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Conserved domains on  [gi|1949443035|gb|KAG0510541|]
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MAG: putative kinesin K39 [Limisphaerales bacterium]

Protein Classification

Graphical summary

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List of domain hits

 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 1949443035 1556 TDVEAARQQAEQETTQRRSLEDALQQSHGE---VELRVSE-RTAGLNAHVQQLEAELAEAQRAEEQLRHR-RIEAVSTLA 1630
Cdd:COG3852     60 SPLRELLERALAEGQPVTEREVTLRRKDGEerpVDVSVSPlRDAEGEGGVLLVLRDITERKRLERELRRAeKLAAVGELA 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1631 GGMAHELNNVLAPVLMAAQLLRKQVS-GKSRTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQE 1709
Cdd:COG3852    140 AGLAHEIRNPLTGIRGAAQLLERELPdDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRA 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1710 TFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfiHHRRATGAKPGNYVLFRVT 1789
Cdd:COG3852    220 EAPKNIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVE-------RQVTLGGLRPRLYVRIEVI 292

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 1790 DSGVGIPRDILPRIFEPFFTTKEPGQsvGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAASAETSE 1860
Cdd:COG3852    293 DNGPGIPEEILDRIFEPFFTTKEKGT--GLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 361
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 1949443035 1875 LMLADDEQGVLDVTAEILEWHG--YKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:COG4753      2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDL--VITDINMPGMDGLELLEAIRELDPDTKIIIL 79

                           90       100
                   ....*....|....*....|....
gi 1949443035 1953 SGMGHEKFVTDLRELGVPLFLKKP 1976
Cdd:COG4753     80 SGYSDFEYAQEAIKLGADDYLLKP 103
Smc super family cl34174
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];


The actual alignment was detected with superfamily member COG1196:

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 1949443035  855 RQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRssEERVALLASELEAAREALRSESARREELETALPKT 934
Cdd:COG1196    216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEL--EAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  935 KTELGQRLAEAAAEAAGLrarmdfEAAERERVEAAWKLAnsATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRA 1014
Cdd:COG1196    294 LAELARLEQDIARLEERR------RELEERLEELEEELA--ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1015 ELEatnaessrALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDA 1094
Cdd:COG1196    366 ALL--------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1095 ERTTEALQADLDAALKACEEEAARRSQAEETARQshtefthRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKK 1174
Cdd:COG1196    438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEE-------AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1175 ELEKELADANLELLDIRSRLDHEAAARRQAEESAkqgSASADQRLAERLSEVQTLQERLRSEAAQRETtevELRDTRAAL 1254
Cdd:COG1196    511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL---AAALQNIVVEDDEVAAAAIEYLKAAKAGRAT---FLPLDKIRA 584

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1255 EKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDR 1334
Cdd:COG1196    585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1335 LTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRL 1414
Cdd:COG1196    665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1949443035 1415 GELTTALRTAEAKAGSDSAELRHAHETLQQAHAEL 1449
Cdd:COG1196    745 EELLEEEALEELPEPPDLEELERELERLEREIEAL 779
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 1949443035   85 APAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLRNKDGSTRWVA 164
Cdd:cd00130      1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                           90       100
                   ....*....|....*....|...
gi 1949443035  165 GHAMRVLDDHEQPNGIIGSILDI 187
Cdd:cd00130     81 VSLTPIRDEGGEVIGLLGVVRDI 103
Smc super family cl34174
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];


The actual alignment was detected with superfamily member COG1196:

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 1949443035  515 QAGAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETaLAELRAQLERTEAARQQ 594
Cdd:COG1196    249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  595 IETTALDLrsnsEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQ 674
Cdd:COG1196    328 LEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  675 PVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQL 754
Cdd:COG1196    404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  755 QAETERREQAESALGQsksETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIK 834
Cdd:COG1196    484 EELAEAAARLLLLLEA---EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  835 ETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAR 914
Cdd:COG1196    561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  915 EALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREE 994
Cdd:COG1196    641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  995 LHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAE 1047
Cdd:COG1196    721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
Smc super family cl34174
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];


The actual alignment was detected with superfamily member COG1196:

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 1949443035  225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEK 304
Cdd:COG1196    236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  305 AELEKRTasspAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:COG1196    316 ERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  385 ---RVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAgQGGGEVNPELAARI 461
Cdd:COG1196    392 lraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLE 470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  462 AALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQr 541
Cdd:COG1196    471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ- 549

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  542 feQRVAELETDNQQLREQASRDTQAATTQRgeqetALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADAR 621
Cdd:COG1196    550 --NIVVEDDEVAAAAIEYLKAAKAGRATFL-----PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  622 QQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSEL 701
Cdd:COG1196    623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  702 ETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSE 774
Cdd:COG1196    703 EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775
EnvC super family cl34844
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];


The actual alignment was detected with superfamily member COG4942:

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 1949443035 1412 RRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAA 1491
Cdd:COG4942      2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1492 RAELDMLNRQFAQRVAELDSTEARLREECAHRERAE--------------AELDRMRDAQDGFQQSTAELNERLTRLTTD 1557
Cdd:COG4942     82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035 1558 VEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERT---AGLNAHVQQLEAELAEAQRAEEQLR 1619
Cdd:COG4942    162 LAALRAELEAERAELEALLAELEEERAALEALKAERQkllARLEKELAELAAELAELQQEAEELE 226
 
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 1949443035 1556 TDVEAARQQAEQETTQRRSLEDALQQSHGE---VELRVSE-RTAGLNAHVQQLEAELAEAQRAEEQLRHR-RIEAVSTLA 1630
Cdd:COG3852     60 SPLRELLERALAEGQPVTEREVTLRRKDGEerpVDVSVSPlRDAEGEGGVLLVLRDITERKRLERELRRAeKLAAVGELA 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1631 GGMAHELNNVLAPVLMAAQLLRKQVS-GKSRTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQE 1709
Cdd:COG3852    140 AGLAHEIRNPLTGIRGAAQLLERELPdDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRA 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1710 TFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfiHHRRATGAKPGNYVLFRVT 1789
Cdd:COG3852    220 EAPKNIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVE-------RQVTLGGLRPRLYVRIEVI 292

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 1790 DSGVGIPRDILPRIFEPFFTTKEPGQsvGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAASAETSE 1860
Cdd:COG3852    293 DNGPGIPEEILDRIFEPFFTTKEKGT--GLGLAIVQKIVEQHGGTIEVESEPGKGTTFRIYLPLEQAEEEP 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 1949443035 1614 AEEQLRH-RRIEAVSTLAGGMAHELNNVLAPVL----MAAQLLRKQVSGKSRTL--VDSVESSAQRGADIVKQVLTFARG 1686
Cdd:PRK13557   150 AEDALRQaQKMEALGQLTGGIAHDFNNLLQVMSgyldVIQAALSHPDADRGRMArsVENIRAAAERAATLTQQLLAFARK 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1687 FHGERAPVSPEMLVRDIAKSVQETFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVVVD 1766
Cdd:PRK13557   230 QRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVEIE 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1767 ESFIHhrRATGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTE 1846
Cdd:PRK13557   310 DEDLA--MYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTT 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1847 FQIYLPAASAETSERPPQAELP--RGNGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAgDIKAVIT 1924
Cdd:PRK13557   388 VRLYFPASDQAENPEQEPKARAidRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHP-EVDLLFT 466

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035 1925 DILMP-FMDGVELCRELRKRDATLPIIVASGMGHEKFvtDLRELGVPLF--LKKPFAAEELLR 1984
Cdd:PRK13557   467 DLIMPgGMNGVMLAREARRRQPKIKVLLTTGYAEASI--ERTDAGGSEFdiLNKPYRRAELAR 527
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 1949443035 1735 LHRVLLNLAVNARDAMPSGGTLKFSAENVVVDESFIHHRRatGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16919      1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYR--DLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVG 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1949443035 1815 QSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:cd16919     79 KGTGLGLSMVYGFVKQSGGHLRIYSEPGVGTTVRIYLP 116
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 1949443035  1730 ADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFT 1809
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERD-----------------GDHVEITVEDNGPGIPPEDLEKIFEPFFR 63

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1949443035  1810 TKEPGQSV---GLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP 1852
Cdd:smart00387   64 TDKRSRKIggtGLGLSIVKKLVELHGGEISVESEPGGGTTFTITLP 109
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 1949443035 1875 LMLADDEQGVLDVTAEILEWHG--YKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:COG4753      2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDL--VITDINMPGMDGLELLEAIRELDPDTKIIIL 79

                           90       100
                   ....*....|....*....|....
gi 1949443035 1953 SGMGHEKFVTDLRELGVPLFLKKP 1976
Cdd:COG4753     80 SGYSDFEYAQEAIKLGADDYLLKP 103
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 1949443035 1730 ADASQLHRVLLNLAVNARDAMPSGGTLKfsaenVVVDEsfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFT 1809
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKAGEIT-----VTLSE-------------GGELTLTVEDNGIGIPPEDLPRIFEPFST 62

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1949443035 1810 TKEPGQS-VGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPAA 1854
Cdd:pfam02518   63 ADKRGGGgTGLGLSIVRKLVELLGGTITVESEPGGGTTVTLTLPLA 108
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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDL--ILLDINMPGMDGLELLKRIRRRDPTTPVIILTAH 79

                           90       100
                   ....*....|....*....|....*...
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDL--VLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78

                           90       100
                   ....*....|....*....|.
gi 1949443035 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 1949443035  855 RQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRssEERVALLASELEAAREALRSESARREELETALPKT 934
Cdd:COG1196    216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEL--EAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  935 KTELGQRLAEAAAEAAGLrarmdfEAAERERVEAAWKLAnsATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRA 1014
Cdd:COG1196    294 LAELARLEQDIARLEERR------RELEERLEELEEELA--ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1015 ELEatnaessrALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDA 1094
Cdd:COG1196    366 ALL--------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1095 ERTTEALQADLDAALKACEEEAARRSQAEETARQshtefthRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKK 1174
Cdd:COG1196    438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEE-------AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1175 ELEKELADANLELLDIRSRLDHEAAARRQAEESAkqgSASADQRLAERLSEVQTLQERLRSEAAQRETtevELRDTRAAL 1254
Cdd:COG1196    511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL---AAALQNIVVEDDEVAAAAIEYLKAAKAGRAT---FLPLDKIRA 584

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1255 EKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDR 1334
Cdd:COG1196    585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1335 LTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRL 1414
Cdd:COG1196    665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1949443035 1415 GELTTALRTAEAKAGSDSAELRHAHETLQQAHAEL 1449
Cdd:COG1196    745 EELLEEEALEELPEPPDLEELERELERLEREIEAL 779
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 1949443035   85 APAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLRNKDGSTRWVA 164
Cdd:cd00130      1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                           90       100
                   ....*....|....*....|...
gi 1949443035  165 GHAMRVLDDHEQPNGIIGSILDI 187
Cdd:cd00130     81 VSLTPIRDEGGEVIGLLGVVRDI 103
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 1949443035  834 KETEDREALEKQLAAARGDLERqLAETKAELDQQLAALAEARSQAER---------------------EAAERRQTEESL 892
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDR-LEDILNELERQLKSLERQAEKAERykelkaelrelelallvlrleELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  893 LQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAwKL 972
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ-LE 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  973 ANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSK 1052
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1053 SALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTE 1132
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1133 FTHRLTAETGAREQLE---KNLRQAAEEATRKAQALQ--AELQRAKKELEKELADANLELLDirSRLDHEAAARRQAEES 1207
Cdd:TIGR02168  487 LQARLDSLERLQENLEgfsEGVKALLKNQSGLSGILGvlSELISVDEGYEAAIEAALGGRLQ--AVVVENLNAAKKAIAF 564

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1208 AKQGSA----------SADQRLAERLSEVQTLQERLRSEAAQRETTEVELR--------------DTRAALEKQ------ 1257
Cdd:TIGR02168  565 LKQNELgrvtflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAkklrpg 644

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1258 ---------LAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAAR 1328
Cdd:TIGR02168  645 yrivtldgdLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1329 RAEVDRLtteqphAIEEATARLKAQLAEQEREREQLRLAAMSAE-QRLRDRATDFEAANAALRGEMEKRLRLELTWQMQR 1407
Cdd:TIGR02168  725 SRQISAL------RKDLARLEAEVEQLEERIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1408 EDFDRRLGELTTALRTAEAKAgsdsAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTN 1487
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1488 LNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDrmrdaqdgfqqstaELNERLTRLTTDVEAARQQAEQ 1567
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--------------ELREKLAQLELRLEGLEVRIDN 940

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|...
gi 1949443035 1568 ETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAE 1610
Cdd:TIGR02168  941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKE 983
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 1949443035  515 QAGAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETaLAELRAQLERTEAARQQ 594
Cdd:COG1196    249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  595 IETTALDLrsnsEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQ 674
Cdd:COG1196    328 LEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  675 PVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQL 754
Cdd:COG1196    404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  755 QAETERREQAESALGQsksETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIK 834
Cdd:COG1196    484 EELAEAAARLLLLLEA---EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  835 ETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAR 914
Cdd:COG1196    561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  915 EALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREE 994
Cdd:COG1196    641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  995 LHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAE 1047
Cdd:COG1196    721 LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLE 773
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 1949443035  225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEK 304
Cdd:COG1196    236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  305 AELEKRTasspAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:COG1196    316 ERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  385 ---RVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAgQGGGEVNPELAARI 461
Cdd:COG1196    392 lraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLE 470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  462 AALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQr 541
Cdd:COG1196    471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ- 549

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  542 feQRVAELETDNQQLREQASRDTQAATTQRgeqetALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADAR 621
Cdd:COG1196    550 --NIVVEDDEVAAAAIEYLKAAKAGRATFL-----PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  622 QQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSEL 701
Cdd:COG1196    623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  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 1949443035   98 ILFVNHRWSALTGRSQAESQGFG--WLLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLRNKDGSTRWVAGHAMRVLDDHE 175
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKGesWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80


                   ....*....
gi 1949443035  176 QPNGIIGSI 184
Cdd:pfam08447   81 KPVRVIGVA 89
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 1949443035  873 EARSQAEREAAERRQTEESLLQASRSSEERVALlASELEAAREALRSESARREEletalPKTKTELGQRLAEAAAEAAGL 952
Cdd:PTZ00121  1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKK-AEDARKAEEARKAEDARKAE-----EARKAEDAKRVEIARKAEDAR 1164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  953 RARMDFEAAERERVEAAWKlansateqhAAELKTllatAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQN 1032
Cdd:PTZ00121  1165 KAEEARKAEDAKKAEAARK---------AEEVRK----AEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1033 ELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELREsltdAERTTEALQADLDAALKAC 1112
Cdd:PTZ00121  1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE----KKKADEAKKAEEKKKADEA 1307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1113 EEEAARRSQAEETARQshtefthrltAETGAREQLEknLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRS 1192
Cdd:PTZ00121  1308 KKKAEEAKKADEAKKK----------AEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1193 RLDHEAAARRQAEESAK----QGSASADQRLAERLSEVQtlQERLRSEAAQRETTEVElrdtRAALEKQLAEASAALREA 1268
Cdd:PTZ00121  1376 AKKKADAAKKKAEEKKKadeaKKKAEEDKKKADELKKAA--AAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEA 1449

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1269 SARLEQERderrrvvesltqTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATA 1348
Cdd:PTZ00121  1450 KKKAEEAK------------KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1349 RLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTA--LRTAEA 1426
Cdd:PTZ00121  1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeeARIEEV 1597

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1427 KAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRV 1506
Cdd:PTZ00121  1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1507 AELDSTE--ARLREECAHRERAEA-ELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQEttqRRSLEdalqqsh 1583
Cdd:PTZ00121  1678 EEAKKAEedEKKAAEALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED---KKKAE------- 1747

                          730       740       750
                   ....*....|....*....|....*....|....
gi 1949443035 1584 gevELRVSERTAGLNAHVQQLEAELAEAQRAEEQ 1617
Cdd:PTZ00121  1748 ---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
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 1949443035 1873 ELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKrDATLPIIVA 1952
Cdd:CHL00148     7 EKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDL--VILDVMMPKLDGYGVCQEIRK-ESDVPIIML 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 ...
 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 1949443035  225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAvaehELAVKTLQAEK 304
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL----AEELAELEEKL 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  305 AELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  385 RVALQteheKAERADAERELSEEAMVQTNTgiQQRLMELNAELERTKEELVAESARRTQAEAGQGggevnpELAARIAAL 464
Cdd:TIGR02168  427 LKKLE----EAELKELQAELEELEEELEEL--QEELERLEEALEELREELEEAEQALDAAERELA------QLQARLDSL 494

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  465 TEAKAQVEKElveqQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEA-----DEAARAQVEADLRAAh 539
Cdd:TIGR02168  495 ERLQENLEGF----SEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvvenLNAAKKAIAFLKQNE- 569

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  540 qrfEQRVAELETDNQQLREQASRDTQAATTQRG------EQETALAELRAQLE-----------RTEAARQQIETTALDL 602
Cdd:TIGR02168  570 ---LGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDPKLRKALSyllggvlvvddLDNALELAKKLRPGYR 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  603 ------------------RSNSEQQLSETQRQLADARQQLQAESERRAQAESALgqskSETERQLAEATAALADTRKQLE 664
Cdd:TIGR02168  647 ivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKAL----AELRKELEELEEELEQLRKELE 722

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  665 EATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQ 744
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  745 QQLAALRQQLQAETERREQAESALGQSKSETERqlaeataalaevraqLEQATTASSQREAEAKQAAAAQQQKLADQDAE 824
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAA---------------TERRLEDLEEQIEELSEDIESLAAEIEELEEL 867

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  825 LKKTWDNLIKETEDREALEKQLAAARGDLE------RQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRS 898
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947

                          730       740       750
                   ....*....|....*....|....*....|....
gi 1949443035  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 1949443035   37 VAVVKDTLFLAAGTVGLFLLLRRDIQKREQTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAES 116
Cdd:COG2202     98 VELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEEL 177

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949443035  117 QGFGWLLAVHPDDNKRVTEEWRKCVRGEKE-FRLDFRLRNKDGSTRWVAGHAmRVLDDHEQPNGIIGSILDINERKVA 193
Cdd:COG2202    178 LGKSLLDLLHPEDRERLLELLRRLLEGGREsYELELRLKDGDGRWVWVEASA-VPLRDGGEVIGVLGIVRDITERKRA 254
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 1949443035  421 MELNAELERTKEEL-VAESARRTQAEAGQgggevnpelAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEA 499
Cdd:PTZ00121  1084 KEDNRADEATEEAFgKAEEAKKTETGKAE---------EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  500 AAARAALEQQLAAASQAGAGRSEADEAARAqvEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALA 579
Cdd:PTZ00121  1155 EIARKAEDARKAEEARKAEDAKKAEAARKA--EEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  580 ElRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLAD--ARQQLQAESERRAQAESALGQSKSETERQLAEATAALA 657
Cdd:PTZ00121  1233 E-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAikAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  658 DTRKQLEEATTKAAELQPVREQLAGEVQ----RGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSR 733
Cdd:PTZ00121  1312 EEAKKADEAKKKAEEAKKKADAAKKKAEeakkAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  734 TVAEQAAAEAQQQLAALRQQLQAETERR--EQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAA 811
Cdd:PTZ00121  1392 KADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  812 AAQqqklADQDAELKKTWDNLIKETEDrealekqlAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEEs 891
Cdd:PTZ00121  1472 ADE----AKKKAEEAKKADEAKKKAEE--------AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE- 1538

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  892 llqASRSSEERVA---LLASELEAAREALRSESARREELETALPKTKTELGQRLAEA--AAEAAGLRARMDFEAAERERV 966
Cdd:PTZ00121  1539 ---AKKAEEKKKAdelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKA 1615

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  967 EAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALA------------------ 1028
Cdd:PTZ00121  1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeakkaeedekkaaealk 1695

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1029 -----AAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQA 1103
Cdd:PTZ00121  1696 keaeeAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1104 DLDAALKAC--EEEAARRSQAEETARQSHTEFThrLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAK-KELEKEL 1180
Cdd:PTZ00121  1776 EKEAVIEEEldEEDEKRRMEVDKKIKDIFDNFA--NIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEaDAFEKHK 1853


                   ....*.
gi 1949443035 1181 ADANLE 1186
Cdd:PTZ00121  1854 FNKNNE 1859
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 1949443035   78 FESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKE-FRLDFRLRNK 156
Cdd:TIGR00229    5 YRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEpVSEERRVRRK 84

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1949443035  157 DGSTRWVAGHAMRVLDDHEQPnGIIGSILDINERK 191
Cdd:TIGR00229   85 DGSEIWVEVSVSPIRTNGGEL-GVVGIVRDITERK 118
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 1949443035 1016 LEATNAESSRALAAAQNELARESAERETTEAEF-QRSKSALAQQLAEAAAAQAELRSRLEKETAARHETER--ELRESLT 1092
Cdd:pfam12128  256 AELRLSHLHFGYKSDETLIASRQEERQETSAELnQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAleDQHGAFL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1093 DAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAR-----EQLEKNLRQAAEEATRKAQALQA 1167
Cdd:pfam12128  336 DADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnnrdiAGIKDKLAKIREARDRQLAVAED 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1168 ELQRAKKELEKELADANLELLDIRSRLdheaaARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVEL 1247
Cdd:pfam12128  416 DLQALESELREQLEAGKLEFNEEEYRL-----KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERL 490

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1248 RDTRAALEKQLAEASAALREASARLEQERDERRRVVESLT-QTSTTLEARATESGSALEVTRRLLNEERAARASALAELA 1326
Cdd:pfam12128  491 QSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFpQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVW 570

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1327 ARRAE-----------VDRLTTEQPHAIEEAtarLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANA----ALRG 1391
Cdd:pfam12128  571 DGSVGgelnlygvkldLKRIDVPEWAASEEE---LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASReetfARTA 647

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1392 EMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTE-RDSELASVREQAAAL 1470
Cdd:pfam12128  648 LKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREaRTEKQAYWQVVEGAL 727

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1471 DAAGTRAQQTTAELQTNlnaARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQ------DGFQQST 1544
Cdd:pfam12128  728 DAQLALLKAAIAARRSG---AKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRqevlryFDWYQET 804

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1545 -------------------AELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSE-RTAGLNAHVQQL 1604
Cdd:pfam12128  805 wlqrrprlatqlsnieraiSELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKlATLKEDANSEQA 884

                          650
                   ....*....|....*...
gi 1949443035 1605 EAELAEAQRAEEQLRHRR 1622
Cdd:pfam12128  885 QGSIGERLAQLEDLKLKR 902
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 1949443035 1336 TTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAE--QRLRDRATDFEAANAALRGEMEKRLRLELtwQMQREDFDRR 1413
Cdd:TIGR02168  177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEEL--QEELKEAEEE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1414 LGELTTALRTAEAKagsdSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARA 1493
Cdd:TIGR02168  255 LEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1494 ELDMLNRQFAQRVAELDSTEARLreecahrERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRR 1573
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEEL-------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1574 SLEDALQQSHGEVELRVSERTAGL----NAHVQQLEAELAEAQRAEEQLRHRRIEAVSTLAggmahELNNVLAPVLMAAQ 1649
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLkkleEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD 478

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1949443035 1650 LLRKQVSgKSRTLVDSVESSAQRGADI---VKQVLTFARGFHGERAPVS 1695
Cdd:TIGR02168  479 AAERELA-QLQARLDSLERLQENLEGFsegVKALLKNQSGLSGILGVLS 526
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 1949443035  245 RQLWAELSGREQVEAELAKARGELDkQVAERTATFTDIISGLEKavaehelAVKTLQAEKAELEK----RTASSPAELEA 320
Cdd:TIGR02169  156 RKIIDEIAGVAEFDRKKEKALEELE-EVEENIERLDLIIDEKRQ-------QLERLRREREKAERyqalLKEKREYEGYE 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  321 LRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLeTELESLRVALQTEHEKAERADA 400
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL-GEEEQLRVKEKIGELEAEIASL 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  401 ERELSEEamvqtntgiQQRLMELNAELERTKEELvaesaRRTQAEAgqgggevnPELAARIAALTEAKAQVEKELVEQQA 480
Cdd:TIGR02169  307 ERSIAEK---------ERELEDAEERLAKLEAEI-----DKLLAEI--------EELEREIEEERKRRDKLTEEYAELKE 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  481 VAKALgdernrlaqelaeaaaaraaleqqlaaasqagagRSEADEaaraqVEADLRAAHQRFEQRVAELETDNQQLRE-Q 559
Cdd:TIGR02169  365 ELEDL----------------------------------RAELEE-----VDKEFAETRDELKDYREKLEKLKREINElK 405

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  560 ASRDTQAATTQRGEQEtaLAELRAQLERTEAARQQIETTALDLR---SNSEQQLSETQRQLADARQQLQAESERRAQAES 636
Cdd:TIGR02169  406 RELDRLQEELQRLSEE--LADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483

                          410
                   ....*....|....*....
gi 1949443035  637 ALGQSKSETERQLAEATAA 655
Cdd:TIGR02169  484 ELSKLQRELAEAEAQARAS 502
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 1949443035   36 VVAVVKDTlflaAGTVGLFLLLRRDIQKREQTHAKNhevRQTFESLTQAAPAG---IFRANQQGDILFVNHRWSALTG-R 111
Cdd:PRK09776   374 AVSLVRDT----DGTPLYFIAQIEDINELKRTEQVN---ERLMERITLANEAGgigIWEWDLKPNIISWDKRMFELYEiP 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  112 SQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLRNKDGsTRWVAGHAMRVLDDHEQPNGIIGSILDINERK 191
Cdd:PRK09776   447 PHIKPTWQVWYACLHPEDRQRVEKEIRDALQGRSPFKLEFRIVVKDG-VRHIRALANRVLNKDGEVERLLGINMDMTEVR 525
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 1949443035  186 DINERKVADDTRTTDQAAALDAAlaRVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAELSGREQVE--AELAK 263
Cdd:PTZ00121  1238 DAEEAKKAEEERNNEEIRKFEEA--RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKkkAEEAK 1315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  264 ARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEKAELEKrtasSPAELEALRKRLSDEATRRQLAEDDLRSLR 343
Cdd:PTZ00121  1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA----AEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  344 EDfDKLQSSATQPDTALETVHhRLHAETERVKRLETELESLRVA--LQTEHEKAERADAERELSEEAMVQTNtgiqqrlM 421
Cdd:PTZ00121  1392 KA-DEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKAEE-------A 1462

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  422 ELNAELERTKEELVAESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKelveqqaVAKAlgdERNRLAQELAEAAA 501
Cdd:PTZ00121  1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-------AKKA---EEAKKADEAKKAEE 1532

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  502 ARAALEQQLAAASQagagrsEADEAARAQveaDLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAEL 581
Cdd:PTZ00121  1533 AKKADEAKKAEEKK------KADELKKAE---ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  582 RAQLERTEAARQQIE-TTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALgqsKSETERQLAEATAALADTR 660
Cdd:PTZ00121  1604 EKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEA 1680

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1949443035  661 KQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQ 705
Cdd:PTZ00121  1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAE 1725
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 1949443035  881 EAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEA 960
Cdd:NF033838    38 EEVRGGNNPTVTSSGNESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTS 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  961 AERERVEAA---WKLANSATEQHAAELKTLLATAREElhAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARE 1037
Cdd:NF033838   118 KTKKELDAAfeqFKKDTLEPGKKVAEATKKVEEAEKK--AKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1038 SAERETTEAEFQRSKSALAQQLAEAaaaqaelrSRLEKETAARHETERELRESLTDAERttEALQADLDAALKACEEEAA 1117
Cdd:NF033838   196 EAKEPRDEEKIKQAKAKVESKKAEA--------TRLEKIKTDREKAEEEAKRRADAKLK--EAVEKNVATSEQDKPKRRA 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1118 RRSQAEETARQSHTEFTHRLTAETGAREQL-------EKNLRQA---AEEATRKAQALQAELQR-----AKKELEKELAD 1182
Cdd:NF033838   266 KRGVLGEPATPDKKENDAKSSDSSVGEETLpspslkpEKKVAEAekkVEEAKKKAKDQKEEDRRnyptnTYKTLELEIAE 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1183 ANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAE--RLSEVQTlQERLRSEAAQRETTEVELRDTRAALEKQLAE 1260
Cdd:NF033838   346 SDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEatRLEKIKT-DRKKAEEEAKRKAAEEDKVKEKPAEQPQPAP 424


                   ....*...
gi 1949443035 1261 ASAALREA 1268
Cdd:NF033838   425 APQPEKPA 432
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 1949443035    76 QTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRK 139
Cdd:smart00091    1 ERLRAILESLPDGIFVLDLDGRILYANPAAEELLGYSPEELIGKSLLELIHPEDRERVQEALQR 64
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 1949443035 1412 RRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAA 1491
Cdd:COG4942      2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1492 RAELDMLNRQFAQRVAELDSTEARLREECAHRERAE--------------AELDRMRDAQDGFQQSTAELNERLTRLTTD 1557
Cdd:COG4942     82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035 1558 VEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERT---AGLNAHVQQLEAELAEAQRAEEQLR 1619
Cdd:COG4942    162 LAALRAELEAERAELEALLAELEEERAALEALKAERQkllARLEKELAELAAELAELQQEAEELE 226
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 1949443035 1342 AIEEATARLKAQLAEQEREREQLrlaamsaEQRLRDRATDFEAANAALRgEMEKRLRlELTWQMQREdFDRRLGELTTAL 1421
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKL-------TEEISELEKRLEEIEQLLE-ELNKKIK-DLGEEEQLR-VKEKIGELEAEI 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1422 RTAEAKAGSDSAELRHAHETLQQAhaeltrrlterDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLnrq 1501
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEERLAKL-----------EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--- 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1502 fAQRVAELDSTEARLREECAHR----ERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLED 1577
Cdd:TIGR02169  370 -RAELEEVDKEFAETRDELKDYreklEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949443035 1578 ALQQSHGEVE------LRVSERTAGLNAHVQQLEAELAEAQRAEEQLRHRRIEAVSTLAGGMAHEL 1637
Cdd:TIGR02169  449 EIKKQEWKLEqlaadlSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
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 1949443035  317 ELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESLRVALQTEHEKAE 396
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  397 RADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPELaaRIAALTEAKAQVEKELV 476
Cdd:pfam02463  247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER--RKVDDEEKLKESEKEKK 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  477 EQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQagagRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQL 556
Cdd:pfam02463  325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK----LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  557 REQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAES 636
Cdd:pfam02463  401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  637 ALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAE 716
Cdd:pfam02463  481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  717 AAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQaesalgqsKSETERQLAEATAALAEVRAQLEQA 796
Cdd:pfam02463  561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ--------LDKATLEADEDDKRAKVVEGILKDT 632

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  797 TTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARS 876
Cdd:pfam02463  633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  877 QAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARM 956
Cdd:pfam02463  713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  957 DFEAAERERVEAAWKLANSATEQHAAELKTLLATArEELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELAR 1036
Cdd:pfam02463  793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE-EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1037 ESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADL-DAALKACEEE 1115
Cdd:pfam02463  872 LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELlLEEADEKEKE 951

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1116 AARRSQAEETARQSHTEFTHRLTAETGAREQLEKNL--RQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSR 1193
Cdd:pfam02463  952 ENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEerYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINK 1031

                          890
                   ....*....|....*.
gi 1949443035 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 1949443035  534 DLRAAHQRFEQRVAEletdnQQLREQASRDTQAaTTQRGEQETALAELRAQLER--------TEAARQQIETTALDL--- 602
Cdd:NF041483    98 DARAQTQRILQEHAE-----HQARLQAELHTEA-VQRRQQLDQELAERRQTVEShvnenvawAEQLRARTESQARRLlde 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  603 -RSNSEQQLS----ETQRQLADARQQLQAESER-RAQAESALGQSKSETERQLAEATAaladtrkQLEEATTKAAELqpv 676
Cdd:NF041483   172 sRAEAEQALAaaraEAERLAEEARQRLGSEAESaRAEAEAILRRARKDAERLLNAAST-------QAQEATDHAEQL--- 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  677 REQLAGEVQRGERAEAELFRSRSELETQQAALAElraraeaaeaarlqvETTAQQSRTVAEQAAAEAQQQLAALRQQLQA 756
Cdd:NF041483   242 RSSTAAESDQARRQAAELSRAAEQRMQEAEEALR---------------EARAEAEKVVAEAKEAAAKQLASAESANEQR 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  757 ETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAElkktwDNLIKET 836
Cdd:NF041483   307 TRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAE-----EVLTKAS 381

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  837 EDREALEKqlaAARGDLERQLAETKAELDQQLAALAEARSQ----AEREAAERRQTEESLLQASRSSEERVALLASELEA 912
Cdd:NF041483   382 EDAKATTR---AAAEEAERIRREAEAEADRLRGEAADQAEQlkgaAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVA 458

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  913 AREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEqhaaelkTLLATAR 992
Cdd:NF041483   459 EGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERATTLRRQAEE-------TLERTRA 531

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  993 EELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAeRETTEAEfQRSKSALAQQLAEAAAAQAELRSR 1072
Cdd:NF041483   532 EAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELT-RLHTEAE-ERLTAAEEALADARAEAERIRREA 609

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1073 LEKETAARHETERELRESLTDAERTTEALQADldaalkACEEEAARRSQAEETARQSHTEFT---HRLTAEtgAREQLEK 1149
Cdd:NF041483   610 AEETERLRTEAAERIRTLQAQAEQEAERLRTE------AAADASAARAEGENVAVRLRSEAAaeaERLKSE--AQESADR 681

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1150 NLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEaaaRRQAEESAKQGSASADQRLAERLSEVQTL 1229
Cdd:NF041483   682 VRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQE---RERAREQSEELLASARKRVEEAQAEAQRL 758

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1230 QERLRSEAAQ----RETTEVELRDTRAALEKQLAEASAALREAsARLEQERDERRRVVESLTQTSTTLEARATESGSALE 1305
Cdd:NF041483   759 VEEADRRATElvsaAEQTAQQVRDSVAGLQEQAEEEIAGLRSA-AEHAAERTRTEAQEEADRVRSDAYAERERASEDANR 837

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1306 VTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATD---- 1381
Cdd:NF041483   838 LRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAqadr 917

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1382 --FEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELR-HAHETL--QQAHAELTRRLTER 1456
Cdd:NF041483   918 liGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRaEAAETVgsAQQHAERIRTEAER 997

                          970       980       990      1000      1010      1020      1030
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035 1457 -DSELASVREQAAAldAAGTRAQQTTAELQTNLNAARAE-LDMLNRQFAQRVAELDSTEARLREEcAHRERAEAE 1529
Cdd:NF041483   998 vKAEAAAEAERLRT--EAREEADRTLDEARKDANKRRSEaAEQADTLITEAAAEADQLTAKAQEE-ALRTTTEAE 1069
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 1949443035  283 ISGLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAED-DLRSLREDFDKLQSSATQPDTA-L 360
Cdd:pfam12128  260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEALEDQHGAFLDAdI 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  361 ETVHhrLHAETERVKRLETELESLRVALQTE-HEKAERA-DAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVA-- 436
Cdd:pfam12128  340 ETAA--ADQEQLPSWQSELENLEERLKALTGkHQDVTAKyNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDdl 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  437 ---ESARRTQAEAGQGggEVNPELAARIAALTEAK-----AQVEKELVEQQAVAKALGD-----------ERNRLAQELA 497
Cdd:pfam12128  418 qalESELREQLEAGKL--EFNEEEYRLKSRLGELKlrlnqATATPELLLQLENFDERIErareeqeaanaEVERLQSELR 495

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  498 EAAAARAALEQQLAAASQAGAGRSEADEAARAQVEAD-------LRAAHQRFEQRVAEL-------ETD----------- 552
Cdd:pfam12128  496 QARKRRDQASEALRQASRRLEERQSALDELELQLFPQagtllhfLRKEAPDWEQSIGKVispellhRTDldpevwdgsvg 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  553 -----------------------NQQLRE---QASRDTQAATTQRGEQETALAELRAQLERTEA----ARQQIETTALDL 602
Cdd:pfam12128  576 gelnlygvkldlkridvpewaasEEELRErldKAEEALQSAREKQAAAEEQLVQANGELEKASReetfARTALKNARLDL 655

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  603 RsnseqQLSETQRQLADARQQlqAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVRE---- 678
Cdd:pfam12128  656 R-----RLFDEKQSEKDKKNK--ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgald 728

                          490       500
                   ....*....|....*....|....*..
gi 1949443035  679 -QLAGEVQRGERAEAELFRSRSELETQ 704
Cdd:pfam12128  729 aQLALLKAAIAARRSGAKAELKALETW 755
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 1949443035  1144 REQLEKNLRQAAEEATrkaqalqAELQRAKKELEKELADANLELLDIRSRLD---HEAAARRQAEESAKQGSASADQRLA 1220
Cdd:smart00787  138 RMKLLEGLKEGLDENL-------EGLKEDYKLLMKELELLNSIKPKLRDRKDaleEELRQLKQLEDELEDCDPTELDRAK 210

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949443035  1221 ERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEAR 1296
Cdd:smart00787  211 EKLKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSL 286
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 1949443035 1471 DAAGTRAQQTTAELQTNLNAARAELDMLNRQ---FAQRVAELDSTEARLREE 1519
Cdd:PRK13729    68 QHATTEMQVTAAQMQKQYEEIRRELDVLNKQrgdDQRRIEKLGQDNAALAEQ 119
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 1949443035  311 TASSPAELEALRKRLS-DEATRRQL-----AEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKR--LETELE 382
Cdd:NF012221  1537 TSESSQQADAVSKHAKqDDAAQNALadkerAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRdaILEESR 1616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  383 SLRVALQTeheKAERADAereLSEEAMVQTNTGIQQRLMELNAELERTKEELvaESARRTQAEAgqgggevnpelaaria 462
Cdd:NF012221  1617 AVTKELTT---LAQGLDA---LDSQATYAGESGDQWRNPFAGGLLDRVQEQL--DDAKKISGKQ---------------- 1672

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  463 aLTEAKAQVEKELVE-QQAVAKalgdernrlaqelaeaaaaraaleqqlaaaSQAGAGRSEADeaaRAQVEADLRAAHQR 541
Cdd:NF012221  1673 -LADAKQRHVDNQQKvKDAVAK------------------------------SEAGVAQGEQN---QANAEQDIDDAKAD 1718

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1949443035  542 FEQRvaELETDNQQLR-EQASRDTQAATT---QRGEQETALAELRAQLERTEAA 591
Cdd:NF012221  1719 AEKR--KDDALAKQNEaQQAESDANAAANdaqSRGEQDASAAENKANQAQADAK 1770
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 1949443035  249 AELSGREQVE--AELAKARGELDKQVAERTAT----FTDIISGLEKAVAEHEL-AVKTLQAEKAELEKRTASSPAELEAL 321
Cdd:NF041483   111 AEHQARLQAElhTEAVQRRQQLDQELAERRQTveshVNENVAWAEQLRARTESqARRLLDESRAEAEQALAAARAEAERL 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  322 ----RKRLSDEA-TRRQLAEDDLRSLREDFDKL----QSSATQPDTALETVHHRLHAETERVKRLETELEslRVALQTEH 392
Cdd:NF041483   191 aeeaRQRLGSEAeSARAEAEAILRRARKDAERLlnaaSTQAQEATDHAEQLRSSTAAESDQARRQAAELS--RAAEQRMQ 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  393 EKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTqaeaGQGGGEVNPELAARIAALTEAKAQVE 472
Cdd:NF041483   269 EAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLV----GEATKEAEALKAEAEQALADARAEAE 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  473 KELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAAR-AQVEAD-LRA-AHQRFEQRVAEL 549
Cdd:NF041483   345 KLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRReAEAEADrLRGeAADQAEQLKGAA 424

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  550 ETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEA-----ARQQIETTAldlrSNSEQQLSETQRQLADARQQL 624
Cdd:NF041483   425 KDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGearreAVQQIEEAA----RTAEELLTKAKADADELRSTA 500

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  625 QAESER------------RAQAESALGQSKSETERQLAEATAALADTRKQLEEAttkAAELQPVREQlaGEVQRGERAEA 692
Cdd:NF041483   501 TAESERvrteaierattlRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERA---ARELREETER--AIAARQAEAAE 575

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  693 ELFRSRSELEtqqaalaelraraeaaeaarlqvettaqqsrtvaeqaaaeaqqqlaalrqqlqaetERREQAESALGQSK 772
Cdd:NF041483   576 ELTRLHTEAE--------------------------------------------------------ERLTAAEEALADAR 599

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  773 SETERQLAEATAALAEVRAQL-EQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLikETEDREALEKQLAAARG 851
Cdd:NF041483   600 AEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRL--RSEAAAEAERLKSEAQE 677

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  852 DLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASelEAAREALRSESARREELETAL 931
Cdd:NF041483   678 SADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAR--EQSEELLASARKRVEEAQAEA 755

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  932 PKTKTELGQRLAEAAAEAAGLRARM-DFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAET-AKRDAAEAAA 1009
Cdd:NF041483   756 QRLVEEADRRATELVSAAEQTAQQVrDSVAGLQEQAEEEIAGLRSAAEHAAERTRTEAQEEADRVRSDAyAERERASEDA 835

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1010 SQVRAELEAtNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLE-KETAARHETERELR 1088
Cdd:NF041483   836 NRLRREAQE-ETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADaREDANRIRSDAAAQ 914

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1089 ESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAE 1168
Cdd:NF041483   915 ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTE 994

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1169 LQRAKKELEKELADANLELLDIRSRLDHEaaARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELR 1248
Cdd:NF041483   995 AERVKAEAAAEAERLRTEAREEADRTLDE--ARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQA 1072

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1249 DTRAALEKQLAE--ASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEEraARASALAELA 1326
Cdd:NF041483  1073 DTMVGAARKEAEriVAEATVEGNSLVEKARTDADELLVGARRDATAIRERAEELRDRITGEIEELHER--ARRESAEQMK 1150

                         1130      1140      1150      1160
                   ....*....|....*....|....*....|....*....|..
gi 1949443035 1327 ARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAA 1368
Cdd:NF041483  1151 SAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIAA 1192
 
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 1949443035 1556 TDVEAARQQAEQETTQRRSLEDALQQSHGE---VELRVSE-RTAGLNAHVQQLEAELAEAQRAEEQLRHR-RIEAVSTLA 1630
Cdd:COG3852     60 SPLRELLERALAEGQPVTEREVTLRRKDGEerpVDVSVSPlRDAEGEGGVLLVLRDITERKRLERELRRAeKLAAVGELA 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1631 GGMAHELNNVLAPVLMAAQLLRKQVS-GKSRTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQE 1709
Cdd:COG3852    140 AGLAHEIRNPLTGIRGAAQLLERELPdDELREYTQLIIEEADRLNNLVDRLLSFSRPRPPEREPVNLHEVLERVLELLRA 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1710 TFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfiHHRRATGAKPGNYVLFRVT 1789
Cdd:COG3852    220 EAPKNIRIVRDYDPSLPEVLGDPDQLIQVLLNLVRNAAEAMPEGGTITIRTRVE-------RQVTLGGLRPRLYVRIEVI 292

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1490 AARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQET 1569
Cdd:COG4191      5 LLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLLLLGL 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1570 TQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEQLRHR-RIEAVSTLAGGMAHELNNVLAPVLMAA 1648
Cdd:COG4191     85 LLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSeKLAALGELAAGIAHEINNPLAAILGNA 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1649 QLLRKQVSGKS-----RTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVA 1722
Cdd:COG4191    165 ELLRRRLEDEPdpeelREALERILEGAERAAEIVRSLRAFSRRDEEEREPVDLNELIDEALELLRPRLKaRGIEVELDLP 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1723 DDLPLISADASQLHRVLLNLAVNARDAMPSG--GTLKFSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIPRDIL 1800
Cdd:COG4191    245 PDLPPVLGDPGQLEQVLLNLLINAIDAMEEGegGRITISTR-----------------REGDYVVISVRDNGPGIPPEVL 307

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1614 AEEQLRH-RRIEAVSTLAGGMAHELNNVLAPVL----MAAQLLRKQVSGKSRTL--VDSVESSAQRGADIVKQVLTFARG 1686
Cdd:PRK13557   150 AEDALRQaQKMEALGQLTGGIAHDFNNLLQVMSgyldVIQAALSHPDADRGRMArsVENIRAAAERAATLTQQLLAFARK 229

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1687 FHGERAPVSPEMLVRDIAKSVQETFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVVVD 1766
Cdd:PRK13557   230 QRLEGRVLNLNGLVSGMGELAERTLGDAVTIETDLAPDLWNCRIDPTQAEVALLNVLINARDAMPEGGRVTIRTRNVEIE 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1767 ESFIHhrRATGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTE 1846
Cdd:PRK13557   310 DEDLA--MYHGLPPGRYVSIAVTDTGSGMPPEILARVMDPFFTTKEEGKGTGLGLSMVYGFAKQSGGAVRIYSEVGEGTT 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1847 FQIYLPAASAETSERPPQAELP--RGNGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAgDIKAVIT 1924
Cdd:PRK13557   388 VRLYFPASDQAENPEQEPKARAidRGGTETILIVDDRPDVAELARMILEDFGYRTLVASNGREALEILDSHP-EVDLLFT 466

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035 1494 ELDMLNRQFAQRVAELDSTEARLREecaHRERAEAELDRMRDAQDGF--QQSTAELNERLTRLT-TDVEAARQQAEQETT 1570
Cdd:COG5000     63 EIGELARAFNRMTDQLKEQREELEE---RRRYLETILENLPAGVIVLdaDGRITLANPAAERLLgIPLEELIGKPLEELL 139

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1571 QRRSLEDALQQS-----HGEVELRVS-ERTAGLNAHVQQLEAELAEAQRAEEQLRHRRIEAVSTLAGGMAHELNNVLAPV 1644
Cdd:COG5000    140 PELDLAELLREAlergwQEEIELTRDgRRTLLVRASPLRDDGYVIVFDDITELLRAERLAAWGELARRIAHEIKNPLTPI 219

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1645 LMAAQLLRKQVSGKS-------RTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQETFPR-NVR 1716
Cdd:COG5000    220 QLSAERLRRKLADKLeedredlERALDTIIRQVDRLKRIVDEFLDFARLPEPQLEPVDLNELLREVLALYEPALKEkDIR 299

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1717 VSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIP 1796
Cdd:COG5000    300 LELDLDPDLPEVLADRDQLEQVLINLLKNAIEAIEEGGEIEVSTR-----------------REDGRVRIEVSDNGPGIP 362

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1523 RERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQ 1602
Cdd:COG0642     12 LLLLLLLLLALLLLLLLLLLLALLLLLALLLLLLLLLLLLLLLALALLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1603 QLEAELAEAQRAEEQLRhrrieAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSRTLVDSVESSAQRGADIVKQVLT 1682
Cdd:COG0642     92 LLLLLLALLLLLEEANE-----AKSRFLANVSHELRTPLTAIRGYLELLLEELDEEQREYLETILRSADRLLRLINDLLD 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1683 FARGFHG----ERAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLK 1757
Cdd:COG0642    167 LSRLEAGklelEPEPVDLAELLEEVVELFRPLAEeKGIELELDLPDDLPTVRGDPDRLRQVLLNLLSNAIKYTPEGGTVT 246

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1758 FSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEP--GQSVGLGLATALGVVQSHGGFI 1835
Cdd:COG0642    247 VSVR-----------------REGDRVRISVEDTGPGIPPEDLERIFEPFFRTDPSrrGGGTGLGLAIVKRIVELHGGTI 309

                          330
                   ....*....|....*....
gi 1949443035 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 1949443035 1442 LQQAHAELTRRLT-ERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRV------AELDSTEA 1514
Cdd:PRK13837   262 LRARTRVLRRRAAfEEVIAAISRCFEAASPHELEASIEAALGILAKFFDADSAALALVDVGGRARIwtfpglTPDPVWPD 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1515 RLREeCAHRERAeAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVEL-RVSER 1593
Cdd:PRK13837   342 RLRA-LASTVKA-AERDVVFVDRNGPVRKRSCLTRRGPALWACLAFKSGDRIVALLGLGRQRYGLRPPAGELQLlELALD 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1594 TAGLNAHVQQLEAELAEAQRAeeqLRH-RRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSRTL--VDSVESSA 1670
Cdd:PRK13837   420 CLAHAIERRRLETERDALERR---LEHaRRLEAVGTLASGIAHNFNNILGAILGYAEMALNKLARHSRAAryIDEIISAG 496

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1671 QRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQETFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAM 1750
Cdd:PRK13837   497 ARARLIIDQILAFGRKGERNTKPFDLSELVTEIAPLLRVSLPPGVELDFDQDQEPAVVEGNPAELQQVLMNLCSNAAQAM 576

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1751 PSGGTLKFSAENVVVdesfihhRRATG-----AKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQsvGLGLATAL 1825
Cdd:PRK13837   577 DGAGRVDISLSRAKL-------RAPKVlshgvLPPGRYVLLRVSDTGAGIDEAVLPHIFEPFFTTRAGGT--GLGLATVH 647

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1826 GVVQSHGGFILLETEEDKGTEFQIYLPAASAETSErpPQAE-----LPRGNGELLMLADDEQGVLDVTAEILEWHGYKVL 1900
Cdd:PRK13837   648 GIVSAHAGYIDVQSTVGRGTRFDVYLPPSSKVPVA--PQAFfgpgpLPRGRGETVLLVEPDDATLERYEEKLAALGYEPV 725

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1901 TARDGQQALSLY--DQHAGDikAVITDilMPFMDGVELCRELRKRDATLPIIVAsGMGHEKFVTDLRELGVPLFLKKPFA 1978
Cdd:PRK13837   726 GFSTLAAAIAWIskGPERFD--LVLVD--DRLLDEEQAAAALHAAAPTLPIILG-GNSKTMALSPDLLASVAEILAKPIS 800

                          570
                   ....*....|....*....
gi 1949443035 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 1949443035 1607 ELAEAQRAEEQLRHRRieavSTLAGGMAHELNNVLAPVLMAAQLLRKQVSG---KSRTLVDSVESSAQRGADIVKQVLTF 1683
Cdd:COG2205      1 ELEEALEELEELERLK----SEFLANVSHELRTPLTSILGAAELLLDEEDLspeERRELLEIIRESAERLLRLIEDLLDL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1684 AR----GFHGERAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKF 1758
Cdd:COG2205     77 SRlesgKLSLELEPVDLAELLEEAVEELRPLAEeKGIRLELDLPPELPLVYADPELLEQVLANLLDNAIKYSPPGGTITI 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1759 SAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG--QSVGLGLATALGVVQSHGGFIL 1836
Cdd:COG2205    157 SARRE-----------------GDGVRISVSDNGPGIPEEELERIFERFYRGDNSRgeGGTGLGLAIVKRIVEAHGGTIW 219

                          250       260
                   ....*....|....*....|
gi 1949443035 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 1949443035 1610 EAQRAEEQLRHR-RIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSRTLVDSVESSAQRGADIVKQVLTFARgfh 1688
Cdd:COG5809    253 ERKKLEELLRKSeKLSVVGELAAGIAHEIRNPLTSLKGFIQLLKDTIDEEQKTYLDIMLSELDRIESIISEFLVLAK--- 329

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1689 geraPVSPEMLVRDIAKSVQETFP--------RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLkfsa 1760
Cdd:COG5809    330 ----PQAIKYEPKDLNTLIEEVIPllqpqallKNVQIELELEDDIPDILGDENQLKQVFINLLKNAIEAMPEGGNI---- 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1761 envvvdesFIHhrraTGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLETE 1840
Cdd:COG5809    402 --------TIE----TKAEDDDKVVISVTDEGCGIPEERLKKLGEPFYTTKEKG--TGLGLMVSYKIIEEHGGKITVESE 467

                          250       260
                   ....*....|....*....|.
gi 1949443035 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 1949443035 1615 EEQLRHRRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSR-TLVDSVESSAQRGADIVKQVLTFARGFHGERAP 1693
Cdd:COG5807    136 DKLLRSEKLSVAGELAAGIAHEIRNPLTSIKGFLQLLQESREDSEReEYFNIIISEIDRINTIITELLVLSKPKKFNFKK 215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1694 VSPEMLVRDIAKSVQETFP-RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAenvvvdesfihh 1772
Cdd:COG5807    216 LNLNDVLEDVIALLSTEAIlKNISIKYDLADDEPVINGDKNQLKQVFINLIKNAIEAMETGGNITIKT------------ 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNARDAMPSGGTLKFSAENVVVDESFIHHRRatGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16919      1 LELAILNLAVNARDAMPEGGRLTIETSNQRVDADYALNYR--DLIPGNYVCLEVSDTGSGMPAEVLRRAFEPFFTTKEVG 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035 1567 QETTQRRSLEDALQQSHGEVELRVSerTAGL-NAHVQQLEA-----ELAEAQRAEEQL-RHRRIEAVSTLAGGMAHELNN 1639
Cdd:PRK11360   326 EHGTEHVDLEISFPGRDRTIELSVS--TSLLhNTHGEMIGAlvifsDLTERKRLQRRVaRQERLAALGELVAGVAHEIRN 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1640 VLAPVLMAAQLLRKQVSGK-SRTLVDSVESSAQRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQETFPRN-VRV 1717
Cdd:PRK11360   404 PLTAIRGYVQIWRQQTSDPpSQEYLSVVLREVDRLNKVIDQLLEFSRPRESQWQPVSLNALVEEVLQLFQTAGVQArVDF 483

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1718 SSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVVVDESFIhhrratgakpgnyvlfRVTDSGVGIPR 1797
Cdd:PRK11360   484 ETELDNELPPIWADPELLKQVLLNILINAVQAISARGKIRIRTWQYSDGQVAV----------------SIEDNGCGIDP 547

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1488 LNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQ 1567
Cdd:COG5002     35 LLLLLLLLLLLLLLLLLLALLLLLLLLLLLLLALLLLLLLLLLLLALALLLLALLLLLLLLLLLLALLILLLLLALLILL 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1568 ETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEQLRHrrieavstLAGGMAHELNNVLAPVLMA 1647
Cdd:COG5002    115 AALLLLLSELLLLLLLLGRLSLRLSALLLGLLLLAAVERDITELERLEQMRRE--------FVANVSHELRTPLTSIRGY 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1648 AQLLRKQVSG---KSRTLVDSVESSAQRGADIVKQVLTFARGFHG----ERAPVSPEMLVRDIAKSVQETFP-RNVRVSS 1719
Cdd:COG5002    187 LELLLDGAADdpeERREYLEIILEEAERLSRLVNDLLDLSRLESGelklEKEPVDLAELLEEVVEELRPLAEeKGIELEL 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1720 EVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDI 1799
Cdd:COG5002    267 DLPEDPLLVLGDPDRLEQVLTNLLDNAIKYTPEGGTITVSLREE-----------------DDQVRISVRDTGIGIPEED 329

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1610 EAQRAEEQLRH-RRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKSRTLvDSVESSAQRGADIVKQVLTFARgfh 1688
Cdd:COG5805    270 EKKEAEELMARsEKLSIAGQLAAGIAHEIRNPLTSIKGFLQLLQPGIEDKEEYF-DIMLSELDRIESIISEFLALAK--- 345

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1689 geraPVSPEMLVRDIAKSVQETFP--------RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLkfsa 1760
Cdd:COG5805    346 ----PQAVNKEKENINELIQDVVTlleteailHNIQIRLELLDEDPFIYCDENQIKQVFINLIKNAIEAMPNGGTI---- 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1761 envvvdesFIHHRRAtgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLETE 1840
Cdd:COG5805    418 --------TIHTEEE-----DNSVIIRVIDEGIGIPEERLKKLGEPFFTTKEKG--TGLGLMVSYKIIENHNGTIDIDSK 482

                          250
                   ....*....|..
gi 1949443035 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 1949443035 1612 QRAEEQLRHRRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSG-KSRTLVDSVESSAQRGADIVKQVLTFARGFHGE 1690
Cdd:COG5808    227 ERVIQEINTQKLELIGTFAASTAHEIRNPLTSIKGFIQLLQEKYPElEDQKYFDIIQEEIQRINQIVSEFLVLGKPTAKK 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1691 RAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSAENvvvdesf 1769
Cdd:COG5808    307 LELDDLNELIEEILSIIDSEANlKNIRVEKQSLDEPLHIKCDKDRIKQVLLNLIKNAIEAMKEGGKLTISIEN------- 379

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1770 ihhrratgakPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLETEEDKGTEFQI 1849
Cdd:COG5808    380 ----------DDEKAVIEVIDNGEGIPEDIIDEIFEPFVTTKEGG--TGLGLSVCKRIVEMHGGEIDIESEEGKGTTFTI 447


                   ....*..
gi 1949443035 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 1949443035 1602 QQLEAELAeaqraeeqlRHRRIEAVSTLAGGMAHELNNVLAPVLMAAQLL--RKQVSGKSRTLVDSVESSAQRGADIVKQ 1679
Cdd:PRK10364   222 QLLQDEMK---------RKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFaeRAPAGGEAHQLAQVMAKEADRLNRVVSE 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1680 VLTFARGFHGERAPVSPEMLVRDIAKSV-QETFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKF 1758
Cdd:PRK10364   293 LLELVKPTHLALQAVDLNDLINHSLQLVsQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISV 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1759 SAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKepGQSVGLGLATALGVVQSHGGFILLE 1838
Cdd:PRK10364   373 TASES-----------------GAGVKISVTDSGKGIAADQLEAIFTPYFTTK--AEGTGLGLAVVHNIVEQHGGTIQVA 433

                          250
                   ....*....|....*.
gi 1949443035 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 1949443035 1342 AIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTAL 1421
Cdd:COG4251      2 LLLALLLLLLLLLLLLLLLLLLLLLVLLLALALLLLLALLVLLLLLIRLLLLLLLSLLALLLLLLLLLLLLLVLAALALL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1422 RTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQ 1501
Cdd:COG4251     82 LLLLLLELALVLLALLLVLLLLLALLLLLALLLLLELLLLLLALLLLLLLLALLLLEELALLRLALALLLLLLLLLLLLL 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1502 FAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQ 1581
Cdd:COG4251    162 LLLALILALLLAALAELELLLLLLLVLLLLLLLLLLLLLLLLRLLLELLLLLEAELLLSLGGGLGLLLLLLLLLVLLLLL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1582 SHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEQlRHRRIEAvstLAGGMAHELNNVLAPVLMAAQLLRK----QVSG 1657
Cdd:COG4251    242 ILLLLLLILVLELLELRLELEELEEELEERTAELER-SNEELEQ---FAYVASHDLREPLRKISGFSQLLEEdygdKLDE 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1658 KSRTLVDSVESSAQRGADIVKQVLTFAR--GFHGERAPVSPEMLVRDIAKSVQETFP-RNVRVsseVADDLPLISADASQ 1734
Cdd:COG4251    318 EGREYLERIRDAAERMQALIDDLLAYSRvgRQELEFEPVDLNELLEEVLEDLEPRIEeRGAEI---EVGPLPTVRGDPTL 394

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1735 LHRVLLNLAVNArdampsggtLKFSAENVVVdesFIHhrrATGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFT--TKE 1812
Cdd:COG4251    395 LRQVFQNLISNA---------IKYSRPGEPP---RIE---IGAEREGGEWVFSVRDNGIGIDPEYAEKIFEIFQRlhSRD 459

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035  1730 ADASQLHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFT 1809
Cdd:smart00387    1 GDPDRLRQVLSNLLDNAIKYTPEGGRITVTLERD-----------------GDHVEITVEDNGPGIPPEDLEKIFEPFFR 63

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*.
gi 1949443035  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 1949443035 1597 LNAHVQQLEAELAEAQRAEeqlrhrRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQvsgksRTLVDSVESSAQ----- 1671
Cdd:COG5806    178 LIENLIENILLRKELQRAE------KLEVVSELAASIAHEVRNPLTVVRGFIQLLQEP-----ELSDEKRKQYIRialee 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1672 --RGADIVKQVLTFARgfhgeraPVSPEMLVRDIAKSVQE----TFP----RNVRVSSEVADDLpLISADASQLHRVLLN 1741
Cdd:COG5806    247 ldRAEAIITDYLTFAK-------PQPEKLEKIDVSEELEHvidvLSPyanmNNVEIQTELEPGL-YIEGDRQKLQQCLIN 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1742 LAVNARDAMPSGGTLKFSAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGqsVGLGL 1821
Cdd:COG5806    319 IIKNGIEAMPNGGTLTIDVSID-----------------KNKVIISIKDTGVGMTKEQLERLGEPYFSTKEKG--TGLGT 379

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNARDAMPSGGTLKFSAENVvvdesfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTK--E 1812
Cdd:cd00075      1 LEQVLSNLLDNALKYSPPGGTIEISLRQE-----------------GDGVVLEVEDNGPGIPEEDLERIFERFYRGDksR 63

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHG--YKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:COG4753      2 VLIVDDEPLIREGLKRILEWEAgfEVVGEAENGEEALELLEEHKPDL--VITDINMPGMDGLELLEAIRELDPDTKIIIL 79

                           90       100
                   ....*....|....*....|....
gi 1949443035 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 1949443035 1733 SQLHRVLLNLAVNARDAMPSGGTLKFsaenvvvdESFIHHRRatgakpgnyVLFRVTDSGVGIPRDILPRIFEPFFTTKE 1812
Cdd:cd16943      2 SQLNQVLLNLLVNAAQAMEGRGRITI--------RTWAHVDQ---------VLIEVEDTGSGIDPEILGRIFDPFFTTKP 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1868 PRGNGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT- 1946
Cdd:COG0784      1 PPLGGKRILVVDDNPDNRELLRRLLERLGYEVTTAEDGAEALELLRAGPPDL--ILLDINMPGMDGLELLRRIRALPRLp 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1730 ADASQLHRVLLNLAVNARDAMPSGGTLKfsaenVVVDEsfihhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFT 1809
Cdd:pfam02518    1 GDELRLRQVLSNLLDNALKHAAKAGEIT-----VTLSE-------------GGELTLTVEDNGIGIPPEDLPRIFEPFST 62

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:COG0745      4 ILVVEDDPDIRELLADALEREGYEVDTAADGEEALELLEEERPDL--ILLDLMLPGMDGLEVCRRLRARPSDIPIIMLTA 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:pfam00072    2 LIVDDDPLIRELLRQLLEKEGYVVAEADDGKEALELLKEERPDL--ILLDINMPGMDGLELLKRIRRRDPTTPVIILTAH 79

                           90       100
                   ....*....|....*....|....*...
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:cd00156      1 LIVDDDPAIRELLKSLLEREGYEVDTAADGEEALELLREERPDL--VLLDLMMPGMDGLELLRKLRELPPDIPVIVLTAK 78

                           90       100
                   ....*....|....*....|.
gi 1949443035 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 1949443035  855 RQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRssEERVALLASELEAAREALRSESARREELETALPKT 934
Cdd:COG1196    216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEL--EAELAELEAELEELRLELEELELELEEAQAEEYEL 293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  935 KTELGQRLAEAAAEAAGLrarmdfEAAERERVEAAWKLAnsATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRA 1014
Cdd:COG1196    294 LAELARLEQDIARLEERR------RELEERLEELEEELA--ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1015 ELEatnaessrALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDA 1094
Cdd:COG1196    366 ALL--------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1095 ERTTEALQADLDAALKACEEEAARRSQAEETARQshtefthRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKK 1174
Cdd:COG1196    438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEE-------AALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGV 510

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1175 ELEKELADANLELLDIRSRLDHEAAARRQAEESAkqgSASADQRLAERLSEVQTLQERLRSEAAQRETtevELRDTRAAL 1254
Cdd:COG1196    511 KAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAL---AAALQNIVVEDDEVAAAAIEYLKAAKAGRAT---FLPLDKIRA 584

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1255 EKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDR 1334
Cdd:COG1196    585 RAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTG 664

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1335 LTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRL 1414
Cdd:COG1196    665 GSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEE 744

                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 1070 RSRLEKETAARHETERELrESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEK 1149
Cdd:COG1196    238 EAELEELEAELEELEAEL-EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1150 NLRQAAEEATRKAQALqAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTL 1229
Cdd:COG1196    317 RLEELEEELAELEEEL-EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1230 QErLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRR 1309
Cdd:COG1196    396 AE-LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1310 LLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAAL 1389
Cdd:COG1196    475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVE 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1390 RGEMEKRLRLELTwqmqredfDRRLGELTT-ALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAA 1468
Cdd:COG1196    555 DDEVAAAAIEYLK--------AAKAGRATFlPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1469 ALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQdgfqQSTAELN 1548
Cdd:COG1196    627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL----EEALLAE 702

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035 1025 RALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQAd 1104
Cdd:COG1196    228 ELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR- 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1105 LDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQR--AKKELEKELAD 1182
Cdd:COG1196    307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAElaEAEEELEELAE 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1183 ANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEAS 1262
Cdd:COG1196    387 ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1263 AALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHA 1342
Cdd:COG1196    467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAA 546

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1343 IEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALR 1422
Cdd:COG1196    547 ALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1423 TAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQF 1502
Cdd:COG1196    627 LVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIVAS 1953
Cdd:COG3706      5 LVVDDDPTNRKLLRRLLEAAGYEVVEAADGEEALELLQEHRPDL--ILLDLEMPDMDGLELCRRLRADPRTadIPIIFLT 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIVAS 1953
Cdd:COG3437     10 LIVDDDPENLELLRQLLRTLGYDVVTAESGEEALELLLEAPPDL--ILLDVRMPGMDGFELLRLLRADPSTrdIPVIFLT 87

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035  761 REQAESALGQSKSETERQLAEATAALAEVRAQLEQATtassQREAEAKQAAAAQQQKLADQDAELKktwdnliKETEDRE 840
Cdd:COG1196    209 AEKAERYRELKEELKELEAELLLLKLRELEAELEELE----AELEELEAELEELEAELAELEAELE-------ELRLELE 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  841 ALEKQLAAARGDlERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSE 920
Cdd:COG1196    278 ELELELEEAQAE-EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  921 SARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAwKLANSATEQHAAELKTLLATAREELHAETA 1000
Cdd:COG1196    357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEL-EEAEEALLERLERLEEELEELEEALAELEE 435

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1001 KRDAAEAAASQVR---AELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKET 1077
Cdd:COG1196    436 EEEEEEEALEEAAeeeAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1078 -AARHETERELRESLTDAERTTEALQADLDAALKA--CEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQA 1154
Cdd:COG1196    516 lAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARG 595

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1155 AEEAtrkAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQrLAERLSEVQTLQERLR 1234
Cdd:COG1196    596 AIGA---AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG-GSAGGSLTGGSRRELL 671

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1235 SEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEE 1314
Cdd:COG1196    672 AALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGY---KVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIV 1951
Cdd:cd17536      1 VLIVDDEPLIREGLKKLIDWEELgfeVVGEAENGEEALELIEEHKPDI--VITDIRMPGMDGLELIEKIRELYPDIKIII 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNARDAMpsggtlkfsaENVVVDESFIHHRRATGAkpgnyVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16976      1 IQQVLMNLLQNALDAM----------GKVENPRIRIAARRLGGR-----LVLVVRDNGPGIAEEHLSRVFDPFFTTKPVG 65

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIVASGMGH- 1957
Cdd:cd17550      5 DDEEDIRESLSGILEDEGYEVDTAADGEEALKLIKERRPD--LVLLDIWLPDMDGLELLKEIKEKYPDLPVIMISGHGTi 82

                           90       100       110
                   ....*....|....*....|....*....|
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:COG2204      5 ILVVDDDPDIRRLLKELLERAGYEVETAASGEEALALLREEPPDL--VLLDLRMPGMDGLELLRELRALDPDLPVILLTG 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:cd17574      1 LVVEDDEEIAELLSDYLEKEGYEVDTAADGEEALELAREEQPDL--IILDVMLPGMDGFEVCRRLREKGSDIPIIMLTAK 78


                   ...
gi 1949443035 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 1949443035  621 RQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQpvrEQLAGEVQRGERAEAELFRSRSE 700
Cdd:COG1196    199 ERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELE---AELEELEAELAELEAELEELRLE 275

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  701 LETQQAALAELRARAEAAEAARLQVEttaqqsrtvaeqaaaeaqqqlaalrQQLQAETERREQAESALGQSKSEterqla 780
Cdd:COG1196    276 LEELELELEEAQAEEYELLAELARLE-------------------------QDIARLEERRRELEERLEELEEE------ 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  781 eataalaevRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAET 860
Cdd:COG1196    325 ---------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  861 KAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQ 940
Cdd:COG1196    396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  941 RLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELeatN 1020
Cdd:COG1196    476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI---V 552

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1021 AESSRALAAAQNELARESAERETteaEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEA 1100
Cdd:COG1196    553 VEDDEVAAAAIEYLKAAKAGRAT---FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVA 629

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1101 LQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEA-------TRKAQALQAELQRAK 1173
Cdd:COG1196    630 ARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERlaeeeleLEEALLAEEEEEREL 709

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035  571 RGEQETALAELRAQLERTEAARQ---QIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETER 647
Cdd:COG1196    195 LGELERQLEPLERQAEKAERYRElkeELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  648 QLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVET 727
Cdd:COG1196    275 ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  728 TAQQSRtvaeqaaaeaqqqlaalrqqlqaetERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEA 807
Cdd:COG1196    355 EAEAEL-------------------------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  808 KQAAAAQQQKLADQDAELkktwDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQ 887
Cdd:COG1196    410 EALLERLERLEEELEELE----EALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  888 TEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVE 967
Cdd:COG1196    486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  968 AAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAE 1047
Cdd:COG1196    566 LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1048 FQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETAR 1127
Cdd:COG1196    646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035   85 APAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLRNKDGSTRWVA 164
Cdd:cd00130      1 LPDGVIVLDLDGRILYANPAAEQLLGYSPEELIGKSLLDLIHPEDREELRERLENLLSGGEPVTLEVRLRRKDGSVIWVL 80

                           90       100
                   ....*....|....*....|...
gi 1949443035  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 1949443035 1724 DLP-LISADASQLHRVLLNLAVNArdampsggtLKFSAENVVVdESFIHHRRATgakpgnyVLFRVTDSGVGIPRDILPR 1802
Cdd:PRK11091   387 PLPhKVITDGTRLRQILWNLISNA---------VKFTQQGGVT-VRVRYEEGDM-------LTFEVEDSGIGIPEDELDK 449

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1803 IFEPFFTTKE-----PGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPA-ASAETSERPPQ-AELPRGNGELL 1875
Cdd:PRK11091   450 IFAMYYQVKDshggkPATGTGIGLAVSKRLAQAMGGDITVTSEEGKGSCFTLTIHApAVAEEVEDAFDeDDMPLPALNIL 529

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1575 LEDALQQSHGEVELRVSERTAglnahvqqleaELAEAQRAEEQLRHRRIEAVSTLAggmaHELNNVLAPVLMAAQLLRK- 1653
Cdd:PRK15347   362 LLDTLNEQYDTLENKVAERTQ-----------ALAEAKQRAEQANKRKSEHLTTIS----HEIRTPLNGVLGALELLQNt 426

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1654 QVSGKSRTLVDSVESSAQRGADIVKQVLTFAR------GFHGERAPVSP----EML---VRDIAKSVQ-ETFprnvrvss 1719
Cdd:PRK15347   427 PLTAEQMDLADTARQCTLSLLAIINNLLDFSRiesgqmTLSLEETALLPlldqAMLtiqGPAQSKSLTlRTF-------- 498

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1720 eVADDLPLISA-DASQLHRVLLNLAVNARDAMPSGGTlkfsaenvvvdesfihhrRATGAKPGNYVLFRVTDSGVGIPRD 1798
Cdd:PRK15347   499 -VGAHVPLYLHlDSLRLRQILVNLLGNAVKFTETGGI------------------RLRVKRHEQQLCFTVEDTGCGIDIQ 559

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1799 ILPRIFEPFFTTKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP------------AASAETSERP---- 1862
Cdd:PRK15347   560 QQQQIFTPFYQADTHSQGTGLGLTIASSLAKMMGGELTLFSTPGVGSCFSLVLPlneyappeplkgELSAPLALHRqlsa 639

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1863 ----PQAELPRG---NGELL----------------------------------MLADDEQGVLDVTAEILEWHGYKVLT 1901
Cdd:PRK15347   640 wgitCQPGHQNPallDPELAylpgrlydllqqiiqgapnepvinlplqpwqlqiLLVDDVETNRDIIGMMLVELGQQVTT 719

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1902 ARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRK----RDATLPIIV----ASGMGHEKfvtdLRELGVPLFL 1973
Cdd:PRK15347   720 AASGTEALELGRQHRFDL--VLMDIRMPGLDGLETTQLWRDdpnnLDPDCMIVAltanAAPEEIHR----CKKAGMNHYL 793

                          490
                   ....*....|...
gi 1949443035 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 1949443035 1607 ELAEAQRAEEQLRHR-----RIEA-VSTLAggmaHELNNVLAPVLMAAQLLRKQVSGKSRT-LVDSVESSAQRGADIVKQ 1679
Cdd:PRK11100   235 ELRELAQALESMRVKlegkaYVEQyVQTLT----HELKSPLAAIRGAAELLQEDPPPEDRArFTGNILTQSARLQQLIDR 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1680 VLTFA----RGFHGERAPVSPEMLVRDIAKSVQETFP-RNVRVSSEVADdlPLISADASQLHRVLLNLAVNARDAMPSGG 1754
Cdd:PRK11100   311 LLELArleqRQELEVLEPVALAALLEELVEAREAQAAaKGITLRLRPDD--ARVLGDPFLLRQALGNLLDNAIDFSPEGG 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1755 TLKFSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQ---SVGLGLATALGVVQSH 1831
Cdd:PRK11100   389 TITLSAE-----------------VDGEQVALSVEDQGPGIPDYALPRIFERFYSLPRPANgrkSTGLGLAFVREVARLH 451

                          250       260
                   ....*....|....*....|....
gi 1949443035 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 1949443035  834 KETEDREALEKQLAAARGDLERqLAETKAELDQQLAALAEARSQAER---------------------EAAERRQTEESL 892
Cdd:TIGR02168  169 KYKERRKETERKLERTRENLDR-LEDILNELERQLKSLERQAEKAERykelkaelrelelallvlrleELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  893 LQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAwKL 972
Cdd:TIGR02168  248 LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ-LE 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  973 ANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSK 1052
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLE 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1053 SALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTE 1132
Cdd:TIGR02168  407 ARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQ 486

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1133 FTHRLTAETGAREQLE---KNLRQAAEEATRKAQALQ--AELQRAKKELEKELADANLELLDirSRLDHEAAARRQAEES 1207
Cdd:TIGR02168  487 LQARLDSLERLQENLEgfsEGVKALLKNQSGLSGILGvlSELISVDEGYEAAIEAALGGRLQ--AVVVENLNAAKKAIAF 564

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1208 AKQGSA----------SADQRLAERLSEVQTLQERLRSEAAQRETTEVELR--------------DTRAALEKQ------ 1257
Cdd:TIGR02168  565 LKQNELgrvtflpldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAkklrpg 644

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1258 ---------LAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAAR 1328
Cdd:TIGR02168  645 yrivtldgdLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL 724

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1329 RAEVDRLtteqphAIEEATARLKAQLAEQEREREQLRLAAMSAE-QRLRDRATDFEAANAALRGEMEKRLRLELTWQMQR 1407
Cdd:TIGR02168  725 SRQISAL------RKDLARLEAEVEQLEERIAQLSKELTELEAEiEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1408 EDFDRRLGELTTALRTAEAKAgsdsAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTN 1487
Cdd:TIGR02168  799 KALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1488 LNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDrmrdaqdgfqqstaELNERLTRLTTDVEAARQQAEQ 1567
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--------------ELREKLAQLELRLEGLEVRIDN 940

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHaGDIKAVITDILMPFMDGVELCRELRKRDA--TLPIIVAS 1953
Cdd:cd17544      4 LVVDDSATSRNHLRALLRRHNFQVLEAANGQEALEVLEQH-PDIKLVITDYNMPEMDGFELVREIRKKYSrdQLAIIGIS 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17542      4 LIVDDAAFMRMMLKDILTKAGYEVVgEAANGEEAVEKYKELKPDL--VTMDITMPEMDGIEALKEIKKIDPNAKVIMCSA 81

                           90       100
                   ....*....|....*....|....*....
gi 1949443035 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 1949443035  515 QAGAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETaLAELRAQLERTEAARQQ 594
Cdd:COG1196    249 EELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER-RRELEERLEELEEELAE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  595 IETTALDLrsnsEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQ 674
Cdd:COG1196    328 LEEELEEL----EEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLE 403

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  675 PVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQL 754
Cdd:COG1196    404 ELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELL 483

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  755 QAETERREQAESALGQsksETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIK 834
Cdd:COG1196    484 EELAEAAARLLLLLEA---EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAA 560

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  835 ETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAR 914
Cdd:COG1196    561 AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAV 640

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  915 EALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREE 994
Cdd:COG1196    641 TLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEE 720

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  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 1949443035 1144 REQLEKNLRQAAEEATRkAQALQAELQRAKKELEKELADAN--LELLDIRSRLDHEAAARRQAEESAKQgsasadQRLAE 1221
Cdd:COG1196    174 KEEAERKLEATEENLER-LEDILGELERQLEPLERQAEKAEryRELKEELKELEAELLLLKLRELEAEL------EELEA 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1222 RLSEVQTLQERLrsEA--AQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATE 1299
Cdd:COG1196    247 ELEELEAELEEL--EAelAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1300 SGSALEVTRRLLNEERAARASALAELAARRAEVDRLtteqpHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRA 1379
Cdd:COG1196    325 LAELEEELEELEEELEELEEELEEAEEELEEAEAEL-----AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELA 399

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1380 TDFEAANAALRGEMEKRLRLELTWQMQREDfDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSE 1459
Cdd:COG1196    400 AQLEELEEAEEALLERLERLEEELEELEEA-LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1460 LASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLN-RQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQD 1538
Cdd:COG1196    479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGlRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEV 558

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1539 GFQQ---STAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEAQRAE 1615
Cdd:COG1196    559 AAAAieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638

                          490
                   ....*....|....*..
gi 1949443035 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 1949443035  225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEK 304
Cdd:COG1196    236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  305 AELEKRTasspAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:COG1196    316 ERLEELE----EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  385 ---RVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAgQGGGEVNPELAARI 461
Cdd:COG1196    392 lraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-EEEALLELLAELLE 470

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  462 AALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQr 541
Cdd:COG1196    471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ- 549

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  542 feQRVAELETDNQQLREQASRDTQAATTQRgeqetALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADAR 621
Cdd:COG1196    550 --NIVVEDDEVAAAAIEYLKAAKAGRATFL-----PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL 622

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  622 QQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSEL 701
Cdd:COG1196    623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  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 1949443035   98 ILFVNHRWSALTGRSQAESQGFG--WLLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLRNKDGSTRWVAGHAMRVLDDHE 175
Cdd:pfam08447    1 IIYWSPRFEEILGYTPEELLGKGesWLDLVHPDDRERVREALWEALKGGEPYSGEYRIRRKDGEYRWVEARARPIRDENG 80


                   ....*....
gi 1949443035  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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD--ATLPIIVAS 1953
Cdd:cd17580      2 LVVDDNEDAAEMLALLLELEGAEVTTAHSGEEALEAAQRFRPDV--ILSDIGMPGMDGYELARRLRELPwlANTPAIALT 79

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1949443035 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 1949443035  873 EARSQAEREAAERRQTEESLLQASRSSEERVALlASELEAAREALRSESARREEletalPKTKTELGQRLAEAAAEAAGL 952
Cdd:PTZ00121  1091 EATEEAFGKAEEAKKTETGKAEEARKAEEAKKK-AEDARKAEEARKAEDARKAE-----EARKAEDAKRVEIARKAEDAR 1164

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  953 RARMDFEAAERERVEAAWKlansateqhAAELKTllatAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQN 1032
Cdd:PTZ00121  1165 KAEEARKAEDAKKAEAARK---------AEEVRK----AEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1033 ELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELREsltdAERTTEALQADLDAALKAC 1112
Cdd:PTZ00121  1232 AEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE----KKKADEAKKAEEKKKADEA 1307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1113 EEEAARRSQAEETARQshtefthrltAETGAREQLEknLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRS 1192
Cdd:PTZ00121  1308 KKKAEEAKKADEAKKK----------AEEAKKKADA--AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEE 1375

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1193 RLDHEAAARRQAEESAK----QGSASADQRLAERLSEVQtlQERLRSEAAQRETTEVElrdtRAALEKQLAEASAALREA 1268
Cdd:PTZ00121  1376 AKKKADAAKKKAEEKKKadeaKKKAEEDKKKADELKKAA--AAKKKADEAKKKAEEKK----KADEAKKKAEEAKKADEA 1449

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1269 SARLEQERderrrvvesltqTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATA 1348
Cdd:PTZ00121  1450 KKKAEEAK------------KAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK 1517

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1349 RLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTA--LRTAEA 1426
Cdd:PTZ00121  1518 AEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAeeARIEEV 1597

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1427 KAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRV 1506
Cdd:PTZ00121  1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKA 1677

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1507 AELDSTE--ARLREECAHRERAEA-ELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQEttqRRSLEdalqqsh 1583
Cdd:PTZ00121  1678 EEAKKAEedEKKAAEALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEED---KKKAE------- 1747

                          730       740       750
                   ....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1419 TALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTT-AELQTNLNAARAELDM 1497
Cdd:PRK11466   209 SALRVQQMVMNLGLEQIQKNAPTLEKQLNNAVKILQRRQIRIEDPGVRAQVATTLTTVSQYSDlLALYQQDSEISNHLQT 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1498 LNR----QFAQRVAEL----DSTEARLREECAHRERAEAE-----------------LDRMRDAQDGFQQSTAELNERLT 1552
Cdd:PRK11466   289 LAQnniaQFAQFSSEVsqlvDTIELRNQHGLAHLEKASARgqysllllgmvslcaliLILWRVVYRSVTRPLAEQTQALQ 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1553 RLTT-DVEAARQQA----EQETTQR-----RSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEAQRAEEqlrhrr 1622
Cdd:PRK11466   369 RLLDgDIDSPFPETagvrELDTIGRlmdafRSNVHALNRHREQLAAQVKARTAELQELVIEHRQARAEAEKASQ------ 442

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1623 ieAVSTLAGGMAHELNNVLAPVLMAAQLL-RKQVSGKSRTLVDSVESSAQRGADIVKQVLTFARGFHGERA------PVS 1695
Cdd:PRK11466   443 --AKSAFLAAMSHEIRTPLYGILGTAQLLaDNPALNAQRDDLRAITDSGESLLTILNDILDYSAIEAGGKNvsvsdePFE 520

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1696 PEMLVRDIAKSVQETF-PRNVRVSSEVADDLP-LISADASQLHRVLLNLAVNArdampsggtLKFSAENVVVDESFIHhr 1773
Cdd:PRK11466   521 PRPLLESTLQLMSGRVkGRPIRLATDIADDLPtALMGDPRRIRQVITNLLSNA---------LRFTDEGSIVLRSRTD-- 589

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1774 ratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLPA 1853
Cdd:PRK11466   590 -------GEQWLVEVEDSGCGIDPAKLAEIFQPFVQVSGKRGGTGLGLTISSRLAQAMGGELSATSTPEVGSCFCLRLPL 662

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1854 ASAETSERPPQAELPRGNGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYdQHAGDIKAVITDILMPFMDG 1933
Cdd:PRK11466   663 RVATAPVPKTVNQAVRLDGLRLLLIEDNPLTQRITAEMLNTSGAQVVAVGNAAQALETL-QNSEPFAAALVDFDLPDYDG 741

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1523 RERAEAELDRMRDAQDGFQQSTAE---LNERLTRLTTDVEAARQQAEQETTQRRSLE---DALQQSHGEVELRVSERTAG 1596
Cdd:COG3290     72 LLKLLEEIARLVEEREAVLESIREgviAVDRDGRITLINDAARRLLGLDAIGRPIDEvlaEVLETGERDEEILLNGRVLV 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1597 LNAHVQQLEAELAEA-----QRAEEQLRHRRIEAVSTLAGGM---AHELNNVLAPVLMAAQLLRKQvsgKSRTLVDSVES 1668
Cdd:COG3290    152 VNRVPIRDDGRVVGAvatfrDRTELERLEEELEGVKELAEALraqRHDFRNHLHTISGLLQLGEYD---EALEYIDEISE 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1669 SAQrgadivkQVLTFARGFHGERAPVSpemLVRDIAKSVQEtfpRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARD 1748
Cdd:COG3290    229 ELQ-------ELIDSLLSRIGNPVLAA---LLLGKAARARE---RGIDLTIDIDSDLPDLPLSDTDLVTILGNLLDNAIE 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1749 AmpsggTLKFSAENVVVDESFIHHrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSvGLGLATALGVV 1828
Cdd:COG3290    296 A-----VEKLPEEERRVELSIRDD--------GDELVIEVEDSGPGIPEELLEKIFERGFSTKLGEGR-GLGLALVKQIV 361

                          330       340
                   ....*....|....*....|....*...
gi 1949443035 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 1949443035  519 GRSEADEAARAQVEAD--LRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIE 596
Cdd:PTZ00121  1054 GNHEGKAEAKAHVGQDegLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEA 1133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  597 TTALDLRSNSEQQLSETQRQLADARQQLQA---ESERRAQAESALGQSKSETERQLAEATAALADTRKQleEATTKAAEL 673
Cdd:PTZ00121  1134 RKAEDARKAEEARKAEDAKRVEIARKAEDArkaEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA--EAARKAEEE 1211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  674 QPVRE-------QLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRtvaeqAAAEAQQQ 746
Cdd:PTZ00121  1212 RKAEEarkaedaKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR-----KADELKKA 1286

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  747 LAALRQQLQAETERREQAESAlgQSKSETERQLAEATAALAEVRAQLEQA-TTASSQREAEAKQAAAAQQQKLADQDAEL 825
Cdd:PTZ00121  1287 EEKKKADEAKKAEEKKKADEA--KKKAEEAKKADEAKKKAEEAKKKADAAkKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  826 KKTWDNLIKETEDREALEKQLAAA---RGDLERQLAETKAELDQQLAALAEARSQAE---REAAERRQTEESLLQA--SR 897
Cdd:PTZ00121  1365 KAEAAEKKKEEAKKKADAAKKKAEekkKADEAKKKAEEDKKKADELKKAAAAKKKADeakKKAEEKKKADEAKKKAeeAK 1444

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  898 SSEErvalLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRArmdfEAAERERVEAAWKLANSAT 977
Cdd:PTZ00121  1445 KADE----AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK----KADEAKKAAEAKKKADEAK 1516

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  978 EQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQ 1057
Cdd:PTZ00121  1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1058 QLAEAAAAQAELRSRLEKETAARHETE--RELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEfth 1135
Cdd:PTZ00121  1597 VMKLYEEEKKMKAEEAKKAEEAKIKAEelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED--- 1673

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1136 RLTAETGAREQLEKnlRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASA 1215
Cdd:PTZ00121  1674 KKKAEEAKKAEEDE--KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNARDAMPSGGtlkfsaenvvvDESFIHHRRATGAKPGnYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16920      1 IQQVLINLVRNGIEAMSEGG-----------CERRELTIRTSPADDR-AVTISVKDTGPGIAEEVAGQLFDPFYTTKSEG 68

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035 1877 LADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMG 1956
Cdd:cd17549      3 LVDDDADVREALQQTLELAGFRVRAFADAEEALAALSPDFPGV--VISDIRMPGMDGLELLAQIRELDPDLPVILITGHG 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1891 ILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD--ATLPIIVASGMGHEKFVTDLRELG 1968
Cdd:cd17598     17 ILEEQGYKVQVARNGREALAMLAEHRPTL--VISDIVMPEMDGYELCRKIKSDPdlKDIPVILLTTLSDPRDVIRGLECG 94

                           90
                   ....*....|....*....
gi 1949443035 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 1949443035 1738 VLLNLAVNArdampsggtLKFSAENVVvdesFIHHRRATGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFF-----TTKE 1812
Cdd:cd16922      4 ILLNLLGNA---------IKFTEEGEV----TLRVSLEEEEEDGVQLRFSVEDTGIGIPEEQQARLFEPFSqadssTTRK 70

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDqhAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17554      3 ILVVDDEENIRELYKEELEDEGYEVVTAGNGEEALEKLE--SEDPDLVILDIKMPGMDGLETLRKIREKKPDLPVIICTA 80


                   ....*
gi 1949443035 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 1949443035  189 ERKVADDTRTTDQAAALDAALARVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGEL 268
Cdd:COG1196    284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  269 DKQVAErtatftdiisgLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDfdk 348
Cdd:COG1196    364 EEALLE-----------AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA--- 429

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  349 LQSSATQPDTALETVHHRLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELE 428
Cdd:COG1196    430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  429 RTKEELVAESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQ 508
Cdd:COG1196    510 VKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALA 589

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  509 QLAAASQAGAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAEL----RAQ 584
Cdd:COG1196    590 AALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLtggsRRE 669

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  585 LERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLE 664
Cdd:COG1196    670 LLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLE 749

                          490       500       510
                   ....*....|....*....|....*....|
gi 1949443035  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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd17614      1 ILVVDDEKPISDILKFNLTKEGYEVVTAYDGREALEKVEEEQPDL--ILLDLMLPEKDGLEVCREVRKT-SNVPIIMLTA 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD---ATLPIIV 1951
Cdd:cd17546      1 VLVVDDNPVNRKVLKKLLEKLGYEVDVAENGQEALELLKEEPFDL--VLMDLQMPVMDGLEATRRIRELEgggRRTPIIA 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIvasgmg 1956
Cdd:cd19920      5 DDVPDNLRLLSELLRAAGYRVLVATDGQQALQRAQAEPPDL--ILLDVMMPGMDGFEVCRRLKADPATrhIPVI------ 76

                           90       100       110
                   ....*....|....*....|....*....|
gi 1949443035 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 1949443035 1873 ELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKrDATLPIIVA 1952
Cdd:CHL00148     7 EKILVVDDEAYIRKILETRLSIIGYEVITASDGEEALKLFRKEQPDL--VILDVMMPKLDGYGVCQEIRK-ESDVPIIML 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035  575 ETALAELRAQLERTEAARQQIETtALDLRsnseQQLSETQRQLADAR-QQLQAESERRAQAESALGQSKSETERQLAEAT 653
Cdd:TIGR02168  192 EDILNELERQLKSLERQAEKAER-YKELK----AELRELELALLVLRlEELREELEELQEELKEAEEELEELTAELQELE 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  654 AALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRAraeaaeaarlqvetTAQQSR 733
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE--------------ELESKL 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  734 TVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAeakqaaaa 813
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER-------- 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  814 qqqkladQDAELKKTWDNLIKETEDREALEKQLA-AARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESL 892
Cdd:TIGR02168  405 -------LEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQAL 477

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  893 LQASRSSEERVALLASeLEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARmdfEAAERERVEA---- 968
Cdd:TIGR02168  478 DAAERELAQLQARLDS-LERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAI---EAALGGRLQAvvve 553

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  969 ---AWKLANSATEQHAAELKTLLA---TAREELHAETAKRDAAEAAASQVRAELEATNAESSRALA------------AA 1030
Cdd:TIGR02168  554 nlnAAKKAIAFLKQNELGRVTFLPldsIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvvddlDN 633

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1031 QNELARESAERE---TTEAEFQRSK---SALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQAD 1104
Cdd:TIGR02168  634 ALELAKKLRPGYrivTLDGDLVRPGgviTGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEE 713

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1105 LDAALKACEEEAARRSQAEE---TARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATrKAQALQAELQRAKKELEKELA 1181
Cdd:TIGR02168  714 LEQLRKELEELSRQISALRKdlaRLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEAQIE 792

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1182 DANLELLDIRSRLDheaAARRQAeesakqgsasadQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEA 1261
Cdd:TIGR02168  793 QLKEELKALREALD---ELRAEL------------TLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1262 SAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASAlaelaarraevdRLTTEQPH 1341
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL------------EELREKLA 925

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1342 AIEEATARLKAQLAE-QEREREQLRLAAMSAEQRLRDRATDFEAANAALrgemeKRLRLELTwqmqredfdrRLGELT-T 1419
Cdd:TIGR02168  926 QLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDDEEEARRRL-----KRLENKIK----------ELGPVNlA 990

                          890       900       910       920
                   ....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035  225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAvaehELAVKTLQAEK 304
Cdd:TIGR02168  271 ELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDEL----AEELAELEEKL 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  305 AELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:TIGR02168  347 EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEEL 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  385 RVALQteheKAERADAERELSEEAMVQTNTgiQQRLMELNAELERTKEELVAESARRTQAEAGQGggevnpELAARIAAL 464
Cdd:TIGR02168  427 LKKLE----EAELKELQAELEELEEELEEL--QEELERLEEALEELREELEEAEQALDAAERELA------QLQARLDSL 494

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  465 TEAKAQVEKElveqQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEA-----DEAARAQVEADLRAAh 539
Cdd:TIGR02168  495 ERLQENLEGF----SEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvvenLNAAKKAIAFLKQNE- 569

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  540 qrfEQRVAELETDNQQLREQASRDTQAATTQRG------EQETALAELRAQLE-----------RTEAARQQIETTALDL 602
Cdd:TIGR02168  570 ---LGRVTFLPLDSIKGTEIQGNDREILKNIEGflgvakDLVKFDPKLRKALSyllggvlvvddLDNALELAKKLRPGYR 646

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  603 ------------------RSNSEQQLSETQRQLADARQQLQAESERRAQAESALgqskSETERQLAEATAALADTRKQLE 664
Cdd:TIGR02168  647 ivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKAL----AELRKELEELEEELEQLRKELE 722

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  665 EATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQ 744
Cdd:TIGR02168  723 ELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  745 QQLAALRQQLQAETERREQAESALGQSKSETERqlaeataalaevraqLEQATTASSQREAEAKQAAAAQQQKLADQDAE 824
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAA---------------TERRLEDLEEQIEELSEDIESLAAEIEELEEL 867

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  825 LKKTWDNLIKETEDREALEKQLAAARGDLE------RQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRS 898
Cdd:TIGR02168  868 IEELESELEALLNERASLEEALALLRSELEelseelRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSE 947

                          730       740       750
                   ....*....|....*....|....*....|....
gi 1949443035  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 1949443035   37 VAVVKDTLFLAAGTVGLFLLLRRDIQKREQTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAES 116
Cdd:COG2202     98 VELSISPVRDEDGEITGFVGIARDITERKRAEEALRESEERLRLLVENAPDGIFVLDLDGRILYVNPAAEELLGYSPEEL 177

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949443035  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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQhAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd18160      2 ILLADDEPSVRKFIVTTLKKAGYAVTEAESGAEALEKLQQ-GKDIDIVVTDIVMPEMDGIELAREARKIDPDVKILFISG 80

                           90       100
                   ....*....|....*....|...
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNARDAMP-SGGTLKFSAEnvvvdesfiHHRRATGAKPGNYVLFRVT--DSGVGIPRDILPRIFEPFFTTK 1811
Cdd:cd16918      1 LIQVFLNLVRNAAQALAgSGGEIILRTR---------TQRQVTLGHPRHRLALRVSviDNGPGIPPDLQDTIFYPMVSGR 71

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1074 EKETAARHETERELRESLtdaerttealqADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKnLRQ 1153
Cdd:PRK02224   198 EKEEKDLHERLNGLESEL-----------AELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIED-LRE 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1154 AAEEATRKAQALQAELQRAKKELEkELADANLELLDI--RSRLDHEAAARRQAEESAKqgsasaDQRLAERLSEVQTLQ- 1230
Cdd:PRK02224   266 TIAETEREREELAEEVRDLRERLE-ELEEERDDLLAEagLDDADAEAVEARREELEDR------DEELRDRLEECRVAAq 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1231 ------ERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSAL 1304
Cdd:PRK02224   339 ahneeaESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELR 418

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1305 EVTRRLLNEERAARASALAELAARRAEVDRLTT-----------EQPHAieEATARLKAQLAEQEREREQLRLAAMSAEQ 1373
Cdd:PRK02224   419 EERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpveGSPHV--ETIEEDRERVEELEAELEDLEEEVEEVEE 496

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1374 RLrDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRR------LGELTTALRTAEAKAGSDSAELRHAHETLQQAHA 1447
Cdd:PRK02224   497 RL-ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKreraeeLRERAAELEAEAEEKREAAAEAEEEAEEAREEVA 575

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1448 ELTRRLTERDSE---LASVREQAAALDAAGTRAQqttaelqtNLNAARAELDMLNRQFAQRVAELDSTEARLREEC--AH 1522
Cdd:PRK02224   576 ELNSKLAELKERiesLERIRTLLAAIADAEDEIE--------RLREKREALAELNDERRERLAEKRERKRELEAEFdeAR 647

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1523 RERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQettqrrslEDALQQSHGEVELRVsERTAGLNAHVQ 1602
Cdd:PRK02224   648 IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEE--------LEELRERREALENRV-EALEALYDEAE 718

                          570       580
                   ....*....|....*....|....*..
gi 1949443035 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 1949443035  225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEK 304
Cdd:COG1196    299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  305 AELEKRTAsspAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:COG1196    379 EELEELAE---ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  385 RVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPELAARIAAL 464
Cdd:COG1196    456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAA 535

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  465 TEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAA--AARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQRF 542
Cdd:COG1196    536 YEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgrATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARY 615

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  543 EQRVAEL--ETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADA 620
Cdd:COG1196    616 YVLGDTLlgRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELEL 695

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  621 RQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSE 700
Cdd:COG1196    696 EEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLERE 775


                   ..
gi 1949443035  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 1949443035 1575 LEDALQQSHG----EVELRVSERTAGLNAHVQQLE-----AELA--EAQR--AEEQLRHRRIEAVSTLAGGMAHELNNVL 1641
Cdd:PRK11073    66 MRESLQAGQGftdnEVTLVIDGRSHILSLTAQRLPegmilLEMApmDNQRrlSQEQLQHAQQVAARDLVRGLAHEIKNPL 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1642 APVLMAAQLLRKQVSGKSRTLVDSV-ESSAQRGADIVKQVLTFARgfHGERAPVSPEMLVRDIAKSVQETFPRNVRVSSE 1720
Cdd:PRK11073   146 GGLRGAAQLLSKALPDPALTEYTKViIEQADRLRNLVDRLLGPQR--PGTHVTESIHKVAERVVQLVSLELPDNVRLIRD 223

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1721 VADDLPLISADASQLHRVLLNLAVNARDAM-PSGGTLKFSAENVVvdESFIHHRRatgakpgnYVL---FRVTDSGVGIP 1796
Cdd:PRK11073   224 YDPSLPELAHDPDQIEQVLLNIVRNALQALgPEGGTITLRTRTAF--QLTLHGER--------YRLaarIDIEDNGPGIP 293

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035 1701 RDIAKSVQETFPrnvrvssevadDLPLISADASQLHRVLLNLAVNArdampsggtLKFSAENVV-VDESFIHhrratgaK 1779
Cdd:PRK09959   806 KSIALSCSSTFP-----------DHYLVKIDPQAFKQVLSNLLSNA---------LKFTTEGAVkITTSLGH-------I 858

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1780 PGNYVLFRVT--DSGVGIPRDILPRIFEPFFTTKEPGQSVG--LGLATALGVVQSHGGFILLETEEDKGTEFQIYLP--- 1852
Cdd:PRK09959   859 DDNHAVIKMTimDSGSGLSQEEQQQLFKRYSQTSAGRQQTGsgLGLMICKELIKNMQGDLSLESHPGIGTTFTITIPvei 938

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1853 ----AASAETSERPpqAELPRGNGelLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILM 1928
Cdd:PRK09959   939 sqqvATVEAKAEQP--ITLPEKLS--ILIADDHPTNRLLLKRQLNLLGYDVDEATDGVQALHKVSMQHYDL--LITDVNM 1012

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17627      1 ILVVDDDRAVRESLRRSLRFEGYEVETAVDGAEALRVISGNRPD--AVVLDVMMPRLDGLEVCRRLRAAGNDLPILVLTA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIva 1952
Cdd:cd17538      2 ILVVDDEPANRELLEALLSAEGYEVLTADSGQEALALAEEELPDL--ILLDVMMPGMDGFEVCRRLKEDPETrhIPVI-- 77

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1949443035 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 1949443035 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 1949443035   66 QTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEK 145
Cdd:COG2202      1 TAEEALEESERRLRALVESSPDAIIITDLDGRILYVNPAFERLTGYSAEELLGKTLRDLLPPEDDDEFLELLRAALAGGG 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1949443035  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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELR--KRDATLPIIVAS 1953
Cdd:cd19937      1 LVVDDEEDIVELLKYNLEKEGYEVVTAYDGEEALKRAKDEKPDL--IILDLMLPGIDGLEVCRILRsdPKTSSIPIIMLT 78

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIKAVITDILMPFMDGVELCRELRKrDATLPIIVASGM 1955
Cdd:cd17584      2 LVVDDDPTCLAILKRMLLRCGYQVTTCTDAEEALSMLRENKDEFDLVITDVHMPDMDGFEFLELIRL-EMDLPVIMMSAD 80

                           90       100
                   ....*....|....*....|....*..
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILE-WHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVAS 1953
Cdd:COG4565      7 LIVEDDPMVAELLRRYLErLPGFEVVgVASSGEEALALLAEHRPDL--ILLDIYLPDGDGLELLRELRARGPDVDVIVIT 84

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1949443035 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 1949443035  421 MELNAELERTKEEL-VAESARRTQAEAGQgggevnpelAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEA 499
Cdd:PTZ00121  1084 KEDNRADEATEEAFgKAEEAKKTETGKAE---------EARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRV 1154

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  500 AAARAALEQQLAAASQAGAGRSEADEAARAqvEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALA 579
Cdd:PTZ00121  1155 EIARKAEDARKAEEARKAEDAKKAEAARKA--EEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKA 1232

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  580 ElRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLAD--ARQQLQAESERRAQAESALGQSKSETERQLAEATAALA 657
Cdd:PTZ00121  1233 E-EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAikAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKA 1311

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  658 DTRKQLEEATTKAAELQPVREQLAGEVQ----RGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSR 733
Cdd:PTZ00121  1312 EEAKKADEAKKKAEEAKKKADAAKKKAEeakkAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  734 TVAEQAAAEAQQQLAALRQQLQAETERR--EQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAA 811
Cdd:PTZ00121  1392 KADEAKKKAEEDKKKADELKKAAAAKKKadEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK 1471

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  812 AAQqqklADQDAELKKTWDNLIKETEDrealekqlAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEEs 891
Cdd:PTZ00121  1472 ADE----AKKKAEEAKKADEAKKKAEE--------AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADE- 1538

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  892 llqASRSSEERVA---LLASELEAAREALRSESARREELETALPKTKTELGQRLAEA--AAEAAGLRARMDFEAAERERV 966
Cdd:PTZ00121  1539 ---AKKAEEKKKAdelKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAriEEVMKLYEEEKKMKAEEAKKA 1615

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  967 EAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALA------------------ 1028
Cdd:PTZ00121  1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeakkaeedekkaaealk 1695

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1029 -----AAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQA 1103
Cdd:PTZ00121  1696 keaeeAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRK 1775

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1104 DLDAALKAC--EEEAARRSQAEETARQSHTEFThrLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAK-KELEKEL 1180
Cdd:PTZ00121  1776 EKEAVIEEEldEEDEKRRMEVDKKIKDIFDNFA--NIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEaDAFEKHK 1853


                   ....*.
gi 1949443035 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 1949443035  225 ELERRADELKK------RDSELESANRQLWAELSGR--EQVEAELAKARGELDKQVAERTAtftdiisgLEKAVAEHELA 296
Cdd:TIGR02168  197 ELERQLKSLERqaekaeRYKELKAELRELELALLVLrlEELREELEELQEELKEAEEELEE--------LTAELQELEEK 268

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  297 VKTLQAEKAELEKRTASSPAELEALRKRLSDeatrrqlAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKR 376
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQKELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  377 LETELESLRVALQTEHEKAERADAERELSEEAMVQtntgIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPE 456
Cdd:TIGR02168  342 LEEKLEELKEELESLEAELEELEAELEELESRLEE----LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  457 -LAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADL 535
Cdd:TIGR02168  418 rLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  536 RAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQ---ETALAELRAQL--ERTEAARQQIET------------- 597
Cdd:TIGR02168  498 QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEaaiEAALGGRLQAVvvENLNAAKKAIAFlkqnelgrvtflp 577

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  598 ----TALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETErqLAEATAALADTRKQL---------- 663
Cdd:TIGR02168  578 ldsiKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD--LDNALELAKKLRPGYrivtldgdlv 655

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  664 ----------EEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSR 733
Cdd:TIGR02168  656 rpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  734 TVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQreaeakqaaaa 813
Cdd:TIGR02168  736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREA----------- 804

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  814 qqqkLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERqLAETKAELDQQLAALAEARSQAEREAAERRQTEESLL 893
Cdd:TIGR02168  805 ----LDELRAELTLLNEEAANLRERLESLERRIAATERRLED-LEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879

                          730       740       750       760
                   ....*....|....*....|....*....|....*....|....*..
gi 1949443035  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 1949443035  532 EADLRAAHQRFEQRVAELETDNQQLREqasrdtqaATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNseqqLS 611
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKE--------AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE----LY 291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  612 ETQRQLADARQQLQAESERRAQAEsalgqskseteRQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAE 691
Cdd:TIGR02168  292 ALANEISRLEQQKQILRERLANLE-----------RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  692 AELFRSRSELETQQAALAEL-RARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQ 770
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQlETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  771 SKSETERQLAEATAALAEVRAQLEQAtTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAAR 850
Cdd:TIGR02168  441 ELEELEEELEELQEELERLEEALEEL-REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLS 519

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  851 GDLER--QLAETKAELDQQLAALAEARSQA--EREAAERRQTEESLLQASRSseeRVALLASELEAAREALRSESARRE- 925
Cdd:TIGR02168  520 GILGVlsELISVDEGYEAAIEAALGGRLQAvvVENLNAAKKAIAFLKQNELG---RVTFLPLDSIKGTEIQGNDREILKn 596

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  926 ---------ELETALPKTKTELG---------QRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHA------ 981
Cdd:TIGR02168  597 iegflgvakDLVKFDPKLRKALSyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSsilerr 676

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  982 ---AELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNA---ESSRALAAAQNELARESAERETTEAEFQRsksaL 1055
Cdd:TIGR02168  677 reiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKeleELSRQISALRKDLARLEAEVEQLEERIAQ----L 752

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1056 AQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQAdLDAALKACEEEAARRSQAEETARQSHTEFTH 1135
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-LREALDELRAELTLLNEEAANLRERLESLER 831

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1136 RLTAETGAREQLEKNLRQAAEEATR------KAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAK 1209
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESlaaeieELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRS 911

                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035  757 ETERREQAESALGQSKSETERQLAEATAALAEVRaQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKET 836
Cdd:PTZ00121  1107 ETGKAEEARKAEEAKKKAEDARKAEEARKAEDAR-KAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE 1185

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  837 EDREALEKQLAA-ARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEEsllQASRSSEERVALLASELEAAR- 914
Cdd:PTZ00121  1186 EVRKAEELRKAEdARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAE---EAKKAEEERNNEEIRKFEEARm 1262

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  915 -------EALRSESARR-EELETALPKTKTElgqrlAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQhAAELKT 986
Cdd:PTZ00121  1263 ahfarrqAAIKAEEARKaDELKKAEEKKKAD-----EAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKK-ADAAKK 1336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  987 LLATAREElhAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAErETTEAEFQRSKSALAQQLAEAAAAQ 1066
Cdd:PTZ00121  1337 KAEEAKKA--AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKKADEAKKKAEEDKKKADELKKA 1413

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1067 AELRSRLEkETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQ 1146
Cdd:PTZ00121  1414 AAAKKKAD-EAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKA 1492

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1147 LE-----KNLRQAAEEATRKAQALQAELQRAKKELEKelADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAE 1221
Cdd:PTZ00121  1493 EEakkkaDEAKKAAEAKKKADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAK 1570

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1222 RLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQL-AEASAALREASARLEQER--DERRRVVESLTQTSTTLEARAT 1298
Cdd:PTZ00121  1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMkAEEAKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAE 1650

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1299 ESGSALEVTR-RLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATAR----LKAQLAEQEREREQLRLA----AM 1369
Cdd:PTZ00121  1651 ELKKAEEENKiKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKkaeeLKKKEAEEKKKAEELKKAeeenKI 1730

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035  366 RLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEEL--VAESARRTQ 443
Cdd:TIGR02168  180 KLERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRLEELREELEELQEELkeAEEELEELT 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  444 AEAGQGGGEVNpELAARIAALTEAKAQVEKELVEQQA------VAKALGDERNRLAQELAEAAAARAALEQQLAAASQAG 517
Cdd:TIGR02168  260 AELQELEEKLE-ELRLEVSELEEEIEELQKELYALANeisrleQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  518 AGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQ--ASRDTQAATTQRGEQETA-LAELRAQLERTEAARQQ 594
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQleTLRSKVAQLELQIASLNNeIERLEARLERLEDRRER 418

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  595 IETTALDLRSN-SEQQLSETQRQLADARQQLQAESERRAQAESALgqskSETERQLAEATAALADTRKQLEEATTKAAEL 673
Cdd:TIGR02168  419 LQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEAL----EELREELEEAEQALDAAERELAQLQARLDSL 494

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  674 QPVREQLAGEvQRGERAE--------------AELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTvAEQA 739
Cdd:TIGR02168  495 ERLQENLEGF-SEGVKALlknqsglsgilgvlSELISVDEGYEAAIEAALGGRLQAVVVENLNAAKKAIAFLKQN-ELGR 572

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  740 AAEAQQQLAALRQQLQAETERREQAESALGQSKSETErqlaEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLA 819
Cdd:TIGR02168  573 VTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVK----FDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIV 648

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  820 DQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAETK---AELDQQLAALAEARSQAEREAAERRQTEESLLQAS 896
Cdd:TIGR02168  649 TLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEekiAELEKALAELRKELEELEEELEQLRKELEELSRQI 728

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  897 RSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAglrarmdfEAAERERVEAAWKLANSA 976
Cdd:TIGR02168  729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA--------EIEELEAQIEQLKEELKA 800

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  977 TEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATnAESSRALAAAQNELARESAERETTEAEFQRSKSALA 1056
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL-EEQIEELSEDIESLAAEIEELEELIEELESELEALL 879

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1057 QQLAEAAAAQAELRSRLEKETAARHETERELREsltdaerttealqadLDAALKACEEEAARRSQAEETARQSHTEFTHR 1136
Cdd:TIGR02168  880 NERASLEEALALLRSELEELSEELRELESKRSE---------------LRRELEELREKLAQLELRLEGLEVRIDNLQER 944

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATlPIIVAS 1953
Cdd:cd19932      3 VLIAEDEALIRMDLREMLEEAGYEVVgEASDGEEAVELAKKHKPDL--VIMDVKMPRLDGIEAAKIITSENIA-PIVLLT 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILE-WHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVAS 1953
Cdd:cd17535      2 LIVDDHPLVREGLRRLLEsEPDIEVVgEAADGEEALALLRELRPDV--VLMDLSMPGMDGIEALRRLRRRYPDLKVIVLT 79

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 1731 DASQLHRVLLNLAVNARDAMPSGGTLKFSAEnvvvdesfihhrratgAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTT 1810
Cdd:cd16925      1 DAEKYERVVLNLLSNAFKFTPDGGRIRCILE----------------KFRLNRFLLTVSDSGPGIPPNLREEIFERFRQG 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNArdampsggtLKFSAENVVVDesfihhrratGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16949      1 LARALENVLRNA---------LRYSPSKILLD----------ISQDGDQWTITITDDGPGVPEDQLEQIFLPFYRVDSAR 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035  189 ERKVADDTRTTDQAAALDAALaRVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAElSGREQVEAELAKARGEL 268
Cdd:PTZ00121  1192 ELRKAEDARKAEAARKAEEER-KAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE-EIRKFEEARMAHFARRQ 1269

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  269 DKQVAERTATFTDIISGLEKAVAEHelAVKTLQAEKAELEKRTASSPAELEALRKRlSDEATRRQlaeddlrslredfDK 348
Cdd:PTZ00121  1270 AAIKAEEARKADELKKAEEKKKADE--AKKAEEKKKADEAKKKAEEAKKADEAKKK-AEEAKKKA-------------DA 1333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  349 LQSSATQPDTALETVHHRLHAETERVKRLETELESLRvaLQTEHEKaERADAERELSEEamVQTNTGIQQRLMELNAELE 428
Cdd:PTZ00121  1334 AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE--KKKEEAK-KKADAAKKKAEE--KKKADEAKKKAEEDKKKAD 1408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  429 RTKEelvAESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGD--ERNRLAQELAEAAAARAAL 506
Cdd:PTZ00121  1409 ELKK---AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKA 1485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  507 EQQLAAASQAGAGRSEADEAARAQVEADlraahqrfEQRVAELETDNQQLReQASRDTQAATTQRGEQETALAELRA--Q 584
Cdd:PTZ00121  1486 DEAKKKAEEAKKKADEAKKAAEAKKKAD--------EAKKAEEAKKADEAK-KAEEAKKADEAKKAEEKKKADELKKaeE 1556

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  585 LERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLE 664
Cdd:PTZ00121  1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  665 EATTKAAELQPVREQLAGEVQRGERAEAELFRSRSEletQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQ 744
Cdd:PTZ00121  1637 QLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  745 QQLAALRQQLQAEtERREQAESAlgQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQ-QQKLADQDA 823
Cdd:PTZ00121  1714 EKKKAEELKKAEE-ENKIKAEEA--KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAViEEELDEEDE 1790

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  824 ELKKTWDNLIKETED-----REALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRS 898
Cdd:PTZ00121  1791 KRRMEVDKKIKDIFDnfaniIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADF 1870

                          730       740       750
                   ....*....|....*....|....*....|....*.
gi 1949443035  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 1949443035 1075 KETAARHETERELRESLTDAERTT--EALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAR-EQLEKNL 1151
Cdd:COG4913    268 RERLAELEYLRAALRLWFAQRRLEllEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREI 347

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1152 RQAAEEATRKAQALqAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQE 1231
Cdd:COG4913    348 ERLERELEERERRR-ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1232 RLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLE-QERDER-RRVVES-LTQTSTTL------EARATESGS 1302
Cdd:COG4913    427 EIASLERRKSNIPARLLALRDALAEALGLDEAELPFVGELIEvRPEEERwRGAIERvLGGFALTLlvppehYAAALRWVN 506

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1303 ALEVTRRL-LNEERAARASALAELAARRAEVDRLTTEqPHaieEATARLKAQLAEQE-----REREQLRLA--AMSAEQR 1374
Cdd:COG4913    507 RLHLRGRLvYERVRTGLPDPERPRLDPDSLAGKLDFK-PH---PFRAWLEAELGRRFdyvcvDSPEELRRHprAITRAGQ 582

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1375 LRDRATdfeaanaalRGEMEKRLRLELTWQM------QREDFDRRLGELTTALRTAEAKAgSDSAELRHAHETLQQAHAE 1448
Cdd:COG4913    583 VKGNGT---------RHEKDDRRRIRSRYVLgfdnraKLAALEAELAELEEELAEAEERL-EALEAELDALQERREALQR 652

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1449 LtRRLTERDSELASVREQAAALDAAgtraqqttaelQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEA 1528
Cdd:COG4913    653 L-AEYSWDEIDVASAEREIAELEAE-----------LERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK 720

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1529 ELDRMRDAQDgfqqstaelneRLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAEL 1608
Cdd:COG4913    721 ELEQAEEELD-----------ELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEEL 789


                   ....*.
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD--ATLPIIV- 1951
Cdd:cd19927      1 ILLVDDDPGIRLAVKDYLEDQGFTVIAASNGLEALDLLNQYIPDL--IISDIIMPGVDGYSLLGKLRKNAdfDTIPVIFl 78

                           90       100
                   ....*....|....*....|....*.
gi 1949443035 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 1949443035 1877 LADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASGMG 1956
Cdd:cd19936      3 LVDDDRNILTSVSMALEAEGFSVETYTDGASALDGLNARPPDL--AILDIKMPRMDGMELLQRLRQK-STLPVIFLTSKD 79

                           90       100
                   ....*....|....*....|.
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQhagDIKAVITDILMPFMDGVELCRELRKRDATlPIIVASG 1954
Cdd:PRK10955     4 ILLVDDDRELTSLLKELLEMEGFNVIVAHDGEQALDLLDD---SIDLLLLDVMMPKKNGIDTLKELRQTHQT-PVIMLTA 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035 1879 DDEQGVLDVTAEILEWHGYKVLT---ARDGQQALSLyDQHAgdikAVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:cd17537      7 DDDEAVRDSLAFLLRSVGLAVKTftsASAFLAAAPP-DQPG----CLVLDVRMPGMSGLELQDELLARGSNIPIIFITGH 81

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM 1955
Cdd:cd17625      1 LVVEDEKDLSEAITKHLKKEGYTVDVCFDGEEGLEYALSGIYDL--IILDIMLPGMDGLEVLKSLREEGIETPVLLLTAL 78

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035  234 KKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATftdiisgleKAVAEHELAVKTLQAEKAELEKRTAS 313
Cdd:PTZ00121  1086 DNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKA---------EEARKAEDARKAEEARKAEDAKRVEI 1156

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  314 SPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETE--LESLRVA--LQ 389
Cdd:PTZ00121  1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAkkAEAVKKAeeAK 1236

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  390 TEHEKAERADAERELSEEAMVQTN--TGIQQRLMELNAELERTKEELVAESARRtQAEAGQGGGEVNPELAARIAALTEA 467
Cdd:PTZ00121  1237 KDAEEAKKAEEERNNEEIRKFEEArmAHFARRQAAIKAEEARKADELKKAEEKK-KADEAKKAEEKKKADEAKKKAEEAK 1315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  468 KAQVEKELVEQqavAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQRfeqrvA 547
Cdd:PTZ00121  1316 KADEAKKKAEE---AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK-----A 1387

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  548 ELETDNQQLREQASRDTQAA--TTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQqlQ 625
Cdd:PTZ00121  1388 EEKKKADEAKKKAEEDKKKAdeLKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKK--K 1465

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  626 AESERRAQ--AESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEvqrgERAEAELFRSRSELET 703
Cdd:PTZ00121  1466 AEEAKKADeaKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKAD----EAKKAEEAKKADEAKK 1541

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  704 QQAALAELRARAEAAEAARLQVETTAQQSR-------TVAEQAAAEAQQQLAALRQQLQAETERREQAESAlgqSKSETE 776
Cdd:PTZ00121  1542 AEEKKKADELKKAEELKKAEEKKKAEEAKKaeedknmALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA---KKAEEA 1618

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  777 RQLAEATAALAEVRAQLEQattassqreaeakqaaaaqqqkLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQ 856
Cdd:PTZ00121  1619 KIKAEELKKAEEEKKKVEQ----------------------LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKK 1676

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1949443035  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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAgDIKAVITDILMP-FMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd18161      2 LVVEDDPDVRRLTAEVLEDLGYTVLEAASGDEALDLLESGP-DIDLLVTDVIMPgGMNGSQLAEEARRRRPDLKVLLTSG 80

                           90       100
                   ....*....|....*....|...
gi 1949443035 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 1949443035 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 1949443035 1873 ELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:cd17553      1 EKILIVDDQYGIRILLNEVFNKEGYQTFQAANGLQALDIVTKERPDL--VLLDMKIPGMDGIEILKRMKVIDENIRVIIM 78

                           90       100       110
                   ....*....|....*....|....*....|
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLydQHAGDIKAVITDILMPFMDGVELCRELRK--RDATLPIIVAS 1953
Cdd:cd17562      4 LAVDDSASIRQMVSFTLRGAGYEVVEAADGRDALSK--AQSKKFDLIITDQNMPNMDGIELIKELRKlpAYKFTPILMLT 81

                           90       100       110
                   ....*....|....*....|....*....|
gi 1949443035 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 1949443035   78 FESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKE-FRLDFRLRNK 156
Cdd:TIGR00229    5 YRAIFESSPDAIIVIDLEGNILYVNPAFEEIFGYSAEELIGRNVLELIPEEDREEVRERIERRLEGEPEpVSEERRVRRK 84

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1949443035  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 1949443035 1876 MLADDEQGVLDVTAEILEWHGY-KVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKR--DATLPIIVa 1952
Cdd:cd17551      4 LIVDDNPTNLLLLEALLRSAGYlEVVSFTDPREALAWCRENPPDL--ILLDYMMPGMDGLEFIRRLRALpgLEDVPIVM- 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd17623      1 ILLIDDDRELTELLTEYLEMEGFNVRAAHDGEQGLAALLEGSPD--LVVLDVMLPKMNGLDVLKELRKT-SQVPVLMLTA 77

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRD-ATLPIIVaS 1953
Cdd:cd17569      3 ILLVDDEPNILKALKRLLRREGYEVLTATSGEEALEILKQEPVDV--VISDQRMPGMDGAELLKRVRERYpDTVRILL-T 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035 1016 LEATNAESSRALAAAQNELARESAERETTEAEF-QRSKSALAQQLAEAAAAQAELRSRLEKETAARHETER--ELRESLT 1092
Cdd:pfam12128  256 AELRLSHLHFGYKSDETLIASRQEERQETSAELnQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAleDQHGAFL 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1093 DAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAR-----EQLEKNLRQAAEEATRKAQALQA 1167
Cdd:pfam12128  336 DADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnnrdiAGIKDKLAKIREARDRQLAVAED 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1168 ELQRAKKELEKELADANLELLDIRSRLdheaaARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVEL 1247
Cdd:pfam12128  416 DLQALESELREQLEAGKLEFNEEEYRL-----KSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERL 490

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1248 RDTRAALEKQLAEASAALREASARLEQERDERRRVVESLT-QTSTTLEARATESGSALEVTRRLLNEERAARASALAELA 1326
Cdd:pfam12128  491 QSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFpQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVW 570

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1327 ARRAE-----------VDRLTTEQPHAIEEAtarLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANA----ALRG 1391
Cdd:pfam12128  571 DGSVGgelnlygvkldLKRIDVPEWAASEEE---LRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASReetfARTA 647

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1392 EMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTE-RDSELASVREQAAAL 1470
Cdd:pfam12128  648 LKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREaRTEKQAYWQVVEGAL 727

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1471 DAAGTRAQQTTAELQTNlnaARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQ------DGFQQST 1544
Cdd:pfam12128  728 DAQLALLKAAIAARRSG---AKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRqevlryFDWYQET 804

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1545 -------------------AELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSE-RTAGLNAHVQQL 1604
Cdd:pfam12128  805 wlqrrprlatqlsnieraiSELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKlATLKEDANSEQA 884

                          650
                   ....*....|....*...
gi 1949443035 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 1949443035 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 1949443035   49 GTVGLFLLLRRDIQKREQTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPD 128
Cdd:COG5809    114 GDIEGMLAISRDITERKRMEEALRESEEKFRLIFNHSPDGIIVTDLDGRIIYANPAACKLLGISIEELIGKSILELIHSD 193

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17615      2 VLVVDDEPNITELLSMALRYEGWDVETAADGAEALAAAREFRPD--AVVLDIMLPDMDGLEVLRRLRADGPDVPVLFLTA 79

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1336 TTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAE--QRLRDRATDFEAANAALRGEMEKRLRLELtwQMQREDFDRR 1413
Cdd:TIGR02168  177 TERKLERTRENLDRLEDILNELERQLKSLERQAEKAEryKELKAELRELELALLVLRLEELREELEEL--QEELKEAEEE 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1414 LGELTTALRTAEAKagsdSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARA 1493
Cdd:TIGR02168  255 LEELTAELQELEEK----LEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1494 ELDMLNRQFAQRVAELDSTEARLreecahrERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRR 1573
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEEL-------ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1574 SLEDALQQSHGEVELRVSERTAGL----NAHVQQLEAELAEAQRAEEQLRHRRIEAVSTLAggmahELNNVLAPVLMAAQ 1649
Cdd:TIGR02168  404 RLEARLERLEDRRERLQQEIEELLkkleEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD 478

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1724 DLP-LISADASQLHRVLLNLAVNArdampsggtLKFSAENVVVdesfIHHRRAtgakpGNYVLFRVTDSGVGIPRDILPR 1802
Cdd:PRK10841   551 DVPvALNGDPMRLQQVISNLLSNA---------IKFTDTGCIV----LHVRVD-----GDYLSFRVRDTGVGIPAKEVVR 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1803 IFEPFFT----TKEPGQSVGLGLATALGVVQSHGGFILLETEEDKGTEFQIYLP-------------------------- 1852
Cdd:PRK10841   613 LFDPFFQvgtgVQRNFQGTGLGLAICEKLINMMDGDISVDSEPGMGSQFTIRIPlygaqypqkkgveglqgkrcwlavrn 692

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1853 --------------------------------------------AASAETSER---PPQA--------------ELP--- 1868
Cdd:PRK10841   693 asleqfletllqrsgiqvqryegqeptpedvlitddpvqkkwqgRAVITFCRRhigIPLEiapgewvhstatphELPall 772

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1869 ----------RGNGELLMLADDEQGVL-DVTAEILEWH--------------GYKVLTARDGQQALSLYDQHAGDIkaVI 1923
Cdd:PRK10841   773 ariyrielesDDSANALPSTDKAVSDNdDMMILVVDDHpinrrlladqlgslGYQCKTANDGVDALNVLSKNHIDI--VL 850

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSL-----YDqhagdikAVITDILMPFMDGVELCRELRKRDATLPI 1949
Cdd:cd19935      1 ILVVEDEKKLAEYLKKGLTEEGYAVDVAYDGEDGLHLaltneYD-------LIILDVMLPGLDGLEVLRRLRAAGKQTPV 73


                   .
gi 1949443035 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 1949443035 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMGHe 1958
Cdd:COG4566      6 DDDEAVRDSLAFLLESAGLRVETFASAEAFLAALDPDRPGC--LLLDVRMPGMSGLELQEELAARGSPLPVIFLTGHGD- 82

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035  245 RQLWAELSGREQVEAELAKARGELDkQVAERTATFTDIISGLEKavaehelAVKTLQAEKAELEK----RTASSPAELEA 320
Cdd:TIGR02169  156 RKIIDEIAGVAEFDRKKEKALEELE-EVEENIERLDLIIDEKRQ-------QLERLRREREKAERyqalLKEKREYEGYE 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  321 LRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLeTELESLRVALQTEHEKAERADA 400
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL-GEEEQLRVKEKIGELEAEIASL 306

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  401 ERELSEEamvqtntgiQQRLMELNAELERTKEELvaesaRRTQAEAgqgggevnPELAARIAALTEAKAQVEKELVEQQA 480
Cdd:TIGR02169  307 ERSIAEK---------ERELEDAEERLAKLEAEI-----DKLLAEI--------EELEREIEEERKRRDKLTEEYAELKE 364

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  481 VAKALgdernrlaqelaeaaaaraaleqqlaaasqagagRSEADEaaraqVEADLRAAHQRFEQRVAELETDNQQLRE-Q 559
Cdd:TIGR02169  365 ELEDL----------------------------------RAELEE-----VDKEFAETRDELKDYREKLEKLKREINElK 405

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  560 ASRDTQAATTQRGEQEtaLAELRAQLERTEAARQQIETTALDLR---SNSEQQLSETQRQLADARQQLQAESERRAQAES 636
Cdd:TIGR02169  406 RELDRLQEELQRLSEE--LADLNAAIAGIEAKINELEEEKEDKAleiKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483

                          410
                   ....*....|....*....
gi 1949443035  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 1949443035 1898 KVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMGHEKFVTDLRELGVPLFLKKPF 1977
Cdd:cd17593     27 EITFAENGEEALEILREGRIDV--LFLDLTMPVMDGYEVLEALPVEQLETKVIVVSGDVQPEAKERVLELGALAFLKKPF 104

                           90
                   ....*....|
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAtLPIIVASG 1954
Cdd:cd19939      2 ILIVEDELELARLTRDYLIKAGLEVSVFTDGQRAVRRIIDEQPSL--VVLDIMLPGMDGLTVCREVREHSH-VPILMLTA 78

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035 1565 AEQETTQRRSLEDALQQSHGEVELRVSERTaGLNAHVQQLEAELAEAQRAEEQLRHRRIEAVSTlaggmahelnnvlaPV 1644
Cdd:TIGR02938  249 SNLREEQERARLSALQALMAEEERLEAIRE-TLSAAIHRLQGPMNLISAAISVLQRRGDDAGNP--------------AS 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1645 LMAAQllrkQVSGKSRTLVDSVESS-AQRGADIVKqvltfargfhgeraPVSPEMLVRD-IAKSVQETFPRNVRVSSEVA 1722
Cdd:TIGR02938  314 AAMLQ----QALSAGREHMEALRQViPQSPQEIVV--------------PVNLNQILRDvITLSTPRLLAAGIVVDWQPA 375

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1723 DDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKfsaenvvvDESFIhhrraTGAKPGNYVLFRVTDSGVGIPRDILPR 1802
Cdd:TIGR02938  376 ATLPAILGRELQLRSLFKALVDNAIEAMNIKGWKR--------RELSI-----TTALNGDLIVVSILDSGPGIPQDLRYK 442

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1566 EQETTQRRSLEDALQQSHgEVELRVSERtaglnahVQQLEAELAEAQRAEEQLRhRRIEAVSTLAGGMAHELNNVLAPVL 1645
Cdd:PRK09303   100 QQEGATYSGLGENLQPSE-IDSGRYSQE-------LLQLSDELFVLRQENETLL-EQLKFKDRVLAMLAHDLRTPLTAAS 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1646 MAAQLLR----KQVSGKSRTLVDSVESSAQRGADIV----KQVLTFARGfHGERAPVSPEMLvrDIAKSVQETF------ 1711
Cdd:PRK09303   171 LALETLElgqiDEDTELKPALIEQLQDQARRQLEEIerliTDLLEVGRT-RWEALRFNPQKL--DLGSLCQEVIlelekr 247

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1712 --PRNVRVSSEVADDLPLISADASQLHRVLLNLAVNARDAMPSGGTLKFSaenvvvdesfIHHRraTGAKpgnyVLFRVT 1789
Cdd:PRK09303   248 wlAKSLEIQTDIPSDLPSVYADQERIRQVLLNLLDNAIKYTPEGGTITLS----------MLHR--TTQK----VQVSIC 311

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNArdampsggtLKFSAENVvvdesfiHHRRATGAKP-GNYVLFRVTDSGVGIPRDILPRIFEPF--FTTK 1811
Cdd:cd16921      1 LGQVLTNLLGNA---------IKFRRPRR-------PPRIEVGAEDvGEEWTFYVRDNGIGIDPEYAEKVFGIFqrLHSR 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1731 DASQLHRVLLNLAVNARDAMPSGGTLKFSAEnvvvDESfihhrratgakpgNYVLFRVTDSGVGIPRDILPRIFEPFFTT 1810
Cdd:cd16975      1 DTLLLSRALINIISNACQYAPEGGTVSISIY----DEE-------------EYLYFEIWDNGHGFSEQDLKKALELFYRD 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1879 DDEQGVLDVTAEILEWHGYKVltaRDGQQALSLYDQHAG-DIKAVITDILMPFMDGVELCRELRKRDATLPIIVASGMGH 1957
Cdd:PRK09390    10 DDDEAMRDSLAFLLDSAGFEV---RLFESAQAFLDALPGlRFGCVVTDVRMPGIDGIELLRRLKARGSPLPVIVMTGHGD 86

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd17621      1 VLVVEDEESFSDPLAYLLRKEGFEVTVATDGPAALAEFDRAGADI--VLLDLMLPGLSGTEVCRQLRAR-SNVPVIMVTA 77

                           90       100
                   ....*....|....*....|..
gi 1949443035 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 1949443035 1337 TEQPHAIEEATARLKAQLAEQEREREQLRLAamsaEQRLRDRATDFEAANAALRGEMEKrLRLELTWQMQR--------E 1408
Cdd:COG4192    108 TQDAGDLRAAVADLRNLLQQLDSLLTQRIAL----RRRLQELLEQINWLHQDFNSELTP-LLQEASWQQTRlldsvettE 182

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1409 DFDRRLGELTTALR--TAEAKAGSDSAElrHAHETLQQAHAELTRRLTERdSELASVREQAAALDAAGTRAQQTTAEL-- 1484
Cdd:COG4192    183 SLRNLQNELQLLLRllAIENQIVSLLRE--VAAARDQADVDNLFDRLQYL-KDELDRNLQALKNYPSTITLRQLIDELla 259

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1485 ----QTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAhrERAEAELDRMRDAQDGFQQSTAE-------------- 1546
Cdd:COG4192    260 igsgEGGLPSLRRDELAAQATLEALAEENNSILEQLRTQIS--GLVGNSREQLVALNQETAQLVQQsgilllaiallsll 337

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1547 -------------LNERLTRLTTDVEA-ARQQAEQETTQRRSleDALqqshGEV--ELRVSERTAglNAHVQQLEAELAE 1610
Cdd:COG4192    338 lavlinyfyvrrrLVKRLNALSDAMAAiAAGDLDVPIPVDGN--DEI----GRIarLLRVFRDQA--IEKTQELETEIEE 409

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1611 AQRAEEQLRH--------RRIEAVSTLAGGMAHELNNVLAPVLMAAQLLRKQVSGKS----RTLVDSVESSAQRGADIVK 1678
Cdd:COG4192    410 RKRIEKNLRQtqdeliqaAKMAVVGQTMTSLAHELNQPLNAMSMYLFSAKKALEQENyaqlPTSLDKIEGLIERMDKIIK 489

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1679 QVLTFARGFHGERAPVSPEMLVRDiAKSVQETFPRNVRVSSEVADDlPLISADASQLHRVLLNLAVNARDAMPsggtlkf 1758
Cdd:COG4192    490 SLRQFSRKSDTPLQPVDLRQVIEQ-AWELVESRAKPQQITLHIPDD-LMVQGDQVLLEQVLVNLLVNALDAVA------- 560

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1759 saenvvvDESFIHHRRATGAKpgnYVLFRVTDSGVGIPrdILPRIFEPFFTTKEPGqsVGLGLATALGVVQSHGGFILLE 1838
Cdd:COG4192    561 -------TQPQISVDLLSNAE---NLRVAISDNGNGWP--LVDKLFTPFTTTKEVG--LGLGLSICRSIMQQFGGDLYLA 626


                   ....*.
gi 1949443035 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 1949443035   78 FESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQG---FGwlLAVHPDDNKRVTEEWRKCVRGEKEFRLDFRLR 154
Cdd:pfam00989    3 LRAILESLPDGIFVVDEDGRILYVNAAAEELLGLSREEVIGkslLD--LIPEEDDAEVAELLRQALLQGEESRGFEVSFR 80

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1949443035  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 1949443035 1874 LLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRkRDATLPIIVAS 1953
Cdd:cd17594      1 HVLVVDDDAAMRHLLILYLRERGFDVTAAADGAEEARLMLHRRVDL--VLLDLRLGQESGLDLLRTIR-ARSDVPIIIIS 77

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1949443035 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 1949443035   55 LLLRRDIQKREQTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVT 134
Cdd:COG5805    136 ILALRDITKKKKIEEILQEQEERLQTLIENSPDLICVIDTDGRILFINESIERLFGAPREELIGKNLLELLHPCDKEEFK 215

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  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 1949443035 1731 DASQLHRVLLNLAVNARDAmpsggtlkfsAENVVVDESFIHHRRATGAKpgNYVLFRVTDSGVGIPRDILPRIFEPFFTT 1810
Cdd:cd16944      1 DTTQISQVLTNILKNAAEA----------IEGRPSDVGEVRIRVEADQD--GRIVLIVCDNGKGFPREMRHRATEPYVTT 68

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILE-WHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDAT--LPIIV 1951
Cdd:cd17552      4 ILVIDDEEDIREVVQACLEkLAGWEVLTASSGQEGLEKAATEQPD--AILLDVMMPDMDGLATLKKLQANPETqsIPVIL 81

                           90       100
                   ....*....|....*....|....*...
gi 1949443035 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 1949443035 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 1949443035   63 KREQTHAKNHEVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVR 142
Cdd:COG5809      2 KSSKMELQLRKSEQRFRSLFENAPDAILILDLEGKILKVNPAAERIFGYTEDELLGTNILDFLHPDDEKELREILKLLKE 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1949443035  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 1949443035  824 ELKKTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESllqaSRSSEERV 903
Cdd:PRK02224   290 ELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER----AEELREEA 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  904 ALLASELEAAREALRSESARREELETALpktktelgqrlaeaaaeaAGLRARMDFEAAERERVEAAWKLANSATEQHAAE 983
Cdd:PRK02224   366 AELESELEEAREAVEDRREEIEELEEEI------------------EELRERFGDAPVDLGNAEDFLEELREERDELRER 427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  984 LKTLLATAREelhAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAA 1063
Cdd:PRK02224   428 EAELEATLRT---ARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1064 AAQAELRSRLEKETAARHETERELRESLTDAERTTEALQ---ADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAE 1140
Cdd:PRK02224   505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELReraAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAEL 584

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1141 TGAREQLEK---------NLRQAAEEATRKAQALQ----------AELQRAKKELEKELADANLElldirsrldhEAAAR 1201
Cdd:PRK02224   585 KERIESLERirtllaaiaDAEDEIERLREKREALAelnderrerlAEKRERKRELEAEFDEARIE----------EARED 654

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNARDAMPSggtlkfsaenvvvDESFIHHRRATGakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEP- 1813
Cdd:cd16953      1 LGQVLRNLIGNAISFSPP-------------DTGRITVSAMPT---GKMVTISVEDEGPGIPQEKLESIFDRFYTERPAn 64

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035   36 VVAVVKDTlflaAGTVGLFLLLRRDIQKREQTHAKNhevRQTFESLTQAAPAG---IFRANQQGDILFVNHRWSALTG-R 111
Cdd:PRK09776   374 AVSLVRDT----DGTPLYFIAQIEDINELKRTEQVN---ERLMERITLANEAGgigIWEWDLKPNIISWDKRMFELYEiP 446

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  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 1949443035  767 ALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQL 846
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEK 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  847 AAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREE 926
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREK 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  927 LEtalpKTKTELGQRLAEAAAEAAGLRARmdfeAAERERVEAAWKlansATEQHAAELKTLLATAREELHAETAKRDAAE 1006
Cdd:TIGR02169  394 LE----KLKREINELKRELDRLQEELQRL----SEELADLNAAIA----GIEAKINELEEEKEDKALEIKKQEWKLEQLA 461

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1007 AAASQVRAELEATNAESSRAlaaaqnELARESAERETTEAEFQRSKSALAQQLAEAAAAQaelrsrLEKETAARHETERE 1086
Cdd:TIGR02169  462 ADLSKYEQELYDLKEEYDRV------EKELSKLQRELAEAEAQARASEERVRGGRAVEEV------LKASIQGVHGTVAQ 529

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1087 LRESltdAERTTEALQA-----------DLDAALKACEEEAARRSQAEET------ARQSHTEFthRLTAETGAREQLEK 1149
Cdd:TIGR02169  530 LGSV---GERYATAIEVaagnrlnnvvvEDDAVAKEAIELLKRRKAGRATflplnkMRDERRDL--SILSEDGVIGFAVD 604

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1150 NLRQAAEEATRKAQALQAELQRAKKELEKELADA------NLELLDIRSRLDHEAAARRQAEESAKQGSASAdQRLAERL 1223
Cdd:TIGR02169  605 LVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKyrmvtlEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL-QRLRERL 683

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1224 SEVQTLQERLRSEAAQRETTEVELRDtraalekQLAEASAALREASARLEQERDERRRVVESLTQtsttLEARATESGSA 1303
Cdd:TIGR02169  684 EGLKRELSSLQSELRRIENRLDELSQ-------ELSDASRKIGEIEKEIEQLEQEEEKLKERLEE----LEEDLSSLEQE 752

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1304 LEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEataRLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFE 1383
Cdd:TIGR02169  753 IENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIP---EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKE 829

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1384 aanaALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAgsdsAELRHAHETLQQAHAELTRRLTERDSELASV 1463
Cdd:TIGR02169  830 ----YLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEEL----EELEAALRDLESRLGDLKKERDELEAQLREL 901

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1464 REQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVaELDSTEARLREECAHRERAEAELDRMRD----AQDG 1539
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQRVEEEIRALEPvnmlAIQE 980

                          810       820       830
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYK-VLTARDGQQALSLYDqhAGDIKAVITDILMPFMDGVELCRELR--KRDATLPIIV 1951
Cdd:cd19923      3 VLVVDDFSTMRRIIKNLLKELGFNnVEEAEDGVDALEKLK--AGGFDFVITDWNMPNMDGLELLKTIRadGALSHLPVLM 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1675 DIVKQVLTFARgfHGERAPVSPEMLVRDIAKSVQETFPRNVRVSSEVADDLPLISADASQLHRVLLNLAVNArdampsgg 1754
Cdd:PRK09467   274 AIIEQFIDYLR--TGQEMPMEMADLNALLGEVIAAESGYEREIETALQPGPIEVPMNPIAIKRALANLVVNA-------- 343

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1755 tLKFSAENVVVDESFihhrratgakPGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEPGQSV--GLGLATALGVVQSHG 1832
Cdd:PRK09467   344 -ARYGNGWIKVSSGT----------EGKRAWFQVEDDGPGIPPEQLKHLFQPFTRGDSARGSSgtGLGLAIVKRIVDQHN 412

                          170       180
                   ....*....|....*....|
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIV--A 1952
Cdd:cd17624      1 ILLVEDDALLGDGLKTGLRKAGYAVDWVRTGAEAEAALASGPYD--LVILDLGLPDGDGLDLLRRWRRQGQSLPVLIltA 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1606 AELAEAQRAEEQLRHRRIEAVStlaggmaHELNNVLAPVLMAAQLLrkqvsgksrTLVDSVESS--AQRGADIVKQVLTF 1683
Cdd:PRK10490   651 EEQARLASEREQLRNALLAALS-------HDLRTPLTVLFGQAEIL---------TLDLASEGSphARQASEIRQQVLNT 714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1684 AR--------------GFHGERAPVSPEMLVRDIAKSVQETFPRNvRVSSEVADDLPLISADASQLHRVLLNLAVNARDA 1749
Cdd:PRK10490   715 TRlvnnlldmariqsgGFNLRKEWLTLEEVVGSALQMLEPGLSGH-PINLSLPEPLTLIHVDGPLFERVLINLLENAVKY 793

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1750 MPSGGTLKFSAEnvvVDESFIHhrratgakpgnyvlFRVTDSGVGIPRDILPRIFEPFFT-TKE---PGqsVGLGLATAL 1825
Cdd:PRK10490   794 AGAQAEIGIDAH---VEGERLQ--------------LDVWDNGPGIPPGQEQLIFDKFARgNKEsaiPG--VGLGLAICR 854

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035  186 DINERKVADDTRTTDQAAALDAAlaRVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAELSGREQVE--AELAK 263
Cdd:PTZ00121  1238 DAEEAKKAEEERNNEEIRKFEEA--RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKkkAEEAK 1315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  264 ARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEKAELEKrtasSPAELEALRKRLSDEATRRQLAEDDLRSLR 343
Cdd:PTZ00121  1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA----AEEKAEAAEKKKEEAKKKADAAKKKAEEKK 1391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  344 EDfDKLQSSATQPDTALETVHhRLHAETERVKRLETELESLRVA--LQTEHEKAERADAERELSEEAMVQTNtgiqqrlM 421
Cdd:PTZ00121  1392 KA-DEAKKKAEEDKKKADELK-KAAAAKKKADEAKKKAEEKKKAdeAKKKAEEAKKADEAKKKAEEAKKAEE-------A 1462

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  422 ELNAELERTKEELVAESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKelveqqaVAKAlgdERNRLAQELAEAAA 501
Cdd:PTZ00121  1463 KKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADE-------AKKA---EEAKKADEAKKAEE 1532

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  502 ARAALEQQLAAASQagagrsEADEAARAQveaDLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAEL 581
Cdd:PTZ00121  1533 AKKADEAKKAEEKK------KADELKKAE---ELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE 1603

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  582 RAQLERTEAARQQIE-TTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALgqsKSETERQLAEATAALADTR 660
Cdd:PTZ00121  1604 EKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI---KAAEEAKKAEEDKKKAEEA 1680

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1949443035  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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATlPIIVASGM 1955
Cdd:cd17620      2 LVIEDEPQIRRFLRTALEAHGYRVFEAETGQEGLLEAATRKPDL--IILDLGLPDMDGLEVIRRLREWSAV-PVIVLSAR 78

                           90       100
                   ....*....|....*....|.
gi 1949443035 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 1949443035 1149 KNLRQAAEEATRKAQALQaELQRAKKELEKELADANlELLDIRSRLDHEAAARRQAEesakqgsasADQRLAERLSEVQT 1228
Cdd:COG4913    238 ERAHEALEDAREQIELLE-PIRELAERYAAARERLA-ELEYLRAALRLWFAQRRLEL---------LEAELEELRAELAR 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1229 LQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTR 1308
Cdd:COG4913    307 LEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALR 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1309 RLLNEERAARASALaelaarraevdrltteqpHAIEEATARLKAQLAEQEREREQLRlaamsAE-QRLRDRATDFEAANA 1387
Cdd:COG4913    387 AEAAALLEALEEEL------------------EALEEALAEAEAALRDLRRELRELE-----AEiASLERRKSNIPARLL 443

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1388 ALRGEMEKRLRL-----------------ELTWQMQREDF-----------DRRLGELTTALRTAEAKAGSDSAELRHAH 1439
Cdd:COG4913    444 ALRDALAEALGLdeaelpfvgelievrpeEERWRGAIERVlggfaltllvpPEHYAAALRWVNRLHLRGRLVYERVRTGL 523

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1440 ETLQQAHAE---LTRRLTERDS--------ELASVREQAAALDAAGTRAQQT--TAELQTNLNAARAELDMLNRQFAQRV 1506
Cdd:COG4913    524 PDPERPRLDpdsLAGKLDFKPHpfrawleaELGRRFDYVCVDSPEELRRHPRaiTRAGQVKGNGTRHEKDDRRRIRSRYV 603

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1507 -------------AELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLtrlttDVEAARQQAEQETTQRR 1573
Cdd:COG4913    604 lgfdnraklaaleAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEAELE 678

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035 1879 DDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIVASGMG 1956
Cdd:cd17618      7 EDEPAIREMIAFNLERAGFDVVEAEDAESAVNLIVEPRPDL--ILLDWMLPGGSGIQFIRRLKRDEMTrdIPIIMLTARG 84

                           90       100
                   ....*....|....*....|....*..
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIV--A 1952
Cdd:cd19934      1 LLLVEDDALLAAQLKEQLSDAGYVVDVAEDGEEALFQGEEEPYD--LVVLDLGLPGMDGLSVLRRWRSEGRATPVLIltA 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRkRDATLPIIVASG 1954
Cdd:cd17622      3 ILLVEDDPKLARLIADFLESHGFNVVVEHRGDRALEVIAREKPDA--VLLDIMLPGIDGLTLCRDLR-PKYQGPILLLTA 79

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035  287 EKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHR 366
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  367 LHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTgiqqRLMELNAELERTKEELVAESARRTQAEA 446
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE----ALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  447 GQGGGEVNPE--------LAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAgA 518
Cdd:TIGR02168  832 RIAATERRLEdleeqieeLSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESK-R 910

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949443035  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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK11361     7 ILIVDDEDNVRRMLSTAFALQGFETHCANNGRTALHLFADIHPDV--VLMDIRMPEMDGIKALKEMRSHETRTPVILMTA 84

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWH-GYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVAS 1953
Cdd:COG3279      5 LIVDDEPLARERLERLLEKYpDLEVVgEASNGEEALELLEEHKPDL--VFLDIQMPGLDGFELARQLRELDPPPPIIFTT 82

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1949443035 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 1949443035  881 EAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEA 960
Cdd:NF033838    38 EEVRGGNNPTVTSSGNESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTS 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  961 AERERVEAA---WKLANSATEQHAAELKTLLATAREElhAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARE 1037
Cdd:NF033838   118 KTKKELDAAfeqFKKDTLEPGKKVAEATKKVEEAEKK--AKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1038 SAERETTEAEFQRSKSALAQQLAEAaaaqaelrSRLEKETAARHETERELRESLTDAERttEALQADLDAALKACEEEAA 1117
Cdd:NF033838   196 EAKEPRDEEKIKQAKAKVESKKAEA--------TRLEKIKTDREKAEEEAKRRADAKLK--EAVEKNVATSEQDKPKRRA 265

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1118 RRSQAEETARQSHTEFTHRLTAETGAREQL-------EKNLRQA---AEEATRKAQALQAELQR-----AKKELEKELAD 1182
Cdd:NF033838   266 KRGVLGEPATPDKKENDAKSSDSSVGEETLpspslkpEKKVAEAekkVEEAKKKAKDQKEEDRRnyptnTYKTLELEIAE 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1183 ANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAE--RLSEVQTlQERLRSEAAQRETTEVELRDTRAALEKQLAE 1260
Cdd:NF033838   346 SDVKVKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEatRLEKIKT-DRKKAEEEAKRKAAEEDKVKEKPAEQPQPAP 424


                   ....*...
gi 1949443035 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 1949443035  253 GREQVEAELAKARGELDKQVAERTATftdiisGLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRR 332
Cdd:PRK02224   177 GVERVLSDQRGSLDQLKAQIEEKEEK------DLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERR 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  333 QlaedDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAmvqt 412
Cdd:PRK02224   251 E----ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR---- 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  413 NTGIQQRLMELNAELERTKEElvAESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGDERNRL 492
Cdd:PRK02224   323 DEELRDRLEECRVAAQAHNEE--AESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERF 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  493 AQELAEAAAARAALEQQLaaasqagagrsEADEAARAQvEADLRAAHQRFEQRVAEletdNQQLREQASRDTQAATTQRG 572
Cdd:PRK02224   401 GDAPVDLGNAEDFLEELR-----------EERDELRER-EAELEATLRTARERVEE----AEALLEAGKCPECGQPVEGS 464

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  573 EQETALAELRAQLERTEAARQQIETT--ALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESalgqskseterQLA 650
Cdd:PRK02224   465 PHVETIEEDRERVEELEAELEDLEEEveEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRE-----------TIE 533

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  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 1949443035 1876 MLADDEQGVLDVTAEILEWH--GYKVLTARDGQQAlslydqhAGDIKA-----VITDILMPFMDGVELCRELRKRDATLP 1948
Cdd:cd17565      2 YIVDDDKNIIKILSDIIEDDdlGEVVGEADNGAQA-------YDEILFlqpdiVLIDLLMPGMDGIQLVRKLKDTGSNGK 74

                           90       100
                   ....*....|....*....|....*...
gi 1949443035 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 1949443035 1223 LSEVQTLQERLRSEAAQREttEVELRDTRAALEKQLAE--------------ASAALREASARLEqERDERRRVVESLTQ 1288
Cdd:PRK02224   182 LSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAEldeeieryeeqreqARETRDEADEVLE-EHEERREELETLEA 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1289 TSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDrLTTEQPHAIEEATARLKAQLAEQEREREQLRLAA 1368
Cdd:PRK02224   259 EIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEECRVAA 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1369 MSAE---QRLRDRATDFEAANAALRgemEKRLRLELTWQMQREDFDRRLGELT------TALRTAEAKAGSDSAELRHAH 1439
Cdd:PRK02224   338 QAHNeeaESLREDADDLEERAEELR---EEAAELESELEEAREAVEDRREEIEeleeeiEELRERFGDAPVDLGNAEDFL 414

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1440 ETLQQAHAELTRRLTERDSELASVREqaaaldaagtraqqTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARlree 1519
Cdd:PRK02224   415 EELREERDELREREAELEATLRTARE--------------RVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRER---- 476

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1520 cahRERAEAELDRMRDAQDgfqqstaELNERLTRLTTDVEAARQqAEQETTQRRSLEDALQQSHGEVELRvSERTAGLNA 1599
Cdd:PRK02224   477 ---VEELEAELEDLEEEVE-------EVEERLERAEDLVEAEDR-IERLEERREDLEELIAERRETIEEK-RERAEELRE 544

                          410       420
                   ....*....|....*....|....*..
gi 1949443035 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 1949443035  225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELdkqVAErtatftdiiSGLEKAVAEhelavkTLQAEK 304
Cdd:PRK02224   255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDL---LAE---------AGLDDADAE------AVEARR 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  305 AELEKRtasspaeLEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESL 384
Cdd:PRK02224   317 EELEDR-------DEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  385 RVALQTEHEKAERADAERELSE---EAMVQTNTGIQQRLMELNAELeRTKEELVAEsARRTQAEAGQGGGEVNPELAARI 461
Cdd:PRK02224   390 EEEIEELRERFGDAPVDLGNAEdflEELREERDELREREAELEATL-RTARERVEE-AEALLEAGKCPECGQPVEGSPHV 467

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  462 AALTEAKAQVEkELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAgagrSEADEAARAQVEADlRAAHQR 541
Cdd:PRK02224   468 ETIEEDRERVE-ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDL----EELIAERRETIEEK-RERAEE 541

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  542 FEQRVAELETDNQQLREQASRDTQAATTQRGEqetaLAELRAQLERTEAARQQIET--TALDLRSNSEQQLSETQRQLAD 619
Cdd:PRK02224   542 LRERAAELEAEAEEKREAAAEAEEEAEEAREE----VAELNSKLAELKERIESLERirTLLAAIADAEDEIERLREKREA 617

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  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 1949443035  219 RKEIGLELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVK 298
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  299 TLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLE 378
Cdd:TIGR02169  319 DAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  379 TELESLRVALQTEHEKAERADAERELSEEAMvqtnTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEvnpela 458
Cdd:TIGR02169  399 REINELKRELDRLQEELQRLSEELADLNAAI----AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYE------ 468

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  459 ARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEAdlrAA 538
Cdd:TIGR02169  469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEV---AA 545

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  539 HQRFEQRVAELETDNQQL-----REQASRDTQAATTQRGEQETALAELRAQ----------------------------- 584
Cdd:TIGR02169  546 GNRLNNVVVEDDAVAKEAiellkRRKAGRATFLPLNKMRDERRDLSILSEDgvigfavdlvefdpkyepafkyvfgdtlv 625

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  585 LERTEAARQQIE-----TTALDL---------RSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLA 650
Cdd:TIGR02169  626 VEDIEAARRLMGkyrmvTLEGELfeksgamtgGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLD 705

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  651 EATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGER----AEAELFRSRSELETQQAALAELRARAEAAEAARLQVE 726
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLE 785

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  727 TTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAE 806
Cdd:TIGR02169  786 ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEE 865

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  807 AKQAAAAQQQKLADQDAELKKTwdnlikeTEDREALEKQLAAARgDLERQLAETKAELDQQLAALAEARSQAEREAA--E 884
Cdd:TIGR02169  866 LEEELEELEAALRDLESRLGDL-------KKERDELEAQLRELE-RKIEELEAQIEKKRKRLSELKAKLEALEEELSeiE 937

                          730       740       750
                   ....*....|....*....|....*....|...
gi 1949443035  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 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK15115     8 LLLVDDDPGLLKLLGMRLTSEGYSVVTAESGQEALRVLNREKVDL--VISDLRMDEMDGMQLFAEIQKVQPGMPVIILTA 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQhaGDIKAVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd17619      3 ILIVEDEPVTRATLKSYFEQEGYDVSEAGDGEEMRQILAR--QDIDLVLLDINLPGKDGLSLTRELREQ-SEVGIILVTG 79

                           90       100
                   ....*....|....*....|....*....
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWH-GYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELR-KRDATLP-II 1950
Cdd:cd17561      4 VLIADDNREFVQLLEEYLNSQpDMEVVgVAHNGQEALELIEEKEPDV--LLLDIIMPHLDGIGVLEKLRrMRLEKRPkII 81

                           90       100
                   ....*....|....*....|....*..
gi 1949443035 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 1949443035 1873 ELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:COG4567      5 RSLLLVDDDEAFARVLARALERRGFEVTTAASVEEALALLEQAPPDY--AVLDLRLGDGSGLDLIEALRERDPDARIVVL 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035    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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVLT-ARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRkRDATLPIIVASG 1954
Cdd:COG3707      7 LVVDDEPLRRADLREGLREAGYEVVAeAADGEDAVELVRELKPDL--VIVDIDMPDRDGLEAARQIS-EERPAPVILLTA 83

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035 1729 SADASQLHR---VLLNLAVNARDAMPS--GGTLKFSaenvvvdesfIHHRRatgakpgNYVLFRVTDSGVGIPRDILPRI 1803
Cdd:PRK11086   425 SGDEDQVHElitILGNLIENALEAVGGeeGGEISVS----------LHYRN-------GWLHCEVSDDGPGIAPDEIDAI 487

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1731 DASQLHRVLLNLAVNARDAMPSGGTLKFSAEnvvvdesfihhrratgaKPGNYVLFRVTDSGVGIPRDILPRIFEPFFTT 1810
Cdd:cd16945      1 DPFLLRQAINNLLDNAIDFSPEGGLIALQLE-----------------ADTEGIELLVFDEGSGIPDYALNRVFERFYSL 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035  964 ERVEAAWKLANSATEQhaaeLKTLLATAREELHAETAKRDAAEAAASQVRAELEatnaESSRALAAAQNELARES--AER 1041
Cdd:pfam15921  285 EKASSARSQANSIQSQ----LEIIQEQARNQNSMYMRQLSDLESTVSQLRSELR----EAKRMYEDKIEELEKQLvlANS 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1042 ETTEAEFQRSK-SALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLD----------AALK 1110
Cdd:pfam15921  357 ELTEARTERDQfSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmevqrleALLK 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1111 ACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQ------AELQRAKKELEKELADAN 1184
Cdd:pfam15921  437 AMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLEssertvSDLTASLQEKERAIEATN 516

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1185 LELLDIRSRLD---HEAAARRQAEESAKQGSASADQ---RLAERLSEVQTLQERLRSE---AAQRETTEVELRDTRAALE 1255
Cdd:pfam15921  517 AEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENMtqlVGQHGRTAGAMQVEKAQLE 596

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1256 KQLAEASAALREASArLEQERDERRRVVESLTQTSTTLEARATESGSA-LEVTR-------RLLNEERAARaSALAELAA 1327
Cdd:pfam15921  597 KEINDRRLELQEFKI-LKDKKDAKIRELEARVSDLELEKVKLVNAGSErLRAVKdikqerdQLLNEVKTSR-NELNSLSE 674

                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035  228 RRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTAtftdiisglekavAEHELAVKTLQAEKAEL 307
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK-------------LEKLLQLLPLYQELEAL 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  308 EKRTASSPAELEALRKRLsdeatrrqlaeDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETE-RVKRLETELESLRV 386
Cdd:COG4717    138 EAELAELPERLEELEERL-----------EELRELEEELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQ 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  387 ALQTEHEKAERADAERELSEEAMVQTNTgiQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPELAARIAALTE 466
Cdd:COG4717    207 RLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  467 AKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQRFEQ-R 545
Cdd:COG4717    285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQ 364

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  546 VAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDL-----RSNSEQQLSETQRQLADA 620
Cdd:COG4717    365 LEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELlealdEEELEEELEELEEELEEL 444

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1949443035  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 1949443035 1078 AARHETERELRESLTDAERTTEALQADLDAALKACEEEAAR-RSQAEETarQSHTEFThrltaETGAREQLEKNLRQAAE 1156
Cdd:pfam15921  249 ALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSaRSQANSI--QSQLEII-----QEQARNQNSMYMRQLSD 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1157 EATRKAQaLQAELQRAKK-------ELEKELADANLELLDIRSRLDHEAAA----------------RRQAEESAKQgsa 1213
Cdd:pfam15921  322 LESTVSQ-LRSELREAKRmyedkieELEKQLVLANSELTEARTERDQFSQEsgnlddqlqklladlhKREKELSLEK--- 397

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1214 SADQRLAERLSEVQTLQERLRSEAAQR----ETTEVELRDTRAALEKQLAEASAALR----------EASARLEQERDER 1279
Cdd:pfam15921  398 EQNKRLWDRDTGNSITIDHLRRELDDRnmevQRLEALLKAMKSECQGQMERQMAAIQgkneslekvsSLTAQLESTKEML 477

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1280 RRVVESLTQTSTTLEaraTESGSALEVTRRLLNEERAARASALAELAARR------AEVDRLTTEQPHA--IEEATARLK 1351
Cdd:pfam15921  478 RKVVEELTAKKMTLE---SSERTVSDLTASLQEKERAIEATNAEITKLRSrvdlklQELQHLKNEGDHLrnVQTECEALK 554

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1352 AQLAEQEREREQLRLAAMSAEQRLrdratdfeaanaALRGEMEKRLRLELTwQMQREDFDRRLgELTTaLRTAEAKAGSD 1431
Cdd:pfam15921  555 LQMAEKDKVIEILRQQIENMTQLV------------GQHGRTAGAMQVEKA-QLEKEINDRRL-ELQE-FKILKDKKDAK 619

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1432 SAELRHAHETLQQAHAELTRRLTERdseLASVREQAAALDAAGTRAQQTTAELqtnlNAARAELDMLNRQFAQRVAELDS 1511
Cdd:pfam15921  620 IRELEARVSDLELEKVKLVNAGSER---LRAVKDIKQERDQLLNEVKTSRNEL----NSLSEDYEVLKRNFRNKSEEMET 692

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1512 TEARLREECahrERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVEL--- 1588
Cdd:pfam15921  693 TTNKLKMQL---KSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFlke 769

                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKrDATLPIIVASG 1954
Cdd:cd17626      3 ILVVDDDAALAEMIGIVLRGEGFDPAFCGDGTQALAAFREVRPDL--VLLDLMLPGIDGIEVCRQIRA-ESGVPIVMLTA 79

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035  982 AELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAEssRALAAAQNELARESAERETTE-----AEFQRSKSALA 1056
Cdd:TIGR02169  166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREYEGYEllkekEALERQKEAIE 243

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1057 QQLAEAAAAQAELRSRLEKETAARHETERELRE------SLTDAE--------RTTEALQADLDAALKACEEEAAR---- 1118
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEElnkkikDLGEEEqlrvkekiGELEAEIASLERSIAEKERELEDaeer 323

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1119 -----------RSQAEETARQSHTEFTHR--LTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEK------E 1179
Cdd:TIGR02169  324 lakleaeidklLAEIEELEREIEEERKRRdkLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkreinE 403

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1180 LADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRA---ALEK 1256
Cdd:TIGR02169  404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEeydRVEK 483

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1257 QLAEASAALREASARLEQERDE---RRRVVESLTQTSTTLEARATESGS-------ALEVTR------------------ 1308
Cdd:TIGR02169  484 ELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGVHGTVAQLGSvgeryatAIEVAAgnrlnnvvveddavakea 563

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1309 -RLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEA-------------------TARLKAQLAEQEREREQLRLAA 1368
Cdd:TIGR02169  564 iELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkyepafkyvfgDTLVVEDIEAARRLMGKYRMVT 643

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1369 MSAE---------------QRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSA 1433
Cdd:TIGR02169  644 LEGElfeksgamtggsrapRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEK 723

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1434 ELRHA---HETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMlnRQFAQRVAELD 1510
Cdd:TIGR02169  724 EIEQLeqeEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELS 801

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1511 STEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVElRV 1590
Cdd:TIGR02169  802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALR-DL 880

                          730       740
                   ....*....|....*....|....*...
gi 1949443035 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 1949443035  201 QAAALDAALARVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAEL----SGREQVEAELAKARGELD------K 270
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLetlrSKVAQLELQIASLNNEIErlearlE 410

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  271 QVAERTATFTDIISGLEKAVAEHELavKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQ 350
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  351 SSAtqpdTALETVHHRLHAETERVKRLETELESLRVALQTEHEKAErADAERELSEEAMVQTNtgIQQRLMELNAELERT 430
Cdd:TIGR02168  489 ARL----DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELIS-VDEGYEAAIEAALGGR--LQAVVVENLNAAKKA 561

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  431 KEELV-AESARRTQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGD---ERNRLAQELAEAAAARAAL 506
Cdd:TIGR02168  562 IAFLKqNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllGGVLVVDDLDNALELAKKL 641

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  507 EQQLAAASQAGagrsEADEAARAQVEADLRAAHQRFEQRvAELETDNQQLREQASRDTqaattqrgEQETALAELRAQLE 586
Cdd:TIGR02168  642 RPGYRIVTLDG----DLVRPGGVITGGSAKTNSSILERR-REIEELEEKIEELEEKIA--------ELEKALAELRKELE 708

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  587 RTEAARQQIETTALDLRsnseQQLSETQRQLADARQQLQAESERRAQAESALgqskSETERQLAEATAALADTRKQLEEA 666
Cdd:TIGR02168  709 ELEEELEQLRKELEELS----RQISALRKDLARLEAEVEQLEERIAQLSKEL----TELEAEIEELEERLEEAEEELAEA 780

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  667 TTKAAELQPVREQLAGEVQRGERAEAELfrsRSELETQQAALaelraraeaaeaarlqvettAQQSRTVAEQAAAEAQQQ 746
Cdd:TIGR02168  781 EAEIEELEAQIEQLKEELKALREALDEL---RAELTLLNEEA--------------------ANLRERLESLERRIAATE 837

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  747 LAALRQQLQAETERREQAESALGQSKSETErqlaeataalaevRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELK 826
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEEL-------------IEELESELEALLNERASLEEALALLRSELEELSEELR 904

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  827 KTWDNLIKETEDREALEKQLAaargDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRsseERVALL 906
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLA----QLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR---RRLKRL 977

                          730       740       750
                   ....*....|....*....|....*....|
gi 1949443035  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 1949443035 1896 GYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGMGHEKFVTDLRELGVPLFLKK 1975
Cdd:cd17572     22 GYKVTHVETGKEALAFLSDQPPDV--VLLDLKLPDMSGMEILKWIQERSLPTSVIVITAHGSVDIAVEAMRLGAYDFLEK 99


                   ....*..
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNARDAmpSGGTLKFSAENvvvdesfihhrratgakPGNYVLFRVTDSGVGIPRDILPRIFEPFF--TTKE 1812
Cdd:cd16950      1 LKRVLSNLVDNALRY--GGGWVEVSSDG-----------------EGNRTRIQVLDNGPGIAPEEVDELFQPFYrgDNAR 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035  517 GAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQAsrdtQAATTQRGEQETALAELRAQLERTEAARQQIE 596
Cdd:pfam02463  161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKE----QAKKALEYYQLKEKLELEEEYLLYLDYLKLNE 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  597 TTALDLRS--NSEQQLSETQRQLADARQQLQAESER------RAQAESALGQSKSETERQLAEATAALADTRKQLEEATT 668
Cdd:pfam02463  237 ERIDLLQEllRDEQEEIESSKQEIEKEEEKLAQVLKenkeeeKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKL 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  669 KAAELQPVREQLAGEVQRGERAEAElfRSRSELETQQaalaelraraeaaEAARLQVETTAQQSRTVAEQAAAEAQQQLA 748
Cdd:pfam02463  317 KESEKEKKKAEKELKKEKEEIEELE--KELKELEIKR-------------EAEEEEEEELEKLQEKLEQLEEELLAKKKL 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  749 ALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKT 828
Cdd:pfam02463  382 ESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  829 WDNLIKETEDREALEKQLAAARGDLERQLAETKAELDqqLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLAS 908
Cdd:pfam02463  462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEER--SQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVE 539

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  909 ELEAAREALRsesarreelETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLL 988
Cdd:pfam02463  540 NYKVAISTAV---------IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDK 610

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  989 AT--AREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARES-AERETTEAEFQRSKSALAQQLAEAAAA 1065
Cdd:pfam02463  611 ATleADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSeVKASLSELTKELLEIQELQEKAESELA 690

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1066 QAELRSR-LEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEfthRLTAETGAR 1144
Cdd:pfam02463  691 KEEILRRqLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLK---KEEKEEEKS 767

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1145 EQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAE---ESAKQGSASADQRLAE 1221
Cdd:pfam02463  768 ELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEkikEEELEELALELKEEQK 847

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1222 RLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESG 1301
Cdd:pfam02463  848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA 927

                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035  820 DQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSS 899
Cdd:COG1754     50 VDDDDKKDDVDDDKKKKKKLLKAAAKKKKALALALAADDEDEELLAADDELEEEKVIKLLLLELAVERVARAAAVRAAAA 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  900 EERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQ 979
Cdd:COG1754    130 EAARLAALLRRRLVLRRLVRRLLVRLLLLRLVLLLLRLLVARRAARRRRRRRRRRARRRELERRRERARAAEAEEAAAAA 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  980 HAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQL 1059
Cdd:COG1754    210 AAAADAGRAAAARDGKGGGKLAAGGAAAAAAAAAAAAAAAAALAEAAAAAAVREPPTPTTTTTAQAATTTTTRAAAARTT 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1060 AEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTA 1139
Cdd:COG1754    290 RSAQQAARRTRLGGEGTYTTTTTTTTTTSAAAAAAAAAAAALAAAAAAAYAPPPPYYYKKKAAAAAAAAAAAAAAAARRP 369

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1140 ETGAREQLEKNLRQAAEEATRK--AQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQ 1217
Cdd:COG1754    370 PAARAALLSDDRLLLELLLLRRtaAAAAAAAAATATTTAAAAAAGAGAVGTAAAGAVFFFGGFLLFAEEEDDDEEDDDDD 449

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035   95 QGDILFVNHRWSALTGRSQAESQG--FGWLLAvHPDDNKRVTEEWRkcvRGEKEFRLDFRLRNKDGSTRWVAGHAMRVLD 172
Cdd:pfam13426    1 DGRIIYVNDAALRLLGYTREELLGksITDLFA-EPEDSERLREALR---EGKAVREFEVVLYRKDGEPFPVLVSLAPIRD 76

                           90
                   ....*....|....*..
gi 1949443035  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 1949443035 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 1949443035 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 1949443035 1871 NGELLMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPII 1950
Cdd:PRK09468     4 ENYKILVVDDDMRLRALLERYLTEQGFQVRSAANAEQMDRLLTRESFHL--MVLDLMLPGEDGLSICRRLRSQNNPTPII 81

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1876 MLADDEQGVLDVTAEILEWHGYKVL-TARDGQQALSLYDQHAGDIkaVITDILMP-FMDGVELCRELRKRdATLPIIVAS 1953
Cdd:cd17534      4 LIVEDEAIIALDLKEILESLGYEVVgIADSGEEAIELAEENKPDL--ILMDINLKgDMDGIEAAREIREK-FDIPVIFLT 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAG-------DIKAVITDILMPFMDGVELCRELRK--RDA 1945
Cdd:cd19924      1 ILVVDDSPTARKQLRDLLKNLGFEIAEAVDGEEALNKLENLAKegndlskELDLIITDIEMPKMDGYELTFELRDdpRLA 80


                   ....*...
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd19938      2 ILIVEDEPKLAQLLIDYLRAAGYAPTLLAHGDQVLPYVRHTPPDL--ILLDLMLPGTDGLTLCREIRRF-SDVPIIMVTA 78

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035  959 EAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAeaaasqvraeleatnAESSRALAAAQNELARES 1038
Cdd:pfam07888   60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKEL---------------SASSEELSEEKDALLAQR 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1039 AERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQAdLDAALKACEEEAAR 1118
Cdd:pfam07888  125 AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRS-LSKEFQELRNSLAQ 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1119 RSQAEETARQSHTEFTHRLTAETGAREQLE------KNLRQAAEEATRKAQALQAELQ-------RAKKELEK---ELAD 1182
Cdd:pfam07888  204 RDTQVLQLQDTITTLTQKLTTAHRKEAENEalleelRSLQERLNASERKVEGLGEELSsmaaqrdRTQAELHQarlQAAQ 283

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1183 ANLELLDIRSRLdHEAAARRQAEESAKQGSASADQRLAERLS-EVQTLQERLRSEAAQRETTEVEL-------RDTRAAL 1254
Cdd:pfam07888  284 LTLQLADASLAL-REGRARWAQERETLQQSAEADKDRIEKLSaELQRLEERLQEERMEREKLEVELgrekdcnRVQLSES 362

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRdATLPIIVASG 1954
Cdd:cd18159      1 ILIVEDDETIASLLKKHLEKWGYEVVLIEDFEDVLEEFLQFKPDL--VLLDINLPYFDGFYWCREIRQI-SNVPIIFISS 77

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1254 LEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATEsgsalevtrrlLNEERAARASALAELAARRAEVD 1333
Cdd:pfam15921   76 IERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQE-----------MQMERDAMADIRRRESQSQEDLR 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1334 RLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAE---QRLRDRATDFEAANAALRGEMEKRLRLEL------TWQ 1404
Cdd:pfam15921  145 NQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHFrslgsaISK 224

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1405 MQREdFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRL-TERDSELASVREQAAAldaAGTRAQQTTAE 1483
Cdd:pfam15921  225 ILRE-LDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLiSEHEVEITGLTEKASS---ARSQANSIQSQ 300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1484 LQTNLNAARAELDMLNRQfaqrVAELDSTEARLREECAHRER---------------AEAELDRMRDAQDGFQQSTAELN 1548
Cdd:pfam15921  301 LEIIQEQARNQNSMYMRQ----LSDLESTVSQLRSELREAKRmyedkieelekqlvlANSELTEARTERDQFSQESGNLD 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1549 ERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVElRVSERTAGLNAHVQQLEAELA----------EAQRAEEQL 1618
Cdd:pfam15921  377 DQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITID-HLRRELDDRNMEVQRLEALLKamksecqgqmERQMAAIQG 455

                          410
                   ....*....|.
gi 1949443035 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 1949443035 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 1949443035  757 ETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKET 836
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  837 EDREALEKQLAAARGDLERQLAETKAELDQQLAALA---EARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAA 913
Cdd:pfam02463  247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKlqeEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  914 REALRSESARREELETALP---KTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLAT 990
Cdd:pfam02463  327 EKELKKEKEEIEELEKELKeleIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  991 AREELHAETAKRDAAEAAASQVRAELEAT----------NAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLA 1060
Cdd:pfam02463  407 AQLLLELARQLEDLLKEEKKEELEILEEEeesielkqgkLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQL 486

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1061 EAAAAQAELRSRLEKETAAR-----------HETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQS 1129
Cdd:pfam02463  487 ELLLSRQKLEERSQKESKARsglkvllalikDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKL 566

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1130 HTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADA----NLELLDIRSRLDHEAAARRQAE 1205
Cdd:pfam02463  567 VRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKrakvVEGILKDTELTKLKESAKAKES 646

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1206 ESAKQGSAS----ADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRR 1281
Cdd:pfam02463  647 GLRKGVSLEeglaEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1282 VVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQERER 1361
Cdd:pfam02463  727 VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRAL 806

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1362 EQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALrtaEAKAGSDSAELRHAHET 1441
Cdd:pfam02463  807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE---ELLQELLLKEEELEEQK 883

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1442 LQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFA--QRVAELDSTEARLREE 1519
Cdd:pfam02463  884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEAdeKEKEENNKEEEEERNK 963

                          810
                   ....*....|
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYK-VLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVAS 1953
Cdd:cd17530      3 VLVLDDDPFQCMMAATILEDLGPGnVDEADDGREALVILLCNAPDI--IICDLKMPDMDGIEFLRHLAESHSNAAVILMS 80

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWH-GYKVL-TARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:cd19925      3 VLIVEDDPMVAEIHRAYVEQVpGFTVIgTAGTGEEALKLLKERQPDL--ILLDIYLPDGNGLDLLRELRAAGHDVDVIVV 80

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1412 RRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAA 1491
Cdd:COG4942      2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1492 RAELDMLNRQFAQRVAELDSTEARLREECAHRERAE--------------AELDRMRDAQDGFQQSTAELNERLTRLTTD 1557
Cdd:COG4942     82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE 161

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035  830 DNLIKETEDREALEK---QLAAARGDLERQLAETKAELDQQLAALAeaRSQAEREAAERRQTEES-----LLQASRSSEE 901
Cdd:pfam01576  194 ERLKKEEKGRQELEKakrKLEGESTDLQEQIAELQAQIAELRAQLA--KKEEELQAALARLEEETaqknnALKKIRELEA 271

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  902 RVALLASELEAAREALRSESARREELETALPKTKTELgqrlaeaaaeaaglRARMDFEAAERErveaawklANSATEQHA 981
Cdd:pfam01576  272 QISELQEDLESERAARNKAEKQRRDLGEELEALKTEL--------------EDTLDTTAAQQE--------LRSKREQEV 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  982 AELKTLLataREELHAETAKRDAAEAAASQVRAELEATNAESSR---ALAAAQNELARESAERETTEAEFQRSKSALAQQ 1058
Cdd:pfam01576  330 TELKKAL---EEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRnkaNLEKAKQALESENAELQAELRTLQQAKQDSEHK 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1059 LAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQshtefthrLT 1138
Cdd:pfam01576  407 RKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQEL--------LQ 478

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1139 AETGAREQLEKNLRQAAEEATRKAQALQAElQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQ---GSASA 1215
Cdd:pfam01576  479 EETRQKLNLSTRLRQLEDERNSLQEQLEEE-EEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRlqrELEAL 557

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1216 DQRLAERLSEVQTLQ---ERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVvesltqtstt 1292
Cdd:pfam01576  558 TQQLEEKAAAYDKLEktkNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRA---------- 627

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1293 lEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEAtarlkaqlAEQEREREQLrlaamsaE 1372
Cdd:pfam01576  628 -EAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNV--------HELERSKRAL-------E 691

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1373 QRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRrlgelttalrtaeakagsdsaELRHAHETLQQAHAELTRR 1452
Cdd:pfam01576  692 QQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFER---------------------DLQARDEQGEEKRRQLVKQ 750

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1453 LTERDSELASVREQAAALDAAGTRaqqttaeLQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDR 1532
Cdd:pfam01576  751 VRELEAELEDERKQRAQAVAAKKK-------LELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDE 823

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1533 MRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAgLNAHVQQLEAELAEAQ 1612
Cdd:pfam01576  824 ILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRR-LEARIAQLEEELEEEQ 902


                   ....*....
gi 1949443035 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 1949443035  847 AAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRsseeRVALLASELEAAREALRSESARREE 926
Cdd:COG4942     19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR----RIRALEQELAALEAELAELEKEIAE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  927 LETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTL------LATAREELHAETA 1000
Cdd:COG4942     95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELradlaeLAALRAELEAERA 174

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1114 EEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQA-ELQRAKKELEKELADANLELldirS 1192
Cdd:COG4717     74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERL----E 149

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1193 RLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARL 1272
Cdd:COG4717    150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1273 EQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLka 1352
Cdd:COG4717    230 EQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL-- 307

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1353 QLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAkagSDS 1432
Cdd:COG4717    308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV---EDE 384

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1433 AELRHAHETLQQAHaELTRRLTERDSELASVREQAAALDAAGTRAQQTT--AELQTNLNAARAELDMLNRQFAQRVAELD 1510
Cdd:COG4717    385 EELRAALEQAEEYQ-ELKEELEELEEQLEELLGELEELLEALDEEELEEelEELEEELEELEEELEELREELAELEAELE 463

                          410       420
                   ....*....|....*....|....*
gi 1949443035 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 1949443035 1049 QRSKSALAQQLAEAAAAQAELRSRLEKETAARhetERELRESLTDAERTTEAlQADLDAALKACEEEAA-------RRSQ 1121
Cdd:pfam17380  279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAR---EVERRRKLEEAEKARQA-EMDRQAAIYAEQERMAmererelERIR 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1122 AEETARQSHTEFTHRLTAETGAREQLE--------KNLRQAAE-EATRKAQALQAELQRAKKELEKELADANLELLDIRS 1192
Cdd:pfam17380  355 QEERKRELERIRQEEIAMEISRMRELErlqmerqqKNERVRQElEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1193 RldheaAARRQAEESAKQGsasadQRLAERLSEVQTLQERLRSEAAQRETTEVELrdtraalEKQLAEASAALREASARL 1272
Cdd:pfam17380  435 R-----EVRRLEEERAREM-----ERVRLEEQERQQQVERLRQQEEERKRKKLEL-------EKEKRDRKRAEEQRRKIL 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1273 EQERDERRRVVESLTQTSTTLEARATESGSAL--EVTRRLLNEERAARASALAElaarraevdRLTTEQPHAIEEATARL 1350
Cdd:pfam17380  498 EKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEMEER---------RRIQEQMRKATEERSRL 568

                          330       340       350
                   ....*....|....*....|....*....|
gi 1949443035 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 1949443035  530 QVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQ 609
Cdd:COG4913    295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP 374

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949443035  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 1949443035   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 1949443035 1633 MAHELNNVLAPVLMAAQ-LLRKQVSGKSrtLVDSVESSA---QRGADIVKQVLTFARGFHGERAPVSPEMLVRDIAKSVQ 1708
Cdd:TIGR01386  248 LAHELRTPLTNLLGQTQvALSQPRTGEE--YREVLESNLeelERLSRMVSDMLFLARADNGQLALERVRLDLAAELAKVA 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1709 ETFP-----RNVRVSSEVADDLPlisADASQLHRVLLNLAVNARDAMPSGGTLKfsaenvvvdesfIHHRRATGAkpgny 1783
Cdd:TIGR01386  326 EYFEplaeeRGVRIRVEGEGLVR---GDPQMFRRAISNLLSNALRHTPDGGTIT------------VRIERRSDE----- 385

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035   73 EVRQTFESLTQAAPAGIFRANQQGDILFVNHRWSALTGRSQAESQG--FGWLLAVHPDDNKRVteeWRKCVRGEKEFRLD 150
Cdd:COG3852      4 ESEELLRAILDSLPDAVIVLDADGRITYVNPAAERLLGLSAEELLGrpLAELFPEDSPLRELL---ERALAEGQPVTERE 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1949443035  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 1949443035  558 EQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESA 637
Cdd:TIGR02169  173 EKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEE 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  638 LGQSKSETErQLAEATAALADTRKQLEEA------------TTKAAELQPVREQLAGEV----QRGERAEAELFRSRSEL 701
Cdd:TIGR02169  253 LEKLTEEIS-ELEKRLEEIEQLLEELNKKikdlgeeeqlrvKEKIGELEAEIASLERSIaekeRELEDAEERLAKLEAEI 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  702 ETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAEsALGQSKSETERQLAE 781
Cdd:TIGR02169  332 DKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE-KLKREINELKRELDR 410

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  782 ATAALAEVRAQLEQAttasSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLeRQLAETK 861
Cdd:TIGR02169  411 LQEELQRLSEELADL----NAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY-DRVEKEL 485

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  862 AELDQQLAALAEARSQAEREAAERRQTEE-----------SLLQASRSSEERVALLASEL------------EAAREALR 918
Cdd:TIGR02169  486 SKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgTVAQLGSVGERYATAIEVAAgnrlnnvvveddAVAKEAIE 565

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  919 SESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDF-EAAERERVEAAWKLANSATEQHAAELKTLLATAReelha 997
Cdd:TIGR02169  566 LLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLvEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYR----- 640

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  998 etakrdaaeaaasqvRAELEATNAESSRALAAAQNelaresaeRETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKET 1077
Cdd:TIGR02169  641 ---------------MVTLEGELFEKSGAMTGGSR--------APRGGILFSRSEPAELQRLRERLEGLKRELSSLQSEL 697

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1078 AARHETERELRESLTDAERTTEALQADLDAALKacEEEAARRSQAEETARQSHTEfthrltAETGAREQLEKNLRQAAEE 1157
Cdd:TIGR02169  698 RRIENRLDELSQELSDASRKIGEIEKEIEQLEQ--EEEKLKERLEELEEDLSSLE------QEIENVKSELKELEARIEE 769

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1158 ATRKAQALQAELQRAKKELE----KELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERL 1233
Cdd:TIGR02169  770 LEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQI 849

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1234 RSEAAQRETTEVELRDtraaLEKQLAEASAALREASARLEQERDERRRVVESLTQtsttLEARATESGSALEVTRRLLNE 1313
Cdd:TIGR02169  850 KSIEKEIENLNGKKEE----LEEELEELEAALRDLESRLGDLKKERDELEAQLRE----LERKIEELEAQIEKKRKRLSE 921

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1314 ERAARASALAELAARRAEVDRLTTEQPHAIEEATarLKAQLAEQEREREQLRLAAMSAEQrlrdratDFEAANAALRGEM 1393
Cdd:TIGR02169  922 LKAKLEALEEELSEIEDPKGEDEEIPEEELSLED--VQAELQRVEEEIRALEPVNMLAIQ-------EYEEVLKRLDELK 992


                   ....*...
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNArdampsggtLKFSAENVVVD-ESFIHhrratgakpGNYVLFRVTDSGVGIPRDILPRIFEPFFTTKEP 1813
Cdd:cd16923      1 LQRVFSNLLSNA---------IKYSPENTRIYiTSFLT---------DDVVNIMFKNPSSHPLDFKLEKLFERFYRGDNS 62

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1874 LLMLADDEQgvldvTAEILEWH----GYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPI 1949
Cdd:cd17616      1 VLLIEDDSA-----TAQSIELMlkseGFNVYTTDLGEEGLDLGKLYDYDI--ILLDLNLPDMSGYEVLRTLRLAKVKTPI 73

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035  226 LERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELavktLQAEKA 305
Cdd:PRK02224   347 LREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEE----LREERD 422

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  306 ELEKRTASSPAELEALRKRLsdEATRRQLAE-------------------DDLRSLREDFDKLQSSATQPDTALETVHHR 366
Cdd:PRK02224   423 ELREREAELEATLRTARERV--EEAEALLEAgkcpecgqpvegsphvetiEEDRERVEELEAELEDLEEEVEEVEERLER 500

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  367 LHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEamvqtntgiqqrLMELNAELERTKEElvAESARRTQAEA 446
Cdd:PRK02224   501 AEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEE------------LRERAAELEAEAEE--KREAAAEAEEE 566

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  447 GQGGGEVNPELAARIAALTEAKAQVEKeLVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEA 526
Cdd:PRK02224   567 AEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE 645

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  527 ARAQveaDLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQEtALAELRAQLERTEAARQQIETtaldLRSNS 606
Cdd:PRK02224   646 ARIE---EAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELE-ELEELRERREALENRVEALEA----LYDEA 717

                          410
                   ....*....|....*...
gi 1949443035  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 1949443035  992 REELHAETAKRDAAEAAASQVRAELE---ATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAE 1068
Cdd:pfam17380  305 KEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQ 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1069 LRsRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFtHRLTAETGAREQLE 1148
Cdd:pfam17380  385 ME-RQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM-ERVRLEEQERQQQV 462

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1149 KNLRQAAEEATRKaqalqaelqraKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQT 1228
Cdd:pfam17380  463 ERLRQQEEERKRK-----------KLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYE 531

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHgYKVLTARDGQQALSLYDQHagDIKAVITDILMPFMDGVELCRELRKR-DATLPIIVAS 1953
Cdd:cd17596      3 ILVVDDEVRSLEALRRTLEED-FDVLTAASAEEALAILEEE--WVQVILCDQRMPGTTGVEFLKEVRERwPEVVRIIISG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNArdampsggtLKFSAENVvvdesfihhrRATGAKPGNYVLFRVTDSGVGIPRDILPRIFEPFF------ 1808
Cdd:cd16939      1 MARALDNLLRNA---------LRYAHRTV----------RIALLVSGGRLTLIVEDDGPGIPAAARERVFEPFVrldpsr 61

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035  527 ARAQVEAdLRAAHQRFEQRVAELETDNQQLREQASRDTQAAT-----TQRGEQETALAELRAQLERTEAARQQIETTALD 601
Cdd:COG4913    608 NRAKLAA-LEAELAELEEELAEAEERLEALEAELDALQERREalqrlAEYSWDEIDVASAEREIAELEAELERLDASSDD 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  602 LRSnSEQQLSETQRQLADARQQLQAESERRAQAESALGQskseTERQLAEATAALADTRKQLEEATtkAAELQPVREQLA 681
Cdd:COG4913    687 LAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQ----AEEELDELQDRLEAAEDLARLEL--RALLEERFAAAL 759

                          170       180
                   ....*....|....*....|....
gi 1949443035  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 1949443035  225 ELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEK 304
Cdd:COG4913    349 RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  305 AELEKRTASSPAELEALRKRLSDEAtrrQLAEDDLR------SLREDFDKLQSSATQ-----------PD-------TAL 360
Cdd:COG4913    429 ASLERRKSNIPARLLALRDALAEAL---GLDEAELPfvgeliEVRPEEERWRGAIERvlggfaltllvPPehyaaalRWV 505

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  361 ETVHHRLHAETERVKRLETELESLRVALQT----------------EHEKAERADAERELSEEAMVQTNTGIqqrlmeln 424
Cdd:COG4913    506 NRLHLRGRLVYERVRTGLPDPERPRLDPDSlagkldfkphpfrawlEAELGRRFDYVCVDSPEELRRHPRAI-------- 577

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  425 aelerTKEELVAESARRtQAEAGQGGGEVNPEL----AARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAA 500
Cdd:COG4913    578 -----TRAGQVKGNGTR-HEKDDRRRIRSRYVLgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQ 651

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  501 AARAALEQQLAAASQagAGRSEADEAARAQVEA---DLRAAHQRFEQRVAELEtDNQQLREQASRDTQAATTQRGEQETA 577
Cdd:COG4913    652 RLAEYSWDEIDVASA--EREIAELEAELERLDAssdDLAALEEQLEELEAELE-ELEEELDELKGEIGRLEKELEQAEEE 728

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949443035  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 1949443035 1113 EEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANlelldiRS 1192
Cdd:PTZ00121  1057 EGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDAR------KA 1130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1193 RLDHEAAARRQAEEsAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARL 1272
Cdd:PTZ00121  1131 EEARKAEDARKAEE-ARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1273 EQERDERRRVVEsltqtsttlEARATESGSALEVTRRllNEERAARASALAELaarraevDRLTTEQPHAIEEATARLKA 1352
Cdd:PTZ00121  1210 EERKAEEARKAE---------DAKKAEAVKKAEEAKK--DAEEAKKAEEERNN-------EEIRKFEEARMAHFARRQAA 1271

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1353 QLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQR-----EDFDRRLGELTTALRTAEAK 1427
Cdd:PTZ00121  1272 IKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEakkkaDAAKKKAEEAKKAAEAAKAE 1351

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1428 AGSDSAELRHAHETlQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQT--TAELQTNLNAARAELDMLNRQfAQR 1505
Cdd:PTZ00121  1352 AEAAADEAEAAEEK-AEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDkkKADELKKAAAAKKKADEAKKK-AEE 1429

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1506 VAELDSTEARlREECAHRERAEAELDRMRDAQDGFQQS----TAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQ 1581
Cdd:PTZ00121  1430 KKKADEAKKK-AEEAKKADEAKKKAEEAKKAEEAKKKAeeakKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508

                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHagDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK11517     3 ILLIEDNQRTQEWVTQGLSEAGYVIDAVSDGRDGLYLALKD--DYALIILDIMLPGMDGWQILQTLRTAKQTPVICLTAR 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035  522 EADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRdtqaATTQRGEQETALAELRAQLERTEAARQQIETTALD 601
Cdd:COG4913    266 AARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELAR----LEAELERLEARLDALREELDELEAQIRGNGGDRLE 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  602 lrsNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLA 681
Cdd:COG4913    342 ---QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418

                          170
                   ....*....|....*...
gi 1949443035  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 1949443035 1199 AARRQAEESAKQGSASADQrlAERLSevQTLQERLRSEAAQRETTEVELrdTRAALEKQLAEASAALREASARLEQERDE 1278
Cdd:PRK10929    58 EERKGSLERAKQYQQVIDN--FPKLS--AELRQQLNNERDEPRSVPPNM--STDALEQEILQVSSQLLEKSRQAQQEQDR 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1279 RRRVVESLTQtsttLEARATESGSAL-EVTRRLLN-------EERAARASALAELAARRAEVDRLTTEQPHA-IEEATAR 1349
Cdd:PRK10929   132 AREISDSLSQ----LPQQQTEARRQLnEIERRLQTlgtpntpLAQAQLTALQAESAALKALVDELELAQLSAnNRQELAR 207

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1350 LKAQLAEQEREREQLRLAAM-SAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDfdrrlgELTTALRTAEAKA 1428
Cdd:PRK10929   208 LRSELAKKRSQQLDAYLQALrNQLNSQRQREAERALESTELLAEQSGDLPKSIVAQFKINR------ELSQALNQQAQRM 281

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1429 GSDSAELRHA-HETLQQAHAeltrrlterdseLASVREQAAALDAAGTraqqttaeLQTNLNAARAEL-DMLNRQfaqrv 1506
Cdd:PRK10929   282 DLIASQQRQAaSQTLQVRQA------------LNTLREQSQWLGVSNA--------LGEALRAQVARLpEMPKPQ----- 336

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1731 DASQLHRVLLNLAVNARDAMPSGGTLKFSAenvvvdesfihhrratGAKPGNYVLFrVTDSGVGIPRDILPRIFEPFFT- 1809
Cdd:cd16946      1 DRDRLQQLFVNLLENSLRYTDTGGKLRIRA----------------AQTPQEVRLD-VEDSAPGVSDDQLARLFERFYRv 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHG--YKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVA 1952
Cdd:cd19930      1 VLIAEDQEMVRGALAALLELEDdlEVVAQASNGQEALRLVLKHSPDV--AILDIEMPGRTGLEVAAELREELPDTKVLIV 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1107 AALKACEEEAArrsQAEEtARQSHTEFTHRLTAETGAREqlEKNLRQAAEEATRKAQALQAELQR--AKKELEKELADAN 1184
Cdd:PRK05035   436 AEIRAIEQEKK---KAEE-AKARFEARQARLEREKAARE--ARHKKAAEARAAKDKDAVAAALARvkAKKAAATQPIVIK 509

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1185 LELLDIRSRLDHEAAARR---QAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEA 1261
Cdd:PRK05035   510 AGARPDNSAVIAAREARKaqaRARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARA 589

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1262 SAALREASARLEQ------ERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRL 1335
Cdd:PRK05035   590 KAKKAAQQAASAEpeeqvaEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEP 669

                          250       260
                   ....*....|....*....|....*.
gi 1949443035 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 1949443035 1730 ADASQLHRVLLNLAVNArdampsggtLKFSAENVVVDESFihhrratgakPGNYVLFRVTDSGVGIPRDILPRIFEPfFT 1809
Cdd:PRK10604   315 LDMRLMERVLDNLLNNA---------LRYAHSRVRVSLLL----------DGNQACLIVEDDGPGIPPEERERVFEP-FV 374

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035  860 TKAELDQQLAALAEARSQAEREAAERRQTEESLL-----QASRSSEERVALLASELEAAREALRSESARREEL--ETALP 932
Cdd:TIGR00618  173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLtlctpCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLtqKREAQ 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  933 KTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHA------------AELKTLLATAREELHAETA 1000
Cdd:TIGR00618  253 EEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAvtqieqqaqrihTELQSKMRSRAKLLMKRAA 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1001 KRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETA-- 1078
Cdd:TIGR00618  333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQAti 412

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1079 -ARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARqshtefthRLTAETGAREQLEKNLRQAAEE 1157
Cdd:TIGR00618  413 dTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ--------ESAQSLKEREQQLQTKEQIHLQ 484

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1158 ATRKAQALQAELQRaKKELEKELadanlelldiRSRLDHEAAARRQAEESAkqgsasADQRLAERLSEvqtlqerlrsEA 1237
Cdd:TIGR00618  485 ETRKKAVVLARLLE-LQEEPCPL----------CGSCIHPNPARQDIDNPG------PLTRRMQRGEQ----------TY 537

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1238 AQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAA 1317
Cdd:TIGR00618  538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHAL 617

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1318 RASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRL 1397
Cdd:TIGR00618  618 LRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKE 697

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1398 RLELTWQMQREDfDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAaldaagtra 1477
Cdd:TIGR00618  698 MLAQCQTLLREL-ETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNN--------- 767

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1478 QQTTAELQT--NLNAARAELDMLNRQFAQRVAELDSTEARLREECAHREraeaelDRMRDAQDGFQQSTAELNERLTRLT 1555
Cdd:TIGR00618  768 EEVTAALQTgaELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDE------DILNLQCETLVQEEEQFLSRLEEKS 841

                          730       740
                   ....*....|....*....|....*..
gi 1949443035 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 1949443035 1210 QGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQT 1289
Cdd:COG4942     16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1290 STTLEARATESGSALEVTRR---------LLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQERE 1360
Cdd:COG4942     96 RAELEAQKEELAELLRALYRlgrqpplalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1162 AQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRE 1241
Cdd:COG3903    500 ALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAA 579

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1242 TTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASA 1321
Cdd:COG3903    580 AALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 659

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1322 LAELAARRAEVDRLTTEQPHAIEEATARLkaqLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLEL 1401
Cdd:COG3903    660 AAAAAALAAAAAAAAAAAAAAAAAAAALA---AAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAAL 736

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1402 TWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTT 1481
Cdd:COG3903    737 AAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAL 816

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1482 AELQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAA 1561
Cdd:COG3903    817 AAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAA 896

                          410       420       430
                   ....*....|....*....|....*....|....
gi 1949443035 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 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLydQHAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK09836     3 LLIVEDEKKTGEYLTKGLTEAGFVVDLADNGLNGYHL--AMTGDYDLIILDIMLPDVNGWDIVRMLRSANKGMPILLLTA 80

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035 1735 LHRVLLNLAVNARDAMPSGGTLKFSAEnvvvdesfihhRRATGAKpgnyvlFRVTDSGVGIPRDILPRIFEPFFTTKEPG 1814
Cdd:cd16952      1 LRSAFSNLVSNAVKYTPPSDTITVRWS-----------QEESGAR------LSVEDTGPGIPPEHIPRLTERFYRVDIER 63

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1342 AIEEATARLKAQLAEQEREREQLrlaamsaEQRLRDRATDFEAANAALRgEMEKRLRlELTWQMQREdFDRRLGELTTAL 1421
Cdd:TIGR02169  234 ALERQKEAIERQLASLEEELEKL-------TEEISELEKRLEEIEQLLE-ELNKKIK-DLGEEEQLR-VKEKIGELEAEI 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1422 RTAEAKAGSDSAELRHAHETLQQAhaeltrrlterDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLnrq 1501
Cdd:TIGR02169  304 ASLERSIAEKERELEDAEERLAKL-----------EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDL--- 369

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1502 fAQRVAELDSTEARLREECAHR----ERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLED 1577
Cdd:TIGR02169  370 -RAELEEVDKEFAETRDELKDYreklEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKAL 448

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1162 AQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQgsasADQRLAERLSEVQTLQERLRSEAAQRE 1241
Cdd:COG4942     18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA----LARRIRALEQELAALEAELAELEKEIA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1242 TTEVELRDTRAALEKQL-----------------AEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSAL 1304
Cdd:COG4942     94 ELRAELEAQKEELAELLralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1305 EVTRRLLNEERAARASALAELAARRAEVDRLTTEQphaieeatARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEA 1384
Cdd:COG4942    174 AELEALLAELEEERAALEALKAERQKLLARLEKEL--------AELAAELAELQQEAEELEALIARLEAEAAAAAERTPA 245

                          250
                   ....*....|
gi 1949443035 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 1949443035  335 AEDDLRSLREDFDKLQSSATQPDTALETVHH-----RLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEeam 409
Cdd:COG4913    223 TFEAADALVEHFDDLERAHEALEDAREQIELlepirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--- 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  410 vqtntgIQQRLMELNAELERTKEELVAESARRTQAEA---GQGGGEVNpELAARIAALTEAKAQVEKELVEQQAVAKALG 486
Cdd:COG4913    300 ------LRAELARLEAELERLEARLDALREELDELEAqirGNGGDRLE-QLEREIERLERELEERERRRARLEALLAALG 372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  487 dernrlaqelaEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQa 566
Cdd:COG4913    373 -----------LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPA- 440

                          250       260
                   ....*....|....*....|....*
gi 1949443035  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 1949443035  519 GRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQasrdtqaattqrgeqetalaelRAQLERTEAARQQiETT 598
Cdd:TIGR00618  194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREA----------------------LQQTQQSHAYLTQ-KRE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  599 ALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKseterqLAEATAALADTRKQLEEATTKAAELQPVRE 678
Cdd:TIGR00618  251 AQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP------LAAHIKAVTQIEQQAQRIHTELQSKMRSRA 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  679 QLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAET 758
Cdd:TIGR00618  325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDI 404

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  759 ERREQAESALGQSKSETERQ----LAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLaDQDAELKKTWDNLIK 834
Cdd:TIGR00618  405 LQREQATIDTRTSAFRDLQGqlahAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL-KEREQQLQTKEQIHL 483

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  835 ETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARS------QAEREAAERRQTEESLLQASRSSEERVALLAS 908
Cdd:TIGR00618  484 QETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPltrrmqRGEQTYAQLETSEEDVYHQLTSERKQRASLKE 563

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  909 ELEAAREALRSESARREELETALPKTKTELGQ-RLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTL 987
Cdd:TIGR00618  564 QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRlQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELAL 643

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  988 LATAREELHAETAKRDAAEAAASqVRAELEATNAESSRALAAAQNELARESAERETTEaefqrsksALAQQLAEAAAAQA 1067
Cdd:TIGR00618  644 KLTALHALQLTLTQERVREHALS-IRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA--------QCQTLLRELETHIE 714

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1068 ELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTH----------RL 1137
Cdd:TIGR00618  715 EYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHlaaeiqffnrLR 794

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035 1670 AQRGADIVKQVLTFARGfhgERAPVS--------PEMLvRDIAKSVQETFPRNVRVSSEVADDLPlISADASQLHRVLLN 1741
Cdd:PRK11006   250 TQRMEGLVKQLLTLSKI---EAAPTIdlnekvdvPMML-RVLEREAQTLSQGKHTITFEVDNSLK-VFGNEDQLRSAISN 324

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1742 LAVNARDAMPSGGTLKFSAENVvvdesfihhrrATGAKpgnyvlFRVTDSGVGIPRDILPRIFEPFF-----TTKEPGQS 1816
Cdd:PRK11006   325 LVYNAVNHTPEGTHITVRWQRV-----------PQGAE------FSVEDNGPGIAPEHIPRLTERFYrvdkaRSRQTGGS 387

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035 1898 KVLTARDGQQALS-LYDQHAGDIKA----VITDILMPFMDGVELCRELRKRDAT--LPIIVASGMGHEKFVTDLRELGVP 1970
Cdd:cd17557     27 ELHVVRDGEEALDfLRGEGEYADAPrpdlILLDLNMPRMDGFEVLREIKADPDLrrIPVVVLTTSDAEEDIERAYELGAN 106

                           90
                   ....*....|....*...
gi 1949443035 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 1949443035 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 1949443035  317 ELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKRLETELESLRVALQTEHEKAE 396
Cdd:pfam02463  167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  397 RADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPELaaRIAALTEAKAQVEKELV 476
Cdd:pfam02463  247 RDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER--RKVDDEEKLKESEKEKK 324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  477 EQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQagagRSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQL 556
Cdd:pfam02463  325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEK----LQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELK 400

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  557 REQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAES 636
Cdd:pfam02463  401 SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  637 ALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAE 716
Cdd:pfam02463  481 KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEV 560

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  717 AAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQaesalgqsKSETERQLAEATAALAEVRAQLEQA 796
Cdd:pfam02463  561 EERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQ--------LDKATLEADEDDKRAKVVEGILKDT 632

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  797 TTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARS 876
Cdd:pfam02463  633 ELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEEL 712

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  877 QAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARM 956
Cdd:pfam02463  713 KKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  957 DFEAAERERVEAAWKLANSATEQHAAELKTLLATArEELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELAR 1036
Cdd:pfam02463  793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQE-EKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1037 ESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADL-DAALKACEEE 1115
Cdd:pfam02463  872 LLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELlLEEADEKEKE 951

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1116 AARRSQAEETARQSHTEFTHRLTAETGAREQLEKNL--RQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSR 1193
Cdd:pfam02463  952 ENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEerYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINK 1031

                          890
                   ....*....|....*.
gi 1949443035 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 1949443035  534 DLRAAHQRFEQRVAEletdnQQLREQASRDTQAaTTQRGEQETALAELRAQLER--------TEAARQQIETTALDL--- 602
Cdd:NF041483    98 DARAQTQRILQEHAE-----HQARLQAELHTEA-VQRRQQLDQELAERRQTVEShvnenvawAEQLRARTESQARRLlde 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  603 -RSNSEQQLS----ETQRQLADARQQLQAESER-RAQAESALGQSKSETERQLAEATAaladtrkQLEEATTKAAELqpv 676
Cdd:NF041483   172 sRAEAEQALAaaraEAERLAEEARQRLGSEAESaRAEAEAILRRARKDAERLLNAAST-------QAQEATDHAEQL--- 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  677 REQLAGEVQRGERAEAELFRSRSELETQQAALAElraraeaaeaarlqvETTAQQSRTVAEQAAAEAQQQLAALRQQLQA 756
Cdd:NF041483   242 RSSTAAESDQARRQAAELSRAAEQRMQEAEEALR---------------EARAEAEKVVAEAKEAAAKQLASAESANEQR 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  757 ETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAElkktwDNLIKET 836
Cdd:NF041483   307 TRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAE-----EVLTKAS 381

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  837 EDREALEKqlaAARGDLERQLAETKAELDQQLAALAEARSQ----AEREAAERRQTEESLLQASRSSEERVALLASELEA 912
Cdd:NF041483   382 EDAKATTR---AAAEEAERIRREAEAEADRLRGEAADQAEQlkgaAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVA 458

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  913 AREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEqhaaelkTLLATAR 992
Cdd:NF041483   459 EGERIRGEARREAVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERATTLRRQAEE-------TLERTRA 531

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  993 EELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAeRETTEAEfQRSKSALAQQLAEAAAAQAELRSR 1072
Cdd:NF041483   532 EAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELT-RLHTEAE-ERLTAAEEALADARAEAERIRREA 609

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1073 LEKETAARHETERELRESLTDAERTTEALQADldaalkACEEEAARRSQAEETARQSHTEFT---HRLTAEtgAREQLEK 1149
Cdd:NF041483   610 AEETERLRTEAAERIRTLQAQAEQEAERLRTE------AAADASAARAEGENVAVRLRSEAAaeaERLKSE--AQESADR 681

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1150 NLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEaaaRRQAEESAKQGSASADQRLAERLSEVQTL 1229
Cdd:NF041483   682 VRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQE---RERAREQSEELLASARKRVEEAQAEAQRL 758

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1230 QERLRSEAAQ----RETTEVELRDTRAALEKQLAEASAALREAsARLEQERDERRRVVESLTQTSTTLEARATESGSALE 1305
Cdd:NF041483   759 VEEADRRATElvsaAEQTAQQVRDSVAGLQEQAEEEIAGLRSA-AEHAAERTRTEAQEEADRVRSDAYAERERASEDANR 837

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1306 VTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATD---- 1381
Cdd:NF041483   838 LRREAQEETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAAAqadr 917

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1382 --FEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELR-HAHETL--QQAHAELTRRLTER 1456
Cdd:NF041483   918 liGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRaEAAETVgsAQQHAERIRTEAER 997

                          970       980       990      1000      1010      1020      1030
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035  898 SSEERVALLASELEAAREALRSESARREELETALpktkTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLAN-SA 976
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAEL----DALQERREALQRLAEYSWDEIDVASAEREIAELEAELERlDA 682

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  977 TEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAEssraLAAAQNELARESAERETTEAEFQRSKSALA 1056
Cdd:COG4913    683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE----LDELQDRLEAAEDLARLELRALLEERFAAA 758

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1057 QQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETarqshtefthr 1136
Cdd:COG4913    759 LGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEED----------- 827

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1137 ltaetGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDI-------------RSRLDHEAAARRQ 1203
Cdd:COG4913    828 -----GLPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDPLNDSLKRIpfgpgrylrlearPRPDPEVREFRQE 902

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035  839 REALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEervallasELEAAREALR 918
Cdd:COG4717     44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELE--------ELEAELEELR 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  919 SESARREELETALPKTKtelgQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSatEQHAAELKTLLATAREELHAE 998
Cdd:COG4717    116 EELEKLEKLLQLLPLYQ----ELEALEAELAELPERLEELEERLEELRELEEELEEL--EAELAELQEELEELLEQLSLA 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  999 TAKRDAAEAAAsqvRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETA 1078
Cdd:COG4717    190 TEEELQDLAEE---LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGG 266

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1079 ARHETERELRESLTDAERTTeALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEA 1158
Cdd:COG4717    267 SLLSLILTIAGVLFLVLGLL-ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR 345

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1159 TRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEesakqgsasADQRLAERLSEVQTLQERLRSEAA 1238
Cdd:COG4717    346 IEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE---------QAEEYQELKEELEELEEQLEELLG 416

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1239 QREttEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQ--TSTTLEARATESGSALEVTRRLLNEERA 1316
Cdd:COG4717    417 ELE--ELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQleEDGELAELLQELEELKAELRELAEEWAA 494


                   ...
gi 1949443035 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 1949443035  188 NERKVADDTRTTDQAAALDAALARVQQEVSYRkeiglELERRADELKKRDSELE----SANRQLWAELSGREQVEAeLAK 263
Cdd:PRK04863   279 NERRVHLEEALELRRELYTSRRQLAAEQYRLV-----EMARELAELNEAESDLEqdyqAASDHLNLVQTALRQQEK-IER 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  264 ARGELDKqvaertatftdiisgLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRrqlaeddlrslr 343
Cdd:PRK04863   353 YQADLEE---------------LEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQA------------ 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  344 edFDKLQSSA---TQPDTALETVHHRLHAETERVKRLETELESLRVALQTEHEkaERADAERELSeeamvqtntgiqqrl 420
Cdd:PRK04863   406 --LDVQQTRAiqyQQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATE--ELLSLEQKLS--------------- 466

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  421 melNAELERTKEELVAESARRTqaeagqgGGEVNPELAARIAalteakAQVEKELVEQQAVAKALGDERNRLAQELAEAA 500
Cdd:PRK04863   467 ---VAQAAHSQFEQAYQLVRKI-------AGEVSRSEAWDVA------RELLRRLREQRHLAEQLQQLRMRLSELEQRLR 530

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  501 AARAALEQQLAAASQAGAGRSEADEAARAQVEA-----DLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQE 575
Cdd:PRK04863   531 QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELearleSLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQD 610

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949443035  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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASg 1954
Cdd:cd19928      1 ILVADDDRAIRTVLTQALGRAGYEVRTTGNAATLWRWVEEGEGDL--VITDVVMPDENGLDLIPRIKKARPDLPIIVMS- 77

                           90       100
                   ....*....|....*....|....
gi 1949443035 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 1949443035 1096 RTTEALQADLDAALKACEEEAARRSQAEEtARQSHTEFTHRLTAETGAREQLEKNLRQAAE--EATRKAQALQAELQRAK 1173
Cdd:PRK04863   276 RHANERRVHLEEALELRRELYTSRRQLAA-EQYRLVEMARELAELNEAESDLEQDYQAASDhlNLVQTALRQQEKIERYQ 354

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1174 KELEKelADANLELLDIRSRLDHEAAARRQAEESAKQGSAsadQRLAERLSEVQTLQERLRSEAAQretteveLRDTRAA 1253
Cdd:PRK04863   355 ADLEE--LEERLEEQNEVVEEADEQQEENEARAEAAEEEV---DELKSQLADYQQALDVQQTRAIQ-------YQQAVQA 422

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1254 LEK---QLAEASAALREASARLEQERDERRRVVESLTQTSTTL---EARATESGSALEVTRRLLNEERAARASALAELAA 1327
Cdd:PRK04863   423 LERakqLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLsvaQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELL 502

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1328 RraevdRLTTEQPHAieEATARLKAQLAEQEREREQLRlaamSAEQRLRdratdfeaanaalrgEMEKRLRLELTWQMQR 1407
Cdd:PRK04863   503 R-----RLREQRHLA--EQLQQLRMRLSELEQRLRQQQ----RAERLLA---------------EFCKRLGKNLDDEDEL 556

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1408 EDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTE---RDSELASVREQAAALDAAGTRAQQTTAEL 1484
Cdd:PRK04863   557 EQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQL 636

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1725 LPLISADASQLHR------------VLLNLAVNARDAmpsggTLKFSAENVVVdESFIhhrratgAKPGNYVLFRVTDSG 1792
Cdd:PRK15053   411 LKMVIVPGSQLSQlppgldstefaaIVGNLLDNAFEA-----SLRSDEGNKIV-ELFL-------SDEGDDVVIEVADQG 477

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 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 1949443035 1342 AIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTAL 1421
Cdd:COG4942     31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1422 RTAEAKAGSDSAELRHAHETLQQA------HAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAEL 1495
Cdd:COG4942    111 RALYRLGRQPPLALLLSPEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1949443035 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 1949443035  283 ISGLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAED-DLRSLREDFDKLQSSATQPDTA-L 360
Cdd:pfam12128  260 LSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADaAVAKDRSELEALEDQHGAFLDAdI 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  361 ETVHhrLHAETERVKRLETELESLRVALQTE-HEKAERA-DAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVA-- 436
Cdd:pfam12128  340 ETAA--ADQEQLPSWQSELENLEERLKALTGkHQDVTAKyNRRRSKIKEQNNRDIAGIKDKLAKIREARDRQLAVAEDdl 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  437 ---ESARRTQAEAGQGggEVNPELAARIAALTEAK-----AQVEKELVEQQAVAKALGD-----------ERNRLAQELA 497
Cdd:pfam12128  418 qalESELREQLEAGKL--EFNEEEYRLKSRLGELKlrlnqATATPELLLQLENFDERIErareeqeaanaEVERLQSELR 495

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  498 EAAAARAALEQQLAAASQAGAGRSEADEAARAQVEAD-------LRAAHQRFEQRVAEL-------ETD----------- 552
Cdd:pfam12128  496 QARKRRDQASEALRQASRRLEERQSALDELELQLFPQagtllhfLRKEAPDWEQSIGKVispellhRTDldpevwdgsvg 575

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  553 -----------------------NQQLRE---QASRDTQAATTQRGEQETALAELRAQLERTEA----ARQQIETTALDL 602
Cdd:pfam12128  576 gelnlygvkldlkridvpewaasEEELRErldKAEEALQSAREKQAAAEEQLVQANGELEKASReetfARTALKNARLDL 655

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  603 RsnseqQLSETQRQLADARQQlqAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVRE---- 678
Cdd:pfam12128  656 R-----RLFDEKQSEKDKKNK--ALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEgald 728

                          490       500
                   ....*....|....*....|....*..
gi 1949443035  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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLydQHAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK11083     6 ILLVEDEQAIADTLVYALQSEGFTVEWFERGLPALDK--LRQQPPDLVILDVGLPDISGFELCRQLLAFHPALPVIFLTA 83

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035  304 KAELEKRTASSPAELEALRKRLSDEATRRQlaedDLRSLREDFDKLQSS------ATQPDTALETVHHRLHAETERVKRL 377
Cdd:PRK04863   781 RAAREKRIEQLRAEREELAERYATLSFDVQ----KLQRLHQAFSRFIGShlavafEADPEAELRQLNRRRVELERALADH 856

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  378 ETELESLRVALQTEHEkaeRADAERELSEEAMVQTNTGIQQRLMELNAELERtkeelvAESARRTQAEAGQGGGEVNPEL 457
Cdd:PRK04863   857 ESQEQQQRSQLEQAKE---GLSALNRLLPRLNLLADETLADRVEEIREQLDE------AEEAKRFVQQHGNALAQLEPIV 927

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  458 AA------RIAALTEAKAQVEKELVEQQAVAKALGDERNRL-----AQELAEAAAARAALEQQLAAASQAGAGRSEADEA 526
Cdd:PRK04863   928 SVlqsdpeQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRahfsyEDAAEMLAKNSDLNEKLRQRLEQAEQERTRAREQ 1007

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  527 ARA---------QVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRgeQETALAELRAQLERTEAARQQIET 597
Cdd:PRK04863  1008 LRQaqaqlaqynQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGAEERARAR--RDELHARLSANRSRRNQLEKQLTF 1085

                          330       340
                   ....*....|....*....|....*..
gi 1949443035  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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIKAVITDILMPFMDGVELCRELRKR--DATLPIIVA 1952
Cdd:cd19933      3 VLLVDDNAVNRMVTKGLLEKLGCEVTTVSSGEECLNLLASAEHSFQLVLLDLCMPEMDGFEVALRIRKLfgRRERPLIVA 82

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1949443035 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 1949443035   96 GDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEKE-FRLDFRLRNKDGSTRWVAGHAMRVLDDH 174
Cdd:PRK09776   303 GQWLQVNKALCQFLGYSQEELRGLTFQQLTWPEDLNKDLQQVEKLLSGEINsYSMEKRYYRRDGEVVWALLAVSLVRDTD 382

                           90
                   ....*....|....*....
gi 1949443035  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 1949443035 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 1949443035  586 ERTEAARQQIETTaldlrsnsEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEE 665
Cdd:TIGR02169  170 RKKEKALEELEEV--------EENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEA 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  666 ATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVEttaqqsrtvaeqaaaeaqq 745
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE------------------- 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  746 qlaalrqqlqaeterREQAESALGQSKSETERQLAEATAALAEVRAQLEQATtassqreaeakqaaaaqqqKLADQDAEL 825
Cdd:TIGR02169  303 ---------------IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE-------------------ELEREIEEE 348

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  826 KKTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQqlaaLAEARSQAEREAAERRQTEESLLQASRSSEERVAL 905
Cdd:TIGR02169  349 RKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD----YREKLEKLKREINELKRELDRLQEELQRLSEELAD 424

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  906 LASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAG-LRARMDFEAAERERVEAAWKLANSATEQHAAEl 984
Cdd:TIGR02169  425 LNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQElYDLKEEYDRVEKELSKLQRELAEAEAQARASE- 503

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  985 ktllATAREELHAETAKRDAAEAAASQVrAELEATNAESSRAL-AAAQNELARESAERETTEAEFQRSKSALAQQLAEAA 1063
Cdd:TIGR02169  504 ----ERVRGGRAVEEVLKASIQGVHGTV-AQLGSVGERYATAIeVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFL 578

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1064 AAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAET-G 1142
Cdd:TIGR02169  579 PLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTgG 658

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1143 AREQLEKNLRQAAEEAtrKAQALQAELQrakkELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASAdQRLAER 1222
Cdd:TIGR02169  659 SRAPRGGILFSRSEPA--ELQRLRERLE----GLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEI-EQLEQE 731

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1223 LSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQ-ERDERRRVVESLTQTSTTLEARATESG 1301
Cdd:TIGR02169  732 EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIE 811

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1302 SALEVTRRLLNEERAARASALAELAARRAEVdRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATD 1381
Cdd:TIGR02169  812 ARLREIEQKLNRLTLEKEYLEKEIQELQEQR-IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE 890

                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1074 EKETAARHETERELRESLTDAERTTEALQADLDA-ALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLR 1152
Cdd:COG3899    738 DPEEEYRLALLLELAEALYLAGRFEEAEALLERAlAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELAL 817

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1153 QAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQER 1232
Cdd:COG3899    818 ALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLL 897

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1233 LRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLN 1312
Cdd:COG3899    898 AAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAA 977

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1313 EERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGE 1392
Cdd:COG3899    978 AAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAA 1057

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1393 MEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDA 1472
Cdd:COG3899   1058 AAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLL 1137

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1473 AGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLT 1552
Cdd:COG3899   1138 LAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLAL 1217

                          490       500
                   ....*....|....*....|....*..
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAtLPIIVASG 1954
Cdd:PRK10529     4 VLIVEDEQAIRRFLRTALEGDGMRVFEAETLQRGLLEAATRKPDL--IILDLGLPDGDGIEFIRDLRQWSA-IPVIVLSA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035  232 ELKKRDSELESANRQlwaelsgREQVEAELAKARGELdKQVAERTATFTDIISGLEKAVAEHELAVKTLQAEKAELEKR- 310
Cdd:COG1579     11 DLQELDSELDRLEHR-------LKELPAELAELEDEL-AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  311 -TASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQssatqpdTALETVHHRLHAETERVKRLETELESLRVALQ 389
Cdd:COG1579     83 gNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELE-------EELAELEAELAELEAELEEKKAELDEELAELE 155

                          170       180
                   ....*....|....*....|
gi 1949443035  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 1949443035  527 ARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSN- 605
Cdd:pfam15921  254 SQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSEl 333

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  606 ------SEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLA-------EATAALADTRKQLEEATTKAAE 672
Cdd:pfam15921  334 reakrmYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLAdlhkrekELSLEKEQNKRLWDRDTGNSIT 413

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  673 LQPVREQLAGEVQRGERAEAELFRSRSE----LETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQqla 748
Cdd:pfam15921  414 IDHLRRELDDRNMEVQRLEALLKAMKSEcqgqMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMT--- 490

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  749 alrqqlqaeTERREQAESALGQSKSETERQLAEATAALAEVRAQ--LEQATTASSQREAEAKQAAAAQQQKLADQDAELK 826
Cdd:pfam15921  491 ---------LESSERTVSDLTASLQEKERAIEATNAEITKLRSRvdLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKD 561

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  827 KTWDNLIKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEEsllQASRSSEERVALL 906
Cdd:pfam15921  562 KVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEA---RVSDLELEKVKLV 638

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  907 ASELEAAReALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKT 986
Cdd:pfam15921  639 NAGSERLR-AVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKS 717

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  987 LLATAREELHAE-------TAKRDAAEAAASQVRAELEA-TNAESSRA-LAAAQNELARE----SAERETTEAEFQRSKS 1053
Cdd:pfam15921  718 MEGSDGHAMKVAmgmqkqiTAKRGQIDALQSKIQFLEEAmTNANKEKHfLKEEKNKLSQElstvATEKNKMAGELEVLRS 797

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1054 ALAQ-QLAEAAAAQAELRSRLE----KETAARHETER---ELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEET 1125
Cdd:pfam15921  798 QERRlKEKVANMEVALDKASLQfaecQDIIQRQEQESvrlKLQHTLDVKELQGPGYTSNSSMKPRLLQPASFTRTHSNVP 877

                          650       660       670
                   ....*....|....*....|....*....|...
gi 1949443035 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 1949443035  1144 REQLEKNLRQAAEEATrkaqalqAELQRAKKELEKELADANLELLDIRSRLD---HEAAARRQAEESAKQGSASADQRLA 1220
Cdd:smart00787  138 RMKLLEGLKEGLDENL-------EGLKEDYKLLMKELELLNSIKPKLRDRKDaleEELRQLKQLEDELEDCDPTELDRAK 210

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1949443035  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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT--LPIIVA 1952
Cdd:PRK10161     5 ILVVEDEAPIREMVCFVLEQNGFQPVEAEDYDSAVNQLNEPWPDL--ILLDWMLPGGSGIQFIKHLKRESMTrdIPVVML 82

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDikAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:cd17563      3 LLLVDDDEVFAERLARALERRGFEVETAHSVEEALALAREEKPD--YAVLDLRLGGDSGLDLIPPLRALQPDARIVVLTG 80

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1145 EQLEKNLRQAAEEATRKAQalqaeLQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQgsasadQRLAERLS 1224
Cdd:COG4717     74 KELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL------EALEAELA 142

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1225 EVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQErderrrvVESLTQTSTTLEARATESGSAL 1304
Cdd:COG4717    143 ELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEE-------LQDLAEELEELQQRLAELEEEL 215

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1305 EVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEA 1384
Cdd:COG4717    216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAR 295

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1385 ANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAH-AELTRRLTERDSELASV 1463
Cdd:COG4717    296 EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEeLEEELQLEELEQEIAAL 375

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1464 REQAAALDAAGTRAQQTTAELQTNLNAARAEL-DMLNRQFAQRVAELDS-TEARLREECAHRERAEAELDRMRDAQdgfQ 1541
Cdd:COG4717    376 LAEAGVEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEEL---R 452

                          410       420       430
                   ....*....|....*....|....*....|..
gi 1949443035 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 1949443035  988 LATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQA 1067
Cdd:TIGR00606  398 LVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1068 ELRSRLEKETAARHETEreLRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAEtgarEQL 1147
Cdd:TIGR00606  478 QELRKAERELSKAEKNS--LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKD----EQI 551

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1148 EKNLRQAAEEATRKAQALQAelqraKKELEKELADANLELLDIRSRLdheaAARRQAEESAKQGSASADQRLAERLSEVQ 1227
Cdd:TIGR00606  552 RKIKSRHSDELTSLLGYFPN-----KKQLEDWLHSKSKEINQTRDRL----AKLNKELASLEQNKNHINNELESKEEQLS 622

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1228 TLQERLrSEAAQRETTEVELRDTRAALEK---QLAEASAALREASARLEQERDERR-------RVVES---LTQTSTTLE 1294
Cdd:TIGR00606  623 SYEDKL-FDVCGSQDEESDLERLKEEIEKsskQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTeaeLQEFISDLQ 701

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1295 ARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQP------HAIEEATARLKAQLAEQEREREQLRLAA 1368
Cdd:TIGR00606  702 SKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPelrnklQKVNRDIQRLKNDIEEQETLLGTIMPEE 781

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1369 MSAE---------QRLRDRATDFEAANAALRGEMEKrLRLELTWQMQREDFDRRLGELTTALRTAE-------------- 1425
Cdd:TIGR00606  782 ESAKvcltdvtimERFQMELKDVERKIAQQAAKLQG-SDLDRTVQQVNQEKQEKQHELDTVVSKIElnrkliqdqqeqiq 860

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1426 ---AKAGSDSAELRHAHETLQQAHA------ELTRRLTERDSELASVREQAAALDAAGTRAQQTTAEL-----------Q 1485
Cdd:TIGR00606  861 hlkSKTNELKSEKLQIGTNLQRRQQfeeqlvELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELissketsnkkaQ 940

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1486 TNLNAARAELDML---------------NRQFAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNER 1550
Cdd:TIGR00606  941 DKVNDIKEKVKNIhgymkdienkiqdgkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDN 1020

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1551 LTRLT-----TDVEAARQQAEQETTQRRSLEDALQQSHGEVELR--------VSERTAGLNAHVQQLEAELAEAQ--RAE 1615
Cdd:TIGR00606 1021 LTLRKrenelKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDlikrnhvlALGRQKGYEKEIKHFKKELREPQfrDAE 1100

                          730
                   ....*....|...
gi 1949443035 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 1949443035 1867 LPRGNGELLMLADDEQGVLDVTAEILEWhGYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDAT 1946
Cdd:PRK10365     1 MTHDNIDILVVDDDISHCTILQALLRGW-GYNVALANSGRQALEQVREQVFDL--VLCDVRMAEMDGIATLKEIKALNPA 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1263 AALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRltteqphA 1342
Cdd:COG3903    549 AALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAA-------A 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1343 IEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALR 1422
Cdd:COG3903    622 ALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAA 701

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1423 TAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQF 1502
Cdd:COG3903    702 ALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAA 781

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1503 AQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQS 1582
Cdd:COG3903    782 AAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAA 861

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035 1071 SRLEKETAARHETERELRESLTDAERTTEALQADLDAALKAceeEAARRSQAE---------ETARQSHTEFTHRLTAET 1141
Cdd:pfam07111   69 SRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVA---EKAGQAEAEglraalagaEMVRKNLEEGSQRELEEI 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1142 GAREQLE-KNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELldirsrldheAAARRQAEESAKQGSasadqRLA 1220
Cdd:pfam07111  146 QRLHQEQlSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQL----------AEAQKEAELLRKQLS-----KTQ 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1221 ERLSEVQTLQERLRSEAAQRETTEVElRDTRAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEARATES 1300
Cdd:pfam07111  211 EELEAQVTLVESLRKYVGEQVPPEVH-SQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRK 289

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1301 GSALEVtrrLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQerereQLRLAAMSAEQRLRDRAT 1380
Cdd:pfam07111  290 IQPSDS---LEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAEL-----QEQVTSQSQEQAILQRAL 361

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1381 DFEAANAALRGEMEKRLRLELT--------WQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELT-- 1450
Cdd:pfam07111  362 QDKAAEVEVERMSAKGLQMELSraqearrrQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSya 441

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1451 -------RRLTERDSELASVREQAAALDAAgtrAQQTTAELQTNLNAARAELDMLNrqfaqrvAELDSTEARLREECAH- 1522
Cdd:pfam07111  442 vrkvhtiKGLMARKVALAQLRQESCPPPPP---APPVDADLSLELEQLREERNRLD-------AELQLSAHLIQQEVGRa 511

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1523 RERAEAELDRMRDAQDGFQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLE-----------DALQQSHGEVELRVS 1591
Cdd:pfam07111  512 REQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRqeltqqqeiygQALQEKVAEVETRLR 591

                          570       580       590
                   ....*....|....*....|....*....|
gi 1949443035 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 1949443035 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 1949443035  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 1949443035 1011 QVRAELEATNAESsrALAAAQNELARESAERETTEAEFQRsksalaqqlaeaAAAQAELRSRLEKETAARHETERELRES 1090
Cdd:pfam00529   46 DVLFQLDPTDYQA--ALDSAEAQLAKAQAQVARLQAELDR------------LQALESELAISRQDYDGATAQLRAAQAA 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1091 LTDAERTTEALQADLdAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEE--ATRKAQALQAE 1168
Cdd:pfam00529  112 VKAAQAQLAQAQIDL-ARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAEnqAEVRSELSGAQ 190

                          170       180
                   ....*....|....*....|....*..
gi 1949443035 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 1949443035 1730 ADASQLHRVLLNLAVNA----RDAMPSGGTLKFSAENVVVDesfihhrratgakpgnyvlfrVTDSGVGIPRDILPRIFE 1805
Cdd:cd16947     16 ANTEALQRILKNLISNAikygSDGKFLGMTLREDEKHVYID---------------------IWDKGKGISETEKDHVFE 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035  525 EAARAQVEA--DLRAAHQRFEQRVAELETdNQQLREQAsrDTQAATTQRGEQETALAELRAQLERTEAARQQIEttaldl 602
Cdd:COG4913    245 EDAREQIELlePIRELAERYAAARERLAE-LEYLRAAL--RLWFAQRRLELLEAELEELRAELARLEAELERLE------ 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  603 rsnseQQLSETQRQLADARQQLQAESerraqaesalGQSKSETERQLAEATAALADTRKQLE-----------EATTKAA 671
Cdd:COG4913    316 -----ARLDALREELDELEAQIRGNG----------GDRLEQLEREIERLERELEERERRRArleallaalglPLPASAE 380

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1949443035  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 1949443035 1097 TTEALQADLDAALKACEEEAarrsqaEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKK-- 1174
Cdd:PRK11281    37 TEADVQAQLDALNKQKLLEA------EDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDdn 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1175 --------------ELEKELADANLELLDIRSRL---DHEAAARRQAEESAKQGSASADQRLAE---RLSEVQTLQERLR 1234
Cdd:PRK11281   111 deetretlstlslrQLESRLAQTLDQLQNAQNDLaeyNSQLVSLQTQPERAQAALYANSQRLQQirnLLKGGKVGGKALR 190

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035   84 AAPAGIFRANQQGDILFVNHRWSALTGRSQAESQGFGWLLAVHPDDNKRVTEEWRKCVRGEK-EFRLDFRLRNkdGSTRW 162
Cdd:pfam08448    3 SLPDALAVLDPDGRVRYANAAAAELFGLPPEELLGKTLAELLPPEDAARLERALRRALEGEEpIDFLEELLLN--GEERH 80

                           90       100
                   ....*....|....*....|....*....
gi 1949443035  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 1949443035  839 REALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQtEESLLQASRSSEERVALLASELEAAREALR 918
Cdd:COG3899    769 ERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELAL-ALAERLGDRRLEARALFNLGFILHWLGPLR 847

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  919 SESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAE 998
Cdd:COG3899    848 EALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAA 927

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  999 TAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETA 1078
Cdd:COG3899    928 AAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAA 1007

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1079 ARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEA 1158
Cdd:COG3899   1008 AAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAA 1087

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1159 TRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAA 1238
Cdd:COG3899   1088 LAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALA 1167

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035  282 IISGLEKAVAEHELAVKTLQAEKAELEKRTASSPAELEALrKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQPDTALE 361
Cdd:COG5278     70 LLTGDESFLEPYEEARAEIDELLAELRSLTADNPEQQARL-DELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGK 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  362 TVHHRLHAETERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARR 441
Cdd:COG5278    149 ALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  442 TQAEAGQGGGEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRS 521
Cdd:COG5278    229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  522 EADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALD 601
Cdd:COG5278    309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  602 LRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLA 681
Cdd:COG5278    389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1949443035  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 1949443035  514 SQAGAGRSEADEAARAQVEADLRAAHQRfeqrvaELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLErteaarq 593
Cdd:PRK11281    24 SAFARAASNGDLPTEADVQAQLDALNKQ------KLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLA------- 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  594 qiettaldlrsNSEQQLSETQRQLADARQQLQAESERRAQAesalgQSKSETERQLAEATAALADTRKQLEEATTKAAEL 673
Cdd:PRK11281    91 -----------QAPAKLRQAQAELEALKDDNDEETRETLST-----LSLRQLESRLAQTLDQLQNAQNDLAEYNSQLVSL 154

                          170       180
                   ....*....|....*....|..
gi 1949443035  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 1949443035 1197 EAAARRQAEESAKQGSASADQRLAerlseVQTLQERLRSeAAQRETTEVELrdtrAALEKQLAEASAALREASARLEQER 1276
Cdd:PRK11281    38 EADVQAQLDALNKQKLLEAEDKLV-----QQDLEQTLAL-LDKIDRQKEET----EQLKQQLAQAPAKLRQAQAELEALK 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1277 DERRRVV-ESLTQTS-TTLEARATESGSALEVTRRLLNEeraarasalaelaarraevdrltteqphaieeatarLKAQL 1354
Cdd:PRK11281   108 DDNDEETrETLSTLSlRQLESRLAQTLDQLQNAQNDLAE------------------------------------YNSQL 151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1355 AEQER--EREQLRLAAMSAE-QRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALrtaeakagSD 1431
Cdd:PRK11281   152 VSLQTqpERAQAALYANSQRlQQIRNLLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKSLEGNTQL--------QD 223

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1432 SAELRHAHETLQQAHAEltrrlterdselasvrEQAAALDAAG-----TRAQQTTAELQTNLNAARAELDML-------N 1499
Cdd:PRK11281   224 LLQKQRDYLTARIQRLE----------------HQLQLLQEAInskrlTLSEKTVQEAQSQDEAARIQANPLvaqeleiN 287

                          330
                   ....*....|....
gi 1949443035 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 1949443035  296 AVKTLQAEKAELEKRTASSPAELEALRKRLsDEATRRQLAEDDLRSLREDFDKLQSSATQPDtALETVHHRLHAETERVK 375
Cdd:COG4913    611 KLAALEAELAELEEELAEAEERLEALEAEL-DALQERREALQRLAEYSWDEIDVASAEREIA-ELEAELERLDASSDDLA 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  376 RLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAE-SARRTQAEAGQGGGEVN 454
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALlEERFAAALGDAVERELR 768

                          170       180
                   ....*....|....*....|....*.
gi 1949443035  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 1949443035  790 RAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLERQLAE----TKAELD 865
Cdd:COG4913    265 AAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLE 344

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  866 QQLAalaearsQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEA 945
Cdd:COG4913    345 REIE-------RLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  946 AAEAAGLRARMDFEAAER----ERVEAAWKLANSATEQHAAELK--------------------TLLATAR------EEL 995
Cdd:COG4913    418 RRELRELEAEIASLERRKsnipARLLALRDALAEALGLDEAELPfvgelievrpeeerwrgaieRVLGGFAltllvpPEH 497

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  996 HAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELAR-----ESAERETTEAEFQRSKSALAQQLAEAAAAQAEL- 1069
Cdd:COG4913    498 YAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGkldfkPHPFRAWLEAELGRRFDYVCVDSPEELRRHPRAi 577

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1070 -RSRLEKETAARHE--TERELRESL---TDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHtefthrltaetgA 1143
Cdd:COG4913    578 tRAGQVKGNGTRHEkdDRRRIRSRYvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQ------------E 645

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1144 REQLEKNLRQAAEEAtRKAQALQAELQRAKKELEkELADANLELLDIRSRLDhEAAARRQAEESAKQGSASADQRLAERL 1223
Cdd:COG4913    646 RREALQRLAEYSWDE-IDVASAEREIAELEAELE-RLDASSDDLAALEEQLE-ELEAELEELEEELDELKGEIGRLEKEL 722

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1224 SEVQTLQERLRSEAAQRETTEVElrDTRAALEKQLAEASAALREasarleqerderRRVVESLTQTSTTLEARATESGSA 1303
Cdd:COG4913    723 EQAEEELDELQDRLEAAEDLARL--ELRALLEERFAAALGDAVE------------RELRENLEERIDALRARLNRAEEE 788

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1304 LEVTRRLLNEE-RAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQE-REREQLRLAAMSAEQRLRDRatd 1381
Cdd:COG4913    789 LERAMRAFNREwPAETADLDADLESLPEYLALLDRLEEDGLPEYEERFKELLNENSiEFVADLLSKLRRAIREIKER--- 865

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1382 FEAANAALRG---EMEKRLRLELTWQMqredfDRRLGELTTALRTAEAKAGSDSAELRHAHEtlqQAHAELTRRLTERDs 1458
Cdd:COG4913    866 IDPLNDSLKRipfGPGRYLRLEARPRP-----DPEVREFRQELRAVTSGASLFDEELSEARF---AALKRLIERLRSEE- 936

                          730
                   ....*....|...
gi 1949443035 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 1949443035  380 ELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGGGEVNPELAA 459
Cdd:COG4995      3 ALALLALLAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALAL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  460 RIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAARAQVEADLRAAH 539
Cdd:COG4995     83 AALALALLAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  540 QRFEQRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQIETTALDLRSNSEQQLSETQRQLAD 619
Cdd:COG4995    163 AALLALALALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLA 242

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  620 ARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRS 699
Cdd:COG4995    243 LAAAAAALAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAA 322

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  700 ELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQL 779
Cdd:COG4995    323 LLLLLAALALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLA 402

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949443035  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 1949443035 1217 QRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAAL---REASARLEQERDERRRVVESLTQTSTTL 1293
Cdd:pfam07888   41 QERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELrqsREKHEELEEKYKELSASSEELSEEKDAL 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1294 EARATESgsalevtRRLLNEERAARASALAELAARRAEVDRLTTEQphaieeatARLKAQLAEQEREREQLRLAAMSAEQ 1373
Cdd:pfam07888  121 LAQRAAH-------EARIRELEEDIKTLTQRVLERETELERMKERA--------KKAGAQRKEEEAERKQLQAKLQQTEE 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1374 RLRDRATDFEAANaalrgemekrlrlelTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRHAHEtlqqahaeltrrl 1453
Cdd:pfam07888  186 ELRSLSKEFQELR---------------NSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLE------------- 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1454 terdsELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARLREECAHRERAEAELdrm 1533
Cdd:pfam07888  238 -----ELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETL--- 309

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1534 rdaqdgfQQSTAELNERLTRLTTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLnahvQQLEAELAEAQR 1613
Cdd:pfam07888  310 -------QQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRREL----QELKASLRVAQK 378

                          410
                   ....*....|.
gi 1949443035 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 1949443035 1151 LRQAAEEATRKAQALQAELQRAKKELEK---ELADANLELLDIRSrlDHEAAARRQAEESAKQGSASADQRLAERLSEVQ 1227
Cdd:COG1579     22 LEHRLKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLEL--EIEEVEARIKKYEEQLGNVRNNKEYEALQKEIE 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035  522 EADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREqASRDTQAATTQRGEQETALAELRAQLERTEAARQ---QIETT 598
Cdd:COG4942     44 AALKKEEKALLKQLAALERRIAALARRIRALEQELAA-LEAELAELEKEIAELRAELEAQKEELAELLRALYrlgRQPPL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  599 ALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVRE 678
Cdd:COG4942    123 ALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLA 202

                          170       180
                   ....*....|....*....|....*.
gi 1949443035  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 1949443035 1404 QMQREDFDRRLGELTTALRTAEAKAGSDSAELrhahETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAE 1483
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQL----AALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1484 LQTNLNAARAELDMLNRQ-------FAQRVAELDSTEARLREECAHRERAEAELDRMRDAQDGFQQSTAELNERLTRLTT 1556
Cdd:COG4942    102 QKEELAELLRALYRLGRQpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGY-KVLTARDGQQALSlyDQHAGDIKAVITDILMPFMDGVELCRELRKRD--ATLPIIV 1951
Cdd:PRK10610     8 FLVVDDFSTMRRIVRNLLKELGFnNVEEAEDGVDALN--KLQAGGFGFVISDWNMPNMDGLELLKTIRADGamSALPVLM 85

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1949443035 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 1949443035  300 LQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAE------DDLRSLREDFDKLQSSATQPDTALETVHHRLHAETER 373
Cdd:COG3096    311 MARELEELSARESDLEQDYQAASDHLNLVQTALRQQEkieryqEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEE 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  374 VKRLETELESLRVALQTEH-------------EKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEEL-VAESA 439
Cdd:COG3096    391 VDSLKSQLADYQQALDVQQtraiqyqqavqalEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLsVADAA 470

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  440 RRTQAEAGQGGGEVNPELAaRIAALTEAKAQVEkELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAG 519
Cdd:COG3096    471 RRQFEKAYELVCKIAGEVE-RSQAWQTARELLR-RYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQ 548

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  520 RSEADEAARAQVEA-----DLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRGEQEtALAELRAQLERTEAARQQ 594
Cdd:COG3096    549 LDAAEELEELLAELeaqleELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQD-ALERLREQSGEALADSQE 627

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1949443035  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 1949443035 1896 GYKVLTARDGQQALSLYDQHagDIKAVITDILMPFMDGVELCRELRKRdATLPIIVASG------------MGHEKFVT- 1962
Cdd:PRK10766    26 GYTVSEAASGAGMREIMQNQ--HVDLILLDINLPGEDGLMLTRELRSR-STVGIILVTGrtdsidrivgleMGADDYVTk 102


                   ....*....
gi 1949443035 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 1949443035 1452 RLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDSTEARLreecahrERAEAELD 1531
Cdd:COG1579     11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-------KKYEEQLG 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1532 RMRDAQDgFQQSTAELnerltrltTDVEAARQQAEQETTQRRSLEDALQQSHGEVELRVSERTAGLNAHVQQLEAELAEA 1611
Cdd:COG1579     84 NVRNNKE-YEALQKEI--------ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154

                          170
                   ....*....|....*...
gi 1949443035 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 1949443035 1124 ETARQSHTEFTHRLTAETGAREQLEKNLRQAA-EEATRKAQALQAELQRAKKE---LEKELADANLELLDIRSRLDHEAA 1199
Cdd:pfam09787    3 ESAKQELADYKQKAARILQSKEKLIASLKEGSgVEGLDSSTALTLELEELRQErdlLREEIQKLRGQIQQLRTELQELEA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1200 ARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARL------- 1272
Cdd:pfam09787   83 QQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLtsksqss 162

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1949443035 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 1949443035 1172 AKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTR 1251
Cdd:pfam15921   72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTV 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1252 AALEKQLAEASAALREASARLEQER----------DERRRVVESLTQTS----------TTLEARATesGSALEVTRRLL 1311
Cdd:pfam15921  152 HELEAAKCLKEDMLEDSNTQIEQLRkmmlshegvlQEIRSILVDFEEASgkkiyehdsmSTMHFRSL--GSAISKILREL 229

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1312 NEEraaRASALAELAARRAEVDRLTTEQPHAIE----EATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANA 1387
Cdd:pfam15921  230 DTE---ISYLKGRIFPVEDQLEALKSESQNKIElllqQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1388 ALRGEMEKRLRleltwqmQREDFDRRLGELTTALRTAEAKAGSDSAELrhaHETLQQAHAELTRRLTERD---SELASVR 1464
Cdd:pfam15921  307 QARNQNSMYMR-------QLSDLESTVSQLRSELREAKRMYEDKIEEL---EKQLVLANSELTEARTERDqfsQESGNLD 376

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1465 EQAAALDA-AGTRAQQTTAELQTNLN------AARAELDMLNRQFAQRVAELDSTEARLReecAHRERAEAELDRMRDAQ 1537
Cdd:pfam15921  377 DQLQKLLAdLHKREKELSLEKEQNKRlwdrdtGNSITIDHLRRELDDRNMEVQRLEALLK---AMKSECQGQMERQMAAI 453

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035  211 RVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAE---LSGREQVEAELAKARGELDKQVAERTATFTDIISGLE 287
Cdd:pfam01576    2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEknaLQEQLQAETELCAEAEEMRARLAARKQELEEILHELE 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  288 KAVAEHELAVKTLQAEKAELEKRTASSPAEL---EALRKRLSDEA----TRRQLAEDDLRSLREDFDKLQSSATQPDTAL 360
Cdd:pfam01576   82 SRLEEEEERSQQLQNEKKKMQQHIQDLEEQLdeeEAARQKLQLEKvtteAKIKKLEEDILLLEDQNSKLSKERKLLEERI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  361 ETVHHRLHAETERVK---RLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELErtkeelvae 437
Cdd:pfam01576  162 SEFTSNLAEEEEKAKslsKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIA--------- 232

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  438 sarrtqaeagqgggEVNPELAARIAALTEAKAQVEKELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAG 517
Cdd:pfam01576  233 --------------ELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG 298

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  518 agrsEADEAARAQVE--ADLRAAHQRFE-QRVAELETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEAARQQ 594
Cdd:pfam01576  299 ----EELEALKTELEdtLDTTAAQQELRsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKAN 374

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  595 IETTALDLRSNseqqlsetqrqladaRQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQ 674
Cdd:pfam01576  375 LEKAKQALESE---------------NAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439

                          490       500       510
                   ....*....|....*....|....*....|
gi 1949443035  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 1949443035  311 TASSPAELEALRKRLS-DEATRRQL-----AEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAETERVKR--LETELE 382
Cdd:NF012221  1537 TSESSQQADAVSKHAKqDDAAQNALadkerAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRdaILEESR 1616

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  383 SLRVALQTeheKAERADAereLSEEAMVQTNTGIQQRLMELNAELERTKEELvaESARRTQAEAgqgggevnpelaaria 462
Cdd:NF012221  1617 AVTKELTT---LAQGLDA---LDSQATYAGESGDQWRNPFAGGLLDRVQEQL--DDAKKISGKQ---------------- 1672

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  463 aLTEAKAQVEKELVE-QQAVAKalgdernrlaqelaeaaaaraaleqqlaaaSQAGAGRSEADeaaRAQVEADLRAAHQR 541
Cdd:NF012221  1673 -LADAKQRHVDNQQKvKDAVAK------------------------------SEAGVAQGEQN---QANAEQDIDDAKAD 1718

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1949443035  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 1949443035 1152 RQA-AEEATRKAQALQAELQRAKKELEKEladanlelldirsRLDHEAAARrqaEESAKQgsaSADQRLAERLSEVQTLQ 1230
Cdd:PRK05035   432 RQAkAEIRAIEQEKKKAEEAKARFEARQA-------------RLEREKAAR---EARHKK---AAEARAAKDKDAVAAAL 492

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1231 ERLRSEAAQRETTEVElrdtrAALEKQLAEASAALREASARLEQERDERRRVVESLTQTSTTLEA---RAtesgsalevt 1307
Cdd:PRK05035   493 ARVKAKKAAATQPIVI-----KAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiaRA---------- 557

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1308 rrllneeRAARASALAELAARRAEVDrlttEQPHAIEEATARLKAQLAEQerereqlrlAAMSAEQRLRDRATDFEAANA 1387
Cdd:PRK05035   558 -------KAKKAAQQAANAEAEEEVD----PKKAAVAAAIARAKAKKAAQ---------QAASAEPEEQVAEVDPKKAAV 617

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1388 ALRGEMEKRLRLELTWQMQREDF-DRRLGELTTALRTAEAKAgsdsaelrhahetLQQAHAEltrrlterDSELASVREQ 1466
Cdd:PRK05035   618 AAAIARAKAKKAEQQANAEPEEPvDPRKAAVAAAIARAKARK-------------AAQQQAN--------AEPEEAEDPK 676

                          330
                   ....*....|....*....
gi 1949443035 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 1949443035  540 QRFEQRVAELETDNQQLREQ-----ASRDTQAATTQRGEQETALAELRAQLERTEAARQQIET-------TALDLRSNSE 607
Cdd:COG3206    185 PELRKELEEAEAALEEFRQKnglvdLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAqlgsgpdALPELLQSPV 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  608 -----QQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERqlaEATAALADTRKQLEEATTKAAELQPVREQLAG 682
Cdd:COG3206    265 iqqlrAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEA 341

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1949443035  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 1949443035 1070 RSRLEKETAARHETERELRESLTDAERTTEALQADLDAAlkacEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEK 1149
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1150 NLRQAAEEATRKAQALQAELQRAKKELekELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTL 1229
Cdd:COG4942     98 ELEAQKEELAELLRALYRLGRQPPLAL--LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYdqHAGDIKAVITDILMPFMDGVELCRELRKRDATLPIIVASG 1954
Cdd:PRK15479     3 LLLAEDNRELAHWLEKALVQNGFAVDCVFDGLAADHLL--QSEMYALAVLDINMPGMDGLEVLQRLRKRGQTLPVLLLTA 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035  520 RSEADEAARAQVEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATtqrgEQETALAELRAQLERTEAARQQIETTA 599
Cdd:COG4717    101 EEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLE----ELEERLEELRELEEELEELEAELAELQ 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  600 LDLRSNSEQQLSETQRQLADARQQLQAESERRAQAesalgqsksetERQLAEATAALADTRKQLEEATTKAAELQPVREQ 679
Cdd:COG4717    177 EELEELLEQLSLATEEELQDLAEELEELQQRLAEL-----------EEELEEAQEELEELEEELEQLENELEAAALEERL 245

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  680 LAGEVQrgeraeAELFRSRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQQLQAETE 759
Cdd:COG4717    246 KEARLL------LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEE 319

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  760 RREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTASSQReaEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDR 839
Cdd:COG4717    320 ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL--QLEELEQEIAALLAEAGVEDEEELRAALEQAEEY 397

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  840 EALEKQLAAARGDLERQLAETKAELDQ-QLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLAS--ELEAAREA 916
Cdd:COG4717    398 QELKEELEELEEQLEELLGELEELLEAlDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEdgELAELLQE 477

                          410
                   ....*....|..
gi 1949443035  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 1949443035  249 AELSGREQVE--AELAKARGELDKQVAERTAT----FTDIISGLEKAVAEHEL-AVKTLQAEKAELEKRTASSPAELEAL 321
Cdd:NF041483   111 AEHQARLQAElhTEAVQRRQQLDQELAERRQTveshVNENVAWAEQLRARTESqARRLLDESRAEAEQALAAARAEAERL 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  322 ----RKRLSDEA-TRRQLAEDDLRSLREDFDKL----QSSATQPDTALETVHHRLHAETERVKRLETELEslRVALQTEH 392
Cdd:NF041483   191 aeeaRQRLGSEAeSARAEAEAILRRARKDAERLlnaaSTQAQEATDHAEQLRSSTAAESDQARRQAAELS--RAAEQRMQ 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  393 EKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTqaeaGQGGGEVNPELAARIAALTEAKAQVE 472
Cdd:NF041483   269 EAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLV----GEATKEAEALKAEAEQALADARAEAE 344

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  473 KELVEQQAVAKALGDERNRLAQELAEAAAARAALEQQLAAASQAGAGRSEADEAAR-AQVEAD-LRA-AHQRFEQRVAEL 549
Cdd:NF041483   345 KLVAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRReAEAEADrLRGeAADQAEQLKGAA 424

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  550 ETDNQQLREQASRDTQAATTQRGEQETALAELRAQLERTEA-----ARQQIETTAldlrSNSEQQLSETQRQLADARQQL 624
Cdd:NF041483   425 KDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGearreAVQQIEEAA----RTAEELLTKAKADADELRSTA 500

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  625 QAESER------------RAQAESALGQSKSETERQLAEATAALADTRKQLEEAttkAAELQPVREQlaGEVQRGERAEA 692
Cdd:NF041483   501 TAESERvrteaierattlRRQAEETLERTRAEAERLRAEAEEQAEEVRAAAERA---ARELREETER--AIAARQAEAAE 575

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  693 ELFRSRSELEtqqaalaelraraeaaeaarlqvettaqqsrtvaeqaaaeaqqqlaalrqqlqaetERREQAESALGQSK 772
Cdd:NF041483   576 ELTRLHTEAE--------------------------------------------------------ERLTAAEEALADAR 599

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  773 SETERQLAEATAALAEVRAQL-EQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLikETEDREALEKQLAAARG 851
Cdd:NF041483   600 AEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRL--RSEAAAEAERLKSEAQE 677

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  852 DLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASelEAAREALRSESARREELETAL 931
Cdd:NF041483   678 SADRVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAR--EQSEELLASARKRVEEAQAEA 755

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  932 PKTKTELGQRLAEAAAEAAGLRARM-DFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAET-AKRDAAEAAA 1009
Cdd:NF041483   756 QRLVEEADRRATELVSAAEQTAQQVrDSVAGLQEQAEEEIAGLRSAAEHAAERTRTEAQEEADRVRSDAyAERERASEDA 835

                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1010 SQVRAELEAtNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLE-KETAARHETERELR 1088
Cdd:NF041483   836 NRLRREAQE-ETEAAKALAERTVSEAIAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADaREDANRIRSDAAAQ 914

                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1089 ESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAE 1168
Cdd:NF041483   915 ADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTE 994

                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1169 LQRAKKELEKELADANLELLDIRSRLDHEaaARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELR 1248
Cdd:NF041483   995 AERVKAEAAAEAERLRTEAREEADRTLDE--ARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQA 1072

                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1249 DTRAALEKQLAE--ASAALREASARLEQERDERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEEraARASALAELA 1326
Cdd:NF041483  1073 DTMVGAARKEAEriVAEATVEGNSLVEKARTDADELLVGARRDATAIRERAEELRDRITGEIEELHER--ARRESAEQMK 1150

                         1130      1140      1150      1160
                   ....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035  599 ALDLRSNSEQQLSETQRQLADARQQLQAESERRAQAESALGQSKSETERQ---LAEATAALADTRKQLE--EATTKAAEL 673
Cdd:pfam17380  283 AVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQaaiYAEQERMAMERERELEriRQEERKREL 362

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  674 QPVR-EQLAGEVQRGERAEaelfrsRSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAEQAAAEAQQQLAALRQ 752
Cdd:pfam17380  363 ERIRqEEIAMEISRMRELE------RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE 436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  753 QLQAETERREQAESAlgqSKSETERQlaeatAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNL 832
Cdd:pfam17380  437 VRRLEEERAREMERV---RLEEQERQ-----QQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM 508

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  833 IKETEDREALEKQLAaargdlERQlaetKAELDQQLAALAEARSQAEREAAERRQTEESLLQASrSSEERVALLASELEA 912
Cdd:pfam17380  509 IEEERKRKLLEKEME------ERQ----KAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAT-EERSRLEAMEREREM 577

                          330       340
                   ....*....|....*....|..
gi 1949443035  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 1949443035 1130 HTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAeLQRAKKELEKELA-DANLELLDIRSRLDHEAaarrQAEESA 1208
Cdd:PRK04863   444 LEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQL-VRKIAGEVSRSEAwDVARELLRRLREQRHLA----EQLQQL 518

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1209 KQGSASADQRLAErlsevQTLQERLRSEAAQR----ETTEVELRDTRAALEKQLAEASAALREASARLEQERDERrrvvE 1284
Cdd:PRK04863   519 RMRLSELEQRLRQ-----QQRAERLLAEFCKRlgknLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQL----E 589

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1285 SLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLtteqpHAIEEATARLKAQLAEQEREREQL 1364
Cdd:PRK04863   590 QLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERE-----RELTVERDELAARKQALDEEIERL 664

                          250
                   ....*....|....*...
gi 1949443035 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 1949443035  818 LADQDAELKKTWDNLIKETEDREALEKQLAAARGDLER-----QLAETKAELDQQLAALAEARSQAEREAAERRQTEESL 892
Cdd:COG3096    301 LAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvqtalRQQEKIERYQEDLEELTERLEEQEEVVEEAAEQLAEA 380

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  893 LQASRSSEERVALLASELEAAREALRSESAR----REELEtALPKTKTELGQRLAEAAAEAAGLRARMDFE-AAERERVE 967
Cdd:COG3096    381 EARLEAAEEEVDSLKSQLADYQQALDVQQTRaiqyQQAVQ-ALEKARALCGLPDLTPENAEDYLAAFRAKEqQATEEVLE 459

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  968 AAWKL--ANSATEQHAAELKTLLATAreelhAETAKRDAAEAAASQVRAeleatnAESSRALAAAQNELARESAERETTE 1045
Cdd:COG3096    460 LEQKLsvADAARRQFEKAYELVCKIA-----GEVERSQAWQTARELLRR------YRSQQALAQRLQQLRAQLAELEQRL 528

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1046 AEFQRSKsalaqqlaeaaaaqaelrsRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEET 1125
Cdd:COG3096    529 RQQQNAE-------------------RLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1126 ARQSHTEFTHRLTAETGAREQLEKnLRQAAEEATRKAQALQAELQRAkkeLEKELAdanlelldiRSRLDHEAAARRQAE 1205
Cdd:COG3096    590 LRARIKELAARAPAWLAAQDALER-LREQSGEALADSQEVTAAMQQL---LERERE---------ATVERDELAARKQAL 656

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1206 ESA----KQGSASADQRL---AER-----LSEV----------------------------QTLQERLRS---------- 1235
Cdd:COG3096    657 ESQierlSQPGGAEDPRLlalAERlggvlLSEIyddvtledapyfsalygparhaivvpdlSAVKEQLAGledcpedlyl 736

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1236 --------EAAQRETTEVELRDT--------------------RAALEKQLAEASAALREASARLEQERDERR---RVVE 1284
Cdd:COG3096    737 iegdpdsfDDSVFDAEELEDAVVvklsdrqwrysrfpevplfgRAAREKRLEELRAERDELAEQYAKASFDVQklqRLHQ 816

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1285 SLTQTSTTLEARATESGSALEVT---------RRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLA 1355
Cdd:COG3096    817 AFSQFVGGHLAVAFAPDPEAELAalrqrrselERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLE 896

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1356 EQEREREQLrLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQM---QREDFDRRLGELTTALRTAEAKAGSDS 1432
Cdd:COG3096    897 ELREELDAA-QEAQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQakeQQRRLKQQIFALSEVVQRRPHFSYEDA 975

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1433 AELRHAHETLQQAhaeLTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQ-RVAELDS 1511
Cdd:COG3096    976 VGLLGENSDLNEK---LRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEElGVQADAE 1052

                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949443035 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 1949443035 1763 VVVDESFIH---HRRATG------AKPGNYVLFRVTDSGVGIPRDILPRIfepfftTKEPGQSVGLGLatalgvVQSHGG 1833
Cdd:cd16924      8 PLVENAIQHglsPLTDKGvvtisaLKEDNHVMIEVEDNGRGIDPKVLNIL------GKKPKEGNGIGL------YNVHQR 75

                           90       100
                   ....*....|....*....|....*...
gi 1949443035 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 1949443035  225 ELERRADELKKRDSELESANRQLwaeLSGREQVEA---------ELAKARGELDKQVAERTATFTDI----ISGLEKAVA 291
Cdd:COG4913    222 DTFEAADALVEHFDDLERAHEAL---EDAREQIELlepirelaeRYAAARERLAELEYLRAALRLWFaqrrLELLEAELE 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  292 EHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRR-QLAEDDLRSLREDFDKLQSSATQPDTALETVHHRLHAE 370
Cdd:COG4913    299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRlEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  371 TERVKRLETELESLRVALQTEHEKAERADAERElseeamvqtntgiqQRLMELNAELERTKEELvaesarrtqAEAGQGG 450
Cdd:COG4913    379 AEEFAALRAEAAALLEALEEELEALEEALAEAE--------------AALRDLRRELRELEAEI---------ASLERRK 435

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  451 GEVNPELAARIAALTEAKAQVEK------ELVE--------QQAVAKALG---------DERNRLAQELAEAAAARAALE 507
Cdd:COG4913    436 SNIPARLLALRDALAEALGLDEAelpfvgELIEvrpeeerwRGAIERVLGgfaltllvpPEHYAAALRWVNRLHLRGRLV 515

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  508 QQLAAASQAGAGRSEADEAARA-QVEADLRAAHQRFEQRVAELE-----TDNQQLREQASRDTQAATT-------QRGEQ 574
Cdd:COG4913    516 YERVRTGLPDPERPRLDPDSLAgKLDFKPHPFRAWLEAELGRRFdyvcvDSPEELRRHPRAITRAGQVkgngtrhEKDDR 595

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  575 ETALAEL------RAQLERTEAARQQIEttaldlrsnseQQLSETQRQLADARQQLQAESERRAQAESALGQSksETERQ 648
Cdd:COG4913    596 RRIRSRYvlgfdnRAKLAALEAELAELE-----------EELAEAEERLEALEAELDALQERREALQRLAEYS--WDEID 662

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  649 LAEATAALADTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELFRSRSELETQQAALAELRARAEAAEAARLQVETT 728
Cdd:COG4913    663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDL 742

                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|
gi 1949443035  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 1949443035  824 ELKKTWDNLIKETEDREALEKQLAAARGDLERQLA-------ETKAELDQQLAALAEARSQAEREAAERRQTEESLLQAS 896
Cdd:pfam05483  286 ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQiatkticQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELL 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  897 RSSEERVALLASELEAAREALRSESARREEL-------ETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVeaa 969
Cdd:pfam05483  366 RTEQQRLEKNEDQLKIITMELQKKSSELEEMtkfknnkEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELI--- 442

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  970 WKLANSATEQHAAELKTLLATAREELHAETAKrdaaeaaasQVRAELEATNAESSRaLAAAQNELARESAE--RETTEAE 1047
Cdd:pfam05483  443 FLLQAREKEIHDLEIQLTAIKTSEEHYLKEVE---------DLKTELEKEKLKNIE-LTAHCDKLLLENKEltQEASDMT 512

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1048 FQRSKSALAQQLAEAAAAqaelrsRLEKETAARHETERELRESLtdaERTTEALQADLDaalkaceEEAARRSQAEETAR 1127
Cdd:pfam05483  513 LELKKHQEDIINCKKQEE------RMLKQIENLEEKEMNLRDEL---ESVREEFIQKGD-------EVKCKLDKSEENAR 576

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1128 QSHTEFTHRlTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKE-----------------LEKELADANLELLDI 1190
Cdd:pfam05483  577 SIEYEVLKK-EKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKgsaenkqlnayeikvnkLELELASAKQKFEEI 655

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1191 RSRLDHEAAARRQAEES----AKQGSASADQ----------RLAERLSEVQTLQERLR-----------SEAAQRETTEV 1245
Cdd:pfam05483  656 IDNYQKEIEDKKISEEKlleeVEKAKAIADEavklqkeidkRCQHKIAEMVALMEKHKhqydkiieerdSELGLYKNKEQ 735

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035  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 1949443035 1150 NLRQAAEEATRKAQALQAELQRAKKELEKELADANlelldirsrlDHEAAARRQAEESAKQGSASADQRLAERLSEVQTL 1229
Cdd:PRK00409   527 ELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQ----------EEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQL 596

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035  525 EAARAQVEADlraaHQRFEQRVAELETdnqqlreqasrdtqaattQRGEQETALAELRAQLERTEAARQQIETTALDLRS 604
Cdd:PRK00409   505 EEAKKLIGED----KEKLNELIASLEE------------------LERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE 562

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  605 NSEQQLSETQRQLADARQQLQAESER--RAQAESALGQSKSETERQLAEAtaaladtRKQLEEATTKAAELQPVREQLAG 682
Cdd:PRK00409   563 EEDKLLEEAEKEAQQAIKEAKKEADEiiKELRQLQKGGYASVKAHELIEA-------RKRLNKANEKKEKKKKKQKEKQE 635


                   ....*...
gi 1949443035  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 1949443035  227 ERRADELKKRDSELESAnRQLWAELsgrEQVEAELAkargELDKQVAERTATFTDIISGLEKAVAEHElavkTLQAEKAE 306
Cdd:PHA02562   213 ENIARKQNKYDELVEEA-KTIKAEI---EELTDELL----NLVMDIEDPSAALNKLNTAAAKIKSKIE----QFQKVIKM 280

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  307 LEKRT---------ASSPAELEALRKRLSDEATRRQLAEDDLRSLRE---DFDKLQSSATQPDTALETVHHRLHAETERV 374
Cdd:PHA02562   281 YEKGGvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKA 360

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1949443035  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 1949443035  579 AELRAQLERTEAARQqiettaLDLRSNSEQQLSETQRQLADARQQLQAE-SERRAQAESALGQSKSETERQLAEATAALA 657
Cdd:TIGR00618  166 KELLMNLFPLDQYTQ------LALMEFAKKKSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQ 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  658 DTRKQLEEATTKAAELQPVREQLAGEVQRGERAEAELfrsrSELETQQAALAELRARAEAAEAARLQVETTAQQSRTVAE 737
Cdd:TIGR00618  240 QSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQE----AVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  738 QAAAEAQQQLAALRQQLQAETERREQAESALGQSKSETERQLAEATAALAEVRAQLEQATTassqrEAEAKQAAAAQQQK 817
Cdd:TIGR00618  316 LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT-----LTQHIHTLQQQKTT 390

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  818 LADQDAELKKtwdnlIKETEDREALEKQ-LAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQAS 896
Cdd:TIGR00618  391 LTQKLQSLCK-----ELDILQREQATIDtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESA 465

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  897 RSSEERVallasELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAwklansa 976
Cdd:TIGR00618  466 QSLKERE-----QQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG------- 533

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  977 tEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALA 1056
Cdd:TIGR00618  534 -EQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC 612

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1057 QQLAEAAAAQAELrSRLEKETAARHETERELRESLTDAERTTEALQADLD---AALKACEEEAARRSQAEETARQSHTEF 1133
Cdd:TIGR00618  613 EQHALLRKLQPEQ-DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVRehaLSIRVLPKELLASRQLALQKMQSEKEQ 691

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1134 THRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSA 1213
Cdd:TIGR00618  692 LTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVT 771

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 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 1949443035  796 ATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDLeRQLAETKAELDQQLAALAEAR 875
Cdd:COG4942     14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAELAELEKEI 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  876 SQAEREAAERRQTEESLLQAS--RSSEERVALLAS-----ELEAAREALRSESARREELETALPKTKTELGQRLAEAAAE 948
Cdd:COG4942     93 AELRAELEAQKEELAELLRALyrLGRQPPLALLLSpedflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1949443035  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 1949443035 1094 AERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAK 1173
Cdd:TIGR00618  194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELR 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1174 KEL-EKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRA 1252
Cdd:TIGR00618  274 AQEaVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQ 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1253 ALEKQLAEASAALREAsaRLEQERDERRRVvESLTQTSTTLEARATESGSALEVtrrlLNEERAARASALAELAARRAEV 1332
Cdd:TIGR00618  354 EIHIRDAHEVATSIRE--ISCQQHTLTQHI-HTLQQQKTTLTQKLQSLCKELDI----LQREQATIDTRTSAFRDLQGQL 426

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1333 DRLTTEQphAIEEATARLKAQLAEQEREREQLRLAAMSaEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDR 1412
Cdd:TIGR00618  427 AHAKKQQ--ELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEP 503

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1413 RLGELTTALRTAEAKAGSDSAELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAAR 1492
Cdd:TIGR00618  504 CPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSK 583

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1493 AELDMLnRQFAQRVaeLDSTEARLREECAHRERAEAELDRMRDAQDGFQQStaelnerltrlTTDVEAARQQAEQETTQR 1572
Cdd:TIGR00618  584 EDIPNL-QNITVRL--QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR-----------LHLQQCSQELALKLTALH 649

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*.
gi 1949443035 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 1949443035 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 1949443035 1875 LMLADDEQGVLDVTAEILEWHGYKVLTARDGQQALSLYDQHAGDIKAVITDILMPFMDGVELCRELRKRDA--TLPIIVA 1952
Cdd:cd17582      1 VLLVENDDSTRQIVTALLRKCSYEVTAASDGLQAWDVLEDEQNEIDLILTEVDLPVSSGFKLLSYIMRHKIckNIPVIMM 80

                           90       100
                   ....*....|....*....|....
gi 1949443035 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 1949443035  909 ELEAAREALRSESARREELEtALPKTKTELgQRLAEAAAEAAGLRARMDFEAAERERVEAawklansatEQHAAELKTLL 988
Cdd:COG4913    236 DLERAHEALEDAREQIELLE-PIRELAERY-AAARERLAELEYLRAALRLWFAQRRLELL---------EAELEELRAEL 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  989 ATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAE 1068
Cdd:COG4913    305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAA 384

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1069 LRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQshtefthrltaetgAREQLE 1148
Cdd:COG4913    385 LRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLA--------------LRDALA 450

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1149 KNLRQAAEEATRKAQALQ--AELQRAKKELEKELADANLELL----------------DIRSRLDHEAAARRQAEEsakQ 1210
Cdd:COG4913    451 EALGLDEAELPFVGELIEvrPEEERWRGAIERVLGGFALTLLvppehyaaalrwvnrlHLRGRLVYERVRTGLPDP---E 527

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1211 GSASADQRLAERLS-EVQTLQERLRSEAAQRE-----TTEVELRDTRAALEKQ-LAEASAALREASARLEQERD-----E 1278
Cdd:COG4913    528 RPRLDPDSLAGKLDfKPHPFRAWLEAELGRRFdyvcvDSPEELRRHPRAITRAgQVKGNGTRHEKDDRRRIRSRyvlgfD 607

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1279 RRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDrltteqphaieeaTARLKAQLAEQE 1358
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-------------VASAEREIAELE 674

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1359 REREQLRlAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSD---SAEL 1435
Cdd:COG4913    675 AELERLD-ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLElraLLEE 753

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1436 RHAHETLQQAHAELTRRLTERDSELASVREQAA-----ALDAAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELD 1510
Cdd:COG4913    754 RFAAALGDAVERELRENLEERIDALRARLNRAEeelerAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYE 833

                          650       660       670       680
                   ....*....|....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035  958 FEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARE 1037
Cdd:COG3899    749 LELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRL 828

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1038 SAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAALKACEEEAA 1117
Cdd:COG3899    829 EARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAA 908

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1118 RRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHE 1197
Cdd:COG3899    909 AAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAA 988

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1198 AAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREASARLEQERD 1277
Cdd:COG3899    989 AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAAL 1068

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1278 ERRRVVESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATARLKAQLAEQ 1357
Cdd:COG3899   1069 LAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAA 1148

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1358 EREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELRH 1437
Cdd:COG3899   1149 LLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLL 1228

                          490
                   ....*....|....*.
gi 1949443035 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 1949443035  870 ALAEARSQAEREAAERRQTEESLLQASRSSEErvaLLASELEAAREALRSESAR-REELETALPKTKTELGQRLAEAAAE 948
Cdd:COG3903    477 AAERLAEAGERAAARRRHADYYLALAERAAAE---LRGPDQLAWLARLDAEHDNlRAALRWALAHGDAELALRLAAALAP 553

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  949 AAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVRAELEATNAESSRALA 1028
Cdd:COG3903    554 FWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAA 633

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1029 AAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTDAERTTEALQADLDAA 1108
Cdd:COG3903    634 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAA 713

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1109 LKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAELQRAKKELEKELADANLELL 1188
Cdd:COG3903    714 AAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAA 793

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1189 DIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRAALEKQLAEASAALREA 1268
Cdd:COG3903    794 AAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAA 873

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035  774 ETERQLAEATAALAEVRAQLEQATTASSQREAEAKQAAAAQQQKLADQDAELKKTWDNLIKETEDREALEKQLAAARGDL 853
Cdd:COG3899    855 EALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALA 934

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  854 ERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALRSESARREELETALPK 933
Cdd:COG3899    935 AAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAA 1014

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  934 TKTELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAETAKRDAAEAAASQVR 1013
Cdd:COG3899   1015 LAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAA 1094

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1014 AELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETAARHETERELRESLTD 1093
Cdd:COG3899   1095 AALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAA 1174

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949443035 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 1949443035 1435 LRHAHETLQQAHAeltrRLTERDSELASVREQAAALD--AAGTRAQQTTAELQTNLNAARAELDMLNRQFAQRVAELDST 1512
Cdd:COG3524    179 VRFAEEEVERAEE----RLRDAREALLAFRNRNGILDpeATAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQL 254

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035  839 REALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERVALLASELEAAREALR 918
Cdd:COG3903    529 RAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAA 608

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  919 SESARREELETALpktktELGQRLAEAAAEAAGLRARMDFEAAERERVEAAWKLANSATEQHAAELKTLLATAREELHAE 998
Cdd:COG3903    609 AAAAAAAAAAAAA-----ALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAA 683

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  999 TAKRDAAEAAASQVRAELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAQQLAEAAAAQAELRSRLEKETA 1078
Cdd:COG3903    684 AAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAAL 763

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1079 ARHETERELRESLTDAERTTEALQADLDAALKACEEEAARRSQAEETARQSHTEFTHRLTAETGAREQLEKNLRQAAEEA 1158
Cdd:COG3903    764 AAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAA 843

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1159 TRKAQALQAELQRAKKELEKELADANLELLDIRSRLDHEAAARRQAEESAKQGSASADQRLAERLSEVQTLQERLRSEAA 1238
Cdd:COG3903    844 AAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAA 923

                          410
                   ....*....|
gi 1949443035 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 1949443035  229 RADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATftdiISGLEKAVAEHELAVKTLQAEKAELE 308
Cdd:COG4942     21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELAELEKEIAELR 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  309 KRTASSPAELEALRKRL------------------SDEATRRQLAEDDLRSLREDFDKLQSSATQpdtaLETVHHRLHAE 370
Cdd:COG4942     97 AELEAQKEELAELLRALyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAE----LAALRAELEAE 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  371 TERVKRLETELESLRVALQTEHEKAERADAERELSEEAMVQTNTGIQQRLMELNAELERTKEELVAESARRTQAEAGQGG 450
Cdd:COG4942    173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252


                   .
gi 1949443035  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 1949443035  825 LKKTWDNL---IKETEDREALEKQLAAARGDLERQLAETKAELDQQLAALAEARSQaEREAAERRQTEESLLQASRSSEE 901
Cdd:PRK03918   160 YENAYKNLgevIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE-LPELREELEKLEKEVKELEELKE 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  902 RVALLASELEAAREALRSESARREELETALPKTKTELGQRLAEAAAEAAGLRARMDFEAAERERVEaawklansaTEQHA 981
Cdd:PRK03918   239 EIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEE---------YLDEL 309

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  982 AELKTLLATAREELHAetakrdaaeaaasqVRAELEATNAESSRA--LAAAQNELARESAERETTEAEFQRSKSALAQQL 1059
Cdd:PRK03918   310 REIEKRLSRLEEEING--------------IEERIKELEEKEERLeeLKKKLKELEKRLEELEERHELYEEAKAKKEELE 375

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1060 AEAAAAQAELRSRLEKE----TAARHETERELREsLTDAERTTEALQADLDAALKACEEEAAR-----RSQAEETARQSH 1130
Cdd:PRK03918   376 RLKKRLTGLTPEKLEKEleelEKAKEEIEEEISK-ITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELL 454

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1131 TEFTHRLTAETGAREQLEKNLRQAAEEATR--KAQALQAELQRAK------KELEKELADANLELLDIRSRlDHEAAARR 1202
Cdd:PRK03918   455 EEYTAELKRIEKELKEIEEKERKLRKELREleKVLKKESELIKLKelaeqlKELEEKLKKYNLEELEKKAE-EYEKLKEK 533

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1203 QAEESAKQGSASAD-QRLAERLSEVQTLQERLRSEAAQRETTEVELRD----TRAALEKQLAEASAA------LREASAR 1271
Cdd:PRK03918   534 LIKLKGEIKSLKKElEKLEELKKKLAELEKKLDELEEELAELLKELEElgfeSVEELEERLKELEPFyneyleLKDAEKE 613

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1272 LEQERDERRRVVESLTQTSTTL---EARATESGSALEVTRRLLNEERAARASALAELAARRAEVDRLTTEQPHAIEEATA 1348
Cdd:PRK03918   614 LEREEKELKKLEEELDKAFEELaetEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK 693

                          570       580       590       600
                   ....*....|....*....|....*....|....*....|..
gi 1949443035 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 1949443035 1014 AELEATNAESSRALAAAQNELARESAERETTEAEFQRSKSALAqqlaeaaaaqaelrsrleketaarhETERELRESLTD 1093
Cdd:COG3096    357 EELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLA-------------------------DYQQALDVQQTR 411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1094 AERTTEALQAdLDAALKACEEEAARRSQAEETarqsHTEFTHRLTAETGAREQLEKNLRQAAEEATRKAQALQAeLQRAK 1173
Cdd:COG3096    412 AIQYQQAVQA-LEKARALCGLPDLTPENAEDY----LAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYEL-VCKIA 485

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1174 KELEKELA-DANLELLdiRSRLDHEAAARRQAEESAKQGSAsadQRLAERLSEVQTLQERLRSEAAQRETTEVELRDTRA 1252
Cdd:COG3096    486 GEVERSQAwQTARELL--RRYRSQQALAQRLQQLRAQLAEL---EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLA 560

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1253 ALEKQLAEASAALREASARLEQERDERrrvvESLTQTSTTLEARATESGSALEVTRRLLNEERAARASALAELAARRAEV 1332
Cdd:COG3096    561 ELEAQLEELEEQAAEAVEQRSELRQQL----EQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLL 636

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1333 DRLtteqpHAIEEATARLKAQLAEQEREREQLRLAAMSAEQRLR--------------------DRATDFEAANAALR-- 1390
Cdd:COG3096    637 ERE-----REATVERDELAARKQALESQIERLSQPGGAEDPRLLalaerlggvllseiyddvtlEDAPYFSALYGPARha 711

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1391 ------GEMEKRL----------------------------RLELTWQMQREDFDRRLGELTTALRTAEAKAGSDSAELR 1436
Cdd:COG3096    712 ivvpdlSAVKEQLagledcpedlyliegdpdsfddsvfdaeELEDAVVVKLSDRQWRYSRFPEVPLFGRAAREKRLEELR 791

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1437 HAHETLQQAHAEL------TRRLTERDS-----------------ELASVREQAAALDAAGTRAQQTTAELQTNLNAARA 1493
Cdd:COG3096    792 AERDELAEQYAKAsfdvqkLQRLHQAFSqfvgghlavafapdpeaELAALRQRRSELERELAQHRAQEQQLRQQLDQLKE 871

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1494 ELDMLNRQFAQRVAELDSTEARLREECahreraEAELDRMRDAQDGFQQ---STAELNERLTRLTTD------VEAARQQ 1564
Cdd:COG3096    872 QLQLLNKLLPQANLLADETLADRLEEL------REELDAAQEAQAFIQQhgkALAQLEPLVAVLQSDpeqfeqLQADYLQ 945

                          650       660       670       680       690       700
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1449 LTRRLTERDSELASVREQAAALDAAGTRAQQTTAELQTNLNAARAELDMLnRQFAQRVAELDSTEARLREECAHREraeA 1528
Cdd:PRK09039    44 LSREISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAA-EAERSRLQALLAELAGAGAAAEGRA---G 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1529 ELDRMRDAQdgfQQSTAELNERLTRLTTDVEAARQQAEqettqrrSLEDALQQShgevelrvSERTAGLNAHVQQLEAEL 1608
Cdd:PRK09039   120 ELAQELDSE---KQVSARALAQVELLNQQIAALRRQLA-------ALEAALDAS--------EKRDRESQAKIADLGRRL 181

                          170
                   ....*....|....*
gi 1949443035 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 1949443035  525 EAARAQVEADLRAAHqrfeqrvAELETDNQQLR-EQASRDTQAATTQRGEQETALAElrAQLERTEAARQQIETTAldlr 603
Cdd:PRK10476    85 ELTVAQAQADLALAD-------AQIMTTQRSVDaERSNAASANEQVERARANAKLAT--RTLERLEPLLAKGYVSA---- 151

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1949443035  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 1949443035  225 ELERRADELKKRDSELESANRQL---WAELSGREQVEAELAKARGELDKQVAERTATFTDIISGLEKAVAEHELAVKTLQ 301
Cdd:COG4913    672 ELEAELERLDASSDDLAALEEQLeelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  302 AEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRSLREDFDKLQSSATQP-DTALETVHH--RLHA--ETERVKR 376
Cdd:COG4913    752 EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADlDADLESLPEylALLDrlEEDGLPE 831

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1949443035  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 1949443035  211 RVQQEVSYRKEIGLELERRADELKKRDSELESANRQLWAELSGREQVEAELAKARGELDKQVAERTATFtDIISGLEKAV 290
Cdd:PRK03918   169 EVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK-EEIEELEKEL 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  291 AEHELAVKTLQAEKAELEKRTASSPAELEALRKRLSDEATRRQLAEDDLRsLREDFDKLQSSATQPDTALETVHHRLHAE 370
Cdd:PRK03918   248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGI 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  371 TERVKRLETELESLRvALQTEHEKAERADAERELSEEAMvqtntgiqQRLMELNAELERTKEELvaesarrtqaeagqgG 450
Cdd:PRK03918   327 EERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELY--------EEAKAKKEELERLKKRL---------------T 382

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  451 GEVNPELAARIAALTEAKAQVEKELVEqqavakaLGDERNRLAQELAEAAAARAALEQQLAAASQAGAgrsEADEAARAQ 530
Cdd:PRK03918   383 GLTPEKLEKELEELEKAKEEIEEEISK-------ITARIGELKKEIKELKKAIEELKKAKGKCPVCGR---ELTEEHRKE 452

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  531 VEADLRAAHQRFEQRVAELETDNQQLREQASRDTQAATTQRG--EQETALAELRA--------QLERTEAARQQIETTAL 600
Cdd:PRK03918   453 LLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESEliKLKELAEQLKEleeklkkyNLEELEKKAEEYEKLKE 532

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035  601 DLRSNSEQQ--LSETQRQLADARQQLQAESERRAQAESALGQSKSETERQLAEATAALADTRKQLEEATTKAAELQPVRE 678
Cdd:PRK03918   533 KLIKLKGEIksLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK 612

                          490       500       510
                   ....*....|....*....|....*....|...
gi 1949443035  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 1949443035 1784 VLFRVTDSGVGIPRDILPRIFEPFFTTKEP------------GQSV-----GLGLATALGVVQSHGGFILLETEEDKGTE 1846
Cdd:cd16929     84 LTIKISDRGGGIPREDLARLFSYMYSTAPQpslddfsdlisgTQPSplagfGYGLPMSRLYAEYFGGDLDLQSMEGYGTD 163


                   ....*.
gi 1949443035 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 1949443035 1342 AIEEATARLKAQLAEQEREREQLRLAAMSAEQRLRDRATDFEAANAALRGEMEKRLRLELTWQMQREDFDRRLGELTTAL 1421
Cdd:COG4942     38 ELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLG 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949443035 1422 RTAEAKAGSDS------------------------AELRHAHETLQQAHAELTRRLTERDSELASVREQAAALDAAGTRA 1477
Cdd:COG4942    118 RQPPLALLLSPedfldavrrlqylkylaparreqaEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAER 197

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1949443035 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 1949443035 1896 GYKVLTARDGQQALSLYDQHAGDIkaVITDILMPFMDGVELCRELRKRDATLPIIVASGM-GHEKFVTDLrELGVPLFLK 1974
Cdd:PRK10816    24 GHQVDAAEDAKEADYYLNEHLPDI--AIVDLGLPDEDGLSLIRRWRSNDVSLPILVLTAReSWQDKVEVL-SAGADDYVT 100

                           90
                   ....*....|....*...
gi 1949443035 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 1949443035 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 1949443035  826 KKTWDNLIKETEDREaLEKqLAAARGDLERQlAETKAELDQQLAALAEARSQAEREAAERRQTEESLLQASRSSEERV 903
Cdd:PLN02316   243 EHSFEDFLLEEKRRE-LEK-LAKEEAERERQ-AEEQRRREEEKAAMEADRAQAKAEVEKRREKLQNLLKKASRSADNV 317
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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