|
Name |
Accession |
Description |
Interval |
E-value |
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
1556-1860 |
3.53e-71 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 243.60 E-value: 3.53e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1556 TDVEAARQQAEQETTQRRSLEDALQQSHGE---VELRVSE-RTAGLNAHVQQLEAELAEAQRAEEQLRHR-RIEAVSTLA 1630
Cdd:COG3852 60 SPLRELLERALAEGQPVTEREVTLRRKDGEerpVDVSVSPlRDAEGEGGVLLVLRDITERKRLERELRRAeKLAAVGELA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1631 GGMAHELNNVLAPVLMAAQLLRKQVS-GKSRTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQE 1709
Cdd:COG3852 140 AGLAHEIRNPLTGIRGAAQLLERELPdDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1710 TFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfiHHRRATGAKPGNYVLFRVT 1789
Cdd:COG3852 220 EAPKNIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVE-------RQVTLGGLRPRLYVRIEVI 292
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 1790 DSGVGIPRDILPRIFEPFFTTKEPGQsvGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAASAETSE 1860
Cdd:COG3852 293 DNGPGIPEEILDRIFEPFFTTKEKGT--GLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
1490-1854 |
6.43e-67 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 231.23 E-value: 6.43e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1490 AARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQET 1569
Cdd:COG4191 5 LLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1570 TQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEQLRHR-RIEAVSTLAGGMAHELNNVLAPVLMAA 1648
Cdd:COG4191 85 LLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSeKLAALGELAAGIAHEINNPLAAILGNA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1649 QLLRKQVSGKS-----RTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVA 1722
Cdd:COG4191 165 ELLRRRLEDEPdpeelREALERILEGAERAAEIVRSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKaRGIEVELDLP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1723 DDLPLISADASQLHRVLLNLAVNARDAMPSG--GTLKFSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIPRDIL 1800
Cdd:COG4191 245 PDLPPVLGDPGQLEQVLLNLLINAIDAMEEGegGRITISTR-----------------REGDYVVISVRDNGPGIPPEVL 307
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 1801 PRIFEPFFTTKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAA 1854
Cdd:COG4191 308 ERIFEPFFTTKPVGKGTGLGLSISYGIVEKHGGRIEVESEPGGGTTFTITLPLA 361
|
|
| PRK13557 |
PRK13557 |
histidine kinase; Provisional |
1614-1984 |
1.95e-64 |
|
histidine kinase; Provisional
Pssm-ID: 237425 [Multi-domain] Cd Length: 540 Bit Score: 229.94 E-value: 1.95e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1614 AEEQLRH-RRIEAVSTLAGGMAHELNNVLAPVL----MAAQLLRKQVSGKSRTL--VDSVESSAQRGADIVKQVLTFARG 1686
Cdd:PRK13557 150 AEDALRQaQKMEALGQLTGGIAHDFNNLLQVMSgyldVIQAALSHPDADRGRMArsVENIRAAAERAATLTQQLLAFARK 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1687 FHGERAPVSPEMLVRDIAKSVQETFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVVVD 1766
Cdd:PRK13557 230 QRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVEIE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1767 ESFIHhrRATGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTE 1846
Cdd:PRK13557 310 DEDLA--MYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTT 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1847 FQIYLPAASAETSERPPQAELP--RGNGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAgDIKAVIT 1924
Cdd:PRK13557 388 VRLYFPASDQAENPEQEPKARAidRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHP-EVDLLFT 466
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 1925 DILMP-FMDGVELCRELRKRDATLPIIVASGMGHEKFvtDLRELGVPLF--LKKPFAAEELLR 1984
Cdd:PRK13557 467 DLIMPgGMNGVMLAREARRRQPKIKVLLTTGYAEASI--ERTDAGGSEFdiLNKPYRRAELAR 527
|
|
| NtrY |
COG5000 |
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ... |
1494-1857 |
1.13e-50 |
|
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: 185.94 E-value: 1.13e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1494 ELDMLNRQFAQRVAELDSTEARLREecaHRERAEAELDRMRDAQDGF--QQSTAELNERLTRLT-TDVEAARQQAEQETT 1570
Cdd:COG5000 63 EIGELARAFNRMTDQLKEQREELEE---RRRYLETILENLPAGVIVLdaDGRITLANPAAERLLgIPLEELIGKPLEELL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1571 QRRSLEDALQQS-----HGEVELRVS-ERTAGLNAHVQQLEAELAEAQRAEEQLRHRRIEAVSTLAGGMAHELNNVLAPV 1644
Cdd:COG5000 140 PELDLAELLREAlergwQEEIELTRDgRRTLLVRASPLRDDGYVIVFDDITELLRAERLAAWGELARRIAHEIKNPLTPI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1645 LMAAQLLRKQVSGKS-------RTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQETFPR-NVR 1716
Cdd:COG5000 220 QLSAERLRRKLADKLeedredlERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPVDLNELLREVLALYEPALKEkDIR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1717 VSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIP 1796
Cdd:COG5000 300 LELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTR-----------------REDGRVRIEVSDNGPGIP 362
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 1797 RDILPRIFEPFFTTKEPGQsvGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAASAE 1857
Cdd:COG5000 363 EEVLERIFEPFFTTKPKGT--GLGLAIVKKIVEEHGGTIELESRPGGGTTFTIRLPLAEEA 421
|
|
| BaeS |
COG0642 |
Signal transduction histidine kinase [Signal transduction mechanisms]; |
1523-1854 |
2.96e-46 |
|
Signal transduction histidine kinase [Signal transduction mechanisms];
Pssm-ID: 440407 [Multi-domain] Cd Length: 328 Bit Score: 170.47 E-value: 2.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1523 RERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQ 1602
Cdd:COG0642 12 LLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1603 QLEAELAEAQRAEEQLRhrrieAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSRTLVDSVESSAQRGADIVKQVLT 1682
Cdd:COG0642 92 LLLLLLALLLLLEEANE-----AKSRFLANVSHELRTPLTAIRGYLELLLEELDEEQREYLETILRSADRLLRLINDLLD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1683 FARGFHG----ERAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLK 1757
Cdd:COG0642 167 LSRLEAGklelEPEPVDLAELLEEVVELFRPLAEeKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTVT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1758 FSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEP--GQSVGLGLATALGVVQSHGGFI 1835
Cdd:COG0642 247 VSVR-----------------REGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSrrGGGTGLGLAIVKRIVELHGGTI 309
|
330
....*....|....*....
gi 1786808614 1836 LLETEEDKGTEFQIYLPAA 1854
Cdd:COG0642 310 EVESEPGKGTTFTVTLPLA 328
|
|
| PRK13837 |
PRK13837 |
two-component system VirA-like sensor kinase; |
1442-1997 |
4.97e-45 |
|
two-component system VirA-like sensor kinase;
Pssm-ID: 237526 [Multi-domain] Cd Length: 828 Bit Score: 177.18 E-value: 4.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1442 LQQAHAELTRRLT-ERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRV------AELDSTEA 1514
Cdd:PRK13837 262 LRARTRVLRRRAAfEEVIAAISRCFEAASPHELEASIEAALGILAKFFDADSAALALVDVGGRARIwtfpglTPDPVWPD 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1515 RLREeCAHRERAeAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVEL-RVSER 1593
Cdd:PRK13837 342 RLRA-LASTVKA-AERDVVFVDRNGPVRKRSCLTRRGPALWACLAFKSGDRIVALLGLGRQRYGLRPPAGELQLlELALD 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1594 TAGLNAHVQQLEAELAEAQRAeeqLRH-RRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSRTL--VDSVESSA 1670
Cdd:PRK13837 420 CLAHAIERRRLETERDALERR---LEHaRRLEAVGTLASGIAHNFNNILGAILGYAEMALNKLARHSRAAryIDEIISAG 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1671 QRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQETFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAM 1750
Cdd:PRK13837 497 ARARLIIDQILAFGRKGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAM 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1751 PSGGTLKFSAENVVVdesfihhRRATG-----AKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQsvGLGLATAL 1825
Cdd:PRK13837 577 DGAGRVDISLSRAKL-------RAPKVlshgvLPPGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTRAGGT--GLGLATVH 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1826 GVVQSHGGFILLETEEDKGTEFQIYLPAASAETSErpPQAE-----LPRGNGELLMLADDEQGVLDVTAEILEWHGYKVL 1900
Cdd:PRK13837 648 GIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPVA--PQAFfgpgpLPRGRGETVLLVEPDDATLERYEEKLAALGYEPV 725
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1901 TARDGQQALSLY--DQHAGDikAVITDilMPFMDGVELCRELRKRDATLPIIVAsGMGHEKFVTDLRELGVPLFLKKPFA 1978
Cdd:PRK13837 726 GFSTLAAAIAWIskGPERFD--LVLVD--DRLLDEEQAAAALHAAAPTLPIILG-GNSKTMALSPDLLASVAEILAKPIS 800
|
570
....*....|....*....
gi 1786808614 1979 AEELLRSLHAELHREESAA 1997
Cdd:PRK13837 801 SRTLAYALRTALATARAAA 819
|
|
| KdpD |
COG2205 |
K+-sensing histidine kinase KdpD [Signal transduction mechanisms]; |
1607-1856 |
6.84e-41 |
|
K+-sensing histidine kinase KdpD [Signal transduction mechanisms];
Pssm-ID: 441807 [Multi-domain] Cd Length: 239 Bit Score: 151.60 E-value: 6.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1607 ELAEAQRAEEQLRHRRieavSTLAGGMAHELNNVLAPVLMAAQLLRKQVSG---KSRTLVDSVESSAQRGADIVKQVLTF 1683
Cdd:COG2205 1 ELEEALEELEELERLK----SEFLANVSHELRTPLTSILGAAELLLDEEDLspeERRELLEIIRESAERLLRLIEDLLDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1684 AR----GFHGERAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKF 1758
Cdd:COG2205 77 SRlesgKLSLELEPVDLAELLEEAVEELRPLAEeKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1759 SAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG--QSVGLGLATALGVVQSHGGFIL 1836
Cdd:COG2205 157 SARRE-----------------GDGVRISVSDNGPGIPEEELERIFERFYRGDNSRgeGGTGLGLAIVKRIVEAHGGTIW 219
|
250 260
....*....|....*....|
gi 1786808614 1837 LETEEDKGTEFQIYLPAASA 1856
Cdd:COG2205 220 VESEPGGGTTFTVTLPLAES 239
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
1610-1861 |
7.01e-40 |
|
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: 156.29 E-value: 7.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1610 EAQRAEEQLRHR-RIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSRTLVDSVESSAQRGADIVKQVLTFARgfh 1688
Cdd:COG5809 253 ERKKLEELLRKSeKLSVVGELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQKTYLDIMLSELDRIESIISEFLVLAK--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1689 geraPVSPEMLVRDIAKSVQETFP--------RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLkfsa 1760
Cdd:COG5809 330 ----PQAIKYEPKDLNTLIEEVIPllqpqallKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNI---- 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1761 envvvdesFIHhrraTGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLETE 1840
Cdd:COG5809 402 --------TIE----TKAEDDDKVVISVTDEGCGIPEERLKKLGEPFYTTKEKG--TGLGLMVSYKIIEEHGGKITVESE 467
|
250 260
....*....|....*....|.
gi 1786808614 1841 EDKGTEFQIYLPAASAETSER 1861
Cdd:COG5809 468 VGKGTTFSITLPIKLSEQVSM 488
|
|
| KinC |
COG5807 |
Sporulation sensor histidine kinase C [Cell cycle control, cell division, chromosome ... |
1615-1852 |
2.06e-39 |
|
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: 151.48 E-value: 2.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1615 EEQLRHRRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSR-TLVDSVESSAQRGADIVKQVLTFARGFHGERAP 1693
Cdd:COG5807 136 DKLLRSEKLSVAGELAAGIAHEIRNPLTSIKGFLQLLQESREDSEReEYFNIIISEIDRINTIITELLVLSKPKKFNFKK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1694 VSPEMLVRDIAKSVQETFP-RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAenvvvdesfihh 1772
Cdd:COG5807 216 LNLNDVLEDVIALLSTEAIlKNISIKYDLADDEPVINGDKNQLKQVFINLIKNAIEAMETGGNITIKT------------ 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1773 rratgAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:COG5807 284 -----YVEGDFVVISVKDEGIGIPEEVLEKIGEPFFTTKEEG--TGLGLSICKKIIEEHNGTIEVESKPGKGTTFTIYLP 356
|
|
| HATPase_CckA-like |
cd16919 |
Histidine kinase-like ATPase domain of two-component sensor hybrid histidine kinases, similar ... |
1735-1852 |
4.28e-39 |
|
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: 141.75 E-value: 4.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNARDAMPSGGTLKFSAENVVVDESFIHHRRatGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16919 1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYR--DLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVG 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 1786808614 1815 QSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16919 79 KGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
|
|
| PRK11360 |
PRK11360 |
two-component system sensor histidine kinase AtoS; |
1567-1858 |
2.91e-36 |
|
two-component system sensor histidine kinase AtoS;
Pssm-ID: 236901 [Multi-domain] Cd Length: 607 Bit Score: 147.42 E-value: 2.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1567 QETTQRRSLEDALQQSHGEVELRVSerTAGL-NAHVQQLEA-----ELAEAQRAEEQL-RHRRIEAVSTLAGGMAHELNN 1639
Cdd:PRK11360 326 EHGTEHVDLEISFPGRDRTIELSVS--TSLLhNTHGEMIGAlvifsDLTERKRLQRRVaRQERLAALGELVAGVAHEIRN 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1640 VLAPVLMAAQLLRKQVSGK-SRTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQETFPRN-VRV 1717
Cdd:PRK11360 404 PLTAIRGYVQIWRQQTSDPpSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQPVSLNALVEEVLQLFQTAGVQArVDF 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1718 SSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVVVDESFIhhrratgakpgnyvlfRVTDSGVGIPR 1797
Cdd:PRK11360 484 ETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTWQYSDGQVAV----------------SIEDNGCGIDP 547
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 1798 DILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAASAET 1858
Cdd:PRK11360 548 ELLKKIFDPFFTTKAKG--TGLGLALSQRIINAHGGDIEVESEPGVGTTFTLYLPINPQGN 606
|
|
| WalK |
COG5002 |
Sensor histidine kinase WalK [Signal transduction mechanisms]; |
1488-1856 |
2.15e-34 |
|
Sensor histidine kinase WalK [Signal transduction mechanisms];
Pssm-ID: 444026 [Multi-domain] Cd Length: 390 Bit Score: 137.38 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1488 LNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQ 1567
Cdd:COG5002 35 LLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1568 ETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEQLRHrrieavstLAGGMAHELNNVLAPVLMA 1647
Cdd:COG5002 115 AALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRRE--------FVANVSHELRTPLTSIRGY 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1648 AQLLRKQVSG---KSRTLVDSVESSAQRGADIVKQVLTFARGFHG----ERAPVSPEMLVRDIAKSVQETFP-RNVRVSS 1719
Cdd:COG5002 187 LELLLDGAADdpeERREYLEIILEEAERLSRLVNDLLDLSRLESGelklEKEPVDLAELLEEVVEELRPLAEeKGIELEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1720 EVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDI 1799
Cdd:COG5002 267 DLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLREE-----------------DDQVRISVRDTGIGIPEED 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1800 LPRIFEPFFT-----TKEPGQSvGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAASA 1856
Cdd:COG5002 330 LPRIFERFYRvdksrSRETGGT-GLGLAIVKHIVEAHGGRIWVESEPGKGTTFTITLPLARE 390
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
1610-1852 |
2.68e-34 |
|
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: 139.48 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1610 EAQRAEEQLRH-RRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSRTLvDSVESSAQRGADIVKQVLTFARgfh 1688
Cdd:COG5805 270 EKKEAEELMARsEKLSIAGQLAAGIAHEIRNPLTSIKGFLQLLQPGIEDKEEYF-DIMLSELDRIESIISEFLALAK--- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1689 geraPVSPEMLVRDIAKSVQETFP--------RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLkfsa 1760
Cdd:COG5805 346 ----PQAVNKEKENINELIQDVVTlleteailHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTI---- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1761 envvvdesFIHHRRAtgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLETE 1840
Cdd:COG5805 418 --------TIHTEEE-----DNSVIIRVIDEGIGIPEERLKKLGEPFFTTKEKG--TGLGLMVSYKIIENHNGTIDIDSK 482
|
250
....*....|..
gi 1786808614 1841 EDKGTEFQIYLP 1852
Cdd:COG5805 483 VGKGTTFTITLP 494
|
|
| KinD |
COG5808 |
Sporulation sensor histidine kinase D [Cell cycle control, cell division, chromosome ... |
1612-1856 |
1.05e-32 |
|
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: 134.11 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1612 QRAEEQLRHRRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSG-KSRTLVDSVESSAQRGADIVKQVLTFARGFHGE 1690
Cdd:COG5808 227 ERVIQEINTQKLELIGTFAASTAHEIRNPLTSIKGFIQLLQEKYPElEDQKYFDIIQEEIQRINQIVSEFLVLGKPTAKK 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1691 RAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENvvvdesf 1769
Cdd:COG5808 307 LELDDLNELIEEILSIIDSEANlKNIRVEKQSLDEPLHIKCDKDRIKQVLLNLIKNAIEAMKEGGKLTISIEN------- 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1770 ihhrratgakPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLETEEDKGTEFQI 1849
Cdd:COG5808 380 ----------DDEKAVIEVIDNGEGIPEDIIDEIFEPFVTTKEGG--TGLGLSVCKRIVEMHGGEIDIESEEGKGTTFTI 447
|
....*..
gi 1786808614 1850 YLPAASA 1856
Cdd:COG5808 448 RLPLKKE 454
|
|
| PRK10364 |
PRK10364 |
two-component system sensor histidine kinase ZraS; |
1602-1854 |
9.50e-31 |
|
two-component system sensor histidine kinase ZraS;
Pssm-ID: 236674 [Multi-domain] Cd Length: 457 Bit Score: 128.37 E-value: 9.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1602 QQLEAELAeaqraeeqlRHRRIEAVSTLAGGMAHELNNVLAPVLMAAQLL--RKQVSGKSRTLVDSVESSAQRGADIVKQ 1679
Cdd:PRK10364 222 QLLQDEMK---------RKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFaeRAPAGGEAHQLAQVMAKEADRLNRVVSE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1680 VLTFARGFHGERAPVSPEMLVRDIAKSV-QETFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKF 1758
Cdd:PRK10364 293 LLELVKPTHLALQAVDLNDLINHSLQLVsQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISV 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1759 SAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKepGQSVGLGLATALGVVQSHGGFILLE 1838
Cdd:PRK10364 373 TASES-----------------GAGVKISVTDSGKGIAADQLEAIFTPYFTTK--AEGTGLGLAVVHNIVEQHGGTIQVA 433
|
250
....*....|....*.
gi 1786808614 1839 TEEDKGTEFQIYLPAA 1854
Cdd:PRK10364 434 SQEGKGATFTLWLPVN 449
|
|
| COG4251 |
COG4251 |
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal ... |
1342-1856 |
1.10e-27 |
|
Bacteriophytochrome (light-regulated signal transduction histidine kinase) [Signal transduction mechanisms];
Pssm-ID: 443393 [Multi-domain] Cd Length: 503 Bit Score: 119.89 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1342 AIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTAL 1421
Cdd:COG4251 2 LLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1422 RTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQ 1501
Cdd:COG4251 82 LLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1502 FAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQ 1581
Cdd:COG4251 162 LLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1582 SHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEQlRHRRIEAvstLAGGMAHELNNVLAPVLMAAQLLRK----QVSG 1657
Cdd:COG4251 242 ILLLLLLILVLELLELRLELEELEEELEERTAELER-SNEELEQ---FAYVASHDLREPLRKISGFSQLLEEdygdKLDE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1658 KSRTLVDSVESSAQRGADIVKQVLTFAR--GFHGERAPVSPEMLVRDIAKSVQETFP-RNVRVsseVADDLPLISADASQ 1734
Cdd:COG4251 318 EGREYLERIRDAAERMQALIDDLLAYSRvgRQELEFEPVDLNELLEEVLEDLEPRIEeRGAEI---EVGPLPTVRGDPTL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNArdampsggtLKFSAENVVVdesFIHhrrATGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFT--TKE 1812
Cdd:COG4251 395 LRQVFQNLISNA---------IKYSRPGEPP---RIE---IGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRlhSRD 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1786808614 1813 PGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAASA 1856
Cdd:COG4251 460 EYEGTGIGLAIVKKIVERHGGRIWVESEPGEGATFYFTLPKAPA 503
|
|
| HATPase_c |
smart00387 |
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases. |
1730-1852 |
5.36e-27 |
|
Histidine kinase-like ATPases; Histidine kinase-, DNA gyrase B-, phytochrome-like ATPases.
Pssm-ID: 214643 [Multi-domain] Cd Length: 111 Bit Score: 106.96 E-value: 5.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1730 ADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFT 1809
Cdd:smart00387 1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERD-----------------GDHVEITVEDNGPGIPPEDLEKIFEPFFR 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1786808614 1810 TKEPGQSV---GLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:smart00387 64 TDKRSRKIggtGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
|
|
| KinB |
COG5806 |
Sporulation sensor histidine kinase B [Cell cycle control, cell division, chromosome ... |
1597-1854 |
6.75e-27 |
|
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: 115.73 E-value: 6.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1597 LNAHVQQLEAELAEAQRAEeqlrhrRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQvsgksRTLVDSVESSAQ----- 1671
Cdd:COG5806 178 LIENLIENILLRKELQRAE------KLEVVSELAASIAHEVRNPLTVVRGFIQLLQEP-----ELSDEKRKQYIRialee 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1672 --RGADIVKQVLTFARgfhgeraPVSPEMLVRDIAKSVQE----TFP----RNVRVSSEVADDLpLISADASQLHRVLLN 1741
Cdd:COG5806 247 ldRAEAIITDYLTFAK-------PQPEKLEKIDVSEELEHvidvLSPyanmNNVEIQTELEPGL-YIEGDRQKLQQCLIN 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1742 LAVNARDAMPSGGTLKFSAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGqsVGLGL 1821
Cdd:COG5806 319 IIKNGIEAMPNGGTLTIDVSID-----------------KNKVIISIKDTGVGMTKEQLERLGEPYFSTKEKG--TGLGT 379
|
250 260 270
....*....|....*....|....*....|...
gi 1786808614 1822 ATALGVVQSHGGFILLETEEDKGTEFQIYLPAA 1854
Cdd:COG5806 380 MVSYRIIEAMNGTIRVESEVGKGTTFTITLPLA 412
|
|
| HATPase |
cd00075 |
Histidine kinase-like ATPase domain; This superfamily includes the histidine kinase-like ... |
1735-1851 |
7.04e-26 |
|
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: 103.45 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTK--E 1812
Cdd:cd00075 1 LEQVLSNLLDNALKYSPPGGTIEISLRQE-----------------GDGVVLEVEDNGPGIPEEDLERIFERFYRGDksR 63
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1813 PGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYL 1851
Cdd:cd00075 64 EGGGTGLGLAIVRRIVEAHGGRITVESEPGGGTTFTVTL 102
|
|
| YesN |
COG4753 |
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding ... |
1875-1976 |
9.50e-26 |
|
Two-component response regulator, YesN/AraC family, consists of REC and AraC-type DNA-binding domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 443786 [Multi-domain] Cd Length: 103 Bit Score: 103.31 E-value: 9.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHG--YKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:COG4753 2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDL--VITDINMPGMDGLELLEAIRELDPDTKIIIL 79
|
90 100
....*....|....*....|....
gi 1786808614 1953 SGMGHEKFVTDLRELGVPLFLKKP 1976
Cdd:COG4753 80 SGYSDFEYAQEAIKLGADDYLLKP 103
|
|
| HATPase_AtoS-like |
cd16943 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1733-1852 |
5.72e-25 |
|
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: 100.96 E-value: 5.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1733 SQLHRVLLNLAVNARDAMPSGGTLKFsaenvvvdESFIHHRRatgakpgnyVLFRVTDSGVGIPRDILPRIFEPFFTTKE 1812
Cdd:cd16943 2 SQLNQVLLNLLVNAAQAMEGRGRITI--------RTWAHVDQ---------VLIEVEDTGSGIDPEILGRIFDPFFTTKP 64
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1786808614 1813 PGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16943 65 VGEGTGLGLSLSYRIIQKHGGTIRVASVPGGGTRFTIILP 104
|
|
| CheY |
COG0784 |
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator ... |
1868-1995 |
7.74e-25 |
|
CheY-like REC (receiver) domain, includes chemotaxis protein CheY and sporulation regulator Spo0F [Signal transduction mechanisms];
Pssm-ID: 440547 [Multi-domain] Cd Length: 128 Bit Score: 101.47 E-value: 7.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1868 PRGNGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT- 1946
Cdd:COG0784 1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDL--ILLDINMPGMDGLELLRRIRALPRLp 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1947 -LPIIVASGMGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHREES 1995
Cdd:COG0784 79 dIPIIALTAYADEEDRERALEAGADDYLTKPVDPEELLEALRRLLARASA 128
|
|
| HATPase_c |
pfam02518 |
Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase; This family represents the ... |
1730-1854 |
7.76e-25 |
|
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: 100.91 E-value: 7.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1730 ADASQLHRVLLNLAVNARDAMPSGGTLKfsaenVVVDEsfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFT 1809
Cdd:pfam02518 1 GDELRLRQVLSNLLDNALKHAAKAGEIT-----VTLSE-------------GGELTLTVEDNGIGIPPEDLPRIFEPFST 62
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1786808614 1810 TKEPGQS-VGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAA 1854
Cdd:pfam02518 63 ADKRGGGgTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
|
|
| OmpR |
COG0745 |
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain ... |
1875-1998 |
4.12e-23 |
|
DNA-binding response regulator, OmpR family, contains REC and winged-helix (wHTH) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 440508 [Multi-domain] Cd Length: 204 Bit Score: 99.26 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:COG0745 4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDL--ILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTA 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHREESAAV 1998
Cdd:COG0745 82 RDDEEDRVRGLEAGADDYLTKPFDPEELLARIRALLRRRAAEVL 125
|
|
| Response_reg |
pfam00072 |
Response regulator receiver domain; This domain receives the signal from the sensor partner in ... |
1876-1983 |
7.64e-23 |
|
Response regulator receiver domain; This domain receives the signal from the sensor partner in bacterial two-component systems. It is usually found N-terminal to a DNA binding effector domain.
Pssm-ID: 395025 [Multi-domain] Cd Length: 111 Bit Score: 95.30 E-value: 7.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:pfam00072 2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDL--ILLDINMPGMDGLELLKRIRRRDPTTPVIILTAH 79
|
90 100
....*....|....*....|....*...
gi 1786808614 1956 GHEKFVTDLRELGVPLFLKKPFAAEELL 1983
Cdd:pfam00072 80 GDEDDAVEALEAGADDFLSKPFDPDELL 107
|
|
| REC |
cd00156 |
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response ... |
1876-1976 |
6.79e-22 |
|
phosphoacceptor receiver (REC) domain of response regulators (RRs) and pseudo response regulators (PRRs); Two-component systems (TCSs) involving a sensor and a response regulator are used by bacteria to adapt to changing environments. Processes regulated by two-component systems in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Response regulators (RRs) share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. Response regulators regulate transcription, post-transcription or post-translation, or have functions such as methylesterases, adenylate or diguanylate cyclase, c-di-GMP-specific phosphodiesterases, histidine kinases, serine/threonine protein kinases, and protein phosphatases, depending on their output domains. The function of some output domains are still unknown. TCSs are found in all three domains of life - bacteria, archaea, and eukaryotes, however, the presence and abundance of particular RRs vary between the lineages. Archaea encode very few RRs with DNA-binding output domains; most are stand-alone REC domains. Among eukaryotes, TCSs are found primarily in protozoa, fungi, algae, and green plants. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381085 [Multi-domain] Cd Length: 99 Bit Score: 91.91 E-value: 6.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:cd00156 1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDL--VLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78
|
90 100
....*....|....*....|.
gi 1786808614 1956 GHEKFVTDLRELGVPLFLKKP 1976
Cdd:cd00156 79 ADEEDAVRALELGADDYLVKP 99
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
855-1449 |
1.28e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 855 RQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRssEERVALLASELEAAREALRSESARREELETALPKT 934
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEL--EAELAELEAELEELRLELEELELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 935 KTELGQRLAEAAAEAAGLrarmdfEAAERERVEAAWKLAnsATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRA 1014
Cdd:COG1196 294 LAELARLEQDIARLEERR------RELEERLEELEEELA--ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1015 ELEatnaessrALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDA 1094
Cdd:COG1196 366 ALL--------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1095 ERTTEALQADLDAALKACEEEAARRSQAEETARQshtefthRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKK 1174
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEE-------AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1175 ELEKELADANLELLDIRSRLDHEAAARRQAEESAkqgSASADQRLAERLSEVQTLQERLRSEAAQRETtevELRDTRAAL 1254
Cdd:COG1196 511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL---AAALQNIVVEDDEVAAAAIEYLKAAKAGRAT---FLPLDKIRA 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1255 EKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDR 1334
Cdd:COG1196 585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1335 LTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRL 1414
Cdd:COG1196 665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744
|
570 580 590
....*....|....*....|....*....|....*
gi 1786808614 1415 GELTTALRTAEAKAGSDSAELRHAHETLQQAHAEL 1449
Cdd:COG1196 745 EELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1070-1625 |
1.39e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.71 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1070 RSRLEKETAARHETERELrESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEK 1149
Cdd:COG1196 238 EAELEELEAELEELEAEL-EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1150 NLRQAAEEATRKAQALqAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTL 1229
Cdd:COG1196 317 RLEELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1230 QErLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRR 1309
Cdd:COG1196 396 AE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1310 LLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAAL 1389
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1390 RGEMEKRLRLELTwqmqredfDRRLGELTT-ALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAA 1468
Cdd:COG1196 555 DDEVAAAAIEYLK--------AAKAGRATFlPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1469 ALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQdgfqQSTAELN 1548
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL----EEALLAE 702
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786808614 1549 ERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEQLRhRRIEA 1625
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE-REIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1025-1576 |
1.91e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 102.32 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1025 RALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQAd 1104
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR- 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1105 LDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQR--AKKELEKELAD 1182
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaEAEEELEELAE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1183 ANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEAS 1262
Cdd:COG1196 387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1263 AALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHA 1342
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1343 IEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALR 1422
Cdd:COG1196 547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1423 TAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQF 1502
Cdd:COG1196 627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 1503 AQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLE 1576
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALG 780
|
|
| PleD |
COG3706 |
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate ... |
1876-1986 |
3.08e-21 |
|
Two-component response regulator, PleD family, consists of two REC domains and a diguanylate cyclase (GGDEF) domain [Signal transduction mechanisms, Transcription];
Pssm-ID: 442920 [Multi-domain] Cd Length: 179 Bit Score: 93.05 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIVAS 1953
Cdd:COG3706 5 LVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDL--ILLDLEMPDMDGLELCRRLRADPRTadIPIIFLT 82
|
90 100 110
....*....|....*....|....*....|...
gi 1786808614 1954 GMGHEKFVTDLRELGVPLFLKKPFAAEELLRSL 1986
Cdd:COG3706 83 ALDDEEDRARALEAGADDYLTKPFDPEELLARV 115
|
|
| RpfG |
COG3437 |
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ... |
1876-1992 |
1.16e-20 |
|
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];
Pssm-ID: 442663 [Multi-domain] Cd Length: 224 Bit Score: 92.92 E-value: 1.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIVAS 1953
Cdd:COG3437 10 LIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDL--ILLDVRMPGMDGFELLRLLRADPSTrdIPVIFLT 87
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1954 GMGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:COG3437 88 ALADPEDRERALEAGADDYLTKPFDPEELLARVRNALEL 126
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
761-1367 |
1.37e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 761 REQAESALGQSKSETERQLAEATAALAEVRAQLEQATtassQREAEAKQAAAAQQQKLADQDAELKktwdnliKETEDRE 840
Cdd:COG1196 209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELE-------ELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 841 ALEKQLAAARGDlERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSE 920
Cdd:COG1196 278 ELELELEEAQAE-EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 921 SARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAwKLANSATEQHAAELKTLLATAREELHAETA 1000
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-EEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1001 KRDAAEAAASQVR---AELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKET 1077
Cdd:COG1196 436 EEEEEEEALEEAAeeeAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1078 -AARHETERELRESLTDAERTTEALQADLDAALKA--CEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQA 1154
Cdd:COG1196 516 lAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1155 AEEAtrkAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQrLAERLSEVQTLQERLR 1234
Cdd:COG1196 596 AIGA---AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG-GSAGGSLTGGSRRELL 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1235 SEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEE 1314
Cdd:COG1196 672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786808614 1315 RAARASALAELAARRAEVDRLTTE-------QPHAIEEATAR------LKAQLAEQEREREQLRLA 1367
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREiealgpvNLLAIEEYEELeerydfLSEQREDLEEARETLEEA 817
|
|
| REC_YesN-like |
cd17536 |
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response ... |
1875-1986 |
2.46e-20 |
|
phosphoacceptor receiver (REC) domain of YesN and related helix-turn-helix containing response regulators; This family is composed of uncharacterized response regulators that contain a REC domain and a AraC family helix-turn-helix (HTH) DNA-binding output domain, including Bacillus subtilis uncharacterized transcriptional regulatory protein YesN and Staphylococcus aureus uncharacterized response regulatory protein SAR0214. YesN is a member of the two-component regulatory system YesM/YesN and SAR0214 is a member of the probable two-component regulatory system SAR0215/SAR0214. Also included in this family is the AlgR-like group of LytTR/AlgR family response, which includes Pseudomonas aeruginosa positive alginate biosynthesis regulatory protein AlgR and Bacillus subtilis sensory transduction protein LytT, among others. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381091 [Multi-domain] Cd Length: 121 Bit Score: 88.16 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGY---KVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIV 1951
Cdd:cd17536 1 VLIVDDEPLIREGLKKLIDWEELgfeVVGEAENGEEALELIEEHKPDI--VITDIRMPGMDGLELIEKIRELYPDIKIII 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1786808614 1952 ASgmGHEKF----------VTDlrelgvplFLKKPFAAEELLRSL 1986
Cdd:cd17536 79 LS--GYDDFeyaqkairlgVVD--------YLLKPVDEEELEEAL 113
|
|
| HATPase_HupT_MifS-like |
cd16976 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1851 |
4.65e-20 |
|
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: 87.13 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNARDAMpsggtlkfsaENVVVDESFIHHRRATGAkpgnyVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16976 1 IQQVLMNLLQNALDAM----------GKVENPRIRIAARRLGGR-----LVLVVRDNGPGIAEEHLSRVFDPFFTTKPVG 65
|
90 100 110
....*....|....*....|....*....|....*..
gi 1786808614 1815 QSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYL 1851
Cdd:cd16976 66 KGTGLGLSISYGIVEEHGGRLSVANEEGAGARFTFDL 102
|
|
| REC_NtrX-like |
cd17550 |
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and ... |
1879-1987 |
4.74e-20 |
|
phosphoacceptor receiver (REC) domain of nitrogen assimilation regulatory protein NtrX and similar proteins; NtrX is part of the two-component regulatory system NtrY/NtrX that is involved in the activation of nitrogen assimilatory genes such as Gln. It is phosphorylated by the histidine kinase NtrY and interacts with sigma-54. NtrX is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. NtrC family response regulators are sigma54-dependent transcriptional activators. Also included in this subfamily is Aquifex aeolicus NtrC4. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381102 [Multi-domain] Cd Length: 115 Bit Score: 87.17 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIVASGMGH- 1957
Cdd:cd17550 5 DDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPD--LVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHGTi 82
|
90 100 110
....*....|....*....|....*....|
gi 1786808614 1958 EKFVTDLReLGVPLFLKKPFAAEELLRSLH 1987
Cdd:cd17550 83 ETAVKATK-LGAYDFIEKPLSLDRLLLTIE 111
|
|
| AtoC |
COG2204 |
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ... |
1875-1994 |
5.46e-20 |
|
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, and a Fis-type DNA-binding domains [Signal transduction mechanisms];
Pssm-ID: 441806 [Multi-domain] Cd Length: 418 Bit Score: 95.03 E-value: 5.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:COG2204 5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDL--VLLDLRMPGMDGLELLRELRALDPDLPVILLTG 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHREE 1994
Cdd:COG2204 83 YGDVETAVEAIKAGAFDYLTKPFDLEELLAAVERALERRR 122
|
|
| REC_OmpR |
cd17574 |
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins ... |
1876-1958 |
1.30e-19 |
|
phosphoacceptor receiver (REC) domain of OmpR family response regulators; OmpR-like proteins are one of the most widespread transcriptional regulators. OmpR family members contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domain. They are involved in the control of environmental stress tolerance (such as the oxidative, osmotic and acid stress response), motility, virulence, outer membrane biogenesis and other processes. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381116 [Multi-domain] Cd Length: 99 Bit Score: 85.54 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:cd17574 1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDL--IILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAK 78
|
...
gi 1786808614 1956 GHE 1958
Cdd:cd17574 79 DEE 81
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
621-1241 |
1.35e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.16 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 621 RQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQpvrEQLAGEVQRGERAEAELFRSRSE 700
Cdd:COG1196 199 ERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELE---AELEELEAELAELEAELEELRLE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 701 LETQQAALAELRARAEAAEAARLQVEttaqqsrtvaeqaaaeaqqqlaalrQQLQAETERREQAESALGQSKSEterqla 780
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLE-------------------------QDIARLEERRRELEERLEELEEE------ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 781 eataalaevRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAET 860
Cdd:COG1196 325 ---------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 861 KAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQ 940
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 941 RLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELeatN 1020
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI---V 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1021 AESSRALAAAQNELARESAERETteaEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEA 1100
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRAT---FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1101 LQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEA-------TRKAQALQAELQRAK 1173
Cdd:COG1196 630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERlaeeeleLEEALLAEEEEEREL 709
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786808614 1174 KELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRE 1241
Cdd:COG1196 710 AEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
571-1178 |
5.88e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.23 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 571 RGEQETALAELRAQLERTEAARQ---QIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETER 647
Cdd:COG1196 195 LGELERQLEPLERQAEKAERYRElkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 648 QLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVET 727
Cdd:COG1196 275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 728 TAQQSRtvaeqaaaeaqqqlaalrqqlqaetERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEA 807
Cdd:COG1196 355 EAEAEL-------------------------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 808 KQAAAAQQQKLADQDAELkktwDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQ 887
Cdd:COG1196 410 EALLERLERLEEELEELE----EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 888 TEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVE 967
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 968 AAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAE 1047
Cdd:COG1196 566 LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1048 FQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETAR 1127
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 1128 QSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKA--QALQAELQRAKKELEK 1178
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPPdlEELERELERLEREIEA 778
|
|
| PAS |
cd00130 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
85-187 |
6.84e-19 |
|
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: 83.84 E-value: 6.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 85 APAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLRNKDGSTRWVA 164
Cdd:cd00130 1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80
|
90 100
....*....|....*....|...
gi 1786808614 165 GHAMRVLDDHEQPNGIIGSILDI 187
Cdd:cd00130 81 VSLTPIRDEGGEVIGLLGVVRDI 103
|
|
| PRK11091 |
PRK11091 |
aerobic respiration control sensor protein ArcB; Provisional |
1724-1952 |
8.48e-19 |
|
aerobic respiration control sensor protein ArcB; Provisional
Pssm-ID: 236842 [Multi-domain] Cd Length: 779 Bit Score: 93.47 E-value: 8.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1724 DLP-LISADASQLHRVLLNLAVNArdampsggtLKFSAENVVVdESFIHHRRATgakpgnyVLFRVTDSGVGIPRDILPR 1802
Cdd:PRK11091 387 PLPhKVITDGTRLRQILWNLISNA---------VKFTQQGGVT-VRVRYEEGDM-------LTFEVEDSGIGIPEDELDK 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1803 IFEPFFTTKE-----PGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPA-ASAETSERPPQ-AELPRGNGELL 1875
Cdd:PRK11091 450 IFAMYYQVKDshggkPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHApAVAEEVEDAFDeDDMPLPALNIL 529
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786808614 1876 MLADDEQGVLdVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIVA 1952
Cdd:PRK11091 530 LVEDIELNVI-VARSVLEKLGNSVDVAMTGKEALEMFDPDEYDL--VLLDIQLPDMTGLDIARELRERYPRedLPPLVA 605
|
|
| PRK15347 |
PRK15347 |
two component system sensor kinase; |
1575-1986 |
1.51e-18 |
|
two component system sensor kinase;
Pssm-ID: 237951 [Multi-domain] Cd Length: 921 Bit Score: 92.78 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1575 LEDALQQSHGEVELRVSERTAglnahvqqleaELAEAQRAEEQLRHRRIEAVSTLAggmaHELNNVLAPVLMAAQLLRK- 1653
Cdd:PRK15347 362 LLDTLNEQYDTLENKVAERTQ-----------ALAEAKQRAEQANKRKSEHLTTIS----HEIRTPLNGVLGALELLQNt 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1654 QVSGKSRTLVDSVESSAQRGADIVKQVLTFAR------GFHGERAPVSP----EML---VRDIAKSVQ-ETFprnvrvss 1719
Cdd:PRK15347 427 PLTAEQMDLADTARQCTLSLLAIINNLLDFSRiesgqmTLSLEETALLPlldqAMLtiqGPAQSKSLTlRTF-------- 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1720 eVADDLPLISA-DASQLHRVLLNLAVNARDAMPSGGTlkfsaenvvvdesfihhrRATGAKPGNYVLFRVTDSGVGIPRD 1798
Cdd:PRK15347 499 -VGAHVPLYLHlDSLRLRQILVNLLGNAVKFTETGGI------------------RLRVKRHEQQLCFTVEDTGCGIDIQ 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1799 ILPRIFEPFFTTKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP------------AASAETSERP---- 1862
Cdd:PRK15347 560 QQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPlneyappeplkgELSAPLALHRqlsa 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1863 ----PQAELPRG---NGELL----------------------------------MLADDEQGVLDVTAEILEWHGYKVLT 1901
Cdd:PRK15347 640 wgitCQPGHQNPallDPELAylpgrlydllqqiiqgapnepvinlplqpwqlqiLLVDDVETNRDIIGMMLVELGQQVTT 719
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1902 ARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRK----RDATLPIIV----ASGMGHEKfvtdLRELGVPLFL 1973
Cdd:PRK15347 720 AASGTEALELGRQHRFDL--VLMDIRMPGLDGLETTQLWRDdpnnLDPDCMIVAltanAAPEEIHR----CKKAGMNHYL 793
|
490
....*....|...
gi 1786808614 1974 KKPFAAEELLRSL 1986
Cdd:PRK15347 794 TKPVTLAQLARAL 806
|
|
| PRK11100 |
PRK11100 |
sensory histidine kinase CreC; Provisional |
1607-1855 |
2.20e-18 |
|
sensory histidine kinase CreC; Provisional
Pssm-ID: 236846 [Multi-domain] Cd Length: 475 Bit Score: 90.67 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1607 ELAEAQRAEEQLRHR-----RIEA-VSTLAggmaHELNNVLAPVLMAAQLLRKQVSGKSRT-LVDSVESSAQRGADIVKQ 1679
Cdd:PRK11100 235 ELRELAQALESMRVKlegkaYVEQyVQTLT----HELKSPLAAIRGAAELLQEDPPPEDRArFTGNILTQSARLQQLIDR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1680 VLTFA----RGFHGERAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVADdlPLISADASQLHRVLLNLAVNARDAMPSGG 1754
Cdd:PRK11100 311 LLELArleqRQELEVLEPVALAALLEELVEAREAQAAaKGITLRLRPDD--ARVLGDPFLLRQALGNLLDNAIDFSPEGG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1755 TLKFSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQ---SVGLGLATALGVVQSH 1831
Cdd:PRK11100 389 TITLSAE-----------------VDGEQVALSVEDQGPGIPDYALPRIFERFYSLPRPANgrkSTGLGLAFVREVARLH 451
|
250 260
....*....|....*....|....
gi 1786808614 1832 GGFILLETEEDKGTEFQIYLPAAS 1855
Cdd:PRK11100 452 GGEVTLRNRPEGGVLATLTLPRHF 475
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
834-1610 |
8.41e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 90.50 E-value: 8.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 834 KETEDREALEKQLAAARGDLERqLAETKAELDQQLAALAEARSQAER---------------------EAAERRQTEESL 892
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDR-LEDILNELERQLKSLERQAEKAERykelkaelrelelallvlrleELREELEELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 893 LQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAwKL 972
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ-LE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 973 ANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSK 1052
Cdd:TIGR02168 327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1053 SALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTE 1132
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1133 FTHRLTAETGAREQLE---KNLRQAAEEATRKAQALQ--AELQRAKKELEKELADANLELLDirSRLDHEAAARRQAEES 1207
Cdd:TIGR02168 487 LQARLDSLERLQENLEgfsEGVKALLKNQSGLSGILGvlSELISVDEGYEAAIEAALGGRLQ--AVVVENLNAAKKAIAF 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1208 AKQGSA----------SADQRLAERLSEVQTLQERLRSEAAQRETTEVELR--------------DTRAALEKQ------ 1257
Cdd:TIGR02168 565 LKQNELgrvtflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAkklrpg 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1258 ---------LAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAAR 1328
Cdd:TIGR02168 645 yrivtldgdLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1329 RAEVDRLtteqphAIEEATARLKAQLAEQEREREQLRLAAMSAE-QRLRDRATDFEAANAALRGEMEKRLRLELTWQMQR 1407
Cdd:TIGR02168 725 SRQISAL------RKDLARLEAEVEQLEERIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1408 EDFDRRLGELTTALRTAEAKAgsdsAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTN 1487
Cdd:TIGR02168 799 KALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1488 LNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDrmrdaqdgfqqstaELNERLTRLTTDVEAARQQAEQ 1567
Cdd:TIGR02168 875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--------------ELREKLAQLELRLEGLEVRIDN 940
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1786808614 1568 ETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAE 1610
Cdd:TIGR02168 941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| REC_2_GGDEF |
cd17544 |
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This ... |
1876-1982 |
1.30e-17 |
|
second phosphoacceptor receiver (REC) domain of uncharacterized GGDEF domain proteins; This family is composed of uncharacterized PleD-like response regulators that contain two N-terminal REC domains and a C-terminal diguanylate cyclase output domain with the characteristic GGDEF motif at the active site. Unlike PleD which contains a REC-like adaptor domain, the second REC domain of these uncharacterized GGDEF domain proteins, described in this model, contains characteristic metal-binding and active site residues. PleD response regulators are global regulators of cell metabolism in some important human pathogens. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381098 [Multi-domain] Cd Length: 122 Bit Score: 80.64 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHaGDIKAVITDILMPFMDGVELCRELRKRDA--TLPIIVAS 1953
Cdd:cd17544 4 LVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQH-PDIKLVITDYNMPEMDGFELVREIRKKYSrdQLAIIGIS 82
|
90 100 110
....*....|....*....|....*....|...
gi 1786808614 1954 GMGHE----KFVtdlrELGVPLFLKKPFAAEEL 1982
Cdd:cd17544 83 ASGDNalsaRFI----KAGANDFLTKPFLPEEF 111
|
|
| REC_CheY |
cd17542 |
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response ... |
1876-1983 |
1.40e-17 |
|
phosphoacceptor receiver (REC) domain of chemotaxis protein CheY; The chemotaxis response regulator CheY contains a stand-alone REC domain. Chemotaxis is a behavior known for motile bacteria that directs their movement in response to chemical gradients. CheY is involved in transmitting sensory signals from chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381097 [Multi-domain] Cd Length: 117 Bit Score: 80.40 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17542 4 LIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDL--VTMDITMPEMDGIEALKEIKKIDPNAKVIMCSA 81
|
90 100
....*....|....*....|....*....
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELL 1983
Cdd:cd17542 82 MGQEEMVKEAIKAGAKDFIVKPFQPERVL 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
515-1047 |
1.47e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 515 QAGAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETaLAELRAQLERTEAARQQ 594
Cdd:COG1196 249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 595 IETTALDLrsnsEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQ 674
Cdd:COG1196 328 LEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 675 PVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQL 754
Cdd:COG1196 404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 755 QAETERREQAESALGQsksETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIK 834
Cdd:COG1196 484 EELAEAAARLLLLLEA---EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 835 ETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAR 914
Cdd:COG1196 561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 915 EALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREE 994
Cdd:COG1196 641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 995 LHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAE 1047
Cdd:COG1196 721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1144-1632 |
4.37e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 88.07 E-value: 4.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1144 REQLEKNLRQAAEEATRkAQALQAELQRAKKELEKELADAN--LELLDIRSRLDHEAAARRQAEESAKQgsasadQRLAE 1221
Cdd:COG1196 174 KEEAERKLEATEENLER-LEDILGELERQLEPLERQAEKAEryRELKEELKELEAELLLLKLRELEAEL------EELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1222 RLSEVQTLQERLrsEA--AQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATE 1299
Cdd:COG1196 247 ELEELEAELEEL--EAelAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1300 SGSALEVTRRLLNEERAARASALAELAARRAEVDRLtteqpHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRA 1379
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAEL-----AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1380 TDFEAANAALRGEMEKRLRLELTWQMQREDfDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSE 1459
Cdd:COG1196 400 AQLEELEEAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1460 LASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLN-RQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQD 1538
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1539 GFQQ---STAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEAQRAE 1615
Cdd:COG1196 559 AAAAieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
490
....*....|....*..
gi 1786808614 1616 EQLRHRRIEAVSTLAGG 1632
Cdd:COG1196 639 AVTLAGRLREVTLEGEG 655
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-774 |
5.35e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 87.68 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEK 304
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 305 AELEKRTasspAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:COG1196 316 ERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 385 ---RVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAgQGGGEVNPELAARI 461
Cdd:COG1196 392 lraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLE 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 462 AALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQr 541
Cdd:COG1196 471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ- 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 542 feQRVAELETDNQQLREQASRDTQAATTQRgeqetALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADAR 621
Cdd:COG1196 550 --NIVVEDDEVAAAAIEYLKAAKAGRATFL-----PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 622 QQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSEL 701
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 702 ETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSE 774
Cdd:COG1196 703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
|
| PAS_3 |
pfam08447 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
98-184 |
7.98e-17 |
|
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: 77.38 E-value: 7.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 98 ILFVNHRWSALTGRSQAESQGFG--WLLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLRNKDGSTRWVAGHAMRVLDDHE 175
Cdd:pfam08447 1 IIYWSPRFEEILGYTPEELLGKGesWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80
|
....*....
gi 1786808614 176 QPNGIIGSI 184
Cdd:pfam08447 81 KPVRVIGVA 89
|
|
| REC_2_DhkD-like |
cd17580 |
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal ... |
1876-1986 |
1.18e-16 |
|
second phosphoacceptor receiver (REC) domain of Dictyostelium discoideum hybrid signal transduction histidine kinase D and similar domains; Dictyostelium discoideum hybrid signal transduction histidine kinase D (DhkD) is a large protein that contains two histidine kinase (HK) and two REC domains on the intracellular side of a single pass transmembrane domain, and extracellular PAS and PAC domains that likely are involved in ligand binding. This model represents the second REC domain and similar domains. DhkD activates the cAMP phosphodiesterase RegA to ensure proper prestalk and prespore patterning, tip formation, and the vertical elongation of the mound into a finger, in Dictyostelium discoideum. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381118 [Multi-domain] Cd Length: 112 Bit Score: 77.50 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD--ATLPIIVAS 1953
Cdd:cd17580 2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDV--ILSDIGMPGMDGYELARRLRELPwlANTPAIALT 79
|
90 100 110
....*....|....*....|....*....|...
gi 1786808614 1954 GMGHEKFVTDLRELGVPLFLKKPFAAEELLRSL 1986
Cdd:cd17580 80 GYGQPEDRERALEAGFDAHLVKPVDPDELIELI 112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
873-1617 |
1.27e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 87.12 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 873 EARSQAEREAAERRQTEESLLQASRSSEERVALlASELEAAREALRSESARREEletalPKTKTELGQRLAEAAAEAAGL 952
Cdd:PTZ00121 1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKK-AEDARKAEEARKAEDARKAE-----EARKAEDAKRVEIARKAEDAR 1164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 953 RARMDFEAAERERVEAAWKlansateqhAAELKTllatAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQN 1032
Cdd:PTZ00121 1165 KAEEARKAEDAKKAEAARK---------AEEVRK----AEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1033 ELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELREsltdAERTTEALQADLDAALKAC 1112
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE----KKKADEAKKAEEKKKADEA 1307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1113 EEEAARRSQAEETARQshtefthrltAETGAREQLEknLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRS 1192
Cdd:PTZ00121 1308 KKKAEEAKKADEAKKK----------AEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1193 RLDHEAAARRQAEESAK----QGSASADQRLAERLSEVQtlQERLRSEAAQRETTEVElrdtRAALEKQLAEASAALREA 1268
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKadeaKKKAEEDKKKADELKKAA--AAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEA 1449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1269 SARLEQERderrrvvesltqTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATA 1348
Cdd:PTZ00121 1450 KKKAEEAK------------KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1349 RLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTA--LRTAEA 1426
Cdd:PTZ00121 1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeeARIEEV 1597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1427 KAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRV 1506
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1507 AELDSTE--ARLREECAHRERAEA-ELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQEttqRRSLEdalqqsh 1583
Cdd:PTZ00121 1678 EEAKKAEedEKKAAEALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED---KKKAE------- 1747
|
730 740 750
....*....|....*....|....*....|....
gi 1786808614 1584 gevELRVSERTAGLNAHVQQLEAELAEAQRAEEQ 1617
Cdd:PTZ00121 1748 ---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| PRK11466 |
PRK11466 |
hybrid sensory histidine kinase TorS; Provisional |
1419-1984 |
1.82e-16 |
|
hybrid sensory histidine kinase TorS; Provisional
Pssm-ID: 236914 [Multi-domain] Cd Length: 914 Bit Score: 86.11 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1419 TALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTT-AELQTNLNAARAELDM 1497
Cdd:PRK11466 209 SALRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIEDPGVRAQVATTLTTVSQYSDlLALYQQDSEISNHLQT 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1498 LNR----QFAQRVAEL----DSTEARLREECAHRERAEAE-----------------LDRMRDAQDGFQQSTAELNERLT 1552
Cdd:PRK11466 289 LAQnniaQFAQFSSEVsqlvDTIELRNQHGLAHLEKASARgqysllllgmvslcaliLILWRVVYRSVTRPLAEQTQALQ 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1553 RLTT-DVEAARQQA----EQETTQR-----RSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEqlrhrr 1622
Cdd:PRK11466 369 RLLDgDIDSPFPETagvrELDTIGRlmdafRSNVHALNRHREQLAAQVKARTAELQELVIEHRQARAEAEKASQ------ 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1623 ieAVSTLAGGMAHELNNVLAPVLMAAQLL-RKQVSGKSRTLVDSVESSAQRGADIVKQVLTFARGFHGERA------PVS 1695
Cdd:PRK11466 443 --AKSAFLAAMSHEIRTPLYGILGTAQLLaDNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGGKNvsvsdePFE 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1696 PEMLVRDIAKSVQETF-PRNVRVSSEVADDLP-LISADASQLHRVLLNLAVNArdampsggtLKFSAENVVVDESFIHhr 1773
Cdd:PRK11466 521 PRPLLESTLQLMSGRVkGRPIRLATDIADDLPtALMGDPRRIRQVITNLLSNA---------LRFTDEGSIVLRSRTD-- 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1774 ratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPA 1853
Cdd:PRK11466 590 -------GEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPL 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1854 ASAETSERPPQAELPRGNGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYdQHAGDIKAVITDILMPFMDG 1933
Cdd:PRK11466 663 RVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETL-QNSEPFAAALVDFDLPDYDG 741
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786808614 1934 VELCRELRKRDATLPIIvasgmGHEKFVTD--LRELGVPLF---LKKPFAAEELLR 1984
Cdd:PRK11466 742 ITLARQLAQQYPSLVLI-----GFSAHVIDetLRQRTSSLFrgiIPKPVPREVLGQ 792
|
|
| CitA |
COG3290 |
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction ... |
1523-1856 |
2.41e-16 |
|
Sensor histidine kinase DipB regulating citrate/malate metabolism [Signal transduction mechanisms];
Pssm-ID: 442519 [Multi-domain] Cd Length: 389 Bit Score: 83.36 E-value: 2.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1523 RERAEAELDRMRDAQDGFQQSTAE---LNERLTRLTTDVEAARQQAEQETTQRRSLE---DALQQSHGEVELRVSERTAG 1596
Cdd:COG3290 72 LLKLLEEIARLVEEREAVLESIREgviAVDRDGRITLINDAARRLLGLDAIGRPIDEvlaEVLETGERDEEILLNGRVLV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1597 LNAHVQQLEAELAEA-----QRAEEQLRHRRIEAVSTLAGGM---AHELNNVLAPVLMAAQLLRKQvsgKSRTLVDSVES 1668
Cdd:COG3290 152 VNRVPIRDDGRVVGAvatfrDRTELERLEEELEGVKELAEALraqRHDFRNHLHTISGLLQLGEYD---EALEYIDEISE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1669 SAQrgadivkQVLTFARGFHGERAPVSpemLVRDIAKSVQEtfpRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARD 1748
Cdd:COG3290 229 ELQ-------ELIDSLLSRIGNPVLAA---LLLGKAARARE---RGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIE 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1749 AmpsggTLKFSAENVVVDESFIHHrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSvGLGLATALGVV 1828
Cdd:COG3290 296 A-----VEKLPEEERRVELSIRDD--------GDELVIEVEDSGPGIPEELLEKIFERGFSTKLGEGR-GLGLALVKQIV 361
|
330 340
....*....|....*....|....*...
gi 1786808614 1829 QSHGGFILLETEEDKGTEFQIYLPAASA 1856
Cdd:COG3290 362 EKYGGTIEVESEEGEGTVFTVRLPKEGE 389
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
519-1255 |
2.65e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 2.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 519 GRSEADEAARAQVEAD--LRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIE 596
Cdd:PTZ00121 1054 GNHEGKAEAKAHVGQDegLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEA 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 597 TTALDLRSNSEQQLSETQRQLADARQQLQA---ESERRAQAESALGQSKSETERQLAEATAALADTRKQleEATTKAAEL 673
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKRVEIARKAEDArkaEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA--EAARKAEEE 1211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 674 QPVRE-------QLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRtvaeqAAAEAQQQ 746
Cdd:PTZ00121 1212 RKAEEarkaedaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR-----KADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 747 LAALRQQLQAETERREQAESAlgQSKSETERQLAEATAALAEVRAQLEQA-TTASSQREAEAKQAAAAQQQKLADQDAEL 825
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKKADAAkKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 826 KKTWDNLIKETEDREALEKQLAAA---RGDLERQLAETKAELDQQLAALAEARSQAE---REAAERRQTEESLLQA--SR 897
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEekkKADEAKKKAEEDKKKADELKKAAAAKKKADeakKKAEEKKKADEAKKKAeeAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 898 SSEErvalLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRArmdfEAAERERVEAAWKLANSAT 977
Cdd:PTZ00121 1445 KADE----AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK----KADEAKKAAEAKKKADEAK 1516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 978 EQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQ 1057
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1058 QLAEAAAAQAELRSRLEKETAARHETE--RELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEfth 1135
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--- 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1136 RLTAETGAREQLEKnlRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASA 1215
Cdd:PTZ00121 1674 KKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1786808614 1216 DQ----RLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALE 1255
Cdd:PTZ00121 1752 DEeekkKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRME 1795
|
|
| HATPase_TmoS-FixL-DctS-like |
cd16920 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1852 |
3.99e-16 |
|
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: 75.90 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNARDAMPSGGtlkfsaenvvvDESFIHHRRATGAKPGnYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16920 1 IQQVLINLVRNGIEAMSEGG-----------CERRELTIRTSPADDR-AVTISVKDTGPGIAEEVAGQLFDPFYTTKSEG 68
|
90 100 110
....*....|....*....|....*....|....*...
gi 1786808614 1815 qsVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16920 69 --LGMGLSICRSIIEAHGGRLSVESPAGGGATFQFTLP 104
|
|
| REC_DctD-like |
cd17549 |
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and ... |
1877-1987 |
4.52e-16 |
|
phosphoacceptor receiver (REC) domain of C4-dicarboxylic acid transport protein D (DctD) and similar proteins; C4-dicarboxylic acid transport protein D (DctD) is part of the two-component regulatory system DctB/DctD, which regulates C4-dicarboxylate transport via regulation of expression of the dctPQM operon and dctA. It is an activator of sigma(54)-RNA polymerase holoenzyme that uses the energy released from ATP hydrolysis to stimulate the isomerization of a closed promoter complex to an open complex capable of initiating transcription. DctD is a member of the NtrC family, characterized by a domain architecture containing an N-terminal REC domain, followed by a central sigma-54 interaction/ATPase domain, and a C-terminal DNA binding domain. The ability of the central domain to hydrolyze ATP and thus to interact effectively with a complex of RNA polymerase, sigma54, and promoter, is controlled by the phosphorylation status of the REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381101 [Multi-domain] Cd Length: 130 Bit Score: 76.37 E-value: 4.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1877 LADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMG 1956
Cdd:cd17549 3 LVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGV--VISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80
|
90 100 110
....*....|....*....|....*....|.
gi 1786808614 1957 HEKFVTDLRELGVPLFLKKPFAAEELLRSLH 1987
Cdd:cd17549 81 DVPMAVEAMRAGAYDFLEKPFDPERLLDVVR 111
|
|
| REC_hyHK |
cd17598 |
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase ... |
1891-1987 |
5.87e-16 |
|
phosphoacceptor receiver (REC) domain of uncharacterized hybrid sensor histidine kinase/response regulators; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase/response regulators contain all the elements of a classical TCS in a single polypeptide chain. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381128 [Multi-domain] Cd Length: 118 Bit Score: 75.83 E-value: 5.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1891 ILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD--ATLPIIVASGMGHEKFVTDLRELG 1968
Cdd:cd17598 17 ILEEQGYKVQVARNGREALAMLAEHRPTL--VISDIVMPEMDGYELCRKIKSDPdlKDIPVILLTTLSDPRDVIRGLECG 94
|
90
....*....|....*....
gi 1786808614 1969 VPLFLKKPFAAEELLRSLH 1987
Cdd:cd17598 95 ADNFITKPYDEKYLLSRIK 113
|
|
| HATPase_EvgS-ArcB-TorS-like |
cd16922 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases, many are hybrid ... |
1738-1852 |
6.06e-16 |
|
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: 75.61 E-value: 6.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1738 VLLNLAVNArdampsggtLKFSAENVVvdesFIHHRRATGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFF-----TTKE 1812
Cdd:cd16922 4 ILLNLLGNA---------IKFTEEGEV----TLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSqadssTTRK 70
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1786808614 1813 PGQSvGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16922 71 YGGT-GLGLAISKKLVELMGGDISVESEPGQGSTFTFTLP 109
|
|
| REC_TrrA-like |
cd17554 |
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and ... |
1875-1959 |
9.27e-16 |
|
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator TrrA and similar domains; Thermotoga maritima contains a two-component signal transduction system (TCS) composed of the ThkA sensory histidine kinase (HK) and its cognate response regulator (RR) TrrA; the specific function of the system is unknown. TCSs couple environmental stimuli to adaptive responses. TrrA is a stand-alone RR containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381106 [Multi-domain] Cd Length: 113 Bit Score: 74.95 E-value: 9.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDqhAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17554 3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLE--SEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80
|
....*
gi 1786808614 1955 MGHEK 1959
Cdd:cd17554 81 YSEYK 85
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
189-694 |
1.43e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 189 ERKVADDTRTTDQAAALDAALARVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGEL 268
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 269 DKQVAErtatftdiisgLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDfdk 348
Cdd:COG1196 364 EEALLE-----------AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA--- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 349 LQSSATQPDTALETVHHRLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELE 428
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 429 RTKEELVAESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQ 508
Cdd:COG1196 510 VKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALA 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 509 QLAAASQAGAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAEL----RAQ 584
Cdd:COG1196 590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLtggsRRE 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 585 LERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLE 664
Cdd:COG1196 670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749
|
490 500 510
....*....|....*....|....*....|
gi 1786808614 665 EATTKAAELQPVREQLAGEVQRGERAEAEL 694
Cdd:COG1196 750 EEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| REC_OmpR_YycF-like |
cd17614 |
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF ... |
1875-1992 |
3.99e-15 |
|
phosphoacceptor receiver (REC) domain of YrcF-like OmpR family response regulators; YycF appears to play an important role in cell wall integrity in a wide range of gram-positive bacteria, and may also modulate cell membrane integrity. It functions as part of a phosphotransfer system that ultimately controls the levels of competence within the bacteria. YycF belongs to the OmpR family of response regulators, which are characterized by a REC domain and a winged helix-turn-helix effector domain involved in DNA binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381130 [Multi-domain] Cd Length: 115 Bit Score: 73.23 E-value: 3.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd17614 1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDL--ILLDLMLPEKDGLEVCREVRKT-SNVPIIMLTA 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1955 MGHE-KFVTDLrELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:cd17614 78 KDSEvDKVLGL-ELGADDYVTKPFSNRELLARVKANLRR 115
|
|
| REC_hyHK_CKI1_RcsC-like |
cd17546 |
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators ... |
1875-1986 |
4.37e-15 |
|
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinases/response regulators similar to Arabidopsis thaliana CKI1 and Escherichia coli RcsC; This family is composed of hybrid sensor histidine kinases/response regulators that are sensor histidine kinases (HKs) fused with a REC domain, similar to the sensor histidine kinase CKI1 from Arabidopsis thaliana, which is involved in multi-step phosphorelay (MSP) signaling that mediates responses to a variety of important stimuli in plants. MSP involves a signal being transferred from HKs via histidine phosphotransfer proteins (AHP1-AHP5) to nuclear response regulators. The CKI1 REC domain specifically interacts with the downstream signaling protein AHP2, AHP3 and AHP5. The plant MSP system has evolved from the prokaryotic two-component system (TCS), which allows organisms to sense and respond to changes in environmental conditions. This family also includes bacterial hybrid sensor HKs such as Escherichia coli RcsC, which is a component of the Rcs signalling pathway that controls a variety of physiological functions like capsule synthesis, cell division, and motility. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381099 [Multi-domain] Cd Length: 113 Bit Score: 73.27 E-value: 4.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD---ATLPIIV 1951
Cdd:cd17546 1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDL--VLMDLQMPVMDGLEATRRIRELEgggRRTPIIA 78
|
90 100 110
....*....|....*....|....*....|....*
gi 1786808614 1952 ASGMGHEKFVTDLRELGVPLFLKKPFAAEELLRSL 1986
Cdd:cd17546 79 LTANALEEDREKCLEAGMDDYLSKPVKLDQLKEVL 113
|
|
| REC_PA4781-like |
cd19920 |
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar ... |
1879-1977 |
8.08e-15 |
|
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase PA4781 and similar domains; Pseudomonas aeruginosa cyclic di-GMP phosphodiesterase PA4781 contains an N-terminal REC domain and a C-terminal catalytic HD-GYP domain, characteristics of RpfG family response regulators. PA4781 is involved in cyclic di-3',5'-GMP (c-di-GMP) hydrolysis/degradation in a two-step reaction via the linear intermediate pGpG to produce GMP. Its unphosphorylated REC domain prevents accessibility of c-di-GMP to the active site. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381147 [Multi-domain] Cd Length: 103 Bit Score: 72.16 E-value: 8.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIvasgmg 1956
Cdd:cd19920 5 DDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDL--ILLDVMMPGMDGFEVCRRLKADPATrhIPVI------ 76
|
90 100 110
....*....|....*....|....*....|
gi 1786808614 1957 hekFVTDLR---------ELGVPLFLKKPF 1977
Cdd:cd19920 77 ---FLTALTdtedkvkgfELGAVDYITKPF 103
|
|
| orf27 |
CHL00148 |
Ycf27; Reviewed |
1873-1997 |
8.97e-15 |
|
Ycf27; Reviewed
Pssm-ID: 214376 [Multi-domain] Cd Length: 240 Bit Score: 75.91 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1873 ELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKrDATLPIIVA 1952
Cdd:CHL00148 7 EKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDL--VILDVMMPKLDGYGVCQEIRK-ESDVPIIML 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1786808614 1953 SGMGHEK-FVTDLrELGVPLFLKKPFAAEELLRSLHAELHREESAA 1997
Cdd:CHL00148 84 TALGDVSdRITGL-ELGADDYVVKPFSPKELEARIRSVLRRTNKKS 128
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
575-1456 |
9.85e-15 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.49 E-value: 9.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 575 ETALAELRAQLERTEAARQQIETtALDLRsnseQQLSETQRQLADAR-QQLQAESERRAQAESALGQSKSETERQLAEAT 653
Cdd:TIGR02168 192 EDILNELERQLKSLERQAEKAER-YKELK----AELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 654 AALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRAraeaaeaarlqvetTAQQSR 733
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE--------------ELESKL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 734 TVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAeakqaaaa 813
Cdd:TIGR02168 333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-------- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 814 qqqkladQDAELKKTWDNLIKETEDREALEKQLA-AARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESL 892
Cdd:TIGR02168 405 -------LEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 893 LQASRSSEERVALLASeLEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARmdfEAAERERVEA---- 968
Cdd:TIGR02168 478 DAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI---EAALGGRLQAvvve 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 969 ---AWKLANSATEQHAAELKTLLA---TAREELHAETAKRDAAEAAASQVRAELEATNAESSRALA------------AA 1030
Cdd:TIGR02168 554 nlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDN 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1031 QNELARESAERE---TTEAEFQRSK---SALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQAD 1104
Cdd:TIGR02168 634 ALELAKKLRPGYrivTLDGDLVRPGgviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1105 LDAALKACEEEAARRSQAEE---TARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATrKAQALQAELQRAKKELEKELA 1181
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKdlaRLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIE 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1182 DANLELLDIRSRLDheaAARRQAeesakqgsasadQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEA 1261
Cdd:TIGR02168 793 QLKEELKALREALD---ELRAEL------------TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1262 SAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASAlaelaarraevdRLTTEQPH 1341
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL------------EELREKLA 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1342 AIEEATARLKAQLAE-QEREREQLRLAAMSAEQRLRDRATDFEAANAALrgemeKRLRLELTwqmqredfdrRLGELT-T 1419
Cdd:TIGR02168 926 QLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRL-----KRLENKIK----------ELGPVNlA 990
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1786808614 1420 ALRTAEAKAG------SDSAELRHAHETLQQAHAELTRRLTER 1456
Cdd:TIGR02168 991 AIEEYEELKErydfltAQKEDLTEAKETLEEAIEEIDREARER 1033
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-931 |
1.39e-14 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 80.10 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAvaehELAVKTLQAEK 304
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL----AEELAELEEKL 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 305 AELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:TIGR02168 347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 385 RVALQteheKAERADAERELSEEAMVQTNTgiQQRLMELNAELERTKEELVAESARRTQAEAGQGggevnpELAARIAAL 464
Cdd:TIGR02168 427 LKKLE----EAELKELQAELEELEEELEEL--QEELERLEEALEELREELEEAEQALDAAERELA------QLQARLDSL 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 465 TEAKAQVEKElveqQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEA-----DEAARAQVEADLRAAh 539
Cdd:TIGR02168 495 ERLQENLEGF----SEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvvenLNAAKKAIAFLKQNE- 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 540 qrfEQRVAELETDNQQLREQASRDTQAATTQRG------EQETALAELRAQLE-----------RTEAARQQIETTALDL 602
Cdd:TIGR02168 570 ---LGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDPKLRKALSyllggvlvvddLDNALELAKKLRPGYR 646
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 603 ------------------RSNSEQQLSETQRQLADARQQLQAESERRAQAESALgqskSETERQLAEATAALADTRKQLE 664
Cdd:TIGR02168 647 ivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKAL----AELRKELEELEEELEQLRKELE 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 665 EATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQ 744
Cdd:TIGR02168 723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 745 QQLAALRQQLQAETERREQAESALGQSKSETERqlaeataalaevraqLEQATTASSQREAEAKQAAAAQQQKLADQDAE 824
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAA---------------TERRLEDLEEQIEELSEDIESLAAEIEELEEL 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 825 LKKTWDNLIKETEDREALEKQLAAARGDLE------RQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRS 898
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947
|
730 740 750
....*....|....*....|....*....|....
gi 1786808614 899 SEERVALLASELEAAREALRSESARR-EELETAL 931
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRlKRLENKI 981
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
37-193 |
1.47e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 75.83 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 37 VAVVKDTLFLAAGTVGLFLLLRRDIQKREQTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAES 116
Cdd:COG2202 98 VELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEEL 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786808614 117 QGFGWLLAVHPDDNKRVTEEWRKCVRGEKE-FRLDFRLRNKDGSTRWVAGHAmRVLDDHEQPNGIIGSILDINERKVA 193
Cdd:COG2202 178 LGKSLLDLLHPEDRERLLELLRRLLEGGREsYELELRLKDGDGRWVWVEASA-VPLRDGGEVIGVLGIVRDITERKRA 254
|
|
| REC_CpdR_CckA-like |
cd18160 |
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; ... |
1875-1977 |
1.54e-14 |
|
phosphoacceptor receiver (REC) domain of Brucella abortus CpdR and CckA, and similar domains; Two-component systems (TCSs), consisting of a sensor and a response regulator, are used by bacteria to adapt to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis and membrane transport. Response regulators share the common phosphoacceptor REC domain and differ output domains such as DNA, RNA, ligand, and protein-binding, or enzymatic domain. CpdR is a stand-alone REC protein. CckA is a sensor histidine kinase containing N-terminal PAS domains and a C-terminal REC domain. CpdR and CckA are components of a regulatory phosphorelay system (composed of CckA, ChpT, CtrA and CpdR) that controls Brucella abortus cell growth, division, and intracellular survival inside mammalian host cells. CckA autophosphorylates in the presence of ATP and transfers a phosphoryl group to the conserved aspartic acid residue on its C-terminal REC domain, which is relayed to the ChpT phosphotransferase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381144 [Multi-domain] Cd Length: 103 Bit Score: 71.38 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQhAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd18160 2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQ-GKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80
|
90 100
....*....|....*....|...
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPF 1977
Cdd:cd18160 81 GAAAAPELLSDAVGDNATLKKPF 103
|
|
| HATPase_Glnl-NtrB-like |
cd16918 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1852 |
1.58e-14 |
|
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: 71.28 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNARDAMP-SGGTLKFSAEnvvvdesfiHHRRATGAKPGNYVLFRVT--DSGVGIPRDILPRIFEPFFTTK 1811
Cdd:cd16918 1 LIQVFLNLVRNAAQALAgSGGEIILRTR---------TQRQVTLGHPRHRLALRVSviDNGPGIPPDLQDTIFYPMVSGR 71
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1786808614 1812 EPGqsVGLGLATALGVVQSHGGFIllETEEDKG-TEFQIYLP 1852
Cdd:cd16918 72 ENG--TGLGLAIAQNIVSQHGGVI--ECDSQPGhTVFSVSLP 109
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1074-1629 |
1.62e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 79.70 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1074 EKETAARHETERELRESLtdaerttealqADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKnLRQ 1153
Cdd:PRK02224 198 EKEEKDLHERLNGLESEL-----------AELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED-LRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1154 AAEEATRKAQALQAELQRAKKELEkELADANLELLDI--RSRLDHEAAARRQAEESAKqgsasaDQRLAERLSEVQTLQ- 1230
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLE-ELEEERDDLLAEagLDDADAEAVEARREELEDR------DEELRDRLEECRVAAq 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1231 ------ERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSAL 1304
Cdd:PRK02224 339 ahneeaESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1305 EVTRRLLNEERAARASALAELAARRAEVDRLTT-----------EQPHAieEATARLKAQLAEQEREREQLRLAAMSAEQ 1373
Cdd:PRK02224 419 EERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpveGSPHV--ETIEEDRERVEELEAELEDLEEEVEEVEE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1374 RLrDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRR------LGELTTALRTAEAKAGSDSAELRHAHETLQQAHA 1447
Cdd:PRK02224 497 RL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKreraeeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1448 ELTRRLTERDSE---LASVREQAAALDAAGTRAQqttaelqtNLNAARAELDMLNRQFAQRVAELDSTEARLREEC--AH 1522
Cdd:PRK02224 576 ELNSKLAELKERiesLERIRTLLAAIADAEDEIE--------RLREKREALAELNDERRERLAEKRERKRELEAEFdeAR 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1523 RERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQettqrrslEDALQQSHGEVELRVsERTAGLNAHVQ 1602
Cdd:PRK02224 648 IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE--------LEELRERREALENRV-EALEALYDEAE 718
|
570 580
....*....|....*....|....*..
gi 1786808614 1603 QLEAELAEAqRAEeqLRHRRIEAVSTL 1629
Cdd:PRK02224 719 ELESMYGDL-RAE--LRQRNVETLERM 742
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
225-702 |
2.18e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 79.21 E-value: 2.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEK 304
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 305 AELEKRTAsspAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:COG1196 379 EELEELAE---ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 385 RVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPELAARIAAL 464
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 465 TEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAA--AARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQRF 542
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 543 EQRVAEL--ETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADA 620
Cdd:COG1196 616 YVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 621 RQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSE 700
Cdd:COG1196 696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
|
..
gi 1786808614 701 LE 702
Cdd:COG1196 776 IE 777
|
|
| glnL |
PRK11073 |
nitrogen regulation protein NR(II); |
1575-1852 |
3.20e-14 |
|
nitrogen regulation protein NR(II);
Pssm-ID: 182947 [Multi-domain] Cd Length: 348 Bit Score: 76.27 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1575 LEDALQQSHG----EVELRVSERTAGLNAHVQQLE-----AELA--EAQR--AEEQLRHRRIEAVSTLAGGMAHELNNVL 1641
Cdd:PRK11073 66 MRESLQAGQGftdnEVTLVIDGRSHILSLTAQRLPegmilLEMApmDNQRrlSQEQLQHAQQVAARDLVRGLAHEIKNPL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1642 APVLMAAQLLRKQVSGKSRTLVDSV-ESSAQRGADIVKQVLTFARgfHGERAPVSPEMLVRDIAKSVQETFPRNVRVSSE 1720
Cdd:PRK11073 146 GGLRGAAQLLSKALPDPALTEYTKViIEQADRLRNLVDRLLGPQR--PGTHVTESIHKVAERVVQLVSLELPDNVRLIRD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1721 VADDLPLISADASQLHRVLLNLAVNARDAM-PSGGTLKFSAENVVvdESFIHHRRatgakpgnYVL---FRVTDSGVGIP 1796
Cdd:PRK11073 224 YDPSLPELAHDPDQIEQVLLNIVRNALQALgPEGGTITLRTRTAF--QLTLHGER--------YRLaarIDIEDNGPGIP 293
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786808614 1797 RDILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFIllETEEDKG-TEFQIYLP 1852
Cdd:PRK11073 294 PHLQDTLFYPMVSGREGG--TGLGLSIARNLIDQHSGKI--EFTSWPGhTEFSVYLP 346
|
|
| PRK09959 |
PRK09959 |
acid-sensing system histidine kinase EvgS; |
1701-1992 |
4.36e-14 |
|
acid-sensing system histidine kinase EvgS;
Pssm-ID: 182169 [Multi-domain] Cd Length: 1197 Bit Score: 78.24 E-value: 4.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1701 RDIAKSVQETFPrnvrvssevadDLPLISADASQLHRVLLNLAVNArdampsggtLKFSAENVV-VDESFIHhrratgaK 1779
Cdd:PRK09959 806 KSIALSCSSTFP-----------DHYLVKIDPQAFKQVLSNLLSNA---------LKFTTEGAVkITTSLGH-------I 858
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1780 PGNYVLFRVT--DSGVGIPRDILPRIFEPFFTTKEPGQSVG--LGLATALGVVQSHGGFILLETEEDKGTEFQIYLP--- 1852
Cdd:PRK09959 859 DDNHAVIKMTimDSGSGLSQEEQQQLFKRYSQTSAGRQQTGsgLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPvei 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1853 ----AASAETSERPpqAELPRGNGelLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILM 1928
Cdd:PRK09959 939 sqqvATVEAKAEQP--ITLPEKLS--ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDL--LITDVNM 1012
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786808614 1929 PFMDGVELCRELRKRDATLPI--IVASGMGHEKfvTDLRELGVPLFLKKPFAAeELLRSLHAELHR 1992
Cdd:PRK09959 1013 PNMDGFELTRKLREQNSSLPIwgLTANAQANER--EKGLSCGMNLCLFKPLTL-DVLKTHLSQLHQ 1075
|
|
| REC_OmpR_PrrA-like |
cd17627 |
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The ... |
1875-1992 |
5.59e-14 |
|
phosphoacceptor receiver (REC) domain of PrrA-like OmpR family response regulators; The Mycobacterium tuberculosis PrrA is part of the PrrA/PrrB two-component system (TCS) that has been implicated in early intracellular multiplication and is essential for viability. Also included in this subfamily is Mycobacterium tuberculosis MprA, part of the MprAB TCS that regulates EspR, a key regulator of the ESX-1 secretion system, and is required for establishment and maintenance of persistent infection in a tissue- and stage-specific fashion. PrrA and MprA belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381142 [Multi-domain] Cd Length: 116 Bit Score: 70.10 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17627 1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPD--AVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTA 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1955 MGH-EKFVTDLrELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:cd17627 79 RDSvSDRVAGL-DAGADDYLVKPFALEELLARVRALLRR 116
|
|
| REC_D1_PleD-like |
cd17538 |
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar ... |
1875-1977 |
5.81e-14 |
|
first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains; PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381093 [Multi-domain] Cd Length: 104 Bit Score: 69.45 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIva 1952
Cdd:cd17538 2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDL--ILLDVMMPGMDGFEVCRRLKEDPETrhIPVI-- 77
|
90 100 110
....*....|....*....|....*....|....
gi 1786808614 1953 sgmghekFVTDLR---------ELGVPLFLKKPF 1977
Cdd:cd17538 78 -------MITALDdredrirglEAGADDFLSKPI 104
|
|
| REC_RssB-like |
cd17555 |
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; ... |
1879-1956 |
6.16e-14 |
|
phosphoacceptor receiver (REC) domain of Pseudomonas aeruginosa RssB and similar domains; Pseudomonas aeruginosa RssB is an orphan atypical response regulator containing a REC domain and a PP2C-type protein phosphatase output domain. Its function is still unknown. Escherichia RssB, which is not included in this subfamily, is a ClpX adaptor protein which alters ClpX specificity by mediating a specific interaction between ClpX and the substrates such as RpoS, an RNA polymerase sigma factor. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381107 [Multi-domain] Cd Length: 116 Bit Score: 69.92 E-value: 6.16e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786808614 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMG 1956
Cdd:cd17555 7 DDDEVVRESIAAYLEDSGFQVLQAADGRQGLELFRSEQPDL--VLCDLRMPEMDGLEVLKQITKESPDTPVIVVSGAG 82
|
|
| PAS |
COG2202 |
PAS domain [Signal transduction mechanisms]; |
66-193 |
6.69e-14 |
|
PAS domain [Signal transduction mechanisms];
Pssm-ID: 441804 [Multi-domain] Cd Length: 258 Bit Score: 73.91 E-value: 6.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 66 QTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEK 145
Cdd:COG2202 1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1786808614 146 EFRLDFRLRNKDGSTRWVAGHAMRVLDDHEQPNGIIGSILDINERKVA 193
Cdd:COG2202 81 VWRGELRNRRKDGSLFWVELSISPVRDEDGEITGFVGIARDITERKRA 128
|
|
| REC_OmpR_BsPhoP-like |
cd19937 |
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus ... |
1876-1983 |
6.91e-14 |
|
phosphoacceptor receiver (REC) domain of BsPhoP-like OmpR family response regulators; Bacillus subtilis PhoP (BsPhoP) is part of the PhoPR two-component system that participates in a signal transduction network that controls adaptation of the bacteria to phosphate deficiency by regulating (activating or repressing) genes of the Pho regulon upon phosphorylation by PhoR. When activated, PhoPR directs expression of phosphate scavenging enzymes, lowers synthesis of the phosphate-rich wall teichoic acid (WTA) and initiates synthesis of teichuronic acid, a non-phosphate containing replacement anionic polymer. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381164 [Multi-domain] Cd Length: 116 Bit Score: 69.99 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELR--KRDATLPIIVAS 1953
Cdd:cd19937 1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDL--IILDLMLPGIDGLEVCRILRsdPKTSSIPIIMLT 78
|
90 100 110
....*....|....*....|....*....|.
gi 1786808614 1954 GMGHE-KFVTDLrELGVPLFLKKPFAAEELL 1983
Cdd:cd19937 79 AKGEEfDKVLGL-ELGADDYITKPFSPRELL 108
|
|
| REC_typeB_ARR-like |
cd17584 |
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and ... |
1876-1982 |
8.33e-14 |
|
phosphoacceptor receiver (REC) domain of type B Arabidopsis response regulators (ARRs) and similar domains; Type-B ARRs (Arabidopsis response regulators) are a class of MYB-type transcription factors that act as major players in the transcriptional activation of cytokinin-responsive genes. They directly regulate the expression of type-A ARR genes and other downstream target genes. Cytokinin is a plant hormone implicated in many growth and development processes including shoot organogenesis, leaf senescence, sink/source relationships, vascular development, lateral bud release, and photomorphogenic development. Cytokinin signaling involves a phosphorelay cascade by histidine kinase receptors (AHKs), histidine phosphotransfer proteins (AHPs) and downstream ARRs. ARRs are divided into two groups, type-A and -B, according to their sequence and domain structure. Type-B ARRs contain a receiver (REC) domain and a large C-terminal extension that has characteristics of an effector or output domain, with a Myb-like DNA binding domain referred to as the GARP domain. The GARP domain is a motif specific to plant transcription factors. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381121 [Multi-domain] Cd Length: 115 Bit Score: 69.58 E-value: 8.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIKAVITDILMPFMDGVELCRELRKrDATLPIIVASGM 1955
Cdd:cd17584 2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIRL-EMDLPVIMMSAD 80
|
90 100
....*....|....*....|....*..
gi 1786808614 1956 GHEKFVTDLRELGVPLFLKKPFAAEEL 1982
Cdd:cd17584 81 GSTSTVMKGLAHGACDYLLKPVSIEDL 107
|
|
| CitB |
COG4565 |
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal ... |
1876-1986 |
1.29e-13 |
|
DNA-binding response regulator DpiB of citrate/malate metabolism [Transcription, Signal transduction mechanisms];
Pssm-ID: 443622 [Multi-domain] Cd Length: 138 Bit Score: 69.61 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILE-WHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVAS 1953
Cdd:COG4565 7 LIVEDDPMVAELLRRYLErLPGFEVVgVASSGEEALALLAEHRPDL--ILLDIYLPDGDGLELLRELRARGPDVDVIVIT 84
|
90 100 110
....*....|....*....|....*....|...
gi 1786808614 1954 GMGHEKFVTDLRELGVPLFLKKPFAAEELLRSL 1986
Cdd:COG4565 85 AARDPETVREALRAGVVDYLIKPFTFERLREAL 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
421-1186 |
1.40e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 77.10 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 421 MELNAELERTKEEL-VAESARRTQAEAGQgggevnpelAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEA 499
Cdd:PTZ00121 1084 KEDNRADEATEEAFgKAEEAKKTETGKAE---------EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 500 AAARAALEQQLAAASQAGAGRSEADEAARAqvEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALA 579
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKA--EEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 580 ElRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLAD--ARQQLQAESERRAQAESALGQSKSETERQLAEATAALA 657
Cdd:PTZ00121 1233 E-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAikAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 658 DTRKQLEEATTKAAELQPVREQLAGEVQ----RGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSR 733
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEeakkAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 734 TVAEQAAAEAQQQLAALRQQLQAETERR--EQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAA 811
Cdd:PTZ00121 1392 KADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 812 AAQqqklADQDAELKKTWDNLIKETEDrealekqlAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEEs 891
Cdd:PTZ00121 1472 ADE----AKKKAEEAKKADEAKKKAEE--------AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE- 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 892 llqASRSSEERVA---LLASELEAAREALRSESARREELETALPKTKTELGQRLAEA--AAEAAGLRARMDFEAAERERV 966
Cdd:PTZ00121 1539 ---AKKAEEKKKAdelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKA 1615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 967 EAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALA------------------ 1028
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeakkaeedekkaaealk 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1029 -----AAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQA 1103
Cdd:PTZ00121 1696 keaeeAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1104 DLDAALKAC--EEEAARRSQAEETARQSHTEFThrLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAK-KELEKEL 1180
Cdd:PTZ00121 1776 EKEAVIEEEldEEDEKRRMEVDKKIKDIFDNFA--NIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEaDAFEKHK 1853
|
....*.
gi 1786808614 1181 ADANLE 1186
Cdd:PTZ00121 1854 FNKNNE 1859
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
225-940 |
1.55e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 76.63 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 225 ELERRADELKK------RDSELESANRQLWAELSGR--EQVEAELAKARGELDKQVAERTAtftdiisgLEKAVAEHELA 296
Cdd:TIGR02168 197 ELERQLKSLERqaekaeRYKELKAELRELELALLVLrlEELREELEELQEELKEAEEELEE--------LTAELQELEEK 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 297 VKTLQAEKAELEKRTASSPAELEALRKRLSDeatrrqlAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKR 376
Cdd:TIGR02168 269 LEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 377 LETELESLRVALQTEHEKAERADAERELSEEAMVQtntgIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPE 456
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 457 -LAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADL 535
Cdd:TIGR02168 418 rLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 536 RAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQ---ETALAELRAQL--ERTEAARQQIET------------- 597
Cdd:TIGR02168 498 QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEaaiEAALGGRLQAVvvENLNAAKKAIAFlkqnelgrvtflp 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 598 ----TALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETErqLAEATAALADTRKQL---------- 663
Cdd:TIGR02168 578 ldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD--LDNALELAKKLRPGYrivtldgdlv 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 664 ----------EEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSR 733
Cdd:TIGR02168 656 rpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 734 TVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQreaeakqaaaa 813
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----------- 804
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 814 qqqkLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERqLAETKAELDQQLAALAEARSQAEREAAERRQTEESLL 893
Cdd:TIGR02168 805 ----LDELRAELTLLNEEAANLRERLESLERRIAATERRLED-LEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 1786808614 894 QASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQ 940
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
532-1278 |
2.51e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.86 E-value: 2.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 532 EADLRAAHQRFEQRVAELETDNQQLREqasrdtqaATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNseqqLS 611
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKE--------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 612 ETQRQLADARQQLQAESERRAQAEsalgqskseteRQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAE 691
Cdd:TIGR02168 292 ALANEISRLEQQKQILRERLANLE-----------RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 692 AELFRSRSELETQQAALAEL-RARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQ 770
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 771 SKSETERQLAEATAALAEVRAQLEQAtTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAAR 850
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEEL-REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 851 GDLER--QLAETKAELDQQLAALAEARSQA--EREAAERRQTEESLLQASRSseeRVALLASELEAAREALRSESARRE- 925
Cdd:TIGR02168 520 GILGVlsELISVDEGYEAAIEAALGGRLQAvvVENLNAAKKAIAFLKQNELG---RVTFLPLDSIKGTEIQGNDREILKn 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 926 ---------ELETALPKTKTELG---------QRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHA------ 981
Cdd:TIGR02168 597 iegflgvakDLVKFDPKLRKALSyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSsilerr 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 982 ---AELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNA---ESSRALAAAQNELARESAERETTEAEFQRsksaL 1055
Cdd:TIGR02168 677 reiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleELSRQISALRKDLARLEAEVEQLEERIAQ----L 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1056 AQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQAdLDAALKACEEEAARRSQAEETARQSHTEFTH 1135
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLNEEAANLRERLESLER 831
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1136 RLTAETGAREQLEKNLRQAAEEATR------KAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAK 1209
Cdd:TIGR02168 832 RIAATERRLEDLEEQIEELSEDIESlaaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 1210 QGSASAdQRLAERLSEVQTLQERLRSEAAQ-----RETTEVELRDTrAALEKQLAEASAALREASARLEQERDE 1278
Cdd:TIGR02168 912 ELRREL-EELREKLAQLELRLEGLEVRIDNlqerlSEEYSLTLEEA-EALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
757-1414 |
4.20e-13 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 75.18 E-value: 4.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 757 ETERREQAESALGQSKSETERQLAEATAALAEVRaQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKET 836
Cdd:PTZ00121 1107 ETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR-KAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 837 EDREALEKQLAA-ARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEEsllQASRSSEERVALLASELEAAR- 914
Cdd:PTZ00121 1186 EVRKAEELRKAEdARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARm 1262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 915 -------EALRSESARR-EELETALPKTKTElgqrlAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQhAAELKT 986
Cdd:PTZ00121 1263 ahfarrqAAIKAEEARKaDELKKAEEKKKAD-----EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK-ADAAKK 1336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 987 LLATAREElhAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAErETTEAEFQRSKSALAQQLAEAAAAQ 1066
Cdd:PTZ00121 1337 KAEEAKKA--AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADELKKA 1413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1067 AELRSRLEkETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQ 1146
Cdd:PTZ00121 1414 AAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1147 LE-----KNLRQAAEEATRKAQALQAELQRAKKELEKelADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAE 1221
Cdd:PTZ00121 1493 EEakkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1222 RLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQL-AEASAALREASARLEQER--DERRRVVESLTQTSTTLEARAT 1298
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAE 1650
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1299 ESGSALEVTR-RLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATAR----LKAQLAEQEREREQLRLA----AM 1369
Cdd:PTZ00121 1651 ELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaeeLKKKEAEEKKKAEELKKAeeenKI 1730
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 1370 SAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQ-------------------MQREDFDRRL 1414
Cdd:PTZ00121 1731 KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEeekkaeeirkekeavieeeLDEEDEKRRM 1794
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
366-1176 |
4.45e-13 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 75.09 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 366 RLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEEL--VAESARRTQ 443
Cdd:TIGR02168 180 KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELkeAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 444 AEAGQGGGEVNpELAARIAALTEAKAQVEKELVEQQA------VAKALGDERNRLAQELAEAAAARAALEQQLAAASQAG 517
Cdd:TIGR02168 260 AELQELEEKLE-ELRLEVSELEEEIEELQKELYALANeisrleQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 518 AGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQ--ASRDTQAATTQRGEQETA-LAELRAQLERTEAARQQ 594
Cdd:TIGR02168 339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQleTLRSKVAQLELQIASLNNeIERLEARLERLEDRRER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 595 IETTALDLRSN-SEQQLSETQRQLADARQQLQAESERRAQAESALgqskSETERQLAEATAALADTRKQLEEATTKAAEL 673
Cdd:TIGR02168 419 LQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEAL----EELREELEEAEQALDAAERELAQLQARLDSL 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 674 QPVREQLAGEvQRGERAE--------------AELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTvAEQA 739
Cdd:TIGR02168 495 ERLQENLEGF-SEGVKALlknqsglsgilgvlSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQN-ELGR 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 740 AAEAQQQLAALRQQLQAETERREQAESALGQSKSETErqlaEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLA 819
Cdd:TIGR02168 573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVK----FDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 820 DQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAETK---AELDQQLAALAEARSQAEREAAERRQTEESLLQAS 896
Cdd:TIGR02168 649 TLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQI 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 897 RSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAglrarmdfEAAERERVEAAWKLANSA 976
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA--------EIEELEAQIEQLKEELKA 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 977 TEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATnAESSRALAAAQNELARESAERETTEAEFQRSKSALA 1056
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL-EEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1057 QQLAEAAAAQAELRSRLEKETAARHETERELREsltdaerttealqadLDAALKACEEEAARRSQAEETARQSHTEFTHR 1136
Cdd:TIGR02168 880 NERASLEEALALLRSELEELSEELRELESKRSE---------------LRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1786808614 1137 LTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKEL 1176
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| REC_PdtaR-like |
cd19932 |
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes ... |
1875-1992 |
4.75e-13 |
|
phosphoacceptor receiver (REC) domain of PdtaR and similar proteins; This subfamily includes Mycobacterium tuberculosis PdtaR, also called Rv1626, and similar proteins containing a REC domain and an ANTAR (AmiR and NasR transcription antitermination regulators) RNA-binding output domain. PdtaR is a response regulator that acts at the level of transcriptional antitermination and is a member of the PdtaR/PdtaS two-component regulatory system. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381159 [Multi-domain] Cd Length: 118 Bit Score: 67.44 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATlPIIVAS 1953
Cdd:cd19932 3 VLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDL--VIMDVKMPRLDGIEAAKIITSENIA-PIVLLT 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1954 GMGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:cd19932 80 AYSQQDLVERAKEAGAMAYLVKPFSESDLIPAIEMAIAR 118
|
|
| REC_NarL-like |
cd17535 |
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family ... |
1876-1988 |
1.04e-12 |
|
phosphoacceptor receiver (REC) domain of NarL (Nitrate/Nitrite response regulator L) family response regulators; The NarL family is one of the more abundant families of DNA-binding response regulators (RRs). Members of the NarL family contain a REC domain and a helix-turn-helix (HTH) DNA-binding output domain, with a majority of members containing a LuxR-type HTH domain. They function as transcriptional regulators. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381090 [Multi-domain] Cd Length: 117 Bit Score: 66.38 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILE-WHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVAS 1953
Cdd:cd17535 2 LIVDDHPLVREGLRRLLEsEPDIEVVgEAADGEEALALLRELRPDV--VLMDLSMPGMDGIEALRRLRRRYPDLKVIVLT 79
|
90 100 110
....*....|....*....|....*....|....*
gi 1786808614 1954 GMGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHA 1988
Cdd:cd17535 80 AHDDPEYVLRALKAGAAGYLLKDSSPEELIEAIRA 114
|
|
| HATPase_TutC-TodS-like |
cd16925 |
Histidine kinase-like ATPase domain of hybrid sensor histidine kinases similar to Pseudomonas ... |
1731-1852 |
1.32e-12 |
|
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: 65.98 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1731 DASQLHRVLLNLAVNARDAMPSGGTLKFSAEnvvvdesfihhrratgAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTT 1810
Cdd:cd16925 1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILE----------------KFRLNRFLLTVSDSGPGIPPNLREEIFERFRQG 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1786808614 1811 KEPGQ----SVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16925 65 DGSSTrahgGTGLGLSIVKEFVELHGGTVTVSDAPGGGALFQVELP 110
|
|
| HATPase_CpxA-like |
cd16949 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1853 |
1.34e-12 |
|
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: 65.81 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNArdampsggtLKFSAENVVVDesfihhrratGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16949 1 LARALENVLRNA---------LRYSPSKILLD----------ISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSAR 61
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1786808614 1815 QS----VGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPA 1853
Cdd:cd16949 62 DResggTGLGLAIAERAIEQHGGKIKASNRKPGGLRVRIWLPA 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
189-934 |
1.36e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 73.64 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 189 ERKVADDTRTTDQAAALDAALaRVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAElSGREQVEAELAKARGEL 268
Cdd:PTZ00121 1192 ELRKAEDARKAEAARKAEEER-KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE-EIRKFEEARMAHFARRQ 1269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 269 DKQVAERTATFTDIISGLEKAVAEHelAVKTLQAEKAELEKRTASSPAELEALRKRlSDEATRRQlaeddlrslredfDK 348
Cdd:PTZ00121 1270 AAIKAEEARKADELKKAEEKKKADE--AKKAEEKKKADEAKKKAEEAKKADEAKKK-AEEAKKKA-------------DA 1333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 349 LQSSATQPDTALETVHHRLHAETERVKRLETELESLRvaLQTEHEKaERADAERELSEEamVQTNTGIQQRLMELNAELE 428
Cdd:PTZ00121 1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAK-KKADAAKKKAEE--KKKADEAKKKAEEDKKKAD 1408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 429 RTKEelvAESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGD--ERNRLAQELAEAAAARAAL 506
Cdd:PTZ00121 1409 ELKK---AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKA 1485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 507 EQQLAAASQAGAGRSEADEAARAQVEADlraahqrfEQRVAELETDNQQLReQASRDTQAATTQRGEQETALAELRA--Q 584
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKAD--------EAKKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELKKaeE 1556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 585 LERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLE 664
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 665 EATTKAAELQPVREQLAGEVQRGERAEAELFRSRSEletQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQ 744
Cdd:PTZ00121 1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 745 QQLAALRQQLQAEtERREQAESAlgQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQ-QQKLADQDA 823
Cdd:PTZ00121 1714 EKKKAEELKKAEE-ENKIKAEEA--KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDE 1790
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 824 ELKKTWDNLIKETED-----REALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRS 898
Cdd:PTZ00121 1791 KRRMEVDKKIKDIFDnfaniIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADF 1870
|
730 740 750
....*....|....*....|....*....|....*.
gi 1786808614 899 SEERvALLASELEAAREALRSESARREELETALPKT 934
Cdd:PTZ00121 1871 NKEK-DLKEDDEEEIEEADEIEKIDKDDIEREIPNN 1905
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1075-1614 |
2.74e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.26 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1075 KETAARHETERELRESLTDAERTT--EALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAR-EQLEKNL 1151
Cdd:COG4913 268 RERLAELEYLRAALRLWFAQRRLEllEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1152 RQAAEEATRKAQALqAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQE 1231
Cdd:COG4913 348 ERLERELEERERRR-ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1232 RLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLE-QERDER-RRVVES-LTQTSTTL------EARATESGS 1302
Cdd:COG4913 427 EIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGELIEvRPEEERwRGAIERvLGGFALTLlvppehYAAALRWVN 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1303 ALEVTRRL-LNEERAARASALAELAARRAEVDRLTTEqPHaieEATARLKAQLAEQE-----REREQLRLA--AMSAEQR 1374
Cdd:COG4913 507 RLHLRGRLvYERVRTGLPDPERPRLDPDSLAGKLDFK-PH---PFRAWLEAELGRRFdyvcvDSPEELRRHprAITRAGQ 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1375 LRDRATdfeaanaalRGEMEKRLRLELTWQM------QREDFDRRLGELTTALRTAEAKAgSDSAELRHAHETLQQAHAE 1448
Cdd:COG4913 583 VKGNGT---------RHEKDDRRRIRSRYVLgfdnraKLAALEAELAELEEELAEAEERL-EALEAELDALQERREALQR 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1449 LtRRLTERDSELASVREQAAALDAAgtraqqttaelQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEA 1528
Cdd:COG4913 653 L-AEYSWDEIDVASAEREIAELEAE-----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1529 ELDRMRDAQDgfqqstaelneRLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAEL 1608
Cdd:COG4913 721 ELEQAEEELD-----------ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
....*.
gi 1786808614 1609 AEAQRA 1614
Cdd:COG4913 790 ERAMRA 795
|
|
| REC_Ycf29 |
cd19927 |
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a ... |
1875-1976 |
2.97e-12 |
|
phosphoacceptor receiver (REC) domain of probable transcriptional regulator Ycf29; Ycf29 is a probable response regulator of a two-component system (TCS), typically consisting a sensor and a response regulator, that functions in adaptation to changing environments. Processes regulated by TCSs in bacteria include sporulation, pathogenicity, virulence, chemotaxis, and membrane transport. Ycf29 contains an N-terminal REC domain and a LuxR-type helix-turn-helix DNA-binding output domain. REC domains function as phosphorylation-mediated switches within RRs, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381154 [Multi-domain] Cd Length: 102 Bit Score: 64.71 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD--ATLPIIV- 1951
Cdd:cd19927 1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDL--IISDIIMPGVDGYSLLGKLRKNAdfDTIPVIFl 78
|
90 100
....*....|....*....|....*.
gi 1786808614 1952 -ASGMGHEKFVTdlRELGVPLFLKKP 1976
Cdd:cd19927 79 tAKGMTSDRIKG--YNAGCDGYLSKP 102
|
|
| REC_OmpR_ChvI-like |
cd19936 |
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; ... |
1877-1976 |
3.05e-12 |
|
phosphoacceptor receiver (REC) domain of ChvI-like OmpR family response regulators; Sinorhizobium meliloti ChvI is part of the ExoS/ChvI two-component regulatory system (TCS) that is required for nitrogen-fixing symbiosis and exopolysaccharide synthesis. ExoS/ChvI also play important roles in regulating biofilm formation, motility, nutrient utilization, and the viability of free-living bacteria. ChvI belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381163 [Multi-domain] Cd Length: 99 Bit Score: 64.39 E-value: 3.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1877 LADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASGMG 1956
Cdd:cd19936 3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDL--AILDIKMPRMDGMELLQRLRQK-STLPVIFLTSKD 79
|
90 100
....*....|....*....|.
gi 1786808614 1957 HE-KFVTDLReLGVPLFLKKP 1976
Cdd:cd19936 80 DEiDEVFGLR-MGADDYITKP 99
|
|
| PRK10955 |
PRK10955 |
envelope stress response regulator transcription factor CpxR; |
1875-1992 |
3.34e-12 |
|
envelope stress response regulator transcription factor CpxR;
Pssm-ID: 182864 [Multi-domain] Cd Length: 232 Bit Score: 68.29 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQhagDIKAVITDILMPFMDGVELCRELRKRDATlPIIVASG 1954
Cdd:PRK10955 4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD---SIDLLLLDVMMPKKNGIDTLKELRQTHQT-PVIMLTA 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:PRK10955 80 RGSELDRVLGLELGADDYLPKPFNDRELVARIRAILRR 117
|
|
| REC_FixJ |
cd17537 |
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response ... |
1879-1986 |
4.52e-12 |
|
phosphoacceptor receiver (REC) domain of FixJ family response regulators; FixJ family response regulators contain an N-terminal receiver domain (REC) and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. The Sinorhizobium meliloti two-component system FixL/FixJ regulates nitrogen fixation in response to oxygen during symbiosis. Under microaerobic conditions, the kinase FixL phosphorylates the response regulator FixJ resulting in the regulation of nitrogen fixation genes such as nifA and fixK. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381092 [Multi-domain] Cd Length: 116 Bit Score: 64.54 E-value: 4.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1879 DDEQGVLDVTAEILEWHGYKVLT---ARDGQQALSLyDQHAgdikAVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:cd17537 7 DDDEAVRDSLAFLLRSVGLAVKTftsASAFLAAAPP-DQPG----CLVLDVRMPGMSGLELQDELLARGSNIPIIFITGH 81
|
90 100 110
....*....|....*....|....*....|.
gi 1786808614 1956 GHEKFVTDLRELGVPLFLKKPFAAEELLRSL 1986
Cdd:cd17537 82 GDVPMAVEAMKAGAVDFLEKPFRDQVLLDAI 112
|
|
| REC_OmpR_DrrD-like |
cd17625 |
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a ... |
1876-1992 |
5.96e-12 |
|
phosphoacceptor receiver (REC) domain of DrrD-like OmpR family response regulators; DrrD is a OmpR/PhoB homolog from Thermotoga maritima whose function is not yet known. This subfamily also includes Streptococcus agalactiae transcriptional regulatory protein DltR, part of the DltS/DltR two-component system (TCS), and Pseudomonas aeruginosa transcriptional activator protein PfeR, part of the PfeR/PfeS TCS, which activates expression of the ferric enterobactin receptor. The DltS/DltR TCS regulates the expression of the dlt operon, which comprises four genes (dltA, dltB, dltC, and dltD) that catalyze the incorporation of D-alanine residues into the lipoteichoic acids. Members of this subfamily belong to the OmpR/PhoB family, which comprises of two domains, an N-terminal receiver domain and a C-terminal DNA-binding winged helix-turn-helix effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381140 [Multi-domain] Cd Length: 115 Bit Score: 64.16 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:cd17625 1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDL--IILDIMLPGMDGLEVLKSLREEGIETPVLLLTAL 78
|
90 100 110
....*....|....*....|....*....|....*..
gi 1786808614 1956 GHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:cd17625 79 DAVEDRVKGLDLGADDYLPKPFSLAELLARIRALLRR 115
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
234-928 |
8.39e-12 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 70.94 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 234 KKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATftdiisgleKAVAEHELAVKTLQAEKAELEKRTAS 313
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA---------EEARKAEDARKAEEARKAEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 314 SPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETE--LESLRVA--LQ 389
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAkkAEAVKKAeeAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 390 TEHEKAERADAERELSEEAMVQTN--TGIQQRLMELNAELERTKEELVAESARRtQAEAGQGGGEVNPELAARIAALTEA 467
Cdd:PTZ00121 1237 KDAEEAKKAEEERNNEEIRKFEEArmAHFARRQAAIKAEEARKADELKKAEEKK-KADEAKKAEEKKKADEAKKKAEEAK 1315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 468 KAQVEKELVEQqavAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQRfeqrvA 547
Cdd:PTZ00121 1316 KADEAKKKAEE---AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-----A 1387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 548 ELETDNQQLREQASRDTQAA--TTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQqlQ 625
Cdd:PTZ00121 1388 EEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK--K 1465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 626 AESERRAQ--AESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEvqrgERAEAELFRSRSELET 703
Cdd:PTZ00121 1466 AEEAKKADeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD----EAKKAEEAKKADEAKK 1541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 704 QQAALAELRARAEAAEAARLQVETTAQQSR-------TVAEQAAAEAQQQLAALRQQLQAETERREQAESAlgqSKSETE 776
Cdd:PTZ00121 1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKaeedknmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA---KKAEEA 1618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 777 RQLAEATAALAEVRAQLEQattassqreaeakqaaaaqqqkLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQ 856
Cdd:PTZ00121 1619 KIKAEELKKAEEEKKKVEQ----------------------LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786808614 857 LAET-KAELDQQLAALAEARSQAEREAAE--RRQTEESLLQAS--RSSEERVALLASEL--EAAREALRSESARREELE 928
Cdd:PTZ00121 1677 AEEAkKAEEDEKKAAEALKKEAEEAKKAEelKKKEAEEKKKAEelKKAEEENKIKAEEAkkEAEEDKKKAEEAKKDEEE 1755
|
|
| REC_hyHK_blue-like |
cd18161 |
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators ... |
1876-1977 |
8.95e-12 |
|
phosphoacceptor receiver (REC) domain of hybrid sensor histidine kinase/response regulators similar to Pseudomonas savastanoi blue-light-activated histidine kinase; Typically, two-component regulatory systems (TCSs) consist of a sensor (histidine kinase) that responds to specific input(s) by modifying the output of a cognate response regulator (RR). TCSs allow organisms to sense and respond to changes in environmental conditions. Hybrid sensor histidine kinase (HK)/response regulators contain all the elements of a classical TCS in a single polypeptide chain. Pseudomonas savastanoi blue-light-activated histidine kinase is a photosensitive HK and RR that is involved in increased bacterial virulence upon exposure to light. RRs share the common phosphoacceptor REC domain and different effector/output domains such as DNA, RNA, ligand-binding, protein-binding, or enzymatic domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381145 [Multi-domain] Cd Length: 102 Bit Score: 63.13 E-value: 8.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAgDIKAVITDILMP-FMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd18161 2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGP-DIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80
|
90 100
....*....|....*....|...
gi 1786808614 1955 MGHEKFVTDLRELGVPLfLKKPF 1977
Cdd:cd18161 81 YAENAIEGGDLAPGVDV-LSKPF 102
|
|
| HATPase_BceS-YxdK-YvcQ-like |
cd16948 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1781-1852 |
9.76e-12 |
|
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: 63.46 E-value: 9.76e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 1781 GNYVLFRVTDSGVGIPRDILPRIFEPFFTTK---EPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16948 35 EQGVVLSIKDFGIGIPEEDLPRVFDKGFTGEngrNFQESTGMGLYLVKKLCDKLGHKIDVESEVGEGTTFTITFP 109
|
|
| REC_Spo0F-like |
cd17553 |
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone ... |
1873-1982 |
1.08e-11 |
|
phosphoacceptor receiver (REC) domain of Spo0F and similar domains; Spo0F, a stand-alone response regulator containing only a REC domain with no output/effector domain, controls sporulation in Bacillus subtilis through the exchange of a phosphoryl group. Bacillus subtilis forms spores when conditions for growth become unfavorable. The initiation of sporulation is controlled by a phosphorelay (an expanded version of the two-component system) that consists of four main components: a histidine kinase (KinA), a secondary messenger (Spo0F), a phosphotransferase (Spo0B), and a transcription factor (Spo0A). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381105 [Multi-domain] Cd Length: 117 Bit Score: 63.73 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1873 ELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:cd17553 1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDL--VLLDMKIPGMDGIEILKRMKVIDENIRVIIM 78
|
90 100 110
....*....|....*....|....*....|
gi 1786808614 1953 SGMGHEKFVTDLRELGVPLFLKKPFAAEEL 1982
Cdd:cd17553 79 TAYGELDMIQESKELGALTHFAKPFDIDEI 108
|
|
| REC_CheY4-like |
cd17562 |
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY ... |
1876-1983 |
1.63e-11 |
|
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY4 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY4 and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381110 [Multi-domain] Cd Length: 118 Bit Score: 63.09 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLydQHAGDIKAVITDILMPFMDGVELCRELRK--RDATLPIIVAS 1953
Cdd:cd17562 4 LAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSK--AQSKKFDLIITDQNMPNMDGIELIKELRKlpAYKFTPILMLT 81
|
90 100 110
....*....|....*....|....*....|
gi 1786808614 1954 GMGHEKFVTDLRELGVPLFLKKPFAAEELL 1983
Cdd:cd17562 82 TESSDEKKQEGKAAGATGWLVKPFDPEQLL 111
|
|
| sensory_box |
TIGR00229 |
PAS domain S-box; The PAS domain was previously described. This sensory box, or S-box domain ... |
78-191 |
1.97e-11 |
|
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: 63.08 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 78 FESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKE-FRLDFRLRNK 156
Cdd:TIGR00229 5 YRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEpVSEERRVRRK 84
|
90 100 110
....*....|....*....|....*....|....*
gi 1786808614 157 DGSTRWVAGHAMRVLDDHEQPnGIIGSILDINERK 191
Cdd:TIGR00229 85 DGSEIWVEVSVSPIRTNGGEL-GVVGIVRDITERK 118
|
|
| REC_RpfG-like |
cd17551 |
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator ... |
1876-1983 |
3.13e-11 |
|
phosphoacceptor receiver (REC) domain of cyclic di-GMP phosphodiesterase response regulator RpfG and similar proteins; Cyclic di-GMP phosphodiesterase response regulator RpfG, together with sensory/regulatory protein RpfC, constitute a two-component system implicated in sensing and responding to the diffusible signal factor (DSF) that is essential for cell-cell signaling. RpfC is a hybrid sensor/histidine kinase that phosphorylates and activates RpfG, which degrades cyclic di-GMP to GMP, leading to the activation of Clp, a global transcriptional regulator that regulates a large set of genes in the DSF pathway. RpfG contains a CheY-like receiver domain attached to a histidine-aspartic acid-glycine-tyrosine-proline (HD-GYP) cyclic di-GMP phosphodiesterase domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381103 [Multi-domain] Cd Length: 118 Bit Score: 62.07 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGY-KVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKR--DATLPIIVa 1952
Cdd:cd17551 4 LIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDL--ILLDYMMPGMDGLEFIRRLRALpgLEDVPIVM- 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1786808614 1953 sgmghekfVT-----DLR----ELGVPLFLKKPFAAEELL 1983
Cdd:cd17551 81 --------ITadtdrEVRlralEAGATDFLTKPFDPVELL 112
|
|
| REC_OmpR_CpxR |
cd17623 |
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is ... |
1875-1992 |
4.11e-11 |
|
phosphoacceptor receiver (REC) domain of CpxR-like OmpR family response regulators; CpxR is part of the CpxA/CpxR two-component regulatory system that mediates envelope stress responses that is key for virulence and antibiotic resistance in several Gram negative pathogens. CpxR is a transcription factor/response regulator that controls the expression of numerous genes, including those of the classical porins OmpF and OmpC. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381138 [Multi-domain] Cd Length: 115 Bit Score: 61.94 E-value: 4.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd17623 1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPD--LVVLDVMLPKMNGLDVLKELRKT-SQVPVLMLTA 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1955 MGHE-KFVTDLrELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:cd17623 78 RGDDiDRILGL-ELGADDYLPKPFNPRELVARIRAILRR 115
|
|
| REC_HupR-like |
cd17569 |
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar ... |
1875-1990 |
5.70e-11 |
|
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR) and similar domains; This family is composed of mostly uncharacterized response regulators with similarity to the REC domains of response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It contains an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. Members of this family contain a REC domain and various output domains including the cyclase homology domain (CHD) and the c-di-GMP phosphodiesterase domains, HD-GYP and EAL. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381113 [Multi-domain] Cd Length: 118 Bit Score: 61.65 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD-ATLPIIVaS 1953
Cdd:cd17569 3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDV--VISDQRMPGMDGAELLKRVRERYpDTVRILL-T 79
|
90 100 110
....*....|....*....|....*....|....*...
gi 1786808614 1954 GMGHEKFVTD-LRELGVPLFLKKPFAAEELLRSLHAEL 1990
Cdd:cd17569 80 GYADLDAAIEaINEGEIYRFLTKPWDDEELKETIRQAL 117
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1016-1622 |
6.37e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 67.94 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1016 LEATNAESSRALAAAQNELARESAERETTEAEF-QRSKSALAQQLAEAAAAQAELRSRLEKETAARHETER--ELRESLT 1092
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLIASRQEERQETSAELnQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAleDQHGAFL 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1093 DAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAR-----EQLEKNLRQAAEEATRKAQALQA 1167
Cdd:pfam12128 336 DADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnnrdiAGIKDKLAKIREARDRQLAVAED 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1168 ELQRAKKELEKELADANLELLDIRSRLdheaaARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVEL 1247
Cdd:pfam12128 416 DLQALESELREQLEAGKLEFNEEEYRL-----KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1248 RDTRAALEKQLAEASAALREASARLEQERDERRRVVESLT-QTSTTLEARATESGSALEVTRRLLNEERAARASALAELA 1326
Cdd:pfam12128 491 QSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFpQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVW 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1327 ARRAE-----------VDRLTTEQPHAIEEAtarLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANA----ALRG 1391
Cdd:pfam12128 571 DGSVGgelnlygvkldLKRIDVPEWAASEEE---LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASReetfARTA 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1392 EMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTE-RDSELASVREQAAAL 1470
Cdd:pfam12128 648 LKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREaRTEKQAYWQVVEGAL 727
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1471 DAAGTRAQQTTAELQTNlnaARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQ------DGFQQST 1544
Cdd:pfam12128 728 DAQLALLKAAIAARRSG---AKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRqevlryFDWYQET 804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1545 -------------------AELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSE-RTAGLNAHVQQL 1604
Cdd:pfam12128 805 wlqrrprlatqlsnieraiSELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKlATLKEDANSEQA 884
|
650
....*....|....*...
gi 1786808614 1605 EAELAEAQRAEEQLRHRR 1622
Cdd:pfam12128 885 QGSIGERLAQLEDLKLKR 902
|
|
| HATPase_DpiB-CitA-like |
cd16915 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1781-1852 |
9.41e-11 |
|
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: 60.38 E-value: 9.41e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1781 GNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSvGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16915 34 GDDLVIEVRDTGPGIAPELRDKVFERGVSTKGQGER-GIGLALVRQSVERLGGSITVESEPGGGTTFSIRIP 104
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
49-191 |
9.94e-11 |
|
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: 66.54 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 49 GTVGLFLLLRRDIQKREQTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPD 128
Cdd:COG5809 114 GDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSD 193
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 129 DNKRVTEEWRKCVRGEKEFRLDFRLRNKDGSTRWVAGHAMRvLDDHEQPNGIIGSILDINERK 191
Cdd:COG5809 194 DQENVAAFISQLLKDGGIAQGEVRFWTKDGRWRLLEASGAP-IKKNGEVDGIVIIFRDITERK 255
|
|
| REC_OmpR_MtPhoP-like |
cd17615 |
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; ... |
1875-1992 |
1.06e-10 |
|
phosphoacceptor receiver (REC) domain of MtPhoP-like OmpR family response regulators; Mycobacterium tuberculosis PhoP (MtPhoP) is part of the PhoP/PhoR two-component system that is involved in phosphate control by stimulating expression of genes involved in scavenging, transport and mobilization of phosphate, and repressing the utilization of nitrogen sources. Also included in this subfamily is Mycobacterium tuberculosis transcriptional regulatory protein TcrX, part of the two-component regulatory system TcrY/TcrX that may be involved in virulence. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381131 [Multi-domain] Cd Length: 118 Bit Score: 60.83 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17615 2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPD--AVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTA 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1955 M-GHEKFVTDLrELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:cd17615 80 KdSVEDRIAGL-TAGGDDYVTKPFSLEEVVARLRALLRR 117
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1336-1695 |
1.82e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1336 TTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAE--QRLRDRATDFEAANAALRGEMEKRLRLELtwQMQREDFDRR 1413
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEEL--QEELKEAEEE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1414 LGELTTALRTAEAKagsdSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARA 1493
Cdd:TIGR02168 255 LEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1494 ELDMLNRQFAQRVAELDSTEARLreecahrERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRR 1573
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEEL-------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1574 SLEDALQQSHGEVELRVSERTAGL----NAHVQQLEAELAEAQRAEEQLRHRRIEAVSTLAggmahELNNVLAPVLMAAQ 1649
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLkkleEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD 478
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1786808614 1650 LLRKQVSgKSRTLVDSVESSAQRGADI---VKQVLTFARGFHGERAPVS 1695
Cdd:TIGR02168 479 AAERELA-QLQARLDSLERLQENLEGFsegVKALLKNQSGLSGILGVLS 526
|
|
| PRK10841 |
PRK10841 |
two-component system sensor histidine kinase RcsC; |
1724-1959 |
1.88e-10 |
|
two-component system sensor histidine kinase RcsC;
Pssm-ID: 182772 [Multi-domain] Cd Length: 924 Bit Score: 66.15 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1724 DLP-LISADASQLHRVLLNLAVNArdampsggtLKFSAENVVVdesfIHHRRAtgakpGNYVLFRVTDSGVGIPRDILPR 1802
Cdd:PRK10841 551 DVPvALNGDPMRLQQVISNLLSNA---------IKFTDTGCIV----LHVRVD-----GDYLSFRVRDTGVGIPAKEVVR 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1803 IFEPFFT----TKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP-------------------------- 1852
Cdd:PRK10841 613 LFDPFFQvgtgVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPlygaqypqkkgveglqgkrcwlavrn 692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1853 --------------------------------------------AASAETSER---PPQA--------------ELP--- 1868
Cdd:PRK10841 693 asleqfletllqrsgiqvqryegqeptpedvlitddpvqkkwqgRAVITFCRRhigIPLEiapgewvhstatphELPall 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1869 ----------RGNGELLMLADDEQGVL-DVTAEILEWH--------------GYKVLTARDGQQALSLYDQHAGDIkaVI 1923
Cdd:PRK10841 773 ariyrielesDDSANALPSTDKAVSDNdDMMILVVDDHpinrrlladqlgslGYQCKTANDGVDALNVLSKNHIDI--VL 850
|
330 340 350
....*....|....*....|....*....|....*...
gi 1786808614 1924 TDILMPFMDGVELCRELRKRDATLPII--VASGMGHEK 1959
Cdd:PRK10841 851 TDVNMPNMDGYRLTQRLRQLGLTLPVIgvTANALAEEK 888
|
|
| REC_OmpR_CusR-like |
cd19935 |
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; ... |
1875-1950 |
2.12e-10 |
|
phosphoacceptor receiver (REC) domain of CusR-like OmpR family response regulators; Escherichia coli CusR is part of the CusS/CusR two-component system (TCS) that is involved in response to copper and silver. Other members of this subfamily include Escherichia coli PcoR, Pseudomonas syringae CopR, and Streptomyces coelicolor CutR, which are all transcriptional regulatory proteins and components of TCSs that regulate genes involved in copper resistance and/or metabolism. member of the subfamily is Escherichia coli HprR (hydrogen peroxide response regulator), previously called YdeW, which is part of the HprSR (or YedVW) TCS involved in stress response to hydrogen peroxide, as well as Cupriavidus metallidurans CzcR, which is part of the CzcS/CzcR TCS involved in the control of cobalt, zinc, and cadmium homeostasis. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381162 [Multi-domain] Cd Length: 100 Bit Score: 59.38 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSL-----YDqhagdikAVITDILMPFMDGVELCRELRKRDATLPI 1949
Cdd:cd19935 1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLaltneYD-------LIILDVMLPGLDGLEVLRRLRAAGKQTPV 73
|
.
gi 1786808614 1950 I 1950
Cdd:cd19935 74 L 74
|
|
| FixJ |
COG4566 |
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal ... |
1879-1997 |
2.40e-10 |
|
DNA-binding response regulator, FixJ family, consists of REC and HTH domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 443623 [Multi-domain] Cd Length: 196 Bit Score: 62.04 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMGHe 1958
Cdd:COG4566 6 DDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGC--LLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHGD- 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1959 kfvtdlrelgVPL-----------FLKKPFAAEELLRSLHAELHREESAA 1997
Cdd:COG4566 83 ----------VPMavramkagavdFLEKPFDDQALLDAVRRALARDRARR 122
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
245-655 |
3.03e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 245 RQLWAELSGREQVEAELAKARGELDkQVAERTATFTDIISGLEKavaehelAVKTLQAEKAELEK----RTASSPAELEA 320
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELE-EVEENIERLDLIIDEKRQ-------QLERLRREREKAERyqalLKEKREYEGYE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 321 LRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLeTELESLRVALQTEHEKAERADA 400
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL-GEEEQLRVKEKIGELEAEIASL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 401 ERELSEEamvqtntgiQQRLMELNAELERTKEELvaesaRRTQAEAgqgggevnPELAARIAALTEAKAQVEKELVEQQA 480
Cdd:TIGR02169 307 ERSIAEK---------ERELEDAEERLAKLEAEI-----DKLLAEI--------EELEREIEEERKRRDKLTEEYAELKE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 481 VAKALgdernrlaqelaeaaaaraaleqqlaaasqagagRSEADEaaraqVEADLRAAHQRFEQRVAELETDNQQLRE-Q 559
Cdd:TIGR02169 365 ELEDL----------------------------------RAELEE-----VDKEFAETRDELKDYREKLEKLKREINElK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 560 ASRDTQAATTQRGEQEtaLAELRAQLERTEAARQQIETTALDLR---SNSEQQLSETQRQLADARQQLQAESERRAQAES 636
Cdd:TIGR02169 406 RELDRLQEELQRLSEE--LADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483
|
410
....*....|....*....
gi 1786808614 637 ALGQSKSETERQLAEATAA 655
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARAS 502
|
|
| REC_CheC-like |
cd17593 |
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC ... |
1898-1987 |
3.14e-10 |
|
phosphoacceptor receiver (REC) domain of uncharacterized response regulators containing a CheC domain; This subfamily is composed of uncharacterized proteins containing an N-terminal REC domain and a C-terminal CheC domain that may function as the output/effector domain of a response regulator. CheC is a CheY-P phosphatase, affecting the level of phosphorylated CheY which controls the sense of flagella rotation and determine swimming behavior of chemotactic bacteria. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381124 [Multi-domain] Cd Length: 117 Bit Score: 59.47 E-value: 3.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1898 KVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMGHEKFVTDLRELGVPLFLKKPF 1977
Cdd:cd17593 27 EITFAENGEEALEILREGRIDV--LFLDLTMPVMDGYEVLEALPVEQLETKVIVVSGDVQPEAKERVLELGALAFLKKPF 104
|
90
....*....|
gi 1786808614 1978 AAEELLRSLH 1987
Cdd:cd17593 105 DPEKLAQLLE 114
|
|
| REC_OmpR_BfmR-like |
cd19939 |
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; ... |
1875-1992 |
4.10e-10 |
|
phosphoacceptor receiver (REC) domain of BfmR-like OmpR family response regulators; Acinetobacter baumannii BfmR is part of the BfmR/S two-component system that functions as the master regulator of biofilm initiation. BfmR confers resistance to complement-mediated bactericidal activity, independent of capsular polysaccharide, and also increases resistance to the clinically important antimicrobials meropenem and colistin, making it a potential antimicrobial target. Its inhibition would have the dual benefit of significantly decreasing in vivo survival and increasing sensitivity to selected antimicrobials. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381166 [Multi-domain] Cd Length: 116 Bit Score: 58.92 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAtLPIIVASG 1954
Cdd:cd19939 2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSL--VVLDIMLPGMDGLTVCREVREHSH-VPILMLTA 78
|
90 100 110
....*....|....*....|....*....|....*...
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:cd19939 79 RTEEMDRVLGLEMGADDYLCKPFSPRELLARVRALLRR 116
|
|
| nifL_nitrog |
TIGR02938 |
nitrogen fixation negative regulator NifL; NifL is a modulator of the nitrogen fixation ... |
1565-1852 |
5.91e-10 |
|
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: 64.15 E-value: 5.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1565 AEQETTQRRSLEDALQQSHGEVELRVSERTaGLNAHVQQLEAELAEAQRAEEQLRHRRIEAVSTlaggmahelnnvlaPV 1644
Cdd:TIGR02938 249 SNLREEQERARLSALQALMAEEERLEAIRE-TLSAAIHRLQGPMNLISAAISVLQRRGDDAGNP--------------AS 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1645 LMAAQllrkQVSGKSRTLVDSVESS-AQRGADIVKqvltfargfhgeraPVSPEMLVRD-IAKSVQETFPRNVRVSSEVA 1722
Cdd:TIGR02938 314 AAMLQ----QALSAGREHMEALRQViPQSPQEIVV--------------PVNLNQILRDvITLSTPRLLAAGIVVDWQPA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1723 DDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKfsaenvvvDESFIhhrraTGAKPGNYVLFRVTDSGVGIPRDILPR 1802
Cdd:TIGR02938 376 ATLPAILGRELQLRSLFKALVDNAIEAMNIKGWKR--------RELSI-----TTALNGDLIVVSILDSGPGIPQDLRYK 442
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 1803 IFEPFFTTKEP-GQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:TIGR02938 443 VFEPFFTTKGGsRKHIGMGLSVAQEIVADHGGIIDLDDDYSEGCRIIVEFR 493
|
|
| PRK09303 |
PRK09303 |
histidine kinase; |
1566-1852 |
6.07e-10 |
|
histidine kinase;
Pssm-ID: 236462 [Multi-domain] Cd Length: 380 Bit Score: 63.43 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1566 EQETTQRRSLEDALQQSHgEVELRVSERtaglnahVQQLEAELAEAQRAEEQLRhRRIEAVSTLAGGMAHELNNVLAPVL 1645
Cdd:PRK09303 100 QQEGATYSGLGENLQPSE-IDSGRYSQE-------LLQLSDELFVLRQENETLL-EQLKFKDRVLAMLAHDLRTPLTAAS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1646 MAAQLLR----KQVSGKSRTLVDSVESSAQRGADIV----KQVLTFARGfHGERAPVSPEMLvrDIAKSVQETF------ 1711
Cdd:PRK09303 171 LALETLElgqiDEDTELKPALIEQLQDQARRQLEEIerliTDLLEVGRT-RWEALRFNPQKL--DLGSLCQEVIlelekr 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1712 --PRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSaenvvvdesfIHHRraTGAKpgnyVLFRVT 1789
Cdd:PRK09303 248 wlAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNAIKYTPEGGTITLS----------MLHR--TTQK----VQVSIC 311
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 1790 DSGVGIPRDILPRIFEPFFTTKEPGQS--VGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:PRK09303 312 DTGPGIPEEEQERIFEDRVRLPRDEGTegYGIGLSVCRRIVRVHYGQIWVDSEPGQGSCFHFTLP 376
|
|
| HATPase_FilI-like |
cd16921 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1852 |
7.47e-10 |
|
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: 58.11 E-value: 7.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNArdampsggtLKFSAENVvvdesfiHHRRATGAKP-GNYVLFRVTDSGVGIPRDILPRIFEPF--FTTK 1811
Cdd:cd16921 1 LGQVLTNLLGNA---------IKFRRPRR-------PPRIEVGAEDvGEEWTFYVRDNGIGIDPEYAEKVFGIFqrLHSR 64
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1786808614 1812 EPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16921 65 EEYEGTGVGLAIVRKIIERHGGRIWLESEPGEGTTFYFTLP 105
|
|
| HATPase_SpaK_NisK-like |
cd16975 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1731-1849 |
9.79e-10 |
|
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: 57.86 E-value: 9.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1731 DASQLHRVLLNLAVNARDAMPSGGTLKFSAEnvvvDESfihhrratgakpgNYVLFRVTDSGVGIPRDILPRIFEPFFTT 1810
Cdd:cd16975 1 DTLLLSRALINIISNACQYAPEGGTVSISIY----DEE-------------EYLYFEIWDNGHGFSEQDLKKALELFYRD 63
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1786808614 1811 KEPGQS---VGLGLATALGVVQSHGGFILLETEEDKGTEFQI 1849
Cdd:cd16975 64 DTSRRSgghYGMGLYIAKNLVEKHGGSLIIENSQKGGAEVTV 105
|
|
| fixJ |
PRK09390 |
response regulator FixJ; Provisional |
1879-1999 |
1.01e-09 |
|
response regulator FixJ; Provisional
Pssm-ID: 181815 [Multi-domain] Cd Length: 202 Bit Score: 60.40 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1879 DDEQGVLDVTAEILEWHGYKVltaRDGQQALSLYDQHAG-DIKAVITDILMPFMDGVELCRELRKRDATLPIIVASGMGH 1957
Cdd:PRK09390 10 DDDEAMRDSLAFLLDSAGFEV---RLFESAQAFLDALPGlRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGD 86
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1786808614 1958 EKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHREESAAVG 1999
Cdd:PRK09390 87 VPLAVEAMKLGAVDFIEKPFEDERLIGAIERALAQAPEAAKS 128
|
|
| REC_OmpR_RegX3-like |
cd17621 |
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is ... |
1875-1976 |
1.17e-09 |
|
phosphoacceptor receiver (REC) domain of RegX3-like OmpR family response regulators; RegX3 is a member of the SenX3-RegX3 two-component system that is involved in phosphate-sensing signal transduction. Phosphorylated RegX3 functions as a transcriptional activator of phoA. It induces transcription in phosphate limiting environment and also controls expression of several critical metabolic enzymes in aerobic condition. RegX3 belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381136 [Multi-domain] Cd Length: 99 Bit Score: 57.21 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd17621 1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADI--VLLDLMLPGLSGTEVCRQLRAR-SNVPVIMVTA 77
|
90 100
....*....|....*....|..
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKP 1976
Cdd:cd17621 78 KDSEIDKVVGLELGADDYVTKP 99
|
|
| COG4192 |
COG4192 |
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal ... |
1337-1844 |
1.42e-09 |
|
Signal transduction histidine kinase regulating phosphoglycerate transport system [Signal transduction mechanisms];
Pssm-ID: 443346 [Multi-domain] Cd Length: 640 Bit Score: 63.17 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1337 TEQPHAIEEATARLKAQLAEQEREREQLRLAamsaEQRLRDRATDFEAANAALRGEMEKrLRLELTWQMQR--------E 1408
Cdd:COG4192 108 TQDAGDLRAAVADLRNLLQQLDSLLTQRIAL----RRRLQELLEQINWLHQDFNSELTP-LLQEASWQQTRlldsvettE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1409 DFDRRLGELTTALR--TAEAKAGSDSAElrHAHETLQQAHAELTRRLTERdSELASVREQAAALDAAGTRAQQTTAEL-- 1484
Cdd:COG4192 183 SLRNLQNELQLLLRllAIENQIVSLLRE--VAAARDQADVDNLFDRLQYL-KDELDRNLQALKNYPSTITLRQLIDELla 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1485 ----QTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAhrERAEAELDRMRDAQDGFQQSTAE-------------- 1546
Cdd:COG4192 260 igsgEGGLPSLRRDELAAQATLEALAEENNSILEQLRTQIS--GLVGNSREQLVALNQETAQLVQQsgilllaiallsll 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1547 -------------LNERLTRLTTDVEA-ARQQAEQETTQRRSleDALqqshGEV--ELRVSERTAglNAHVQQLEAELAE 1610
Cdd:COG4192 338 lavlinyfyvrrrLVKRLNALSDAMAAiAAGDLDVPIPVDGN--DEI----GRIarLLRVFRDQA--IEKTQELETEIEE 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1611 AQRAEEQLRH--------RRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKS----RTLVDSVESSAQRGADIVK 1678
Cdd:COG4192 410 RKRIEKNLRQtqdeliqaAKMAVVGQTMTSLAHELNQPLNAMSMYLFSAKKALEQENyaqlPTSLDKIEGLIERMDKIIK 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1679 QVLTFARGFHGERAPVSPEMLVRDiAKSVQETFPRNVRVSSEVADDlPLISADASQLHRVLLNLAVNARDAMPsggtlkf 1758
Cdd:COG4192 490 SLRQFSRKSDTPLQPVDLRQVIEQ-AWELVESRAKPQQITLHIPDD-LMVQGDQVLLEQVLVNLLVNALDAVA------- 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1759 saenvvvDESFIHHRRATGAKpgnYVLFRVTDSGVGIPrdILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLE 1838
Cdd:COG4192 561 -------TQPQISVDLLSNAE---NLRVAISDNGNGWP--LVDKLFTPFTTTKEVG--LGLGLSICRSIMQQFGGDLYLA 626
|
....*.
gi 1786808614 1839 TEEDKG 1844
Cdd:COG4192 627 STLERG 632
|
|
| PAS |
pfam00989 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
78-187 |
1.55e-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: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 78 FESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQG---FGwlLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLR 154
Cdd:pfam00989 3 LRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGkslLD--LIPEEDDAEVAELLRQALLQGEESRGFEVSFR 80
|
90 100 110
....*....|....*....|....*....|...
gi 1786808614 155 NKDGSTRWVAGHAMRVLDDHEQPNGIIGSILDI 187
Cdd:pfam00989 81 VPDGRPRHVEVRASPVRDAGGEILGFLGVLRDI 113
|
|
| REC_OmpR_VirG |
cd17594 |
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is ... |
1874-1983 |
1.96e-09 |
|
phosphoacceptor receiver (REC) domain of VirG-like OmpR family response regulators; VirG is part of the VirA/VirG two-component system that regulates the expression of virulence (vir) genes. The histidine kinase VirA senses a phenolic wound response signal, undergoes autophosphorylation, and phosphorelays to the VirG response regulator, which induces transcription of the vir regulon. VirG belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381125 [Multi-domain] Cd Length: 113 Bit Score: 57.07 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1874 LLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRkRDATLPIIVAS 1953
Cdd:cd17594 1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDL--VLLDLRLGQESGLDLLRTIR-ARSDVPIIIIS 77
|
90 100 110
....*....|....*....|....*....|.
gi 1786808614 1954 G-MGHEKFVTDLRELGVPLFLKKPFAAEELL 1983
Cdd:cd17594 78 GdRRDEIDRVVGLELGADDYLAKPFGLRELL 108
|
|
| KinA |
COG5805 |
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle ... |
55-194 |
2.06e-09 |
|
Sporulation sensor histidine kinase A (Stage II sporulation protein SpoIIF/SpoIIJ) [Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];
Pssm-ID: 444507 [Multi-domain] Cd Length: 496 Bit Score: 62.44 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 55 LLLRRDIQKREQTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVT 134
Cdd:COG5805 136 ILALRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFK 215
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 135 EEWRKCVRGEKEFRLDFRLRNKDGSTRWVAGHAMRVLDDHEQPNGIIGSILDINERKVAD 194
Cdd:COG5805 216 ERIESITEVWQEFIIEREIITKDGRIRYFEAVIVPLIDTDGSVKGILVILRDITEKKEAE 275
|
|
| HATPase_NtrY-like |
cd16944 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1731-1852 |
2.29e-09 |
|
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: 56.78 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1731 DASQLHRVLLNLAVNARDAmpsggtlkfsAENVVVDESFIHHRRATGAKpgNYVLFRVTDSGVGIPRDILPRIFEPFFTT 1810
Cdd:cd16944 1 DTTQISQVLTNILKNAAEA----------IEGRPSDVGEVRIRVEADQD--GRIVLIVCDNGKGFPREMRHRATEPYVTT 68
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1786808614 1811 KEPGqsVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16944 69 RPKG--TGLGLAIVKKIMEEHGGRISLSNREAGGACIRIILP 108
|
|
| REC_RR468-like |
cd17552 |
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and ... |
1875-1977 |
2.35e-09 |
|
phosphoacceptor receiver (REC) domain of Thermotoga maritima response regulator RR468 and similar domains; Thermotoga maritima RR468 (encoded by gene TM0468) is the cognate response regulator (RR) of the class I histidine kinase HK853 (product of gene TM0853). HK853/RR468 comprise a two-component system (TCS) that couples environmental stimuli to adaptive responses. This subfamily also includes Fremyella diplosiphon complementary adaptation response regulator homolog RcaF, a small RR that is involved in four-step phosphorelays of the complementary chromatic adaptation (CCA) system that occurs in many cyanobacteria. Both RR468 and RcaF are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381104 [Multi-domain] Cd Length: 121 Bit Score: 57.18 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILE-WHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDAT--LPIIV 1951
Cdd:cd17552 4 ILVIDDEEDIREVVQACLEkLAGWEVLTASSGQEGLEKAATEQPD--AILLDVMMPDMDGLATLKKLQANPETqsIPVIL 81
|
90 100
....*....|....*....|....*...
gi 1786808614 1952 --ASGMGHEKfvTDLRELGVPLFLKKPF 1977
Cdd:cd17552 82 ltAKAQPSDR--QRFASLGVAGVIAKPF 107
|
|
| REC_DivK-like |
cd17548 |
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus ... |
1890-1950 |
2.49e-09 |
|
phosphoacceptor receiver (REC) domain of DivK and similar proteins; Caulobacter crescentus DivK is an essential response regulator that is involved in the complex phosphorelay pathways controlling both cell division and motility. It localizes cell cycle regulators to specific poles of the cell during division. DivK contains a stand-alone REC domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381100 [Multi-domain] Cd Length: 115 Bit Score: 56.78 E-value: 2.49e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 1890 EILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPII 1950
Cdd:cd17548 17 DLLESAGYEVLEAADGEEALEIARKEKPDL--ILMDIQLPGMDGLEATRLLKEDPATrdIPVI 77
|
|
| KinE |
COG5809 |
Sporulation sensor histidine kinase E [Cell cycle control, cell division, chromosome ... |
63-191 |
3.26e-09 |
|
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: 61.53 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 63 KREQTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVR 142
Cdd:COG5809 2 KSSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1786808614 143 GEKEFRLDFRLRNKDGSTRWVAGHAMRVLDDHEQPNGIIGSILDINERK 191
Cdd:COG5809 82 GESRDELEFELRHKNGKRLEFSSKLSPIFDQNGDIEGMLAISRDITERK 130
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
824-1273 |
3.42e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 824 ELKKTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESllqaSRSSEERV 903
Cdd:PRK02224 290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER----AEELREEA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 904 ALLASELEAAREALRSESARREELETALpktktelgqrlaeaaaeaAGLRARMDFEAAERERVEAAWKLANSATEQHAAE 983
Cdd:PRK02224 366 AELESELEEAREAVEDRREEIEELEEEI------------------EELRERFGDAPVDLGNAEDFLEELREERDELRER 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 984 LKTLLATAREelhAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAA 1063
Cdd:PRK02224 428 EAELEATLRT---ARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1064 AAQAELRSRLEKETAARHETERELRESLTDAERTTEALQ---ADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAE 1140
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELReraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL 584
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1141 TGAREQLEK---------NLRQAAEEATRKAQALQ----------AELQRAKKELEKELADANLElldirsrldhEAAAR 1201
Cdd:PRK02224 585 KERIESLERirtllaaiaDAEDEIERLREKREALAelnderrerlAEKRERKRELEAEFDEARIE----------EARED 654
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1202 RQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQREttevELRDTRAALEKQLaEASAALREASARLE 1273
Cdd:PRK02224 655 KERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELE----ELRERREALENRV-EALEALYDEAEELE 721
|
|
| HATPase_BvrS-ChvG-like |
cd16953 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1852 |
3.64e-09 |
|
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: 56.04 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNARDAMPSggtlkfsaenvvvDESFIHHRRATGakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEP- 1813
Cdd:cd16953 1 LGQVLRNLIGNAISFSPP-------------DTGRITVSAMPT---GKMVTISVEDEGPGIPQEKLESIFDRFYTERPAn 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1786808614 1814 ---GQSVGLGLATALGVVQSHGGFILLETEED----KGTEFQIYLP 1852
Cdd:cd16953 65 eafGQHSGLGLSISRQIIEAHGGISVAENHNQpgqvIGARFTVQLP 110
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
36-191 |
3.94e-09 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 62.00 E-value: 3.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 36 VVAVVKDTlflaAGTVGLFLLLRRDIQKREQTHAKNhevRQTFESLTQAAPAG---IFRANQQGDILFVNHRWSALTG-R 111
Cdd:PRK09776 374 AVSLVRDT----DGTPLYFIAQIEDINELKRTEQVN---ERLMERITLANEAGgigIWEWDLKPNIISWDKRMFELYEiP 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 112 SQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLRNKDGsTRWVAGHAMRVLDDHEQPNGIIGSILDINERK 191
Cdd:PRK09776 447 PHIKPTWQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVR 525
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
767-1574 |
4.09e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.01 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 767 ALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQL 846
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 847 AAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREE 926
Cdd:TIGR02169 314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 927 LEtalpKTKTELGQRLAEAAAEAAGLRARmdfeAAERERVEAAWKlansATEQHAAELKTLLATAREELHAETAKRDAAE 1006
Cdd:TIGR02169 394 LE----KLKREINELKRELDRLQEELQRL----SEELADLNAAIA----GIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1007 AAASQVRAELEATNAESSRAlaaaqnELARESAERETTEAEFQRSKSALAQQLAEAAAAQaelrsrLEKETAARHETERE 1086
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRV------EKELSKLQRELAEAEAQARASEERVRGGRAVEEV------LKASIQGVHGTVAQ 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1087 LRESltdAERTTEALQA-----------DLDAALKACEEEAARRSQAEET------ARQSHTEFthRLTAETGAREQLEK 1149
Cdd:TIGR02169 530 LGSV---GERYATAIEVaagnrlnnvvvEDDAVAKEAIELLKRRKAGRATflplnkMRDERRDL--SILSEDGVIGFAVD 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1150 NLRQAAEEATRKAQALQAELQRAKKELEKELADA------NLELLDIRSRLDHEAAARRQAEESAKQGSASAdQRLAERL 1223
Cdd:TIGR02169 605 LVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKyrmvtlEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL-QRLRERL 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1224 SEVQTLQERLRSEAAQRETTEVELRDtraalekQLAEASAALREASARLEQERDERRRVVESLTQtsttLEARATESGSA 1303
Cdd:TIGR02169 684 EGLKRELSSLQSELRRIENRLDELSQ-------ELSDASRKIGEIEKEIEQLEQEEEKLKERLEE----LEEDLSSLEQE 752
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1304 LEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEataRLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFE 1383
Cdd:TIGR02169 753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP---EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1384 aanaALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAgsdsAELRHAHETLQQAHAELTRRLTERDSELASV 1463
Cdd:TIGR02169 830 ----YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL----EELEAALRDLESRLGDLKKERDELEAQLREL 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1464 REQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVaELDSTEARLREECAHRERAEAELDRMRD----AQDG 1539
Cdd:TIGR02169 902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIRALEPvnmlAIQE 980
|
810 820 830
....*....|....*....|....*....|....*...
gi 1786808614 1540 FQQSTA---ELNERLTRLTTDVEAARQQAEQETTQRRS 1574
Cdd:TIGR02169 981 YEEVLKrldELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| REC_CheY_CheY3 |
cd19923 |
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY ... |
1875-1982 |
4.35e-09 |
|
phosphoacceptor receiver (REC) domain of chemotaxis response regulator CheY3 and similar CheY family proteins; CheY family chemotaxis response regulators (RRs) comprise about 17% of bacterial RRs and almost half of all RRs in archaea. This subfamily contains Vibrio cholerae CheY3, Escherichia coli CheY, and similar CheY family RRs. CheY proteins control bacterial motility and participate in signaling phosphorelays and in protein-protein interactions. CheY RRs contain only the REC domain with no output/effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381150 [Multi-domain] Cd Length: 119 Bit Score: 56.19 E-value: 4.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYK-VLTARDGQQALSLYDqhAGDIKAVITDILMPFMDGVELCRELR--KRDATLPIIV 1951
Cdd:cd19923 3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLK--AGGFDFVITDWNMPNMDGLELLKTIRadGALSHLPVLM 80
|
90 100 110
....*....|....*....|....*....|.
gi 1786808614 1952 ASGMGHEKFVTDLRELGVPLFLKKPFAAEEL 1982
Cdd:cd19923 81 VTAEAKKENVIAAAQAGVNNYIVKPFTAATL 111
|
|
| envZ |
PRK09467 |
osmolarity sensor protein; Provisional |
1675-1852 |
4.84e-09 |
|
osmolarity sensor protein; Provisional
Pssm-ID: 236531 [Multi-domain] Cd Length: 435 Bit Score: 61.08 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1675 DIVKQVLTFARgfHGERAPVSPEMLVRDIAKSVQETFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNArdampsgg 1754
Cdd:PRK09467 274 AIIEQFIDYLR--TGQEMPMEMADLNALLGEVIAAESGYEREIETALQPGPIEVPMNPIAIKRALANLVVNA-------- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1755 tLKFSAENVVVDESFihhrratgakPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSV--GLGLATALGVVQSHG 1832
Cdd:PRK09467 344 -ARYGNGWIKVSSGT----------EGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSARGSSgtGLGLAIVKRIVDQHN 412
|
170 180
....*....|....*....|
gi 1786808614 1833 GFILLETEEDKGTEFQIYLP 1852
Cdd:PRK09467 413 GKVELGNSEEGGLSARAWLP 432
|
|
| REC_OmpR_PmrA-like |
cd17624 |
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This ... |
1875-1988 |
5.21e-09 |
|
phosphoacceptor receiver (REC) domain of PmrA-like OmpR family response regulators; This subfamily contains various OmpR family response regulators including PmrA, BasR, QseB, tctD, and RssB, which are components of two-component regulatory systems (TCSs). The PmrA/PmrB TCS controls transcription of genes that are involved in lipopolysaccharide modification in the outer membrane of bacteria, increasing bacterial resistance to host-derived antimicrobial peptides. The BasS/BasR TCS functions as an iron- and zinc-sensing transcription regulator. The QseB/QseC TCS activates the flagella regulon by activating transcription of FlhDC. The RssA/RssB TCS regulates swarming behavior in Serratia marcescens. OmpR family DNA-binding response regulators contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381139 [Multi-domain] Cd Length: 115 Bit Score: 55.95 E-value: 5.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIV--A 1952
Cdd:cd17624 1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYD--LVILDLGLPDGDGLDLLRRWRRQGQSLPVLIltA 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1786808614 1953 SGMGHEKfVTDLrELGVPLFLKKPFAAEELLRSLHA 1988
Cdd:cd17624 79 RDGVDDR-VAGL-DAGADDYLVKPFALEELLARLRA 112
|
|
| PRK10490 |
PRK10490 |
sensor protein KdpD; Provisional |
1606-1866 |
5.74e-09 |
|
sensor protein KdpD; Provisional
Pssm-ID: 236701 [Multi-domain] Cd Length: 895 Bit Score: 61.59 E-value: 5.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1606 AELAEAQRAEEQLRHRRIEAVStlaggmaHELNNVLAPVLMAAQLLrkqvsgksrTLVDSVESS--AQRGADIVKQVLTF 1683
Cdd:PRK10490 651 EEQARLASEREQLRNALLAALS-------HDLRTPLTVLFGQAEIL---------TLDLASEGSphARQASEIRQQVLNT 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1684 AR--------------GFHGERAPVSPEMLVRDIAKSVQETFPRNvRVSSEVADDLPLISADASQLHRVLLNLAVNARDA 1749
Cdd:PRK10490 715 TRlvnnlldmariqsgGFNLRKEWLTLEEVVGSALQMLEPGLSGH-PINLSLPEPLTLIHVDGPLFERVLINLLENAVKY 793
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1750 MPSGGTLKFSAEnvvVDESFIHhrratgakpgnyvlFRVTDSGVGIPRDILPRIFEPFFT-TKE---PGqsVGLGLATAL 1825
Cdd:PRK10490 794 AGAQAEIGIDAH---VEGERLQ--------------LDVWDNGPGIPPGQEQLIFDKFARgNKEsaiPG--VGLGLAICR 854
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1786808614 1826 GVVQSHGGFILLETEEDKGTEFQIYLPAasaetsERPPQAE 1866
Cdd:PRK10490 855 AIVEVHGGTIWAENRPEGGACFRVTLPL------ETPPELE 889
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
186-705 |
6.50e-09 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 61.70 E-value: 6.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 186 DINERKVADDTRTTDQAAALDAAlaRVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAELSGREQVE--AELAK 263
Cdd:PTZ00121 1238 DAEEAKKAEEERNNEEIRKFEEA--RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKkkAEEAK 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 264 ARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEKAELEKrtasSPAELEALRKRLSDEATRRQLAEDDLRSLR 343
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA----AEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 344 EDfDKLQSSATQPDTALETVHhRLHAETERVKRLETELESLRVA--LQTEHEKAERADAERELSEEAMVQTNtgiqqrlM 421
Cdd:PTZ00121 1392 KA-DEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKAEE-------A 1462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 422 ELNAELERTKEELVAESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKelveqqaVAKAlgdERNRLAQELAEAAA 501
Cdd:PTZ00121 1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-------AKKA---EEAKKADEAKKAEE 1532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 502 ARAALEQQLAAASQagagrsEADEAARAQveaDLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAEL 581
Cdd:PTZ00121 1533 AKKADEAKKAEEKK------KADELKKAE---ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 582 RAQLERTEAARQQIE-TTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALgqsKSETERQLAEATAALADTR 660
Cdd:PTZ00121 1604 EKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEA 1680
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1786808614 661 KQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQ 705
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
|
|
| REC_OmpR_KdpE-like |
cd17620 |
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a ... |
1876-1976 |
6.63e-09 |
|
phosphoacceptor receiver (REC) domain of KdpE-like OmpR family response regulators; KdpE is a component of the KdpD/KdpE two-component system (TCS) and is activated when histidine kinase KdpD senses a drop in external K+ concentration or upshift in ionic osmolarity, resulting in the expression of a heterooligomeric transporter KdpFABC. In addition, the KdpD/KdpE TCS is also an adaptive regulator involved in the virulence and intracellular survival of pathogenic bacteria. KdpE is a member of the OmpR family of DNA-binding response regulators that contain REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381135 [Multi-domain] Cd Length: 99 Bit Score: 54.86 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATlPIIVASGM 1955
Cdd:cd17620 2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDL--IILDLGLPDMDGLEVIRRLREWSAV-PVIVLSAR 78
|
90 100
....*....|....*....|.
gi 1786808614 1956 GHEKFVTDLRELGVPLFLKKP 1976
Cdd:cd17620 79 DEESDKIAALDAGADDYLTKP 99
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1149-1630 |
8.83e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.08 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1149 KNLRQAAEEATRKAQALQaELQRAKKELEKELADANlELLDIRSRLDHEAAARRQAEesakqgsasADQRLAERLSEVQT 1228
Cdd:COG4913 238 ERAHEALEDAREQIELLE-PIRELAERYAAARERLA-ELEYLRAALRLWFAQRRLEL---------LEAELEELRAELAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1229 LQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTR 1308
Cdd:COG4913 307 LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1309 RLLNEERAARASALaelaarraevdrltteqpHAIEEATARLKAQLAEQEREREQLRlaamsAE-QRLRDRATDFEAANA 1387
Cdd:COG4913 387 AEAAALLEALEEEL------------------EALEEALAEAEAALRDLRRELRELE-----AEiASLERRKSNIPARLL 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1388 ALRGEMEKRLRL-----------------ELTWQMQREDF-----------DRRLGELTTALRTAEAKAGSDSAELRHAH 1439
Cdd:COG4913 444 ALRDALAEALGLdeaelpfvgelievrpeEERWRGAIERVlggfaltllvpPEHYAAALRWVNRLHLRGRLVYERVRTGL 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1440 ETLQQAHAE---LTRRLTERDS--------ELASVREQAAALDAAGTRAQQT--TAELQTNLNAARAELDMLNRQFAQRV 1506
Cdd:COG4913 524 PDPERPRLDpdsLAGKLDFKPHpfrawleaELGRRFDYVCVDSPEELRRHPRaiTRAGQVKGNGTRHEKDDRRRIRSRYV 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1507 -------------AELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLtrlttDVEAARQQAEQETTQRR 1573
Cdd:COG4913 604 lgfdnraklaaleAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELE 678
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786808614 1574 SLEDAlqqshgevelrvSERTAGLNAHVQQLEAELAEAQRAEEQLRHRRIEAVSTLA 1630
Cdd:COG4913 679 RLDAS------------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELE 723
|
|
| REC_OmpR_PhoB |
cd17618 |
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The ... |
1879-1983 |
1.02e-08 |
|
phosphoacceptor receiver (REC) domain of PhoB response regulator from the OmpR family; The transcription factor PhoB is a component of the PhoR/PhoB two-component system, a key regulatory protein network that facilitates response to inorganic phosphate (Pi) starvation conditions by turning on the phosphate (pho) regulon whose products are involved in phosphorus uptake and metabolism. PhoB is a member of the OmpR family of DNA-binding response regulators that contains REC and winged helix-turn-helix (wHTH) DNA-binding output effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381133 [Multi-domain] Cd Length: 118 Bit Score: 54.95 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIVASGMG 1956
Cdd:cd17618 7 EDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDL--ILLDWMLPGGSGIQFIRRLKRDEMTrdIPIIMLTARG 84
|
90 100
....*....|....*....|....*..
gi 1786808614 1957 HEKFVTDLRELGVPLFLKKPFAAEELL 1983
Cdd:cd17618 85 EEEDKVRGLEAGADDYITKPFSPRELV 111
|
|
| REC_OmpR_EcPhoP-like |
cd19934 |
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; ... |
1875-1992 |
1.09e-08 |
|
phosphoacceptor receiver (REC) domain of EcPhoP-like OmpR family response regulators; Escherichia coli PhoP (EcPhoP) is part of the PhoQ/PhoP two-component system (TCS) that regulates virulence genes and plays an essential role in the response of the bacteria to the environment of their mammalian hosts, sensing several stimuli such as extracellular magnesium limitation, low pH, the presence of cationic antimicrobial peptides, and osmotic upshift. This subfamily also includes Brucella suis FeuP, part of the FeuPQ TCS that is involved in the regulation of iron uptake, and Microchaete diplosiphon RcaC, which is required for chromatic adaptation. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381161 [Multi-domain] Cd Length: 117 Bit Score: 54.98 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIV--A 1952
Cdd:cd19934 1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYD--LVVLDLGLPGMDGLSVLRRWRSEGRATPVLIltA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1786808614 1953 SGMGHEKfVTDLRElGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:cd19934 79 RDSWQDK-VEGLDA-GADDYLTKPFHIEELLARLRALIRR 116
|
|
| REC_OmpR_kpRstA-like |
cd17622 |
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; ... |
1875-1990 |
1.20e-08 |
|
phosphoacceptor receiver (REC) domain of kpRstA-like OmpR family response regulators; Klebsiella pneumoniae RstA (kpRstA) is part of the RstA/RstB two-component regulatory system that may play a regulatory role in virulence. It belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381137 [Multi-domain] Cd Length: 116 Bit Score: 54.69 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRkRDATLPIIVASG 1954
Cdd:cd17622 3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDA--VLLDIMLPGIDGLTLCRDLR-PKYQGPILLLTA 79
|
90 100 110
....*....|....*....|....*....|....*..
gi 1786808614 1955 MGHE-KFVTDLrELGVPLFLKKPFAAEELLRSLHAEL 1990
Cdd:cd17622 80 LDSDiDHILGL-ELGADDYVVKPVEPAVLLARLRALL 115
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
287-595 |
1.32e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.46 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 287 EKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHR 366
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 367 LHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTgiqqRLMELNAELERTKEELVAESARRTQAEA 446
Cdd:TIGR02168 756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE----ALDELRAELTLLNEEAANLRERLESLER 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 447 GQGGGEVNPE--------LAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAgA 518
Cdd:TIGR02168 832 RIAATERRLEdleeqieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK-R 910
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786808614 519 GRSEADEAARAQVEADLRAAHQRFEQRVAELetdNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQI 595
Cdd:TIGR02168 911 SELRRELEELREKLAQLELRLEGLEVRIDNL---QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| PRK11361 |
PRK11361 |
acetoacetate metabolism transcriptional regulator AtoC; |
1875-1996 |
1.80e-08 |
|
acetoacetate metabolism transcriptional regulator AtoC;
Pssm-ID: 183099 [Multi-domain] Cd Length: 457 Bit Score: 59.09 E-value: 1.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK11361 7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDV--VLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 1955 MGH-EKFVTDLRElGVPLFLKKPFAAEEL---------LRSLHAE---LHREESA 1996
Cdd:PRK11361 85 YAEvETAVEALRC-GAFDYVIKPFDLDELnlivqralqLQSMKKEirhLHQALST 138
|
|
| LytT |
COG3279 |
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction ... |
1876-1986 |
1.82e-08 |
|
DNA-binding response regulator, LytR/AlgR family [Transcription, Signal transduction mechanisms];
Pssm-ID: 442510 [Multi-domain] Cd Length: 235 Bit Score: 57.13 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWH-GYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVAS 1953
Cdd:COG3279 5 LIVDDEPLARERLERLLEKYpDLEVVgEASNGEEALELLEEHKPDL--VFLDIQMPGLDGFELARQLRELDPPPPIIFTT 82
|
90 100 110
....*....|....*....|....*....|...
gi 1786808614 1954 gmGHEKFVTDLRELGVPLFLKKPFAAEELLRSL 1986
Cdd:COG3279 83 --AYDEYALEAFEVNAVDYLLKPIDEERLAKAL 113
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
881-1268 |
2.06e-08 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 59.26 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 881 EAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEA 960
Cdd:NF033838 38 EEVRGGNNPTVTSSGNESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 961 AERERVEAA---WKLANSATEQHAAELKTLLATAREElhAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARE 1037
Cdd:NF033838 118 KTKKELDAAfeqFKKDTLEPGKKVAEATKKVEEAEKK--AKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1038 SAERETTEAEFQRSKSALAQQLAEAaaaqaelrSRLEKETAARHETERELRESLTDAERttEALQADLDAALKACEEEAA 1117
Cdd:NF033838 196 EAKEPRDEEKIKQAKAKVESKKAEA--------TRLEKIKTDREKAEEEAKRRADAKLK--EAVEKNVATSEQDKPKRRA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1118 RRSQAEETARQSHTEFTHRLTAETGAREQL-------EKNLRQA---AEEATRKAQALQAELQR-----AKKELEKELAD 1182
Cdd:NF033838 266 KRGVLGEPATPDKKENDAKSSDSSVGEETLpspslkpEKKVAEAekkVEEAKKKAKDQKEEDRRnyptnTYKTLELEIAE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1183 ANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAE--RLSEVQTlQERLRSEAAQRETTEVELRDTRAALEKQLAE 1260
Cdd:NF033838 346 SDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEatRLEKIKT-DRKKAEEEAKRKAAEEDKVKEKPAEQPQPAP 424
|
....*...
gi 1786808614 1261 ASAALREA 1268
Cdd:NF033838 425 APQPEKPA 432
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
253-703 |
2.13e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.67 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 253 GREQVEAELAKARGELDKQVAERTATftdiisGLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRR 332
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKAQIEEKEEK------DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 333 QlaedDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAmvqt 412
Cdd:PRK02224 251 E----ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR---- 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 413 NTGIQQRLMELNAELERTKEElvAESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGDERNRL 492
Cdd:PRK02224 323 DEELRDRLEECRVAAQAHNEE--AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 493 AQELAEAAAARAALEQQLaaasqagagrsEADEAARAQvEADLRAAHQRFEQRVAEletdNQQLREQASRDTQAATTQRG 572
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELR-----------EERDELRER-EAELEATLRTARERVEE----AEALLEAGKCPECGQPVEGS 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 573 EQETALAELRAQLERTEAARQQIETT--ALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESalgqskseterQLA 650
Cdd:PRK02224 465 PHVETIEEDRERVEELEAELEDLEEEveEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRE-----------TIE 533
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 651 EATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELET 703
Cdd:PRK02224 534 EKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
|
| REC_GlnL-like |
cd17565 |
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar ... |
1876-1976 |
2.35e-08 |
|
phosphoacceptor receiver (REC) domain of transcriptional regulatory protein GlnL and similar proteins; Bacillus subtilis GlnL is part of the GlnK-GlnL (formerly YcbA-YcbB) two-component system that positively regulates the expression of the glsA-glnT (formerly ybgJ-ybgH) operon in response to glutamine. It contains a REC domain and a DNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381112 [Multi-domain] Cd Length: 103 Bit Score: 53.43 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWH--GYKVLTARDGQQAlslydqhAGDIKA-----VITDILMPFMDGVELCRELRKRDATLP 1948
Cdd:cd17565 2 YIVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQA-------YDEILFlqpdiVLIDLLMPGMDGIQLVRKLKDTGSNGK 74
|
90 100
....*....|....*....|....*...
gi 1786808614 1949 IIVASGMGHEKFVTDLRELGVPLFLKKP 1976
Cdd:cd17565 75 FIMISQVSDKEMIGKAYQAGIEFFINKP 102
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1223-1626 |
2.55e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1223 LSEVQTLQERLRSEAAQREttEVELRDTRAALEKQLAE--------------ASAALREASARLEqERDERRRVVESLTQ 1288
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAEldeeieryeeqreqARETRDEADEVLE-EHEERREELETLEA 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1289 TSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDrLTTEQPHAIEEATARLKAQLAEQEREREQLRLAA 1368
Cdd:PRK02224 259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEECRVAA 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1369 MSAE---QRLRDRATDFEAANAALRgemEKRLRLELTWQMQREDFDRRLGELT------TALRTAEAKAGSDSAELRHAH 1439
Cdd:PRK02224 338 QAHNeeaESLREDADDLEERAEELR---EEAAELESELEEAREAVEDRREEIEeleeeiEELRERFGDAPVDLGNAEDFL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1440 ETLQQAHAELTRRLTERDSELASVREqaaaldaagtraqqTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARlree 1519
Cdd:PRK02224 415 EELREERDELREREAELEATLRTARE--------------RVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRER---- 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1520 cahRERAEAELDRMRDAQDgfqqstaELNERLTRLTTDVEAARQqAEQETTQRRSLEDALQQSHGEVELRvSERTAGLNA 1599
Cdd:PRK02224 477 ---VEELEAELEDLEEEVE-------EVEERLERAEDLVEAEDR-IERLEERREDLEELIAERRETIEEK-RERAEELRE 544
|
410 420
....*....|....*....|....*..
gi 1786808614 1600 HVQQLEAElAEAQRAEEQLRHRRIEAV 1626
Cdd:PRK02224 545 RAAELEAE-AEEKREAAAEAEEEAEEA 570
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
225-674 |
2.84e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 59.28 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELdkqVAErtatftdiiSGLEKAVAEhelavkTLQAEK 304
Cdd:PRK02224 255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL---LAE---------AGLDDADAE------AVEARR 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 305 AELEKRtasspaeLEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:PRK02224 317 EELEDR-------DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 385 RVALQTEHEKAERADAERELSE---EAMVQTNTGIQQRLMELNAELeRTKEELVAEsARRTQAEAGQGGGEVNPELAARI 461
Cdd:PRK02224 390 EEEIEELRERFGDAPVDLGNAEdflEELREERDELREREAELEATL-RTARERVEE-AEALLEAGKCPECGQPVEGSPHV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 462 AALTEAKAQVEkELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAgagrSEADEAARAQVEADlRAAHQR 541
Cdd:PRK02224 468 ETIEEDRERVE-ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL----EELIAERRETIEEK-RERAEE 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 542 FEQRVAELETDNQQLREQASRDTQAATTQRGEqetaLAELRAQLERTEAARQQIET--TALDLRSNSEQQLSETQRQLAD 619
Cdd:PRK02224 542 LRERAAELEAEAEEKREAAAEAEEEAEEAREE----VAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKREA 617
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 620 -------ARQQLQAESERRAQAESALGQSKSETERQ-LAEATAALADTRKQLEEATTKAAELQ 674
Cdd:PRK02224 618 laelndeRRERLAEKRERKRELEAEFDEARIEEAREdKERAEEYLEQVEEKLDELREERDDLQ 680
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
219-917 |
3.23e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 58.93 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 219 RKEIGLELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVK 298
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 299 TLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLE 378
Cdd:TIGR02169 319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 379 TELESLRVALQTEHEKAERADAERELSEEAMvqtnTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEvnpela 458
Cdd:TIGR02169 399 REINELKRELDRLQEELQRLSEELADLNAAI----AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE------ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 459 ARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEAdlrAA 538
Cdd:TIGR02169 469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEV---AA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 539 HQRFEQRVAELETDNQQL-----REQASRDTQAATTQRGEQETALAELRAQ----------------------------- 584
Cdd:TIGR02169 546 GNRLNNVVVEDDAVAKEAiellkRRKAGRATFLPLNKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlv 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 585 LERTEAARQQIE-----TTALDL---------RSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLA 650
Cdd:TIGR02169 626 VEDIEAARRLMGkyrmvTLEGELfeksgamtgGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 651 EATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGER----AEAELFRSRSELETQQAALAELRARAEAAEAARLQVE 726
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 727 TTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAE 806
Cdd:TIGR02169 786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 807 AKQAAAAQQQKLADQDAELKKTwdnlikeTEDREALEKQLAAARgDLERQLAETKAELDQQLAALAEARSQAEREAA--E 884
Cdd:TIGR02169 866 LEEELEELEAALRDLESRLGDL-------KKERDELEAQLRELE-RKIEELEAQIEKKRKRLSELKAKLEALEEELSeiE 937
|
730 740 750
....*....|....*....|....*....|...
gi 1786808614 885 RRQTEESLLQASRSSEERVALLASELEAAREAL 917
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
|
|
| REC_CheB-like |
cd17541 |
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate ... |
1899-1958 |
3.49e-08 |
|
phosphoacceptor receiver (REC) domain of chemotaxis response regulator protein-glutamate methylesterase CheB and similar chemotaxis proteins; Methylesterase CheB is a chemotaxis response regulator with an N-terminal REC domain and a C-terminal methylesterase domain. Chemotaxis is a behavior known in motile bacteria that directs their movement in response to chemical gradients. CheB is a phosphorylation-activated response regulator involved in the reversible modification of bacterial chemotaxis receptors. It catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins) by CheR. The CheB REC domain packs against the active site of the C-terminal domain and inhibits methylesterase activity by directly restricting access to the active site. Also included in this family is chemotaxis response regulator CheY, which contains a stand-alone REC domain, and an uncharacterized subfamily composed of proteins containing an N-terminal REC domain and a C-terminal CheY-P phosphatase (CheC) domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381096 [Multi-domain] Cd Length: 125 Bit Score: 53.93 E-value: 3.49e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 1899 VLTARDGQQALSLYDQHAGDikaVIT-DILMPFMDGVELCRELRKRDATlPIIVASGMGHE 1958
Cdd:cd17541 29 VGTARDGEEALEKIKELKPD---VITlDIEMPVMDGLEALRRIMAERPT-PVVMVSSLTEE 85
|
|
| PRK15115 |
PRK15115 |
response regulator GlrR; Provisional |
1875-1999 |
3.50e-08 |
|
response regulator GlrR; Provisional
Pssm-ID: 185070 [Multi-domain] Cd Length: 444 Bit Score: 58.31 E-value: 3.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK15115 8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDL--VISDLRMDEMDGMQLFAEIQKVQPGMPVIILTA 85
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELhrEESAAVG 1999
Cdd:PRK15115 86 HGSIPDAVAATQQGVFSFLTKPVDRDALYKAIDDAL--EQSAPAT 128
|
|
| PRK10693 |
PRK10693 |
two-component system response regulator RssB; |
1902-1976 |
4.38e-08 |
|
two-component system response regulator RssB;
Pssm-ID: 182652 [Multi-domain] Cd Length: 303 Bit Score: 56.92 E-value: 4.38e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 1902 ARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMGHEKFVTDLRELGVPLFLKKP 1976
Cdd:PRK10693 3 AANGVDALELLGGFTPDL--IICDLAMPRMNGIEFVEHLRNRGDQTPVLVISATENMADIAKALRLGVQDVLLKP 75
|
|
| REC_OmpR_ArcA_TorR-like |
cd17619 |
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; ... |
1875-1983 |
5.38e-08 |
|
phosphoacceptor receiver (REC) domain of ArcA- and TorR-like OmpR family response regulators; This subfamily includes Escherichia coli TorR and ArcA, both OmpR family response regulators that mediate adaptation to changes in various respiratory growth conditions. The TorS-TorR two-component system (TCS) is responsible for the tight regulation of the torCAD operon, which encodes the trimethylamine N-oxide (TMAO) reductase respiratory system in response to anaerobic conditions and the presence of TMAO. The ArcA-ArcB TCS is involved in cell growth during anaerobiosis. ArcA is a global regulator that controls more than 30 operons involved in redox regulation (the Arc modulon). OmpR family DNA-binding response regulators are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381134 [Multi-domain] Cd Length: 113 Bit Score: 52.77 E-value: 5.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQhaGDIKAVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd17619 3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILAR--QDIDLVLLDINLPGKDGLSLTRELREQ-SEVGIILVTG 79
|
90 100
....*....|....*....|....*....
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELL 1983
Cdd:cd17619 80 RDDEVDRIVGLEIGADDYVTKPFNPRELL 108
|
|
| REC_Spo0A |
cd17561 |
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the ... |
1875-1977 |
6.27e-08 |
|
phosphoacceptor receiver (REC) domain of Spo0A; Spo0A is a response regulator of the phosphorelay system in the early stage of spore formation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress and may act in the with sigma factor spo0H to control the expression of some genes that are critical to the sporulation process. Spo0A contains a regulatory N-terminal REC domain and a C-terminal DNA-binding transcription activation domain as its effector/output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381109 [Multi-domain] Cd Length: 108 Bit Score: 52.61 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWH-GYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELR-KRDATLP-II 1950
Cdd:cd17561 4 VLIADDNREFVQLLEEYLNSQpDMEVVgVAHNGQEALELIEEKEPDV--LLLDIIMPHLDGIGVLEKLRrMRLEKRPkII 81
|
90 100
....*....|....*....|....*..
gi 1786808614 1951 VASGMGHEKFVTDLRELGVPLFLKKPF 1977
Cdd:cd17561 82 MLTAFGQEDITQRAVELGASYYILKPF 108
|
|
| COG4567 |
COG4567 |
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains ... |
1873-1997 |
7.20e-08 |
|
DNA-binding response regulator, ActR/RegA family, consists of REC and Fis-type HTH domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 443624 [Multi-domain] Cd Length: 177 Bit Score: 54.15 E-value: 7.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1873 ELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:COG4567 5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDY--AVLDLRLGDGSGLDLIEALRERDPDARIVVL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1786808614 1953 SGMGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHREESAA 1997
Cdd:COG4567 83 TGYASIATAVEAIKLGADDYLAKPADADDLLAALERAEGDAPAPP 127
|
|
| PAS |
smart00091 |
PAS domain; PAS motifs appear in archaea, eubacteria and eukarya. Probably the most surprising ... |
76-139 |
8.59e-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: 50.86 E-value: 8.59e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 76 QTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRK 139
Cdd:smart00091 1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
|
|
| AmiR |
COG3707 |
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding ... |
1876-1992 |
8.91e-08 |
|
Two-component response regulator, AmiR/NasT family, consists of REC and RNA-binding antiterminator (ANTAR) domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 442921 [Multi-domain] Cd Length: 194 Bit Score: 54.19 E-value: 8.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVLT-ARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRkRDATLPIIVASG 1954
Cdd:COG3707 7 LVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDL--VIVDIDMPDRDGLEAARQIS-EERPAPVILLTA 83
|
90 100 110
....*....|....*....|....*....|....*...
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:COG3707 84 YSDPELIERALEAGVSAYLVKPLDPEDLLPALELALAR 121
|
|
| PRK11086 |
PRK11086 |
sensory histidine kinase DcuS; Provisional |
1729-1852 |
9.16e-08 |
|
sensory histidine kinase DcuS; Provisional
Pssm-ID: 236839 [Multi-domain] Cd Length: 542 Bit Score: 57.23 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1729 SADASQLHR---VLLNLAVNARDAMPS--GGTLKFSaenvvvdesfIHHRRatgakpgNYVLFRVTDSGVGIPRDILPRI 1803
Cdd:PRK11086 425 SGDEDQVHElitILGNLIENALEAVGGeeGGEISVS----------LHYRN-------GWLHCEVSDDGPGIAPDEIDAI 487
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1786808614 1804 FEPFFTTKEPGQSVGLGLATAlgVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:PRK11086 488 FDKGYSTKGSNRGVGLYLVKQ--SVENLGGSIAVESEPGVGTQFFVQIP 534
|
|
| HATPase_CreC-like |
cd16945 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1731-1847 |
1.02e-07 |
|
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: 52.08 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1731 DASQLHRVLLNLAVNARDAMPSGGTLKFSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTT 1810
Cdd:cd16945 1 DPFLLRQAINNLLDNAIDFSPEGGLIALQLE-----------------ADTEGIELLVFDEGSGIPDYALNRVFERFYSL 63
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1786808614 1811 KEP--GQ-SVGLGLATALGVVQSHGGFILLETEEDKGTEF 1847
Cdd:cd16945 64 PRPhsGQkSTGLGLAFVQEVAQLHGGRITLRNRPDGVLAF 103
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
964-1372 |
1.09e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 57.44 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 964 ERVEAAWKLANSATEQhaaeLKTLLATAREELHAETAKRDAAEAAASQVRAELEatnaESSRALAAAQNELARES--AER 1041
Cdd:pfam15921 285 EKASSARSQANSIQSQ----LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEDKIEELEKQLvlANS 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1042 ETTEAEFQRSK-SALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLD----------AALK 1110
Cdd:pfam15921 357 ELTEARTERDQfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmevqrleALLK 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1111 ACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQ------AELQRAKKELEKELADAN 1184
Cdd:pfam15921 437 AMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEssertvSDLTASLQEKERAIEATN 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1185 LELLDIRSRLD---HEAAARRQAEESAKQGSASADQ---RLAERLSEVQTLQERLRSE---AAQRETTEVELRDTRAALE 1255
Cdd:pfam15921 517 AEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENMtqlVGQHGRTAGAMQVEKAQLE 596
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1256 KQLAEASAALREASArLEQERDERRRVVESLTQTSTTLEARATESGSA-LEVTR-------RLLNEERAARaSALAELAA 1327
Cdd:pfam15921 597 KEINDRRLELQEFKI-LKDKKDAKIRELEARVSDLELEKVKLVNAGSErLRAVKdikqerdQLLNEVKTSR-NELNSLSE 674
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1786808614 1328 RRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAE 1372
Cdd:pfam15921 675 DYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
228-674 |
1.47e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 228 RRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTAtftdiisglekavAEHELAVKTLQAEKAEL 307
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-------------LEKLLQLLPLYQELEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 308 EKRTASSPAELEALRKRLsdeatrrqlaeDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETE-RVKRLETELESLRV 386
Cdd:COG4717 138 EAELAELPERLEELEERL-----------EELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 387 ALQTEHEKAERADAERELSEEAMVQTNTgiQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPELAARIAALTE 466
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 467 AKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQRFEQ-R 545
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 546 VAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDL-----RSNSEQQLSETQRQLADA 620
Cdd:COG4717 365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlealdEEELEEELEELEEELEEL 444
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 621 RQQLQAESERRAQAESALGQskSETERQLAEATAALADTRKQLEEATTKAAELQ 674
Cdd:COG4717 445 EEELEELREELAELEAELEQ--LEEDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1078-1621 |
1.66e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1078 AARHETERELRESLTDAERTTEALQADLDAALKACEEEAAR-RSQAEETarQSHTEFThrltaETGAREQLEKNLRQAAE 1156
Cdd:pfam15921 249 ALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSaRSQANSI--QSQLEII-----QEQARNQNSMYMRQLSD 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1157 EATRKAQaLQAELQRAKK-------ELEKELADANLELLDIRSRLDHEAAA----------------RRQAEESAKQgsa 1213
Cdd:pfam15921 322 LESTVSQ-LRSELREAKRmyedkieELEKQLVLANSELTEARTERDQFSQEsgnlddqlqklladlhKREKELSLEK--- 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1214 SADQRLAERLSEVQTLQERLRSEAAQR----ETTEVELRDTRAALEKQLAEASAALR----------EASARLEQERDER 1279
Cdd:pfam15921 398 EQNKRLWDRDTGNSITIDHLRRELDDRnmevQRLEALLKAMKSECQGQMERQMAAIQgkneslekvsSLTAQLESTKEML 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1280 RRVVESLTQTSTTLEaraTESGSALEVTRRLLNEERAARASALAELAARR------AEVDRLTTEQPHA--IEEATARLK 1351
Cdd:pfam15921 478 RKVVEELTAKKMTLE---SSERTVSDLTASLQEKERAIEATNAEITKLRSrvdlklQELQHLKNEGDHLrnVQTECEALK 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1352 AQLAEQEREREQLRLAAMSAEQRLrdratdfeaanaALRGEMEKRLRLELTwQMQREDFDRRLgELTTaLRTAEAKAGSD 1431
Cdd:pfam15921 555 LQMAEKDKVIEILRQQIENMTQLV------------GQHGRTAGAMQVEKA-QLEKEINDRRL-ELQE-FKILKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1432 SAELRHAHETLQQAHAELTRRLTERdseLASVREQAAALDAAGTRAQQTTAELqtnlNAARAELDMLNRQFAQRVAELDS 1511
Cdd:pfam15921 620 IRELEARVSDLELEKVKLVNAGSER---LRAVKDIKQERDQLLNEVKTSRNEL----NSLSEDYEVLKRNFRNKSEEMET 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1512 TEARLREECahrERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVEL--- 1588
Cdd:pfam15921 693 TTNKLKMQL---KSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFlke 769
|
570 580 590
....*....|....*....|....*....|....*.
gi 1786808614 1589 ---RVSERTAGLNAHVQQLEAELAEAQRAEEQLRHR 1621
Cdd:pfam15921 770 eknKLSQELSTVATEKNKMAGELEVLRSQERRLKEK 805
|
|
| REC_OmpR_MtrA-like |
cd17626 |
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is ... |
1875-1990 |
1.69e-07 |
|
phosphoacceptor receiver (REC) domain of MtrA-like OmpR family response regulators; MtrA is part of MtrA/MtrB (or MtrAB), a highly conserved two-component system (TCS) implicated in the regulation of cell division in the actinobacteria. In unicellular Mycobacterium tuberculosis, MtrAB coordinates DNA replication with cell division and regulates the transcription of resuscitation-promoting factor B. In filamentous Streptomyces venezuelae, it links antibiotic production to sporulation. MtrA belongs to the OmpR family of DNA-binding response regulators that contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381141 [Multi-domain] Cd Length: 115 Bit Score: 51.70 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKrDATLPIIVASG 1954
Cdd:cd17626 3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDL--VLLDLMLPGIDGIEVCRQIRA-ESGVPIVMLTA 79
|
90 100 110
....*....|....*....|....*....|....*.
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAEL 1990
Cdd:cd17626 80 KSDTVDVVLGLESGADDYVAKPFKPKELVARIRARL 115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
982-1618 |
1.79e-07 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 56.61 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 982 AELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAEssRALAAAQNELARESAERETTE-----AEFQRSKSALA 1056
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREYEGYEllkekEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1057 QQLAEAAAAQAELRSRLEKETAARHETERELRE------SLTDAE--------RTTEALQADLDAALKACEEEAAR---- 1118
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEqlrvkekiGELEAEIASLERSIAEKERELEDaeer 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1119 -----------RSQAEETARQSHTEFTHR--LTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEK------E 1179
Cdd:TIGR02169 324 lakleaeidklLAEIEELEREIEEERKRRdkLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1180 LADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRA---ALEK 1256
Cdd:TIGR02169 404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEK 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1257 QLAEASAALREASARLEQERDE---RRRVVESLTQTSTTLEARATESGS-------ALEVTR------------------ 1308
Cdd:TIGR02169 484 ELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHGTVAQLGSvgeryatAIEVAAgnrlnnvvveddavakea 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1309 -RLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEA-------------------TARLKAQLAEQEREREQLRLAA 1368
Cdd:TIGR02169 564 iELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkyepafkyvfgDTLVVEDIEAARRLMGKYRMVT 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1369 MSAE---------------QRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSA 1433
Cdd:TIGR02169 644 LEGElfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1434 ELRHA---HETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMlnRQFAQRVAELD 1510
Cdd:TIGR02169 724 EIEQLeqeEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELS 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1511 STEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVElRV 1590
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR-DL 880
|
730 740
....*....|....*....|....*...
gi 1786808614 1591 SERTAGLNAHVQQLEAELAEAQRAEEQL 1618
Cdd:TIGR02169 881 ESRLGDLKKERDELEAQLRELERKIEEL 908
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
201-929 |
1.86e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 201 QAAALDAALARVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAEL----SGREQVEAELAKARGELD------K 270
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrSKVAQLELQIASLNNEIErlearlE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 271 QVAERTATFTDIISGLEKAVAEHELavKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQ 350
Cdd:TIGR02168 411 RLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 351 SSAtqpdTALETVHHRLHAETERVKRLETELESLRVALQTEHEKAErADAERELSEEAMVQTNtgIQQRLMELNAELERT 430
Cdd:TIGR02168 489 ARL----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS-VDEGYEAAIEAALGGR--LQAVVVENLNAAKKA 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 431 KEELV-AESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGD---ERNRLAQELAEAAAARAAL 506
Cdd:TIGR02168 562 IAFLKqNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllGGVLVVDDLDNALELAKKL 641
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 507 EQQLAAASQAGagrsEADEAARAQVEADLRAAHQRFEQRvAELETDNQQLREQASRDTqaattqrgEQETALAELRAQLE 586
Cdd:TIGR02168 642 RPGYRIVTLDG----DLVRPGGVITGGSAKTNSSILERR-REIEELEEKIEELEEKIA--------ELEKALAELRKELE 708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 587 RTEAARQQIETTALDLRsnseQQLSETQRQLADARQQLQAESERRAQAESALgqskSETERQLAEATAALADTRKQLEEA 666
Cdd:TIGR02168 709 ELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEERIAQLSKEL----TELEAEIEELEERLEEAEEELAEA 780
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 667 TTKAAELQPVREQLAGEVQRGERAEAELfrsRSELETQQAALaelraraeaaeaarlqvettAQQSRTVAEQAAAEAQQQ 746
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDEL---RAELTLLNEEA--------------------ANLRERLESLERRIAATE 837
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 747 LAALRQQLQAETERREQAESALGQSKSETErqlaeataalaevRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELK 826
Cdd:TIGR02168 838 RRLEDLEEQIEELSEDIESLAAEIEELEEL-------------IEELESELEALLNERASLEEALALLRSELEELSEELR 904
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 827 KTWDNLIKETEDREALEKQLAaargDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRsseERVALL 906
Cdd:TIGR02168 905 ELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR---RRLKRL 977
|
730 740 750
....*....|....*....|....*....|
gi 1786808614 907 ASELE-------AAREALRSESARREELET 929
Cdd:TIGR02168 978 ENKIKelgpvnlAAIEEYEELKERYDFLTA 1007
|
|
| REC_NtrC1-like |
cd17572 |
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex ... |
1896-1982 |
2.04e-07 |
|
phosphoacceptor receiver (REC) domain of nitrogen regulatory protein C 1 (NtrC1) from Aquifex aeolicus and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include Aquifex aeolicus NtrC1 and Vibrio quorum-sensing signal integrator LuxO. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381114 [Multi-domain] Cd Length: 121 Bit Score: 51.43 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1896 GYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMGHEKFVTDLRELGVPLFLKK 1975
Cdd:cd17572 22 GYKVTHVETGKEALAFLSDQPPDV--VLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHGSVDIAVEAMRLGAYDFLEK 99
|
....*..
gi 1786808614 1976 PFAAEEL 1982
Cdd:cd17572 100 PFDADRL 106
|
|
| HATPase_EnvZ-like |
cd16950 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1852 |
2.13e-07 |
|
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: 50.91 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNARDAmpSGGTLKFSAENvvvdesfihhrratgakPGNYVLFRVTDSGVGIPRDILPRIFEPFF--TTKE 1812
Cdd:cd16950 1 LKRVLSNLVDNALRY--GGGWVEVSSDG-----------------EGNRTRIQVLDNGPGIAPEEVDELFQPFYrgDNAR 61
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1786808614 1813 PGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16950 62 GTSGTGLGLAIVQRISDAHGGSLTLANRAGGGLCARIELP 101
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
517-1363 |
2.91e-07 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 56.13 E-value: 2.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 517 GAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQAsrdtQAATTQRGEQETALAELRAQLERTEAARQQIE 596
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKE----QAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 597 TTALDLRS--NSEQQLSETQRQLADARQQLQAESER------RAQAESALGQSKSETERQLAEATAALADTRKQLEEATT 668
Cdd:pfam02463 237 ERIDLLQEllRDEQEEIESSKQEIEKEEEKLAQVLKenkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 669 KAAELQPVREQLAGEVQRGERAEAElfRSRSELETQQaalaelraraeaaEAARLQVETTAQQSRTVAEQAAAEAQQQLA 748
Cdd:pfam02463 317 KESEKEKKKAEKELKKEKEEIEELE--KELKELEIKR-------------EAEEEEEEELEKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 749 ALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKT 828
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 829 WDNLIKETEDREALEKQLAAARGDLERQLAETKAELDqqLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLAS 908
Cdd:pfam02463 462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER--SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 909 ELEAAREALRsesarreelETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLL 988
Cdd:pfam02463 540 NYKVAISTAV---------IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 989 AT--AREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARES-AERETTEAEFQRSKSALAQQLAEAAAA 1065
Cdd:pfam02463 611 ATleADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSeVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1066 QAELRSR-LEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEfthRLTAETGAR 1144
Cdd:pfam02463 691 KEEILRRqLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK---KEEKEEEKS 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1145 EQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAE---ESAKQGSASADQRLAE 1221
Cdd:pfam02463 768 ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEkikEEELEELALELKEEQK 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1222 RLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESG 1301
Cdd:pfam02463 848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA 927
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1302 SALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQ 1363
Cdd:pfam02463 928 EILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEER 989
|
|
| COG1754 |
COG1754 |
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown]; |
820-1284 |
3.38e-07 |
|
Uncharacterized C-terminal domain of topoisomerase IA [Function unknown];
Pssm-ID: 441360 [Multi-domain] Cd Length: 892 Bit Score: 55.59 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 820 DQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSS 899
Cdd:COG1754 50 VDDDDKKDDVDDDKKKKKKLLKAAAKKKKALALALAADDEDEELLAADDELEEEKVIKLLLLELAVERVARAAAVRAAAA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 900 EERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQ 979
Cdd:COG1754 130 EAARLAALLRRRLVLRRLVRRLLVRLLLLRLVLLLLRLLVARRAARRRRRRRRRRARRRELERRRERARAAEAEEAAAAA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 980 HAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQL 1059
Cdd:COG1754 210 AAAADAGRAAAARDGKGGGKLAAGGAAAAAAAAAAAAAAAAALAEAAAAAAVREPPTPTTTTTAQAATTTTTRAAAARTT 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1060 AEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTA 1139
Cdd:COG1754 290 RSAQQAARRTRLGGEGTYTTTTTTTTTTSAAAAAAAAAAAALAAAAAAAYAPPPPYYYKKKAAAAAAAAAAAAAAAARRP 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1140 ETGAREQLEKNLRQAAEEATRK--AQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQ 1217
Cdd:COG1754 370 PAARAALLSDDRLLLELLLLRRtaAAAAAAAAATATTTAAAAAAGAGAVGTAAAGAVFFFGGFLLFAEEEDDDEEDDDDD 449
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 1218 RLAERLSEVQTLQErlrSEAAQRETTEVELRDTRAALEKQLAEASAALRE--------ASARLEQERDERRRVVE 1284
Cdd:COG1754 450 DLPALEEGLPLLKE---GVLADQHFTQPPPRYTEAPLVKRMEELGIGRPStyasilstLADRIYVRLDKRRLIPE 521
|
|
| PAS_9 |
pfam13426 |
PAS domain; This domain is found in many signalling proteins in which it functions as a sensor ... |
95-189 |
3.60e-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: 49.77 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 95 QGDILFVNHRWSALTGRSQAESQG--FGWLLAvHPDDNKRVTEEWRkcvRGEKEFRLDFRLRNKDGSTRWVAGHAMRVLD 172
Cdd:pfam13426 1 DGRIIYVNDAALRLLGYTREELLGksITDLFA-EPEDSERLREALR---EGKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76
|
90
....*....|....*..
gi 1786808614 173 DHEQPNGIIGSILDINE 189
Cdd:pfam13426 77 DGGELVGIIAILRDITE 93
|
|
| REC_PatA-like |
cd17602 |
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) ... |
1879-1954 |
3.87e-07 |
|
phosphoacceptor receiver (REC) domain of PatA and similar domains; Nostoc sp. (or Anabaena sp.) PatA is necessary for proper patterning of heterocysts along filaments. PatA contains phosphoacceptor REC domain at its C-terminus and an N-terminal PATAN (PatA N-terminus) domain, which was proposed in a bioinformatics study to mediate protein-protein interactions. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays. Some members of this group may have an inactive REC domain, lacking canonical metal-binding and active site residues.
Pssm-ID: 381129 [Multi-domain] Cd Length: 102 Bit Score: 50.06 E-value: 3.87e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786808614 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDA--TLPIIVASG 1954
Cdd:cd17602 5 DDRPSIQKMIEYFLEKQGFRVVVIDDPLRALTTLLNSKPDL--ILIDIDMPDLDGYELCSLLRKSSAlkDTPIIMLTG 80
|
|
| REC_NtrC |
cd19919 |
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; ... |
1879-1951 |
4.58e-07 |
|
phosphoacceptor receiver (REC) domain of DNA-binding transcriptional regulator NtrC; DNA-binding transcriptional regulator NtrC is also called nitrogen regulation protein NR(I) or nitrogen regulator I (NRI). It contains an N-terminal receiver (REC) domain, followed by a sigma-54 interaction domain, and a C-terminal helix-turn-helix DNA-binding domain. It is part of the two-component regulatory system NtrB/NtrC, which controls expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. DNA-binding response regulator NtrC is phosphorylated by NtrB; phosphorylation of the N-terminal REC domain activates the central sigma-54 interaction domain and leads to the transcriptional activation from promoters that require sigma(54)-containing RNA polymerase. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381146 [Multi-domain] Cd Length: 116 Bit Score: 50.35 E-value: 4.58e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIV 1951
Cdd:cd19919 7 DDDSSIRWVLERALAGAGLTVTSFENAQEALAALASSQPD--VLISDIRMPGMDGLALLAQIKQRHPDLPVII 77
|
|
| ompR |
PRK09468 |
osmolarity response regulator; Provisional |
1871-1999 |
5.37e-07 |
|
osmolarity response regulator; Provisional
Pssm-ID: 181883 [Multi-domain] Cd Length: 239 Bit Score: 53.05 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1871 NGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPII 1950
Cdd:PRK09468 4 ENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHL--MVLDLMLPGEDGLSICRRLRSQNNPTPII 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1786808614 1951 VASGMGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHREESAAVG 1999
Cdd:PRK09468 82 MLTAKGEEVDRIVGLEIGADDYLPKPFNPRELLARIRAVLRRQAPELPG 130
|
|
| REC_DC-like |
cd17534 |
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; ... |
1876-1986 |
5.42e-07 |
|
phosphoacceptor receiver (REC) domain of modulated diguanylate cyclase and similar domains; This groups includes a modulated diguanylate cyclase containing a PAS sensor domain from Desulfovibrio desulfuricans G20. Members of this group contain N-terminal REC domains and various output domains including the GGDEF, histidine kinase, and helix-turn-helix (HTH) DNA binding domains. Also included in this family is Mycobacterium tuberculosis PdtaR, a transcriptional antiterminator that contains a REC domain and an ANTAR RNA-binding output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381089 [Multi-domain] Cd Length: 117 Bit Score: 50.10 E-value: 5.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1876 MLADDEQGVLDVTAEILEWHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMP-FMDGVELCRELRKRdATLPIIVAS 1953
Cdd:cd17534 4 LIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDL--ILMDINLKgDMDGIEAAREIREK-FDIPVIFLT 80
|
90 100 110
....*....|....*....|....*....|....
gi 1786808614 1954 GMGHEKFVTDLRELGvPL-FLKKPFAAEELLRSL 1986
Cdd:cd17534 81 AYSDEETLERAKETN-PYgYLVKPFNERELKAAI 113
|
|
| REC_CheV-like |
cd19924 |
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This ... |
1875-1953 |
5.45e-07 |
|
phosphoacceptor receiver (REC) domain of chemotaxis protein CheV and similar proteins; This subfamily includes the REC domains of Bacillus subtilis chemotaxis protein CheV, Myxococcus xanthus gliding motility regulatory protein FrzE, and similar proteins. CheV is a hybrid protein with an N-terminal CheW-like domain and a C-terminal CheY-like REC domain. The CheV pathway is one of three systems employed by B. subtilis for sensory adaptation that contribute to chemotaxis. It is involved in the transmission of sensory signals from chemoreceptors to flagellar motors. Together with CheW, it is involved in the coupling of methyl-accepting chemoreceptors to the central two-component histidine kinase CheA. FrzE is a hybrid sensor histidine kinase/response regulator that is part of the Frz pathway that controls cell reversal frequency to support directional motility during swarming and fruiting body formation. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381151 [Multi-domain] Cd Length: 111 Bit Score: 50.07 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAG-------DIKAVITDILMPFMDGVELCRELRK--RDA 1945
Cdd:cd19924 1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskELDLIITDIEMPKMDGYELTFELRDdpRLA 80
|
....*...
gi 1786808614 1946 TLPIIVAS 1953
Cdd:cd19924 81 NIPVILNS 88
|
|
| REC_OmpR_BaeR-like |
cd19938 |
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is ... |
1875-1990 |
5.59e-07 |
|
phosphoacceptor receiver (REC) domain of BaeR-like OmpR family response regulators; BaeR is part of the BaeSR two-component system that is involved in regulating genes that confer multidrug and metal resistance. In Salmonella, BaeSR induces AcrD and MdtABC drug efflux systems, increasing multidrug and metal resistance. In Escherichia coli, BaeR stimulates multidrug resistance via mdtABC (multidrug transporter ABC, formerly known as yegMNO) genes, which encode a resistance-nodulation-cell division (RND) drug efflux system. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which are characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381165 [Multi-domain] Cd Length: 114 Bit Score: 50.07 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd19938 2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDL--ILLDLMLPGTDGLTLCREIRRF-SDVPIIMVTA 78
|
90 100 110
....*....|....*....|....*....|....*.
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAEL 1990
Cdd:cd19938 79 RVEEIDRLLGLELGADDYICKPYSPREVVARVKAIL 114
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
959-1303 |
8.44e-07 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 53.75 E-value: 8.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 959 EAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAeaaasqvraeleatnAESSRALAAAQNELARES 1038
Cdd:pfam07888 60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL---------------SASSEELSEEKDALLAQR 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1039 AERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQAdLDAALKACEEEAAR 1118
Cdd:pfam07888 125 AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS-LSKEFQELRNSLAQ 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1119 RSQAEETARQSHTEFTHRLTAETGAREQLE------KNLRQAAEEATRKAQALQAELQ-------RAKKELEK---ELAD 1182
Cdd:pfam07888 204 RDTQVLQLQDTITTLTQKLTTAHRKEAENEalleelRSLQERLNASERKVEGLGEELSsmaaqrdRTQAELHQarlQAAQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1183 ANLELLDIRSRLdHEAAARRQAEESAKQGSASADQRLAERLS-EVQTLQERLRSEAAQRETTEVEL-------RDTRAAL 1254
Cdd:pfam07888 284 LTLQLADASLAL-REGRARWAQERETLQQSAEADKDRIEKLSaELQRLEERLQEERMEREKLEVELgrekdcnRVQLSES 362
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1786808614 1255 EKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSA 1303
Cdd:pfam07888 363 RRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVADAKWSE 411
|
|
| REC_OmpR_NsrR-like |
cd18159 |
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family ... |
1875-1990 |
9.75e-07 |
|
phosphoacceptor receiver (REC) domain of Streptococcus agalactiae NsrR-like OmpR family response regulators; Streptococcus agalactiae NsrR is a lantibiotic resistance-associated response regulator and is part of the nisin resistance operon. It is a member of the NsrRK two-component system (TCS) that is involved in the regulation of lantibiotic resistance genes such as a membrane-associated lipoprotein of LanI, and the nsr gene cluster which encodes for the resistance protein NSR and the ABC transporter NsrFP, both conferring resistance against nisin. This subfamily also includes Staphylococcus epidermidis GraR, part of the GraR/GraS TCS involved in resistance against cationic antimicrobial peptides, and Bacillus subtilis BceR, part of the BceS/BceR TCS involved in the regulation of bacitracin resistance. Members of this subfamily belong to the OmpR family of DNA-binding response regulators, which contain N-terminal receiver (REC) and C-terminal DNA-binding winged helix-turn-helix effector domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381143 [Multi-domain] Cd Length: 113 Bit Score: 49.20 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd18159 1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDL--VLLDINLPYFDGFYWCREIRQI-SNVPIIFISS 77
|
90 100 110
....*....|....*....|....*....|....*.
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAEL 1990
Cdd:cd18159 78 RDDNMDQVMAINMGGDDYITKPFDLDVLLAKIKAIL 113
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1254-1629 |
1.22e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.97 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1254 LEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATEsgsalevtrrlLNEERAARASALAELAARRAEVD 1333
Cdd:pfam15921 76 IERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQE-----------MQMERDAMADIRRRESQSQEDLR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1334 RLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAE---QRLRDRATDFEAANAALRGEMEKRLRLEL------TWQ 1404
Cdd:pfam15921 145 NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHFrslgsaISK 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1405 MQREdFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRL-TERDSELASVREQAAAldaAGTRAQQTTAE 1483
Cdd:pfam15921 225 ILRE-LDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLiSEHEVEITGLTEKASS---ARSQANSIQSQ 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1484 LQTNLNAARAELDMLNRQfaqrVAELDSTEARLREECAHRER---------------AEAELDRMRDAQDGFQQSTAELN 1548
Cdd:pfam15921 301 LEIIQEQARNQNSMYMRQ----LSDLESTVSQLRSELREAKRmyedkieelekqlvlANSELTEARTERDQFSQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1549 ERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVElRVSERTAGLNAHVQQLEAELA----------EAQRAEEQL 1618
Cdd:pfam15921 377 DQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITID-HLRRELDDRNMEVQRLEALLKamksecqgqmERQMAAIQG 455
|
410
....*....|.
gi 1786808614 1619 RHRRIEAVSTL 1629
Cdd:pfam15921 456 KNESLEKVSSL 466
|
|
| pleD |
PRK09581 |
response regulator PleD; Reviewed |
1897-1950 |
1.29e-06 |
|
response regulator PleD; Reviewed
Pssm-ID: 236577 [Multi-domain] Cd Length: 457 Bit Score: 53.37 E-value: 1.29e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1786808614 1897 YKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPII 1950
Cdd:PRK09581 27 YTVLTASSGAEAIAICEREQPDI--ILLDVMMPGMDGFEVCRRLKSDPATthIPVV 80
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
757-1529 |
1.32e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.82 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 757 ETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKET 836
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 837 EDREALEKQLAAARGDLERQLAETKAELDQQLAALA---EARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAA 913
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKlqeEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 914 REALRSESARREELETALP---KTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLAT 990
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKeleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 991 AREELHAETAKRDAAEAAASQVRAELEAT----------NAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLA 1060
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEeesielkqgkLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1061 EAAAAQAELRSRLEKETAAR-----------HETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQS 1129
Cdd:pfam02463 487 ELLLSRQKLEERSQKESKARsglkvllalikDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1130 HTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADA----NLELLDIRSRLDHEAAARRQAE 1205
Cdd:pfam02463 567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKrakvVEGILKDTELTKLKESAKAKES 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1206 ESAKQGSAS----ADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRR 1281
Cdd:pfam02463 647 GLRKGVSLEeglaEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1282 VVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQERER 1361
Cdd:pfam02463 727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1362 EQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALrtaEAKAGSDSAELRHAHET 1441
Cdd:pfam02463 807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE---ELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1442 LQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFA--QRVAELDSTEARLREE 1519
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAdeKEKEENNKEEEEERNK 963
|
810
....*....|
gi 1786808614 1520 CAHRERAEAE 1529
Cdd:pfam02463 964 RLLLAKEELG 973
|
|
| REC_RocR |
cd17530 |
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR ... |
1875-1983 |
1.61e-06 |
|
phosphoacceptor receiver (REC) domain of response regulator RocR; The response regulator RocR from some pathogens contains an N-terminal phosphoreceiver (REC) domain and a C-terminal EAL domain that possesses c-di-GMP specific phosphodiesterase activity. The RocR REC domain is phosphorylated and modulates its EAL domain enzymatic activity, regulating the local level of c-di-GMP. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381086 [Multi-domain] Cd Length: 123 Bit Score: 48.98 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYK-VLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVAS 1953
Cdd:cd17530 3 VLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDI--IICDLKMPDMDGIEFLRHLAESHSNAAVILMS 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1786808614 1954 GMG---HEKFVTDLRELGVPLF--LKKPFAAEELL 1983
Cdd:cd17530 81 GLDggiLESAETLAGANGLNLLgtLSKPFSPEELT 115
|
|
| REC_citrate_TCS |
cd19925 |
phosphoacceptor receiver (REC) domain of citrate family two-component system response ... |
1875-1986 |
1.76e-06 |
|
phosphoacceptor receiver (REC) domain of citrate family two-component system response regulators; This family includes Lactobacillus paracasei MaeR, Escherichia coli DcuR and DpiA, Klebsiella pneumoniae CitB, as well as Bacillus DctR, MalR, and CitT. These are all response regulators of two-component systems (TCSs) from the citrate family, and are involved in the transcriptional regulation of genes associated with L-malate catabolism (MaeRK), citrate-specific fermentation (DpiAB, CitAB), plasmid inheritance (DpiAB), anaerobic fumarate respiratory system (DcuRS), and malate transport/utilization (MalKR). REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381152 [Multi-domain] Cd Length: 118 Bit Score: 48.78 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWH-GYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:cd19925 3 VLIVEDDPMVAEIHRAYVEQVpGFTVIgTAGTGEEALKLLKERQPDL--ILLDIYLPDGNGLDLLRELRAAGHDVDVIVV 80
|
90 100 110
....*....|....*....|....*....|....
gi 1786808614 1953 SGMGHEKFVTDLRELGVPLFLKKPFAAEELLRSL 1986
Cdd:cd19925 81 TAANDVETVREALRLGVVDYLIKPFTFERLRQRL 114
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1412-1619 |
1.79e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1412 RRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAA 1491
Cdd:COG4942 2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1492 RAELDMLNRQFAQRVAELDSTEARLREECAHRERAE--------------AELDRMRDAQDGFQQSTAELNERLTRLTTD 1557
Cdd:COG4942 82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 1558 VEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERT---AGLNAHVQQLEAELAEAQRAEEQLR 1619
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALKAERQkllARLEKELAELAAELAELQQEAEELE 226
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
830-1621 |
2.26e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.87 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 830 DNLIKETEDREALEK---QLAAARGDLERQLAETKAELDQQLAALAeaRSQAEREAAERRQTEES-----LLQASRSSEE 901
Cdd:pfam01576 194 ERLKKEEKGRQELEKakrKLEGESTDLQEQIAELQAQIAELRAQLA--KKEEELQAALARLEEETaqknnALKKIRELEA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 902 RVALLASELEAAREALRSESARREELETALPKTKTELgqrlaeaaaeaaglRARMDFEAAERErveaawklANSATEQHA 981
Cdd:pfam01576 272 QISELQEDLESERAARNKAEKQRRDLGEELEALKTEL--------------EDTLDTTAAQQE--------LRSKREQEV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 982 AELKTLLataREELHAETAKRDAAEAAASQVRAELEATNAESSR---ALAAAQNELARESAERETTEAEFQRSKSALAQQ 1058
Cdd:pfam01576 330 TELKKAL---EEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRnkaNLEKAKQALESENAELQAELRTLQQAKQDSEHK 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1059 LAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQshtefthrLT 1138
Cdd:pfam01576 407 RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQEL--------LQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1139 AETGAREQLEKNLRQAAEEATRKAQALQAElQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQ---GSASA 1215
Cdd:pfam01576 479 EETRQKLNLSTRLRQLEDERNSLQEQLEEE-EEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRlqrELEAL 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1216 DQRLAERLSEVQTLQ---ERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVvesltqtstt 1292
Cdd:pfam01576 558 TQQLEEKAAAYDKLEktkNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRA---------- 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1293 lEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEAtarlkaqlAEQEREREQLrlaamsaE 1372
Cdd:pfam01576 628 -EAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNV--------HELERSKRAL-------E 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1373 QRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRrlgelttalrtaeakagsdsaELRHAHETLQQAHAELTRR 1452
Cdd:pfam01576 692 QQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFER---------------------DLQARDEQGEEKRRQLVKQ 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1453 LTERDSELASVREQAAALDAAGTRaqqttaeLQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDR 1532
Cdd:pfam01576 751 VRELEAELEDERKQRAQAVAAKKK-------LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDE 823
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1533 MRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAgLNAHVQQLEAELAEAQ 1612
Cdd:pfam01576 824 ILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRR-LEARIAQLEEELEEEQ 902
|
....*....
gi 1786808614 1613 RAEEQLRHR 1621
Cdd:pfam01576 903 SNTELLNDR 911
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
847-1050 |
2.44e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.07 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 847 AAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRsseeRVALLASELEAAREALRSESARREE 926
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR----RIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 927 LETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTL------LATAREELHAETA 1000
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELradlaeLAALRAELEAERA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1001 KRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQR 1050
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1114-1533 |
2.75e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1114 EEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQA-ELQRAKKELEKELADANLELldirS 1192
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERL----E 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1193 RLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARL 1272
Cdd:COG4717 150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1273 EQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLka 1352
Cdd:COG4717 230 EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL-- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1353 QLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAkagSDS 1432
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV---EDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1433 AELRHAHETLQQAHaELTRRLTERDSELASVREQAAALDAAGTRAQQTT--AELQTNLNAARAELDMLNRQFAQRVAELD 1510
Cdd:COG4717 385 EELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELAELEAELE 463
|
410 420
....*....|....*....|....*
gi 1786808614 1511 --STEARLREECAHRERAEAELDRM 1533
Cdd:COG4717 464 qlEEDGELAELLQELEELKAELREL 488
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1049-1380 |
2.95e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1049 QRSKSALAQQLAEAAAAQAELRSRLEKETAARhetERELRESLTDAERTTEAlQADLDAALKACEEEAA-------RRSQ 1121
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAR---EVERRRKLEEAEKARQA-EMDRQAAIYAEQERMAmererelERIR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1122 AEETARQSHTEFTHRLTAETGAREQLE--------KNLRQAAE-EATRKAQALQAELQRAKKELEKELADANLELLDIRS 1192
Cdd:pfam17380 355 QEERKRELERIRQEEIAMEISRMRELErlqmerqqKNERVRQElEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1193 RldheaAARRQAEESAKQGsasadQRLAERLSEVQTLQERLRSEAAQRETTEVELrdtraalEKQLAEASAALREASARL 1272
Cdd:pfam17380 435 R-----EVRRLEEERAREM-----ERVRLEEQERQQQVERLRQQEEERKRKKLEL-------EKEKRDRKRAEEQRRKIL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1273 EQERDERRRVVESLTQTSTTLEARATESGSAL--EVTRRLLNEERAARASALAElaarraevdRLTTEQPHAIEEATARL 1350
Cdd:pfam17380 498 EKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEMEER---------RRIQEQMRKATEERSRL 568
|
330 340 350
....*....|....*....|....*....|
gi 1786808614 1351 KAqlaeQEREREQLRLAAMSAEQRLRDRAT 1380
Cdd:pfam17380 569 EA----MEREREMMRQIVESEKARAEYEAT 594
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
530-681 |
3.00e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 530 QVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQ 609
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786808614 610 LSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKA----AELQPVREQLA 681
Cdd:COG4913 375 LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKsnipARLLALRDALA 450
|
|
| PAC |
smart00086 |
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif ... |
149-190 |
3.87e-06 |
|
Motif C-terminal to PAS motifs (likely to contribute to PAS structural domain); PAC motif occurs C-terminal to a subset of all known PAS motifs. It is proposed to contribute to the PAS domain fold.
Pssm-ID: 197509 Cd Length: 43 Bit Score: 45.25 E-value: 3.87e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1786808614 149 LDFRLRNKDGSTRWVAGHAMRVLDDHEQPNGIIGSILDINER 190
Cdd:smart00086 2 VEYRLRRKDGSYIWVLVSASPIRDEDGEVEGILGVVRDITER 43
|
|
| cztS_silS_copS |
TIGR01386 |
heavy metal sensor kinase; Members of this family contain a sensor histidine kinase domain ... |
1633-1833 |
4.10e-06 |
|
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: 51.62 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1633 MAHELNNVLAPVLMAAQ-LLRKQVSGKSrtLVDSVESSA---QRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQ 1708
Cdd:TIGR01386 248 LAHELRTPLTNLLGQTQvALSQPRTGEE--YREVLESNLeelERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVA 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1709 ETFP-----RNVRVSSEVADDLPlisADASQLHRVLLNLAVNARDAMPSGGTLKfsaenvvvdesfIHHRRATGAkpgny 1783
Cdd:TIGR01386 326 EYFEplaeeRGVRIRVEGEGLVR---GDPQMFRRAISNLLSNALRHTPDGGTIT------------VRIERRSDE----- 385
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 1784 VLFRVTDSGVGIPRDILPRIFEPFF----TTKEPGQSVGLGLATALGVVQSHGG 1833
Cdd:TIGR01386 386 VRVSVSNPGPGIPPEHLSRLFDRFYrvdpARSNSGEGTGLGLAIVRSIMEAHGG 439
|
|
| NtrB |
COG3852 |
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms]; |
73-191 |
4.16e-06 |
|
Signal transduction histidine kinase NtrB, nitrogen specific [Signal transduction mechanisms];
Pssm-ID: 443061 [Multi-domain] Cd Length: 361 Bit Score: 51.39 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 73 EVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQG--FGWLLAVHPDDNKRVteeWRKCVRGEKEFRLD 150
Cdd:COG3852 4 ESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGrpLAELFPEDSPLRELL---ERALAEGQPVTERE 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1786808614 151 FRLRNKDGSTRWVAGHAMRvLDDHEQPNGIIGSILDINERK 191
Cdd:COG3852 81 VTLRRKDGEERPVDVSVSP-LRDAEGEGGVLLVLRDITERK 120
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
558-1401 |
4.58e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.99 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 558 EQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESA 637
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 638 LGQSKSETErQLAEATAALADTRKQLEEA------------TTKAAELQPVREQLAGEV----QRGERAEAELFRSRSEL 701
Cdd:TIGR02169 253 LEKLTEEIS-ELEKRLEEIEQLLEELNKKikdlgeeeqlrvKEKIGELEAEIASLERSIaekeRELEDAEERLAKLEAEI 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 702 ETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAEsALGQSKSETERQLAE 781
Cdd:TIGR02169 332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE-KLKREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 782 ATAALAEVRAQLEQAttasSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLeRQLAETK 861
Cdd:TIGR02169 411 LQEELQRLSEELADL----NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY-DRVEKEL 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 862 AELDQQLAALAEARSQAEREAAERRQTEE-----------SLLQASRSSEERVALLASEL------------EAAREALR 918
Cdd:TIGR02169 486 SKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgTVAQLGSVGERYATAIEVAAgnrlnnvvveddAVAKEAIE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 919 SESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDF-EAAERERVEAAWKLANSATEQHAAELKTLLATAReelha 997
Cdd:TIGR02169 566 LLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYR----- 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 998 etakrdaaeaaasqvRAELEATNAESSRALAAAQNelaresaeRETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKET 1077
Cdd:TIGR02169 641 ---------------MVTLEGELFEKSGAMTGGSR--------APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1078 AARHETERELRESLTDAERTTEALQADLDAALKacEEEAARRSQAEETARQSHTEfthrltAETGAREQLEKNLRQAAEE 1157
Cdd:TIGR02169 698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQ--EEEKLKERLEELEEDLSSLE------QEIENVKSELKELEARIEE 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1158 ATRKAQALQAELQRAKKELE----KELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERL 1233
Cdd:TIGR02169 770 LEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1234 RSEAAQRETTEVELRDtraaLEKQLAEASAALREASARLEQERDERRRVVESLTQtsttLEARATESGSALEVTRRLLNE 1313
Cdd:TIGR02169 850 KSIEKEIENLNGKKEE----LEEELEELEAALRDLESRLGDLKKERDELEAQLRE----LERKIEELEAQIEKKRKRLSE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1314 ERAARASALAELAARRAEVDRLTTEQPHAIEEATarLKAQLAEQEREREQLRLAAMSAEQrlrdratDFEAANAALRGEM 1393
Cdd:TIGR02169 922 LKAKLEALEEELSEIEDPKGEDEEIPEEELSLED--VQAELQRVEEEIRALEPVNMLAIQ-------EYEEVLKRLDELK 992
|
....*...
gi 1786808614 1394 EKRLRLEL 1401
Cdd:TIGR02169 993 EKRAKLEE 1000
|
|
| HATPase_VanS-like |
cd16923 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1852 |
4.85e-06 |
|
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: 47.00 E-value: 4.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNArdampsggtLKFSAENVVVD-ESFIHhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEP 1813
Cdd:cd16923 1 LQRVFSNLLSNA---------IKYSPENTRIYiTSFLT---------DDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS 62
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1786808614 1814 GQSVG--LGLATALGVVQSHGGFILLETeEDKGTEFQIYLP 1852
Cdd:cd16923 63 RNTEGagLGLSIAKAIIELHGGSASAEY-DDNHDLFKVRLP 102
|
|
| REC_OmpR_CtrA |
cd17616 |
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is ... |
1874-1988 |
5.04e-06 |
|
phosphoacceptor receiver (REC) domain of CtrA-like OmpR family response regulators; CtrA is part of the CckA-ChpT-CtrA phosphorelay that is conserved in alphaproteobacteria and is important in orchestrating the cell cycle, polar development, and flagellar biogenesis. CtrA is the master regulator of flagella synthesis genes and also regulates genes involved in the cell cycle, exopolysaccharide synthesis, and cyclic-di-GMP signaling. CtrA is active as a transcription factor when phosphorylated. It is a member of the OmpR family of DNA-binding response regulators, characterized by a REC domain and a winged helix-turn-helix (wHTH) DNA-binding output effector domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381132 [Multi-domain] Cd Length: 114 Bit Score: 47.40 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1874 LLMLADDEQgvldvTAEILEWH----GYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPI 1949
Cdd:cd17616 1 VLLIEDDSA-----TAQSIELMlkseGFNVYTTDLGEEGLDLGKLYDYDI--ILLDLNLPDMSGYEVLRTLRLAKVKTPI 73
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1786808614 1950 IVASGM-GHEKFVTDLrELGVPLFLKKPFAAEELLRSLHA 1988
Cdd:cd17616 74 LILSGLaDIEDKVKGL-GFGADDYMTKPFHKDELVARIHA 112
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
226-623 |
5.89e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 226 LERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELavktLQAEKA 305
Cdd:PRK02224 347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE----LREERD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 306 ELEKRTASSPAELEALRKRLsdEATRRQLAE-------------------DDLRSLREDFDKLQSSATQPDTALETVHHR 366
Cdd:PRK02224 423 ELREREAELEATLRTARERV--EEAEALLEAgkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLER 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 367 LHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEamvqtntgiqqrLMELNAELERTKEElvAESARRTQAEA 446
Cdd:PRK02224 501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE------------LRERAAELEAEAEE--KREAAAEAEEE 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 447 GQGGGEVNPELAARIAALTEAKAQVEKeLVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEA 526
Cdd:PRK02224 567 AEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE 645
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 527 ARAQveaDLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQEtALAELRAQLERTEAARQQIETtaldLRSNS 606
Cdd:PRK02224 646 ARIE---EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE-ELEELRERREALENRVEALEA----LYDEA 717
|
410
....*....|....*...
gi 1786808614 607 EqQLSETQRQL-ADARQQ 623
Cdd:PRK02224 718 E-ELESMYGDLrAELRQR 734
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
992-1285 |
6.02e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 6.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 992 REELHAETAKRDAAEAAASQVRAELE---ATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAE 1068
Cdd:pfam17380 305 KEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQ 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1069 LRsRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFtHRLTAETGAREQLE 1148
Cdd:pfam17380 385 ME-RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1149 KNLRQAAEEATRKaqalqaelqraKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQT 1228
Cdd:pfam17380 463 ERLRQQEEERKRK-----------KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE 531
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1786808614 1229 LQERLRSEAAQRETTEVElrdTRAALEKQLAEASAALREASArLEQERDERRRVVES 1285
Cdd:pfam17380 532 EERRREAEEERRKQQEME---ERRRIQEQMRKATEERSRLEA-MEREREMMRQIVES 584
|
|
| REC_HupR |
cd17596 |
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of ... |
1875-1993 |
7.00e-06 |
|
phosphoacceptor receiver (REC) domain of hydrogen uptake protein regulator (HupR); Members of this subfamily are response regulator components of two-component systems that regulates hydrogenase activity, including HupR and HoxA. HupR is part of the HupT/HupR system that controls the synthesis of the membrane-bound [NiFe]hydrogenase, HupSL, of the photosynthetic bacterium Rhodobacter capsulatus. It belongs to the nitrogen regulatory protein C (NtrC) family of response regulators, which activate transcription by RNA polymerase (RNAP) in response to a change in the environment. HupR is an unusual member of this family as it activates transcription when unphosphorylated, and transcription is inhibited by phosphorylation. Proteins in this subfamily contain an N-terminal REC domain, a central sigma-54 interaction domain that lacks ATPase activity, and a C-terminal DNA-binding domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381127 [Multi-domain] Cd Length: 133 Bit Score: 47.36 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHgYKVLTARDGQQALSLYDQHagDIKAVITDILMPFMDGVELCRELRKR-DATLPIIVAS 1953
Cdd:cd17596 3 ILVVDDEVRSLEALRRTLEED-FDVLTAASAEEALAILEEE--WVQVILCDQRMPGTTGVEFLKEVRERwPEVVRIIISG 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1786808614 1954 GMGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHA-----ELHRE 1993
Cdd:cd17596 80 YTDSEDIIAGINEAGIYQYLTKPWHPDQLLLTVRNaarlfELQRE 124
|
|
| HATPase_RstB-like |
cd16939 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1853 |
8.11e-06 |
|
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: 46.27 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNArdampsggtLKFSAENVvvdesfihhrRATGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFF------ 1808
Cdd:cd16939 1 MARALDNLLRNA---------LRYAHRTV----------RIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVrldpsr 61
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1786808614 1809 TTKEPGqsVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPA 1853
Cdd:cd16939 62 DRATGG--FGLGLAIVHRVALWHGGHVECDDSELGGACFRLTWPR 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
527-705 |
8.40e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 527 ARAQVEAdLRAAHQRFEQRVAELETDNQQLREQASRDTQAAT-----TQRGEQETALAELRAQLERTEAARQQIETTALD 601
Cdd:COG4913 608 NRAKLAA-LEAELAELEEELAEAEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAELEAELERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 602 LRSnSEQQLSETQRQLADARQQLQAESERRAQAESALGQskseTERQLAEATAALADTRKQLEEATtkAAELQPVREQLA 681
Cdd:COG4913 687 LAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQ----AEEELDELQDRLEAAEDLARLEL--RALLEERFAAAL 759
|
170 180
....*....|....*....|....
gi 1786808614 682 GEvQRGERAEAELFRSRSELETQQ 705
Cdd:COG4913 760 GD-AVERELRENLEERIDALRARL 782
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-638 |
8.61e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 8.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEK 304
Cdd:COG4913 349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 305 AELEKRTASSPAELEALRKRLSDEAtrrQLAEDDLR------SLREDFDKLQSSATQ-----------PD-------TAL 360
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEAL---GLDEAELPfvgeliEVRPEEERWRGAIERvlggfaltllvPPehyaaalRWV 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 361 ETVHHRLHAETERVKRLETELESLRVALQT----------------EHEKAERADAERELSEEAMVQTNTGIqqrlmeln 424
Cdd:COG4913 506 NRLHLRGRLVYERVRTGLPDPERPRLDPDSlagkldfkphpfrawlEAELGRRFDYVCVDSPEELRRHPRAI-------- 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 425 aelerTKEELVAESARRtQAEAGQGGGEVNPEL----AARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAA 500
Cdd:COG4913 578 -----TRAGQVKGNGTR-HEKDDRRRIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ 651
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 501 AARAALEQQLAAASQagAGRSEADEAARAQVEA---DLRAAHQRFEQRVAELEtDNQQLREQASRDTQAATTQRGEQETA 577
Cdd:COG4913 652 RLAEYSWDEIDVASA--EREIAELEAELERLDAssdDLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEE 728
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 578 LAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESAL 638
Cdd:COG4913 729 LDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1113-1619 |
9.22e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.30 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1113 EEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANlelldiRS 1192
Cdd:PTZ00121 1057 EGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDAR------KA 1130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1193 RLDHEAAARRQAEEsAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARL 1272
Cdd:PTZ00121 1131 EEARKAEDARKAEE-ARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1273 EQERDERRRVVEsltqtsttlEARATESGSALEVTRRllNEERAARASALAELaarraevDRLTTEQPHAIEEATARLKA 1352
Cdd:PTZ00121 1210 EERKAEEARKAE---------DAKKAEAVKKAEEAKK--DAEEAKKAEEERNN-------EEIRKFEEARMAHFARRQAA 1271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1353 QLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQR-----EDFDRRLGELTTALRTAEAK 1427
Cdd:PTZ00121 1272 IKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakkkaDAAKKKAEEAKKAAEAAKAE 1351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1428 AGSDSAELRHAHETlQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQT--TAELQTNLNAARAELDMLNRQfAQR 1505
Cdd:PTZ00121 1352 AEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkKADELKKAAAAKKKADEAKKK-AEE 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1506 VAELDSTEARlREECAHRERAEAELDRMRDAQDGFQQS----TAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQ 1581
Cdd:PTZ00121 1430 KKKADEAKKK-AEEAKKADEAKKKAEEAKKAEEAKKKAeeakKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500 510
....*....|....*....|....*....|....*...
gi 1786808614 1582 SHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEQLR 1619
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK 1546
|
|
| PRK11517 |
PRK11517 |
DNA-binding response regulator HprR; |
1875-1997 |
1.10e-05 |
|
DNA-binding response regulator HprR;
Pssm-ID: 183172 [Multi-domain] Cd Length: 223 Bit Score: 48.74 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHagDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK11517 3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKD--DYALIILDIMLPGMDGWQILQTLRTAKQTPVICLTAR 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1786808614 1955 MGHEKFVTDLrELGVPLFLKKPFAAEELLRSLHAELHREESAA 1997
Cdd:PRK11517 81 DSVDDRVRGL-DSGANDYLVKPFSFSELLARVRAQLRQHHALN 122
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
522-699 |
1.41e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 522 EADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRdtqaATTQRGEQETALAELRAQLERTEAARQQIETTALD 601
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELAR----LEAELERLEARLDALREELDELEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 602 lrsNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLA 681
Cdd:COG4913 342 ---QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
170
....*....|....*...
gi 1786808614 682 GEVQRGERAEAELFRSRS 699
Cdd:COG4913 419 RELRELEAEIASLERRKS 436
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1199-1580 |
1.47e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1199 AARRQAEESAKQGSASADQrlAERLSevQTLQERLRSEAAQRETTEVELrdTRAALEKQLAEASAALREASARLEQERDE 1278
Cdd:PRK10929 58 EERKGSLERAKQYQQVIDN--FPKLS--AELRQQLNNERDEPRSVPPNM--STDALEQEILQVSSQLLEKSRQAQQEQDR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1279 RRRVVESLTQtsttLEARATESGSAL-EVTRRLLN-------EERAARASALAELAARRAEVDRLTTEQPHA-IEEATAR 1349
Cdd:PRK10929 132 AREISDSLSQ----LPQQQTEARRQLnEIERRLQTlgtpntpLAQAQLTALQAESAALKALVDELELAQLSAnNRQELAR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1350 LKAQLAEQEREREQLRLAAM-SAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDfdrrlgELTTALRTAEAKA 1428
Cdd:PRK10929 208 LRSELAKKRSQQLDAYLQALrNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINR------ELSQALNQQAQRM 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1429 GSDSAELRHA-HETLQQAHAeltrrlterdseLASVREQAAALDAAGTraqqttaeLQTNLNAARAEL-DMLNRQfaqrv 1506
Cdd:PRK10929 282 DLIASQQRQAaSQTLQVRQA------------LNTLREQSQWLGVSNA--------LGEALRAQVARLpEMPKPQ----- 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 1507 aELDSTEARLReecAHRERAEAELDRMRDAQDGFQQSTAELNErltrlttdvEAARQQAEQETTQRRSLEDALQ 1580
Cdd:PRK10929 337 -QLDTEMAQLR---VQRLRYEDLLNKQPQLRQIRQADGQPLTA---------EQNRILDAQLRTQRELLNSLLS 397
|
|
| HATPase_BaeS-like |
cd16946 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1731-1852 |
1.51e-05 |
|
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: 45.92 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1731 DASQLHRVLLNLAVNARDAMPSGGTLKFSAenvvvdesfihhrratGAKPGNYVLFrVTDSGVGIPRDILPRIFEPFFT- 1809
Cdd:cd16946 1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRA----------------AQTPQEVRLD-VEDSAPGVSDDQLARLFERFYRv 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1786808614 1810 ----TKEPGQSvGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16946 64 essrNRASGGS-GLGLAICHNIALAHGGTISAEHSPLGGLRLVLTLP 109
|
|
| REC_DesR-like |
cd19930 |
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of ... |
1875-1988 |
1.55e-05 |
|
phosphoacceptor receiver (REC) domain of DesR and similar proteins; This group is composed of Bacillus subtilis DesR, Streptococcus pneumoniae response regulator spr1814, and similar proteins, all containing an N-terminal REC domain and a C-terminal LuxR family helix-turn-helix (HTH) DNA-binding output domain. DesR is a response regulator that, together with its cognate sensor kinase DesK, comprises a two-component regulatory system that controls membrane fluidity. Phosphorylation of the REC domain of DesR is allosterically coupled to two distinct exposed surfaces of the protein, controlling noncanonical dimerization/tetramerization, cooperative activation, and DesK binding. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381157 [Multi-domain] Cd Length: 117 Bit Score: 46.11 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHG--YKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:cd19930 1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDV--AILDIEMPGRTGLEVAAELREELPDTKVLIV 78
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1953 SGMGHEKFVTDLRELGVPLFLKKPFAAEEL---LRSLHA 1988
Cdd:cd19930 79 TTFGRPGYFRRALAAGVDGYVLKDRPIEELadaIRTVHA 117
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1107-1358 |
1.63e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.95 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1107 AALKACEEEAArrsQAEEtARQSHTEFTHRLTAETGAREqlEKNLRQAAEEATRKAQALQAELQR--AKKELEKELADAN 1184
Cdd:PRK05035 436 AEIRAIEQEKK---KAEE-AKARFEARQARLEREKAARE--ARHKKAAEARAAKDKDAVAAALARvkAKKAAATQPIVIK 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1185 LELLDIRSRLDHEAAARR---QAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEA 1261
Cdd:PRK05035 510 AGARPDNSAVIAAREARKaqaRARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARA 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1262 SAALREASARLEQ------ERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRL 1335
Cdd:PRK05035 590 KAKKAAQQAASAEpeeqvaEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEP 669
|
250 260
....*....|....*....|....*.
gi 1786808614 1336 TTEQ---PHAIEEATARLKAQLAEQE 1358
Cdd:PRK05035 670 EEAEdpkKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK10604 |
PRK10604 |
sensor protein RstB; Provisional |
1730-1852 |
2.41e-05 |
|
sensor protein RstB; Provisional
Pssm-ID: 236724 [Multi-domain] Cd Length: 433 Bit Score: 49.22 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1730 ADASQLHRVLLNLAVNArdampsggtLKFSAENVVVDESFihhrratgakPGNYVLFRVTDSGVGIPRDILPRIFEPfFT 1809
Cdd:PRK10604 315 LDMRLMERVLDNLLNNA---------LRYAHSRVRVSLLL----------DGNQACLIVEDDGPGIPPEERERVFEP-FV 374
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1786808614 1810 TKEPGQS-----VGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:PRK10604 375 RLDPSRDratggCGLGLAIVHSIALAMGGSVNCDESELGGARFSFSWP 422
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
860-1582 |
2.41e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.58 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 860 TKAELDQQLAALAEARSQAEREAAERRQTEESLL-----QASRSSEERVALLASELEAAREALRSESARREEL--ETALP 932
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLtlctpCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLtqKREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 933 KTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHA------------AELKTLLATAREELHAETA 1000
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAvtqieqqaqrihTELQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1001 KRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETA-- 1078
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAti 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1079 -ARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARqshtefthRLTAETGAREQLEKNLRQAAEE 1157
Cdd:TIGR00618 413 dTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ--------ESAQSLKEREQQLQTKEQIHLQ 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1158 ATRKAQALQAELQRaKKELEKELadanlelldiRSRLDHEAAARRQAEESAkqgsasADQRLAERLSEvqtlqerlrsEA 1237
Cdd:TIGR00618 485 ETRKKAVVLARLLE-LQEEPCPL----------CGSCIHPNPARQDIDNPG------PLTRRMQRGEQ----------TY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1238 AQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAA 1317
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1318 RASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRL 1397
Cdd:TIGR00618 618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1398 RLELTWQMQREDfDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAaldaagtra 1477
Cdd:TIGR00618 698 MLAQCQTLLREL-ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNN--------- 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1478 QQTTAELQT--NLNAARAELDMLNRQFAQRVAELDSTEARLREECAHREraeaelDRMRDAQDGFQQSTAELNERLTRLT 1555
Cdd:TIGR00618 768 EEVTAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE------DILNLQCETLVQEEEQFLSRLEEKS 841
|
730 740
....*....|....*....|....*..
gi 1786808614 1556 TDVEAARQQAEQETTQRRSLEDALQQS 1582
Cdd:TIGR00618 842 ATLGEITHQLLKYEECSKQLAQLTQEQ 868
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1210-1432 |
2.68e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1210 QGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQT 1289
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1290 STTLEARATESGSALEVTRR---------LLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQERE 1360
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1361 REQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDS 1432
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1162-1595 |
2.82e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 49.25 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1162 AQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRE 1241
Cdd:COG3903 500 ALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAA 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1242 TTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASA 1321
Cdd:COG3903 580 AALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 659
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1322 LAELAARRAEVDRLTTEQPHAIEEATARLkaqLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLEL 1401
Cdd:COG3903 660 AAAAAALAAAAAAAAAAAAAAAAAAAALA---AAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAAL 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1402 TWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTT 1481
Cdd:COG3903 737 AAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAL 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1482 AELQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAA 1561
Cdd:COG3903 817 AAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAA 896
|
410 420 430
....*....|....*....|....*....|....
gi 1786808614 1562 RQQAEQETTQRRSLEDALQQSHGEVELRVSERTA 1595
Cdd:COG3903 897 AAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAA 930
|
|
| HATPase_BasS-like |
cd16940 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1785-1851 |
3.12e-05 |
|
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: 45.09 E-value: 3.12e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786808614 1785 LFRVTDSGVGIPRDILPRIFEPFF-TTKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYL 1851
Cdd:cd16940 46 VIRVEDNGPGIDEEELEALFERFYrSDGQNYGGSGLGLSIVKRIVELHGGQIFLGNAQGGGLEAWVRL 113
|
|
| PRK09836 |
PRK09836 |
DNA-binding transcriptional activator CusR; Provisional |
1875-1992 |
3.27e-05 |
|
DNA-binding transcriptional activator CusR; Provisional
Pssm-ID: 182102 [Multi-domain] Cd Length: 227 Bit Score: 47.23 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLydQHAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK09836 3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHL--AMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1955 MGH-EKFVTDLrELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:PRK09836 81 LGTiEHRVKGL-ELGADDYLVKPFAFAELLARVRTLLRR 118
|
|
| HATPase_EcPhoR-like |
cd16952 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1735-1854 |
3.79e-05 |
|
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: 44.50 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1735 LHRVLLNLAVNARDAMPSGGTLKFSAEnvvvdesfihhRRATGAKpgnyvlFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16952 1 LRSAFSNLVSNAVKYTPPSDTITVRWS-----------QEESGAR------LSVEDTGPGIPPEHIPRLTERFYRVDIER 63
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1786808614 1815 QS----VGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAA 1854
Cdd:cd16952 64 CRntggTGLGLAIVKHVMSRHDARLLIASELGKGSRFTCLFPSS 107
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1342-1637 |
4.25e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1342 AIEEATARLKAQLAEQEREREQLrlaamsaEQRLRDRATDFEAANAALRgEMEKRLRlELTWQMQREdFDRRLGELTTAL 1421
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKL-------TEEISELEKRLEEIEQLLE-ELNKKIK-DLGEEEQLR-VKEKIGELEAEI 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1422 RTAEAKAGSDSAELRHAHETLQQAhaeltrrlterDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLnrq 1501
Cdd:TIGR02169 304 ASLERSIAEKERELEDAEERLAKL-----------EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--- 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1502 fAQRVAELDSTEARLREECAHR----ERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLED 1577
Cdd:TIGR02169 370 -RAELEEVDKEFAETRDELKDYreklEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786808614 1578 ALQQSHGEVE------LRVSERTAGLNAHVQQLEAELAEAQRAEEQLRHRRIEAVSTLAGGMAHEL 1637
Cdd:TIGR02169 449 EIKKQEWKLEqlaadlSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1162-1393 |
4.28e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1162 AQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQgsasADQRLAERLSEVQTLQERLRSEAAQRE 1241
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA----LARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1242 TTEVELRDTRAALEKQL-----------------AEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSAL 1304
Cdd:COG4942 94 ELRAELEAQKEELAELLralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1305 EVTRRLLNEERAARASALAELAARRAEVDRLTTEQphaieeatARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEA 1384
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKEL--------AELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245
|
250
....*....|
gi 1786808614 1385 AN-AALRGEM 1393
Cdd:COG4942 246 AGfAALKGKL 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
335-591 |
4.70e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.76 E-value: 4.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 335 AEDDLRSLREDFDKLQSSATQPDTALETVHH-----RLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEeam 409
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELlepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 410 vqtntgIQQRLMELNAELERTKEELVAESARRTQAEA---GQGGGEVNpELAARIAALTEAKAQVEKELVEQQAVAKALG 486
Cdd:COG4913 300 ------LRAELARLEAELERLEARLDALREELDELEAqirGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALG 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 487 dernrlaqelaEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQa 566
Cdd:COG4913 373 -----------LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA- 440
|
250 260
....*....|....*....|....*
gi 1786808614 567 attqrgEQETALAELRAQLERTEAA 591
Cdd:COG4913 441 ------RLLALRDALAEALGLDEAE 459
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
519-1210 |
4.98e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 48.43 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 519 GRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQasrdtqaattqrgeqetalaelRAQLERTEAARQQiETT 598
Cdd:TIGR00618 194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA----------------------LQQTQQSHAYLTQ-KRE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 599 ALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKseterqLAEATAALADTRKQLEEATTKAAELQPVRE 678
Cdd:TIGR00618 251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP------LAAHIKAVTQIEQQAQRIHTELQSKMRSRA 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 679 QLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAET 758
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 759 ERREQAESALGQSKSETERQ----LAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLaDQDAELKKTWDNLIK 834
Cdd:TIGR00618 405 LQREQATIDTRTSAFRDLQGqlahAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL-KEREQQLQTKEQIHL 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 835 ETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARS------QAEREAAERRQTEESLLQASRSSEERVALLAS 908
Cdd:TIGR00618 484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPltrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 909 ELEAAREALRSESARREELETALPKTKTELGQ-RLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTL 987
Cdd:TIGR00618 564 QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRlQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 988 LATAREELHAETAKRDAAEAAASqVRAELEATNAESSRALAAAQNELARESAERETTEaefqrsksALAQQLAEAAAAQA 1067
Cdd:TIGR00618 644 KLTALHALQLTLTQERVREHALS-IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA--------QCQTLLRELETHIE 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1068 ELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTH----------RL 1137
Cdd:TIGR00618 715 EYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHlaaeiqffnrLR 794
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 1138 TAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQ 1210
Cdd:TIGR00618 795 EEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQE 867
|
|
| phoR |
PRK11006 |
phosphate regulon sensor histidine kinase PhoR; |
1670-1853 |
5.12e-05 |
|
phosphate regulon sensor histidine kinase PhoR;
Pssm-ID: 182895 [Multi-domain] Cd Length: 430 Bit Score: 48.08 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1670 AQRGADIVKQVLTFARGfhgERAPVS--------PEMLvRDIAKSVQETFPRNVRVSSEVADDLPlISADASQLHRVLLN 1741
Cdd:PRK11006 250 TQRMEGLVKQLLTLSKI---EAAPTIdlnekvdvPMML-RVLEREAQTLSQGKHTITFEVDNSLK-VFGNEDQLRSAISN 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1742 LAVNARDAMPSGGTLKFSAENVvvdesfihhrrATGAKpgnyvlFRVTDSGVGIPRDILPRIFEPFF-----TTKEPGQS 1816
Cdd:PRK11006 325 LVYNAVNHTPEGTHITVRWQRV-----------PQGAE------FSVEDNGPGIAPEHIPRLTERFYrvdkaRSRQTGGS 387
|
170 180 190
....*....|....*....|....*....|....*..
gi 1786808614 1817 vGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPA 1853
Cdd:PRK11006 388 -GLGLAIVKHALSHHDSRLEIESEVGKGTRFSFVLPE 423
|
|
| REC_Rcp-like |
cd17557 |
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and ... |
1898-1988 |
5.26e-05 |
|
phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains; This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381108 [Multi-domain] Cd Length: 129 Bit Score: 44.71 E-value: 5.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1898 KVLTARDGQQALS-LYDQHAGDIKA----VITDILMPFMDGVELCRELRKRDAT--LPIIVASGMGHEKFVTDLRELGVP 1970
Cdd:cd17557 27 ELHVVRDGEEALDfLRGEGEYADAPrpdlILLDLNMPRMDGFEVLREIKADPDLrrIPVVVLTTSDAEEDIERAYELGAN 106
|
90
....*....|....*...
gi 1786808614 1971 LFLKKPFAAEELLRSLHA 1988
Cdd:cd17557 107 SYIVKPVDFEEFVEAIRS 124
|
|
| CitB |
COG2197 |
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal ... |
1875-1940 |
5.43e-05 |
|
DNA-binding response regulator, NarL/FixJ family, contains REC and HTH domains [Signal transduction mechanisms, Transcription];
Pssm-ID: 441799 [Multi-domain] Cd Length: 131 Bit Score: 44.88 E-value: 5.43e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWH-GYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCREL 1940
Cdd:COG2197 4 VLIVDDHPLVREGLRALLEAEpDIEVVgEAADGEEALELLEELRPDV--VLLDIRMPGMDGLEALRRL 69
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
317-1209 |
5.58e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.43 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 317 ELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESLRVALQTEHEKAE 396
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 397 RADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPELaaRIAALTEAKAQVEKELV 476
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER--RKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 477 EQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQagagRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQL 556
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK----LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 557 REQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAES 636
Cdd:pfam02463 401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 637 ALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAE 716
Cdd:pfam02463 481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 717 AAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQaesalgqsKSETERQLAEATAALAEVRAQLEQA 796
Cdd:pfam02463 561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ--------LDKATLEADEDDKRAKVVEGILKDT 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 797 TTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARS 876
Cdd:pfam02463 633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 877 QAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARM 956
Cdd:pfam02463 713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 957 DFEAAERERVEAAWKLANSATEQHAAELKTLLATArEELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELAR 1036
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE-EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1037 ESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADL-DAALKACEEE 1115
Cdd:pfam02463 872 LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELlLEEADEKEKE 951
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1116 AARRSQAEETARQSHTEFTHRLTAETGAREQLEKNL--RQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSR 1193
Cdd:pfam02463 952 ENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEerYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINK 1031
|
890
....*....|....*.
gi 1786808614 1194 LDHEAAARRQAEESAK 1209
Cdd:pfam02463 1032 GWNKVFFYLELGGSAE 1047
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
534-1529 |
5.79e-05 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 48.28 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 534 DLRAAHQRFEQRVAEletdnQQLREQASRDTQAaTTQRGEQETALAELRAQLER--------TEAARQQIETTALDL--- 602
Cdd:NF041483 98 DARAQTQRILQEHAE-----HQARLQAELHTEA-VQRRQQLDQELAERRQTVEShvnenvawAEQLRARTESQARRLlde 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 603 -RSNSEQQLS----ETQRQLADARQQLQAESER-RAQAESALGQSKSETERQLAEATAaladtrkQLEEATTKAAELqpv 676
Cdd:NF041483 172 sRAEAEQALAaaraEAERLAEEARQRLGSEAESaRAEAEAILRRARKDAERLLNAAST-------QAQEATDHAEQL--- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 677 REQLAGEVQRGERAEAELFRSRSELETQQAALAElraraeaaeaarlqvETTAQQSRTVAEQAAAEAQQQLAALRQQLQA 756
Cdd:NF041483 242 RSSTAAESDQARRQAAELSRAAEQRMQEAEEALR---------------EARAEAEKVVAEAKEAAAKQLASAESANEQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 757 ETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAElkktwDNLIKET 836
Cdd:NF041483 307 TRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAE-----EVLTKAS 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 837 EDREALEKqlaAARGDLERQLAETKAELDQQLAALAEARSQ----AEREAAERRQTEESLLQASRSSEERVALLASELEA 912
Cdd:NF041483 382 EDAKATTR---AAAEEAERIRREAEAEADRLRGEAADQAEQlkgaAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 913 AREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEqhaaelkTLLATAR 992
Cdd:NF041483 459 EGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERATTLRRQAEE-------TLERTRA 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 993 EELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAeRETTEAEfQRSKSALAQQLAEAAAAQAELRSR 1072
Cdd:NF041483 532 EAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELT-RLHTEAE-ERLTAAEEALADARAEAERIRREA 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1073 LEKETAARHETERELRESLTDAERTTEALQADldaalkACEEEAARRSQAEETARQSHTEFT---HRLTAEtgAREQLEK 1149
Cdd:NF041483 610 AEETERLRTEAAERIRTLQAQAEQEAERLRTE------AAADASAARAEGENVAVRLRSEAAaeaERLKSE--AQESADR 681
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1150 NLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEaaaRRQAEESAKQGSASADQRLAERLSEVQTL 1229
Cdd:NF041483 682 VRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQE---RERAREQSEELLASARKRVEEAQAEAQRL 758
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1230 QERLRSEAAQ----RETTEVELRDTRAALEKQLAEASAALREAsARLEQERDERRRVVESLTQTSTTLEARATESGSALE 1305
Cdd:NF041483 759 VEEADRRATElvsaAEQTAQQVRDSVAGLQEQAEEEIAGLRSA-AEHAAERTRTEAQEEADRVRSDAYAERERASEDANR 837
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1306 VTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATD---- 1381
Cdd:NF041483 838 LRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAqadr 917
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1382 --FEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELR-HAHETL--QQAHAELTRRLTER 1456
Cdd:NF041483 918 liGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRaEAAETVgsAQQHAERIRTEAER 997
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 1457 -DSELASVREQAAAldAAGTRAQQTTAELQTNLNAARAE-LDMLNRQFAQRVAELDSTEARLREEcAHRERAEAE 1529
Cdd:NF041483 998 vKAEAAAEAERLRT--EAREEADRTLDEARKDANKRRSEaAEQADTLITEAAAEADQLTAKAQEE-ALRTTTEAE 1069
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
898-1246 |
6.05e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 6.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 898 SSEERVALLASELEAAREALRSESARREELETALpktkTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLAN-SA 976
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAEL----DALQERREALQRLAEYSWDEIDVASAEREIAELEAELERlDA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 977 TEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAEssraLAAAQNELARESAERETTEAEFQRSKSALA 1056
Cdd:COG4913 683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFAAA 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1057 QQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETarqshtefthr 1136
Cdd:COG4913 759 LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED----------- 827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1137 ltaetGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDI-------------RSRLDHEAAARRQ 1203
Cdd:COG4913 828 -----GLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIpfgpgrylrlearPRPDPEVREFRQE 902
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1786808614 1204 AEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVE 1246
Cdd:COG4913 903 LRAVTSGASLFDEELSEARFAALKRLIERLRSEEEESDRRWRA 945
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
839-1319 |
6.14e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.23 E-value: 6.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 839 REALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEervallasELEAAREALR 918
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE--------ELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 919 SESARREELETALPKTKtelgQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSatEQHAAELKTLLATAREELHAE 998
Cdd:COG4717 116 EELEKLEKLLQLLPLYQ----ELEALEAELAELPERLEELEERLEELRELEEELEEL--EAELAELQEELEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 999 TAKRDAAEAAAsqvRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETA 1078
Cdd:COG4717 190 TEEELQDLAEE---LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGG 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1079 ARHETERELRESLTDAERTTeALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEA 1158
Cdd:COG4717 267 SLLSLILTIAGVLFLVLGLL-ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1159 TRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEesakqgsasADQRLAERLSEVQTLQERLRSEAA 1238
Cdd:COG4717 346 IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE---------QAEEYQELKEELEELEEQLEELLG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1239 QREttEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQ--TSTTLEARATESGSALEVTRRLLNEERA 1316
Cdd:COG4717 417 ELE--ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAA 494
|
...
gi 1786808614 1317 ARA 1319
Cdd:COG4717 495 LKL 497
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
188-651 |
7.42e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 7.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 188 NERKVADDTRTTDQAAALDAALARVQQEVSYRkeiglELERRADELKKRDSELE----SANRQLWAELSGREQVEAeLAK 263
Cdd:PRK04863 279 NERRVHLEEALELRRELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEqdyqAASDHLNLVQTALRQQEK-IER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 264 ARGELDKqvaertatftdiisgLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRrqlaeddlrslr 343
Cdd:PRK04863 353 YQADLEE---------------LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQA------------ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 344 edFDKLQSSA---TQPDTALETVHHRLHAETERVKRLETELESLRVALQTEHEkaERADAERELSeeamvqtntgiqqrl 420
Cdd:PRK04863 406 --LDVQQTRAiqyQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATE--ELLSLEQKLS--------------- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 421 melNAELERTKEELVAESARRTqaeagqgGGEVNPELAARIAalteakAQVEKELVEQQAVAKALGDERNRLAQELAEAA 500
Cdd:PRK04863 467 ---VAQAAHSQFEQAYQLVRKI-------AGEVSRSEAWDVA------RELLRRLREQRHLAEQLQQLRMRLSELEQRLR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 501 AARAALEQQLAAASQAGAGRSEADEAARAQVEA-----DLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQE 575
Cdd:PRK04863 531 QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELearleSLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD 610
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786808614 576 tALAELRAQLERTEAARQQIETTALDLRSNsEQQLSETQRQLADARQQLQAESERRAQAESalgqSKSETERQLAE 651
Cdd:PRK04863 611 -ALARLREQSGEEFEDSQDVTEYMQQLLER-ERELTVERDELAARKQALDEEIERLSQPGG----SEDPRLNALAE 680
|
|
| REC_RcNtrC-like |
cd19928 |
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C ... |
1875-1976 |
9.98e-05 |
|
phosphoacceptor receiver (REC) domain of Rhodobacter capsulatus nitrogen regulatory protein C (NtrC) and similar NtrC family response regulators; NtrC family proteins are transcriptional regulators that have REC, AAA+ ATPase/sigma-54 interaction, and DNA-binding output domains. This subfamily of NtrC proteins include NtrC, also called nitrogen regulator I (NRI), from Rhodobacter capsulatus, Azospirillum brasilense, and Azorhizobium caulinodans. NtrC is part of the NtrB/NtrC two-component system that controls the expression of the nitrogen-regulated (ntr) genes in response to nitrogen limitation. The N-terminal REC domain of NtrC proteins regulate the activity of the protein and its phosphorylation controls the AAA+ domain oligomerization, while the central AAA+ domain participates in nucleotide binding, hydrolysis, oligomerization, and sigma54 interaction. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381155 [Multi-domain] Cd Length: 100 Bit Score: 43.26 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASg 1954
Cdd:cd19928 1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDL--VITDVVMPDENGLDLIPRIKKARPDLPIIVMS- 77
|
90 100
....*....|....*....|....
gi 1786808614 1955 mGHEKFVTDLR--ELGVPLFLKKP 1976
Cdd:cd19928 78 -AQNTLMTAVKaaERGAFEYLPKP 100
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1096-1516 |
1.10e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1096 RTTEALQADLDAALKACEEEAARRSQAEEtARQSHTEFTHRLTAETGAREQLEKNLRQAAE--EATRKAQALQAELQRAK 1173
Cdd:PRK04863 276 RHANERRVHLEEALELRRELYTSRRQLAA-EQYRLVEMARELAELNEAESDLEQDYQAASDhlNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1174 KELEKelADANLELLDIRSRLDHEAAARRQAEESAKQGSAsadQRLAERLSEVQTLQERLRSEAAQretteveLRDTRAA 1253
Cdd:PRK04863 355 ADLEE--LEERLEEQNEVVEEADEQQEENEARAEAAEEEV---DELKSQLADYQQALDVQQTRAIQ-------YQQAVQA 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1254 LEK---QLAEASAALREASARLEQERDERRRVVESLTQTSTTL---EARATESGSALEVTRRLLNEERAARASALAELAA 1327
Cdd:PRK04863 423 LERakqLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLsvaQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELL 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1328 RraevdRLTTEQPHAieEATARLKAQLAEQEREREQLRlaamSAEQRLRdratdfeaanaalrgEMEKRLRLELTWQMQR 1407
Cdd:PRK04863 503 R-----RLREQRHLA--EQLQQLRMRLSELEQRLRQQQ----RAERLLA---------------EFCKRLGKNLDDEDEL 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1408 EDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTE---RDSELASVREQAAALDAAGTRAQQTTAEL 1484
Cdd:PRK04863 557 EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQL 636
|
410 420 430
....*....|....*....|....*....|..
gi 1786808614 1485 QTNLNAARAELDmlnrQFAQRVAELDSTEARL 1516
Cdd:PRK04863 637 LERERELTVERD----ELAARKQALDEEIERL 664
|
|
| dpiB |
PRK15053 |
sensor histidine kinase DpiB; Provisional |
1725-1852 |
1.19e-04 |
|
sensor histidine kinase DpiB; Provisional
Pssm-ID: 185013 [Multi-domain] Cd Length: 545 Bit Score: 47.13 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1725 LPLISADASQLHR------------VLLNLAVNARDAmpsggTLKFSAENVVVdESFIhhrratgAKPGNYVLFRVTDSG 1792
Cdd:PRK15053 411 LKMVIVPGSQLSQlppgldstefaaIVGNLLDNAFEA-----SLRSDEGNKIV-ELFL-------SDEGDDVVIEVADQG 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1793 VGIPRDILPRIFEPFFTTK--EPGQSvGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:PRK15053 478 CGVPESLRDKIFEQGVSTRadEPGEH-GIGLYLIASYVTRCGGVITLEDNDPCGTLFSIFIP 538
|
|
| HisKA |
cd00082 |
Histidine Kinase A (dimerization/phosphoacceptor) domain; Histidine Kinase A dimers are formed ... |
1623-1685 |
1.23e-04 |
|
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: 41.81 E-value: 1.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 1623 IEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKS--RTLVDSVESSAQRGADIVKQVLTFAR 1685
Cdd:cd00082 1 LQAKGEFLANVSHELRTPLTAIRGALELLEEELLDDEeqREYLERIREEAERLLRLINDLLDLSR 65
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1342-1533 |
1.25e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.68 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1342 AIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTAL 1421
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1422 RTAEAKAGSDSAELRHAHETLQQA------HAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAEL 1495
Cdd:COG4942 111 RALYRLGRQPPLALLLSPEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 1786808614 1496 DMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRM 1533
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
283-704 |
1.28e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 47.14 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 283 ISGLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAED-DLRSLREDFDKLQSSATQPDTA-L 360
Cdd:pfam12128 260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEALEDQHGAFLDAdI 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 361 ETVHhrLHAETERVKRLETELESLRVALQTE-HEKAERA-DAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVA-- 436
Cdd:pfam12128 340 ETAA--ADQEQLPSWQSELENLEERLKALTGkHQDVTAKyNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDdl 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 437 ---ESARRTQAEAGQGggEVNPELAARIAALTEAK-----AQVEKELVEQQAVAKALGD-----------ERNRLAQELA 497
Cdd:pfam12128 418 qalESELREQLEAGKL--EFNEEEYRLKSRLGELKlrlnqATATPELLLQLENFDERIErareeqeaanaEVERLQSELR 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 498 EAAAARAALEQQLAAASQAGAGRSEADEAARAQVEAD-------LRAAHQRFEQRVAEL-------ETD----------- 552
Cdd:pfam12128 496 QARKRRDQASEALRQASRRLEERQSALDELELQLFPQagtllhfLRKEAPDWEQSIGKVispellhRTDldpevwdgsvg 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 553 -----------------------NQQLRE---QASRDTQAATTQRGEQETALAELRAQLERTEA----ARQQIETTALDL 602
Cdd:pfam12128 576 gelnlygvkldlkridvpewaasEEELRErldKAEEALQSAREKQAAAEEQLVQANGELEKASReetfARTALKNARLDL 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 603 RsnseqQLSETQRQLADARQQlqAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVRE---- 678
Cdd:pfam12128 656 R-----RLFDEKQSEKDKKNK--ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgald 728
|
490 500
....*....|....*....|....*..
gi 1786808614 679 -QLAGEVQRGERAEAELFRSRSELETQ 704
Cdd:pfam12128 729 aQLALLKAAIAARRSGAKAELKALETW 755
|
|
| PRK11083 |
PRK11083 |
DNA-binding response regulator CreB; Provisional |
1875-1992 |
1.36e-04 |
|
DNA-binding response regulator CreB; Provisional
Pssm-ID: 236838 [Multi-domain] Cd Length: 228 Bit Score: 45.34 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLydQHAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK11083 6 ILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDK--LRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTA 83
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1955 MGHE-KFVTDLrELGVPLFLKKPFAAEELLRSLHAELHR 1992
Cdd:PRK11083 84 RSDEvDRLVGL-EIGADDYVAKPFSPREVAARVRTILRR 121
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
304-624 |
1.58e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.87 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 304 KAELEKRTASSPAELEALRKRLSDEATRRQlaedDLRSLREDFDKLQSS------ATQPDTALETVHHRLHAETERVKRL 377
Cdd:PRK04863 781 RAAREKRIEQLRAEREELAERYATLSFDVQ----KLQRLHQAFSRFIGShlavafEADPEAELRQLNRRRVELERALADH 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 378 ETELESLRVALQTEHEkaeRADAERELSEEAMVQTNTGIQQRLMELNAELERtkeelvAESARRTQAEAGQGGGEVNPEL 457
Cdd:PRK04863 857 ESQEQQQRSQLEQAKE---GLSALNRLLPRLNLLADETLADRVEEIREQLDE------AEEAKRFVQQHGNALAQLEPIV 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 458 AA------RIAALTEAKAQVEKELVEQQAVAKALGDERNRL-----AQELAEAAAARAALEQQLAAASQAGAGRSEADEA 526
Cdd:PRK04863 928 SVlqsdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 527 ARA---------QVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRgeQETALAELRAQLERTEAARQQIET 597
Cdd:PRK04863 1008 LRQaqaqlaqynQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARAR--RDELHARLSANRSRRNQLEKQLTF 1085
|
330 340
....*....|....*....|....*..
gi 1786808614 598 TALDLRsNSEQQLSETQRQLADARQQL 624
Cdd:PRK04863 1086 CEAEMD-NLTKKLRKLERDYHEMREQV 1111
|
|
| REC_ETR-like |
cd19933 |
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and ... |
1875-1990 |
1.71e-04 |
|
phosphoacceptor receiver (REC) domain of plant ethylene receptors ETR1, ETR2, and EIN4, and similar proteins; Plant ethylene receptors contain N-terminal transmembrane domains that contain an ethylene binding site and also serve in localization of the receptor to the endoplasmic reticulum or the Golgi apparatus and a C-terminal histidine kinase (HK)-like domain. There are five ethylene receptors (ETR1, ERS1, ETR2, ERS2, and EIN4) in Arabidopsis thaliana. ETR1, ETR2, and EIN4 also contain REC domains C-terminal to the HK domain. ETR1 and ERS1 belong to subfamily 1, and have functional HK domains while ETR2, ERS2, and EIN4 belong to subfamily 2, and lack the necessary residues for HK activity and may function as serine/threonine kinases. The plant hormone ethylene plays an important role in plant growth and development. It regulates seed germination, seedling growth, leaf and petal abscission, fruit ripening, organ senescence, and pathogen responses. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381160 [Multi-domain] Cd Length: 117 Bit Score: 43.16 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIKAVITDILMPFMDGVELCRELRKR--DATLPIIVA 1952
Cdd:cd19933 3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKLfgRRERPLIVA 82
|
90 100 110
....*....|....*....|....*....|....*....
gi 1786808614 1953 SGMGHEKFVTDL-RELGVPLFLKKPFaaeeLLRSLHAEL 1990
Cdd:cd19933 83 LTANTDDSTREKcLSLGMNGVITKPV----SLHALGDEL 117
|
|
| PRK09776 |
PRK09776 |
putative diguanylate cyclase; Provisional |
96-193 |
1.72e-04 |
|
putative diguanylate cyclase; Provisional
Pssm-ID: 182070 [Multi-domain] Cd Length: 1092 Bit Score: 46.97 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 96 GDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKE-FRLDFRLRNKDGSTRWVAGHAMRVLDDH 174
Cdd:PRK09776 303 GQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSGEINsYSMEKRYYRRDGEVVWALLAVSLVRDTD 382
|
90
....*....|....*....
gi 1786808614 175 EQPNGIIGSILDINERKVA 193
Cdd:PRK09776 383 GTPLYFIAQIEDINELKRT 401
|
|
| HisKA |
pfam00512 |
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine ... |
1625-1685 |
1.83e-04 |
|
His Kinase A (phospho-acceptor) domain; dimerization and phospho-acceptor domain of histidine kinases.
Pssm-ID: 459839 [Multi-domain] Cd Length: 66 Bit Score: 41.43 E-value: 1.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1625 AVSTLAGGMAHELNNVLAPVLMAAQLLRK-QVSGKSRTLVDSVESSAQRGADIVKQVLTFAR 1685
Cdd:pfam00512 1 AKSEFLANLSHELRTPLTAIRGYLELLRDeKLDEEQREYLETILRSAERLLRLINDLLDLSR 62
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
586-1425 |
1.89e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 586 ERTEAARQQIETTaldlrsnsEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEE 665
Cdd:TIGR02169 170 RKKEKALEELEEV--------EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 666 ATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVEttaqqsrtvaeqaaaeaqq 745
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE------------------- 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 746 qlaalrqqlqaeterREQAESALGQSKSETERQLAEATAALAEVRAQLEQATtassqreaeakqaaaaqqqKLADQDAEL 825
Cdd:TIGR02169 303 ---------------IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE-------------------ELEREIEEE 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 826 KKTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQqlaaLAEARSQAEREAAERRQTEESLLQASRSSEERVAL 905
Cdd:TIGR02169 349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD----YREKLEKLKREINELKRELDRLQEELQRLSEELAD 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 906 LASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAG-LRARMDFEAAERERVEAAWKLANSATEQHAAEl 984
Cdd:TIGR02169 425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElYDLKEEYDRVEKELSKLQRELAEAEAQARASE- 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 985 ktllATAREELHAETAKRDAAEAAASQVrAELEATNAESSRAL-AAAQNELARESAERETTEAEFQRSKSALAQQLAEAA 1063
Cdd:TIGR02169 504 ----ERVRGGRAVEEVLKASIQGVHGTV-AQLGSVGERYATAIeVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1064 AAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAET-G 1142
Cdd:TIGR02169 579 PLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTgG 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1143 AREQLEKNLRQAAEEAtrKAQALQAELQrakkELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASAdQRLAER 1222
Cdd:TIGR02169 659 SRAPRGGILFSRSEPA--ELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQE 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1223 LSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQ-ERDERRRVVESLTQTSTTLEARATESG 1301
Cdd:TIGR02169 732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1302 SALEVTRRLLNEERAARASALAELAARRAEVdRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATD 1381
Cdd:TIGR02169 812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1786808614 1382 FEAANAALRgEMEKRLRlELTWqmQREDFDRRLGELTTALRTAE 1425
Cdd:TIGR02169 891 RDELEAQLR-ELERKIE-ELEA--QIEKKRKRLSELKAKLEALE 930
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1074-1579 |
1.90e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 46.78 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1074 EKETAARHETERELRESLTDAERTTEALQADLDA-ALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLR 1152
Cdd:COG3899 738 DPEEEYRLALLLELAEALYLAGRFEEAEALLERAlAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELAL 817
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1153 QAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQER 1232
Cdd:COG3899 818 ALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLL 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1233 LRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLN 1312
Cdd:COG3899 898 AAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1313 EERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGE 1392
Cdd:COG3899 978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1393 MEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDA 1472
Cdd:COG3899 1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1473 AGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLT 1552
Cdd:COG3899 1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217
|
490 500
....*....|....*....|....*..
gi 1786808614 1553 RLTTDVEAARQQAEQETTQRRSLEDAL 1579
Cdd:COG3899 1218 EAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| PRK10529 |
PRK10529 |
DNA-binding transcriptional activator KdpE; Provisional |
1875-1997 |
2.18e-04 |
|
DNA-binding transcriptional activator KdpE; Provisional
Pssm-ID: 182522 [Multi-domain] Cd Length: 225 Bit Score: 44.80 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAtLPIIVASG 1954
Cdd:PRK10529 4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDL--IILDLGLPDGDGIEFIRDLRQWSA-IPVIVLSA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHREESAA 1997
Cdd:PRK10529 81 RSEESDKIAALDAGADDYLSKPFGIGELQARLRVALRRHSATP 123
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
232-407 |
2.45e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 232 ELKKRDSELESANRQlwaelsgREQVEAELAKARGELdKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEKAELEKR- 310
Cdd:COG1579 11 DLQELDSELDRLEHR-------LKELPAELAELEDEL-AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 311 -TASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQssatqpdTALETVHHRLHAETERVKRLETELESLRVALQ 389
Cdd:COG1579 83 gNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELE-------EELAELEAELAELEAELEEKKAELDEELAELE 155
|
170 180
....*....|....*....|
gi 1786808614 390 TEHEK--AERADAERELSEE 407
Cdd:COG1579 156 AELEEleAEREELAAKIPPE 175
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
527-1157 |
2.72e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 527 ARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSN- 605
Cdd:pfam15921 254 SQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSEl 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 606 ------SEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLA-------EATAALADTRKQLEEATTKAAE 672
Cdd:pfam15921 334 reakrmYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkrekELSLEKEQNKRLWDRDTGNSIT 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 673 LQPVREQLAGEVQRGERAEAELFRSRSE----LETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQqla 748
Cdd:pfam15921 414 IDHLRRELDDRNMEVQRLEALLKAMKSEcqgqMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMT--- 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 749 alrqqlqaeTERREQAESALGQSKSETERQLAEATAALAEVRAQ--LEQATTASSQREAEAKQAAAAQQQKLADQDAELK 826
Cdd:pfam15921 491 ---------LESSERTVSDLTASLQEKERAIEATNAEITKLRSRvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKD 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 827 KTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEEsllQASRSSEERVALL 906
Cdd:pfam15921 562 KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA---RVSDLELEKVKLV 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 907 ASELEAAReALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKT 986
Cdd:pfam15921 639 NAGSERLR-AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 987 LLATAREELHAE-------TAKRDAAEAAASQVRAELEA-TNAESSRA-LAAAQNELARE----SAERETTEAEFQRSKS 1053
Cdd:pfam15921 718 MEGSDGHAMKVAmgmqkqiTAKRGQIDALQSKIQFLEEAmTNANKEKHfLKEEKNKLSQElstvATEKNKMAGELEVLRS 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1054 ALAQ-QLAEAAAAQAELRSRLE----KETAARHETER---ELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEET 1125
Cdd:pfam15921 798 QERRlKEKVANMEVALDKASLQfaecQDIIQRQEQESvrlKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVP 877
|
650 660 670
....*....|....*....|....*....|...
gi 1786808614 1126 ARQSHTEF-THRLTAETGAREQLEKNLRQAAEE 1157
Cdd:pfam15921 878 SSQSTASFlSHHSRKTNALKEDPTRDLKQLLQE 910
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1144-1296 |
2.73e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 45.39 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1144 REQLEKNLRQAAEEATrkaqalqAELQRAKKELEKELADANLELLDIRSRLD---HEAAARRQAEESAKQGSASADQRLA 1220
Cdd:smart00787 138 RMKLLEGLKEGLDENL-------EGLKEDYKLLMKELELLNSIKPKLRDRKDaleEELRQLKQLEDELEDCDPTELDRAK 210
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1786808614 1221 ERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEAR 1296
Cdd:smart00787 211 EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSL 286
|
|
| PRK10161 |
PRK10161 |
phosphate response regulator transcription factor PhoB; |
1875-1998 |
2.76e-04 |
|
phosphate response regulator transcription factor PhoB;
Pssm-ID: 182277 [Multi-domain] Cd Length: 229 Bit Score: 44.71 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIVA 1952
Cdd:PRK10161 5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDL--ILLDWMLPGGSGIQFIKHLKRESMTrdIPVVML 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1786808614 1953 SGMGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHREESAAV 1998
Cdd:PRK10161 83 TARGEEEDRVRGLETGADDYITKPFSPKELVARIKAVMRRISPMAV 128
|
|
| REC_RegA-like |
cd17563 |
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; ... |
1875-1986 |
3.18e-04 |
|
phosphoacceptor receiver (REC) domain of photosynthetic apparatus regulatory protein RegA; Rhodobacter sphaeroides RegA, also called response regulator PrrA, is the DNA binding regulatory protein of a redox-responsive two-component regulatory system RegB/RegA that is involved in transactivating anaerobic expression of the photosynthetic apparatus. It contains a REC domain and a DNA-binding helix-turn-helix output domain. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.
Pssm-ID: 381111 [Multi-domain] Cd Length: 112 Bit Score: 42.04 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17563 3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPD--YAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTG 80
|
90 100 110
....*....|....*....|....*....|..
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSL 1986
Cdd:cd17563 81 YASIATAVEAIKLGADDYLAKPADADEILAAL 112
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1145-1573 |
3.23e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.53 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1145 EQLEKNLRQAAEEATRKAQalqaeLQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQgsasadQRLAERLS 1224
Cdd:COG4717 74 KELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL------EALEAELA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1225 EVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQErderrrvVESLTQTSTTLEARATESGSAL 1304
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-------LQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1305 EVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEA 1384
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1385 ANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAH-AELTRRLTERDSELASV 1463
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEeLEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1464 REQAAALDAAGTRAQQTTAELQTNLNAARAEL-DMLNRQFAQRVAELDS-TEARLREECAHRERAEAELDRMRDAQdgfQ 1541
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEEL---R 452
|
410 420 430
....*....|....*....|....*....|..
gi 1786808614 1542 QSTAELNERLTRLTTDVEAARQQAEQETTQRR 1573
Cdd:COG4717 453 EELAELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
988-1628 |
3.43e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.81 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 988 LATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQA 1067
Cdd:TIGR00606 398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1068 ELRSRLEKETAARHETEreLRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAEtgarEQL 1147
Cdd:TIGR00606 478 QELRKAERELSKAEKNS--LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD----EQI 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1148 EKNLRQAAEEATRKAQALQAelqraKKELEKELADANLELLDIRSRLdheaAARRQAEESAKQGSASADQRLAERLSEVQ 1227
Cdd:TIGR00606 552 RKIKSRHSDELTSLLGYFPN-----KKQLEDWLHSKSKEINQTRDRL----AKLNKELASLEQNKNHINNELESKEEQLS 622
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1228 TLQERLrSEAAQRETTEVELRDTRAALEK---QLAEASAALREASARLEQERDERR-------RVVES---LTQTSTTLE 1294
Cdd:TIGR00606 623 SYEDKL-FDVCGSQDEESDLERLKEEIEKsskQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTeaeLQEFISDLQ 701
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1295 ARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQP------HAIEEATARLKAQLAEQEREREQLRLAA 1368
Cdd:TIGR00606 702 SKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPelrnklQKVNRDIQRLKNDIEEQETLLGTIMPEE 781
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1369 MSAE---------QRLRDRATDFEAANAALRGEMEKrLRLELTWQMQREDFDRRLGELTTALRTAE-------------- 1425
Cdd:TIGR00606 782 ESAKvcltdvtimERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVNQEKQEKQHELDTVVSKIElnrkliqdqqeqiq 860
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1426 ---AKAGSDSAELRHAHETLQQAHA------ELTRRLTERDSELASVREQAAALDAAGTRAQQTTAEL-----------Q 1485
Cdd:TIGR00606 861 hlkSKTNELKSEKLQIGTNLQRRQQfeeqlvELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELissketsnkkaQ 940
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1486 TNLNAARAELDML---------------NRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNER 1550
Cdd:TIGR00606 941 DKVNDIKEKVKNIhgymkdienkiqdgkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDN 1020
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1551 LTRLT-----TDVEAARQQAEQETTQRRSLEDALQQSHGEVELR--------VSERTAGLNAHVQQLEAELAEAQ--RAE 1615
Cdd:TIGR00606 1021 LTLRKrenelKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDlikrnhvlALGRQKGYEKEIKHFKKELREPQfrDAE 1100
|
730
....*....|...
gi 1786808614 1616 EQLRHRRIEAVST 1628
Cdd:TIGR00606 1101 EKYREMMIVMRTT 1113
|
|
| PRK10365 |
PRK10365 |
sigma-54-dependent response regulator transcription factor ZraR; |
1867-1997 |
3.88e-04 |
|
sigma-54-dependent response regulator transcription factor ZraR;
Pssm-ID: 182412 [Multi-domain] Cd Length: 441 Bit Score: 45.02 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1867 LPRGNGELLMLADDEQGVLDVTAEILEWhGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT 1946
Cdd:PRK10365 1 MTHDNIDILVVDDDISHCTILQALLRGW-GYNVALANSGRQALEQVREQVFDL--VLCDVRMAEMDGIATLKEIKALNPA 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1947 LPIIVASGMGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAEL-HREESAA 1997
Cdd:PRK10365 78 IPVLIMTAYSSVETAVEALKTGALDYLIKPLDFDNLQATLEKALaHTHSIDA 129
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1263-1652 |
4.37e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.39 E-value: 4.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1263 AALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRltteqphA 1342
Cdd:COG3903 549 AALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAA-------A 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1343 IEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALR 1422
Cdd:COG3903 622 ALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAA 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1423 TAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQF 1502
Cdd:COG3903 702 ALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAA 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1503 AQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQS 1582
Cdd:COG3903 782 AAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAA 861
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1583 HGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEQLRHRRIEAVSTLAGGMAHELNNVLAPVLMAAQLLR 1652
Cdd:COG3903 862 AAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1071-1621 |
4.42e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 45.51 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1071 SRLEKETAARHETERELRESLTDAERTTEALQADLDAALKAceeEAARRSQAE---------ETARQSHTEFTHRLTAET 1141
Cdd:pfam07111 69 SRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVA---EKAGQAEAEglraalagaEMVRKNLEEGSQRELEEI 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1142 GAREQLE-KNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELldirsrldheAAARRQAEESAKQGSasadqRLA 1220
Cdd:pfam07111 146 QRLHQEQlSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQL----------AEAQKEAELLRKQLS-----KTQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1221 ERLSEVQTLQERLRSEAAQRETTEVElRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATES 1300
Cdd:pfam07111 211 EELEAQVTLVESLRKYVGEQVPPEVH-SQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1301 GSALEVtrrLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQerereQLRLAAMSAEQRLRDRAT 1380
Cdd:pfam07111 290 IQPSDS---LEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL-----QEQVTSQSQEQAILQRAL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1381 DFEAANAALRGEMEKRLRLELT--------WQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELT-- 1450
Cdd:pfam07111 362 QDKAAEVEVERMSAKGLQMELSraqearrrQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSya 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1451 -------RRLTERDSELASVREQAAALDAAgtrAQQTTAELQTNLNAARAELDMLNrqfaqrvAELDSTEARLREECAH- 1522
Cdd:pfam07111 442 vrkvhtiKGLMARKVALAQLRQESCPPPPP---APPVDADLSLELEQLREERNRLD-------AELQLSAHLIQQEVGRa 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1523 RERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLE-----------DALQQSHGEVELRVS 1591
Cdd:pfam07111 512 REQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRqeltqqqeiygQALQEKVAEVETRLR 591
|
570 580 590
....*....|....*....|....*....|
gi 1786808614 1592 ERTAGLNAHVQQLEAELAEAQRAEEQLRHR 1621
Cdd:pfam07111 592 EQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
|
|
| PRK13729 |
PRK13729 |
conjugal transfer pilus assembly protein TraB; Provisional |
1471-1519 |
4.50e-04 |
|
conjugal transfer pilus assembly protein TraB; Provisional
Pssm-ID: 184281 [Multi-domain] Cd Length: 475 Bit Score: 45.20 E-value: 4.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1471 DAAGTRAQQTTAELQTNLNAARAELDMLNRQ---FAQRVAELDSTEARLREE 1519
Cdd:PRK13729 68 QHATTEMQVTAAQMQKQYEEIRRELDVLNKQrgdDQRRIEKLGQDNAALAEQ 119
|
|
| HisKA |
smart00388 |
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine ... |
1625-1685 |
4.53e-04 |
|
His Kinase A (phosphoacceptor) domain; Dimerisation and phosphoacceptor domain of histidine kinases.
Pssm-ID: 214644 [Multi-domain] Cd Length: 66 Bit Score: 40.24 E-value: 4.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1625 AVSTLAGGMAHELNNVLAPVLMAAQLLRKQ-VSGKSRTLVDSVESSAQRGADIVKQVLTFAR 1685
Cdd:smart00388 1 AKREFLANLSHELRTPLTAIRGYLELLLDTeLSEEQREYLETILREAERLLRLINDLLDLSR 62
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1011-1195 |
4.99e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 44.34 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1011 QVRAELEATNAESsrALAAAQNELARESAERETTEAEFQRsksalaqqlaeaAAAQAELRSRLEKETAARHETERELRES 1090
Cdd:pfam00529 46 DVLFQLDPTDYQA--ALDSAEAQLAKAQAQVARLQAELDR------------LQALESELAISRQDYDGATAQLRAAQAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1091 LTDAERTTEALQADLdAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEE--ATRKAQALQAE 1168
Cdd:pfam00529 112 VKAAQAQLAQAQIDL-ARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAEnqAEVRSELSGAQ 190
|
170 180
....*....|....*....|....*..
gi 1786808614 1169 LQRAKKELEKELADANLELLDIRSRLD 1195
Cdd:pfam00529 191 LQIAEAEAELKLAKLDLERTEIRAPVD 217
|
|
| HATPase_YcbM-like |
cd16947 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1730-1851 |
5.01e-04 |
|
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: 41.73 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1730 ADASQLHRVLLNLAVNA----RDAMPSGGTLKFSAENVVVDesfihhrratgakpgnyvlfrVTDSGVGIPRDILPRIFE 1805
Cdd:cd16947 16 ANTEALQRILKNLISNAikygSDGKFLGMTLREDEKHVYID---------------------IWDKGKGISETEKDHVFE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1806 PFFTTKEPG----QSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYL 1851
Cdd:cd16947 75 RLYTLEDSRnsakQGNGLGLTITKRLAESMGGSIYVNSKPYEKTVFTVTL 124
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
525-705 |
5.17e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 525 EAARAQVEA--DLRAAHQRFEQRVAELETdNQQLREQAsrDTQAATTQRGEQETALAELRAQLERTEAARQQIEttaldl 602
Cdd:COG4913 245 EDAREQIELlePIRELAERYAAARERLAE-LEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLE------ 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 603 rsnseQQLSETQRQLADARQQLQAESerraqaesalGQSKSETERQLAEATAALADTRKQLE-----------EATTKAA 671
Cdd:COG4913 316 -----ARLDALREELDELEAQIRGNG----------GDRLEQLEREIERLERELEERERRRArleallaalglPLPASAE 380
|
170 180 190
....*....|....*....|....*....|....
gi 1786808614 672 ELQPVREQLAGEVQRGERAEAELFRSRSELETQQ 705
Cdd:COG4913 381 EFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1097-1294 |
6.21e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 6.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1097 TTEALQADLDAALKACEEEAarrsqaEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKK-- 1174
Cdd:PRK11281 37 TEADVQAQLDALNKQKLLEA------EDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDdn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1175 --------------ELEKELADANLELLDIRSRL---DHEAAARRQAEESAKQGSASADQRLAE---RLSEVQTLQERLR 1234
Cdd:PRK11281 111 deetretlstlslrQLESRLAQTLDQLQNAQNDLaeyNSQLVSLQTQPERAQAALYANSQRLQQirnLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 1235 SEAAQRETTEVELRDTRAALEKQLAEASAAL-----------REASARLEQERDERRRVVES--LTQTSTTLE 1294
Cdd:PRK11281 191 PSQRVLLQAEQALLNAQNDLQRKSLEGNTQLqdllqkqrdylTARIQRLEHQLQLLQEAINSkrLTLSEKTVQ 263
|
|
| PAS_4 |
pfam08448 |
PAS fold; The PAS fold corresponds to the structural domain that has previously been defined ... |
84-191 |
6.27e-04 |
|
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: 41.25 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 84 AAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEK-EFRLDFRLRNkdGSTRW 162
Cdd:pfam08448 3 SLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEpIDFLEELLLN--GEERH 80
|
90 100
....*....|....*....|....*....
gi 1786808614 163 VAGHAMRVLDDHEQPNGIIGSILDINERK 191
Cdd:pfam08448 81 YELRLTPLRDPDGEVIGVLVISRDITERR 109
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
839-1311 |
7.07e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 44.85 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 839 REALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQtEESLLQASRSSEERVALLASELEAAREALR 918
Cdd:COG3899 769 ERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELAL-ALAERLGDRRLEARALFNLGFILHWLGPLR 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 919 SESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAE 998
Cdd:COG3899 848 EALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAA 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 999 TAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETA 1078
Cdd:COG3899 928 AAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAA 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1079 ARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEA 1158
Cdd:COG3899 1008 AAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAA 1087
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1159 TRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAA 1238
Cdd:COG3899 1088 LAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALA 1167
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 1239 QRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLL 1311
Cdd:COG3899 1168 ALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLAL 1240
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
282-732 |
7.28e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.51 E-value: 7.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 282 IISGLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALrKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALE 361
Cdd:COG5278 70 LLTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARL-DELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 362 TVHHRLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARR 441
Cdd:COG5278 149 ALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 442 TQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRS 521
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 522 EADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALD 601
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 602 LRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLA 681
Cdd:COG5278 389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 682 GEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQS 732
Cdd:COG5278 469 AAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAA 519
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
514-695 |
7.41e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 514 SQAGAGRSEADEAARAQVEADLRAAHQRfeqrvaELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLErteaarq 593
Cdd:PRK11281 24 SAFARAASNGDLPTEADVQAQLDALNKQ------KLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLA------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 594 qiettaldlrsNSEQQLSETQRQLADARQQLQAESERRAQAesalgQSKSETERQLAEATAALADTRKQLEEATTKAAEL 673
Cdd:PRK11281 91 -----------QAPAKLRQAQAELEALKDDNDEETRETLST-----LSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL 154
|
170 180
....*....|....*....|..
gi 1786808614 674 QpvreqlagevQRGERAEAELF 695
Cdd:PRK11281 155 Q----------TQPERAQAALY 166
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1197-1513 |
7.41e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.90 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1197 EAAARRQAEESAKQGSASADQRLAerlseVQTLQERLRSeAAQRETTEVELrdtrAALEKQLAEASAALREASARLEQER 1276
Cdd:PRK11281 38 EADVQAQLDALNKQKLLEAEDKLV-----QQDLEQTLAL-LDKIDRQKEET----EQLKQQLAQAPAKLRQAQAELEALK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1277 DERRRVV-ESLTQTS-TTLEARATESGSALEVTRRLLNEeraarasalaelaarraevdrltteqphaieeatarLKAQL 1354
Cdd:PRK11281 108 DDNDEETrETLSTLSlRQLESRLAQTLDQLQNAQNDLAE------------------------------------YNSQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1355 AEQER--EREQLRLAAMSAE-QRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALrtaeakagSD 1431
Cdd:PRK11281 152 VSLQTqpERAQAALYANSQRlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQL--------QD 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1432 SAELRHAHETLQQAHAEltrrlterdselasvrEQAAALDAAG-----TRAQQTTAELQTNLNAARAELDML-------N 1499
Cdd:PRK11281 224 LLQKQRDYLTARIQRLE----------------HQLQLLQEAInskrlTLSEKTVQEAQSQDEAARIQANPLvaqeleiN 287
|
330
....*....|....
gi 1786808614 1500 RQFAQRVaeLDSTE 1513
Cdd:PRK11281 288 LQLSQRL--LKATE 299
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
296-480 |
7.75e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 296 AVKTLQAEKAELEKRTASSPAELEALRKRLsDEATRRQLAEDDLRSLREDFDKLQSSATQPDtALETVHHRLHAETERVK 375
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELERLDASSDDLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 376 RLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAE-SARRTQAEAGQGGGEVN 454
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGDAVERELR 768
|
170 180
....*....|....*....|....*.
gi 1786808614 455 PELAARIAALTEAKAQVEKELVEQQA 480
Cdd:COG4913 769 ENLEERIDALRARLNRAEEELERAMR 794
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
790-1471 |
8.36e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 790 RAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAE----TKAELD 865
Cdd:COG4913 265 AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 866 QQLAalaearsQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEA 945
Cdd:COG4913 345 REIE-------RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 946 AAEAAGLRARMDFEAAER----ERVEAAWKLANSATEQHAAELK--------------------TLLATAR------EEL 995
Cdd:COG4913 418 RRELRELEAEIASLERRKsnipARLLALRDALAEALGLDEAELPfvgelievrpeeerwrgaieRVLGGFAltllvpPEH 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 996 HAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELAR-----ESAERETTEAEFQRSKSALAQQLAEAAAAQAEL- 1069
Cdd:COG4913 498 YAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGkldfkPHPFRAWLEAELGRRFDYVCVDSPEELRRHPRAi 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1070 -RSRLEKETAARHE--TERELRESL---TDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHtefthrltaetgA 1143
Cdd:COG4913 578 tRAGQVKGNGTRHEkdDRRRIRSRYvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ------------E 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1144 REQLEKNLRQAAEEAtRKAQALQAELQRAKKELEkELADANLELLDIRSRLDhEAAARRQAEESAKQGSASADQRLAERL 1223
Cdd:COG4913 646 RREALQRLAEYSWDE-IDVASAEREIAELEAELE-RLDASSDDLAALEEQLE-ELEAELEELEEELDELKGEIGRLEKEL 722
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1224 SEVQTLQERLRSEAAQRETTEVElrDTRAALEKQLAEASAALREasarleqerderRRVVESLTQTSTTLEARATESGSA 1303
Cdd:COG4913 723 EQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGDAVE------------RELRENLEERIDALRARLNRAEEE 788
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1304 LEVTRRLLNEE-RAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQE-REREQLRLAAMSAEQRLRDRatd 1381
Cdd:COG4913 789 LERAMRAFNREwPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENSiEFVADLLSKLRRAIREIKER--- 865
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1382 FEAANAALRG---EMEKRLRLELTWQMqredfDRRLGELTTALRTAEAKAGSDSAELRHAHEtlqQAHAELTRRLTERDs 1458
Cdd:COG4913 866 IDPLNDSLKRipfGPGRYLRLEARPRP-----DPEVREFRQELRAVTSGASLFDEELSEARF---AALKRLIERLRSEE- 936
|
730
....*....|...
gi 1786808614 1459 ELASVREQAAALD 1471
Cdd:COG4913 937 EESDRRWRARVLD 949
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
380-846 |
8.96e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 44.19 E-value: 8.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 380 ELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPELAA 459
Cdd:COG4995 3 ALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 460 RIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAH 539
Cdd:COG4995 83 AALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 540 QRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLAD 619
Cdd:COG4995 163 AALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 620 ARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRS 699
Cdd:COG4995 243 LAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 700 ELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQL 779
Cdd:COG4995 323 LLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLA 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786808614 780 AEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQL 846
Cdd:COG4995 403 LAAAQLLRLLLAALALLLALAAYAAARLALLALIEYIILPDRLYAFVQLYQLLIAPIEAELPGIKRL 469
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1217-1624 |
9.07e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 9.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1217 QRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAAL---REASARLEQERDERRRVVESLTQTSTTL 1293
Cdd:pfam07888 41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELrqsREKHEELEEKYKELSASSEELSEEKDAL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1294 EARATESgsalevtRRLLNEERAARASALAELAARRAEVDRLTTEQphaieeatARLKAQLAEQEREREQLRLAAMSAEQ 1373
Cdd:pfam07888 121 LAQRAAH-------EARIRELEEDIKTLTQRVLERETELERMKERA--------KKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1374 RLRDRATDFEAANaalrgemekrlrlelTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHEtlqqahaeltrrl 1453
Cdd:pfam07888 186 ELRSLSKEFQELR---------------NSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE------------- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1454 terdsELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELdrm 1533
Cdd:pfam07888 238 -----ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETL--- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1534 rdaqdgfQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLnahvQQLEAELAEAQR 1613
Cdd:pfam07888 310 -------QQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRREL----QELKASLRVAQK 378
|
410
....*....|.
gi 1786808614 1614 AEEQLRHRRIE 1624
Cdd:pfam07888 379 EKEQLQAEKQE 389
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1151-1299 |
9.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.99 E-value: 9.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1151 LRQAAEEATRKAQALQAELQRAKKELEK---ELADANLELLDIRSrlDHEAAARRQAEESAKQGSASADQRLAERLSEVQ 1227
Cdd:COG1579 22 LEHRLKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLEL--EIEEVEARIKKYEEQLGNVRNNKEYEALQKEIE 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1228 TLQERLrseaAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATE 1299
Cdd:COG1579 100 SLKRRI----SDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
522-704 |
9.55e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 9.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 522 EADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREqASRDTQAATTQRGEQETALAELRAQLERTEAARQ---QIETT 598
Cdd:COG4942 44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAELLRALYrlgRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 599 ALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVRE 678
Cdd:COG4942 123 ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202
|
170 180
....*....|....*....|....*.
gi 1786808614 679 QLAGEVQRGERAEAELFRSRSELETQ 704
Cdd:COG4942 203 RLEKELAELAAELAELQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1404-1621 |
9.72e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 9.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1404 QMQREDFDRRLGELTTALRTAEAKAGSDSAELrhahETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAE 1483
Cdd:COG4942 26 EAELEQLQQEIAELEKELAALKKEEKALLKQL----AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1484 LQTNLNAARAELDMLNRQ-------FAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTT 1556
Cdd:COG4942 102 QKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 1557 DVEAARQQAEQETTQRRSLEDALQQSHGEVElrvsERTAGLNAHVQQLEAELAEAQRAEEQLRHR 1621
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELA----AELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK10610 |
PRK10610 |
chemotaxis protein CheY; |
1875-1986 |
1.01e-03 |
|
chemotaxis protein CheY;
Pssm-ID: 170568 [Multi-domain] Cd Length: 129 Bit Score: 41.11 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGY-KVLTARDGQQALSlyDQHAGDIKAVITDILMPFMDGVELCRELRKRD--ATLPIIV 1951
Cdd:PRK10610 8 FLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALN--KLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSALPVLM 85
|
90 100 110
....*....|....*....|....*....|....*
gi 1786808614 1952 ASGMGHEKFVTDLRELGVPLFLKKPFAAEELLRSL 1986
Cdd:PRK10610 86 VTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKL 120
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
300-637 |
1.03e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 44.17 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 300 LQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAE------DDLRSLREDFDKLQSSATQPDTALETVHHRLHAETER 373
Cdd:COG3096 311 MARELEELSARESDLEQDYQAASDHLNLVQTALRQQEkieryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEE 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 374 VKRLETELESLRVALQTEH-------------EKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEEL-VAESA 439
Cdd:COG3096 391 VDSLKSQLADYQQALDVQQtraiqyqqavqalEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLsVADAA 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 440 RRTQAEAGQGGGEVNPELAaRIAALTEAKAQVEkELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAG 519
Cdd:COG3096 471 RRQFEKAYELVCKIAGEVE-RSQAWQTARELLR-RYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQ 548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 520 RSEADEAARAQVEA-----DLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQEtALAELRAQLERTEAARQQ 594
Cdd:COG3096 549 LDAAEELEELLAELeaqleELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQD-ALERLREQSGEALADSQE 627
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1786808614 595 IeTTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESA 637
Cdd:COG3096 628 V-TAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGA 669
|
|
| PRK10766 |
PRK10766 |
two-component system response regulator TorR; |
1896-1969 |
1.06e-03 |
|
two-component system response regulator TorR;
Pssm-ID: 182711 [Multi-domain] Cd Length: 221 Bit Score: 42.72 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1896 GYKVLTARDGQQALSLYDQHagDIKAVITDILMPFMDGVELCRELRKRdATLPIIVASG------------MGHEKFVT- 1962
Cdd:PRK10766 26 GYTVSEAASGAGMREIMQNQ--HVDLILLDINLPGEDGLMLTRELRSR-STVGIILVTGrtdsidrivgleMGADDYVTk 102
|
....*....
gi 1786808614 1963 --DLRELGV 1969
Cdd:PRK10766 103 plELRELLV 111
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1452-1629 |
1.08e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1452 RLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARLreecahrERAEAELD 1531
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-------KKYEEQLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1532 RMRDAQDgFQQSTAELnerltrltTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEA 1611
Cdd:COG1579 84 NVRNNKE-YEALQKEI--------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
|
170
....*....|....*...
gi 1786808614 1612 QRAEEQLRHRRIEAVSTL 1629
Cdd:COG1579 155 EAELEELEAEREELAAKI 172
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1124-1302 |
1.10e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.21 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1124 ETARQSHTEFTHRLTAETGAREQLEKNLRQAA-EEATRKAQALQAELQRAKKE---LEKELADANLELLDIRSRLDHEAA 1199
Cdd:pfam09787 3 ESAKQELADYKQKAARILQSKEKLIASLKEGSgVEGLDSSTALTLELEELRQErdlLREEIQKLRGQIQQLRTELQELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1200 ARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARL------- 1272
Cdd:pfam09787 83 QQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLtsksqss 162
|
170 180 190
....*....|....*....|....*....|...
gi 1786808614 1273 --EQERDER-RRVVESLTQTSTTLEARATESGS 1302
Cdd:pfam09787 163 ssQSELENRlHQLTETLIQKQTMLEALSTEKNS 195
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1172-1610 |
1.12e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 44.34 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1172 AKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTR 1251
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1252 AALEKQLAEASAALREASARLEQER----------DERRRVVESLTQTS----------TTLEARATesGSALEVTRRLL 1311
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSNTQIEQLRkmmlshegvlQEIRSILVDFEEASgkkiyehdsmSTMHFRSL--GSAISKILREL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1312 NEEraaRASALAELAARRAEVDRLTTEQPHAIE----EATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANA 1387
Cdd:pfam15921 230 DTE---ISYLKGRIFPVEDQLEALKSESQNKIElllqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1388 ALRGEMEKRLRleltwqmQREDFDRRLGELTTALRTAEAKAGSDSAELrhaHETLQQAHAELTRRLTERD---SELASVR 1464
Cdd:pfam15921 307 QARNQNSMYMR-------QLSDLESTVSQLRSELREAKRMYEDKIEEL---EKQLVLANSELTEARTERDqfsQESGNLD 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1465 EQAAALDA-AGTRAQQTTAELQTNLN------AARAELDMLNRQFAQRVAELDSTEARLReecAHRERAEAELDRMRDAQ 1537
Cdd:pfam15921 377 DQLQKLLAdLHKREKELSLEKEQNKRlwdrdtGNSITIDHLRRELDDRNMEVQRLEALLK---AMKSECQGQMERQMAAI 453
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 1538 DGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDAlqqshgevELRVSERTAGLNAHVQQLEAELAE 1610
Cdd:pfam15921 454 QGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS--------ERTVSDLTASLQEKERAIEATNAE 518
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
211-704 |
1.30e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.01 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 211 RVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAE---LSGREQVEAELAKARGELDKQVAERTATFTDIISGLE 287
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEknaLQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 288 KAVAEHELAVKTLQAEKAELEKRTASSPAEL---EALRKRLSDEA----TRRQLAEDDLRSLREDFDKLQSSATQPDTAL 360
Cdd:pfam01576 82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLdeeEAARQKLQLEKvtteAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 361 ETVHHRLHAETERVK---RLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELErtkeelvae 437
Cdd:pfam01576 162 SEFTSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA--------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 438 sarrtqaeagqgggEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAG 517
Cdd:pfam01576 233 --------------ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 518 agrsEADEAARAQVE--ADLRAAHQRFE-QRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQ 594
Cdd:pfam01576 299 ----EELEALKTELEdtLDTTAAQQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKAN 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 595 IETTALDLRSNseqqlsetqrqladaRQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQ 674
Cdd:pfam01576 375 LEKAKQALESE---------------NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
490 500 510
....*....|....*....|....*....|
gi 1786808614 675 PVREQLAGEVQRGERAEAELFRSRSELETQ 704
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQ 469
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
311-591 |
1.30e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 44.05 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 311 TASSPAELEALRKRLS-DEATRRQL-----AEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKR--LETELE 382
Cdd:NF012221 1537 TSESSQQADAVSKHAKqDDAAQNALadkerAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRdaILEESR 1616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 383 SLRVALQTeheKAERADAereLSEEAMVQTNTGIQQRLMELNAELERTKEELvaESARRTQAEAgqgggevnpelaaria 462
Cdd:NF012221 1617 AVTKELTT---LAQGLDA---LDSQATYAGESGDQWRNPFAGGLLDRVQEQL--DDAKKISGKQ---------------- 1672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 463 aLTEAKAQVEKELVE-QQAVAKalgdernrlaqelaeaaaaraaleqqlaaaSQAGAGRSEADeaaRAQVEADLRAAHQR 541
Cdd:NF012221 1673 -LADAKQRHVDNQQKvKDAVAK------------------------------SEAGVAQGEQN---QANAEQDIDDAKAD 1718
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 542 FEQRvaELETDNQQLR-EQASRDTQAATT---QRGEQETALAELRAQLERTEAA 591
Cdd:NF012221 1719 AEKR--KDDALAKQNEaQQAESDANAAANdaqSRGEQDASAAENKANQAQADAK 1770
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1152-1485 |
1.39e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1152 RQA-AEEATRKAQALQAELQRAKKELEKEladanlelldirsRLDHEAAARrqaEESAKQgsaSADQRLAERLSEVQTLQ 1230
Cdd:PRK05035 432 RQAkAEIRAIEQEKKKAEEAKARFEARQA-------------RLEREKAAR---EARHKK---AAEARAAKDKDAVAAAL 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1231 ERLRSEAAQRETTEVElrdtrAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEA---RAtesgsalevt 1307
Cdd:PRK05035 493 ARVKAKKAAATQPIVI-----KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiaRA---------- 557
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1308 rrllneeRAARASALAELAARRAEVDrlttEQPHAIEEATARLKAQLAEQerereqlrlAAMSAEQRLRDRATDFEAANA 1387
Cdd:PRK05035 558 -------KAKKAAQQAANAEAEEEVD----PKKAAVAAAIARAKAKKAAQ---------QAASAEPEEQVAEVDPKKAAV 617
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1388 ALRGEMEKRLRLELTWQMQREDF-DRRLGELTTALRTAEAKAgsdsaelrhahetLQQAHAEltrrlterDSELASVREQ 1466
Cdd:PRK05035 618 AAAIARAKAKKAEQQANAEPEEPvDPRKAAVAAAIARAKARK-------------AAQQQAN--------AEPEEAEDPK 676
|
330
....*....|....*....
gi 1786808614 1467 AAALDAAGTRAQQTTAELQ 1485
Cdd:PRK05035 677 KAAVAAAIARAKAKKAAQQ 695
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
540-730 |
1.49e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 540 QRFEQRVAELETDNQQLREQ-----ASRDTQAATTQRGEQETALAELRAQLERTEAARQQIET-------TALDLRSNSE 607
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAqlgsgpdALPELLQSPV 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 608 -----QQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERqlaEATAALADTRKQLEEATTKAAELQPVREQLAG 682
Cdd:COG3206 265 iqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEA 341
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1786808614 683 EVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQ 730
Cdd:COG3206 342 RLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1070-1303 |
1.54e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1070 RSRLEKETAARHETERELRESLTDAERTTEALQADLDAAlkacEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEK 1149
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1150 NLRQAAEEATRKAQALQAELQRAKKELekELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTL 1229
Cdd:COG4942 98 ELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1786808614 1230 QERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSA 1303
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFA 249
|
|
| PRK15479 |
PRK15479 |
transcriptional regulator TctD; |
1875-1994 |
1.79e-03 |
|
transcriptional regulator TctD;
Pssm-ID: 185376 [Multi-domain] Cd Length: 221 Bit Score: 42.02 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYdqHAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK15479 3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLL--QSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1786808614 1955 MGHEKFVTDLRELGVPLFLKKPFAAEELLRSLHAELHREE 1994
Cdd:PRK15479 81 RSAVADRVKGLNVGADDYLPKPFELEELDARLRALLRRSA 120
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
520-928 |
1.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 520 RSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATtqrgEQETALAELRAQLERTEAARQQIETTA 599
Cdd:COG4717 101 EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELEAELAELQ 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 600 LDLRSNSEQQLSETQRQLADARQQLQAESERRAQAesalgqsksetERQLAEATAALADTRKQLEEATTKAAELQPVREQ 679
Cdd:COG4717 177 EELEELLEQLSLATEEELQDLAEELEELQQRLAEL-----------EEELEEAQEELEELEEELEQLENELEAAALEERL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 680 LAGEVQrgeraeAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETE 759
Cdd:COG4717 246 KEARLL------LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 760 RREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQReaEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDR 839
Cdd:COG4717 320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 840 EALEKQLAAARGDLERQLAETKAELDQ-QLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLAS--ELEAAREA 916
Cdd:COG4717 398 QELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQE 477
|
410
....*....|..
gi 1786808614 917 LRSESARREELE 928
Cdd:COG4717 478 LEELKAELRELA 489
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
249-1368 |
1.99e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 43.28 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 249 AELSGREQVE--AELAKARGELDKQVAERTAT----FTDIISGLEKAVAEHEL-AVKTLQAEKAELEKRTASSPAELEAL 321
Cdd:NF041483 111 AEHQARLQAElhTEAVQRRQQLDQELAERRQTveshVNENVAWAEQLRARTESqARRLLDESRAEAEQALAAARAEAERL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 322 ----RKRLSDEA-TRRQLAEDDLRSLREDFDKL----QSSATQPDTALETVHHRLHAETERVKRLETELEslRVALQTEH 392
Cdd:NF041483 191 aeeaRQRLGSEAeSARAEAEAILRRARKDAERLlnaaSTQAQEATDHAEQLRSSTAAESDQARRQAAELS--RAAEQRMQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 393 EKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTqaeaGQGGGEVNPELAARIAALTEAKAQVE 472
Cdd:NF041483 269 EAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLV----GEATKEAEALKAEAEQALADARAEAE 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 473 KELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAAR-AQVEAD-LRA-AHQRFEQRVAEL 549
Cdd:NF041483 345 KLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRReAEAEADrLRGeAADQAEQLKGAA 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 550 ETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEA-----ARQQIETTAldlrSNSEQQLSETQRQLADARQQL 624
Cdd:NF041483 425 KDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGearreAVQQIEEAA----RTAEELLTKAKADADELRSTA 500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 625 QAESER------------RAQAESALGQSKSETERQLAEATAALADTRKQLEEAttkAAELQPVREQlaGEVQRGERAEA 692
Cdd:NF041483 501 TAESERvrteaierattlRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERA---ARELREETER--AIAARQAEAAE 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 693 ELFRSRSELEtqqaalaelraraeaaeaarlqvettaqqsrtvaeqaaaeaqqqlaalrqqlqaetERREQAESALGQSK 772
Cdd:NF041483 576 ELTRLHTEAE--------------------------------------------------------ERLTAAEEALADAR 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 773 SETERQLAEATAALAEVRAQL-EQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLikETEDREALEKQLAAARG 851
Cdd:NF041483 600 AEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRL--RSEAAAEAERLKSEAQE 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 852 DLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASelEAAREALRSESARREELETAL 931
Cdd:NF041483 678 SADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAR--EQSEELLASARKRVEEAQAEA 755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 932 PKTKTELGQRLAEAAAEAAGLRARM-DFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAET-AKRDAAEAAA 1009
Cdd:NF041483 756 QRLVEEADRRATELVSAAEQTAQQVrDSVAGLQEQAEEEIAGLRSAAEHAAERTRTEAQEEADRVRSDAyAERERASEDA 835
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1010 SQVRAELEAtNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLE-KETAARHETERELR 1088
Cdd:NF041483 836 NRLRREAQE-ETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADaREDANRIRSDAAAQ 914
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1089 ESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAE 1168
Cdd:NF041483 915 ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTE 994
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1169 LQRAKKELEKELADANLELLDIRSRLDHEaaARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELR 1248
Cdd:NF041483 995 AERVKAEAAAEAERLRTEAREEADRTLDE--ARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQA 1072
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1249 DTRAALEKQLAE--ASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEEraARASALAELA 1326
Cdd:NF041483 1073 DTMVGAARKEAEriVAEATVEGNSLVEKARTDADELLVGARRDATAIRERAEELRDRITGEIEELHER--ARRESAEQMK 1150
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|..
gi 1786808614 1327 ARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAA 1368
Cdd:NF041483 1151 SAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAA 1192
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
599-934 |
2.01e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.19 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 599 ALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQ---LAEATAALADTRKQLE--EATTKAAEL 673
Cdd:pfam17380 283 AVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQaaiYAEQERMAMERERELEriRQEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 674 QPVR-EQLAGEVQRGERAEaelfrsRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQ 752
Cdd:pfam17380 363 ERIRqEEIAMEISRMRELE------RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 753 QLQAETERREQAESAlgqSKSETERQlaeatAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNL 832
Cdd:pfam17380 437 VRRLEEERAREMERV---RLEEQERQ-----QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 833 IKETEDREALEKQLAaargdlERQlaetKAELDQQLAALAEARSQAEREAAERRQTEESLLQASrSSEERVALLASELEA 912
Cdd:pfam17380 509 IEEERKRKLLEKEME------ERQ----KAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT-EERSRLEAMEREREM 577
|
330 340
....*....|....*....|..
gi 1786808614 913 AREALRSESARReELETALPKT 934
Cdd:pfam17380 578 MRQIVESEKARA-EYEATTPIT 598
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1130-1382 |
2.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1130 HTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAeLQRAKKELEKELA-DANLELLDIRSRLDHEAaarrQAEESA 1208
Cdd:PRK04863 444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQL-VRKIAGEVSRSEAwDVARELLRRLREQRHLA----EQLQQL 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1209 KQGSASADQRLAErlsevQTLQERLRSEAAQR----ETTEVELRDTRAALEKQLAEASAALREASARLEQERDERrrvvE 1284
Cdd:PRK04863 519 RMRLSELEQRLRQ-----QQRAERLLAEFCKRlgknLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQL----E 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1285 SLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLtteqpHAIEEATARLKAQLAEQEREREQL 1364
Cdd:PRK04863 590 QLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERE-----RELTVERDELAARKQALDEEIERL 664
|
250
....*....|....*...
gi 1786808614 1365 RLAAMSAEQRLRDRATDF 1382
Cdd:PRK04863 665 SQPGGSEDPRLNALAERF 682
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
818-1567 |
2.19e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.40 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 818 LADQDAELKKTWDNLIKETEDREALEKQLAAARGDLER-----QLAETKAELDQQLAALAEARSQAEREAAERRQTEESL 892
Cdd:COG3096 301 LAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvqtalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEA 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 893 LQASRSSEERVALLASELEAAREALRSESAR----REELEtALPKTKTELGQRLAEAAAEAAGLRARMDFE-AAERERVE 967
Cdd:COG3096 381 EARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyQQAVQ-ALEKARALCGLPDLTPENAEDYLAAFRAKEqQATEEVLE 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 968 AAWKL--ANSATEQHAAELKTLLATAreelhAETAKRDAAEAAASQVRAeleatnAESSRALAAAQNELARESAERETTE 1045
Cdd:COG3096 460 LEQKLsvADAARRQFEKAYELVCKIA-----GEVERSQAWQTARELLRR------YRSQQALAQRLQQLRAQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1046 AEFQRSKsalaqqlaeaaaaqaelrsRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEET 1125
Cdd:COG3096 529 RQQQNAE-------------------RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1126 ARQSHTEFTHRLTAETGAREQLEKnLRQAAEEATRKAQALQAELQRAkkeLEKELAdanlelldiRSRLDHEAAARRQAE 1205
Cdd:COG3096 590 LRARIKELAARAPAWLAAQDALER-LREQSGEALADSQEVTAAMQQL---LERERE---------ATVERDELAARKQAL 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1206 ESA----KQGSASADQRL---AER-----LSEV----------------------------QTLQERLRS---------- 1235
Cdd:COG3096 657 ESQierlSQPGGAEDPRLlalAERlggvlLSEIyddvtledapyfsalygparhaivvpdlSAVKEQLAGledcpedlyl 736
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1236 --------EAAQRETTEVELRDT--------------------RAALEKQLAEASAALREASARLEQERDERR---RVVE 1284
Cdd:COG3096 737 iegdpdsfDDSVFDAEELEDAVVvklsdrqwrysrfpevplfgRAAREKRLEELRAERDELAEQYAKASFDVQklqRLHQ 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1285 SLTQTSTTLEARATESGSALEVT---------RRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLA 1355
Cdd:COG3096 817 AFSQFVGGHLAVAFAPDPEAELAalrqrrselERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLE 896
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1356 EQEREREQLrLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQM---QREDFDRRLGELTTALRTAEAKAGSDS 1432
Cdd:COG3096 897 ELREELDAA-QEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQakeQQRRLKQQIFALSEVVQRRPHFSYEDA 975
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1433 AELRHAHETLQQAhaeLTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQ-RVAELDS 1511
Cdd:COG3096 976 VGLLGENSDLNEK---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElGVQADAE 1052
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 1512 TEARLREEcahRERAEAELDRMR------DAQDGFQQS-TAELNERLTRLTTDVEAARQQAEQ 1567
Cdd:COG3096 1053 AEERARIR---RDELHEELSQNRsrrsqlEKQLTRCEAeMDSLQKRLRKAERDYKQEREQVVQ 1112
|
|
| HATPase_YpdA-YehU-LytS-like |
cd16924 |
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to ... |
1763-1852 |
2.30e-03 |
|
Histidine kinase-like ATPase domain of two-component sensor histidine kinases similar to Escherichia coli YpdA, YehU, Bacillus subtilis LytS, and some hybrid sensor histidine kinases; 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. It also includes the HATPase domains of Escherichia coli YpdA and YehU, HKs of YpdA-YpdB and YehU-YehTCSs, which are involved together in a nutrient sensing regulatory network. Proteins having this HATPase domain also contain a histidine kinase domain (His-kinase), some having accessory sensor domain(s) such as Cache, HAMP or GAF; some are hybrid sensor histidine kinases as they also contain a REC signal receiver domain.
Pssm-ID: 340401 [Multi-domain] Cd Length: 103 Bit Score: 39.35 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1763 VVVDESFIH---HRRATG------AKPGNYVLFRVTDSGVGIPRDILPRIfepfftTKEPGQSVGLGLatalgvVQSHGG 1833
Cdd:cd16924 8 PLVENAIQHglsPLTDKGvvtisaLKEDNHVMIEVEDNGRGIDPKVLNIL------GKKPKEGNGIGL------YNVHQR 75
|
90 100
....*....|....*....|....*...
gi 1786808614 1834 FILL---------ETEEDKGTEFQIYLP 1852
Cdd:cd16924 76 LILLfgedygihiASEPDKGTRITFTIP 103
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-778 |
2.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 225 ELERRADELKKRDSELESANRQLwaeLSGREQVEA---------ELAKARGELDKQVAERTATFTDI----ISGLEKAVA 291
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEAL---EDAREQIELlepirelaeRYAAARERLAELEYLRAALRLWFaqrrLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 292 EHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRR-QLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAE 370
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 371 TERVKRLETELESLRVALQTEHEKAERADAERElseeamvqtntgiqQRLMELNAELERTKEELvaesarrtqAEAGQGG 450
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEALEEALAEAE--------------AALRDLRRELRELEAEI---------ASLERRK 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 451 GEVNPELAARIAALTEAKAQVEK------ELVE--------QQAVAKALG---------DERNRLAQELAEAAAARAALE 507
Cdd:COG4913 436 SNIPARLLALRDALAEALGLDEAelpfvgELIEvrpeeerwRGAIERVLGgfaltllvpPEHYAAALRWVNRLHLRGRLV 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 508 QQLAAASQAGAGRSEADEAARA-QVEADLRAAHQRFEQRVAELE-----TDNQQLREQASRDTQAATT-------QRGEQ 574
Cdd:COG4913 516 YERVRTGLPDPERPRLDPDSLAgKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRHPRAITRAGQVkgngtrhEKDDR 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 575 ETALAEL------RAQLERTEAARQQIEttaldlrsnseQQLSETQRQLADARQQLQAESERRAQAESALGQSksETERQ 648
Cdd:COG4913 596 RRIRSRYvlgfdnRAKLAALEAELAELE-----------EELAEAEERLEALEAELDALQERREALQRLAEYS--WDEID 662
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 649 LAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETT 728
Cdd:COG4913 663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1786808614 729 AQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQ 778
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERA 792
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
824-1296 |
2.76e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.79 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 824 ELKKTWDNLIKETEDREALEKQLAAARGDLERQLA-------ETKAELDQQLAALAEARSQAEREAAERRQTEESLLQAS 896
Cdd:pfam05483 286 ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 897 RSSEERVALLASELEAAREALRSESARREEL-------ETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVeaa 969
Cdd:pfam05483 366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMtkfknnkEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELI--- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 970 WKLANSATEQHAAELKTLLATAREELHAETAKrdaaeaaasQVRAELEATNAESSRaLAAAQNELARESAE--RETTEAE 1047
Cdd:pfam05483 443 FLLQAREKEIHDLEIQLTAIKTSEEHYLKEVE---------DLKTELEKEKLKNIE-LTAHCDKLLLENKEltQEASDMT 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1048 FQRSKSALAQQLAEAAAAqaelrsRLEKETAARHETERELRESLtdaERTTEALQADLDaalkaceEEAARRSQAEETAR 1127
Cdd:pfam05483 513 LELKKHQEDIINCKKQEE------RMLKQIENLEEKEMNLRDEL---ESVREEFIQKGD-------EVKCKLDKSEENAR 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1128 QSHTEFTHRlTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKE-----------------LEKELADANLELLDI 1190
Cdd:pfam05483 577 SIEYEVLKK-EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKgsaenkqlnayeikvnkLELELASAKQKFEEI 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1191 RSRLDHEAAARRQAEES----AKQGSASADQ----------RLAERLSEVQTLQERLR-----------SEAAQRETTEV 1245
Cdd:pfam05483 656 IDNYQKEIEDKKISEEKlleeVEKAKAIADEavklqkeidkRCQHKIAEMVALMEKHKhqydkiieerdSELGLYKNKEQ 735
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 1246 ELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEAR 1296
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENTAILKDK 786
|
|
| PRK13560 |
PRK13560 |
hypothetical protein; Provisional |
125-195 |
2.92e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 106506 [Multi-domain] Cd Length: 807 Bit Score: 42.74 E-value: 2.92e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 125 VHPDDNKRVTEEWRKCV-RGEKEFRLDFRLRNKDGSTRWVAGHAMRVLDDHEQPNGIIGSILDINERKVADD 195
Cdd:PRK13560 525 IHPADLEQVAAEVAEFAaQGVDRFEQEYRILGKGGAVCWIDDQSAAERDEEGQISHFEGIVIDISERKHAEE 596
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1150-1294 |
2.98e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1150 NLRQAAEEATRKAQALQAELQRAKKELEKELADANlelldirsrlDHEAAARRQAEESAKQGSASADQRLAERLSEVQTL 1229
Cdd:PRK00409 527 ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ----------EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786808614 1230 QERLRSEAAQRETTEVelrdtRAALEKQLAEASAALREASARLE--QERDERRrvVESLTQTSTTLE 1294
Cdd:PRK00409 597 QKGGYASVKAHELIEA-----RKRLNKANEKKEKKKKKQKEKQEelKVGDEVK--YLSLGQKGEVLS 656
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
525-690 |
3.01e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 525 EAARAQVEADlraaHQRFEQRVAELETdnqqlreqasrdtqaattQRGEQETALAELRAQLERTEAARQQIETTALDLRS 604
Cdd:PRK00409 505 EEAKKLIGED----KEKLNELIASLEE------------------LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 605 NSEQQLSETQRQLADARQQLQAESER--RAQAESALGQSKSETERQLAEAtaaladtRKQLEEATTKAAELQPVREQLAG 682
Cdd:PRK00409 563 EEDKLLEEAEKEAQQAIKEAKKEADEiiKELRQLQKGGYASVKAHELIEA-------RKRLNKANEKKEKKKKKQKEKQE 635
|
....*...
gi 1786808614 683 EVQRGERA 690
Cdd:PRK00409 636 ELKVGDEV 643
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
227-406 |
3.16e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 42.31 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 227 ERRADELKKRDSELESAnRQLWAELsgrEQVEAELAkargELDKQVAERTATFTDIISGLEKAVAEHElavkTLQAEKAE 306
Cdd:PHA02562 213 ENIARKQNKYDELVEEA-KTIKAEI---EELTDELL----NLVMDIEDPSAALNKLNTAAAKIKSKIE----QFQKVIKM 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 307 LEKRT---------ASSPAELEALRKRLSDEATRRQLAEDDLRSLRE---DFDKLQSSATQPDTALETVHHRLHAETERV 374
Cdd:PHA02562 281 YEKGGvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKA 360
|
170 180 190
....*....|....*....|....*....|..
gi 1786808614 375 KRLETELESLrvalqteheKAERADAERELSE 406
Cdd:PHA02562 361 KKVKAAIEEL---------QAEFVDNAEELAK 383
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
579-1293 |
3.28e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 579 AELRAQLERTEAARQqiettaLDLRSNSEQQLSETQRQLADARQQLQAE-SERRAQAESALGQSKSETERQLAEATAALA 657
Cdd:TIGR00618 166 KELLMNLFPLDQYTQ------LALMEFAKKKSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 658 DTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELfrsrSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAE 737
Cdd:TIGR00618 240 QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQE----AVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 738 QAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTassqrEAEAKQAAAAQQQK 817
Cdd:TIGR00618 316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT-----LTQHIHTLQQQKTT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 818 LADQDAELKKtwdnlIKETEDREALEKQ-LAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQAS 896
Cdd:TIGR00618 391 LTQKLQSLCK-----ELDILQREQATIDtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESA 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 897 RSSEERVallasELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAwklansa 976
Cdd:TIGR00618 466 QSLKERE-----QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG------- 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 977 tEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALA 1056
Cdd:TIGR00618 534 -EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1057 QQLAEAAAAQAELrSRLEKETAARHETERELRESLTDAERTTEALQADLD---AALKACEEEAARRSQAEETARQSHTEF 1133
Cdd:TIGR00618 613 EQHALLRKLQPEQ-DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRehaLSIRVLPKELLASRQLALQKMQSEKEQ 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1134 THRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSA 1213
Cdd:TIGR00618 692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1214 SADQRLAERLSEVQTLQERLRseaaQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTL 1293
Cdd:TIGR00618 772 AALQTGAELSHLAAEIQFFNR----LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
796-1023 |
3.44e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 796 ATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLeRQLAETKAELDQQLAALAEAR 875
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 876 SQAEREAAERRQTEESLLQAS--RSSEERVALLAS-----ELEAAREALRSESARREELETALPKTKTELGQRLAEAAAE 948
Cdd:COG4942 93 AELRAELEAQKEELAELLRALyrLGRQPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1786808614 949 AAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAES 1023
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1094-1618 |
3.72e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1094 AERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAK 1173
Cdd:TIGR00618 194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1174 KEL-EKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRA 1252
Cdd:TIGR00618 274 AQEaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1253 ALEKQLAEASAALREAsaRLEQERDERRRVvESLTQTSTTLEARATESGSALEVtrrlLNEERAARASALAELAARRAEV 1332
Cdd:TIGR00618 354 EIHIRDAHEVATSIRE--ISCQQHTLTQHI-HTLQQQKTTLTQKLQSLCKELDI----LQREQATIDTRTSAFRDLQGQL 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1333 DRLTTEQphAIEEATARLKAQLAEQEREREQLRLAAMSaEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDR 1412
Cdd:TIGR00618 427 AHAKKQQ--ELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1413 RLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAAR 1492
Cdd:TIGR00618 504 CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1493 AELDMLnRQFAQRVaeLDSTEARLREECAHRERAEAELDRMRDAQDGFQQStaelnerltrlTTDVEAARQQAEQETTQR 1572
Cdd:TIGR00618 584 EDIPNL-QNITVRL--QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR-----------LHLQQCSQELALKLTALH 649
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1786808614 1573 RSLEDALQQSHGEVELRVSERTAGLnahVQQLEAELAEAQRAEEQL 1618
Cdd:TIGR00618 650 ALQLTLTQERVREHALSIRVLPKEL---LASRQLALQKMQSEKEQL 692
|
|
| YesM |
COG2972 |
Sensor histidine kinase YesM [Signal transduction mechanisms]; |
1781-1852 |
3.80e-03 |
|
Sensor histidine kinase YesM [Signal transduction mechanisms];
Pssm-ID: 442211 [Multi-domain] Cd Length: 445 Bit Score: 41.93 E-value: 3.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1786808614 1781 GNYVLFRVTDSGVGIPRDILPRIFEPFfttKEPGQSVGLGLATalgvVQS-----HGGFILLETE--EDKGTEFQIYLP 1852
Cdd:COG2972 370 GDRLVITVEDNGVGMPEEKLEKLLEEL---SSKGEGRGIGLRN----VRErlklyYGEEYGLEIEsePGEGTTVTIRIP 441
|
|
| psREC_PRR |
cd17582 |
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response ... |
1875-1976 |
3.98e-03 |
|
pseudo receiver domain of pseudo-response regulators; In Arabidopsis, five pseudo-response regulators (PRRs), also called APRRs, comprise a core group of clock components that controls the pace of the central oscillator of the circadian clock, an endogenous time-keeping mechanism that enables organisms to adapt to external daily cycles. The coordinated sequential expression of PRR9 (APRR9), PRR7 (APRR7), PRR5 (APRR5), PRR3 (APRR3), and PRR1 (APRR1) results in circadian waves that may be at the basis of the endogenous circadian clock. PRRs contain an N-terminal pseudo receiver (psREC) domain that resembles the receiver domain of a two-component response regulator, but lacks an aspartate residue that accepts a phosphoryl group from the sensor kinase, and a CCT motif at the C-terminus that contains a putative nuclear localization signal. The psREC domain is involved in protein-protein interactions.
Pssm-ID: 381120 [Multi-domain] Cd Length: 104 Bit Score: 38.92 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIKAVITDILMPFMDGVELCRELRKRDA--TLPIIVA 1952
Cdd:cd17582 1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKIckNIPVIMM 80
|
90 100
....*....|....*....|....
gi 1786808614 1953 SGMGHEKFVTDLRELGVPLFLKKP 1976
Cdd:cd17582 81 SSQDSVGVVFKCLSKGAADYLVKP 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
909-1554 |
4.26e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 909 ELEAAREALRSESARREELEtALPKTKTELgQRLAEAAAEAAGLRARMDFEAAERERVEAawklansatEQHAAELKTLL 988
Cdd:COG4913 236 DLERAHEALEDAREQIELLE-PIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELL---------EAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 989 ATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAE 1068
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1069 LRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQshtefthrltaetgAREQLE 1148
Cdd:COG4913 385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA--------------LRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1149 KNLRQAAEEATRKAQALQ--AELQRAKKELEKELADANLELL----------------DIRSRLDHEAAARRQAEEsakQ 1210
Cdd:COG4913 451 EALGLDEAELPFVGELIEvrPEEERWRGAIERVLGGFALTLLvppehyaaalrwvnrlHLRGRLVYERVRTGLPDP---E 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1211 GSASADQRLAERLS-EVQTLQERLRSEAAQRE-----TTEVELRDTRAALEKQ-LAEASAALREASARLEQERD-----E 1278
Cdd:COG4913 528 RPRLDPDSLAGKLDfKPHPFRAWLEAELGRRFdyvcvDSPEELRRHPRAITRAgQVKGNGTRHEKDDRRRIRSRyvlgfD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1279 RRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDrltteqphaieeaTARLKAQLAEQE 1358
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-------------VASAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1359 REREQLRlAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSD---SAEL 1435
Cdd:COG4913 675 AELERLD-ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElraLLEE 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1436 RHAHETLQQAHAELTRRLTERDSELASVREQAA-----ALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELD 1510
Cdd:COG4913 754 RFAAALGDAVERELRENLEERIDALRARLNRAEeelerAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYE 833
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 1786808614 1511 STEARLREECAHRERAE--AELDR-MRDAQDGFqqstAELNERLTRL 1554
Cdd:COG4913 834 ERFKELLNENSIEFVADllSKLRRaIREIKERI----DPLNDSLKRI 876
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
958-1453 |
4.29e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.15 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 958 FEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARE 1037
Cdd:COG3899 749 LELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRL 828
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1038 SAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAA 1117
Cdd:COG3899 829 EARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAA 908
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1118 RRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHE 1197
Cdd:COG3899 909 AAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAA 988
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1198 AAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERD 1277
Cdd:COG3899 989 AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAAL 1068
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1278 ERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQ 1357
Cdd:COG3899 1069 LAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAA 1148
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1358 EREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRH 1437
Cdd:COG3899 1149 LLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLL 1228
|
490
....*....|....*.
gi 1786808614 1438 AHETLQQAHAELTRRL 1453
Cdd:COG3899 1229 AALALAAALLALRLLA 1244
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
870-1319 |
4.74e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.93 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 870 ALAEARSQAEREAAERRQTEESLLQASRSSEErvaLLASELEAAREALRSESAR-REELETALPKTKTELGQRLAEAAAE 948
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAE---LRGPDQLAWLARLDAEHDNlRAALRWALAHGDAELALRLAAALAP 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 949 AAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALA 1028
Cdd:COG3903 554 FWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAA 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1029 AAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAA 1108
Cdd:COG3903 634 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAA 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1109 LKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELL 1188
Cdd:COG3903 714 AAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAA 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1189 DIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREA 1268
Cdd:COG3903 794 AAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAA 873
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 1269 SARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARA 1319
Cdd:COG3903 874 AAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAA 924
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
774-1160 |
4.87e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 42.15 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 774 ETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDL 853
Cdd:COG3899 855 EALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALA 934
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 854 ERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPK 933
Cdd:COG3899 935 AAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAA 1014
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 934 TKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVR 1013
Cdd:COG3899 1015 LAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAA 1094
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1014 AELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTD 1093
Cdd:COG3899 1095 AALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAA 1174
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786808614 1094 AERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATR 1160
Cdd:COG3899 1175 LAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALR 1241
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1435-1564 |
4.95e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 41.37 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1435 LRHAHETLQQAHAeltrRLTERDSELASVREQAAALD--AAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDST 1512
Cdd:COG3524 179 VRFAEEEVERAEE----RLRDAREALLAFRNRNGILDpeATAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQL 254
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1786808614 1513 EARLReecAHRERAEAELDRMRDAQDGfqQSTAELNERLTRLTTDVEAARQQ 1564
Cdd:COG3524 255 RRRIA---ALEKQIAAERARLTGASGG--DSLASLLAEYERLELEREFAEKA 301
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
839-1248 |
5.38e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 41.93 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 839 REALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALR 918
Cdd:COG3903 529 RAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAA 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 919 SESARREELETALpktktELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAE 998
Cdd:COG3903 609 AAAAAAAAAAAAA-----ALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAA 683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 999 TAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETA 1078
Cdd:COG3903 684 AAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAAL 763
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1079 ARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEA 1158
Cdd:COG3903 764 AAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAA 843
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1159 TRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAA 1238
Cdd:COG3903 844 AAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAA 923
|
410
....*....|
gi 1786808614 1239 QRETTEVELR 1248
Cdd:COG3903 924 AAAAAAAAAA 933
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
229-451 |
5.77e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 41.29 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 229 RADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATftdiISGLEKAVAEHELAVKTLQAEKAELE 308
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 309 KRTASSPAELEALRKRL------------------SDEATRRQLAEDDLRSLREDFDKLQSSATQpdtaLETVHHRLHAE 370
Cdd:COG4942 97 AELEAQKEELAELLRALyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE----LAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 371 TERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGG 450
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
.
gi 1786808614 451 G 451
Cdd:COG4942 253 G 253
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
825-1384 |
5.97e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.59 E-value: 5.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 825 LKKTWDNL---IKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQaEREAAERRQTEESLLQASRSSEE 901
Cdd:PRK03918 160 YENAYKNLgevIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE-LPELREELEKLEKEVKELEELKE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 902 RVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEaawklansaTEQHA 981
Cdd:PRK03918 239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE---------YLDEL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 982 AELKTLLATAREELHAetakrdaaeaaasqVRAELEATNAESSRA--LAAAQNELARESAERETTEAEFQRSKSALAQQL 1059
Cdd:PRK03918 310 REIEKRLSRLEEEING--------------IEERIKELEEKEERLeeLKKKLKELEKRLEELEERHELYEEAKAKKEELE 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1060 AEAAAAQAELRSRLEKE----TAARHETERELREsLTDAERTTEALQADLDAALKACEEEAAR-----RSQAEETARQSH 1130
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKEleelEKAKEEIEEEISK-ITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELL 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1131 TEFTHRLTAETGAREQLEKNLRQAAEEATR--KAQALQAELQRAK------KELEKELADANLELLDIRSRlDHEAAARR 1202
Cdd:PRK03918 455 EEYTAELKRIEKELKEIEEKERKLRKELREleKVLKKESELIKLKelaeqlKELEEKLKKYNLEELEKKAE-EYEKLKEK 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1203 QAEESAKQGSASAD-QRLAERLSEVQTLQERLRSEAAQRETTEVELRD----TRAALEKQLAEASAA------LREASAR 1271
Cdd:PRK03918 534 LIKLKGEIKSLKKElEKLEELKKKLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFyneyleLKDAEKE 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1272 LEQERDERRRVVESLTQTSTTL---EARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATA 1348
Cdd:PRK03918 614 LEREEKELKKLEEELDKAFEELaetEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1786808614 1349 R----LKAQLAEQEREREQLRL--AAMSAEQRLRDRATDFEA 1384
Cdd:PRK03918 694 KtlekLKEELEEREKAKKELEKleKALERVEELREKVKKYKA 735
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1014-1621 |
6.08e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 41.86 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1014 AELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAqqlaeaaaaqaelrsrleketaarhETERELRESLTD 1093
Cdd:COG3096 357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA-------------------------DYQQALDVQQTR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1094 AERTTEALQAdLDAALKACEEEAARRSQAEETarqsHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAeLQRAK 1173
Cdd:COG3096 412 AIQYQQAVQA-LEKARALCGLPDLTPENAEDY----LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYEL-VCKIA 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1174 KELEKELA-DANLELLdiRSRLDHEAAARRQAEESAKQGSAsadQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRA 1252
Cdd:COG3096 486 GEVERSQAwQTARELL--RRYRSQQALAQRLQQLRAQLAEL---EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1253 ALEKQLAEASAALREASARLEQERDERrrvvESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEV 1332
Cdd:COG3096 561 ELEAQLEELEEQAAEAVEQRSELRQQL----EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLL 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1333 DRLtteqpHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLR--------------------DRATDFEAANAALR-- 1390
Cdd:COG3096 637 ERE-----REATVERDELAARKQALESQIERLSQPGGAEDPRLLalaerlggvllseiyddvtlEDAPYFSALYGPARha 711
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1391 ------GEMEKRL----------------------------RLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELR 1436
Cdd:COG3096 712 ivvpdlSAVKEQLagledcpedlyliegdpdsfddsvfdaeELEDAVVVKLSDRQWRYSRFPEVPLFGRAAREKRLEELR 791
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1437 HAHETLQQAHAEL------TRRLTERDS-----------------ELASVREQAAALDAAGTRAQQTTAELQTNLNAARA 1493
Cdd:COG3096 792 AERDELAEQYAKAsfdvqkLQRLHQAFSqfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQQLRQQLDQLKE 871
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1494 ELDMLNRQFAQRVAELDSTEARLREECahreraEAELDRMRDAQDGFQQ---STAELNERLTRLTTD------VEAARQQ 1564
Cdd:COG3096 872 QLQLLNKLLPQANLLADETLADRLEEL------REELDAAQEAQAFIQQhgkALAQLEPLVAVLQSDpeqfeqLQADYLQ 945
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 1565 AEQETTQRRSLEDALQQSHGEVELRVSERTAGL----NAHVQQLEAELAEAQRAEEQLRHR 1621
Cdd:COG3096 946 AKEQQRRLKQQIFALSEVVQRRPHFSYEDAVGLlgenSDLNEKLRARLEQAEEARREAREQ 1006
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
1449-1621 |
6.65e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.10 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1449 LTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLnRQFAQRVAELDSTEARLREECAHREraeA 1528
Cdd:PRK09039 44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAA-EAERSRLQALLAELAGAGAAAEGRA---G 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1529 ELDRMRDAQdgfQQSTAELNERLTRLTTDVEAARQQAEqettqrrSLEDALQQShgevelrvSERTAGLNAHVQQLEAEL 1608
Cdd:PRK09039 120 ELAQELDSE---KQVSARALAQVELLNQQIAALRRQLA-------ALEAALDAS--------EKRDRESQAKIADLGRRL 181
|
170
....*....|....*
gi 1786808614 1609 --AEAQRAEEQLRHR 1621
Cdd:PRK09039 182 nvALAQRVQELNRYR 196
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
525-670 |
7.57e-03 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 40.78 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 525 EAARAQVEADLRAAHqrfeqrvAELETDNQQLR-EQASRDTQAATTQRGEQETALAElrAQLERTEAARQQIETTAldlr 603
Cdd:PRK10476 85 ELTVAQAQADLALAD-------AQIMTTQRSVDaERSNAASANEQVERARANAKLAT--RTLERLEPLLAKGYVSA---- 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1786808614 604 snseQQLSETQRQLADARQQLQAESERRAQAESALGQSKSEtERQLAEATAALADTRKQLEEATTKA 670
Cdd:PRK10476 152 ----QQVDQARTAQRDAEVSLNQALLQAQAAAAAVGGVDAL-VAQRAAREAALAIAELHLEDTTVRA 213
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
225-429 |
7.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 225 ELERRADELKKRDSELESANRQL---WAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQ 301
Cdd:COG4913 672 ELEAELERLDASSDDLAALEEQLeelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 302 AEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQP-DTALETVHH--RLHA--ETERVKR 376
Cdd:COG4913 752 EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADlDADLESLPEylALLDrlEEDGLPE 831
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1786808614 377 LETELESLRvalqTEHEKAERADAERELSEEAmvqtnTGIQQRLMELNAELER 429
Cdd:COG4913 832 YEERFKELL----NENSIEFVADLLSKLRRAI-----REIKERIDPLNDSLKR 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
211-711 |
7.76e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 7.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 211 RVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFtDIISGLEKAV 290
Cdd:PRK03918 169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK-EEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 291 AEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRsLREDFDKLQSSATQPDTALETVHHRLHAE 370
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGI 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 371 TERVKRLETELESLRvALQTEHEKAERADAERELSEEAMvqtntgiqQRLMELNAELERTKEELvaesarrtqaeagqgG 450
Cdd:PRK03918 327 EERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELY--------EEAKAKKEELERLKKRL---------------T 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 451 GEVNPELAARIAALTEAKAQVEKELVEqqavakaLGDERNRLAQELAEAAAARAALEQQLAAASQAGAgrsEADEAARAQ 530
Cdd:PRK03918 383 GLTPEKLEKELEELEKAKEEIEEEISK-------ITARIGELKKEIKELKKAIEELKKAKGKCPVCGR---ELTEEHRKE 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 531 VEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRG--EQETALAELRA--------QLERTEAARQQIETTAL 600
Cdd:PRK03918 453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKEleeklkkyNLEELEKKAEEYEKLKE 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 601 DLRSNSEQQ--LSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVRE 678
Cdd:PRK03918 533 KLIKLKGEIksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK 612
|
490 500 510
....*....|....*....|....*....|...
gi 1786808614 679 QLAGEVQRGERAEAELFRSRSELETQQAALAEL 711
Cdd:PRK03918 613 ELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
|
| HATPase_PDK-like |
cd16929 |
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain ... |
1784-1852 |
7.83e-03 |
|
Histidine kinase-like ATPase domain of pyruvate dehydrogenase kinase, branched-chain alpha-ketoacid dehydrogenase kinase and related domains; This family includes the histidine kinase-like ATPase (HATPase) domains of all four PDK isoforms (pyruvate dehydrogenase kinases 1-4) that have been described in mammals, and other PDKs including Saccharomyces Pkp1p and Pkp2p. PDKs and phosphatases tightly regulate the mitochondrial pyruvate dehydrogenase complex (PDC) by reversible phosphorylation. PDC catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA, connecting glycolysis and the TCA acid cycle. Also included in this family is mammalian branched-chain alpha-ketoacid dehydrogenase kinase (BDK), a mitochondrial protein kinase that phosphorylates a subunit of the branched-chain a-ketoacid dehydrogenase (BCKD) complex, which catalyzes the oxidative decarboxylation of branched-chain alpha-ketoacids derived from leucine, isoleucine, and valine, a rate-limiting step in the oxidative degradation of these branched-chain amino acids.
Pssm-ID: 340406 [Multi-domain] Cd Length: 169 Bit Score: 39.25 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1784 VLFRVTDSGVGIPRDILPRIFEPFFTTKEP------------GQSV-----GLGLATALGVVQSHGGFILLETEEDKGTE 1846
Cdd:cd16929 84 LTIKISDRGGGIPREDLARLFSYMYSTAPQpslddfsdlisgTQPSplagfGYGLPMSRLYAEYFGGDLDLQSMEGYGTD 163
|
....*.
gi 1786808614 1847 FQIYLP 1852
Cdd:cd16929 164 VYIYLK 169
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1342-1528 |
8.51e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 8.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1342 AIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTAL 1421
Cdd:COG4942 38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1422 RTAEAKAGSDS------------------------AELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRA 1477
Cdd:COG4942 118 RQPPLALLLSPedfldavrrlqylkylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1786808614 1478 QQTTAELQTNLNAARAELDMLnrqfAQRVAELDSTEARLREECAHRERAEA 1528
Cdd:COG4942 198 QKLLARLEKELAELAAELAEL----QQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK10816 |
PRK10816 |
two-component system response regulator PhoP; |
1896-1992 |
8.81e-03 |
|
two-component system response regulator PhoP;
Pssm-ID: 182755 [Multi-domain] Cd Length: 223 Bit Score: 39.72 E-value: 8.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1896 GYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM-GHEKFVTDLrELGVPLFLK 1974
Cdd:PRK10816 24 GHQVDAAEDAKEADYYLNEHLPDI--AIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAReSWQDKVEVL-SAGADDYVT 100
|
90
....*....|....*...
gi 1786808614 1975 KPFAAEELLRSLHAELHR 1992
Cdd:PRK10816 101 KPFHIEEVMARMQALMRR 118
|
|
| PRK10710 |
PRK10710 |
DNA-binding transcriptional regulator BaeR; Provisional |
1871-1950 |
9.38e-03 |
|
DNA-binding transcriptional regulator BaeR; Provisional
Pssm-ID: 182665 [Multi-domain] Cd Length: 240 Bit Score: 40.05 E-value: 9.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1786808614 1871 NGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRkRDATLPII 1950
Cdd:PRK10710 9 NTPRILIVEDEPKLGQLLIDYLQAASYATTLLSHGDEVLPYVRQTPPDL--ILLDLMLPGTDGLTLCREIR-RFSDIPIV 85
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
826-903 |
1.00e-02 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 41.01 E-value: 1.00e-02
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1786808614 826 KKTWDNLIKETEDREaLEKqLAAARGDLERQlAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERV 903
Cdd:PLN02316 243 EHSFEDFLLEEKRRE-LEK-LAKEEAERERQ-AEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNV 317
|
|
|