd00075      4 VLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREGGGTGLGLAIVRRIVEAHG 83
                           90
                   ....*....|....*....
gi 1085344563 2515 GIITVKSELNAGTTFTVKI 2533
Cdd:cd00075     84 GRITVESEPGGGTTFTVTL 102
PAS COG2202
PAS domain [Signal transduction mechanisms];
974-1233 3.24e-34

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 133.61  E-value: 3.24e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  974 RNLSESERRLTEAQRIANVGYWERDFVNNKIILSDESCRIFGLQQEnyhkelDEWHKQWLQLILPEDKERAEKTAIDAVQ 1053
Cdd:COG2202      4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAE------ELLGKTLRDLLPPEDDDEFLELLRAALA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1054 KDIPYNLDYRIIRHNGELRYIHSEANVRRDSSGKPIFMLGMMQDITVRKRAEESLLESETKLRIMFENSRDALGV-SKKG 1132
Cdd:COG2202     78 GGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVlDLDG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1133 VHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIPSFYETRGRKRDGSEFDFEINISTYELNG 1212
Cdd:COG2202    158 RILYVNPAAEELLGYSP-EELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGG 236
                          250       260
                   ....*....|....*....|..
gi 1085344563 1213 EI-YTLANIRDITSRKLLEKSL 1233
Cdd:COG2202    237 EViGVLGIVRDITERKRAEEAL 258
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
2428-2537 3.61e-33

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 124.79  E-value: 3.61e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQlRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKnTTDISGTGLGLSIVK 2507
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEITVTLSE-GGELTLTVEDNGIGIPPEDLPRIFEPFSTAD-KRGGGGTGLGLSIVR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1085344563 2508 RAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:pfam02518   80 KLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
2301-2536 4.57e-32

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 133.61  E-value: 4.57e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2301 LQHSLEKEKELSELKSRFISTTSHEFRTPLTTVRVSAEMIQRYRkrwteDKLDVFLDK----IKNSVDYLTKLLDDVLTI 2376
Cdd:NF040691   257 LQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSR-----DDFDPATARsaelLHTELDRFESLLSDLLEI 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2377 SRSESGKIVLNREEIDLHEFCLDVIEEAKISATEAH-KLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSpKGGKIEL 2455
Cdd:NF040691   332 SRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGvELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHG-EGKPVVV 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2456 TIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRA----KNTTdiSGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTV 2531
Cdd:NF040691   411 TVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRAdparARTT--GGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRL 488

                   ....*
gi 1085344563 2532 KIPLE 2536
Cdd:NF040691   489 TLPRV 493
PRK09303 PRK09303
histidine kinase;
2305-2534 3.93e-31

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 127.76  E-value: 3.93e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2305 LEKEKE-LSE---LKSRFISTTSHEFRTPLTTVRVSAEMIQRYRKRWTEDK----LDVFLDKIKNSVDYLTKLLDDVLTI 2376
Cdd:PRK09303   137 LRQENEtLLEqlkFKDRVLAMLAHDLRTPLTAASLALETLELGQIDEDTELkpalIEQLQDQARRQLEEIERLITDLLEV 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2377 SRSESGKIVLNREEIDLHEFCLDVIEEakisateahkLIFNFTLKKIHYRLD-----------PKLMKFILLNLLSNAIK 2445
Cdd:PRK09303   217 GRTRWEALRFNPQKLDLGSLCQEVILE----------LEKRWLAKSLEIQTDipsdlpsvyadQERIRQVLLNLLDNAIK 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2446 YSPKGGKIELTI----KQlrgKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKS 2521
Cdd:PRK09303   287 YTPEGGTITLSMlhrtTQ---KVQVSICDTGPGIPEEEQERIFEDRVRLPRDEGTEGYGIGLSVCRRIVRVHYGQIWVDS 363
                          250
                   ....*....|...
gi 1085344563 2522 ELNAGTTFTVKIP 2534
Cdd:PRK09303   364 EPGQGSCFHFTLP 376
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
1779-1896 5.79e-24

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: 99.29  E-value: 5.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1779 SEERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTAL--AERN 1856
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPvsEERR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1085344563 1857 LIRNDGSLLPVEISGIMLPD----KRFLGIVRDITERKKNEAAL 1896
Cdd:TIGR00229   81 VRRKDGSEIWVEVSVSPIRTnggeLGVVGIVRDITERKEAEEAL 124
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
2234-2534 2.01e-23

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 106.45  E-value: 2.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2234 LIEELANDLAFGIITLQTRAERKRVEKELE-LHR----DHLQELVNVRTEELDKVNKKLIIefekekefermLQHSLEKE 2308
Cdd:NF012163   168 LIVALALLLAALAAFLLARGLLAPVKRLVEaTHRlaagDYTTRVTPTSNDELGKLAQDFNQ-----------LASTLEKN 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2309 KELselKSRFISTTSHEFRTPLTTVRVSAEMIQRYRKRWTEDKldvfLDKIKNSVDYLTKLLDDVLTISRSESGKIVLNR 2388
Cdd:NF012163   237 EQM---RRDFMADISHELRTPLAVLRAELEAIQDGIRKFTPES----LDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQK 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2389 EEIDLHEfcldVIEeakiSATEAHKLIFNFTLKKIHYRL--------DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQL 2460
Cdd:NF012163   310 ASVDLVP----LLE----VEGGAFRERFASAGLELEVSLpdsslvfgDRDRLMQLFNNLLENSLRYTDSGGSLHISASQR 381
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 2461 RGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDIS--GTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:NF012163   382 PKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRAsgGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
PRK13560 PRK13560
hypothetical protein; Provisional
388-806 3.11e-23

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 108.22  E-value: 3.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  388 DVVLLDEMVKDISFAMEFIeSEAERRDAEnalylsEERFRRLAENAPDVIYRMSLaDGKYEYISPAAL----TIFGYSPD 463
Cdd:PRK13560    39 DVEELQELLRGHAYDARAI-AEAEAQDCR------EQCERNLKANIPGGMFLFAL-DGDGTFSFPSLLdangELAAIAKH 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  464 DYYDNPLLFKQSIHSDWIKYF-------EEHWANLQKGILPQTYEYQIIHksGEARWLNqrNILVLDEGGNS-VAIEGVV 535
Cdd:PRK13560   111 DLMADKGLLAMLIGGDDGDFFfanpfrsAETIAMALQSDDWQEEEGHFRC--GDGRFID--CCLRFERHAHAdDQVDGFA 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  536 TDITERKQAEQALQKAAEEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGkMKFTDIITPKSLKTFNE-N 614
Cdd:PRK13560   187 EDITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIG-MSIHDFAPAQPADDYQEaD 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  615 FPGFKEKGwIKNLEFELIRKDGSILP--ILASATAIKDSDGNYLMSRSTVNDIAELKLAELQLRNSEREFRTLAENLPDH 692
Cdd:PRK13560   266 AAKFDADG-SQIIEAEFQNKDGRTRPvdVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPIA 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  693 IIRYDIDCRVIYLNHVVAatnytnSSLVGKLSAEIQFNEAKGLE-EYNEKL-----RRVIKTGTEDEMEI--MLRDIEGN 764
Cdd:PRK13560   345 AIGLDADGNICFVNNNAA------ERMLGWSAAEVMGKPLPGMDpELNEEFwcgdfQEWYPDGRPMAFDAcpMAKTIKGG 418
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563  765 LHIHEVHFLAER----------------DIEGKIVGALAIGHDISERKQAEEE-RQANL 806
Cdd:PRK13560   419 KIFDGQEVLIEReddgpadcsayaeplhDADGNIIGAIALLVDITERKQVEEQlLLANL 477
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
974-1231 5.88e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 104.37  E-value: 5.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  974 RNLSESER-RLTEAQRIAN----VGYWERDFVNNkIILSDEscRIFGLQQENYHKELDEwhKQWLQLILPEDKERAEKTA 1048
Cdd:PRK09776   398 LKRTEQVNeRLMERITLANeaggIGIWEWDLKPN-IISWDK--RMFELYEIPPHIKPTW--QVWYACLHPEDRQRVEKEI 472
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1049 IDAVQKDIPYNLDYRIIRHNGeLRYIHSEANVRRDSSGKPIFMLGMMQDITVRKRAEESLLESETKLRIMFENSRDALGV 1128
Cdd:PRK09776   473 RDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVRQLNEALFQEKERLHITLDSIGEAVVC 551
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1129 SKKGVHV-FANPAYLKLFGYeKLEEIVGTSILECIapshhqqiieNVKRRDSGEEIPSFY---ETRG----------RKR 1194
Cdd:PRK09776   552 TDMAMKVtFMNPVAEKMTGW-TQEEALGVPLLTVL----------HITFGDNGPLMENIYsclTSRSaayleqdvvlHCR 620
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1085344563 1195 DGSEFDFEINI---STyeLNGE-IYTLANIRDIT-SRKLLEK 1231
Cdd:PRK09776   621 SGGSYDVHYSItplST--LDGEnIGSVLVIQDVTeSRKMLRQ 660
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
1488-1767 1.60e-21

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 103.21  E-value: 1.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1488 RDEQNKVTSVLAIGRDITERKRAEETIKKSEAQLNEAQRIAQIGSWELDIANNILRWSDEIFRIFEIDPKEfGSSYEAFL 1567
Cdd:PRK09776   379 RDTDGTPLYFIAQIEDINELKRTEQVNERLMERITLANEAGGIGIWEWDLKPNIISWDKRMFELYEIPPHI-KPTWQVWY 457
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1568 NAIHPDDREVVNTAYSNSLVNRTPYAIDHRLRFDDGrIKFVHEQCETIYNEENKPLRSIGTVQDITDRKLAEEALKESEE 1647
Cdd:PRK09776   458 ACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVRQLNEALFQEKE 536
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1648 KYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGkKAIDPAWHFYREDgTVLPLEEypVNYVLATRK--ELR 1725
Cdd:PRK09776   537 RLHITLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALG-VPLLTVLHITFGD-NGPLMEN--IYSCLTSRSaaYLE 612
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1085344563 1726 NYVVGVHRTNYKNDVWvlVNADPVWSNENELTQVIVTFSDIT 1767
Cdd:PRK09776   613 QDVVLHCRSGGSYDVH--YSITPLSTLDGENIGSVLVIQDVT 652
GAF COG2203
GAF domain [Signal transduction mechanisms];
180-558 1.88e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 99.11  E-value: 1.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  180 RAYNQLEEENNLRKEAEKELRTINDELEDRVEERTIELHHANVQLEDELAVRQRAESQIRKLNRIYAVLSNINQAIVRIR 259
Cdd:COG2203    127 ARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSAL 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  260 NTKEVFDEACRIATEYGKFTMVWIGIINAKNNKVDVAASSGVESSYLDNLvidlndvQRSSGPTGIAIRTGKHKISNNII 339
Cdd:COG2203    207 DLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRL-------PLGEGLAGRALRTGEPVVVNDAS 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  340 DDDSML-LWKNEAIQYGYKSTASFPLIVFGKVVGAFCIYSDELNFFEDDDVVLLDEMVKDISFAMEFIESEAERRDAENA 418
Cdd:COG2203    280 TDPRFApSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  419 LylsEERFRRLAENAPDVIYRMSLADGKYEYISPAALTIFGYSPDDYYDNPLLFKQSIHSDWIKYFEEHWANLQKGILPQ 498
Cdd:COG2203    360 L---LQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRI 436
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  499 TYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQALQKAAEEIRDL 558
Cdd:COG2203    437 LLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLA 496
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
1111-1233 2.21e-20

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: 88.89  E-value: 2.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1111 SETKLRIMFENSRDALGV-SKKGVHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIPSFYET 1189
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIViDLEGNILYVNPAFEEIFGYSA-EELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEER 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1085344563 1190 RGRKRDGSEFDFEINISTYELNGEI-YTLANIRDITSRKLLEKSL 1233
Cdd:TIGR00229   80 RVRRKDGSEIWVEVSVSPIRTNGGElGVVGIVRDITERKEAEEAL 124
GAF COG2203
GAF domain [Signal transduction mechanisms];
1895-2280 3.84e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 97.96  E-value: 3.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1895 ALNERIKHSQSLLRLSKNLEFAQTYSQALTAALNEIKNILGYKTVWVYLLSEDKKYFNALVARGDFEDIVMSPEGTLILP 1974
Cdd:COG2203      1 LLSVLALALAREVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1975 IEGDRMLEEIAEAKEIVIVEDARADERTNKKIVETLGNRTIINVPIYLLDKHLGTVGTGTFSDEGVRIPTRSEKEFLLAM 2054
Cdd:COG2203     81 IDALVLLSLVATAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2055 ASHLAVTLDRLHLLVERQEAEKALLRLN-RELKAISNCNQSLLRAEDEQSLLNEICRIICEEAGYDFAWVGYTEHsDANT 2133
Cdd:COG2203    161 TDLVGQLAALAGLILDIARLLTQRARLElERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDE-DGGE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2134 IHPVAWAGIDIDLKAKEKFDWSeeiecglrPAQKVIQTGDIIYVQDFSSDASLESWCQKAL-QRGYRSGMALPLKNENsQ 2212
Cdd:COG2203    240 LELVAAPGLPEEELGRLPLGEG--------LAGRALRTGEPVVVNDASTDPRFAPSLRELLlALGIRSLLCVPLLVDG-R 310
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 2213 VFGVILIYSTNRNVITQDEIRLIEELANDLAFGIITLQTRAERKRVEKELELHRDHLQELVNVRTEEL 2280
Cdd:COG2203    311 LIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLL 378
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
553-801 1.71e-19

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: 94.80  E-value: 1.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  553 EEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKMkFTDIITPKSLKTFNENFPGFKEKGWIKNLEFELi 632
Cdd:COG5805     34 EELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKT-IFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIY- 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  633 RKDGSILPILASATAIkdSDGNYLMSRSTVNDIAELKLAELQLRNSEREFRTLAENLPDHIIRYDIDCRVIYLNHVVAA- 711
Cdd:COG5805    112 CKDGELIYVEVKLFPI--YNQNGQAAILALRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERl 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  712 TNYTNSSLVGKLSAEiqFNEAKGLEEYNEKLRRVIKTGTEDEMEIMLRDIEGNLHIHEVHFLAERDIEGKIVGALAIGHD 791
Cdd:COG5805    190 FGAPREELIGKNLLE--LLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRD 267
                          250
                   ....*....|
gi 1085344563  792 ISERKQAEEE 801
Cdd:COG5805    268 ITEKKEAEEL 277
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1541-1629 7.78e-18

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: 80.46  E-value: 7.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1541 ILRWSDEIFRIFEIDPKEFGSSYEAFLNAIHPDDREVVNTAYSNSLVNRTPYAIDHRLRFDDGRIKFVHEQCETIYNEEN 1620
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                   ....*....
gi 1085344563 1621 KPLRSIGTV 1629
Cdd:pfam08447   81 KPVRVIGVA 89
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
259-404 1.01e-16

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 79.05  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  259 RNTKEVFDEACRIATEYGKFTMVWIGIINAKNNKVdvaassgvESSYLDNLVIDLNDVQRSSGPTGIAIRTGKHKISNNI 338
Cdd:pfam13185    2 ADLEELLDAVLEAAVELGASAVGFILLVDDDGRLA--------AWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDL 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563  339 IDDDSMLLWknEAIQYGYKSTASFPLIVFGKVVGAFCIYSDELNFFEDDDVVLLDEMVKDISFAME 404
Cdd:pfam13185   74 AADPAKKGL--PAGHAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
PRK13560 PRK13560
hypothetical protein; Provisional
1551-1896 2.69e-16

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 85.49  E-value: 2.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1551 IFEIDPKEFGSSYEAFLNAIHPDDREVVNTAysnslVNRTPYAIDHRLRFDDGRIKFVHEQC------ETIYNEENKPLR 1624
Cdd:PRK13560   104 LAAIAKHDLMADKGLLAMLIGGDDGDFFFAN-----PFRSAETIAMALQSDDWQEEEGHFRCgdgrfiDCCLRFERHAHA 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1625 SI---GTVQDITDRKLAEEALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKA--IDPAwhf 1699
Cdd:PRK13560   179 DDqvdGFAEDITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIhdFAPA--- 255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1700 YREDgtvlpleeypvNYVLATRKELRNYVVGVHRTNYKN------DVWVLVNADPVWSNENELTQVIVTFSDITMRKNAE 1773
Cdd:PRK13560   256 QPAD-----------DYQEADAAKFDADGSQIIEAEFQNkdgrtrPVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAE 324
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1774 VALKLSEERYRTLVEQAMDGIFIADSNGNYIDVNRSGC-NMLGYTRDQLLKLRMQDLIPAEEQQ------------TTPI 1840
Cdd:PRK13560   325 RELLEKEDMLRAIIEAAPIAAIGLDADGNICFVNNNAAeRMLGWSAAEVMGKPLPGMDPELNEEfwcgdfqewypdGRPM 404
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 1841 QFE------KLRSGKTALAERNLI-RNDGSLLPVEI--SGIMLPDKRFLG---IVRDITERKKNEAAL 1896
Cdd:PRK13560   405 AFDacpmakTIKGGKIFDGQEVLIeREDDGPADCSAyaEPLHDADGNIIGaiaLLVDITERKQVEEQL 472
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1003-1093 7.86e-16

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: 74.68  E-value: 7.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1003 KIILSDESCRIFGLQQEnyhkELDEWHKQWLQLILPEDKERAEKTAIDAVQKDIPYNLDYRIIRHNGELRYIHSEANVRR 1082
Cdd:pfam08447    1 IIYWSPRFEEILGYTPE----ELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR 76
                           90
                   ....*....|.
gi 1085344563 1083 DSSGKPIFMLG 1093
Cdd:pfam08447   77 DENGKPVRVIG 87
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
2098-2246 9.67e-14

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 70.57  E-value: 9.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2098 AEDEQSLLNEICRIICEEAGYDFAWVGYTEHSDantiHPVAWAGIDIDLKAKEKFDWSEEiecglrPAQKVIQTGDIIYV 2177
Cdd:pfam13185    1 AADLEELLDAVLEAAVELGASAVGFILLVDDDG----RLAAWGGAADELSAALDDPPGEG------LVGEALRTGRPVIV 70
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563 2178 QDFSSDASLESWcqKALQRGYRSGMALPLKNENsQVFGVILIYSTNRNVITQDEIRLIEELANDLAFGI 2246
Cdd:pfam13185   71 NDLAADPAKKGL--PAGHAGLRSFLSVPLVSGG-RVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
422-548 1.18e-13

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: 69.63  E-value: 1.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  422 SEERFRRLAENAPDVIYRMSLaDGKYEYISPAALTIFGYSPDDYYD-NPLLFKQSIHSDWIK-YFEEHwanLQKGILPQT 499
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDL-EGNILYVNPAFEEIFGYSAEELIGrNVLELIPEEDREEVReRIERR---LEGEPEPVS 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1085344563  500 YEYQIIHKSGEARWLNQRNILVlDEGGNSVAIEGVVTDITERKQAEQAL 548
Cdd:TIGR00229   77 EERRVRRKDGSEIWVEVSVSPI-RTNGGELGVVGIVRDITERKEAEEAL 124
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
449-535 4.54e-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: 63.90  E-value: 4.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  449 YISPAALTIFGYSPDDYYDNPLLFKQSIH-SDWIKYFEEHWANLQKGIlPQTYEYQIIHKSGEARWLNQRNILVLDEGGN 527
Cdd:pfam08447    3 YWSPRFEEILGYTPEELLGKGESWLDLVHpDDRERVREALWEALKGGE-PYSGEYRIRRKDGEYRWVEARARPIRDENGK 81

                   ....*...
gi 1085344563  528 SVAIEGVV 535
Cdd:pfam08447   82 PVRVIGVA 89
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
1800-1888 5.56e-12

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: 64.02  E-value: 5.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1800 NGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFekLRSGKTALA-ERNLIRNDGSLLPVEISGIMLPD-- 1876
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREA--LREGKAVREfEVVLYRKDGEPFPVLVSLAPIRDdg 78
                           90
                   ....*....|....*
gi 1085344563 1877 ---KRFLGIVRDITE 1888
Cdd:pfam13426   79 gelVGIIAILRDITE 93
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
1391-1512 5.83e-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: 5.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1391 REYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGEN-SELEIL 1469
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEpVSEERR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1085344563 1470 VPNPNNEQIVHQIrIIAERDEQNKVTSVLAIGRDITERKRAEE 1512
Cdd:TIGR00229   81 VRRKDGSEIWVEV-SVSPIRTNGGELGVVGIVRDITERKEAEE 122
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
562-665 1.43e-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: 57.26  E-value: 1.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  562 APCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKMkFTDIITPKSLKTFNENFPGFKEKGWIKNLEFELIRKDGSILPI 641
Cdd:cd00130      1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKS-LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWV 79
                           90       100
                   ....*....|....*....|....
gi 1085344563  642 LASATAIKDSDGNYLMSRSTVNDI 665
Cdd:cd00130     80 LVSLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1402-1504 2.97e-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: 56.49  E-value: 2.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1402 LPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGENSELEILVPNPNNEQIVHQ 1481
Cdd:cd00130      1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                           90       100
                   ....*....|....*....|...
gi 1085344563 1482 IRIIAERDEQNKVTSVLAIGRDI 1504
Cdd:cd00130     81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
687-797 6.18e-09

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: 55.88  E-value: 6.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  687 ENLPDHIIRYDIDCRVIYLN-HVVAATNYTNSSLVGKLSAEIqFNEAKGlEEYNEKLRRVIKTG-TEDEMEIMLRDieGN 764
Cdd:pfam08448    2 DSLPDALAVLDPDGRVRYANaAAAELFGLPPEELLGKTLAEL-LPPEDA-ARLERALRRALEGEePIDFLEELLLN--GE 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1085344563  765 LHIHEVHFLAERDIEGKIVGALAIGHDISERKQ 797
Cdd:pfam08448   78 ERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PRK13558 PRK13558
bacterio-opsin activator; Provisional
2070-2265 1.03e-08

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 60.62  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2070 ERQEAEKALLRLNRELKA--------ISNCNQSLLRAEDEQSLLNEICRIICEEAGYDFAWVGYTEHSDAnTIHPVAWAG 2141
Cdd:PRK13558   264 ERKEAELALQRERRKLQRllerveglVNDVTSALVRATDREEIEAAVCDRVGAGGEYDGAWIGEYDPTSG-TITVAEAAG 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2142 iDIDLKAKEKFDWSEEiecglRPAQKVIQT--GDIIYVQdfssDASLESWCQKAlqRGyRSGMALPLKNeNSQVFGVILI 2219
Cdd:PRK13558   343 -GCDGADGDVLDLAAA-----GPAAAALQSvvAETEAVE----STDVDGVSGTV--DG-SAVAAVPLVY-RETTYGVLVV 408
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1085344563 2220 YSTNRNVITQDEIRLIEELANDLAFGIITLQTR---AERKRVEKELELH 2265
Cdd:PRK13558   409 YTAEPDEIDDRERVVLEALGRAVGAAINALESRrtlTTDEVLELEVELS 457
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1781-1847 1.04e-08

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: 53.56  E-value: 1.04e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085344563  1781 ERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRS 1847
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1135-1223 1.14e-08

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: 54.95  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1135 VFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIPSFyETRGRKRDGSEFDFEINIS--TYELNG 1212
Cdd:cd00130     15 LYANPAAEQLLGYSP-EELIGKSLLDLIHPEDREELRERLENLLSGGEPVTL-EVRLRRKDGSVIWVLVSLTpiRDEGGE 92
                           90
                   ....*....|.
gi 1085344563 1213 EIYTLANIRDI 1223
Cdd:cd00130     93 VIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
678-802 1.14e-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: 55.37  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  678 SEREFRTLAENLPDHIIRYDIDCRVIYLNHVVAA-TNYTNSSLVGKLSAEIQFNEakGLEEYNEKLRRVIKTGTED-EME 755
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEiFGYSAEELIGRNVLELIPEE--DREEVRERIERRLEGEPEPvSEE 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1085344563  756 IMLRDIEGNLHIHEVHfLAERDIEGKIVGALAIGHDISERKQAEEER 802
Cdd:TIGR00229   79 RRVRRKDGSEIWVEVS-VSPIRTNGGELGVVGIVRDITERKEAEEAL 124
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1792-1886 8.62e-08

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: 52.25  E-value: 8.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1792 DGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTALA-ERNLIRNDGSLLPVEIS 1870
Cdd:cd00130      3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTlEVRLRRKDGSVIWVLVS 82
                           90       100
                   ....*....|....*....|.
gi 1085344563 1871 GIMLPD-----KRFLGIVRDI 1886
Cdd:cd00130     83 LTPIRDeggevIGLLGVVRDI 103
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
1059-1101 3.28e-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: 48.72  E-value: 3.28e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1085344563  1059 NLDYRIIRHNGELRYIHSEANVRRDSSGKPIFMLGMMQDITVR 1101
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
1246-1379 9.21e-06

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 47.47  E-value: 9.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1246 ENFFDSLAQFLGENLDMDYVVVDKLDDNPEIAETIALYAKGSIVPNIRYalkGTPCENVM-GRQLCFYPKEVQKLFPDDK 1324
Cdd:pfam01590    3 EEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIPP---GTGVTVLRtGRPLVVPDAAGDPRFLDPL 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 1325 LLLE-MGVDSYMGIPLWDSfGKPIGLIALmSSKSHPEDSIAIQVLQLVATRAAAEL 1379
Cdd:pfam01590   80 LLLRnFGIRSLLAVPIIDD-GELLGVLVL-HHPRPPFTEEELELLEVLADQVAIAL 133
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
424-493 1.06e-05

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: 45.08  E-value: 1.06e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563   424 ERFRRLAENAPDVIYRmSLADGKYEYISPAALTIFGYSPDDYYDNPLLfkQSIHSDWIKYFEEHWANLQK 493
Cdd:smart00091    1 ERLRAILESLPDGIFV-LDLDGRILYANPAAEELLGYSPEELIGKSLL--ELIHPEDRERVQEALQRLLS 67
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1394-1459 1.44e-05

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: 1.44e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563  1394 EFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALA 1459
Cdd:smart00091    2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1925-2071 2.37e-05

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.61  E-value: 2.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  1925 AALNEIKNILGYKTVWVYLLSEDKKYFNALVARGDFEDIVMSPEGTLILPIEGdrmleEIAEAKEIVIVEDARADERTNK 2004
Cdd:smart00065    8 TILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLGIRFPLDEGLAG-----RVAETGRPLNIPDVEADPLFAE 82
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563  2005 KIVE-TLGNRTIINVPIYLLDKHLGTVGTgtFSDEGVRIPTRSEKEFLLAMASHLAVTLDrLHLLVER 2071
Cdd:smart00065   83 DLLGrYQGVRSFLAVPLVADGELVGVLAL--HNKKSPRPFTEEDEELLQALANQLAIALA-NAQLYEE 147
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1246-1389 3.75e-05

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.22  E-value: 3.75e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  1246 ENFFDSLAQFLGENLDMDYVVVDKLDDNPE-IAETIALYAKGSIVPNIRYAL-KGTPCENVMGRQLCFYPkEVQK--LFP 1321
Cdd:smart00065    3 EELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLPTLGIRFPLdEGLAGRVAETGRPLNIP-DVEAdpLFA 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085344563  1322 DDKLLLEMGVDSYMGIPLWDSfGKPIGLIALMSSKS----HPEDsiaIQVLQLVATRAAAELERDRSDRILR 1389
Cdd:smart00065   82 EDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSprpfTEED---EELLQALANQLAIALANAQLYEELR 149
 
Name Accession Description Interval E-value
KdpD COG2205
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
2301-2537 2.80e-78

K+-sensing histidine kinase KdpD [Signal transduction mechanisms];


Pssm-ID: 441807 [Multi-domain]  Cd Length: 239  Bit Score: 259.45  E-value: 2.80e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2301 LQHSLEKEKELSELKSRFISTTSHEFRTPLTTVRVSAEMIQRyRKRWTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSE 2380
Cdd:COG2205      2 LEEALEELEELERLKSEFLANVSHELRTPLTSILGAAELLLD-EEDLSPEERRELLEIIRESAERLLRLIEDLLDLSRLE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2381 SGKIVLNREEIDLHEFCLDVIEEAKISATEA-HKLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQ 2459
Cdd:COG2205     81 SGKLSLELEPVDLAELLEEAVEELRPLAEEKgIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITISARR 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 2460 LRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:COG2205    161 EGDGVRISVSDNGPGIPEEELERIFERFYRGDNSRGEGGTGLGLAIVKRIVEAHGGTIWVESEPGGGTTFTVTLPLAE 238
WalK COG5002
Sensor histidine kinase WalK [Signal transduction mechanisms];
2199-2537 1.76e-74

Sensor histidine kinase WalK [Signal transduction mechanisms];


Pssm-ID: 444026 [Multi-domain]  Cd Length: 390  Bit Score: 254.48  E-value: 1.76e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2199 RSGMALPLKNENSQVFGVILIYSTNRNVITQDEIRLIEELANDLAFGIITLQTRAERKRVEKELELHRDHLQELVNVRTE 2278
Cdd:COG5002     49 LLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILLAALLLLLSELLLLL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2279 ELDKVNKKLIIEFEKEKEFERMLQHSLEKEKELSELKSRFISTTSHEFRTPLTTVRVSAEMIQRYRKRwTEDKLDVFLDK 2358
Cdd:COG5002    129 LLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRREFVANVSHELRTPLTSIRGYLELLLDGAAD-DPEERREYLEI 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2359 IKNSVDYLTKLLDDVLTISRSESGKIVLNREEIDLHEFCLDVIEEAKISATEA-HKLIFNFTLKKIHYRLDPKLMKFILL 2437
Cdd:COG5002    208 ILEEAERLSRLVNDLLDLSRLESGELKLEKEPVDLAELLEEVVEELRPLAEEKgIELELDLPEDPLLVLGDPDRLEQVLT 287
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2438 NLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKN--TTDISGTGLGLSIVKRAVDLHNG 2515
Cdd:COG5002    288 NLLDNAIKYTPEGGTITVSLREEDDQVRISVRDTGIGIPEEDLPRIFERFYRVDKsrSRETGGTGLGLAIVKHIVEAHGG 367
                          330       340
                   ....*....|....*....|..
gi 1085344563 2516 IITVKSELNAGTTFTVKIPLEQ 2537
Cdd:COG5002    368 RIWVESEPGKGTTFTITLPLAR 389
BaeS COG0642
Signal transduction histidine kinase [Signal transduction mechanisms];
2214-2536 5.00e-71

Signal transduction histidine kinase [Signal transduction mechanisms];


Pssm-ID: 440407 [Multi-domain]  Cd Length: 328  Bit Score: 242.12  E-value: 5.00e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2214 FGVILIYSTNRNVITQDEIRLIEELANDLAFGIITLQTRAERKRVEKELEL-HRDHLQELVNVRTEELDKVNKKLIIEFE 2292
Cdd:COG0642      8 LVLLLLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALlALLLLLLLLLLLLLLLLLLLLLLLLLLL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2293 KEKEFERMLQHSLEKEKELSELKSRFISTTSHEFRTPLTTVRVSAEMIQRYrkrwTEDKLDVFLDKIKNSVDYLTKLLDD 2372
Cdd:COG0642     88 LLLLLLLLLLALLLLLEEANEAKSRFLANVSHELRTPLTAIRGYLELLLEE----LDEEQREYLETILRSADRLLRLIND 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2373 VLTISRSESGKIVLNREEIDLHEFCLDVIEEAKISATEAH-KLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGG 2451
Cdd:COG0642    164 LLDLSRLEAGKLELEPEPVDLAELLEEVVELFRPLAEEKGiELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGG 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2452 KIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTV 2531
Cdd:COG0642    244 TVTVSVRREGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSRRGGGTGLGLAIVKRIVELHGGTIEVESEPGKGTTFTV 323

                   ....*
gi 1085344563 2532 KIPLE 2536
Cdd:COG0642    324 TLPLA 328
COG4251 COG4251
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ...
2212-2537 9.75e-45

Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];


Pssm-ID: 443393 [Multi-domain]  Cd Length: 503  Bit Score: 171.51  E-value: 9.75e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2212 QVFGVILIYSTNRNVITQDEIRLIEELANDLAFGIITLQTRAERKRVEKELELHRDHLQELVNVRTEELDKVNKKLiief 2291
Cdd:COG4251    207 LELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLLILLLLLLILVLELLELRLELEELEEELEERTAELERSNEEL---- 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2292 ekekefermlqhslekekelselkSRFISTTSHEFRTPLTTVRVSAEMIQ-RYRKRWTEDKLDvFLDKIKNSVDYLTKLL 2370
Cdd:COG4251    283 ------------------------EQFAYVASHDLREPLRKISGFSQLLEeDYGDKLDEEGRE-YLERIRDAAERMQALI 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2371 DDVLTISRSESGKivLNREEIDLHEFCLDVIEEAKISATEAHKLIFNFTLKKIHYrlDPKLMKFILLNLLSNAIKYSPKG 2450
Cdd:COG4251    338 DDLLAYSRVGRQE--LEFEPVDLNELLEEVLEDLEPRIEERGAEIEVGPLPTVRG--DPTLLRQVFQNLISNAIKYSRPG 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2451 --GKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTT 2528
Cdd:COG4251    414 epPRIEIGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRLHSRDEYEGTGIGLAIVKKIVERHGGRIWVESEPGEGAT 493

                   ....*....
gi 1085344563 2529 FTVKIPLEQ 2537
Cdd:COG4251    494 FYFTLPKAP 502
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
2323-2537 2.12e-42

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: 162.05  E-value: 2.12e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2323 SHEFRTPLTTVRVSAEMIQR-YRKRWTEDK--LDVFLDKIKNSVDYLTKLLDDVLTISRSESgkivLNREEIDLHEFCLD 2399
Cdd:COG5000    209 AHEIKNPLTPIQLSAERLRRkLADKLEEDRedLERALDTIIRQVDRLKRIVDEFLDFARLPE----PQLEPVDLNELLRE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2400 VIEEAKISATEAH-KLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTD 2478
Cdd:COG5000    285 VLALYEPALKEKDiRLELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTRREDGRVRIEVSDNGPGIPEE 364
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563 2479 DLKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:COG5000    365 VLERIFEPFF----TTKPKGTGLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAE 419
PAS COG2202
PAS domain [Signal transduction mechanisms];
1638-1896 2.38e-41

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 154.03  E-value: 2.38e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1638 AEEALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDPAWHFYREdgtvlplEEYPVNYV 1717
Cdd:COG2202      2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDD-------EFLELLRA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1718 LATRKELRNYVVGVHRTNyKNDVWVLVNADPVWSNENELTQVIVTFSDITMRKNAEVALKLSEERYRTLVEQAMDGIFIA 1797
Cdd:COG2202     75 ALAGGGVWRGELRNRRKD-GSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1798 DSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTALAERNLIRNDGSLLPVEISGIMLPD- 1876
Cdd:COG2202    154 DLDGRILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLr 233
                          250       260
                   ....*....|....*....|....*
gi 1085344563 1877 -----KRFLGIVRDITERKKNEAAL 1896
Cdd:COG2202    234 dggevIGVLGIVRDITERKRAEEAL 258
PAS COG2202
PAS domain [Signal transduction mechanisms];
415-675 2.15e-40

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 151.33  E-value: 2.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  415 AENALYLSEERFRRLAENAPDVIYRMSLaDGKYEYISPAALTIFGYSPDDYYDNPLLFKqsIHSDWIKYFEEHWANLQKG 494
Cdd:COG2202      2 AEEALEESERRLRALVESSPDAIIITDL-DGRILYVNPAFERLTGYSAEELLGKTLRDL--LPPEDDDEFLELLRAALAG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  495 ILPQTYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQALQKAAEEIRDLYNNAPCGYHSLDKEGT 574
Cdd:COG2202     79 GGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  575 FVRINNTELKWLGYTLEEVIGKmKFTDIITPKSLKTFNENFPGFKEKGwIKNLEFELIRKDGSILPILASATAIKDSDGN 654
Cdd:COG2202    159 ILYVNPAAEELLGYSPEELLGK-SLLDLLHPEDRERLLELLRRLLEGG-RESYELELRLKDGDGRWVWVEASAVPLRDGG 236
                          250       260
                   ....*....|....*....|..
gi 1085344563  655 -YLMSRSTVNDIAELKLAELQL 675
Cdd:COG2202    237 eVIGVLGIVRDITERKRAEEAL 258
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
2324-2537 5.39e-40

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 153.46  E-value: 5.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2324 HEFRTPLTTVRVSAEMIQRyrkRWTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSESgkivLNREEIDLHEFCLDVIEE 2403
Cdd:COG3852    144 HEIRNPLTGIRGAAQLLER---ELPDDELREYTQLIIEEADRLNNLVDRLLSFSRPRP----PEREPVNLHEVLERVLEL 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2404 AKISATEAHKLIFNF--TLKKIhyRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKM----------VISVKDK 2471
Cdd:COG3852    217 LRAEAPKNIRIVRDYdpSLPEV--LGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVERQVTlgglrprlyvRIEVIDN 294
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 2472 GIGIPTDDLKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:COG3852    295 GPGIPEEILDRIFEPFF----TTKEKGTGLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQ 356
TMAO_torS TIGR02956
TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the ...
2249-2537 1.47e-39

TMAO reductase sytem sensor TorS; This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems]


Pssm-ID: 274362 [Multi-domain]  Cd Length: 968  Bit Score: 161.48  E-value: 1.47e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2249 LQTRAERKRVEKELELHRDHLQELVNVRTEELDKVNKKLIIEfekekeferMLQHSLEKE--KELSELKSRFISTTSHEF 2326
Cdd:TIGR02956  405 LKLQADERQVAQELQEHKESLEQLVAQRTQELAETNERLNAE---------VKNHAKARAeaEEANRAKSAFLATMSHEI 475
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2327 RTPLTTVRVSAEMIQryRKRWTEDKLDvFLDKIKNSVDYLTKLLDDVLTISRSESGKIVLNREEIDLHEFCLDVIEEAKI 2406
Cdd:TIGR02956  476 RTPLNGILGTLELLG--DTGLTSQQQQ-YLQVINRSGESLLDILNDILDYSKIEAGHLSISPRPFDLNALLDDVHHLMVS 552
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2407 SATEAH-KLIFNFTLKKIHYRL-DPKLMKFILLNLLSNAIKYSPKgGKIELTIK-QLRGKMVISVKDKGIGIPTDDLKHL 2483
Cdd:TIGR02956  553 RAQLKGiQLRLNIPEQLPNWWQgDGPRIRQVLINLVGNAIKFTDR-GSVVLRVSlNDDSSLLFEVEDTGCGIAEEEQATL 631
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1085344563 2484 FEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:TIGR02956  632 FDAFTQADGRRRSGGTGLGLAISQRLVEAMDGELGVESELGVGSCFWFTLPLTR 685
HATPase_c smart00387
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
2428-2536 9.78e-39

Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.


Pssm-ID: 214643 [Multi-domain]  Cd Length: 111  Bit Score: 140.86  E-value: 9.78e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTT-DISGTGLGLSIV 2506
Cdd:smart00387    2 DPDRLRQVLSNLLDNAIKYTPEGGRITVTLERDGDHVEITVEDNGPGIPPEDLEKIFEPFFRTDKRSrKIGGTGLGLSIV 81
                            90       100       110
                    ....*....|....*....|....*....|
gi 1085344563  2507 KRAVDLHNGIITVKSELNAGTTFTVKIPLE 2536
Cdd:smart00387   82 KKLVELHGGEISVESEPGGGTTFTITLPLE 111
PAS COG2202
PAS domain [Signal transduction mechanisms];
543-802 9.77e-38

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 143.63  E-value: 9.77e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  543 QAEQALQKAAEEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKmKFTDIITPKSLKTFNENFPGFKEKG 622
Cdd:COG2202      1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGK-TLRDLLPPEDDDEFLELLRAALAGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  623 WIKNLEFELIRKDGSILPILASATAIKDSDGNYLMSRSTVNDIAELKLAELQLRNSEREFRTLAENLPDHIIRYDIDCRV 702
Cdd:COG2202     80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  703 IYLNHVVAA-TNYTNSSLVGKLSAEIQFNEAkgLEEYNEKLRRVIKTGTED-EMEIMLRDIEGNLHIHEVHFLAERDiEG 780
Cdd:COG2202    160 LYVNPAAEElLGYSPEELLGKSLLDLLHPED--RERLLELLRRLLEGGRESyELELRLKDGDGRWVWVEASAVPLRD-GG 236
                          250       260
                   ....*....|....*....|..
gi 1085344563  781 KIVGALAIGHDISERKQAEEER 802
Cdd:COG2202    237 EVIGVLGIVRDITERKRAEEAL 258
KinC COG5807
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ...
2316-2535 2.01e-37

Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444509 [Multi-domain]  Cd Length: 358  Bit Score: 145.70  E-value: 2.01e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2316 SRFISTTSHEFRTPLTTVRVSAEMIQryrKRWTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSESgkivLNREEIDLHE 2395
Cdd:COG5807    148 GELAAGIAHEIRNPLTSIKGFLQLLQ---ESREDSEREEYFNIIISEIDRINTIITELLVLSKPKK----FNFKKLNLND 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2396 FCLDVIEEAKISATEAH-KLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIG 2474
Cdd:COG5807    221 VLEDVIALLSTEAILKNiSIKYDLADDEPVINGDKNQLKQVFINLIKNAIEAMETGGNITIKTYVEGDFVVISVKDEGIG 300
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085344563 2475 IPTDDLKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:COG5807    301 IPEEVLEKIGEPFF----TTKEEGTGLGLSICKKIIEEHNGTIEVESKPGKGTTFTIYLPL 357
PAS COG2202
PAS domain [Signal transduction mechanisms];
1383-1642 6.99e-37

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 141.32  E-value: 6.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1383 RSDRILRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGE 1462
Cdd:COG2202      1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1463 NSELEILVPNPNNEQIVHQIRIIAERDEQNKVTSVLAIGRDITERKRAEETIKKSEAQLNEAQRIAQIGSWELDIANNIL 1542
Cdd:COG2202     81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRIL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1543 RWSDEIFRIFEIDPKEFGSSYeaFLNAIHPDDREVVNTAYSNSLVN-RTPYAIDHRLRFDDGRIKFVHEQCETIYNeENK 1621
Cdd:COG2202    161 YVNPAAEELLGYSPEELLGKS--LLDLLHPEDRERLLELLRRLLEGgRESYELELRLKDGDGRWVWVEASAVPLRD-GGE 237
                          250       260
                   ....*....|....*....|.
gi 1085344563 1622 PLRSIGTVQDITDRKLAEEAL 1642
Cdd:COG2202    238 VIGVLGIVRDITERKRAEEAL 258
HATPase cd00075
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ...
2435-2533 1.02e-36

Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ATPase (HATPase) domains of several ATP-binding proteins such as histidine kinase, DNA gyrase B, topoisomerases, heat shock protein 90 (HSP90), phytochrome-like ATPases and DNA mismatch repair proteins. Domains belonging to this superfamily are also referred to as GHKL (gyrase, heat-shock protein 90, histidine kinase, MutL) ATPase domains.


Pssm-ID: 340391 [Multi-domain]  Cd Length: 102  Bit Score: 134.65  E-value: 1.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHN 2514
Cdd:cd00075      4 VLSNLLDNALKYSPPGGTIEISLRQEGDGVVLEVEDNGPGIPEEDLERIFERFYRGDKSREGGGTGLGLAIVRRIVEAHG 83
                           90
                   ....*....|....*....
gi 1085344563 2515 GIITVKSELNAGTTFTVKI 2533
Cdd:cd00075     84 GRITVESEPGGGTTFTVTL 102
KinD COG5808
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ...
2301-2537 2.49e-36

Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444510 [Multi-domain]  Cd Length: 454  Bit Score: 145.28  E-value: 2.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2301 LQHSLEKEKELSE------------LKSRFISTTSHEFRTPLTTVrvsAEMIQRYRKRWTEDKLDVFLDKIKNSVDYLTK 2368
Cdd:COG5808    215 LQYNLLKRKTLLErviqeintqkleLIGTFAASTAHEIRNPLTSI---KGFIQLLQEKYPELEDQKYFDIIQEEIQRINQ 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2369 LLDDVLTISRSESGKIvlnrEEIDLHEFCLDVIEeakISATEAHK----LIFNFTLKKIHYRLDPKLMKFILLNLLSNAI 2444
Cdd:COG5808    292 IVSEFLVLGKPTAKKL----ELDDLNELIEEILS---IIDSEANLknirVEKQSLDEPLHIKCDKDRIKQVLLNLIKNAI 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2445 KYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGIITVKSELN 2524
Cdd:COG5808    365 EAMKEGGKLTISIENDDEKAVIEVIDNGEGIPEDIIDEIFEPFV----TTKEGGTGLGLSVCKRIVEMHGGEIDIESEEG 440
                          250
                   ....*....|...
gi 1085344563 2525 AGTTFTVKIPLEQ 2537
Cdd:COG5808    441 KGTTFTIRLPLKK 453
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
415-680 3.54e-36

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: 145.50  E-value: 3.54e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  415 AENALYLSEERFRRLAENAPDVIYRMSLaDGKYEYISPAALTIFGYSPDDYYDNPLLfkQSIHSDWIKYFEEHWANLQKG 494
Cdd:COG5809      6 MELQLRKSEQRFRSLFENAPDAILILDL-EGKILKVNPAAERIFGYTEDELLGTNIL--DFLHPDDEKELREILKLLKEG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  495 ILPQTYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQALQKAAEEIRDLYNNAPCGYHSLDKEGT 574
Cdd:COG5809     83 ESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  575 FVRINNTELKWLGYTLEEVIGKmKFTDIITPKSLKTFNENFPGFKEKGWIKNLEFELIRKDGSILPILASATAIKDS--- 651
Cdd:COG5809    163 IIYANPAACKLLGISIEELIGK-SILELIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNgev 241
                          250       260
                   ....*....|....*....|....*....
gi 1085344563  652 DGNYLMSRstvnDIAELKLAELQLRNSER 680
Cdd:COG5809    242 DGIVIIFR----DITERKKLEELLRKSEK 266
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
1634-1932 1.34e-35

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: 143.58  E-value: 1.34e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1634 DRKLAEEALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDpawhfyredgtVLPLEEYP 1713
Cdd:COG5809      2 KSSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILD-----------FLHPDDEK 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1714 VNYVLATRKELRNYVVGVH---RTNYKNDVWVLVNADPVWSNENELTQVIVTFSDITMRKNAEVALKLSEERYRTLVEQA 1790
Cdd:COG5809     71 ELREILKLLKEGESRDELEfelRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHS 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1791 MDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEK-LRSGKTALAERNLIRNDGSLLPVEI 1869
Cdd:COG5809    151 PDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQlLKDGGIAQGEVRFWTKDGRWRLLEA 230
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085344563 1870 SGIMLPD----KRFLGIVRDITERKKNEaalnERIKHSQSLLRLSknlEFAqtysqALTAalNEIKN 1932
Cdd:COG5809    231 SGAPIKKngevDGIVIIFRDITERKKLE----ELLRKSEKLSVVG---ELA-----AGIA--HEIRN 283
COG4191 COG4191
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ...
2193-2535 2.23e-35

Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];


Pssm-ID: 443345 [Multi-domain]  Cd Length: 361  Bit Score: 139.93  E-value: 2.23e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2193 ALQRGYRSGMALPLKNENSQVFGVILIYSTNRNVITQDEIRLIEELANDLAFGIITLQTRAERKRVEKELELHRDHLQEL 2272
Cdd:COG4191     25 LLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGLLLLLLLEALLLLLLAALDAE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2273 VNVRTEELDKVNKKLIIEFEKEKEFERMLQHSlEKEKELSELksrfISTTSHEFRTPLTTVRVSAEMIQRY-RKRWTEDK 2351
Cdd:COG4191    105 ENAELEELERDITELERAEEELRELQEQLVQS-EKLAALGEL----AAGIAHEINNPLAAILGNAELLRRRlEDEPDPEE 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2352 LDVFLDKIKNSVDYLTKLLDDVLTISRSESGKivlnREEIDLHEFCLDVIEEAKISATEAHklIfnftlkKIHYRLDPKL 2431
Cdd:COG4191    180 LREALERILEGAERAAEIVRSLRAFSRRDEEE----REPVDLNELIDEALELLRPRLKARG--I------EVELDLPPDL 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2432 MKF---------ILLNLLSNAIK--YSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHraknTT--DISG 2498
Cdd:COG4191    248 PPVlgdpgqleqVLLNLLINAIDamEEGEGGRITISTRREGDYVVISVRDNGPGIPPEVLERIFEPFF----TTkpVGKG 323
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1085344563 2499 TGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:COG4191    324 TGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPL 360
phoR_proteo TIGR02966
phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory ...
2309-2533 1.08e-34

phosphate regulon sensor kinase PhoR; Members of this protein family are the regulatory histidine kinase PhoR associated with the phosphate ABC transporter in most Proteobacteria. Related proteins from Gram-positive organisms are not included in this model. The phoR gene usually is adjacent to the response regulator phoB gene (TIGR02154). [Signal transduction, Two-component systems]


Pssm-ID: 274368 [Multi-domain]  Cd Length: 333  Bit Score: 136.95  E-value: 1.08e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2309 KELSELKSRFISTTSHEFRTPLTTVRVSAEMIQ--------RYRKrwtedkldvFLDKIKNSVDYLTKLLDDVLTISRSE 2380
Cdd:TIGR02966  108 RRLEQMRRDFVANVSHELRTPLTVLRGYLETLAdgpdedpeEWNR---------ALEIMLEQSQRMQSLVEDLLTLSRLE 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2381 SGKIVLNREEIDLHEFCLDVIEEAKISATEA-HKLIFNF-TLKKIhyRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIK 2458
Cdd:TIGR02966  179 SAASPLEDEPVDMPALLDHLRDEAEALSQGKnHQITFEIdGGVDV--LGDEDELRSAFSNLVSNAIKYTPEGGTITVRWR 256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2459 QLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAknttDIS------GTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVK 2532
Cdd:TIGR02966  257 RDGGGAEFSVTDTGIGIAPEHLPRLTERFYRV----DKSrsrdtgGTGLGLAIVKHVLSRHHARLEIESELGKGSTFSFI 332

                   .
gi 1085344563 2533 I 2533
Cdd:TIGR02966  333 F 333
PAS COG2202
PAS domain [Signal transduction mechanisms];
974-1233 3.24e-34

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 133.61  E-value: 3.24e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  974 RNLSESERRLTEAQRIANVGYWERDFVNNKIILSDESCRIFGLQQEnyhkelDEWHKQWLQLILPEDKERAEKTAIDAVQ 1053
Cdd:COG2202      4 EALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAE------ELLGKTLRDLLPPEDDDEFLELLRAALA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1054 KDIPYNLDYRIIRHNGELRYIHSEANVRRDSSGKPIFMLGMMQDITVRKRAEESLLESETKLRIMFENSRDALGV-SKKG 1132
Cdd:COG2202     78 GGGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVlDLDG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1133 VHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIPSFYETRGRKRDGSEFDFEINISTYELNG 1212
Cdd:COG2202    158 RILYVNPAAEELLGYSP-EELLGKSLLDLLHPEDRERLLELLRRLLEGGRESYELELRLKDGDGRWVWVEASAVPLRDGG 236
                          250       260
                   ....*....|....*....|..
gi 1085344563 1213 EI-YTLANIRDITSRKLLEKSL 1233
Cdd:COG2202    237 EViGVLGIVRDITERKRAEEAL 258
HATPase_c pfam02518
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ...
2428-2537 3.61e-33

Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.


Pssm-ID: 460579 [Multi-domain]  Cd Length: 109  Bit Score: 124.79  E-value: 3.61e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQlRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKnTTDISGTGLGLSIVK 2507
Cdd:pfam02518    2 DELRLRQVLSNLLDNALKHAAKAGEITVTLSE-GGELTLTVEDNGIGIPPEDLPRIFEPFSTAD-KRGGGGTGLGLSIVR 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1085344563 2508 RAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:pfam02518   80 KLVELLGGTITVESEPGGGTTVTLTLPLAQ 109
MtrAB_MtrB NF040691
MtrAB system histidine kinase MtrB;
2301-2536 4.57e-32

MtrAB system histidine kinase MtrB;


Pssm-ID: 468655 [Multi-domain]  Cd Length: 507  Bit Score: 133.61  E-value: 4.57e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2301 LQHSLEKEKELSELKSRFISTTSHEFRTPLTTVRVSAEMIQRYRkrwteDKLDVFLDK----IKNSVDYLTKLLDDVLTI 2376
Cdd:NF040691   257 LQRQIRQLEELSRLQQRFVSDVSHELRTPLTTIRMAADVIHDSR-----DDFDPATARsaelLHTELDRFESLLSDLLEI 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2377 SRSESGKIVLNREEIDLHEFCLDVIEEAKISATEAH-KLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSpKGGKIEL 2455
Cdd:NF040691   332 SRFDAGAAELDVEPVDLRPLVRRVVDALRQLAERAGvELRVDAPGTPVVAEVDPRRVERVLRNLVVNAIEHG-EGKPVVV 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2456 TIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRA----KNTTdiSGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTV 2531
Cdd:NF040691   411 TVAQDDTAVAVTVRDHGVGLKPGEVALVFDRFWRAdparARTT--GGTGLGLAIALEDARLHGGWLEAWGRPGQGSQFRL 488

                   ....*
gi 1085344563 2532 KIPLE 2536
Cdd:NF040691   489 TLPRV 493
HATPase_EvgS-ArcB-TorS-like cd16922
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ...
2435-2535 5.52e-32

Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid sensor histidine kinases, similar to Escherichia coli EvgS, ArcB, TorS, BarA, RcsC; This family contains the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinases (HKs), including the following Escherichia coli HKs: EvgS, a HK of the EvgS-EvgA two-component system (TCS) that confers acid resistance; ArcB, a HK of the ArcB-ArcA TCS that modulates the expression of numerous genes in response to respiratory growth conditions; TorS, a HK of the TorS-TorR TCS which is involved in the anaerobic utilization of trimethylamine-N-oxide; BarA, a HK of the BarA-UvrY TCS involved in the regulation of carbon metabolism; and RcsC, a HK of the RcsB-RcsC TCS which regulates the expression of the capsule operon and of the cell division gene ftsZ. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), with most having accessory sensor domain(s) such as GAF, PAS and CHASE; many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340399 [Multi-domain]  Cd Length: 110  Bit Score: 121.45  E-value: 5.52e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKYSPKGGkIELTIK---------QLRgkmvISVKDKGIGIPTDDLKHLFEPFHRAKNTT--DISGTGLGL 2503
Cdd:cd16922      4 ILLNLLGNAIKFTEEGE-VTLRVSleeeeedgvQLR----FSVEDTGIGIPEEQQARLFEPFSQADSSTtrKYGGTGLGL 78
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1085344563 2504 SIVKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:cd16922     79 AISKKLVELMGGDISVESEPGQGSTFTFTLPL 110
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
2299-2537 8.81e-32

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: 132.41  E-value: 8.81e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2299 RMLQHSLEKEKELSELkSRFISTTSHEFRTPLTTVRvsaEMIQRYRKRWTEDKLDvFLDKIKNSVDYLTKLLDDVLTISR 2378
Cdd:COG5809    255 KKLEELLRKSEKLSVV-GELAAGIAHEIRNPLTSLK---GFIQLLKDTIDEEQKT-YLDIMLSELDRIESIISEFLVLAK 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2379 SESGKIvlnrEEIDLHEFCLDVIEeakISATEAhklifnfTLKKIHYRL-----------DPKLMKFILLNLLSNAIKYS 2447
Cdd:COG5809    330 PQAIKY----EPKDLNTLIEEVIP---LLQPQA-------LLKNVQIELeleddipdilgDENQLKQVFINLLKNAIEAM 395
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2448 PKGGKIELTIKQLR-GKMVISVKDKGIGIPTDDLKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAG 2526
Cdd:COG5809    396 PEGGNITIETKAEDdDKVVISVTDEGCGIPEERLKKLGEPFY----TTKEKGTGLGLMVSYKIIEEHGGKITVESEVGKG 471
                          250
                   ....*....|.
gi 1085344563 2527 TTFTVKIPLEQ 2537
Cdd:COG5809    472 TTFSITLPIKL 482
PRK09303 PRK09303
histidine kinase;
2305-2534 3.93e-31

histidine kinase;


Pssm-ID: 236462 [Multi-domain]  Cd Length: 380  Bit Score: 127.76  E-value: 3.93e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2305 LEKEKE-LSE---LKSRFISTTSHEFRTPLTTVRVSAEMIQRYRKRWTEDK----LDVFLDKIKNSVDYLTKLLDDVLTI 2376
Cdd:PRK09303   137 LRQENEtLLEqlkFKDRVLAMLAHDLRTPLTAASLALETLELGQIDEDTELkpalIEQLQDQARRQLEEIERLITDLLEV 216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2377 SRSESGKIVLNREEIDLHEFCLDVIEEakisateahkLIFNFTLKKIHYRLD-----------PKLMKFILLNLLSNAIK 2445
Cdd:PRK09303   217 GRTRWEALRFNPQKLDLGSLCQEVILE----------LEKRWLAKSLEIQTDipsdlpsvyadQERIRQVLLNLLDNAIK 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2446 YSPKGGKIELTI----KQlrgKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKS 2521
Cdd:PRK09303   287 YTPEGGTITLSMlhrtTQ---KVQVSICDTGPGIPEEEQERIFEDRVRLPRDEGTEGYGIGLSVCRRIVRVHYGQIWVDS 363
                          250
                   ....*....|...
gi 1085344563 2522 ELNAGTTFTVKIP 2534
Cdd:PRK09303   364 EPGQGSCFHFTLP 376
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
2324-2536 9.79e-31

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 130.86  E-value: 9.79e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2324 HEFRTPLTTVRVSAEMIQRYRKR--WTEdkldvFLDKIKNSVDYLTKLLDDVLTISRSESGKIVlnreEIDLHEFcldvI 2401
Cdd:PRK11360   399 HEIRNPLTAIRGYVQIWRQQTSDppSQE-----YLSVVLREVDRLNKVIDQLLEFSRPRESQWQ----PVSLNAL----V 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2402 EEAKISATEAHK-------LIFNFTLKKIHyrLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLR-GKMVISVKDKGI 2473
Cdd:PRK11360   466 EEVLQLFQTAGVqarvdfeTELDNELPPIW--ADPELLKQVLLNILINAVQAISARGKIRIRTWQYSdGQVAVSIEDNGC 543
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085344563 2474 GIPTDDLKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLE 2536
Cdd:PRK11360   544 GIDPELLKKIFDPFF----TTKAKGTGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPIN 602
PAS COG2202
PAS domain [Signal transduction mechanisms];
1509-1776 4.09e-30

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 121.67  E-value: 4.09e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1509 RAEETIKKSEAQLNEAQRIAQIGSWELDIANNILRWSDEIFRIFEIDPKEFGSSYEAFLnaIHPDDREVVNTAYSNSLVN 1588
Cdd:COG2202      1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDL--LPPEDDDEFLELLRAALAG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1589 RTPYAIDHRLRFDDGRIKFVHEQCETIYNEENKPLRSIGTVQDITDRKLAEEALKESEEKYRTLIQKIQTAVIVHTPDTQ 1668
Cdd:COG2202     79 GGVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1669 ILICNHSAEILLGLSEDQLLGKKAIDPAWHFYREDGTVLpleeypVNYVLATRKELRNYvvgVHRTNYKNDVWVLVNADP 1748
Cdd:COG2202    159 ILYVNPAAEELLGYSPEELLGKSLLDLLHPEDRERLLEL------LRRLLEGGRESYEL---ELRLKDGDGRWVWVEASA 229
                          250       260
                   ....*....|....*....|....*....
gi 1085344563 1749 VW-SNENELTQVIVTFSDITMRKNAEVAL 1776
Cdd:COG2202    230 VPlRDGGEVIGVLGIVRDITERKRAEEAL 258
PRK15347 PRK15347
two component system sensor kinase;
2303-2536 2.62e-28

two component system sensor kinase;


Pssm-ID: 237951 [Multi-domain]  Cd Length: 921  Bit Score: 125.14  E-value: 2.62e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2303 HSLEKEKELSEL----KSRFISTTSHEFRTPLTTVRVSAEMIQRyrKRWTEDKLDVfLDKIKNSVDYLTKLLDDVLTISR 2378
Cdd:PRK15347   382 QALAEAKQRAEQankrKSEHLTTISHEIRTPLNGVLGALELLQN--TPLTAEQMDL-ADTARQCTLSLLAIINNLLDFSR 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2379 SESGKIVLNREEIDLhefcLDVIEEAKI---SATEAHKLifnfTLKKI-------HYRLDPKLMKFILLNLLSNAIKYSP 2448
Cdd:PRK15347   459 IESGQMTLSLEETAL----LPLLDQAMLtiqGPAQSKSL----TLRTFvgahvplYLHLDSLRLRQILVNLLGNAVKFTE 530
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2449 KGGkIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKntTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTT 2528
Cdd:PRK15347   531 TGG-IRLRVKRHEQQLCFTVEDTGCGIDIQQQQQIFTPFYQAD--THSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSC 607

                   ....*...
gi 1085344563 2529 FTVKIPLE 2536
Cdd:PRK15347   608 FSLVLPLN 615
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
540-801 1.89e-26

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: 116.23  E-value: 1.89e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  540 ERKQAEQALQKAAEEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGkMKFTDIITPKSLKTFNENFPGFK 619
Cdd:COG5809      2 KSSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLG-TNILDFLHPDDEKELREILKLLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  620 EKGWIKNLEFELIRKDGSILPILASATAIKDSDGNYLMSRSTVNDIAELKLAELQLRNSEREFRTLAENLPDHIIRYDID 699
Cdd:COG5809     81 EGESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  700 CRVIYLNHVVAA-TNYTNSSLVGKLSAEIQFNEAKglEEYNEKLRRVIKTGTEDEMEIMLRDIEGNLHIHEVHFlAERDI 778
Cdd:COG5809    161 GRIIYANPAACKlLGISIEELIGKSILELIHSDDQ--ENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASG-APIKK 237
                          250       260
                   ....*....|....*....|...
gi 1085344563  779 EGKIVGALAIGHDISERKQAEEE 801
Cdd:COG5809    238 NGEVDGIVIIFRDITERKKLEEL 260
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
2324-2535 2.78e-26

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: 115.60  E-value: 2.78e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2324 HEFRTPLTTVRVSAEMIQRYRKRwTEDKLDVFLDKIknsvDYLTKLLDDVLTISRSESgkivLNREEIDLHEFCLDVIee 2403
Cdd:COG5805    296 HEIRNPLTSIKGFLQLLQPGIED-KEEYFDIMLSEL----DRIESIISEFLALAKPQA----VNKEKENINELIQDVV-- 364
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2404 aKISATEAH----KLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDD 2479
Cdd:COG5805    365 -TLLETEAIlhniQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTITIHTEEEDNSVIIRVIDEGIGIPEER 443
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 2480 LKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:COG5805    444 LKKLGEPFF----TTKEKGTGLGLMVSYKIIENHNGTIDIDSKVGKGTTFTITLPL 495
cztS_silS_copS TIGR01386
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ...
2316-2534 4.63e-25

heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain (pfam00512) and a domain found in bacterial signal proteins (pfam00672). This group is separated phylogenetically from related proteins with similar architecture and contains a number of proteins associated with heavy metal resistance efflux systems for copper, silver, cadmium, and/or zinc.


Pssm-ID: 273593 [Multi-domain]  Cd Length: 457  Bit Score: 111.33  E-value: 4.63e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2316 SRFISTTSHEFRTPLTTVRVSAEMIQRyRKRWTEDKLDVFLDkikNSVDY--LTKLLDDVLTISRSESGKIVLNREEIDL 2393
Cdd:TIGR01386  242 SQFSADLAHELRTPLTNLLGQTQVALS-QPRTGEEYREVLES---NLEELerLSRMVSDMLFLARADNGQLALERVRLDL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2394 HEFCLDVIEEAKISATEAHKLIF---NFTLkkihyRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKD 2470
Cdd:TIGR01386  318 AAELAKVAEYFEPLAEERGVRIRvegEGLV-----RGDPQMFRRAISNLLSNALRHTPDGGTITVRIERRSDEVRVSVSN 392
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 2471 KGIGIPTDDLKHLFEPFHRA--KNTTDISGTGLGLSIVKRAVDLHNGIITVKSeLNAGTTFTVKIP 2534
Cdd:TIGR01386  393 PGPGIPPEHLSRLFDRFYRVdpARSNSGEGTGLGLAIVRSIMEAHGGRASAES-PDGKTRFILRFP 457
cpxA PRK09470
envelope stress sensor histidine kinase CpxA;
2317-2537 1.75e-24

envelope stress sensor histidine kinase CpxA;


Pssm-ID: 236532 [Multi-domain]  Cd Length: 461  Bit Score: 109.64  E-value: 1.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2317 RFISTTSHEFRTPLTTVRVSAEMIqryRKRWTEDKLdvfLDKIKNSVDYLTKLLDDVLTISRSESgKIVLNREEIDLHEF 2396
Cdd:PRK09470   245 RLLSDISHELRTPLTRLQLATALL---RRRQGESKE---LERIETEAQRLDSMINDLLVLSRNQQ-KNHLERETFKANSL 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2397 CLDVIEEAKISATEAHK-LIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKggKIELTIKQLRGKMVISVKDKGIGI 2475
Cdd:PRK09470   318 WSEVLEDAKFEAEQMGKsLTVSAPPGPWPINGNPNALASALENIVRNALRYSHT--KIEVAFSVDKDGLTITVDDDGPGV 395
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085344563 2476 PTDDLKHLFEPFHRAKNTTDIS--GTGLGLSIVKRAVDLHNG-IITVKSELnAGTTFTVKIPLEQ 2537
Cdd:PRK09470   396 PEEEREQIFRPFYRVDEARDREsgGTGLGLAIVENAIQQHRGwVKAEDSPL-GGLRLTIWLPLYK 459
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
1779-1896 5.79e-24

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: 99.29  E-value: 5.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1779 SEERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTAL--AERN 1856
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEPvsEERR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1085344563 1857 LIRNDGSLLPVEISGIMLPD----KRFLGIVRDITERKKNEAAL 1896
Cdd:TIGR00229   81 VRRKDGSEIWVEVSVSPIRTnggeLGVVGIVRDITERKEAEEAL 124
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
1011-1233 7.65e-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: 108.14  E-value: 7.65e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1011 CRIFGLQQEnyhkELDewHKQWLQLILPEDKERAEKTAIDAVQKDIPYNLDYRIIRHNGELRYIHSEANVRRDSSGKPIF 1090
Cdd:COG5809     45 ERIFGYTED----ELL--GTNILDFLHPDDEKELREILKLLKEGESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEG 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1091 MLGMMQDITVRKRAEESLLESETKLRIMFENSRDALGVS-KKGVHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQ 1169
Cdd:COG5809    119 MLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTdLDGRIIYANPAACKLLGISI-EELIGKSILELIHSDDQEN 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085344563 1170 IIENVKRRDSGEEIPSFyETRGRKRDGSEFDFEINISTYELNGEIYTLANI-RDITSRKLLEKSL 1233
Cdd:COG5809    198 VAAFISQLLKDGGIAQG-EVRFWTKDGRWRLLEASGAPIKKNGEVDGIVIIfRDITERKKLEELL 261
HATPase_BceS-YxdK-YvcQ-like cd16948
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2428-2534 8.22e-24

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis BceS, YxdK, and Bacillus thuringiensis YvcQ; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis BceS and Bacillus thuringiensis YvcQ, the HKs of the two-component regulatory system (TCSs) BceS-BceR and YvcQ-YvcP, repsectively, which are both involved in regulating bacitracin resistance. It also includes the HATPase domain of YxdK, the HK of YxdK-YxdJ TCS involved in sensing antimicrobial compounds.


Pssm-ID: 340424 [Multi-domain]  Cd Length: 109  Bit Score: 98.13  E-value: 8.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKN-TTDISGTGLGLSIV 2506
Cdd:cd16948      2 DAKWLSFIIGQIVSNALKYSKQGGKIEIYSETNEQGVVLSIKDFGIGIPEEDLPRVFDKGFTGENgRNFQESTGMGLYLV 81
                           90       100
                   ....*....|....*....|....*...
gi 1085344563 2507 KRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16948     82 KKLCDKLGHKIDVESEVGEGTTFTITFP 109
BaeS_SmeS NF012163
sensor histidine kinase efflux regulator BaeS;
2234-2534 2.01e-23

sensor histidine kinase efflux regulator BaeS;


Pssm-ID: 411086 [Multi-domain]  Cd Length: 457  Bit Score: 106.45  E-value: 2.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2234 LIEELANDLAFGIITLQTRAERKRVEKELE-LHR----DHLQELVNVRTEELDKVNKKLIIefekekefermLQHSLEKE 2308
Cdd:NF012163   168 LIVALALLLAALAAFLLARGLLAPVKRLVEaTHRlaagDYTTRVTPTSNDELGKLAQDFNQ-----------LASTLEKN 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2309 KELselKSRFISTTSHEFRTPLTTVRVSAEMIQRYRKRWTEDKldvfLDKIKNSVDYLTKLLDDVLTISRSESGKIVLNR 2388
Cdd:NF012163   237 EQM---RRDFMADISHELRTPLAVLRAELEAIQDGIRKFTPES----LDSLQAEVGTLTKLVDDLHDLSMSDEGALAYQK 309
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2389 EEIDLHEfcldVIEeakiSATEAHKLIFNFTLKKIHYRL--------DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQL 2460
Cdd:NF012163   310 ASVDLVP----LLE----VEGGAFRERFASAGLELEVSLpdsslvfgDRDRLMQLFNNLLENSLRYTDSGGSLHISASQR 381
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 2461 RGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDIS--GTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:NF012163   382 PKEVTLTVADSAPGVSDEQLARLFERFYRVEVSRNRAsgGSGLGLAISLNIVQAHGGTLHAAHSPLGGLRIVVTLP 457
PRK11107 PRK11107
hybrid sensory histidine kinase BarA; Provisional
2310-2536 2.78e-23

hybrid sensory histidine kinase BarA; Provisional


Pssm-ID: 236848 [Multi-domain]  Cd Length: 919  Bit Score: 108.78  E-value: 2.78e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2310 ELSELKSRFISTTSHEFRTPLTTVrvsaemI----QRYRKRWTEDKLDvFLDKIKNSVDYLTKLLDDVLTISRSESGKIV 2385
Cdd:PRK11107   288 EAARIKSEFLANMSHELRTPLNGV------IgftrQTLKTPLTPTQRD-YLQTIERSANNLLAIINDILDFSKLEAGKLV 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2386 LnrEEI--DLHEfCLDviEEAKISATEAHKLIFNFTLKkIHYRL------DPKLMKFILLNLLSNAIKYSPKGG---KIE 2454
Cdd:PRK11107   361 L--ENIpfSLRE-TLD--EVVTLLAHSAHEKGLELTLN-IDPDVpdnvigDPLRLQQIITNLVGNAIKFTESGNidiLVE 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2455 LT-IKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKntTDIS----GTGLGLSIVKRAVDLHNGIITVKSELNAGTTF 2529
Cdd:PRK11107   435 LRaLSNTKVQLEVQIRDTGIGISERQQSQLFQAFRQAD--ASISrrhgGTGLGLVITQKLVNEMGGDISFHSQPNRGSTF 512

                   ....*..
gi 1085344563 2530 TVKIPLE 2536
Cdd:PRK11107   513 WFHLPLD 519
PRK13560 PRK13560
hypothetical protein; Provisional
388-806 3.11e-23

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 108.22  E-value: 3.11e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  388 DVVLLDEMVKDISFAMEFIeSEAERRDAEnalylsEERFRRLAENAPDVIYRMSLaDGKYEYISPAAL----TIFGYSPD 463
Cdd:PRK13560    39 DVEELQELLRGHAYDARAI-AEAEAQDCR------EQCERNLKANIPGGMFLFAL-DGDGTFSFPSLLdangELAAIAKH 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  464 DYYDNPLLFKQSIHSDWIKYF-------EEHWANLQKGILPQTYEYQIIHksGEARWLNqrNILVLDEGGNS-VAIEGVV 535
Cdd:PRK13560   111 DLMADKGLLAMLIGGDDGDFFfanpfrsAETIAMALQSDDWQEEEGHFRC--GDGRFID--CCLRFERHAHAdDQVDGFA 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  536 TDITERKQAEQALQKAAEEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGkMKFTDIITPKSLKTFNE-N 614
Cdd:PRK13560   187 EDITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIG-MSIHDFAPAQPADDYQEaD 265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  615 FPGFKEKGwIKNLEFELIRKDGSILP--ILASATAIKDSDGNYLMSRSTVNDIAELKLAELQLRNSEREFRTLAENLPDH 692
Cdd:PRK13560   266 AAKFDADG-SQIIEAEFQNKDGRTRPvdVIFNHAEFDDKENHCAGLVGAITDISGRRAAERELLEKEDMLRAIIEAAPIA 344
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  693 IIRYDIDCRVIYLNHVVAatnytnSSLVGKLSAEIQFNEAKGLE-EYNEKL-----RRVIKTGTEDEMEI--MLRDIEGN 764
Cdd:PRK13560   345 AIGLDADGNICFVNNNAA------ERMLGWSAAEVMGKPLPGMDpELNEEFwcgdfQEWYPDGRPMAFDAcpMAKTIKGG 418
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563  765 LHIHEVHFLAER----------------DIEGKIVGALAIGHDISERKQAEEE-RQANL 806
Cdd:PRK13560   419 KIFDGQEVLIEReddgpadcsayaeplhDADGNIIGAIALLVDITERKQVEEQlLLANL 477
PRK11091 PRK11091
aerobic respiration control sensor protein ArcB; Provisional
2302-2535 8.01e-23

aerobic respiration control sensor protein ArcB; Provisional


Pssm-ID: 236842 [Multi-domain]  Cd Length: 779  Bit Score: 106.95  E-value: 8.01e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2302 QHSLEKEkelSELKSRFISTTSHEFRTPLTTVRVSAEMIqryrkrwtedkLDVFLDK--------IKNSVDYLTKLLDDV 2373
Cdd:PRK11091   273 QDALEKA---SRDKTTFISTISHELRTPLNGIVGLSRIL-----------LDTELTAeqrkylktIHVSAITLGNIFNDI 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2374 LTISRSESGKIVLNREEIDLHEFCLDVIEEAKISAtEAHKLIFNFTLKK---IHYRLDPKLMKFILLNLLSNAIKYSPKG 2450
Cdd:PRK11091   339 IDMDKMERRKLQLDNQPIDFTDFLADLENLSGLQA-EQKGLRFDLEPLLplpHKVITDGTRLRQILWNLISNAVKFTQQG 417
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2451 GkIELTIKQLRGKMV-ISVKDKGIGIPTDDLKHLFEPFHRAKNTTD---ISGTGLGLSIVKRAVDLHNGIITVKSELNAG 2526
Cdd:PRK11091   418 G-VTVRVRYEEGDMLtFEVEDSGIGIPEDELDKIFAMYYQVKDSHGgkpATGTGIGLAVSKRLAQAMGGDITVTSEEGKG 496

                   ....*....
gi 1085344563 2527 TTFTVKIPL 2535
Cdd:PRK11091   497 SCFTLTIHA 505
HATPase_TutC-TodS-like cd16925
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ...
2428-2534 8.32e-23

Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas putida TodS and Thauera aromatica TutC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) such Pseudomonas putida TodS HK of the TodS-TodT two-component regulatory system (TCS) which controls the expression of a toluene degradation pathway. Thauera aromatica TutC may be part of a TCS that is involved in anaerobic toluene metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), PAS sensor domain(s) and a REC domain.


Pssm-ID: 340402 [Multi-domain]  Cd Length: 110  Bit Score: 95.25  E-value: 8.32e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLR-GKMVISVKDKGIGIPTDDLKHLFEPFHRA--KNTTDISGTGLGLS 2504
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILEKFRlNRFLLTVSDSGPGIPPNLREEIFERFRQGdgSSTRAHGGTGLGLS 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1085344563 2505 IVKRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16925     81 IVKEFVELHGGTVTVSDAPGGGALFQVELP 110
phoR PRK11006
phosphate regulon sensor histidine kinase PhoR;
2300-2534 1.48e-22

phosphate regulon sensor histidine kinase PhoR;


Pssm-ID: 182895 [Multi-domain]  Cd Length: 430  Bit Score: 103.17  E-value: 1.48e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2300 MLQHSLEKEKELSELKSRFISTTSHEFRTPLTTVRVSAEMIQryrkrwtEDKLDVFL-DKIKNSVDYLTK----LLDDVL 2374
Cdd:PRK11006   189 MVARDVTQMHQLEGARRNFFANVSHELRTPLTVLQGYLEMMQ-------DQPLEGALrEKALHTMREQTQrmegLVKQLL 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2375 TISRSESGKIVLNREEIDLhEFCLDVIE-EAKISATEAHKLIFNftlkkihyrLDPKLMKF--------ILLNLLSNAIK 2445
Cdd:PRK11006   262 TLSKIEAAPTIDLNEKVDV-PMMLRVLErEAQTLSQGKHTITFE---------VDNSLKVFgnedqlrsAISNLVYNAVN 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2446 YSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKN--TTDISGTGLGLSIVKRAVDLHNGIITVKSEL 2523
Cdd:PRK11006   332 HTPEGTHITVRWQRVPQGAEFSVEDNGPGIAPEHIPRLTERFYRVDKarSRQTGGSGLGLAIVKHALSHHDSRLEIESEV 411
                          250
                   ....*....|.
gi 1085344563 2524 NAGTTFTVKIP 2534
Cdd:PRK11006   412 GKGTRFSFVLP 422
KinB COG5806
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ...
2323-2535 1.63e-22

Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 444508 [Multi-domain]  Cd Length: 412  Bit Score: 103.02  E-value: 1.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2323 SHEFRTPLTTVRVSAEMIQRYRKrwTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSESGKIvlnrEEIDLHEFCLDVIE 2402
Cdd:COG5806    209 AHEVRNPLTVVRGFIQLLQEPEL--SDEKRKQYIRIALEELDRAEAIITDYLTFAKPQPEKL----EKIDVSEELEHVID 282
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2403 ---------EAKISATEAHKLifnftlkKIHYrlDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGI 2473
Cdd:COG5806    283 vlspyanmnNVEIQTELEPGL-------YIEG--DRQKLQQCLINIIKNGIEAMPNGGTLTIDVSIDKNKVIISIKDTGV 353
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085344563 2474 GIPTDDLKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:COG5806    354 GMTKEQLERLGEPYF----STKEKGTGLGTMVSYRIIEAMNGTIRVESEVGKGTTFTITLPL 411
PAS COG2202
PAS domain [Signal transduction mechanisms];
1772-1957 2.13e-22

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 99.33  E-value: 2.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1772 AEVALKLSEERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEK-LRSGKT 1850
Cdd:COG2202      2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAaLAGGGV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1851 ALAERNLIRNDGSLLPVEISGIMLPDK-----RFLGIVRDITERKKNEAALNERIKHSQSLLRLSKNLEFAQTYSQALTA 1925
Cdd:COG2202     82 WRGELRNRRKDGSLFWVELSISPVRDEdgeitGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILY 161
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1085344563 1926 ALNEIKNILGY-------KTVWVYLLSEDKKYFNALVAR 1957
Cdd:COG2202    162 VNPAAEELLGYspeellgKSLLDLLHPEDRERLLELLRR 200
PRK10337 PRK10337
sensor protein QseC; Provisional
2317-2513 3.56e-22

sensor protein QseC; Provisional


Pssm-ID: 182388 [Multi-domain]  Cd Length: 449  Bit Score: 102.42  E-value: 3.56e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2317 RFISTTSHEFRTPLTTVRVSAEMIQ------RYRKRwtedkldvFLDKIKNSVDYLTKLLDDVLTISRSESGKIVLNREE 2390
Cdd:PRK10337   239 RFTSDAAHELRSPLAALKVQTEVAQlsdddpQARKK--------ALLQLHAGIDRATRLVDQLLTLSRLDSLDNLQDVAE 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2391 IDLHEFCLDVIEEAKISATEAHK-LIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRgkmvISVK 2469
Cdd:PRK10337   311 IPLEDLLQSAVMDIYHTAQQAGIdVRLTLNAHPVIRTGQPLLLSLLVRNLLDNAIRYSPQGSVVDVTLNARN----FTVR 386
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1085344563 2470 DKGIGIPTDDLKHLFEPFHRAKNtTDISGTGLGLSIVKRAVDLH 2513
Cdd:PRK10337   387 DNGPGVTPEALARIGERFYRPPG-QEATGSGLGLSIVRRIAKLH 429
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
974-1231 5.88e-22

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 104.37  E-value: 5.88e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  974 RNLSESER-RLTEAQRIAN----VGYWERDFVNNkIILSDEscRIFGLQQENYHKELDEwhKQWLQLILPEDKERAEKTA 1048
Cdd:PRK09776   398 LKRTEQVNeRLMERITLANeaggIGIWEWDLKPN-IISWDK--RMFELYEIPPHIKPTW--QVWYACLHPEDRQRVEKEI 472
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1049 IDAVQKDIPYNLDYRIIRHNGeLRYIHSEANVRRDSSGKPIFMLGMMQDITVRKRAEESLLESETKLRIMFENSRDALGV 1128
Cdd:PRK09776   473 RDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVRQLNEALFQEKERLHITLDSIGEAVVC 551
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1129 SKKGVHV-FANPAYLKLFGYeKLEEIVGTSILECIapshhqqiieNVKRRDSGEEIPSFY---ETRG----------RKR 1194
Cdd:PRK09776   552 TDMAMKVtFMNPVAEKMTGW-TQEEALGVPLLTVL----------HITFGDNGPLMENIYsclTSRSaayleqdvvlHCR 620
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1085344563 1195 DGSEFDFEINI---STyeLNGE-IYTLANIRDIT-SRKLLEK 1231
Cdd:PRK09776   621 SGGSYDVHYSItplST--LDGEnIGSVLVIQDVTeSRKMLRQ 660
PRK13837 PRK13837
two-component system VirA-like sensor kinase;
2299-2535 7.27e-22

two-component system VirA-like sensor kinase;


Pssm-ID: 237526 [Multi-domain]  Cd Length: 828  Bit Score: 103.99  E-value: 7.27e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2299 RMLQHSLEKEKELsELKSRFISTTSHEFRTPLTTVRVSAEMIQryrkrwteDKLDV------FLDKIKNSVDYLTKLLDD 2372
Cdd:PRK13837   435 DALERRLEHARRL-EAVGTLASGIAHNFNNILGAILGYAEMAL--------NKLARhsraarYIDEIISAGARARLIIDQ 505
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2373 VLTISRsesgKIVLNREEIDLHEFCLDVIEEAKISATEAHKLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGK 2452
Cdd:PRK13837   506 ILAFGR----KGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAMDGAGR 581
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2453 IELTIKQ--LRGK-------------MVISVKDKGIGIPTDDLKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGII 2517
Cdd:PRK13837   582 VDISLSRakLRAPkvlshgvlppgryVLLRVSDTGAGIDEAVLPHIFEPFF----TTRAGGTGLGLATVHGIVSAHAGYI 657
                          250
                   ....*....|....*...
gi 1085344563 2518 TVKSELNAGTTFTVKIPL 2535
Cdd:PRK13837   658 DVQSTVGRGTRFDVYLPP 675
PRK11100 PRK11100
sensory histidine kinase CreC; Provisional
2317-2535 1.49e-21

sensory histidine kinase CreC; Provisional


Pssm-ID: 236846 [Multi-domain]  Cd Length: 475  Bit Score: 100.69  E-value: 1.49e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2317 RFISTTSHEFRTPLTTVRVSAEMIQryrKRWTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSESGKIVLNREEIDLHEf 2396
Cdd:PRK11100   258 QYVQTLTHELKSPLAAIRGAAELLQ---EDPPPEDRARFTGNILTQSARLQQLIDRLLELARLEQRQELEVLEPVALAA- 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2397 CLDVIEEAKISATEAHKLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIP 2476
Cdd:PRK11100   334 LLEELVEAREAQAAAKGITLRLRPDDARVLGDPFLLRQALGNLLDNAIDFSPEGGTITLSAEVDGEQVALSVEDQGPGIP 413
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2477 TDDLKHLFEPFHR-AKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:PRK11100   414 DYALPRIFERFYSlPRPANGRKSTGLGLAFVREVARLHGGEVTLRNRPEGGVLATLTLPR 473
HATPase_BasS-like cd16940
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2428-2532 1.54e-21

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BasS HK of the BasS-BasR two-component regulatory system (TCS). Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some contain a HAMP sensory domain, while some an N-terminal two-component sensor kinase domain.


Pssm-ID: 340417 [Multi-domain]  Cd Length: 113  Bit Score: 91.70  E-value: 1.54e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIkQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTdISGTGLGLSIVK 2507
Cdd:cd16940     10 DALLLFLLLRNLVDNAVRYSPQGSRVEIKL-SADDGAVIRVEDNGPGIDEEELEALFERFYRSDGQN-YGGSGLGLSIVK 87
                           90       100
                   ....*....|....*....|....*
gi 1085344563 2508 RAVDLHNGIITVKSELNAGTTFTVK 2532
Cdd:cd16940     88 RIVELHGGQIFLGNAQGGGLEAWVR 112
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
1488-1767 1.60e-21

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 103.21  E-value: 1.60e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1488 RDEQNKVTSVLAIGRDITERKRAEETIKKSEAQLNEAQRIAQIGSWELDIANNILRWSDEIFRIFEIDPKEfGSSYEAFL 1567
Cdd:PRK09776   379 RDTDGTPLYFIAQIEDINELKRTEQVNERLMERITLANEAGGIGIWEWDLKPNIISWDKRMFELYEIPPHI-KPTWQVWY 457
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1568 NAIHPDDREVVNTAYSNSLVNRTPYAIDHRLRFDDGrIKFVHEQCETIYNEENKPLRSIGTVQDITDRKLAEEALKESEE 1647
Cdd:PRK09776   458 ACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVRQLNEALFQEKE 536
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1648 KYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGkKAIDPAWHFYREDgTVLPLEEypVNYVLATRK--ELR 1725
Cdd:PRK09776   537 RLHITLDSIGEAVVCTDMAMKVTFMNPVAEKMTGWTQEEALG-VPLLTVLHITFGD-NGPLMEN--IYSCLTSRSaaYLE 612
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1085344563 1726 NYVVGVHRTNYKNDVWvlVNADPVWSNENELTQVIVTFSDIT 1767
Cdd:PRK09776   613 QDVVLHCRSGGSYDVH--YSITPLSTLDGENIGSVLVIQDVT 652
PRK10841 PRK10841
two-component system sensor histidine kinase RcsC;
2312-2535 1.91e-21

two-component system sensor histidine kinase RcsC;


Pssm-ID: 182772 [Multi-domain]  Cd Length: 924  Bit Score: 102.74  E-value: 1.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2312 SELKSRFISTTSHEFRTPLTTVRVSAEMIQRyrKRWTEDkLDVFLDKIKNSVDYLTKLLDDVLTISRSESGKIvlnreEI 2391
Cdd:PRK10841   444 SQSKSMFLATVSHELRTPLYGIIGNLDLLQT--KELPKG-VDRLVTAMNNSSSLLLKIISDILDFSKIESEQL-----KI 515
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2392 DLHEF-CLDVIeeakisateAHkLIFNF---TLKKihyRL----------------DPKLMKFILLNLLSNAIKYSPKGG 2451
Cdd:PRK10841   516 EPREFsPREVI---------NH-ITANYlplVVKK---RLglycfiepdvpvalngDPMRLQQVISNLLSNAIKFTDTGC 582
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2452 kIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTD--ISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTF 2529
Cdd:PRK10841   583 -IVLHVRVDGDYLSFRVRDTGVGIPAKEVVRLFDPFFQVGTGVQrnFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQF 661

                   ....*.
gi 1085344563 2530 TVKIPL 2535
Cdd:PRK10841   662 TIRIPL 667
PRK10364 PRK10364
two-component system sensor histidine kinase ZraS;
2323-2535 3.29e-21

two-component system sensor histidine kinase ZraS;


Pssm-ID: 236674 [Multi-domain]  Cd Length: 457  Bit Score: 99.48  E-value: 3.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2323 SHEFRTPLTTVRVSAEMIQRYRKRWTEDKldVFLDKIKNSVDYLTKLLDDVLTISRSES---GKIVLNreeiDLHEFCLD 2399
Cdd:PRK10364   245 AHEIRNPLSSIKGLAKYFAERAPAGGEAH--QLAQVMAKEADRLNRVVSELLELVKPTHlalQAVDLN----DLINHSLQ 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2400 VIEEAKISATEAHKLIFNFTLKKIhyRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDD 2479
Cdd:PRK10364   319 LVSQDANSREIQLRFTANDTLPEI--QADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQ 396
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 2480 LKHLFEPFHraknTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:PRK10364   397 LEAIFTPYF----TTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGATFTLWLPV 448
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
1644-1897 4.23e-21

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: 99.81  E-value: 4.23e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1644 ESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDpawhfyredgtvlpLEEYPVNYVLATRKE 1723
Cdd:COG5805     31 EITEELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTIFD--------------FLEKEYHYRVKTRIE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1724 --LRNYVVGVHRTNYKND---VWVLVNADPVWSNENELTqvIVTFSDITMRKNAEVALKLSEERYRTLVEQAMDGIFIAD 1798
Cdd:COG5805     97 rlQKGYDVVMIEQIYCKDgelIYVEVKLFPIYNQNGQAA--ILALRDITKKKKIEEILQEQEERLQTLIENSPDLICVID 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1799 SNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTAL-AERNLIRNDGSLLPVEISGIMLPD- 1876
Cdd:COG5805    175 TDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKERIESITEVWQEFiIEREIITKDGRIRYFEAVIVPLIDt 254
                          250       260
                   ....*....|....*....|....*
gi 1085344563 1877 ----KRFLGIVRDITERKKNEAALN 1897
Cdd:COG5805    255 dgsvKGILVILRDITEKKEAEELMA 279
envZ PRK09467
osmolarity sensor protein; Provisional
2323-2537 7.20e-21

osmolarity sensor protein; Provisional


Pssm-ID: 236531 [Multi-domain]  Cd Length: 435  Bit Score: 98.06  E-value: 7.20e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2323 SHEFRTPLTTVRVSAEMI---QRYRKRW----TEDK---LDVFLDKIKN------SVDYLTKLLDDVLTisrSESGkivl 2386
Cdd:PRK09467   237 SHDLRTPLTRIRLATEMMseeDGYLAESinkdIEECnaiIEQFIDYLRTgqempmEMADLNALLGEVIA---AESG---- 309
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2387 nRE-EIDLHefcldvieeakisateahkliFNFTLKKIHYRldPKLMKFILLNLLSNAIKYSpkGGKIELTIKQLRGKMV 2465
Cdd:PRK09467   310 -YErEIETA---------------------LQPGPIEVPMN--PIAIKRALANLVVNAARYG--NGWIKVSSGTEGKRAW 363
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1085344563 2466 ISVKDKGIGIPTDDLKHLFEPFHR---AKNTtdiSGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:PRK09467   364 FQVEDDGPGIPPEQLKHLFQPFTRgdsARGS---SGTGLGLAIVKRIVDQHNGKVELGNSEEGGLSARAWLPLTT 435
PRK10549 PRK10549
two-component system sensor histidine kinase BaeS;
2301-2536 1.33e-20

two-component system sensor histidine kinase BaeS;


Pssm-ID: 182539 [Multi-domain]  Cd Length: 466  Bit Score: 97.78  E-value: 1.33e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2301 LQHSLEKEKELselKSRFISTTSHEFRTPLTTVRVSAEMIQRYRKRWTEDKLDVFLDKIKNsvdyLTKLLDDVLTISRSE 2380
Cdd:PRK10549   229 LASTLEKNEQM---RRDFMADISHELRTPLAVLRGELEAIQDGVRKFTPESVASLQAEVGT----LTKLVDDLHQLSLSD 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2381 SGKIVLNREEIDLhefcLDVIEEAKISATE--AHKLIfnftlkKIHYRLDPKLMKF--------ILLNLLSNAIKYSPKG 2450
Cdd:PRK10549   302 EGALAYRKTPVDL----VPLLEVAGGAFRErfASRGL------TLQLSLPDSATVFgdpdrlmqLFNNLLENSLRYTDSG 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2451 GKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDIS--GTGLGLSIVKRAVDLHNGIITVKSELNAGTT 2528
Cdd:PRK10549   372 GSLHISAEQRDKTLRLTFADSAPGVSDEQLQKLFERFYRTEGSRNRAsgGSGLGLAICLNIVEAHNGRIIAAHSPFGGVS 451

                   ....*...
gi 1085344563 2529 FTVKIPLE 2536
Cdd:PRK10549   452 ITVELPLE 459
GAF COG2203
GAF domain [Signal transduction mechanisms];
180-558 1.88e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 99.11  E-value: 1.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  180 RAYNQLEEENNLRKEAEKELRTINDELEDRVEERTIELHHANVQLEDELAVRQRAESQIRKLNRIYAVLSNINQAIVRIR 259
Cdd:COG2203    127 ARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSAL 206
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  260 NTKEVFDEACRIATEYGKFTMVWIGIINAKNNKVDVAASSGVESSYLDNLvidlndvQRSSGPTGIAIRTGKHKISNNII 339
Cdd:COG2203    207 DLEELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGRL-------PLGEGLAGRALRTGEPVVVNDAS 279
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  340 DDDSML-LWKNEAIQYGYKSTASFPLIVFGKVVGAFCIYSDELNFFEDDDVVLLDEMVKDISFAMEFIESEAERRDAENA 418
Cdd:COG2203    280 TDPRFApSLRELLLALGIRSLLCVPLLVDGRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAA 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  419 LylsEERFRRLAENAPDVIYRMSLADGKYEYISPAALTIFGYSPDDYYDNPLLFKQSIHSDWIKYFEEHWANLQKGILPQ 498
Cdd:COG2203    360 L---LQELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRI 436
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  499 TYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQALQKAAEEIRDL 558
Cdd:COG2203    437 LLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLA 496
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
1111-1233 2.21e-20

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: 88.89  E-value: 2.21e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1111 SETKLRIMFENSRDALGV-SKKGVHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIPSFYET 1189
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIViDLEGNILYVNPAFEEIFGYSA-EELIGRNVLELIPEEDREEVRERIERRLEGEPEPVSEER 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1085344563 1190 RGRKRDGSEFDFEINISTYELNGEI-YTLANIRDITSRKLLEKSL 1233
Cdd:TIGR00229   80 RVRRKDGSEIWVEVSVSPIRTNGGElGVVGIVRDITERKEAEEAL 124
PRK10490 PRK10490
sensor protein KdpD; Provisional
2204-2536 2.77e-20

sensor protein KdpD; Provisional


Pssm-ID: 236701 [Multi-domain]  Cd Length: 895  Bit Score: 98.95  E-value: 2.77e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2204 LPLKNeNSQVFGVILIYSTN-RNVITQDEIRLIEELAndlafgiiTLQTRAerkrvekeleLHRDHLqelvnVRTEELDK 2282
Cdd:PRK10490   600 LPLKS-AQKTYGLLAVEPGNlRQLMIPEQQRLLETFT--------LLIANA----------LERLTL-----TASEEQAR 655
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2283 vnkkliiefekekefermlqhsLEKEKElsELKSRFISTTSHEFRTPLTTVRVSAEMIQryrkrwtedkLDVFLD----- 2357
Cdd:PRK10490   656 ----------------------LASERE--QLRNALLAALSHDLRTPLTVLFGQAEILT----------LDLASEgspha 701
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2358 ----KIKNSVDYLTKLLDDVLTISRSESGKIVLNREEIDLHEF---CLDVIEEAKISATEAHKLIFNFTLkkIHyrLDPK 2430
Cdd:PRK10490   702 rqasEIRQQVLNTTRLVNNLLDMARIQSGGFNLRKEWLTLEEVvgsALQMLEPGLSGHPINLSLPEPLTL--IH--VDGP 777
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2431 LMKFILLNLLSNAIKYSpkGGKIELTIK------QLRgkmvISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLS 2504
Cdd:PRK10490   778 LFERVLINLLENAVKYA--GAQAEIGIDahvegeRLQ----LDVWDNGPGIPPGQEQLIFDKFARGNKESAIPGVGLGLA 851
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1085344563 2505 IVKRAVDLHNGIITVKSELNAGTTFTVKIPLE 2536
Cdd:PRK10490   852 ICRAIVEVHGGTIWAENRPEGGACFRVTLPLE 883
GAF COG2203
GAF domain [Signal transduction mechanisms];
1895-2280 3.84e-20

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 97.96  E-value: 3.84e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1895 ALNERIKHSQSLLRLSKNLEFAQTYSQALTAALNEIKNILGYKTVWVYLLSEDKKYFNALVARGDFEDIVMSPEGTLILP 1974
Cdd:COG2203      1 LLSVLALALAREVAAAELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1975 IEGDRMLEEIAEAKEIVIVEDARADERTNKKIVETLGNRTIINVPIYLLDKHLGTVGTGTFSDEGVRIPTRSEKEFLLAM 2054
Cdd:COG2203     81 IDALVLLSLVATAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2055 ASHLAVTLDRLHLLVERQEAEKALLRLN-RELKAISNCNQSLLRAEDEQSLLNEICRIICEEAGYDFAWVGYTEHsDANT 2133
Cdd:COG2203    161 TDLVGQLAALAGLILDIARLLTQRARLElERLALLNEISQALRSALDLEELLQRILELAGELLGADRGAILLVDE-DGGE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2134 IHPVAWAGIDIDLKAKEKFDWSeeiecglrPAQKVIQTGDIIYVQDFSSDASLESWCQKAL-QRGYRSGMALPLKNENsQ 2212
Cdd:COG2203    240 LELVAAPGLPEEELGRLPLGEG--------LAGRALRTGEPVVVNDASTDPRFAPSLRELLlALGIRSLLCVPLLVDG-R 310
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 2213 VFGVILIYSTNRNVITQDEIRLIEELANDLAFGIITLQTRAERKRVEKELELHRDHLQELVNVRTEEL 2280
Cdd:COG2203    311 LIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLRLLLDLELTLL 378
HATPase_CpxA-like cd16949
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2438-2535 1.62e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CpxA; This family includes the histidine kinase-like ATPase (HATPase) domains of two-component sensor histidine kinase (HKs) similar to Escherichia coli CpxA, HK of the CpxA-CpxR two-component regulatory system (TCS) which may function in acid stress and in cell wall stability. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a CpxA family periplasmic domain.


Pssm-ID: 340425 [Multi-domain]  Cd Length: 104  Bit Score: 85.84  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2438 NLLSNAIKYSPkgGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDIS--GTGLGLSIVKRAVDLHNG 2515
Cdd:cd16949      7 NVLRNALRYSP--SKILLDISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSARDREsgGTGLGLAIAERAIEQHGG 84
                           90       100
                   ....*....|....*....|
gi 1085344563 2516 IITVKSELNAGTTFTVKIPL 2535
Cdd:cd16949     85 KIKASNRKPGGLRVRIWLPA 104
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
553-801 1.71e-19

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: 94.80  E-value: 1.71e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  553 EEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKMkFTDIITPKSLKTFNENFPGFKEKGWIKNLEFELi 632
Cdd:COG5805     34 EELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKT-IFDFLEKEYHYRVKTRIERLQKGYDVVMIEQIY- 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  633 RKDGSILPILASATAIkdSDGNYLMSRSTVNDIAELKLAELQLRNSEREFRTLAENLPDHIIRYDIDCRVIYLNHVVAA- 711
Cdd:COG5805    112 CKDGELIYVEVKLFPI--YNQNGQAAILALRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERl 189
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  712 TNYTNSSLVGKLSAEiqFNEAKGLEEYNEKLRRVIKTGTEDEMEIMLRDIEGNLHIHEVHFLAERDIEGKIVGALAIGHD 791
Cdd:COG5805    190 FGAPREELIGKNLLE--LLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRD 267
                          250
                   ....*....|
gi 1085344563  792 ISERKQAEEE 801
Cdd:COG5805    268 ITEKKEAEEL 277
HATPase_FilI-like cd16921
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2435-2534 2.74e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Methanosaeta harundinacea FilI and some hybrid sensor histidine kinases; This family includes FilI, the histidine kinase (HK) component of FilI-FilRs, a two-component signal transduction system (TCS) of the methanogenic archaeon, Methanosaeta harundinacea, which is involved in regulating methanogenesis. The cytoplasmic HK core consists of a C-terminal HK-like ATPase domain (represented here) and a histidine kinase dimerization and phosphoacceptor domain (HisKA) domain, which, in FilI, are coupled to CHASE, HAMP, PAS, and GAF sensor domains. FilI-FilRs catalyzes the phosphotransfer between FilI (HK) and FilRs (FilR1 and FilR2, response regulators) of the TCS. TCSs are predicted to be of bacterial origin, and acquired by archaea by horizontal gene transfer. This model also includes related HATPase domains such as that of Synechocystis sp. PCC6803 phytochrome-like protein Cph1. Proteins having this HATPase domain and HisKA domain also have accessory sensor domains such as CHASE, GAF, HAMP and PAS; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340398 [Multi-domain]  Cd Length: 105  Bit Score: 85.07  E-value: 2.74e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKYSPKG--GKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDL 2512
Cdd:cd16921      4 VLTNLLGNAIKFRRPRrpPRIEVGAEDVGEEWTFYVRDNGIGIDPEYAEKVFGIFQRLHSREEYEGTGVGLAIVRKIIER 83
                           90       100
                   ....*....|....*....|..
gi 1085344563 2513 HNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16921     84 HGGRIWLESEPGEGTTFYFTLP 105
HATPase_AtoS-like cd16943
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2429-2535 3.18e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 AtoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli AtoS, an HK of the AtoS-AtoC TCS. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have accessory domains such as HAMP or PAS sensor domains or CBS-pair domains.


Pssm-ID: 340419 [Multi-domain]  Cd Length: 105  Bit Score: 84.78  E-value: 3.18e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2429 PKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDisGTGLGLSIVKR 2508
Cdd:cd16943      1 PSQLNQVLLNLLVNAAQAMEGRGRITIRTWAHVDQVLIEVEDTGSGIDPEILGRIFDPFFTTKPVGE--GTGLGLSLSYR 78
                           90       100
                   ....*....|....*....|....*..
gi 1085344563 2509 AVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:cd16943     79 IIQKHGGTIRVASVPGGGTRFTIILPI 105
marine_sort_HK TIGR03785
proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is ...
2318-2534 3.58e-19

proteobacterial dedicated sortase system histidine kinase; This histidine kinase protein is paired with an adjacent response regulator (TIGR03787) gene. It co-occurs with a variant sortase enzyme (TIGR03784), usually in the same gene neighborhood, in proteobacterial species most of which are marine, and with an LPXTG motif-containing sortase target conserved protein (TIGR03788). Sortases and LPXTG proteins are far more common in Gram-positive bacteria, where sortase systems mediate attachment to the cell wall or cross-linking of pilin structures. We give this predicted sensor histidine kinase the gene symbol psdS, for Proteobacterial Dedicated Sortase system Sensor histidine kinase.


Pssm-ID: 163497 [Multi-domain]  Cd Length: 703  Bit Score: 94.81  E-value: 3.58e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2318 FISTTSHEFRTPLTTVRVSAEMIQRYRkrwTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSESGKIVLNREEIDLHEfc 2397
Cdd:TIGR03785  488 MSSRLSHELRTPVAVVRSSLENLELQA---LEQEKQKYLERAREGTERLSMILNNMSEATRLEQAIQSAEVEDFDLSE-- 562
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2398 ldVIEEAKIS---ATEAHKLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIG 2474
Cdd:TIGR03785  563 --VLSGCMQGyqmTYPPQRFELNIPETPLVMRGSPELIAQMLDKLVDNAREFSPEDGLIEVGLSQNKSHALLTVSNEGPP 640
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085344563 2475 IPTDDLKHLFEPF--HRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSEL-NAGTTFTVKIP 2534
Cdd:TIGR03785  641 LPEDMGEQLFDSMvsVRDQGAQDQPHLGLGLYIVRLIADFHQGRIQAENRQqNDGVVFRISLP 703
HATPase_EnvZ-like cd16950
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2432-2534 4.47e-19

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli EnvZ and Pseudomonas aeruginosa BfmS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli EnvZ of the EnvZ-OmpR two-component regulatory system (TCS), which functions in osmoregulation. It also contains the HATPase domain of Pseudomonas aeruginosa BfmS, the HK of the BfmSR TCS, which functions in the regulation of the rhl quorum-sensing system and bacterial virulence in P. aeruginosa. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also contain a periplasmic domain.


Pssm-ID: 340426 [Multi-domain]  Cd Length: 101  Bit Score: 84.42  E-value: 4.47e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2432 MKFILLNLLSNAIKYSpkGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVD 2511
Cdd:cd16950      1 LKRVLSNLVDNALRYG--GGWVEVSSDGEGNRTRIQVLDNGPGIAPEEVDELFQPFYRGDNARGTSGTGLGLAIVQRISD 78
                           90       100
                   ....*....|....*....|...
gi 1085344563 2512 LHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16950     79 AHGGSLTLANRAGGGLCARIELP 101
PAS COG2202
PAS domain [Signal transduction mechanisms];
411-548 4.53e-19

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 89.31  E-value: 4.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  411 ERRDAENALYLSEERFRRLAENAPDVIYRMSLaDGKYEYISPAALTIFGYSPDDYYDNPLLfkQSIHSDWIKYFEEHWAN 490
Cdd:COG2202    124 ERKRAEEALRESEERLRLLVENAPDGIFVLDL-DGRILYVNPAAEELLGYSPEELLGKSLL--DLLHPEDRERLLELLRR 200
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563  491 -LQKGILPQTYEYQIIHKSGEARWLNqRNILVLDEGGNSVAIEGVVTDITERKQAEQAL 548
Cdd:COG2202    201 lLEGGRESYELELRLKDGDGRWVWVE-ASAVPLRDGGEVIGVLGIVRDITERKRAEEAL 258
PRK10604 PRK10604
sensor protein RstB; Provisional
2315-2535 5.10e-19

sensor protein RstB; Provisional


Pssm-ID: 236724 [Multi-domain]  Cd Length: 433  Bit Score: 92.36  E-value: 5.10e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2315 KSRFISTTSHEFRTPLttVRVsaemiqRYRKRWTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSESGKIVLNREEIDLH 2394
Cdd:PRK10604   212 KKQLIDGIAHELRTPL--VRL------RYRLEMSDNLSAAESQALNRDIGQLEALIEELLTYARLDRPQNELHLSEPDLP 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2395 EFCLDVIEEakISATEAHKLIFNFTLKKIHY-RLDPKLMKFILLNLLSNAIKYSpkGGKIELTIKQLRGKMVISVKDKGI 2473
Cdd:PRK10604   284 AWLSTHLAD--IQAVTPEKTVRLDTPHQGDYgALDMRLMERVLDNLLNNALRYA--HSRVRVSLLLDGNQACLIVEDDGP 359
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085344563 2474 GIPTDDLKHLFEPFHRAKNTTDIS--GTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:PRK10604   360 GIPPEERERVFEPFVRLDPSRDRAtgGCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWPV 423
PRK09835 PRK09835
Cu(+)/Ag(+) sensor histidine kinase;
2303-2534 9.56e-19

Cu(+)/Ag(+) sensor histidine kinase;


Pssm-ID: 182101 [Multi-domain]  Cd Length: 482  Bit Score: 92.14  E-value: 9.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2303 HSLEKEKELSELKSRFISTTSHEFRTPLTTVRVSAEMI--QRYRKRWTEDKLDVFLDKIKNsvdyLTKLLDDVLTISRSE 2380
Cdd:PRK09835   250 HMIERIEDVFTRQSNFSADIAHEIRTPITNLITQTEIAlsQSRSQKELEDVLYSNLEELTR----MAKMVSDMLFLAQAD 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2381 SGKIVLNREEIDLHEFCLDVIEEAKISATEAHkLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGGKIELTIKQL 2460
Cdd:PRK09835   326 NNQLIPEKKMLDLADEVGKVFDFFEAWAEERG-VELRFVGDPCQVAGDPLMLRRAISNLLSNALRYTPAGEAITVRCQEV 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2461 RGKMVISVKDKGIGIPTDDLKHLFEPFHRakntTDIS------GTGLGLSIVKRAVDLHNGIITVKSELNAgTTFTVKIP 2534
Cdd:PRK09835   405 DHQVQLVVENPGTPIAPEHLPRLFDRFYR----VDPSrqrkgeGSGIGLAIVKSIVVAHKGTVAVTSDARG-TRFVISLP 479
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
1394-1646 1.28e-18

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: 92.10  E-value: 1.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1394 EFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIrelnPDGSFESYAQAVDN---ALASGENSELEILV 1470
Cdd:COG5805     35 ELETILENLPDAIIAVNREGKVIYINPAMEKLLGYTSEEIIGKTI----FDFLEKEYHYRVKTrieRLQKGYDVVMIEQI 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1471 PNPNNEQIVHQIRIIAERDeQNKVTSVLAIgRDITERKRAEETIKKSEAQLNEAQRIAQIGSWELDIANNILRWSDEIFR 1550
Cdd:COG5805    111 YCKDGELIYVEVKLFPIYN-QNGQAAILAL-RDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIER 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1551 IFEIDPKEF-GSSyeaFLNAIHPDDREVVNTAYSNSLVNRTPYAIDHRLRFDDGRIKFVHEQCETIYNEENKPLRSIGTV 1629
Cdd:COG5805    189 LFGAPREELiGKN---LLELLHPCDKEEFKERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVIL 265
                          250
                   ....*....|....*..
gi 1085344563 1630 QDITDRKLAEEALKESE 1646
Cdd:COG5805    266 RDITEKKEAEELMARSE 282
CitA COG3290
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ...
2299-2536 1.95e-18

Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];


Pssm-ID: 442519 [Multi-domain]  Cd Length: 389  Bit Score: 90.29  E-value: 1.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2299 RMLQHSLEKEKELSELksrfISTTSHEFRTPLTTVrvsAEMIQryrkrwtedkldvfLDKIKNSVDYLTKLLDDVLTISR 2378
Cdd:COG3290    177 ERLEEELEGVKELAEA----LRAQRHDFRNHLHTI---SGLLQ--------------LGEYDEALEYIDEISEELQELID 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2379 SESGKIvlnreeidlHEFCLDVIEEAKISATEAHKLIFNFTlkkIHYRLDPKLMKF-----ILLNLLSNAI----KYSPK 2449
Cdd:COG3290    236 SLLSRI---------GNPVLAALLLGKAARARERGIDLTID---IDSDLPDLPLSDtdlvtILGNLLDNAIeaveKLPEE 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2450 GGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPfhraKNTTDIS-GTGLGLSIVKRAVDLHNGIITVKSELNAGTT 2528
Cdd:COG3290    304 ERRVELSIRDDGDELVIEVEDSGPGIPEELLEKIFER----GFSTKLGeGRGLGLALVKQIVEKYGGTIEVESEEGEGTV 379

                   ....*...
gi 1085344563 2529 FTVKIPLE 2536
Cdd:COG3290    380 FTVRLPKE 387
PRK10755 PRK10755
two-component system sensor histidine kinase PmrB;
2301-2515 5.65e-18

two-component system sensor histidine kinase PmrB;


Pssm-ID: 236751 [Multi-domain]  Cd Length: 356  Bit Score: 88.10  E-value: 5.65e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2301 LQHSLEKEKElselksrFISTTSHEFRTPLTTVRVSAEMIQRyrkrwtEDKLDVflDKIKNSVDYLTKLLDDVLTISRSE 2380
Cdd:PRK10755   130 LTSTLDQERL-------FTADVAHELRTPLAGIRLHLELLEK------QHHIDV--APLIARLDQMMHTVEQLLQLARAG 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2381 ----SGkivlNREEIDLHEfclDVI-----EEAKISATEAHKLIFNFTLKKIHYRLDPKLMKFILLNLLSNAIKYSPKGG 2451
Cdd:PRK10755   195 qsfsSG----HYQTVKLLE---DVIlpsqdELSEMLEQRQQTLLLPESAADITVQGDATLLRLLLRNLVENAHRYSPEGS 267
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085344563 2452 KIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKntTDISGTGLGLSIVKRAVDLHNG 2515
Cdd:PRK10755   268 TITIKLSQEDGGAVLAVEDEGPGIDESKCGELSKAFVRMD--SRYGGIGLGLSIVSRITQLHHG 329
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1541-1629 7.78e-18

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: 80.46  E-value: 7.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1541 ILRWSDEIFRIFEIDPKEFGSSYEAFLNAIHPDDREVVNTAYSNSLVNRTPYAIDHRLRFDDGRIKFVHEQCETIYNEEN 1620
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                   ....*....
gi 1085344563 1621 KPLRSIGTV 1629
Cdd:pfam08447   81 KPVRVIGVA 89
HATPase_EcPhoR-like cd16952
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2438-2534 9.75e-18

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoR; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli or Vibrio cholera PhoR, the histidine kinase (HK) of PhoB-PhoR a two-component signal transduction system (TCS) involved in phosphate regulation. PhoR monitors extracellular inorganic phosphate (Pi) availability and PhoB, the response regulator, regulates transcription of genes of the phosphate regulon. PhoR is a bifunctional histidine autokinase/phospho-PhoB phosphatase; in phosphate deficiency, it autophosphorylates and Pi is transferred to PhoB, and when environmental Pi is abundant, it removes the phosphoryl group from phosphorylated PhoB. Other roles of PhoB-PhoR TCS have been described, including motility, biofilm formation, intestinal colonization, and virulence in V. cholera. E.coli PhoR and Bacillus subtilis PhoR (whose HATPase domain belongs to a different family) sense very different signals in each bacterium. In E. coli the PhoR signal comes from phosphate transport mediated by the PstSCAB2 phosphate transporter and the PhoU chaperone-like protein while in B. subtilis, the PhoR activation signal comes from wall teichoic acid (WTA) metabolism.


Pssm-ID: 340428 [Multi-domain]  Cd Length: 108  Bit Score: 80.71  E-value: 9.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2438 NLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHR-----AKNTtdiSGTGLGLSIVKRAVDL 2512
Cdd:cd16952      7 NLVSNAVKYTPPSDTITVRWSQEESGARLSVEDTGPGIPPEHIPRLTERFYRvdierCRNT---GGTGLGLAIVKHVMSR 83
                           90       100
                   ....*....|....*....|..
gi 1085344563 2513 HNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16952     84 HDARLLIASELGKGSRFTCLFP 105
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
1775-1935 1.56e-17

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 86.82  E-value: 1.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1775 ALKLSEERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQfEKLRSGKTALA- 1853
Cdd:COG3852      1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDSPLRELLE-RALAEGQPVTEr 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1854 ERNLIRNDGSLLPVEISGIMLPDK----RFLGIVRDITERKKNEAALNERIKHsQSLLRLSKNLefAqtysqaltaalNE 1929
Cdd:COG3852     80 EVTLRRKDGEERPVDVSVSPLRDAegegGVLLVLRDITERKRLERELRRAEKL-AAVGELAAGL--A-----------HE 145

                   ....*.
gi 1085344563 1930 IKNILG 1935
Cdd:COG3852    146 IRNPLT 151
PRK11466 PRK11466
hybrid sensory histidine kinase TorS; Provisional
2253-2535 2.71e-17

hybrid sensory histidine kinase TorS; Provisional


Pssm-ID: 236914 [Multi-domain]  Cd Length: 914  Bit Score: 89.19  E-value: 2.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2253 AERKRVEKeLELHRDHLQELVNVRTEELDKVnkkliiefekekeferMLQHS---LEKEKElSELKSRFISTTSHEFRTP 2329
Cdd:PRK11466   397 AFRSNVHA-LNRHREQLAAQVKARTAELQEL----------------VIEHRqarAEAEKA-SQAKSAFLAAMSHEIRTP 458
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2330 LTTVRVSAEMI--QRYRKRWTEDkldvfLDKIKNSVDYLTKLLDDVLTISRSESG--KIVLNREEIdlhefcldvieeak 2405
Cdd:PRK11466   459 LYGILGTAQLLadNPALNAQRDD-----LRAITDSGESLLTILNDILDYSAIEAGgkNVSVSDEPF-------------- 519
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2406 isateAHKLIFNFTLKKIHYRL---------------------DPKLMKFILLNLLSNAIKYSPKGgKIELTIKQLRGKM 2464
Cdd:PRK11466   520 -----EPRPLLESTLQLMSGRVkgrpirlatdiaddlptalmgDPRRIRQVITNLLSNALRFTDEG-SIVLRSRTDGEQW 593
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085344563 2465 VISVKDKGIGIPTDDLKHLFEPFHRAknTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:PRK11466   594 LVEVEDSGCGIDPAKLAEIFQPFVQV--SGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPL 662
PRK09959 PRK09959
acid-sensing system histidine kinase EvgS;
2299-2536 3.25e-17

acid-sensing system histidine kinase EvgS;


Pssm-ID: 182169 [Multi-domain]  Cd Length: 1197  Bit Score: 89.02  E-value: 3.25e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2299 RMLQHSLEKEKE----LSELKSRFISTTSHEFRTPLTTVRVSAEMIQRyrKRWTEDKLDVFLDKIKNSVDYLTKLLDDVL 2374
Cdd:PRK09959   692 RDLIHALEVERNkainATVAKSQFLATMSHEIRTPISSIMGFLELLSG--SGLSKEQRVEAISLAYATGQSLLGLIGEIL 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2375 TISRSESGKIVLNREEIDLHEFCLDVIEE-AKISATEAHKLIFNFTLKKiHY--RLDPKLMKFILLNLLSNAIKYSPKGG 2451
Cdd:PRK09959   770 DVDKIESGNYQLQPQWVDIPTLVQNTCHSfGAIAASKSIALSCSSTFPD-HYlvKIDPQAFKQVLSNLLSNALKFTTEGA 848
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2452 -KIELTIKQLRGKMVI---SVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGT 2527
Cdd:PRK09959   849 vKITTSLGHIDDNHAVikmTIMDSGSGLSQEEQQQLFKRYSQTSAGRQQTGSGLGLMICKELIKNMQGDLSLESHPGIGT 928

                   ....*....
gi 1085344563 2528 TFTVKIPLE 2536
Cdd:PRK09959   929 TFTITIPVE 937
HATPase_TmoS-FixL-DctS-like cd16920
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2435-2534 9.64e-17

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhizobium meliloti FixL, and Rhodobacter capsulatus DctS; includes hybrid sensor histidine kinase similar to Pseudomonas mendocina TmoS; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs), such as Pseudomonas mendocina TmoS HK of the TmoS-TmoT TCS, which controls the expression of the toluene-4-monooxygenase pathway, Rhizobium meliloti FixL HK of the FixL-FixJ TCS, which regulates the expression of the genes related to nitrogen fixation in the root nodule in response to O(2) levels, and Rhodobacter capsulatus DctS of the DctS-DctR TCS, which controls synthesis of the high-affinity C4-dicarboxylate transport system. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and PAS sensor domain(s); many are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340397 [Multi-domain]  Cd Length: 104  Bit Score: 77.82  E-value: 9.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKYSPKGG--KIELTIKQLR---GKMVISVKDKGIGIPTDDLKHLFEPFHraknTTDISGTGLGLSIVKRA 2509
Cdd:cd16920      4 VLINLVRNGIEAMSEGGceRRELTIRTSPaddRAVTISVKDTGPGIAEEVAGQLFDPFY----TTKSEGLGMGLSICRSI 79
                           90       100
                   ....*....|....*....|....*
gi 1085344563 2510 VDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16920     80 IEAHGGRLSVESPAGGGATFQFTLP 104
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
259-404 1.01e-16

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 79.05  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  259 RNTKEVFDEACRIATEYGKFTMVWIGIINAKNNKVdvaassgvESSYLDNLVIDLNDVQRSSGPTGIAIRTGKHKISNNI 338
Cdd:pfam13185    2 ADLEELLDAVLEAAVELGASAVGFILLVDDDGRLA--------AWGGAADELSAALDDPPGEGLVGEALRTGRPVIVNDL 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563  339 IDDDSMLLWknEAIQYGYKSTASFPLIVFGKVVGAFCIYSDELNFFEDDDVVLLDEMVKDISFAME 404
Cdd:pfam13185   74 AADPAKKGL--PAGHAGLRSFLSVPLVSGGRVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAIE 137
PAS COG2202
PAS domain [Signal transduction mechanisms];
671-837 1.80e-16

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 81.61  E-value: 1.80e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  671 AELQLRNSEREFRTLAENLPDHIIRYDIDCRVIYLNHVVAA-TNYTNSSLVGKLSAEIQFNEAkgLEEYNEKLRRVIKTG 749
Cdd:COG2202      2 AEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERlTGYSAEELLGKTLRDLLPPED--DDEFLELLRAALAGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  750 TEDEMEIMLRDIEGNLHIHEVHFLAERDIEGKIVGALAIGHDISERKQAEEERQANLRFFenmdrinRAIQEANNVEQMM 829
Cdd:COG2202     80 GVWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERL-------RLLVENAPDGIFV 152

                   ....*...
gi 1085344563  830 SDVLDIIL 837
Cdd:COG2202    153 LDLDGRIL 160
HATPase_VanS-like cd16923
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2438-2534 2.33e-16

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Enterococcus faecium VanS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Enterococcus faecium VanS HK of the VanS-VanR two-component regulatory system (TCS) which activates the transcription of vanH, vanA and vanX vancomycin resistance genes. It also contains Ecoli YedV and PcoS, probable members of YedW-YedV TCS and PcoS-PcoR TCS, repectively. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); most also have a HAMP sensor domain.


Pssm-ID: 340400 [Multi-domain]  Cd Length: 102  Bit Score: 76.66  E-value: 2.33e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2438 NLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISGTGLGLSIVKRAVDLHNGII 2517
Cdd:cd16923      7 NLLSNAIKYSPENTRIYITSFLTDDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNSRNTEGAGLGLSIAKAIIELHGGSA 86
                           90
                   ....*....|....*..
gi 1085344563 2518 TVKSElNAGTTFTVKIP 2534
Cdd:cd16923     87 SAEYD-DNHDLFKVRLP 102
PRK13560 PRK13560
hypothetical protein; Provisional
1551-1896 2.69e-16

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 85.49  E-value: 2.69e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1551 IFEIDPKEFGSSYEAFLNAIHPDDREVVNTAysnslVNRTPYAIDHRLRFDDGRIKFVHEQC------ETIYNEENKPLR 1624
Cdd:PRK13560   104 LAAIAKHDLMADKGLLAMLIGGDDGDFFFAN-----PFRSAETIAMALQSDDWQEEEGHFRCgdgrfiDCCLRFERHAHA 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1625 SI---GTVQDITDRKLAEEALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKA--IDPAwhf 1699
Cdd:PRK13560   179 DDqvdGFAEDITERKRAEERIDEALHFLQQLLDNIADPAFWKDEDAKVFGCNDAACLACGFRREEIIGMSIhdFAPA--- 255
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1700 YREDgtvlpleeypvNYVLATRKELRNYVVGVHRTNYKN------DVWVLVNADPVWSNENELTQVIVTFSDITMRKNAE 1773
Cdd:PRK13560   256 QPAD-----------DYQEADAAKFDADGSQIIEAEFQNkdgrtrPVDVIFNHAEFDDKENHCAGLVGAITDISGRRAAE 324
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1774 VALKLSEERYRTLVEQAMDGIFIADSNGNYIDVNRSGC-NMLGYTRDQLLKLRMQDLIPAEEQQ------------TTPI 1840
Cdd:PRK13560   325 RELLEKEDMLRAIIEAAPIAAIGLDADGNICFVNNNAAeRMLGWSAAEVMGKPLPGMDPELNEEfwcgdfqewypdGRPM 404
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 1841 QFE------KLRSGKTALAERNLI-RNDGSLLPVEI--SGIMLPDKRFLG---IVRDITERKKNEAAL 1896
Cdd:PRK13560   405 AFDacpmakTIKGGKIFDGQEVLIeREDDGPADCSAyaEPLHDADGNIIGaiaLLVDITERKQVEEQL 472
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
1388-1646 3.31e-16

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: 84.26  E-value: 3.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1388 LRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDgSFESYAQAVDNALASGEN-SEL 1466
Cdd:COG5809     10 LRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHP-DDEKELREILKLLKEGESrDEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1467 EILVPNPNNEQIVHQIRIIAERDEQNKVTSVLAIGRDITERKRAEETIKKSEAQLneaqRIAqigsweLDIANNILRWSD 1546
Cdd:COG5809     89 EFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKF----RLI------FNHSPDGIIVTD 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1547 EIFRIFEIDP---KEFGSSYEAFLNA-----IHPDDREVVNTAYSNSLVNRTPYAIDHRLRFDDGRIKFVHEQCETIyNE 1618
Cdd:COG5809    159 LDGRIIYANPaacKLLGISIEELIGKsilelIHSDDQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAPI-KK 237
                          250       260
                   ....*....|....*....|....*...
gi 1085344563 1619 ENKPLRSIGTVQDITDRKLAEEALKESE 1646
Cdd:COG5809    238 NGEVDGIVIIFRDITERKKLEELLRKSE 265
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
1294-1518 5.85e-16

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: 83.63  E-value: 5.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1294 YALKGTPCENVMGRQLC-FYPKEVQKLFPDDKLLLEMGVDSYMGIPLWDSFGKPIGLIALMSSKSHPEDSIAIqvlqlVA 1372
Cdd:COG5805     64 EKLLGYTSEEIIGKTIFdFLEKEYHYRVKTRIERLQKGYDVVMIEQIYCKDGELIYVEVKLFPIYNQNGQAAI-----LA 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1373 TRAAAELERDRSdrILRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQ 1452
Cdd:COG5805    139 LRDITKKKKIEE--ILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFKE 216
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 1453 AVDNALASGENSELEILVPNPNNEQIVHQIRIIAERDEQNKVTSVLAIGRDITERKRAEETIKKSE 1518
Cdd:COG5805    217 RIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMARSE 282
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1003-1093 7.86e-16

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: 74.68  E-value: 7.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1003 KIILSDESCRIFGLQQEnyhkELDEWHKQWLQLILPEDKERAEKTAIDAVQKDIPYNLDYRIIRHNGELRYIHSEANVRR 1082
Cdd:pfam08447    1 IIYWSPRFEEILGYTPE----ELLGKGESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIR 76
                           90
                   ....*....|.
gi 1085344563 1083 DSSGKPIFMLG 1093
Cdd:pfam08447   77 DENGKPVRVIG 87
PRK13560 PRK13560
hypothetical protein; Provisional
405-806 1.50e-15

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 83.18  E-value: 1.50e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  405 FIESEAERRDAENALYLSEERFRRLAENAPDVIYRMSlADGKYEYISPAALTIFGYSPDDyydnplLFKQSIH----SDW 480
Cdd:PRK13560   185 FAEDITERKRAEERIDEALHFLQQLLDNIADPAFWKD-EDAKVFGCNDAACLACGFRREE------IIGMSIHdfapAQP 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  481 IK-YFEEHWANLQ-KGIlpQTYEYQIIHKSGEARWLNQR-NILVLDEGGNSVA-IEGVVTDITERKQAEQALQKAAEEIR 556
Cdd:PRK13560   258 ADdYQEADAAKFDaDGS--QIIEAEFQNKDGRTRPVDVIfNHAEFDDKENHCAgLVGAITDISGRRAAERELLEKEDMLR 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  557 DLYNNAPCGYHSLDKEGTFVRINNTEL-KWLGYTLEEVIGK-MKFTDIITPKSL--KTFNENFPGFKEKGW--------- 623
Cdd:PRK13560   336 AIIEAAPIAAIGLDADGNICFVNNNAAeRMLGWSAAEVMGKpLPGMDPELNEEFwcGDFQEWYPDGRPMAFdacpmakti 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  624 -----IKNLEFELIRKDGSILPILASATAIKDSDGNYLMSRSTVNDIAELKLAELQLRNSErefrTLAENLPDHIIRYDI 698
Cdd:PRK13560   416 kggkiFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLAN----LIVENSPLVLFRWKA 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  699 D--CRVIYLNHVVAATNYTNSSLVG---------------KLSAEIQFNEAKGLEEYNEKLRRVIKTGtedemEIMLRDI 761
Cdd:PRK13560   492 EegWPVELVSKNITQFGYEPDEFISgkrmfaaiihpadleQVAAEVAEFAAQGVDRFEQEYRILGKGG-----AVCWIDD 566
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1085344563  762 EGNlhihevhflAERDIEGKIVGALAIGHDISERKQAEEERQANL 806
Cdd:PRK13560   567 QSA---------AERDEEGQISHFEGIVIDISERKHAEEKIKAAL 602
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
1388-1520 1.81e-15

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 80.66  E-value: 1.81e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1388 LRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSfeSYAQAVDNALASGENS-EL 1466
Cdd:COG3852      2 LRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGRPLAELFPEDS--PLRELLERALAEGQPVtER 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1085344563 1467 EILVPNPNNEQIVHQIRIIAERDEQNKvTSVLAIGRDITERKRAEETIKKSEAQ 1520
Cdd:COG3852     80 EVTLRRKDGEERPVDVSVSPLRDAEGE-GGVLLVLRDITERKRLERELRRAEKL 132
HATPase_RstB-like cd16939
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2432-2535 2.47e-15

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Salmonella typhimurium RstB; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Salmonella typhimurium RstB HK of the RstA-RstB two-component regulatory system (TCS), which regulates expression of the constituents participating in pyrimidine metabolism and iron acquisition, and may be required for regulation of Salmonella motility and invasion. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensor domain.


Pssm-ID: 340416 [Multi-domain]  Cd Length: 104  Bit Score: 74.00  E-value: 2.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2432 MKFILLNLLSNAIKYSPKGGKIELTIKQlrGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDIS--GTGLGLSIVKRA 2509
Cdd:cd16939      1 MARALDNLLRNALRYAHRTVRIALLVSG--GRLTLIVEDDGPGIPAAARERVFEPFVRLDPSRDRAtgGFGLGLAIVHRV 78
                           90       100
                   ....*....|....*....|....*..
gi 1085344563 2510 VDLHNGIITV-KSELnAGTTFTVKIPL 2535
Cdd:cd16939     79 ALWHGGHVECdDSEL-GGACFRLTWPR 104
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
411-550 4.05e-15

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: 80.93  E-value: 4.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  411 ERRDAENALYLSEERFRRLAENAPDVIYRMSLaDGKYEYISPAALTIFGYSPDDYYDNPLLFKqsIHSDWIKYFEEHWAN 490
Cdd:COG5805    144 KKKKIEEILQEQEERLQTLIENSPDLICVIDT-DGRILFINESIERLFGAPREELIGKNLLEL--LHPCDKEEFKERIES 220
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  491 LQKGILPQTYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQALQK 550
Cdd:COG5805    221 ITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAEELMAR 280
PAS COG2202
PAS domain [Signal transduction mechanisms];
1103-1514 4.08e-15

PAS domain [Signal transduction mechanisms];


Pssm-ID: 441804 [Multi-domain]  Cd Length: 258  Bit Score: 77.76  E-value: 4.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1103 RAEESLLESETKLRIMFENSRDA-LGVSKKGVHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGE 1181
Cdd:COG2202      1 TAEEALEESERRLRALVESSPDAiIITDLDGRILYVNPAFERLTGYSA-EELLGKTLRDLLPPEDDDEFLELLRAALAGG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1182 EIPSFyETRGRKRDGSEFDFEINIST-YELNGEI-YTLANIRDITSRKLLEKSlffvaergwqtgeenffdslaqflgen 1259
Cdd:COG2202     80 GVWRG-ELRNRRKDGSLFWVELSISPvRDEDGEItGFVGIARDITERKRAEEA--------------------------- 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1260 ldmdyvvvdklddnpeiaetialyakgsivpniryalkgtpcenvmgrqlcfypkevqklfpddklllemgvdsymgipl 1339
Cdd:COG2202        --------------------------------------------------------------------------------
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1340 wdsfgkpiglialmsskshpedsiaiqvlqlvatraaaelerdrsdriLRKREYEFRTLAESLPDNIVRYDRNGRTVYVN 1419
Cdd:COG2202    132 ------------------------------------------------LRESEERLRLLVENAPDGIFVLDLDGRILYVN 163
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1420 PILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASG-ENSELEILVPNPNNEQIVHQIRIIAERDEQNkVTSVL 1498
Cdd:COG2202    164 PAAEELLGYSPEELLGKSLLDLLHPEDRERLLELLRRLLEGGrESYELELRLKDGDGRWVWVEASAVPLRDGGE-VIGVL 242
                          410
                   ....*....|....*.
gi 1085344563 1499 AIGRDITERKRAEETI 1514
Cdd:COG2202    243 GIVRDITERKRAEEAL 258
HATPase_SpaK_NisK-like cd16975
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2428-2533 1.72e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Bacillus subtilis SpaK and Lactococcus lactis NisK. SpaK is the histidine kinase (HK) of the SpaK-SpaR two-component regulatory system (TCS), which is involved in the regulation of the biosynthesis of lantibiotic subtilin. NisK is the HK of the NisK-NisR TCS, which is involved in the regulation of the biosynthesis of lantibiotic nisin. SpaK and NisK may function as membrane-associated protein kinases that phosphorylate SpaR and NisR, respectively, in response to environmental signals.


Pssm-ID: 340434 [Multi-domain]  Cd Length: 107  Bit Score: 71.72  E-value: 1.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDISG-TGLGLSIV 2506
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEGGTVSISIYDEEEYLYFEIWDNGHGFSEQDLKKALELFYRDDTSRRSGGhYGMGLYIA 80
                           90       100
                   ....*....|....*....|....*..
gi 1085344563 2507 KRAVDLHNGIITVKSELNAGTTFTVKI 2533
Cdd:cd16975     81 KNLVEKHGGSLIIENSQKGGAEVTVKI 107
HATPase_CckA-like cd16919
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ...
2436-2534 2.61e-14

Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar to Brucella abortus 2308 CckA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component hybrid sensor histidine kinase (HKs) similar to Brucella abortus 2308 CckA, which is a component of an essential protein phosphorelay that regulates expression of genes required for growth, division, and intracellular survival; phosphoryl transfer initiates from the sensor kinase CckA and proceeds via the ChpT phosphotransferase to two regulatory substrates: the DNA-binding response regulator CtrA and the phospho-receiver protein CpdR. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), a REC signal receiver domain, and some contain PAS or PAS and GAF sensor domain(s).


Pssm-ID: 340396 [Multi-domain]  Cd Length: 116  Bit Score: 71.26  E-value: 2.61e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2436 LLNLLSNAIKYSPKGGKIELTIKQ----LRGKM-----------VISVKDKGIGIPTDDLKHLFEPFHRAKNTTdiSGTG 2500
Cdd:cd16919      5 ILNLAVNARDAMPEGGRLTIETSNqrvdADYALnyrdlipgnyvCLEVSDTGSGMPAEVLRRAFEPFFTTKEVG--KGTG 82
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1085344563 2501 LGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16919     83 LGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
HATPase_BaeS-like cd16946
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2428-2534 2.66e-14

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli BasS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) similar to Escherichia coli BaeS HK of the BaeS/BaeR two-component regulatory system (TCS), which responds to envelope stress. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and a HAMP sensory domain.


Pssm-ID: 340422 [Multi-domain]  Cd Length: 109  Bit Score: 70.95  E-value: 2.66e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDIS--GTGLGLSI 2505
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRAAQTPQEVRLDVEDSAPGVSDDQLARLFERFYRVESSRNRAsgGSGLGLAI 80
                           90       100
                   ....*....|....*....|....*....
gi 1085344563 2506 VKRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16946     81 CHNIALAHGGTISAEHSPLGGLRLVLTLP 109
GAF COG2203
GAF domain [Signal transduction mechanisms];
1764-2338 3.83e-14

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 78.70  E-value: 3.83e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1764 SDITMRKNAEVALKLSEERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFE 1843
Cdd:COG2203     53 LLERLTELRAAARLAAEAAEAALLLILLIDALVLLSLVATAGLVLELADLLLLLRLLALLVLLLVALALAEALAARLLDL 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1844 KLRSGKTALAERNLIRNDGSLLPVEISGIMLPDKRFLGIVRDITERKKNEAALNERIKHSQSLLRLSKNLEFAQTYSQAL 1923
Cdd:COG2203    133 LLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLILDIARLLTQRARLELERLALLNEISQALRSALDLEELL 212
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1924 TAALNEIKNILGYKTVWVYLLSEDKKYFNALVARGDFEDIVMSpegtliLPIEGDrMLEEIAEAKEIVIVEDARADERTN 2003
Cdd:COG2203    213 QRILELAGELLGADRGAILLVDEDGGELELVAAPGLPEEELGR------LPLGEG-LAGRALRTGEPVVVNDASTDPRFA 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2004 ---KKIVETLGNRTIINVPIYLLDKHLGTVGtgtFSDEGVRIPTRSEKEFLLAMASHLAVTLDRLHLLVERQEAEKALLR 2080
Cdd:COG2203    286 pslRELLLALGIRSLLCVPLLVDGRLIGVLA---LYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQ 362
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2081 LNRELKAISNCNQSLLRAEDEQSLLNEICRIICEEAGYDFAWVGYTEHSDANTIHPVAWAGIDIDLKAKEKFDWSEEIEC 2160
Cdd:COG2203    363 ELALLRLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVL 442
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2161 GLRPAQKVIQTGDIIYVQDFSSDASLESWCQKALQRGYRSGMALPLKNENSQVFGVILIYSTNRNVITQDEIRLIEELAN 2240
Cdd:COG2203    443 RRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLL 522
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2241 DLAFGIITLQTRAERKRVEKELELHRDHLQELVNVRTEELDKVNKKLIIEFEKEKEFERMLQHSLEKEKELSELKSRFIS 2320
Cdd:COG2203    523 LLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALALLELLLVAVGDLLL 602
                          570
                   ....*....|....*...
gi 1085344563 2321 TTSHEFRTPLTTVRVSAE 2338
Cdd:COG2203    603 LERDLLLLLVLLVRLLLE 620
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1400-1509 4.29e-14

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: 70.52  E-value: 4.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1400 ESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGENSELEIlVPNPNNEQIV 1479
Cdd:pfam08448    2 DSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLE-ELLLNGEERH 80
                           90       100       110
                   ....*....|....*....|....*....|
gi 1085344563 1480 HQIRIIAERDEQNKVTSVLAIGRDITERKR 1509
Cdd:pfam08448   81 YELRLTPLRDPDGEVIGVLVISRDITERRR 110
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
1535-1780 6.92e-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: 76.94  E-value: 6.92e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1535 LDIANNILRWSDEIFRIFEIDPKEFgsSYEAFLNAIHPDDREVVNTAYSNSLVNRTPYAIDHRLRFDDGRIKFVHEQCET 1614
Cdd:COG5809     31 LDLEGKILKVNPAAERIFGYTEDEL--LGTNILDFLHPDDEKELREILKLLKEGESRDELEFELRHKNGKRLEFSSKLSP 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1615 IYNEENKPLRSIGTVQDITDRKLAEEALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAID 1694
Cdd:COG5809    109 IFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILE 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1695 PAWHFYREdgtvlpLEEYPVNYVLATRKELRNYVvgVHRTNYKNDVWVLVNADPVWSNENELTQVIVtFSDITMRKNAEV 1774
Cdd:COG5809    189 LIHSDDQE------NVAAFISQLLKDGGIAQGEV--RFWTKDGRWRLLEASGAPIKKNGEVDGIVII-FRDITERKKLEE 259

                   ....*.
gi 1085344563 1775 ALKLSE 1780
Cdd:COG5809    260 LLRKSE 265
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
1030-1234 7.95e-14

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: 76.69  E-value: 7.95e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1030 KQWLQLILPEDKERAeKTAIDAVQKDIPYNLDYRIIRHNGELRYIHSEANVRRDSSGKPIFMLGMmqDITVRKRAEESLL 1109
Cdd:COG5805     77 KTIFDFLEKEYHYRV-KTRIERLQKGYDVVMIEQIYCKDGELIYVEVKLFPIYNQNGQAAILALR--DITKKKKIEEILQ 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1110 ESETKLRIMFENSRDALGV-SKKGVHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGEEiPSFYE 1188
Cdd:COG5805    154 EQEERLQTLIENSPDLICViDTDGRILFINESIERLFGAPR-EELIGKNLLELLHPCDKEEFKERIESITEVWQ-EFIIE 231
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1085344563 1189 TRGRKRDGSEFDFEINISTY--ELNGEIYTLANIRDITSRKLLEKSLF 1234
Cdd:COG5805    232 REIITKDGRIRYFEAVIVPLidTDGSVKGILVILRDITEKKEAEELMA 279
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
2098-2246 9.67e-14

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 70.57  E-value: 9.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2098 AEDEQSLLNEICRIICEEAGYDFAWVGYTEHSDantiHPVAWAGIDIDLKAKEKFDWSEEiecglrPAQKVIQTGDIIYV 2177
Cdd:pfam13185    1 AADLEELLDAVLEAAVELGASAVGFILLVDDDG----RLAAWGGAADELSAALDDPPGEG------LVGEALRTGRPVIV 70
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563 2178 QDFSSDASLESWcqKALQRGYRSGMALPLKNENsQVFGVILIYSTNRNVITQDEIRLIEELANDLAFGI 2246
Cdd:pfam13185   71 NDLAADPAKKGL--PAGHAGLRSFLSVPLVSGG-RVVGVLALGSNRPGAFDEEDLELLELLAEQAAIAI 136
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
411-556 1.15e-13

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: 76.17  E-value: 1.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  411 ERRDAENALYLSEERFRRLAENAPDVIYrMSLADGKYEYISPAALTIFGYSPDDYYDNPllFKQSIHSDWIKYFEEHWAN 490
Cdd:COG5809    128 ERKRMEEALRESEEKFRLIFNHSPDGII-VTDLDGRIIYANPAACKLLGISIEELIGKS--ILELIHSDDQENVAAFISQ 204
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563  491 LQKGILPQTYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIeGVVTDITERKQAEQALQKA-------------AEEIR 556
Cdd:COG5809    205 LLKDGGIAQGEVRFWTKDGRWRLLEASGAPIKKNGEVDGIV-IIFRDITERKKLEELLRKSeklsvvgelaagiAHEIR 282
PRK13560 PRK13560
hypothetical protein; Provisional
1034-1660 1.17e-13

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 77.02  E-value: 1.17e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1034 QLILPEDKE-------RAEKTAIDAVQKDiPYNLDYRIIRHnGELRYIHSEANVRRDSSGKpIFMLGMMQDITVRKRAEE 1106
Cdd:PRK13560   121 MLIGGDDGDfffanpfRSAETIAMALQSD-DWQEEEGHFRC-GDGRFIDCCLRFERHAHAD-DQVDGFAEDITERKRAEE 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1107 SLLESETKLRIMFENSRD-ALGVSKKGVHVFANPAYLKLFGYEKlEEIVGTSILEcIAPSHHQQIIENV---KRRDSGEE 1182
Cdd:PRK13560   198 RIDEALHFLQQLLDNIADpAFWKDEDAKVFGCNDAACLACGFRR-EEIIGMSIHD-FAPAQPADDYQEAdaaKFDADGSQ 275
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1183 IpsfYETRGRKRDGSEFDFEINISTYELNGEIYTLAN----IRDITSRKLLEKSLFFvaergwqtgEENFFDSLAQFLge 1258
Cdd:PRK13560   276 I---IEAEFQNKDGRTRPVDVIFNHAEFDDKENHCAGlvgaITDISGRRAAERELLE---------KEDMLRAIIEAA-- 341
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1259 nldmdyvvvdklddnPEIAetIALYAKGSIvpniryalkgtpcenvmgrqlCFYPKevqklfPDDKLLLEMGVDSYMGIP 1338
Cdd:PRK13560   342 ---------------PIAA--IGLDADGNI---------------------CFVNN------NAAERMLGWSAAEVMGKP 377
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1339 LWDsfgkpiglialmsskSHPEdsiaiqvlqlvatraaaelerdrsdrilRKREYEFRTLAESLPDnivrydrnGRTVYV 1418
Cdd:PRK13560   378 LPG---------------MDPE----------------------------LNEEFWCGDFQEWYPD--------GRPMAF 406
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1419 NPILEKTLATGASAMIGTTIRELNPDGsfeSYAQAVdnalasgenseleiLVPNPnneqiVHqiriiaerDEQNKVTSVL 1498
Cdd:PRK13560   407 DACPMAKTIKGGKIFDGQEVLIEREDD---GPADCS--------------AYAEP-----LH--------DADGNIIGAI 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1499 AIGRDITERKRAEETIKKSEAQLNEAQ----RIAQIGSWELD-IANNILRwsdeifriFEIDPKEFGSSYEAFLNAIHPD 1573
Cdd:PRK13560   457 ALLVDITERKQVEEQLLLANLIVENSPlvlfRWKAEEGWPVElVSKNITQ--------FGYEPDEFISGKRMFAAIIHPA 528
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1574 DREVVN---TAYSNSLVNRtpYAIDHRLRFDDGRIKFVHEQCETIYNEENKPLRSIGTVQDITDRKLAEEALKESEEKYR 1650
Cdd:PRK13560   529 DLEQVAaevAEFAAQGVDR--FEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIKAALTEKE 606
                          650
                   ....*....|
gi 1085344563 1651 TLIQKIQTAV 1660
Cdd:PRK13560   607 VLLKEIHHRV 616
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
422-548 1.18e-13

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: 69.63  E-value: 1.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  422 SEERFRRLAENAPDVIYRMSLaDGKYEYISPAALTIFGYSPDDYYD-NPLLFKQSIHSDWIK-YFEEHwanLQKGILPQT 499
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDL-EGNILYVNPAFEEIFGYSAEELIGrNVLELIPEEDREEVReRIERR---LEGEPEPVS 76
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1085344563  500 YEYQIIHKSGEARWLNQRNILVlDEGGNSVAIEGVVTDITERKQAEQAL 548
Cdd:TIGR00229   77 EERRVRRKDGSEIWVEVSVSPI-RTNGGELGVVGIVRDITERKEAEEAL 124
HATPase_CreC-like cd16945
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2428-2520 1.29e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli CreC; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli CreC of the CreC-CreB two-component regulatory system (TCS) involved in catabolic regulation. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), and accessory sensory domain(s) such as HAMP, CACHE or PAS.


Pssm-ID: 340421 [Multi-domain]  Cd Length: 106  Bit Score: 69.03  E-value: 1.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHR-AKNTTDISGTGLGLSIV 2506
Cdd:cd16945      1 DPFLLRQAINNLLDNAIDFSPEGGLIALQLEADTEGIELLVFDEGSGIPDYALNRVFERFYSlPRPHSGQKSTGLGLAFV 80
                           90
                   ....*....|....
gi 1085344563 2507 KRAVDLHNGIITVK 2520
Cdd:cd16945     81 QEVAQLHGGRITLR 94
HATPase_YcbM-like cd16947
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2435-2533 1.46e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis YcbM; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis YcbM, a HK of the two-component system YcbM-YcbL. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA).


Pssm-ID: 340423 [Multi-domain]  Cd Length: 125  Bit Score: 69.46  E-value: 1.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTD--ISGTGLGLSIVKRAVDL 2512
Cdd:cd16947     24 ILKNLISNAIKYGSDGKFLGMTLREDEKHVYIDIWDKGKGISETEKDHVFERLYTLEDSRNsaKQGNGLGLTITKRLAES 103
                           90       100
                   ....*....|....*....|.
gi 1085344563 2513 HNGIITVKSELNAGTTFTVKI 2533
Cdd:cd16947    104 MGGSIYVNSKPYEKTVFTVTL 124
HATPase_DpiB-CitA-like cd16915
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2435-2534 3.68e-13

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli K-12 DpiB, DcuS, and Bacillus subtilis CitS, DctS, and YufL; This family includes histidine kinase-like ATPase domains of Escherichia coli K-12 DpiB and DcuS, and Bacillus subtilis CitS, DctS and MalK histidine kinases (HKs) all of which are two component transduction systems (TCSs). E. coli K-12 DpiB (also known as CitA) is the histidine kinase (HK) of DpiA-DpiB, a two-component signal transduction system (TCS) required for the expression of citrate-specific fermentation genes and genes involved in plasmid inheritance. E. coli K-12 DcuS (also known as YjdH) is the HK of DcuS-DcuR, a TCS that in the presence of the extracellular C4-dicarboxlates, activates the expression of the genes of anaerobic fumarate respiration and of aerobic C4-dicarboxylate uptake. CitS is the HK of Bacillus subtilis CitS-CitT, a TCS which regulates expression of CitM, the Mg-citrate transporter. Bacillus subtilis DctS forms a tripartite sensor unit (DctS/DctA/DctB) for sensing C4 dicarboxylates. Bacillus subtilis MalK (also known as YfuL) is the HK of MalK-MalR (YufL-YufM) a TCS which regulates the expression of the malate transporters MaeN (YufR) and YflS, and is essential for utilization of malate in minimal medium. Proteins having this DpiB-CitA-like HATPase domain generally have sensor domains such as Cache and PAS, and a histidine kinase A (HisKA)-like SpoOB-type, alpha-helical domain.


Pssm-ID: 340392 [Multi-domain]  Cd Length: 104  Bit Score: 67.70  E-value: 3.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKYS----PKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEpfhRAKNTTDISGTGLGLSIVKRAV 2510
Cdd:cd16915      4 IVGNLIDNALDALaatgAPNKQVEVFLRDEGDDLVIEVRDTGPGIAPELRDKVFE---RGVSTKGQGERGIGLALVRQSV 80
                           90       100
                   ....*....|....*....|....
gi 1085344563 2511 DLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16915     81 ERLGGSITVESEPGGGTTFSIRIP 104
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
1641-1780 5.78e-13

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 72.96  E-value: 5.78e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1641 ALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKkaidPAWHFYREDGTVLPLeeypVNYVLAT 1720
Cdd:COG3852      1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGR----PLAELFPEDSPLREL----LERALAE 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1721 RKELRNYVVGVHRTNyKNDVWVLVNADPVwSNENELTQVIVTFSDITMRKNAEVALKLSE 1780
Cdd:COG3852     73 GQPVTEREVTLRRKD-GEERPVDVSVSPL-RDAEGEGGVLLVLRDITERKRLERELRRAE 130
HATPase_CheA-like cd16916
Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some ...
2436-2534 6.48e-13

Histidine kinase-like ATPase domain of the chemotaxis protein histidine kinase CheA, and some hybrid sensor histidine kinases; This family includes the cytoplasmic histidine kinase (HK) CheA, a transmembrane receptor which, together with cytoplasmic adaptor protein (CheW), forms the lattice at the core of the chemosensory array that controls the cellular chemotaxis of motile bacteria and archaea. CheA forms a two-component signal transduction system (TCS) with the response regulator CheY. Proteins having this CheA-like HATPase domain generally also have a histidine-phosphotransfer domain, a histidine kinase homodimeric domain, and a regulatory domain; some are hybrid sensor histidine kinases as they contain a REC signal receiver domain.


Pssm-ID: 340393 [Multi-domain]  Cd Length: 178  Bit Score: 69.15  E-value: 6.48e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2436 LLNLLSNAIKYS------------PKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKH--------------------- 2482
Cdd:cd16916     43 LTHLLRNAVDHGieapeerlaagkPPEGTITLRAEHQGNQVVIEVSDDGRGIDREKIREkaierglitadeaatlsddev 122
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 2483 ---LFEP-FHRAKNTTDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16916    123 lnlIFAPgFSTAEQVTDVSGRGVGMDVVKRSIESLGGTIEVESEPGQGTTFTIRLP 178
YesM COG2972
Sensor histidine kinase YesM [Signal transduction mechanisms];
2422-2537 6.90e-13

Sensor histidine kinase YesM [Signal transduction mechanisms];


Pssm-ID: 442211 [Multi-domain]  Cd Length: 445  Bit Score: 73.51  E-value: 6.90e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2422 KIHYRLDPKLM-----KFILLNLLSNAIKY----SPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKN 2492
Cdd:COG2972    322 EVEIEIDEELLdllipKLILQPLVENAIEHgiepKEGGGTIRISIRKEGDRLVITVEDNGVGMPEEKLEKLLEELSSKGE 401
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1085344563 2493 ttdisGTGLGLSIVKRAVDLHNGI---ITVKSELNAGTTFTVKIPLEQ 2537
Cdd:COG2972    402 -----GRGIGLRNVRERLKLYYGEeygLEIESEPGEGTTVTIRIPLEE 444
HisKA pfam00512
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ...
2315-2382 2.04e-12

His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.


Pssm-ID: 459839 [Multi-domain]  Cd Length: 66  Bit Score: 64.15  E-value: 2.04e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 2315 KSRFISTTSHEFRTPLTTVRVSAEMIQRYRkrwTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSESG 2382
Cdd:pfam00512    2 KSEFLANLSHELRTPLTAIRGYLELLRDEK---LDEEQREYLETILRSAERLLRLINDLLDLSRIEAG 66
HATPase_HupT_MifS-like cd16976
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2435-2531 3.35e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Rhodobacter capsulatus HupT and Pseudomonas aeruginosa MifS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Rhodobacter capsulatus HupT of the HupT-HupR two-component regulatory system (TCS), which regulates the synthesis of HupSL, a membrane bound [NiFe]hydrogenase. It also contains the HATPase domain of Pseudomonas aeruginosa MifS, the HK of the MifS-MifR TCS, which may be involved in sensing alpha-ketoglutarate and regulating its transport and subsequent metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also have a C-terminal PAS sensor domain.


Pssm-ID: 340435 [Multi-domain]  Cd Length: 102  Bit Score: 64.79  E-value: 3.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIK--YSPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTTDisGTGLGLSIVKRAVDL 2512
Cdd:cd16976      4 VLMNLLQNALDamGKVENPRIRIAARRLGGRLVLVVRDNGPGIAEEHLSRVFDPFFTTKPVGK--GTGLGLSISYGIVEE 81
                           90
                   ....*....|....*....
gi 1085344563 2513 HNGIITVKSELNAGTTFTV 2531
Cdd:cd16976     82 HGGRLSVANEEGAGARFTF 100
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
674-803 3.65e-12

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 70.65  E-value: 3.65e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  674 QLRNSEREFRTLAENLPDHIIRYDIDCRVIYLNHVVAA-TNYTNSSLVGKLSAEIqFNEAKGLEEYnekLRRVIKTG-TE 751
Cdd:COG3852      1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERlLGLSAEELLGRPLAEL-FPEDSPLREL---LERALAEGqPV 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1085344563  752 DEMEIMLRDIEGNLHIHEVHFLAERDIEGKIvGALAIGHDISERKQAEEERQ 803
Cdd:COG3852     77 TEREVTLRRKDGEERPVDVSVSPLRDAEGEG-GVLLVLRDITERKRLERELR 127
HATPase_BvrS-ChvG-like cd16953
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2435-2534 3.97e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Brucella abortus BvrS and Sinorhizobium meliloti ChvG; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Brucella abortus BvrS of the BvrR-BvrS two-component regulatory system (TCS), which controls cell invasion and intracellular survival, as well as Sinorhizobium meliloti and Agrobacterium tumefaciens ChvG of the ChvI-ChvG TCS necessary for endosymbiosis and pathogenicity in plants. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA), an accessory HAMP sensor domain, a periplasmic stimulus-sensing domain, and some also have a sensor N-terminal transmembrane domain.


Pssm-ID: 340429 [Multi-domain]  Cd Length: 110  Bit Score: 64.90  E-value: 3.97e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKYSP-KGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFH--RAKNTTDISGTGLGLSIVKRAVD 2511
Cdd:cd16953      4 VLRNLIGNAISFSPpDTGRITVSAMPTGKMVTISVEDEGPGIPQEKLESIFDRFYteRPANEAFGQHSGLGLSISRQIIE 83
                           90       100
                   ....*....|....*....|....*..
gi 1085344563 2512 LHNGIITVKS----ELNAGTTFTVKIP 2534
Cdd:cd16953     84 AHGGISVAENhnqpGQVIGARFTVQLP 110
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
449-535 4.54e-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: 63.90  E-value: 4.54e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  449 YISPAALTIFGYSPDDYYDNPLLFKQSIH-SDWIKYFEEHWANLQKGIlPQTYEYQIIHKSGEARWLNQRNILVLDEGGN 527
Cdd:pfam08447    3 YWSPRFEEILGYTPEELLGKGESWLDLVHpDDRERVREALWEALKGGE-PYSGEYRIRRKDGEYRWVEARARPIRDENGK 81

                   ....*...
gi 1085344563  528 SVAIEGVV 535
Cdd:pfam08447   82 PVRVIGVA 89
HATPase_Glnl-NtrB-like cd16918
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2435-2534 4.80e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli GlnL (synonyms NtrB and NRII); This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs), similar to Escherichia coli GlnL/NtrB/NRII HK of the two-component regulatory system (TCS) GlnL/GlnG (NtrB-NtrC, or NRII-NRI), which regulates the transcription of genes encoding metabolic enzymes and permeases in response to carbon and nitrogen status in E. coli and related bacteria. Also included in this family are Rhodobacter capsulatus NtrB, Azospirillum brasilense NtrB, Vibrio alginolyticus NtrB, Rhizobium leguminosarum biovar phaseoli NtrB, and Herbaspirillum seropedicae NtrB. Escherichia coli GlnL/NtrB/NRII is both a kinase and a phosphatase, catalyzing the phosphorylation and dephosphorylation of GlnG/NtrC/NRI. The kinase and phosphatase activities of GlnL/NtrB/NRII are regulated by the PII signal transduction protein, which on binding to GlnL/NtrB/NRII, inhibits the kinase activity of GlnL/NtrB/NRII and activates the GlnL/NtrB/NRII phosphatase activity. Proteins having this HATPase domain also have a histidine kinase dimerization and phosphoacceptor domain (HisKA); some also contain PAS sensor domain(s).


Pssm-ID: 340395 [Multi-domain]  Cd Length: 109  Bit Score: 64.73  E-value: 4.80e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIK-YSPKGGKI--------ELTIKQLRGKMV--ISVKDKGIGIPTDDLKHLFEPFhrakNTTDISGTGLGL 2503
Cdd:cd16918      4 VFLNLVRNAAQaLAGSGGEIilrtrtqrQVTLGHPRHRLAlrVSVIDNGPGIPPDLQDTIFYPM----VSGRENGTGLGL 79
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1085344563 2504 SIVKRAVDLHNGIITVKSElNAGTTFTVKIP 2534
Cdd:cd16918     80 AIAQNIVSQHGGVIECDSQ-PGHTVFSVSLP 109
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
1800-1888 5.56e-12

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: 64.02  E-value: 5.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1800 NGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFekLRSGKTALA-ERNLIRNDGSLLPVEISGIMLPD-- 1876
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREA--LREGKAVREfEVVLYRKDGEPFPVLVSLAPIRDdg 78
                           90
                   ....*....|....*
gi 1085344563 1877 ---KRFLGIVRDITE 1888
Cdd:pfam13426   79 gelVGIIAILRDITE 93
PRK13560 PRK13560
hypothetical protein; Provisional
1500-1922 5.67e-12

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 71.63  E-value: 5.67e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1500 IGRDITERKRAEEtikkseaQLNEAQRIAQigsWELDIANNILRWSDEIFRIFEID-----------PKEFGSSYEAFLN 1568
Cdd:PRK13560   185 FAEDITERKRAEE-------RIDEALHFLQ---QLLDNIADPAFWKDEDAKVFGCNdaaclacgfrrEEIIGMSIHDFAP 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1569 AIHPDDREVVNTAYSNSLVNRTpYAIDHRLRfdDGRIKFVheqcETIYNE------ENKPLRSIGTVQDITDRKLAEEAL 1642
Cdd:PRK13560   255 AQPADDYQEADAAKFDADGSQI-IEAEFQNK--DGRTRPV----DVIFNHaefddkENHCAGLVGAITDISGRRAAEREL 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1643 KESEEKYRTLIQKIQTAVIVHTPDTQI-LICNHSAEILLGLSEDQLLGKK--AIDP---------AWHFYREDGTVLPLE 1710
Cdd:PRK13560   328 LEKEDMLRAIIEAAPIAAIGLDADGNIcFVNNNAAERMLGWSAAEVMGKPlpGMDPelneefwcgDFQEWYPDGRPMAFD 407
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1711 EYPVNYVLATRKELRNYVVGVHRTNyKNDVWVLVNADPVWSNENELTQVIVTFSDITMRKNAEVALKLSEeryrTLVEQA 1790
Cdd:PRK13560   408 ACPMAKTIKGGKIFDGQEVLIERED-DGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQLLLAN----LIVENS 482
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1791 MDGIFIADSNGNY-IDVNRSGCNMLGYTRDQLL--KLRMQDLI-PAEEQQTTPIQFEKLRSGKTAL-AERNLIRNDGSLL 1865
Cdd:PRK13560   483 PLVLFRWKAEEGWpVELVSKNITQFGYEPDEFIsgKRMFAAIIhPADLEQVAAEVAEFAAQGVDRFeQEYRILGKGGAVC 562
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563 1866 PVEISGIMLPDKR-----FLGIVRDITERKKNEAALNERIKHSQSLL-----RLSKNLEFAQT--YSQA 1922
Cdd:PRK13560   563 WIDDQSAAERDEEgqishFEGIVIDISERKHAEEKIKAALTEKEVLLkeihhRVKNNLQIISSllDLQA 631
PRK13560 PRK13560
hypothetical protein; Provisional
405-681 5.77e-12

hypothetical protein; Provisional


Pssm-ID: 106506 [Multi-domain]  Cd Length: 807  Bit Score: 71.63  E-value: 5.77e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  405 FIESEAERRDAENALYLSEERFRRLAENAPDVIYRMSLADGKYEYISPAALTIFGYSPDDYYDNPLLFKQSIHSD--WIK 482
Cdd:PRK13560   313 AITDISGRRAAERELLEKEDMLRAIIEAAPIAAIGLDADGNICFVNNNAAERMLGWSAAEVMGKPLPGMDPELNEefWCG 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  483 YFEEHWAN--------------LQKGILPQTYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQAL 548
Cdd:PRK13560   393 DFQEWYPDgrpmafdacpmaktIKGGKIFDGQEVLIEREDDGPADCSAYAEPLHDADGNIIGAIALLVDITERKQVEEQL 472
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  549 QKAaeeiRDLYNNAPCG-YHSLDKEGTFVRINNTELKWLGYTLEEVI-GKMKFTDIITPKSLKTFNENFPGFKEKGWIK- 625
Cdd:PRK13560   473 LLA----NLIVENSPLVlFRWKAEEGWPVELVSKNITQFGYEPDEFIsGKRMFAAIIHPADLEQVAAEVAEFAAQGVDRf 548
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563  626 NLEFELIRKDGSILPILASATAIKDSDGNYLMSRSTVNDIAELKLAELQLRNSERE 681
Cdd:PRK13560   549 EQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEEKIKAALTE 604
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
1380-1518 6.33e-12

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: 70.77  E-value: 6.33e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1380 ERDRSDRILRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALA 1459
Cdd:COG5809    128 ERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSDDQENVAAFISQLLK 207
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563 1460 SGENSELEILVPNPNNEQIVHQIRiIAERDEQNKVTSVLAIGRDITERKRAEETIKKSE 1518
Cdd:COG5809    208 DGGIAQGEVRFWTKDGRWRLLEAS-GAPIKKNGEVDGIVIIFRDITERKKLEELLRKSE 265
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
572-667 6.44e-12

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: 63.63  E-value: 6.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  572 EGTFVRINNTELKWLGYTLEEVIGKmKFTDIITPKSLKTFNENFpgFKEKGWIKNLEFELIRKDGSILPILASATAIKDS 651
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGK-SITDLFAEPEDSERLREA--LREGKAVREFEVVLYRKDGEPFPVLVSLAPIRDD 77
                           90
                   ....*....|....*.
gi 1085344563  652 DGNYLMSRSTVNDIAE 667
Cdd:pfam13426   78 GGELVGIIAILRDITE 93
HATPase_NtrY-like cd16944
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2428-2534 9.15e-12

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Azorhizobium caulinodans NtrY; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Azorhizobium caulinodans ORS571 NtrY of the NtrY-NtrX TCS, which is involved in nitrogen fixation and metabolism. Proteins having this HATPase domain also contain a histidine kinase dimerization and phosphoacceptor domain (HisKA) and a HAMP sensor domain; some also have PAS sensor domains.


Pssm-ID: 340420 [Multi-domain]  Cd Length: 108  Bit Score: 63.71  E-value: 9.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNA---IKYSPKGgKIELTIK---QLRGKMVISVKDKGIGIPTDDLKHLFEPFhrakNTTDISGTGL 2501
Cdd:cd16944      1 DTTQISQVLTNILKNAaeaIEGRPSD-VGEVRIRveaDQDGRIVLIVCDNGKGFPREMRHRATEPY----VTTRPKGTGL 75
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1085344563 2502 GLSIVKRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16944     76 GLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
PRK11086 PRK11086
sensory histidine kinase DcuS; Provisional
2435-2536 1.83e-11

sensory histidine kinase DcuS; Provisional


Pssm-ID: 236839 [Multi-domain]  Cd Length: 542  Bit Score: 69.56  E-value: 1.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKY--SPKGGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNttdiSGTGLGLSIVKRAVDL 2512
Cdd:PRK11086   437 ILGNLIENALEAvgGEEGGEISVSLHYRNGWLHCEVSDDGPGIAPDEIDAIFDKGYSTKG----SNRGVGLYLVKQSVEN 512
                           90       100
                   ....*....|....*....|....
gi 1085344563 2513 HNGIITVKSELNAGTTFTVKIPLE 2536
Cdd:PRK11086   513 LGGSIAVESEPGVGTQFFVQIPWD 536
HisKA cd00082
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ...
2312-2378 4.10e-11

Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed through parallel association of 2 domains creating 4-helix bundles; usually these domains contain a conserved His residue and are activated via trans-autophosphorylation by the catalytic domain of the histidine kinase. They subsequently transfer the phosphoryl group to the Asp acceptor residue of a response regulator protein. Two-component signalling systems, consisting of a histidine protein kinase that senses a signal input and a response regulator that mediates the output, are ancient and evolutionarily conserved signaling mechanisms in prokaryotes and eukaryotes.


Pssm-ID: 119399 [Multi-domain]  Cd Length: 65  Bit Score: 60.30  E-value: 4.10e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085344563 2312 SELKSRFISTTSHEFRTPLTTVRVSAEMIQRYRKRwtEDKLDVFLDKIKNSVDYLTKLLDDVLTISR 2378
Cdd:cd00082      1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLD--DEEQREYLERIREEAERLLRLINDLLDLSR 65
HisKA smart00388
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ...
2315-2382 7.38e-11

His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.


Pssm-ID: 214644 [Multi-domain]  Cd Length: 66  Bit Score: 59.89  E-value: 7.38e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563  2315 KSRFISTTSHEFRTPLTTVRVSAEMIQRyrkRWTEDKLDVFLDKIKNSVDYLTKLLDDVLTISRSESG 2382
Cdd:smart00388    2 KREFLANLSHELRTPLTAIRGYLELLLD---TELSEEQREYLETILREAERLLRLINDLLDLSRIEAG 66
CheA COG0643
Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];
2451-2535 8.64e-11

Chemotaxis protein histidine kinase CheA [Signal transduction mechanisms];


Pssm-ID: 440408 [Multi-domain]  Cd Length: 563  Bit Score: 67.13  E-value: 8.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2451 GKIELTIKQLRGKMVISVKDKGIGIPTDDLKH------------------------LFEP-FHRAKNTTDISGTGLGLSI 2505
Cdd:COG0643    309 GTITLSAYHEGGRVVIEVSDDGRGLDLEKIRAkaiekglitaeeaaalsdeellelIFAPgFSTAEEVTDLSGRGVGMDV 388
                           90       100       110
                   ....*....|....*....|....*....|
gi 1085344563 2506 VKRAVDLHNGIITVKSELNAGTTFTVKIPL 2535
Cdd:COG0643    389 VKTNIEALGGTIEIESEPGKGTTFTLRLPL 418
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
1107-1233 9.91e-11

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 66.02  E-value: 9.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1107 SLLESETKLRIMFENSRDA-LGVSKKGVHVFANPAYLKLFGYEKlEEIVGTSILECIAPSH-HQQIIENVkrRDSGEEIP 1184
Cdd:COG3852      1 ALRESEELLRAILDSLPDAvIVLDADGRITYVNPAAERLLGLSA-EELLGRPLAELFPEDSpLRELLERA--LAEGQPVT 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1185 SfYETRGRKRDGSEFDFEINIST-YELNGEIYTLANIRDITSRKLLEKSL 1233
Cdd:COG3852     78 E-REVTLRRKDGEERPVDVSVSPlRDAEGEGGVLLVLRDITERKRLEREL 126
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
1773-1933 3.62e-10

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: 64.79  E-value: 3.62e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1773 EVALKLSEERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPaeeqqTTPIQfEKLRSGKTAL 1852
Cdd:COG3829      3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIP-----NSPLL-EVLKTGKPVT 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1853 AErnLIRNDGSLLPVEISGI-MLPDKRFLGIV---RDITERKKneaaLNERIKHSQSLLRLSKNLEFAQ--TYSQALTAA 1926
Cdd:COG3829     77 GV--IQKTGGKGKTVIVTAIpIFEDGEVIGAVetfRDITELKR----LERKLREEELERGLSAKYTFDDiiGKSPAMKEL 150

                   ....*..
gi 1085344563 1927 LNEIKNI 1933
Cdd:COG3829    151 LELAKRV 157
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
1391-1512 5.83e-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: 5.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1391 REYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGEN-SELEIL 1469
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEpVSEERR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1085344563 1470 VPNPNNEQIVHQIrIIAERDEQNKVTSVLAIGRDITERKRAEE 1512
Cdd:TIGR00229   81 VRRKDGSEIWVEV-SVSPIRTNGGELGVVGIVRDITERKEAEE 122
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
418-552 5.88e-10

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 63.71  E-value: 5.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  418 ALYLSEERFRRLAENAPDVIYRMSlADGKYEYISPAALTIFGYSPDDYYDNPLlfkQSIHSDWIKYFEEHWANLQKGILP 497
Cdd:COG3852      1 ALRESEELLRAILDSLPDAVIVLD-ADGRITYVNPAAERLLGLSAEELLGRPL---AELFPEDSPLRELLERALAEGQPV 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1085344563  498 QTYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIeGVVTDITERKQAEQALQKAA 552
Cdd:COG3852     77 TEREVTLRRKDGEERPVDVSVSPLRDAEGEGGVL-LVLRDITERKRLERELRRAE 130
ComP COG4585
Signal transduction histidine kinase ComP [Signal transduction mechanisms];
2330-2537 8.54e-10

Signal transduction histidine kinase ComP [Signal transduction mechanisms];


Pssm-ID: 443642 [Multi-domain]  Cd Length: 252  Bit Score: 61.94  E-value: 8.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2330 LTTVRVSAEMIQRYRKRWTEDKLDVfLDKIKNSVDyltKLLDDVLTISRsesgkiVLNREEIDLHEFCLDVIEEAKiSAT 2409
Cdd:COG4585     69 LSAIKLQLEAARRLLDADPEAAREE-LEEIRELAR---EALAELRRLVR------GLRPPALDDLGLAAALEELAE-RLL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2410 EAHKLIFNFTLKKIHYRLDPKLMK---FILLNLLSNAIKYSpKGGKIELTIKQLRGKMVISVKDKGIGIPTDDlkhlfep 2486
Cdd:COG4585    138 RAAGIRVELDVDGDPDRLPPEVELalyRIVQEALTNALKHA-GATRVTVTLEVDDGELTLTVRDDGVGFDPEA------- 209
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1085344563 2487 fhraknttdISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIPLEQ 2537
Cdd:COG4585    210 ---------APGGGLGLRGMRERAEALGGTLTIGSAPGGGTRVRATLPLAA 251
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
1388-1518 8.93e-10

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: 63.64  E-value: 8.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1388 LRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGsfesyaqAVDNALASGENSELE 1467
Cdd:COG3829      6 LKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTELIPNS-------PLLEVLKTGKPVTGV 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1085344563 1468 ILVPNPNNEQIVHQIRIIaerDEQNKVTSVLAIGRDITERKRAEETIKKSE 1518
Cdd:COG3829     79 IQKTGGKGKTVIVTAIPI---FEDGEVIGAVETFRDITELKRLERKLREEE 126
HATPase_PhoQ-like cd16954
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2435-2533 1.40e-09

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG; This family includes histidine kinase-like ATPase (HATPase) domain of two-component sensor histidine kinases similar to Escherichia coli PhoQ and Providencia stuartii AarG. PhoQ is the histidine kinase (HK) of the PhoP-PhoQ two-component regulatory system (TCS), which responds to the levels of Mg2+ and Ca2+, controls virulence, mediates the adaptation to Mg2+-limiting environments, and regulates numerous cellular activities. Providencia stuartii AarG is a putative sensor kinase which controls the expression of the 2'-N-acetyltransferase and an intrinsic multiple antibiotic resistance (Mar) response in Providencia stuartii. The AarG product is similar to PhoQ in that it is able to restore wild-type levels of resistance to a Salmonella typhimurium phoQ mutant. However, the expression of the 2'-N-acetyltransferase gene and of aarP (a gene encoding a transcriptional activator of 2'-N-acetyltransferase) are not significantly affected by the levels of Mg2+ or Ca2+. Most proteins in this group contain a histidine kinase dimerization and phosphoacceptor domain (HisKA); some have an accessory HAMP sensor domain, and some have an intracellular membrane -interaction PhoQ sensor domain.


Pssm-ID: 340430 [Multi-domain]  Cd Length: 135  Bit Score: 58.41  E-value: 1.40e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAIKYSPKggKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKntTDISGTGLGLSIVKRAVDLHN 2514
Cdd:cd16954     41 LLGNLLDNACKWCLE--FVEVTARQTDGGLHLIVDDDGPGVPESQRSKIFQRGQRLD--EQRPGQGLGLAIAKEIVEQYG 116
                           90
                   ....*....|....*....
gi 1085344563 2515 GIITVKSELNAGTTFTVKI 2533
Cdd:cd16954    117 GELSLSDSPLGGARFEVVF 135
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
562-665 1.43e-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: 57.26  E-value: 1.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  562 APCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKMkFTDIITPKSLKTFNENFPGFKEKGWIKNLEFELIRKDGSILPI 641
Cdd:cd00130      1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKS-LLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWV 79
                           90       100
                   ....*....|....*....|....
gi 1085344563  642 LASATAIKDSDGNYLMSRSTVNDI 665
Cdd:cd00130     80 LVSLTPIRDEGGEVIGLLGVVRDI 103
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1781-1886 1.60e-09

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: 57.43  E-value: 1.60e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1781 ERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTA--LAERNLI 1858
Cdd:pfam00989    1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEEsrGFEVSFR 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1085344563 1859 RNDGSLLPVEI--SGIMLPDKR---FLGIVRDI 1886
Cdd:pfam00989   81 VPDGRPRHVEVraSPVRDAGGEilgFLGVLRDI 113
glnL PRK11073
nitrogen regulation protein NR(II);
2428-2535 2.03e-09

nitrogen regulation protein NR(II);


Pssm-ID: 182947 [Multi-domain]  Cd Length: 348  Bit Score: 62.02  E-value: 2.03e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIK-YSPKGGKI--------ELTIKQLRGKMV--ISVKDKGIGIPTDDLKHLFEPFHRAKNttdi 2496
Cdd:PRK11073   234 DPDQIEQVLLNIVRNALQaLGPEGGTItlrtrtafQLTLHGERYRLAarIDIEDNGPGIPPHLQDTLFYPMVSGRE---- 309
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1085344563 2497 SGTGLGLSIVKRAVDLHNGIITVKSeLNAGTTFTVKIPL 2535
Cdd:PRK11073   310 GGTGLGLSIARNLIDQHSGKIEFTS-WPGHTEFSVYLPI 347
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1402-1504 2.97e-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: 56.49  E-value: 2.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1402 LPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGENSELEILVPNPNNEQIVHQ 1481
Cdd:cd00130      1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                           90       100
                   ....*....|....*....|...
gi 1085344563 1482 IRIIAERDEQNKVTSVLAIGRDI 1504
Cdd:cd00130     81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
687-797 6.18e-09

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: 55.88  E-value: 6.18e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  687 ENLPDHIIRYDIDCRVIYLN-HVVAATNYTNSSLVGKLSAEIqFNEAKGlEEYNEKLRRVIKTG-TEDEMEIMLRDieGN 764
Cdd:pfam08448    2 DSLPDALAVLDPDGRVRYANaAAAELFGLPPEELLGKTLAEL-LPPEDA-ARLERALRRALEGEePIDFLEELLLN--GE 77
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1085344563  765 LHIHEVHFLAERDIEGKIVGALAIGHDISERKQ 797
Cdd:pfam08448   78 ERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
399-827 9.62e-09

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 61.23  E-value: 9.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  399 ISFAMEfiESEAERRDaenaLYLSEERFRRLAENAPdviYRMSL--ADGKYEYISPAALTIFGYSPDDYYDnpLLFKQSI 476
Cdd:PRK09776   264 MTMVMY--AFRAERKH----ISESETRFRNAMEYSA---IGMALvgTEGQWLQVNKALCQFLGYSQEELRG--LTFQQLT 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  477 HSDWIKYFEEHWANLQKG-ILPQTYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQAEQALQKAAEEI 555
Cdd:PRK09776   333 WPEDLNKDLQQVEKLLSGeINSYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKRTEQVNERLMERI 412
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  556 RdLYNNA-----------PCGYHsLDKE-----GTFVRINNTELKWLGYTLEEVIGKMKFTDIITPKSLKTFnenfpgfk 619
Cdd:PRK09776   413 T-LANEAggigiwewdlkPNIIS-WDKRmfelyEIPPHIKPTWQVWYACLHPEDRQRVEKEIRDALQGRSPF-------- 482
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  620 ekgwikNLEFELIRKDGsILPILASATAIKDSDGNYLMSRSTVNDIAELK-LAELQLRNSEREFRTLaENLPDHIIRYDI 698
Cdd:PRK09776   483 ------KLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVRqLNEALFQEKERLHITL-DSIGEAVVCTDM 554
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  699 DCRVIYLNHVVAA-TNYTNSSLVGkLSAEIQFN---EAKGLEEYNEKLRRVIKTGTEDEMEIMLRDIEGNlhIHEVHFLA 774
Cdd:PRK09776   555 AMKVTFMNPVAEKmTGWTQEEALG-VPLLTVLHitfGDNGPLMENIYSCLTSRSAAYLEQDVVLHCRSGG--SYDVHYSI 631
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563  775 E--RDIEGKIVGALAIGHDISE-RKQAEE----------ERQANLRFFENmdRINRAIQEANNVEQ 827
Cdd:PRK09776   632 TplSTLDGENIGSVLVIQDVTEsRKMLRQlsysashdalTHLANRASFEK--QLRRLLQTVNSTHQ 695
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
443-538 9.93e-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: 54.95  E-value: 9.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  443 ADGKYEYISPAALTIFGYSPDDYYDNPLLfkQSIHSDWIKYFEEHWANLQKGILPQTYEYQIIHKSGEARWLNQRNILVL 522
Cdd:cd00130     10 LDGRILYANPAAEQLLGYSPEELIGKSLL--DLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVLVSLTPIR 87
                           90
                   ....*....|....*.
gi 1085344563  523 DEGGNSVAIEGVVTDI 538
Cdd:cd00130     88 DEGGEVIGLLGVVRDI 103
PRK13558 PRK13558
bacterio-opsin activator; Provisional
2070-2265 1.03e-08

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 60.62  E-value: 1.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2070 ERQEAEKALLRLNRELKA--------ISNCNQSLLRAEDEQSLLNEICRIICEEAGYDFAWVGYTEHSDAnTIHPVAWAG 2141
Cdd:PRK13558   264 ERKEAELALQRERRKLQRllerveglVNDVTSALVRATDREEIEAAVCDRVGAGGEYDGAWIGEYDPTSG-TITVAEAAG 342
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2142 iDIDLKAKEKFDWSEEiecglRPAQKVIQT--GDIIYVQdfssDASLESWCQKAlqRGyRSGMALPLKNeNSQVFGVILI 2219
Cdd:PRK13558   343 -GCDGADGDVLDLAAA-----GPAAAALQSvvAETEAVE----STDVDGVSGTV--DG-SAVAAVPLVY-RETTYGVLVV 408
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1085344563 2220 YSTNRNVITQDEIRLIEELANDLAFGIITLQTR---AERKRVEKELELH 2265
Cdd:PRK13558   409 YTAEPDEIDDRERVVLEALGRAVGAAINALESRrtlTTDEVLELEVELS 457
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1781-1847 1.04e-08

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: 53.56  E-value: 1.04e-08
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085344563  1781 ERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRS 1847
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
PRK13557 PRK13557
histidine kinase; Provisional
2426-2534 1.10e-08

histidine kinase; Provisional


Pssm-ID: 237425 [Multi-domain]  Cd Length: 540  Bit Score: 60.45  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2426 RLDPKLMKFILLNLLSNAIKYSPKGGKIEL-------------TIKQLR-GKMV-ISVKDKGIGIPTDDLKHLFEPFHRA 2490
Cdd:PRK13557   272 RIDPTQAEVALLNVLINARDAMPEGGRVTIrtrnveiededlaMYHGLPpGRYVsIAVTDTGSGMPPEILARVMDPFFTT 351
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1085344563 2491 KNttDISGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:PRK13557   352 KE--EGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTTVRLYFP 393
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1135-1223 1.14e-08

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: 54.95  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1135 VFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIPSFyETRGRKRDGSEFDFEINIS--TYELNG 1212
Cdd:cd00130     15 LYANPAAEQLLGYSP-EELIGKSLLDLIHPEDREELRERLENLLSGGEPVTL-EVRLRRKDGSVIWVLVSLTpiRDEGGE 92
                           90
                   ....*....|.
gi 1085344563 1213 EIYTLANIRDI 1223
Cdd:cd00130     93 VIGLLGVVRDI 103
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
678-802 1.14e-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: 55.37  E-value: 1.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  678 SEREFRTLAENLPDHIIRYDIDCRVIYLNHVVAA-TNYTNSSLVGKLSAEIQFNEakGLEEYNEKLRRVIKTGTED-EME 755
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEiFGYSAEELIGRNVLELIPEE--DREEVRERIERRLEGEPEPvSEE 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1085344563  756 IMLRDIEGNLHIHEVHfLAERDIEGKIVGALAIGHDISERKQAEEER 802
Cdd:TIGR00229   79 RRVRRKDGSEIWVEVS-VSPIRTNGGELGVVGIVRDITERKEAEEAL 124
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
2100-2246 1.69e-08

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 55.18  E-value: 1.69e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2100 DEQSLLNEICRIICEEAGYDFAWVGYTEHSDANTIHPVAwagididlkakeKFDWSEEIECGLRPAQKVIQTGDIIYVQD 2179
Cdd:pfam01590    1 DLEEILQTILEELRELLGADRCALYLPDADGLEYLPPGA------------RWLKAAGLEIPPGTGVTVLRTGRPLVVPD 68
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1085344563 2180 FSSDASLESWCQKALQRGYRSGMALPLKNENsQVFGVILIYSTnRNVITQDEIRLIEELANDLAFGI 2246
Cdd:pfam01590   69 AAGDPRFLDPLLLLRNFGIRSLLAVPIIDDG-ELLGVLVLHHP-RPPFTEEELELLEVLADQVAIAL 133
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
1639-1799 2.19e-08

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: 59.40  E-value: 2.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1639 EEALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDpawhfyredgtVLPleEYPVNYVL 1718
Cdd:COG3829      3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGKNVTE-----------LIP--NSPLLEVL 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1719 ATRKElrnyVVGVHRTNYKNDVWVLVNADPVWSNeNELTQVIVTFSDITMRKNAEVALKLSEERYRTLVEQAMDGIfIAD 1798
Cdd:COG3829     70 KTGKP----VTGVIQKTGGKGKTVIVTAIPIFED-GEVIGAVETFRDITELKRLERKLREEELERGLSAKYTFDDI-IGK 143

                   .
gi 1085344563 1799 S 1799
Cdd:COG3829    144 S 144
NtrB COG3852
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
547-680 2.20e-08

Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];


Pssm-ID: 443061 [Multi-domain]  Cd Length: 361  Bit Score: 58.70  E-value: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  547 ALQKAAEEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKmKFTDIITPKSLktFNENFPGFKEKGW-IK 625
Cdd:COG3852      1 ALRESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGR-PLAELFPEDSP--LRELLERALAEGQpVT 77
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1085344563  626 NLEFELIRKDGSILPILASATAIKDSDGNYLMSrSTVNDIAELKLAELQLRNSER 680
Cdd:COG3852     78 EREVTLRRKDGEERPVDVSVSPLRDAEGEGGVL-LVLRDITERKRLERELRRAEK 131
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1787-1890 2.93e-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 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: 53.96  E-value: 2.93e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1787 VEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTALAERNLIRNDGSLLP 1866
Cdd:pfam08448    1 LDSLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEERH 80
                           90       100
                   ....*....|....*....|....*....
gi 1085344563 1867 VEISGIMLPDKR-----FLGIVRDITERK 1890
Cdd:pfam08448   81 YELRLTPLRDPDgevigVLVISRDITERR 109
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
2435-2537 3.22e-08

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 58.76  E-value: 3.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLN-LLSNAIKY---SPKGGKIELTIKQLRGKMVISVKDKGIGIPTDdlkhlFEPfhraknttdISGTGLGLSIVKRAV 2510
Cdd:COG3920    402 LILNeLVTNALKHaflSGEGGRIRVSWRREDGRLRLTVSDNGVGLPED-----VDP---------PARKGLGLRLIRALV 467
                           90       100
                   ....*....|....*....|....*..
gi 1085344563 2511 DLHNGIITVKSElnAGTTFTVKIPLEQ 2537
Cdd:COG3920    468 RQLGGTLELDRP--EGTRVRITFPLAE 492
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
1779-1901 4.32e-08

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 58.92  E-value: 4.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1779 SEERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGK--TALAERN 1856
Cdd:PRK09776   281 SETRFRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSGEinSYSMEKR 360
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 1857 LIRNDG----SLLPVEI----SGIMLpdkRFLGIVRDITERKKNE---AALNERIK 1901
Cdd:PRK09776   361 YYRRDGevvwALLAVSLvrdtDGTPL---YFIAQIEDINELKRTEqvnERLMERIT 413
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
1135-1224 4.73e-08

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: 52.85  E-value: 4.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1135 VFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIpsfYETRGRKRDGSEFDFEINISTYELNGEI 1214
Cdd:pfam13426    5 IYVNDAALRLLGYTR-EELLGKSITDLFAEPEDSERLREALREGKAVRE---FEVVLYRKDGEPFPVLVSLAPIRDDGGE 80
                           90
                   ....*....|..
gi 1085344563 1215 YTL--ANIRDIT 1224
Cdd:pfam13426   81 LVGiiAILRDIT 92
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
1386-1541 6.61e-08

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 58.06  E-value: 6.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1386 RILRKREYEfRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIREL-NPDGSFESYaqaVDNALASGENS 1464
Cdd:PRK11360   256 ALRETRSLN-ELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKPYSELfPPNTPFASP---LLDTLEHGTEH 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1465 -ELEILVPNPNNEqivhqIRIIAE----RDEQNKVTSVLAIGRDITERKRAEEtikkseaQLNEAQRIAQIGSWELDIAN 1539
Cdd:PRK11360   332 vDLEISFPGRDRT-----IELSVStsllHNTHGEMIGALVIFSDLTERKRLQR-------RVARQERLAALGELVAGVAH 399

                   ..
gi 1085344563 1540 NI 1541
Cdd:PRK11360   400 EI 401
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
1904-2084 7.12e-08

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 54.90  E-value: 7.12e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1904 QSLLRLSKNLEFAQTYSQALTAALNEIKNILGYKTVWVYLLSEDKKYFNALVARGDFEDIVmspeGTLILPIeGDRMLEE 1983
Cdd:COG3605      4 KALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSIYLLDPDGGRLELRATEGLNPEAV----GKVRLPL-GEGLVGL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1984 IAEAKEIVIVEDARADER--TNKKIVETlGNRTIINVPIYLLDKHLGTVGTGTFSdegVRIPTRSEKEFLLAMASHLAVT 2061
Cdd:COG3605     79 VAERGEPLNLADAASHPRfkYFPETGEE-GFRSFLGVPIIRRGRVLGVLVVQSRE---PREFTEEEVEFLVTLAAQLAEA 154
                          170       180
                   ....*....|....*....|...
gi 1085344563 2062 LDRLHLLVERQEAEKALLRLNRE 2084
Cdd:COG3605    155 IANAELLGELRAALAELSLAREE 177
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1531-1632 7.45e-08

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: 52.64  E-value: 7.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1531 GSWELDIANNILRWSDEIFRIFEIDPKEF-GSSYEAFlnaIHPDDREVVNTAYSNSLVNRTPYAIDHRLRFDDGRIKFVH 1609
Cdd:cd00130      4 GVIVLDLDGRILYANPAAEQLLGYSPEELiGKSLLDL---IHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
                           90       100
                   ....*....|....*....|...
gi 1085344563 1610 EQCETIYNEENKPLRSIGTVQDI 1632
Cdd:cd00130     81 VSLTPIRDEGGEVIGLLGVVRDI 103
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1792-1886 8.62e-08

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: 52.25  E-value: 8.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1792 DGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQQTTPIQFEKLRSGKTALA-ERNLIRNDGSLLPVEIS 1870
Cdd:cd00130      3 DGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTlEVRLRRKDGSVIWVLVS 82
                           90       100
                   ....*....|....*....|.
gi 1085344563 1871 GIMLPD-----KRFLGIVRDI 1886
Cdd:cd00130     83 LTPIRDeggevIGLLGVVRDI 103
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
669-811 8.98e-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: 57.29  E-value: 8.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  669 KLAELQLRNSEREFRTLAENLPDHIIRYDIDCRVIYLNHV-VAATNYTNSSLVGKLSaeIQFNEAKGLEEYNEKLRRVIK 747
Cdd:COG5809      4 SKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAaERIFGYTEDELLGTNI--LDFLHPDDEKELREILKLLKE 81
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085344563  748 TGTEDEMEIMLRDIEGNLHIHEVHFLAERDIEGKIVGALAIGHDISERKQAEEERQANLRFFEN 811
Cdd:COG5809     82 GESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERKRMEEALRESEEKFRL 145
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
444-540 1.00e-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: 51.69  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  444 DGKYEYISPAALTIFGYSPDDYYDNPL--LFKQSIHSDWIKYFeehwanLQKGILPQTYEYQIIHKSGEARWLNQRNILV 521
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSItdLFAEPEDSERLREA------LREGKAVREFEVVLYRKDGEPFPVLVSLAPI 74
                           90
                   ....*....|....*....
gi 1085344563  522 LDEGGNSVAIEGVVTDITE 540
Cdd:pfam13426   75 RDDGGELVGIIAILRDITE 93
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
2083-2271 1.13e-07

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 54.13  E-value: 1.13e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2083 RELKAISNCNQSLLRAEDEQSLLNEICRIICEEAGYDFAWVgYTEHSDANTIHPVAWAGIDIDLKAKEKFDWSEEIeCGL 2162
Cdd:COG3605      1 EMLKALRRISEAVASALDLDEALDRIVRRIAEALGVDVCSI-YLLDPDGGRLELRATEGLNPEAVGKVRLPLGEGL-VGL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2163 rpaqkVIQTGDIIYVQDFSSDASLeSWCQKALQRGYRSGMALPLKNENsQVFGVILIYSTNRNVITQDEIRLIEELANDL 2242
Cdd:COG3605     79 -----VAERGEPLNLADAASHPRF-KYFPETGEEGFRSFLGVPIIRRG-RVLGVLVVQSREPREFTEEEVEFLVTLAAQL 151
                          170       180
                   ....*....|....*....|....*....
gi 1085344563 2243 AFGIITLQTRAERKRVEKELELHRDHLQE 2271
Cdd:COG3605    152 AEAIANAELLGELRAALAELSLAREEERE 180
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
543-694 1.19e-07

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: 56.70  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  543 QAEQALQKAAEEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKmKFTDIITPKSLKTFnenfpgFKEKg 622
Cdd:COG3829      1 AEELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERILGLPREEVIGK-NVTELIPNSPLLEV------LKTG- 72
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085344563  623 wiKNLEFELIRKDGSILPILASATAIKDsDGNYLMSRSTVNDIAELKLAELQLRNSEREFRTLAENLPDHII 694
Cdd:COG3829     73 --KPVTGVIQKTGGKGKTVIVTAIPIFE-DGEVIGAVETFRDITELKRLERKLREEELERGLSAKYTFDDII 141
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
990-1098 1.31e-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: 51.87  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  990 ANVGYWERDFvNNKIIL-SDESCRIFGLQQENYHkeldewHKQWLQLILPEDKERAEKTAIDAVQKDIPYNLDYRIIRHN 1068
Cdd:cd00130      1 LPDGVIVLDL-DGRILYaNPAAEQLLGYSPEELI------GKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKD 73
                           90       100       110
                   ....*....|....*....|....*....|
gi 1085344563 1069 GELRYIHSEANVRRDSSGKPIFMLGMMQDI 1098
Cdd:cd00130     74 GSVIWVLVSLTPIRDEGGEVIGLLGVVRDI 103
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1647-1766 1.99e-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 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: 51.65  E-value: 1.99e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1647 EKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDPAWHFYREDGTVLpleeypVNYVLATRKELRN 1726
Cdd:pfam00989    1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAEL------LRQALLQGEESRG 74
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1085344563 1727 YVVGVhRTNYKNDVWVLVNADPVWSNENELTQVIVTFSDI 1766
Cdd:pfam00989   75 FEVSF-RVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
PAS_3 pfam08447
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
575-654 2.96e-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.


Pssm-ID: 430001 [Multi-domain]  Cd Length: 89  Bit Score: 50.42  E-value: 2.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  575 FVRINNTELKWLGYTLEEVIGK-MKFTDIITPKSLKTFNENFPGFKEKGWIKNLEFELIRKDGSILPILASATAIKDSDG 653
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKgESWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80

                   .
gi 1085344563  654 N 654
Cdd:pfam08447   81 K 81
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
1059-1101 3.28e-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: 48.72  E-value: 3.28e-07
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1085344563  1059 NLDYRIIRHNGELRYIHSEANVRRDSSGKPIFMLGMMQDITVR 1101
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
PRK13558 PRK13558
bacterio-opsin activator; Provisional
404-558 3.40e-07

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 56.00  E-value: 3.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  404 EFIESEA--ERRDAENALYLSE---ERFRRLAENAPD------VIYRMSLADGKYEYISPAALTIFGYSPDDYYDNPLLF 472
Cdd:PRK13558   119 ERIESAVpeHSRDTEARMPISDltvESDRRLKERALDeapvgiTIADATLPDEPLIYINDAFERITGYSPDEVLGRNCRF 198
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  473 KQSIHSDwikyfEEHWANLQKGIL---PQTYEYQIIHKSGEARWlNQRNIL-VLDEGGNSVAIEGVVTDITERKQAEQAL 548
Cdd:PRK13558   199 LQGEDTN-----EERVAELREAIDeerPTSVELRNYRKDGSTFW-NQVDIApIRDEDGTVTHYVGFQTDVTERKEAELAL 272
                          170
                   ....*....|
gi 1085344563  549 QKAAEEIRDL 558
Cdd:PRK13558   273 QRERRKLQRL 282
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
1412-1506 4.50e-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: 50.15  E-value: 4.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1412 NGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGEnsELEILVPNPNNEQIVHQIRIIAERDEQ 1491
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGKSITDLFAEPEDSERLREALREGKAVR--EFEVVLYRKDGEPFPVLVSLAPIRDDG 78
                           90
                   ....*....|....*
gi 1085344563 1492 NKVTSVLAIGRDITE 1506
Cdd:pfam13426   79 GELVGIIAILRDITE 93
RsbW COG2172
Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];
2439-2535 8.01e-07

Anti-sigma regulatory factor (Ser/Thr protein kinase) [Signal transduction mechanisms];


Pssm-ID: 441775 [Multi-domain]  Cd Length: 127  Bit Score: 50.30  E-value: 8.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2439 LLSNAIKYSPKG---GKIELTIKQLRGKMVISVKDKGIGIPTDDLKhlfEPFHraknttDISGTGLGLSIVKRAVDLhng 2515
Cdd:COG2172     42 AVTNAVRHAYGGdpdGPVEVELELDPDGLEIEVRDEGPGFDPEDLP---DPYS------TLAEGGRGLFLIRRLMDE--- 109
                           90       100
                   ....*....|....*....|
gi 1085344563 2516 iITVKSELNaGTTFTVKIPL 2535
Cdd:COG2172    110 -VEYESDPG-GTTVRLVKRL 127
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
1921-2062 1.12e-06

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 50.17  E-value: 1.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1921 QALTAALNEIKNILGYKTVWVYLLSEDKKYFNALVARGDFEDIVMSPEGTLIlpiegdrmleEIAEAKEIVIVEDARADE 2000
Cdd:pfam01590    4 EILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIPPGTGV----------TVLRTGRPLVVPDAAGDP 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085344563 2001 R--TNKKIVETLGNRTIINVPIYLLDKHLGTVgtgTFSDEGVRIpTRSEKEFLLAMASHLAVTL 2062
Cdd:pfam01590   74 RflDPLLLLRNFGIRSLLAVPIIDDGELLGVL---VLHHPRPPF-TEEELELLEVLADQVAIAL 133
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
672-801 1.26e-06

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: 53.62  E-value: 1.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  672 ELQLRNSEREFRTLAENLPDHIIRYDIDCRVIYLNHVVAA-TNYTNSSLVGKLSAEIqfneakgleEYNEKLRRVIKTGT 750
Cdd:COG3829      3 ELELKELEEELEAILDSLDDGIIVVDADGRITYVNRAAERiLGLPREEVIGKNVTEL---------IPNSPLLEVLKTGK 73
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1085344563  751 EDEMEIMlrdiegNLHIHEVHFLAER---DIEGKIVGALAIGHDISERKQAEEE 801
Cdd:COG3829     74 PVTGVIQ------KTGGKGKTVIVTAipiFEDGEVIGAVETFRDITELKRLERK 121
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
1517-1642 1.54e-06

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: 49.21  E-value: 1.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1517 SEAQLNEAQRIAQIGSWELDIANNILRWSDEIFRIFEIDPKEFGSSYeaFLNAIHPDDREVVNTAYSNSLVNR-TPYAID 1595
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRN--VLELIPEEDREEVRERIERRLEGEpEPVSEE 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1085344563 1596 HRLRFDDGRIKFVHEQcETIYNEENKPLRSIGTVQDITDRKLAEEAL 1642
Cdd:TIGR00229   79 RRVRRKDGSEIWVEVS-VSPIRTNGGELGVVGIVRDITERKEAEEAL 124
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
1645-1776 1.87e-06

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: 49.21  E-value: 1.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1645 SEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDPAWHFYREdgtvlPLEEYpvnyvLATRKEL 1724
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDRE-----EVRER-----IERRLEG 70
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1085344563 1725 RNYVVGVHRTNYKND---VWVLVNADPVWSNeNELTQVIVTFSDITMRKNAEVAL 1776
Cdd:TIGR00229   71 EPEPVSEERRVRRKDgseIWVEVSVSPIRTN-GGELGVVGIVRDITERKEAEEAL 124
PRK10618 PRK10618
phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional
2283-2537 2.31e-06

phosphotransfer intermediate protein in two-component regulatory system with RcsBC; Provisional


Pssm-ID: 236726 [Multi-domain]  Cd Length: 894  Bit Score: 53.40  E-value: 2.31e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2283 VNKKLiiefekekefermLQHSLEKEKELSELKsRFISTTSHEFRTPLTTVrvsAEMIQRYRKRWTEDKLDVFLDKIKNS 2362
Cdd:PRK10618   432 VNKKL-------------QQAQREYEKNQQARK-AFLQNIGDELKQPLQSL---AQLAAQLRQTSDEEQQQPELDQLAEQ 494
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2363 VDYLTKLLDDVLTISRSESGKIVLNREEIDLHEFCLDVIEEA--KISAtEAHKLIFNFTLK-KIHYRLDPKLMKFILLNL 2439
Cdd:PRK10618   495 SDVLVRLVDNIQLLNMLETQDWKPEQELFSLQDLIDEVLPEVlpAIKR-KGLQLLIHNHLKaEQLRIGDRDALRKILLLL 573
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2440 LSNAIKYSPKgGKIELTI---KQLRGKMVISVKDKGIGIPTDDLKHLFEPF-HRAKNTTDISGTGLGLSIVKRAVDLHNG 2515
Cdd:PRK10618   574 LNYAITTTAY-GKITLEVdqdESSPDRLTIRILDTGAGVSIKELDNLHFPFlNQTQGDRYGKASGLTFFLCNQLCRKLGG 652
                          250       260
                   ....*....|....*....|..
gi 1085344563 2516 IITVKSELNAGTTFTVKIPLEQ 2537
Cdd:PRK10618   653 HLTIKSREGLGTRYSIHLKMLA 674
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
1105-1233 2.43e-06

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: 52.47  E-value: 2.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1105 EESLLESETKLRIMFENSRDA-LGVSKKGVHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENvKRRDSGEei 1183
Cdd:COG3829      3 ELELKELEEELEAILDSLDDGiIVVDADGRITYVNRAAERILGLPR-EEVIGKNVTELIPNSPLLEVLKT-GKPVTGV-- 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1085344563 1184 psFYETRGRKRdgsefdfEINISTYEL--NGEI-YTLANIRDITSRKLLEKSL 1233
Cdd:COG3829     79 --IQKTGGKGK-------TVIVTAIPIfeDGEViGAVETFRDITELKRLERKL 122
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
1376-1512 2.54e-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: 52.66  E-value: 2.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1376 AAELERDRSDriLRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFesyAQAVD 1455
Cdd:COG5000     75 TDQLKEQREE--LEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDL---AELLR 149
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1085344563 1456 NALASGENSELEIlvpnPNNEQIVHQIRIIAERDEqnkvtSVLAIGRDITERKRAEE 1512
Cdd:COG5000    150 EALERGWQEEIEL----TRDGRRTLLVRASPLRDD-----GYVIVFDDITELLRAER 197
PAS_8 pfam13188
PAS domain; PAS domains are involved in many signalling proteins where they are used as a ...
1781-1835 2.69e-06

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: 46.77  E-value: 2.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1085344563 1781 ERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQDLIPAEEQ 1835
Cdd:pfam13188    1 ERLRALFESSPDGILVLDEGGRIIYVNPAALELLGYELLGELLGELLDLLDPLLE 55
PAS cd00130
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1656-1766 2.98e-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: 48.01  E-value: 2.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1656 IQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDPAWHFYREDgtvlpLEEYpVNYVLATRKELRNYVVGVHRTN 1735
Cdd:cd00130      1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREE-----LRER-LENLLSGGEPVTLEVRLRRKDG 74
                           90       100       110
                   ....*....|....*....|....*....|.
gi 1085344563 1736 YKndVWVLVNADPVWSNENELTQVIVTFSDI 1766
Cdd:cd00130     75 SV--IWVLVSLTPIRDEGGEVIGLLGVVRDI 103
PAS_9 pfam13426
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ...
1666-1767 4.33e-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: 4.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1666 DTQILICNHSAEILLGLSEDQLLGKkaidPAWHFYREDGTVLPLEEypvnyVLATRKELRNYVVgVHRTNYKNDVWVLVN 1745
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGK----SITDLFAEPEDSERLRE-----ALREGKAVREFEV-VLYRKDGEPFPVLVS 70
                           90       100
                   ....*....|....*....|..
gi 1085344563 1746 ADPVWSNENELTQVIVTFSDIT 1767
Cdd:pfam13426   71 LAPIRDDGGELVGIIAILRDIT 92
nifL_nitrog TIGR02938
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ...
2299-2535 4.45e-06

nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation positive regulator protein NifA, and is therefore a negative regulator. It binds NifA. NifA and NifL are encoded by adjacent genes. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, Protein interactions]


Pssm-ID: 131984 [Multi-domain]  Cd Length: 494  Bit Score: 51.83  E-value: 4.45e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2299 RMLQHSLEKEKELSELKSRFiSTTSHEFRTPLTTVRVSAEMIQRYRKRWTEDKLDVFLDKIKNSVDYLTKLLDDVLTISR 2378
Cdd:TIGR02938  261 SALQALMAEEERLEAIRETL-SAAIHRLQGPMNLISAAISVLQRRGDDAGNPASAAMLQQALSAGREHMEALRQVIPQSP 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2379 SESGKIV-LNREEIDLHEFCLDVIEEAKISATEAHKLifnfTLKKIHYRldPKLMKFILLNLLSNAIKYSPKGG--KIEL 2455
Cdd:TIGR02938  340 QEIVVPVnLNQILRDVITLSTPRLLAAGIVVDWQPAA----TLPAILGR--ELQLRSLFKALVDNAIEAMNIKGwkRREL 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2456 TI-KQLRGKMV-ISVKDKGIGIPTDDLKHLFEPFHRAKNTTDIsGTGLGLSIVKRAVDLHNGIITVKSELNAGTTFTVKI 2533
Cdd:TIGR02938  414 SItTALNGDLIvVSILDSGPGIPQDLRYKVFEPFFTTKGGSRK-HIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIVEF 492

                   ..
gi 1085344563 2534 PL 2535
Cdd:TIGR02938  493 RV 494
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1531-1632 5.90e-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: 47.41  E-value: 5.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1531 GSWELDIANNILRWSDEIFRIFEIDPKE-FGSSYeafLNAIHPDDREVVNTAYSNSLVNRTPY-AIDHRLRFDDGRIKFV 1608
Cdd:pfam00989   13 GIFVVDEDGRILYVNAAAEELLGLSREEvIGKSL---LDLIPEEDDAEVAELLRQALLQGEESrGFEVSFRVPDGRPRHV 89
                           90       100
                   ....*....|....*....|....
gi 1085344563 1609 HEQCETIYNEENKPLRSIGTVQDI 1632
Cdd:pfam00989   90 EVRASPVRDAGGEILGFLGVLRDI 113
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1647-1694 5.95e-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: 45.85  E-value: 5.95e-06
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*...
gi 1085344563  1647 EKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAID 1694
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLE 48
GAF_2 pfam13185
GAF domain; The GAF domain is named after some of the proteins it is found in, including ...
1916-2063 5.96e-06

GAF domain; The GAF domain is named after some of the proteins it is found in, including cGMP-specific phosphodiesterases, adenylyl cyclases and FhlA. It is also found in guanylyl cyclases and phytochromes. The structure of a GAF domain shows that the domain shares a similar fold with the PAS domain. This domain can bind O2, CO and NO (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433019 [Multi-domain]  Cd Length: 137  Bit Score: 48.23  E-value: 5.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1916 AQTYSQALTAALNEIKNILGYKTVWVYLLSEDKKYFNALVARGDFEDIVMSPEGtlilpiEGdrMLEEIAEAKEIVIVED 1995
Cdd:pfam13185    1 AADLEELLDAVLEAAVELGASAVGFILLVDDDGRLAAWGGAADELSAALDDPPG------EG--LVGEALRTGRPVIVND 72
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 1996 ARADERTNKKIVETLGNRTIINVPIYLLDKHLGTVGtgtFSDEGVRIPTRSEKEFLLAMASHLAVTLD 2063
Cdd:pfam13185   73 LAADPAKKGLPAGHAGLRSFLSVPLVSGGRVVGVLA---LGSNRPGAFDEEDLELLELLAEQAAIAIE 137
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
556-675 6.09e-06

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: 47.67  E-value: 6.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  556 RDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKmKFTDIITP----KSLKTFNENFPGFKEkgwIKNLEFEL 631
Cdd:TIGR00229    6 RAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGR-NVLELIPEedreEVRERIERRLEGEPE---PVSEERRV 81
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1085344563  632 IRKDGSILPILASATAIkDSDGNYLMSRSTVNDIAELKLAELQL 675
Cdd:TIGR00229   82 RRKDGSEIWVEVSVSPI-RTNGGELGVVGIVRDITERKEAEEAL 124
GAF COG2203
GAF domain [Signal transduction mechanisms];
1246-1688 6.63e-06

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 51.73  E-value: 6.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1246 ENFFDSLAQFLGENLDMDYVVVDKLDDNPEIAETIALYAKgSIVPNIRYALKGTPCENVMGRQ----LCFYPKEVQKLFP 1321
Cdd:COG2203    209 EELLQRILELAGELLGADRGAILLVDEDGGELELVAAPGL-PEEELGRLPLGEGLAGRALRTGepvvVNDASTDPRFAPS 287
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1322 DDKLLLEMGVDSYMGIPLWDSfGKPIGLIALMSSKSHPEDSIAIQVLQLVATRAAAELERDRSDRILRKREYEFRTLAES 1401
Cdd:COG2203    288 LRELLLALGIRSLLCVPLLVD-GRLIGVLALYSKEPRAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELAL 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1402 LpdniVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGENSELEILVPNPNNEQIVHQ 1481
Cdd:COG2203    367 L----RLLLDLELTLLRLRQLLLELLLALLLLLSLLGAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVL 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1482 IRIIAERDEQNKVTSVLAIGRDITERKRAEETIKKSEAQLNEAQRIAQIGSWELDIANNILRWSDEIFRIFEIDPKEFGS 1561
Cdd:COG2203    443 RRLLLGDEEGLVLLLALAELELLEILELLVLLAVILLALALLAALLLLLLLLLALLALSALAVLASLLLALLLLLLLLLL 522
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1562 SYEAFLNAIHPDDREVVNTAYSNSLVNRTPYAIDHRLRFDDGRIKFVHEQCETIYNEENKPLRSIGTVQDITDRKLAEEA 1641
Cdd:COG2203    523 LLLLGLLAALAADLLLLAAALLEDLLILLLVLLLERELLTLVGVLLLLGLSVLLIELALALILALALLELLLVAVGDLLL 602
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 1085344563 1642 LKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLL 1688
Cdd:COG2203    603 LERDLLLLLVLLVRLLLELLVVTLELTVLVVLAAVEDSALLLRLALA 649
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
1246-1379 9.21e-06

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 47.47  E-value: 9.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1246 ENFFDSLAQFLGENLDMDYVVVDKLDDNPEIAETIALYAKGSIVPNIRYalkGTPCENVM-GRQLCFYPKEVQKLFPDDK 1324
Cdd:pfam01590    3 EEILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLEIPP---GTGVTVLRtGRPLVVPDAAGDPRFLDPL 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563 1325 LLLE-MGVDSYMGIPLWDSfGKPIGLIALmSSKSHPEDSIAIQVLQLVATRAAAEL 1379
Cdd:pfam01590   80 LLLRnFGIRSLLAVPIIDD-GELLGVLVL-HHPRPPFTEEELELLEVLADQVAIAL 133
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
424-493 1.06e-05

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: 45.08  E-value: 1.06e-05
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563   424 ERFRRLAENAPDVIYRmSLADGKYEYISPAALTIFGYSPDDYYDNPLLfkQSIHSDWIKYFEEHWANLQK 493
Cdd:smart00091    1 ERLRAILESLPDGIFV-LDLDGRILYANPAAEELLGYSPEELIGKSLL--ELIHPEDRERVQEALQRLLS 67
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1393-1504 1.19e-05

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: 46.64  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1393 YEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALASGENSE-LEILVP 1471
Cdd:pfam00989    1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRgFEVSFR 80
                           90       100       110
                   ....*....|....*....|....*....|...
gi 1085344563 1472 NPNNEQIVHQIRIIAERDEQNKVTSVLAIGRDI 1504
Cdd:pfam00989   81 VPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1394-1459 1.44e-05

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: 1.44e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1085344563  1394 EFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIRELNPDGSFESYAQAVDNALA 1459
Cdd:smart00091    2 RLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQRLLS 67
GAF_3 pfam13492
GAF domain;
2100-2246 2.09e-05

GAF domain;


Pssm-ID: 433253 [Multi-domain]  Cd Length: 129  Bit Score: 46.21  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2100 DEQSLLNEICRIICEEAGYDF-AWVGYTEhsDANTIHPVAwagididlKAKEKFDWSEEIECGLRPAQKVIQTGDIIYVQ 2178
Cdd:pfam13492    1 SLDEILEALLKLLVRLLGAERaAVYLLDE--DGNKLQVAA--------GYDGEPDPSESLDADSPLARRALSSGEPISGL 70
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 2179 DFSSDASLESwcqkalqrgyRSGMALPLKNEnSQVFGVILIYSTNRNVITQDEIRLIEELANDLAFGI 2246
Cdd:pfam13492   71 GSAGEDGLPD----------GPALVVPLVAG-RRVIGVLALASSKPRAFDAEDLRLLESLAAQIATAI 127
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1925-2071 2.37e-05

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.61  E-value: 2.37e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  1925 AALNEIKNILGYKTVWVYLLSEDKKYFNALVARGDFEDIVMSPEGTLILPIEGdrmleEIAEAKEIVIVEDARADERTNK 2004
Cdd:smart00065    8 TILEELRQLLGADRVLIYLVDENDRGELVLVAADGLTLPTLGIRFPLDEGLAG-----RVAETGRPLNIPDVEADPLFAE 82
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563  2005 KIVE-TLGNRTIINVPIYLLDKHLGTVGTgtFSDEGVRIPTRSEKEFLLAMASHLAVTLDrLHLLVER 2071
Cdd:smart00065   83 DLLGrYQGVRSFLAVPLVADGELVGVLAL--HNKKSPRPFTEEDEELLQALANQLAIALA-NAQLYEE 147
PtsP COG3605
Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];
248-425 3.03e-05

Signal transduction protein containing GAF and PtsI domains [Signal transduction mechanisms];


Pssm-ID: 442824 [Multi-domain]  Cd Length: 188  Bit Score: 47.20  E-value: 3.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  248 LSNINQAIVRIRNTKEVFDEACRIATEygkfTMVW----IGIINAKNNKVDVAASSGVESSYLDNLVIDLNDvqrssGPT 323
Cdd:COG3605      6 LRRISEAVASALDLDEALDRIVRRIAE----ALGVdvcsIYLLDPDGGRLELRATEGLNPEAVGKVRLPLGE-----GLV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  324 GIAIRTGKHKISNNIIDDDSMLlWKNEAIQYGYKSTASFPLIVFGKVVGAFCIYSDELNFFEDDDVVLLDEMVkdiSFAM 403
Cdd:COG3605     77 GLVAERGEPLNLADAASHPRFK-YFPETGEEGFRSFLGVPIIRRGRVLGVLVVQSREPREFTEEEVEFLVTLA---AQLA 152
                          170       180
                   ....*....|....*....|....*..
gi 1085344563  404 EFIES-----EAERRDAENALYLSEER 425
Cdd:COG3605    153 EAIANaellgELRAALAELSLAREEER 179
COG4192 COG4192
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ...
2428-2526 3.09e-05

Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];


Pssm-ID: 443346 [Multi-domain]  Cd Length: 640  Bit Score: 49.30  E-value: 3.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2428 DPKLMKFILLNLLSNAIKYSPKGGKIELTIKQLRGKMVISVKDKGIGIPtdDLKHLFEPFhrakNTTDISGTGLGLSIVK 2507
Cdd:COG4192    540 DQVLLEQVLVNLLVNALDAVATQPQISVDLLSNAENLRVAISDNGNGWP--LVDKLFTPF----TTTKEVGLGLGLSICR 613
                           90
                   ....*....|....*....
gi 1085344563 2508 RAVDLHNGIITVKSELNAG 2526
Cdd:COG4192    614 SIMQQFGGDLYLASTLERG 632
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1114-1176 3.38e-05

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: 43.93  E-value: 3.38e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085344563  1114 KLRIMFENSRDAL-GVSKKGVHVFANPAYLKLFGYEKlEEIVGTSILECIAPSHHQQIIENVKR 1176
Cdd:smart00091    2 RLRAILESLPDGIfVLDLDGRILYANPAAEELLGYSP-EELIGKSLLELIHPEDRERVQEALQR 64
HATPase_LytS-like cd16957
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2434-2534 3.71e-05

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Bacillus subtilis LytS and Staphylococcus aureus LytS; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Bacillus subtilis LytS, a HK of the two-component system (TCS) LytS-LytR needed for growth on pyruvate, and Staphylococcus aureus LytS-LytR TCS involved in the adaptation of S. aureus to cationic antimicrobial peptides. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and a GAF sensor domain; most contain a DUF3816 domain.


Pssm-ID: 340433 [Multi-domain]  Cd Length: 106  Bit Score: 44.72  E-value: 3.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2434 FILLNLLSNAIKYSPK----GGKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFE-PFHRAKnttdisGTGLGLSIVKR 2508
Cdd:cd16957      4 FALQVLVENAIRHAFPkrkeNNEVRVVVKKDQHKVHVSVSDNGQGIPEERLDLLGKtTVTSEK------GTGTALENLNR 77
                           90       100
                   ....*....|....*....|....*....
gi 1085344563 2509 AVDL---HNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16957     78 RLIGlfgSEACLHIESEVHGGTEVWFVIP 106
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
1246-1389 3.75e-05

Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these domains in PDE6B result in autosomal recessive inheritance of retinitis pigmentosa.


Pssm-ID: 214500 [Multi-domain]  Cd Length: 149  Bit Score: 46.22  E-value: 3.75e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  1246 ENFFDSLAQFLGENLDMDYVVVDKLDDNPE-IAETIALYAKGSIVPNIRYAL-KGTPCENVMGRQLCFYPkEVQK--LFP 1321
Cdd:smart00065    3 EELLQTILEELRQLLGADRVLIYLVDENDRgELVLVAADGLTLPTLGIRFPLdEGLAGRVAETGRPLNIP-DVEAdpLFA 81
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085344563  1322 DDKLLLEMGVDSYMGIPLWDSfGKPIGLIALMSSKS----HPEDsiaIQVLQLVATRAAAELERDRSDRILR 1389
Cdd:smart00065   82 EDLLGRYQGVRSFLAVPLVAD-GELVGVLALHNKKSprpfTEED---EELLQALANQLAIALANAQLYEELR 149
KinA COG5805
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ...
956-1117 3.80e-05

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: 48.96  E-value: 3.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  956 LKEISTRLTDGLTSLLTLRNLSESERRLTEAQRIANVGYW----ERDFV-----NNKIILSDESC-RIFGLQQENYHKel 1025
Cdd:COG5805    122 VKLFPIYNQNGQAAILALRDITKKKKIEEILQEQEERLQTlienSPDLIcvidtDGRILFINESIeRLFGAPREELIG-- 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1026 dewhKQWLQLILPEDKERAEK--TAIDAVQKDIPYNldYRIIRHNGELRYIHSEANVRRDSSGKPIFMLGMMQDITVRKR 1103
Cdd:COG5805    200 ----KNLLELLHPCDKEEFKEriESITEVWQEFIIE--REIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKE 273
                          170
                   ....*....|....
gi 1085344563 1104 AEESLLESEtKLRI 1117
Cdd:COG5805    274 AEELMARSE-KLSI 286
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1119-1227 3.88e-05

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: 45.10  E-value: 3.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1119 FENSRDALGV-SKKGVHVFANPAYLKLFGYEkLEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIPSFYETRGRKRDGS 1197
Cdd:pfam08448    1 LDSLPDALAVlDPDGRVRYANAAAAELFGLP-PEELLGKTLAELLPPEDAARLERALRRALEGEEPIDFLEELLLNGEER 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1085344563 1198 EFDFEINISTYELNGEIYTLANIRDITSRK 1227
Cdd:pfam08448   80 HYELRLTPLRDPDGEVIGVLVISRDITERR 109
sensory_box TIGR00229
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ...
979-1108 3.89e-05

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: 45.36  E-value: 3.89e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  979 SERRLTEAQRIANVGYWERDfVNNKIIL-SDESCRIFGLQQEnyhkELDEwhKQWLQLILPEDKERAEKTAIDAVQKDI- 1056
Cdd:TIGR00229    1 SEERYRAIFESSPDAIIVID-LEGNILYvNPAFEEIFGYSAE----ELIG--RNVLELIPEEDREEVRERIERRLEGEPe 73
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1085344563 1057 PYNLDYRIIRHNGELRYIhsEANVRR-DSSGKPIFMLGMMQDITVRKRAEESL 1108
Cdd:TIGR00229   74 PVSEERRVRRKDGSEIWV--EVSVSPiRTNGGELGVVGIVRDITERKEAEEAL 124
GAF COG2203
GAF domain [Signal transduction mechanisms];
627-1128 4.51e-05

GAF domain [Signal transduction mechanisms];


Pssm-ID: 441805 [Multi-domain]  Cd Length: 712  Bit Score: 49.04  E-value: 4.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  627 LEFELIRKDGSILPILASATAIKDSDGNYLMSRSTVNDIAELKLAELQLRNSEREFRTLAENLPDHIIRYDIDCRVIYLN 706
Cdd:COG2203     16 AELLEELATLLLALLLLALQALERVLETTELALALELLLERLTELRAAARLAAEAAEAALLLILLIDALVLLSLVATAGL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  707 HVVAATNYTNSSLVGKLSAEIQFNEAKGLEEYNEKLRRVIKTGTEDEMEIMLRDIEGNLHIHEVHFLAERDIEGKIVGAL 786
Cdd:COG2203     96 VLELADLLLLLRLLALLVLLLVALALAEALAARLLDLLLLGLGGRLRGVVLRGLRSAALLLSRVDTDLVGQLAALAGLIL 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  787 AIGHDISERKQAEEERQANLRffenmdRINRAIQEANNVEQMMSDVLDIILSTFDCDRAsFIYPCDIEASSWKVPIERTK 866
Cdd:COG2203    176 DIARLLTQRARLELERLALLN------EISQALRSALDLEELLQRILELAGELLGADRG-AILLVDEDGGELELVAAPGL 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  867 PEhPGAMILGVEIPVDSEAIRVFKAVLAACYPVGFGPgneEPLPQKVSESFNIKSQLAISLHPKiDKPW-MFVLHQcSRN 945
Cdd:COG2203    249 PE-EELGRLPLGEGLAGRALRTGEPVVVNDASTDPRF---APSLRELLLALGIRSLLCVPLLVD-GRLIgVLALYS-KEP 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  946 RSWTSEEKKLLKEISTRLTDGLTSLLTLRNLSESERRLTEAQRIANvgywERDFVNNKIILSDESCRIFGLQQENYHKEL 1025
Cdd:COG2203    323 RAFTEEDLELLEALADQAAIAIERARLYEALEAALAALLQELALLR----LLLDLELTLLRLRQLLLELLLALLLLLSLL 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1026 DEWHKQWLQLILPEDKERAEKTAIDAVQKDIPYNLDYRIIRHNGELRYIHSEANVRRDSSGKPIFMLGMMQDITVRKRAE 1105
Cdd:COG2203    399 GAELLLLLLDAADLSGLLALEGLLLLDLLLLLLLLRRILLLRVLRRLLLGDEEGLVLLLALAELELLEILELLVLLAVIL 478
                          490       500
                   ....*....|....*....|...
gi 1085344563 1106 ESLLESETKLRIMFENSRDALGV 1128
Cdd:COG2203    479 LALALLAALLLLLLLLLALLALS 501
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
1113-1223 5.13e-05

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: 44.72  E-value: 5.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1113 TKLRIMFENSRDA-LGVSKKGVHVFANPAYLKLFGYeKLEEIVGTSILECIAPSHHQQIIENVKRRDSGEEIPSFYETRG 1191
Cdd:pfam00989    1 EDLRAILESLPDGiFVVDEDGRILYVNAAAEELLGL-SREEVIGKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVSF 79
                           90       100       110
                   ....*....|....*....|....*....|....
gi 1085344563 1192 RKRDGSEFDFEINISTYELNGE--IYTLANIRDI 1223
Cdd:pfam00989   80 RVPDGRPRHVEVRASPVRDAGGeiLGFLGVLRDI 113
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
553-665 6.87e-05

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: 44.33  E-value: 6.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  553 EEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKMKFTDIITPKSLKT---FNENFPGFKEKgwiKNLEF 629
Cdd:pfam00989    1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGKSLLDLIPEEDDAEVaelLRQALLQGEES---RGFEV 77
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1085344563  630 ELIRKDGSILPILASATAIKDSDGNYLMSRSTVNDI 665
Cdd:pfam00989   78 SFRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
dpiB PRK15053
sensor histidine kinase DpiB; Provisional
2427-2534 8.22e-05

sensor histidine kinase DpiB; Provisional


Pssm-ID: 185013 [Multi-domain]  Cd Length: 545  Bit Score: 47.91  E-value: 8.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2427 LDPKLMKFILLNLLSNAIKYS---PKGGK-IELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKNTtDISGTGLG 2502
Cdd:PRK15053   428 LDSTEFAAIVGNLLDNAFEASlrsDEGNKiVELFLSDEGDDVVIEVADQGCGVPESLRDKIFEQGVSTRAD-EPGEHGIG 506
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1085344563 2503 LSIVKRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:PRK15053   507 LYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
424-538 9.27e-05

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: 43.95  E-value: 9.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  424 ERFRRLAENAPDVIYrMSLADGKYEYISPAALTIFGYSPDDYYdNPLLFKQSIHSDWIKYFEEHWANLQKGILPQTYEYQ 503
Cdd:pfam00989    1 EDLRAILESLPDGIF-VVDEDGRILYVNAAAEELLGLSREEVI-GKSLLDLIPEEDDAEVAELLRQALLQGEESRGFEVS 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1085344563  504 IIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDI 538
Cdd:pfam00989   79 FRVPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
KinE COG5809
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ...
976-1113 1.51e-04

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: 46.89  E-value: 1.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  976 LSESERRLTeaqRIAN-----VGYWERDFvnNKIILSDESCRIFGLQQENYHkeldewHKQWLQLILPEDKERAEKTAID 1050
Cdd:COG5809    136 LRESEEKFR---LIFNhspdgIIVTDLDG--RIIYANPAACKLLGISIEELI------GKSILELIHSDDQENVAAFISQ 204
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085344563 1051 AVQKDIPYNLDYRIIRHNGELRYIHSEANvRRDSSGKPIFMLGMMQDITVRKRAEESLLESET 1113
Cdd:COG5809    205 LLKDGGIAQGEVRFWTKDGRWRLLEASGA-PIKKNGEVDGIVIIFRDITERKKLEELLRKSEK 266
HATPase_UhpB-NarQ-NarX-like cd16917
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2440-2534 1.83e-04

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli UhpB, NarQ and NarX, and Bacillus subtilis YdfH, YhcY and YfiJ; This family includes the histidine kinase-like ATPase (HATPase) domains of various histidine kinases (HKs) of two-component signal transduction systems (TCSs) such as Escherichia coli UhpB, a HK of the UhpB-UhpA TCS, NarQ and NarX, HKs of the NarQ-NarP and NarX-NarL TCSs, respectively, and Bacillus YdfH, YhcY and YfiJ HKs, of the YdfH-YdfI, YhcY-YhcZ and YfiJ-YfiK TCSs, respectively. In addition, it includes Bacillus YxjM, ComP, LiaS and DesK, HKs of the YxjM-YxjML, ComP-ComA, LiaS-LiaR, DesR-DesK TCSs, respectively. Proteins having this HATPase domain have a histidine kinase dimerization and phosphoacceptor domain; some have accessory domains such as GAF, HAMP, PAS and MASE sensor domains.


Pssm-ID: 340394 [Multi-domain]  Cd Length: 87  Bit Score: 42.16  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2440 LSNAIKYSPkGGKIELTIKQLRGKMVISVKDKGIGiptddlkhlFEPFHRAKnttdisGTGLGLSIVKRAVDLHNGIITV 2519
Cdd:cd16917      9 LTNALKHAG-ASRVRVTLSYTADELTLTVVDDGVG---------FDGPAPPG------GGGFGLLGMRERAELLGGTLTI 72
                           90
                   ....*....|....*
gi 1085344563 2520 KSELNAGTTFTVKIP 2534
Cdd:cd16917     73 GSRPGGGTRVTARLP 87
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
1750-1888 2.07e-04

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: 46.49  E-value: 2.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1750 WSNENELTQVIVTFSDITMR-KNAEVALKLSEERYRTLVEQAMDGIFIADSNGNYIDVNRSGCNMLGYTRDQLLKLRMQD 1828
Cdd:COG5000     58 VTGDDEIGELARAFNRMTDQlKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEE 137
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1829 LIPaeEQQTTPIQFEKLRSGKTALAERNLirndGSLLPVEISGIMLPDKRFLGIVRDITE 1888
Cdd:COG5000    138 LLP--ELDLAELLREALERGWQEEIELTR----DGRRTLLVRASPLRDDGYVIVFDDITE 191
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
974-1106 2.68e-04

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 46.59  E-value: 2.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  974 RNLSESERRLTEAQR-----IANVGYWERDFVNNKIIlsdesCRIFGLQQEnyhkELDEWHKQwlQLILPEDKERAEKTA 1048
Cdd:PRK09776   276 KHISESETRFRNAMEysaigMALVGTEGQWLQVNKAL-----CQFLGYSQE----ELRGLTFQ--QLTWPEDLNKDLQQV 344
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563 1049 IDAVQKDIP-YNLDYRIIRHNGELRYIHSEANVRRDSSGKPIFMLGMMQDITVRKRAEE 1106
Cdd:PRK09776   345 EKLLSGEINsYSMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKRTEQ 403
COG3920 COG3920
Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction ...
1360-1657 3.27e-04

Two-component sensor histidine kinase, HisKA and HATPase domains [Signal transduction mechanisms];


Pssm-ID: 443125 [Multi-domain]  Cd Length: 495  Bit Score: 46.05  E-value: 3.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1360 EDSIAIQVLQLVATRAAAELERDRSDRILRKREYEFRTLAESLPDNIVRYDRNGRTVYVNPILEKTLATGASAMIGTTIR 1439
Cdd:COG3920      9 LLLALAALLLLAALLLLAAALLLALLALLLLALLLLALLLASALLALLALSAAALAAALAVALAAAVGAAAALLALLVLL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1440 ELNPDGSFESYAQAVDNALASGENSELEILVPNPNNEQIVHQIRIIAERDEQNKVTSVLAIGRDITERKRAEETIKKSEA 1519
Cdd:COG3920     89 LLLLLAAAALALALLLAALAGLLLLAALLLLRLVALLAALALLALLLLLLLLLAILALAELAVALAELAAALLLLAEELA 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1520 QLNEAQRIAQIGSWELDIannILRWSDEIFRIFEIDPKEFGSSYEAFLNAIHPDDREVVNTAYSNSLVNRTPYAIDHRLR 1599
Cdd:COG3920    169 ALRLAAAALLLLLAALLD---LGLALAALAAAALLALLLALELLLALLLLLLLLLALLLVLLAALLRLRAAVLEELERRR 245
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1085344563 1600 FDDGRIKFVHEQCETIYNEENKPLRSIGTVQDITDRKLAEEALKESEEKYRTLIQKIQ 1657
Cdd:COG3920    246 RARGLGRLLLLLLLLLLLLRALLLLAAGIRLVITERKRAEEELEASLEEKELLLRELH 303
PRK13558 PRK13558
bacterio-opsin activator; Provisional
1769-1907 7.06e-04

bacterio-opsin activator; Provisional


Pssm-ID: 237426 [Multi-domain]  Cd Length: 665  Bit Score: 44.83  E-value: 7.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1769 RKNAEVALKLSE---ERYRTLVEQAMD----GIFIADSNGN---YIDVNRSGCNMLGYTRDQLLKLRMQDLipaEEQQTT 1838
Cdd:PRK13558   129 SRDTEARMPISDltvESDRRLKERALDeapvGITIADATLPdepLIYINDAFERITGYSPDEVLGRNCRFL---QGEDTN 205
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563 1839 PIQFEKLRSG-----KTALAERNLiRNDGSLL--PVEISGIMLPDKR---FLGIVRDITERKKNEAALNERIKHSQSLL 1907
Cdd:PRK13558   206 EERVAELREAideerPTSVELRNY-RKDGSTFwnQVDIAPIRDEDGTvthYVGFQTDVTERKEAELALQRERRKLQRLL 283
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
626-665 7.09e-04

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: 39.47  E-value: 7.09e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|
gi 1085344563   626 NLEFELIRKDGSILPILASATAIKDSDGNYLMSRSTVNDI 665
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDI 40
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
553-615 8.98e-04

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: 39.69  E-value: 8.98e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085344563   553 EEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKMkFTDIITPKSLKTFNENF 615
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKS-LLELIHPEDRERVQEAL 62
PDCD7 pfam16021
Programmed cell death protein 7;
947-1120 1.06e-03

Programmed cell death protein 7;


Pssm-ID: 464979 [Multi-domain]  Cd Length: 305  Bit Score: 43.56  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  947 SWTSEEKKLLkEISTRLTDGLTSLLTLRNLSESERRLTeaqRIANVGYWERDfvnnkiiLSDESCRIFGLQQEN---YHK 1023
Cdd:pfam16021   36 VWSESYSRAA-ELKHELQEKLLLLEDPELLESLKRKLE---RRQKKRLRRKR-------RKEERKEEKKEEQERraeREA 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1024 ELDEWHKQWLQLILPEDKERAEKTAIDAV-------QKDIPYNLDyrIIRHNGELRYIHSEANVRR----DSSGKPIFML 1092
Cdd:pfam16021  105 KIDKWRRKQIQEVEEKKRERELKLAADAVlsevrkkQADAKRMLD--ILRSLEKLRKLRKEAARRKgikpESECDEAFES 182
                          170       180
                   ....*....|....*....|....*...
gi 1085344563 1093 GMMQDITVRKRAEESLLESETKLRIMFE 1120
Cdd:pfam16021  183 HLEKLRSVWKKRTEEYSAEEKALKVMLE 210
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
642-800 1.07e-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: 44.18  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  642 LASAT-AIKDSDGNYLMSRSTVNDIAEL-----------KLAELQLRNSEREFRTLAENLPDHIIRYDIDCRVIYLNHVV 709
Cdd:COG5000     40 LAEATrAVAAGDLSVRLPVTGDDEIGELarafnrmtdqlKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAA 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  710 AA-TNYTNSSLVGKLSAEIQfneakGLEEYNEKLRRVIKTGTEDEMEIMlRDIEGNLHIHEVHFLAErdiegkivGALAI 788
Cdd:COG5000    120 ERlLGIPLEELIGKPLEELL-----PELDLAELLREALERGWQEEIELT-RDGRRTLLVRASPLRDD--------GYVIV 185
                          170
                   ....*....|..
gi 1085344563  789 GHDISERKQAEE 800
Cdd:COG5000    186 FDDITELLRAER 197
PAS pfam00989
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
680-792 1.12e-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: 40.86  E-value: 1.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  680 REFRTLAENLPDHIIRYDIDCRVIYLNHVVAA-TNYTNSSLVGKlSAEIQFNEAKGLEEYnEKLRRVIKTGTEDEMEIML 758
Cdd:pfam00989    1 EDLRAILESLPDGIFVVDEDGRILYVNAAAEElLGLSREEVIGK-SLLDLIPEEDDAEVA-ELLRQALLQGEESRGFEVS 78
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1085344563  759 RDIEGNLHIH-EVHFLAERDIEGKIVGALAIGHDI 792
Cdd:pfam00989   79 FRVPDGRPRHvEVRASPVRDAGGEILGFLGVLRDI 113
PAS_4 pfam08448
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ...
431-543 1.36e-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 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: 40.48  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  431 ENAPDVIYRMSlADGKYEYISPAALTIFGYSPDDYYDNPL--LFKQSIHSDwikyFEEHWANLQKGILPQTYEyQIIHKS 508
Cdd:pfam08448    2 DSLPDALAVLD-PDGRVRYANAAAAELFGLPPEELLGKTLaeLLPPEDAAR----LERALRRALEGEEPIDFL-EELLLN 75
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1085344563  509 GEARWLNQRNILVLDEGGNSVAIEGVVTDITERKQ 543
Cdd:pfam08448   76 GEERHYELRLTPLRDPDGEVIGVLVISRDITERRR 110
HATPase_YpdA-like cd16955
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2429-2534 1.58e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) such as Escherichia coli YpdA, a HK of the two-component system (TCS) YpdA-YpdB which is involved in a nutrient sensing regulatory network with YehU-YehT. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), and some have a GAF sensor domain; some contain a DUF3816 domain; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.


Pssm-ID: 340431 [Multi-domain]  Cd Length: 102  Bit Score: 40.14  E-value: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2429 PKLMkfiLLNLLSNAIKY--SPKGGK--IELTI-KQLRGKMVISVKDKGIGIPTDDLKHLfepfhrakNTTDISGTGLGL 2503
Cdd:cd16955      2 PKLM---IQPLVENAIVHgiQEKKGKgvVKISVkKQLKNRLHIAVEDNGIGISPKVIERV--------EQDEMPGNKIGL 70
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1085344563 2504 SIV-KRAVDLHNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16955     71 LNVhQRLKLGYGEGLHIRSRPDPGTLIAFYIP 102
HATPase_YehU-like cd16956
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2434-2534 1.70e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YehU; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Escherichia coli YehU, a HK of the two-component system (TCS) YehU-YehT which is involved in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase); some have a GAF sensor domain while some have a cupin domain.


Pssm-ID: 340432 [Multi-domain]  Cd Length: 101  Bit Score: 40.11  E-value: 1.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2434 FILLNLLSNAIKYS----PKGGKIELTIKQLRGKMVISVKDKGIGiptddlkhlFEPFHRAKNTTDISGtGLGLSIV-KR 2508
Cdd:cd16956      4 LTLQPIVENAVKHGlsglLDGGRVEITARLDGQHLLLEVEDNGGG---------MDPDTLARILIRSSN-GLGLNLVdKR 73
                           90       100
                   ....*....|....*....|....*...
gi 1085344563 2509 AVDL--HNGIITVKSELNAGTTFTVKIP 2534
Cdd:cd16956     74 LRQAfgNDYGLDIECAPGEGTRITIRLP 101
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
263-403 1.89e-03

GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl cyclases, phytochromes, FhlA and NifA. Adenylyl and guanylyl cyclases catalyze ATP and GTP to the second messengers cAMP and cGMP, respectively, these products up-regulating catalytic activity by binding to the regulatory GAF domain(s). The opposite hydrolysis reaction is catalyzed by phosphodiesterase. cGMP-dependent 3',5'-cyclic phosphodiesterase catalyzes the conversion of guanosine 3',5'-cyclic phosphate to guanosine 5'-phosphate. Here too, cGMP regulates catalytic activity by GAF-domain binding. Phytochromes are regulatory photoreceptors in plants and bacteria which exist in two thermally-stable states that are reversibly inter-convertible by light: the Pr state absorbs maximally in the red region of the spectrum, while the Pfr state absorbs maximally in the far-red region. This domain is also found in FhlA (formate hydrogen lyase transcriptional activator) and NifA, a transcriptional activator which is required for activation of most Nif operons which are directly involved in nitrogen fixation. NifA interacts with sigma-54. This domain can bind biliverdine and phycocyanobilin (Matilla et al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460259 [Multi-domain]  Cd Length: 133  Bit Score: 40.93  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  263 EVFDEACRIATEYGKFTMVWIGIINAKNNKVDVAASSGVESSYLDnlvidlndvqRSSGPTGIAIRTGKHKISNNIIDDD 342
Cdd:pfam01590    4 EILQTILEELRELLGADRCALYLPDADGLEYLPPGARWLKAAGLE----------IPPGTGVTVLRTGRPLVVPDAAGDP 73
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1085344563  343 SMLLWKNEAIQYGYKSTASFPLIVFGKVVGAFCIYSDElNFFEDDDVVLLDEMVKDISFAM 403
Cdd:pfam01590   74 RFLDPLLLLRNFGIRSLLAVPIIDDGELLGVLVLHHPR-PPFTEEELELLEVLADQVAIAL 133
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
546-680 2.15e-03

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 43.42  E-value: 2.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  546 QALQKAAEEIRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEVIGKmKFTDIITPKS------LKTFnenfpgfk 619
Cdd:PRK11360   255 QALRETRSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGK-PYSELFPPNTpfasplLDTL-------- 325
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085344563  620 EKGW-IKNLEFELIRKDGSILpILASATAIKDSDGNYLMSRSTVNDIAELKLAELQLRNSER 680
Cdd:PRK11360   326 EHGTeHVDLEISFPGRDRTIE-LSVSTSLLHNTHGEMIGALVIFSDLTERKRLQRRVARQER 386
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
1631-1744 2.32e-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: 43.03  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1631 DITDR-KLAEEALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKAIDPAWHFYREDGTVLPL 1709
Cdd:COG5000     73 RMTDQlKEQREELEERRRYLETILENLPAGVIVLDADGRITLANPAAERLLGIPLEELIGKPLEELLPELDLAELLREAL 152
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1085344563 1710 EEYPVNYVLATRKELRNYVvgVHRTNYKNDVWVLV 1744
Cdd:COG5000    153 ERGWQEEIELTRDGRRTLL--VRASPLRDDGYVIV 185
PRK09776 PRK09776
putative diguanylate cyclase; Provisional
534-686 3.11e-03

putative diguanylate cyclase; Provisional


Pssm-ID: 182070 [Multi-domain]  Cd Length: 1092  Bit Score: 43.12  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  534 VVTDITERKQAEQALQKAAEE-IRDLYNNAPCGYHSLDKEGTFVRINNTELKWLGYTLEEViGKMKFTDIITPKSLKTFN 612
Cdd:PRK09776   263 IMTMVMYAFRAERKHISESETrFRNAMEYSAIGMALVGTEGQWLQVNKALCQFLGYSQEEL-RGLTFQQLTWPEDLNKDL 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563  613 ENFpgfkEK---GWIKN--LEFELIRKDGSILPILASATAIKDSDGNYLMSRSTVNDIAELKLAELQL-RNSERefRTLA 686
Cdd:PRK09776   342 QQV----EKllsGEINSysMEKRYYRRDGEVVWALLAVSLVRDTDGTPLYFIAQIEDINELKRTEQVNeRLMER--ITLA 415
PRK10935 PRK10935
nitrate/nitrite two-component system sensor histidine kinase NarQ;
2442-2537 3.86e-03

nitrate/nitrite two-component system sensor histidine kinase NarQ;


Pssm-ID: 236800 [Multi-domain]  Cd Length: 565  Bit Score: 42.53  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2442 NAIKYSpKGGKIELT-IKQLRGKMVISVKDKGIGIPtddlkHLFEPF-HraknttdisgtgLGLSIVK-RAVDLHnGIIT 2518
Cdd:PRK10935   482 NAIKHA-NASEIAVScVTNPDGEHTVSIRDDGIGIG-----ELKEPEgH------------YGLNIMQeRAERLG-GTLT 542
                           90
                   ....*....|....*....
gi 1085344563 2519 VKSELNAGTTFTVKIPLEQ 2537
Cdd:PRK10935   543 ISQPPGGGTTVSLTFPSQQ 561
HATPase_AgrC-ComD-like cd16935
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ...
2435-2533 3.94e-03

Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Staphylococcus aureus AgrC and Streptococcus pneumoniae ComD which are involved in quorum sensing; This family includes the histidine kinase-like ATPase (HATPase) domains of various two-component sensor histidine kinase (HKs) including Staphylococcus aureus AgrC which is an HK of the accessory gene regulator (agr) quorum sensing two-component regulatory system (TCS) AgrC-AgrA. The agr system plays a part in the transition from persistent to virulent phenotype. This family also includes Streptococcus pneumoniae ComD HK of the ComD-ComE TCS, involved in quorum sensing and genetic competence.


Pssm-ID: 340412 [Multi-domain]  Cd Length: 134  Bit Score: 39.87  E-value: 3.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2435 ILLNLLSNAI---KYSPKGGK-IELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEpfhraknTTDISGTGLGLSIVKRAV 2510
Cdd:cd16935     40 IFGNLLDNAIeacAKIDKENRfIHLKIRQKKGFLIISIENSYEGELKKKNGLFLS-------TKKDKNHGIGLKSIREIV 112
                           90       100
                   ....*....|....*....|...
gi 1085344563 2511 DLHNGIITVKSELNagtTFTVKI 2533
Cdd:cd16935    113 KKYNGNLSIEYENG---IFTLSI 132
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
1594-1635 4.13e-03

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: 37.16  E-value: 4.13e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|..
gi 1085344563  1594 IDHRLRFDDGRIKFVHEQCETIYNEENKPLRSIGTVQDITDR 1635
Cdd:smart00086    2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
1094-1223 4.24e-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: 42.26  E-value: 4.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1094 MMQDItvrKRAEESLLESETKLRIMFENSRDA-LGVSKKGVHVFANPAYLKLFGYEkLEEIVGTSILECIAPSHHQQIIE 1172
Cdd:COG5000     74 MTDQL---KEQREELEERRRYLETILENLPAGvIVLDADGRITLANPAAERLLGIP-LEELIGKPLEELLPELDLAELLR 149
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1085344563 1173 NVKRRDSGEEIPsfYETRGRKRdgsefdFEINISTYELNGEIYTLANIRDI 1223
Cdd:COG5000    150 EALERGWQEEIE--LTRDGRRT------LLVRASPLRDDGYVIVFDDITEL 192
PRK11360 PRK11360
two-component system sensor histidine kinase AtoS;
1640-1773 4.50e-03

two-component system sensor histidine kinase AtoS;


Pssm-ID: 236901 [Multi-domain]  Cd Length: 607  Bit Score: 42.26  E-value: 4.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 1640 EALKESEEKYRTLIQKIQTAVIVHTPDTQILICNHSAEILLGLSEDQLLGKKaidpawhfYREdgtVLPLEEYPVNYVLA 1719
Cdd:PRK11360   255 QALRETRSLNELILESIADGVIAIDRQGKITTMNPAAEVITGLQRHELVGKP--------YSE---LFPPNTPFASPLLD 323
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1085344563 1720 T---RKELRNYVVGVHrtNYKNDVWVLVNADPVWSNENELTQVIVTFSDITMRKNAE 1773
Cdd:PRK11360   324 TlehGTEHVDLEISFP--GRDRTIELSVSTSLLHNTHGEMIGALVIFSDLTERKRLQ 378
PAS smart00091
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ...
1519-1586 5.49e-03

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: 37.38  E-value: 5.49e-03
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085344563  1519 AQLNEAQRIAQIGSWELDIANNILRWSDEIFRIFEIDPKEF-GSSYEAFlnaIHPDDREVVNTAYSNSL 1586
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELiGKSLLEL---IHPEDRERVQEALQRLL 66
PRK10815 PRK10815
two-component system sensor histidine kinase PhoQ;
2438-2519 5.51e-03

two-component system sensor histidine kinase PhoQ;


Pssm-ID: 182754 [Multi-domain]  Cd Length: 485  Bit Score: 41.93  E-value: 5.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2438 NLLSNAIKYSPKggKIELTIKQLRGKMVISVKDKGIGIPTDDLKHLFEPFHRAKntTDISGTGLGLSIVKRAVDLHNGII 2517
Cdd:PRK10815   385 NVLDNACKYCLE--FVEISARQTDEHLHIVVEDDGPGIPESKRELIFDRGQRAD--TLRPGQGLGLSVAREITEQYEGKI 460

                   ..
gi 1085344563 2518 TV 2519
Cdd:PRK10815   461 SA 462
PAC smart00086
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ...
499-541 6.31e-03

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: 36.78  E-value: 6.31e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 1085344563   499 TYEYQIIHKSGEARWLNQRNILVLDEGGNSVAIEGVVTDITER 541
Cdd:smart00086    1 TVEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
HATPase_SpoIIAB-like cd16942
Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein ...
2426-2532 6.98e-03

Histidine kinase-like ATPase domain of SpoIIAB, an anti sigma-F factor and serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli, and related domains; This family includes histidine kinase-like ATPase (HATPase) domain of SpoIIAB, an anti sigma-F factor and a serine-protein kinase involved in regulating sigma-F during sporulation in Bacilli where, early in sporulation, the cell divides into two unequal compartments: a larger mother cell and a smaller forespore. Sigma-F transcription factor is activated in the forespore directly after the asymmetric septum forms, and its spatial and temporal activation is required for sporulation. Free sigma-F can associate with the RNA polymerase core and activate transcription of the sigma-F regulon, its regulation may comprise a partner-switching mechanism involving SpoIIAB, SpoIIAA, and sigma-F as follows: SpoIIAB can form alternative complexes with either: i) sigma-F, holding it in an inactive form and preventing its association with RNA polymerase, or ii) unphosphorylated SpoIIAA and a nucleotide, either ATP or ADP. In the presence of ATP, SpoIIAB acts as a kinase to specifically phosphorylate a serine residue of SpoIIAA; this phosphorylated form has low affinity for SpoIIAB and dissociates, making SpoIIAB available to capture sigma-F. SpoIIAA may then be dephosphorylated by a SpoIIE serine phosphatase and be free to attack the SpoIIAB sigma-F complex to induce the release of sigma-F.


Pssm-ID: 340418 [Multi-domain]  Cd Length: 135  Bit Score: 39.06  E-value: 6.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085344563 2426 RLDPKL-----MKFILLNLLSNAI--KYSPKGGKI-ELTIKQLRGKMVISVKDKGIGIPtdDLKHLFEPFHRAKNTTDIS 2497
Cdd:cd16942     28 QLDPTIdelteIKTVVSEAVTNAIihGYNNDPNGIvSISVIIEDGVVHLTVRDEGVGIP--DIEEARQPLFTTKPELERS 105
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1085344563 2498 gtGLGLSIVKRAVDLhngiITVKSELNAGTTFTVK 2532
Cdd:cd16942    106 --GMGFTIMENFMDE----VIVESEVNKGTTVYLK 134
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH