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Conserved domains on  [gi|2258821257|gb|USN49054|]
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MAG: sigma 54-interacting transcriptional regulator [Pseudobdellovibrionaceae bacterium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 78-412 1.76e-130

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


:

Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 382.97  E-value: 1.76e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  78 LHARLRHHDQVRMGQTQILFSQRLGdlelkvlnssKNAKWQAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQR 157
Cdd:COG3829   118 LERKLREEELERGLSAKYTFDDIIG----------KSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPR 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 158 SSGPLININCSALSESLVESELFGHTKGSFTGAT-DNRKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGS 236
Cdd:COG3829   188 RDGPFVAVNCAAIPENLLESELFGYEKGAFTGAKkGGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGG 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 237 DTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERMEDFEELLAFFAQKY-------RVRFDLATIK 309
Cdd:COG3829   268 TKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFnkkygknIKGISPEALE 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 310 ELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPMIVDQGLPISNmdwFPRPNGLN-MIQEMEKNLILELLEKNNGNQ 388
Cdd:COG3829   348 LLLAYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYLLEEAEAAS---AAEEGSLKeALEEVEKELIEEALEKTGGNK 424

                         330       340
                  ....*....|....*....|....
gi 2258821257 389 RKTARELGMAKSTLHDRIRSYSID 412
Cdd:COG3829   425 SKAAKALGISRSTLYRKLKKYGIK 448
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
29-97 2.17e-24

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


:

Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 96.18  E-value: 2.17e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLH-ARLRHHDQVRMGQTQILF 97
Cdd:COG1716    24 TIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQRVTEpAPLRDGDVIRLGKTELRF 93
 
Name Accession Description Interval E-value
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 78-412 1.76e-130

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 382.97  E-value: 1.76e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  78 LHARLRHHDQVRMGQTQILFSQRLGdlelkvlnssKNAKWQAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQR 157
Cdd:COG3829   118 LERKLREEELERGLSAKYTFDDIIG----------KSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPR 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 158 SSGPLININCSALSESLVESELFGHTKGSFTGAT-DNRKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGS 236
Cdd:COG3829   188 RDGPFVAVNCAAIPENLLESELFGYEKGAFTGAKkGGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGG 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 237 DTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERMEDFEELLAFFAQKY-------RVRFDLATIK 309
Cdd:COG3829   268 TKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFnkkygknIKGISPEALE 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 310 ELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPMIVDQGLPISNmdwFPRPNGLN-MIQEMEKNLILELLEKNNGNQ 388
Cdd:COG3829   348 LLLAYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYLLEEAEAAS---AAEEGSLKeALEEVEKELIEEALEKTGGNK 424

                         330       340
                  ....*....|....*....|....
gi 2258821257 389 RKTARELGMAKSTLHDRIRSYSID 412
Cdd:COG3829   425 SKAAKALGISRSTLYRKLKKYGIK 448
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
118-403 2.92e-101

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 310.18  E-value: 2.92e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 118 QAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGA 197
Cdd:PRK05022  197 QQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGK 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 198 FNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIR 277
Cdd:PRK05022  277 FELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLS 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 278 TPALSERMEDFeELLA-FFAQKYRVRFDL-------ATIKELKAYSWPGNIRELRNAVARAA--ALVNGH----AVQPNH 343
Cdd:PRK05022  357 VPPLRERGDDV-LLLAgYFLEQNRARLGLrslrlspAAQAALLAYDWPGNVRELEHVISRAAllARARGAgrivTLEAQH 435

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258821257 344 IPMIVDQGLPISNMDWFP-RPNGLNMIQEME---KNLILELLEKNNGNQRKTARELGMAKSTLH 403
Cdd:PRK05022  436 LDLPAEVALPPPEAAAAPaAVVSQNLREATEafqRQLIRQALAQHQGNWAAAARALELDRANLH 499
Sigma54_activat pfam00158
Sigma-54 interaction domain;
114-277 1.46e-87

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 263.11  E-value: 1.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 114 NAKWQAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDN 193
Cdd:pfam00158   5 SPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGADSD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 194 RKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHV 273
Cdd:pfam00158  85 RKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYYRLNV 164


                  ....
gi 2258821257 274 VEIR 277
Cdd:pfam00158 165 IPIE 168
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
 127-416 1.45e-86

Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein for nitrogen fixation. The model produces scores between the trusted and noise cutoffs for a well-described NifA homolog in Aquifex aeolicus (which lacks nitrogenase), for transcriptional activators of alternative nitrogenases (VFe or FeFe instead of MoFe), and truncated forms. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, DNA interactions]


Pssm-ID: 273817 [Multi-domain]  Cd Length: 534  Bit Score: 273.13  E-value: 1.45e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 127 IAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTL 206
Cdd:TIGR01817 215 VARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 207 FLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERME 286
Cdd:TIGR01817 295 FLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERRE 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 287 DFEELLAFFAQKYR------VRFDLATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIpmIVDQGLPISNMDWF 360
Cdd:TIGR01817 375 DIPLLAEAFLEKFNrengrpLTITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITRSDF--SCQSGQCLSPMLAK 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 361 PRPNGLNMIQEM--------------------------EKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRSYSIDVK 414
Cdd:TIGR01817 453 TCPHGHISIDPLagttpphspasaalpgepglsgptlsERERLIAALEQAGWVQAKAARLLGMTPRQVGYALRKLNIEMK 532


                  ..
gi 2258821257 415 VF 416
Cdd:TIGR01817 533 KL 534
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
29-97 2.17e-24

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 96.18  E-value: 2.17e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLH-ARLRHHDQVRMGQTQILF 97
Cdd:COG1716    24 TIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQRVTEpAPLRDGDVIRLGKTELRF 93
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 126-271 2.97e-22

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 92.21  E-value: 2.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 126 AIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTkgsftgATDNRKGAFNAARGGT 205
Cdd:cd00009    14 LELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLLFELAEKAKPGV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258821257 206 LFLDEIGDLPINLQPKMLRALENneikpVGSDTSVSTDVRIIAATHKNIrqkvkSGEFREDLFYRL 271
Cdd:cd00009    88 LFIDEIDSLSRGAQNALLRVLET-----LNDLRIDRENVRVIGATNRPL-----LGDLDRALYDRL 143
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 29-98 2.46e-21

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 87.72  E-value: 2.46e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLH-ARLRHHDQVRMGQTQILFS 98
Cdd:cd00060    22 TIGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNGKRITPpVPLQDGDVIRLGDTTFRFE 92
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 29-90 1.94e-15

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 70.30  E-value: 1.94e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEG-QFFIQDLGSRNGTYVNGAQVLH--ARLRHHDQVRM 90
Cdd:pfam00498   2 TIGRSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGSTNGTFVNGQRLGPepVRLKDGDVIRL 66
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 133-277 3.54e-11

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 60.85  E-value: 3.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  133 PVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVES---ELFGHTKGSFTGATDNRKgAFNAARG---GTL 206
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRL-ALALARKlkpDVL 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258821257  207 FLDEIGDLPINLQPKMLRALENNEikpVGSDTSVSTDVRIIAATHKniRQKVKSGEFREDLFYRLHVVEIR 277
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLLEELR---LLLLLKSEKNLTVILTTND--EKDLGPALLRRRFDRRIVLLLIL 148
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 29-77 3.08e-10

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 55.26  E-value: 3.08e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2258821257   29 SIGR-SADNTLVIQDDFASGRHARVLNKEG-QFFIQDLGSRNGTYVNGAQV 77
Cdd:smart00240   2 TIGRsSEDCDIQLDGPSISRRHAVIVYDGGgRFYLIDLGSTNGTFVNGKRI 52
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 134-176 1.25e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 39.01  E-value: 1.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2258821257 134 VLISGPSGSGKEVVaqtLHKLSQRSSGPLININcSALSESLVE 176
Cdd:NF033453   19 ILLVGPPGSGKTAL---LRELAAKRGAPVINVN-LELSRRLLE 57
PLN02927 PLN02927
antheraxanthin epoxidase/zeaxanthin epoxidase
 14-94 1.78e-03

antheraxanthin epoxidase/zeaxanthin epoxidase


Pssm-ID: 178515 [Multi-domain]  Cd Length: 668  Bit Score: 40.46  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  14 VSEKTVRTVEIGQFASIGRSADNT-----LVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQ--------VLHA 80
Cdd:PLN02927  545 VSETLCLTKDEDQPCIVGSEPDQDfpgmrIVIPSSQVSKMHARVIYKDGAFFLMDLRSEHGTYVTDNEgrryratpNFPA 624

                          90
                  ....*....|....
gi 2258821257  81 RLRHHDQVRMGQTQ 94
Cdd:PLN02927  625 RFRSSDIIEFGSDK 638
 
Name Accession Description Interval E-value
RocR COG3829
RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis ...
 78-412 1.76e-130

RocR-type transcriptional regulator, contains PAS, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 443041 [Multi-domain]  Cd Length: 448  Bit Score: 382.97  E-value: 1.76e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  78 LHARLRHHDQVRMGQTQILFSQRLGdlelkvlnssKNAKWQAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQR 157
Cdd:COG3829   118 LERKLREEELERGLSAKYTFDDIIG----------KSPAMKELLELAKRVAKSDSTVLILGESGTGKELFARAIHNASPR 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 158 SSGPLININCSALSESLVESELFGHTKGSFTGAT-DNRKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGS 236
Cdd:COG3829   188 RDGPFVAVNCAAIPENLLESELFGYEKGAFTGAKkGGKPGLFELADGGTLFLDEIGEMPLSLQAKLLRVLQEKEVRRVGG 267

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 237 DTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERMEDFEELLAFFAQKY-------RVRFDLATIK 309
Cdd:COG3829   268 TKPIPVDVRIIAATNRDLEEMVEEGRFREDLYYRLNVIPIHIPPLRERKEDIPLLAEHFLEKFnkkygknIKGISPEALE 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 310 ELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPMIVDQGLPISNmdwFPRPNGLN-MIQEMEKNLILELLEKNNGNQ 388
Cdd:COG3829   348 LLLAYDWPGNVRELENVIERAVVLSEGDVITPEHLPEYLLEEAEAAS---AAEEGSLKeALEEVEKELIEEALEKTGGNK 424

                         330       340
                  ....*....|....*....|....
gi 2258821257 389 RKTARELGMAKSTLHDRIRSYSID 412
Cdd:COG3829   425 SKAAKALGISRSTLYRKLKKYGIK 448
AtoC COG2204
DNA-binding transcriptional response regulator, NtrC family, contains REC, AAA-type ATPase, ...
 113-409 5.66e-119

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: 352.73  E-value: 5.66e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 113 KNAKWQAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATD 192
Cdd:COG2204   136 RSPAMQEVRRLIEKVAPSDATVLITGESGTGKELVARAIHRLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGAVA 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 193 NRKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLH 272
Cdd:COG2204   216 RRIGKFELADGGTLFLDEIGEMPLALQAKLLRVLQEREFERVGGNKPIPVDVRVIAATNRDLEELVEEGRFREDLYYRLN 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 273 VVEIRTPALSERMEDFEELLAFFAQKY------RVRFDLATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPM 346
Cdd:COG2204   296 VFPIELPPLRERREDIPLLARHFLARFaaelgkPVKLSPEALEALLAYDWPGNVRELENVIERAVILADGEVITAEDLPE 375

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258821257 347 IVDqglpisnmdwfprpnglnmiqEMEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRSY 409
Cdd:COG2204   376 ALE---------------------EVERELIERALEETGGNVSRAAELLGISRRTLYRKLKKY 417
AcoR COG3284
Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];
73-409 2.87e-109

Transcriptional regulator DhaR of acetoin/glycerol metabolism [Transcription];


Pssm-ID: 442514 [Multi-domain]  Cd Length: 625  Bit Score: 334.56  E-value: 2.87e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  73 NGAQVLHARLRHHDQVRMGQTQILFSQRLGDLELKVLNSsknAKWQAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLH 152
Cdd:COG3284   289 RDGRRLGALLRLRPARRAARAAPAGAPAPAALAALAGGD---PAMRRALRRARRLADRDIPVLILGETGTGKELFARAIH 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 153 KLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDN-RKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEI 231
Cdd:COG3284   366 AASPRADGPFVAVNCAAIPEELIESELFGYEPGAFTGARRKgRPGKIEQADGGTLFLDEIGDMPLALQARLLRVLQEREV 445

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 232 KPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERmEDFEELLAFFAQKY-----RVRFDLA 306
Cdd:COG3284   446 TPLGGTKPIPVDVRLIAATHRDLRELVAAGRFREDLYYRLNGLTLTLPPLRER-EDLPALIEHLLRELaagrgPLRLSPE 524

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 307 TIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPMIVDQGLPISNMDwfpRPNGLNMIQEMEKNLILELLEKNNG 386
Cdd:COG3284   525 ALALLAAYPWPGNVRELRNVLRTALALADGGVITVEDLPDELRAELAAAAPA---AAAPLTSLEEAERDAILRALRACGG 601

                         330       340
                  ....*....|....*....|...
gi 2258821257 387 NQRKTARELGMAKSTLHDRIRSY 409
Cdd:COG3284   602 NVSAAARALGISRSTLYRKLKRY 624
PRK05022 PRK05022
nitric oxide reductase transcriptional regulator NorR;
118-403 2.92e-101

nitric oxide reductase transcriptional regulator NorR;


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 310.18  E-value: 2.92e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 118 QAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGA 197
Cdd:PRK05022  197 QQLKKEIEVVAASDLNVLILGETGVGKELVARAIHAASPRADKPLVYLNCAALPESLAESELFGHVKGAFTGAISNRSGK 276

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 198 FNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIR 277
Cdd:PRK05022  277 FELADGGTLFLDEIGELPLALQAKLLRVLQYGEIQRVGSDRSLRVDVRVIAATNRDLREEVRAGRFRADLYHRLSVFPLS 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 278 TPALSERMEDFeELLA-FFAQKYRVRFDL-------ATIKELKAYSWPGNIRELRNAVARAA--ALVNGH----AVQPNH 343
Cdd:PRK05022  357 VPPLRERGDDV-LLLAgYFLEQNRARLGLrslrlspAAQAALLAYDWPGNVRELEHVISRAAllARARGAgrivTLEAQH 435

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258821257 344 IPMIVDQGLPISNMDWFP-RPNGLNMIQEME---KNLILELLEKNNGNQRKTARELGMAKSTLH 403
Cdd:PRK05022  436 LDLPAEVALPPPEAAAAPaAVVSQNLREATEafqRQLIRQALAQHQGNWAAAARALELDRANLH 499
PRK10365 PRK10365
sigma-54-dependent response regulator transcription factor ZraR;
86-402 1.54e-90

sigma-54-dependent response regulator transcription factor ZraR;


Pssm-ID: 182412 [Multi-domain]  Cd Length: 441  Bit Score: 280.76  E-value: 1.54e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  86 DQVRMGQTQILFSQRLGDLELKVLNSS------KNAKWQAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSS 159
Cdd:PRK10365  111 DNLQATLEKALAHTHSIDAETPAVTASqfgmvgKSPAMQHLLSEIALVAPSEATVLIHGDSGTGKELVARAIHASSARSE 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 160 GPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTS 239
Cdd:PRK10365  191 KPLVTLNCAALNESLLESELFGHEKGAFTGADKRREGRFVEADGGTLFLDEIGDISPMMQVRLLRAIQEREVQRVGSNQT 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 240 VSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERMEDFEELLAFFAQKYRVR-------FDLATIKELK 312
Cdd:PRK10365  271 ISVDVRLIAATHRDLAAEVNAGRFRQDLYYRLNVVAIEVPSLRQRREDIPLLAGHFLQRFAERnrkavkgFTPQAMDLLI 350

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 313 AYSWPGNIRELRNAVARAAALVNGHAVQPNHIPM-IVDQGLPISNMDwfprpnGLNMIQEMEKNLILELLEKNNGNQRKT 391
Cdd:PRK10365  351 HYDWPGNIRELENAVERAVVLLTGEYISERELPLaIASTPIPLGQSQ------DIQPLVEVEKEVILAALEKTGGNKTEA 424

                         330
                  ....*....|.
gi 2258821257 392 ARELGMAKSTL 402
Cdd:PRK10365  425 ARQLGITRKTL 435
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
127-412 6.91e-89

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 276.73  E-value: 6.91e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 127 IAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTL 206
Cdd:PRK11361  162 IALSQASVLISGESGTGKELIARAIHYNSRRAKGPFIKVNCAALPESLLESELFGHEKGAFTGAQTLRQGLFERANEGTL 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 207 FLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERME 286
Cdd:PRK11361  242 LLDEIGEMPLVLQAKLLRILQEREFERIGGHQTIKVDIRIIAATNRDLQAMVKEGTFREDLFYRLNVIHLILPPLRDRRE 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 287 DFEELLAFFAQKYR-------VRFDLATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPMIVDQGL-PISNMD 358
Cdd:PRK11361  322 DISLLANHFLQKFSsenqrdiIDIDPMAMSLLTAWSWPGNIRELSNVIERAVVMNSGPIIFSEDLPPQIRQPVcNAGEVK 401

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2258821257 359 WFP--RPNGLNMIQEMEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRSYSID 412
Cdd:PRK11361  402 TAPvgERNLKEEIKRVEKRIIMEVLEQQEGNRTRTALMLGISRRALMYKLQEYGID 457
Sigma54_activat pfam00158
Sigma-54 interaction domain;
114-277 1.46e-87

Sigma-54 interaction domain;


Pssm-ID: 425491 [Multi-domain]  Cd Length: 168  Bit Score: 263.11  E-value: 1.46e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 114 NAKWQAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDN 193
Cdd:pfam00158   5 SPAMQEVLEQAKRVAPTDAPVLITGESGTGKELFARAIHQLSPRADGPFVAVNCAAIPEELLESELFGHEKGAFTGADSD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 194 RKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHV 273
Cdd:pfam00158  85 RKGLFELADGGTLFLDEIGELPLELQAKLLRVLQEGEFERVGGTKPIKVDVRIIAATNRDLEEAVAEGRFREDLYYRLNV 164


                  ....
gi 2258821257 274 VEIR 277
Cdd:pfam00158 165 IPIE 168
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
 127-416 1.45e-86

Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein for nitrogen fixation. The model produces scores between the trusted and noise cutoffs for a well-described NifA homolog in Aquifex aeolicus (which lacks nitrogenase), for transcriptional activators of alternative nitrogenases (VFe or FeFe instead of MoFe), and truncated forms. [Central intermediary metabolism, Nitrogen fixation, Regulatory functions, DNA interactions]


Pssm-ID: 273817 [Multi-domain]  Cd Length: 534  Bit Score: 273.13  E-value: 1.45e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 127 IAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTL 206
Cdd:TIGR01817 215 VARSNSTVLLRGESGTGKELIAKAIHYLSPRAKRPFVKVNCAALSETLLESELFGHEKGAFTGAIAQRKGRFELADGGTL 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 207 FLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERME 286
Cdd:TIGR01817 295 FLDEIGEISPAFQAKLLRVLQEGEFERVGGNRTLKVDVRLVAATNRDLEEAVAKGEFRADLYYRINVVPIFLPPLRERRE 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 287 DFEELLAFFAQKYR------VRFDLATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIpmIVDQGLPISNMDWF 360
Cdd:TIGR01817 375 DIPLLAEAFLEKFNrengrpLTITPSAIRVLMSCKWPGNVRELENCLERTATLSRSGTITRSDF--SCQSGQCLSPMLAK 452

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 361 PRPNGLNMIQEM--------------------------EKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRSYSIDVK 414
Cdd:TIGR01817 453 TCPHGHISIDPLagttpphspasaalpgepglsgptlsERERLIAALEQAGWVQAKAARLLGMTPRQVGYALRKLNIEMK 532


                  ..
gi 2258821257 415 VF 416
Cdd:TIGR01817 533 KL 534
ntrC TIGR01818
nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response ...
 127-407 2.98e-84

nitrogen regulation protein NR(I); This model represents NtrC, a DNA-binding response regulator that is phosphorylated by NtrB and interacts with sigma-54. NtrC usually controls the expression of glutamine synthase, GlnA, and may be called GlnL, GlnG, etc. [Central intermediary metabolism, Nitrogen metabolism, Regulatory functions, DNA interactions, Signal transduction, Two-component systems]


Pssm-ID: 273818 [Multi-domain]  Cd Length: 463  Bit Score: 265.06  E-value: 2.98e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 127 IAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTL 206
Cdd:TIGR01818 153 LSRSDITVLINGESGTGKELVARALHRHSPRANGPFIALNMAAIPKDLIESELFGHEKGAFTGANTRRQGRFEQADGGTL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 207 FLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERME 286
Cdd:TIGR01818 233 FLDEIGDMPLDAQTRLLRVLADGEFYRVGGRTPIKVDVRIVAATHQNLEALVRQGKFREDLFHRLNVIRIHLPPLRERRE 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 287 DFEEL----LAFFAQKYRV---RFDLATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIP-------MIVDQGL 352
Cdd:TIGR01818 313 DIPRLarhfLALAARELDVepkLLDPEALERLKQLRWPGNVRQLENLCRWLTVMASGDEVLVSDLPaelaltgRPASAPD 392

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258821257 353 PISNMDW-----------FPR-PNGL--NMIQEMEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIR 407
Cdd:TIGR01818 393 SDGQDSWdealeawakqaLSRgEQGLldRALPEFERPLLEAALQHTRGHKQEAAALLGWGRNTLTRKLK 461
PRK15115 PRK15115
response regulator GlrR; Provisional
 127-417 2.03e-79

response regulator GlrR; Provisional


Pssm-ID: 185070 [Multi-domain]  Cd Length: 444  Bit Score: 252.07  E-value: 2.03e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 127 IAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTL 206
Cdd:PRK15115  153 VAQSDVSVLINGQSGTGKEILAQAIHNASPRASKPFIAINCGALPEQLLESELFGHARGAFTGAVSNREGLFQAAEGGTL 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 207 FLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERME 286
Cdd:PRK15115  233 FLDEIGDMPAPLQVKLLRVLQERKVRPLGSNRDIDIDVRIISATHRDLPKAMARGEFREDLYYRLNVVSLKIPALAERTE 312

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 287 DF----EELLAFFAQKYR--VR-FDLATIKELKAYSWPGNIRELRNAVARAAALVNGhavqpnhiPMI----VDQGLPIS 355
Cdd:PRK15115  313 DIpllaNHLLRQAAERHKpfVRaFSTDAMKRLMTASWPGNVRQLVNVIEQCVALTSS--------PVIsdalVEQALEGE 384

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258821257 356 NMdwfPRPNGLNMIQEMEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRSYSIDVKVFK 417
Cdd:PRK15115  385 NT---ALPTFVEARNQFELNYLRKLLQITKGNVTHAARMAGRNRTEFYKLLSRHELDANDFK 443
PEP_resp_reg TIGR02915
PEP-CTERM-box response regulator transcription factor; Members of this protein family share ...
 127-411 1.35e-78

PEP-CTERM-box response regulator transcription factor; Members of this protein family share full-length homology with (but do not include) the acetoacetate metabolism regulatory protein AtoC (see SP|Q06065). These proteins have a Fis family DNA binding sequence (pfam02954), a response regulator receiver domain (pfam00072), and sigma-54 interaction domain (pfam00158). [Regulatory functions, DNA interactions]


Pssm-ID: 274348 [Multi-domain]  Cd Length: 445  Bit Score: 250.05  E-value: 1.35e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 127 IAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTL 206
Cdd:TIGR02915 158 IAPSDITVLLLGESGTGKEVLARALHQLSDRKDKRFVAINCAAIPENLLESELFGYEKGAFTGAVKQTLGKIEYAHGGTL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 207 FLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERME 286
Cdd:TIGR02915 238 FLDEIGDLPLNLQAKLLRFLQERVIERLGGREEIPVDVRIVCATNQDLKRMIAEGTFREDLFYRIAEISITIPPLRSRDG 317

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 287 DFEELLAFFAQKYRVR-------FDLATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNhipmivDQGLPISNMDW 359
Cdd:TIGR02915 318 DAVLLANAFLERFARElkrktkgFTDDALRALEAHAWPGNVRELENKVKRAVIMAEGNQITAE------DLGLDARERAE 391

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2258821257 360 FPRPNGLNMIQE-MEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRSYSI 411
Cdd:TIGR02915 392 TPLEVNLREVRErAEREAVRKAIARVDGNIARAAELLGITRPTLYDLMKKHGI 444
phageshock_pspF TIGR02974
psp operon transcriptional activator PspF; Members of this protein family are PspF, the ...
 133-397 2.51e-74

psp operon transcriptional activator PspF; Members of this protein family are PspF, the sigma-54-dependent transcriptional activator of the phage shock protein (psp) operon, in Escherichia coli and numerous other species. The psp operon is induced by a number of stress conditions, including heat shock, ethanol, and filamentous phage infection. Changed com_name to adhere to TIGR role notes conventions. 09/15/06 - DMH [Regulatory functions, DNA interactions]


Pssm-ID: 274371 [Multi-domain]  Cd Length: 329  Bit Score: 235.27  E-value: 2.51e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 133 PVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTLFLDEIG 212
Cdd:TIGR02974  24 PVLIIGERGTGKELIAARLHYLSKRWQGPLVKLNCAALSENLLDSELFGHEAGAFTGAQKRHQGRFERADGGTLFLDELA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 213 DLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERMEDFEELL 292
Cdd:TIGR02974 104 TASLLVQEKLLRVIEYGEFERVGGSQTLQVDVRLVCATNADLPALAAEGRFRADLLDRLAFDVITLPPLRERQEDIMLLA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 293 AFFA--------QKYRVRFDLATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHI-------PMIVDQGLP---- 353
Cdd:TIGR02974 184 EHFAirmarelgLPLFPGFTPQAREQLLEYHWPGNVRELKNVVERSVYRHGLEEAPIDEIiidpfasPWRPKQAAPavde 263

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2258821257 354 -ISNMDWFPRPNGLNMI---------QEMEKNLILELLEKNNGNQRKTARELGM 397
Cdd:TIGR02974 264 vNSTPTDLPSPSSIAAAfpldlkqaqQDYEIELLQQALAEAQFNQRKAAELLGL 317
PRK15424 PRK15424
propionate catabolism operon regulatory protein PrpR; Provisional
 128-408 6.59e-74

propionate catabolism operon regulatory protein PrpR; Provisional


Pssm-ID: 237963 [Multi-domain]  Cd Length: 538  Bit Score: 240.39  E-value: 6.59e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 128 AQSHLPVLISGPSGSGKEVVAQTLHK--------LSQRSSGPLININCSALSESLVESELFGHTKGSFTGAT-DNRKGAF 198
Cdd:PRK15424  239 ARSSAAVLIQGETGTGKELAAQAIHReyfarhdaRQGKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRrGGRAGLF 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 199 NAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRT 278
Cdd:PRK15424  319 EIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCDLEEDVRQGRFRRDLFYRLSILRLQL 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 279 PALSERMEDFEELLAFFAQKY----RVRFDLATIKEL-------KAYSWPGNIRELRNAVARAAALVnghAVQPNHI--P 345
Cdd:PRK15424  399 PPLRERVADILPLAESFLKQSlaalSAPFSAALRQGLqqcetllLHYDWPGNVRELRNLMERLALFL---SVEPTPDltP 475

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258821257 346 MIVDQGLP---ISNMDWFPRPNGLNMIQemeknlilELLEKNNGNQRKTARELGMAKSTLHDRIRS 408
Cdd:PRK15424  476 QFLQLLLPelaRESAKTPAPRLLAATLQ--------QALERFNGDKTAAANYLGISRTTLWRRLKA 533
TyrR COG3283
Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid ...
 85-344 3.06e-71

Transcriptional regulator TyrR of aromatic amino acids metabolism [Transcription, Amino acid transport and metabolism];


Pssm-ID: 442513 [Multi-domain]  Cd Length: 514  Bit Score: 232.77  E-value: 3.06e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  85 HDQVRMG-QTQILFSQRLGDLELKVLNSSKNAKWQAQLNRLpaiAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLI 163
Cdd:COG3283   183 KSAARLGeQLQALQVNDDSGFDHIVASSPKMRQVIRQAKKM---AMLDAPLLIQGETGTGKELLARACHLASPRGDKPFL 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 164 NINCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTD 243
Cdd:COG3283   260 ALNCAALPDDVAESELFGYAPGAFGNAREGKKGLFEQANGGTVFLDEIGEMSPQLQAKLLRFLQDGTFRRVGEEQEVKVD 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 244 VRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERMEDFEELLAFFAQKY-------RVRFDLATIKELKAYSW 316
Cdd:COG3283   340 VRVICATQKDLAELVQEGEFREDLYYRLNVLTLTLPPLRERKSDILPLAEHFVARFsqqlgrpRPRLSPDLVDFLQSYPW 419

                         250       260
                  ....*....|....*....|....*...
gi 2258821257 317 PGNIRELRNAVARAAALVNGHAVQPNHI 344
Cdd:COG3283   420 PGNVRQLENALYRAVSLLEGDELTPEDL 447
propionate_PrpR TIGR02329
propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists ...
 128-408 1.05e-69

propionate catabolism operon regulatory protein PrpR; At least five distinct pathways exists for the catabolism of propionate by way of propionyl-CoA. Members of this family represent the transcriptional regulatory protein PrpR, whose gene is found in most cases divergently transcribed from an operon for the methylcitric acid cycle of propionate catabolism. 2-methylcitric acid, a catabolite by this pathway, is a coactivator of PrpR. [Regulatory functions, DNA interactions]


Pssm-ID: 274079 [Multi-domain]  Cd Length: 526  Bit Score: 228.98  E-value: 1.05e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 128 AQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGA-TDNRKGAFNAARGGTL 206
Cdd:TIGR02329 232 ARSDATVLILGESGTGKELVAQAIHQLSGRRDFPFVAINCGAIAESLLEAELFGYEEGAFTGArRGGRTGLIEAAHRGTL 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 207 FLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERME 286
Cdd:TIGR02329 312 FLDEIGEMPLPLQTRLLRVLEEREVVRVGGTEPVPVDVRVVAATHCALTTAVQQGRFRRDLFYRLSILRIALPPLRERPG 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 287 DFEELLAFFAQK-----------YRVRFDLATIKELKAYSWPGNIRELRNAVARAA---ALVNGHAVQPNHIPMIVDQgL 352
Cdd:TIGR02329 392 DILPLAAEYLVQaaaalrlpdseAAAQVLAGVADPLQRYPWPGNVRELRNLVERLAlelSAMPAGALTPDVLRALAPE-L 470

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2258821257 353 PISNMDWFPRPNGLNMIQEMEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRS 408
Cdd:TIGR02329 471 AEASGKGKTSALSLRERSRVEALAVRAALERFGGDRDAAAKALGISRTTLWRRLKA 526
PRK15429 PRK15429
formate hydrogenlyase transcriptional activator FlhA;
121-413 7.68e-69

formate hydrogenlyase transcriptional activator FlhA;


Pssm-ID: 237965 [Multi-domain]  Cd Length: 686  Bit Score: 230.49  E-value: 7.68e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 121 LNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNA 200
Cdd:PRK15429  389 LKQVEMVAQSDSTVLILGETGTGKELIARAIHNLSGRNNRRMVKMNCAAMPAGLLESDLFGHERGAFTGASAQRIGRFEL 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 201 ARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPA 280
Cdd:PRK15429  469 ADKSSLFLDEVGDMPLELQPKLLRVLQEQEFERLGSNKIIQTDVRLIAATNRDLKKMVADREFRSDLYYRLNVFPIHLPP 548

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 281 LSERMEDFEELLAFFAQKYRVRFD-------LATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNhIPmivDQGLP 353
Cdd:PRK15429  549 LRERPEDIPLLVKAFTFKIARRMGrnidsipAETLRTLSNMEWPGNVRELENVIERAVLLTRGNVLQLS-LP---DITLP 624

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258821257 354 ISNMDwfPRPNGLNMIQEMEKNLILELLEKNNG---NQRKTARELGMAKSTLHDRIRSYSIDV 413
Cdd:PRK15429  625 EPETP--PAATVVAQEGEDEYQLIVRVLKETNGvvaGPKGAAQRLGLKRTTLLSRMKRLGIDK 685
FhlA COG3604
FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis ...
 118-412 1.96e-68

FhlA-type transcriptional regulator, contains GAF, AAA-type ATPase, and DNA-binding Fis domains [Transcription, Signal transduction mechanisms];


Pssm-ID: 442823 [Multi-domain]  Cd Length: 338  Bit Score: 220.10  E-value: 1.96e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 118 QAQLNRLPAIAqSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESelfghtkgsftgatdnrkga 197
Cdd:COG3604   103 EEDLRLLETLA-SLAAVAILGETGTGKELVANAIHELSPRADKPFVKVNCAALPESLLES-------------------- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 198 fnaarggtlfldeigdlpinlqpkmlraLENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIR 277
Cdd:COG3604   162 ----------------------------LQEGEFERVGGDETIKVDVRIIAATNRDLEEEVAEGRFREDLYYRLNVFPIR 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 278 TPALSERMEDFEELLAFFAQKYR-------VRFDLATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPmivdq 350
Cdd:COG3604   214 LPPLRERREDIPLLAEHFLEKFSrrlgkpiLRLSPEALEALMAYPWPGNVRELENVIERAVILAEGGVLDADDLA----- 288

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258821257 351 glpisnmdwfprPNGLNMIQEMEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRSYSID 412
Cdd:COG3604   289 ------------PGSREALEEVEREHILEALERTGGNIAGAARLLGLTPSTLRSRMKKLGIK 338
glnG PRK10923
nitrogen regulation protein NR(I); Provisional
 127-412 2.58e-65

nitrogen regulation protein NR(I); Provisional


Pssm-ID: 182842 [Multi-domain]  Cd Length: 469  Bit Score: 215.89  E-value: 2.58e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 127 IAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTL 206
Cdd:PRK10923  157 LSRSSISVLINGESGTGKELVAHALHRHSPRAKAPFIALNMAAIPKDLIESELFGHEKGAFTGANTIRQGRFEQADGGTL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 207 FLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERME 286
Cdd:PRK10923  237 FLDEIGDMPLDVQTRLLRVLADGQFYRVGGYAPVKVDVRIIAATHQNLEQRVQEGKFREDLFHRLNVIRVHLPPLRERRE 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 287 DFEELLAFFAQKYRVRFDLA-------TIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPM-IVDQGLPISNMD 358
Cdd:PRK10923  317 DIPRLARHFLQVAARELGVEakllhpeTEAALTRLAWPGNVRQLENTCRWLTVMAAGQEVLIQDLPGeLFESTVPESTSQ 396

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2258821257 359 WFP------------------RPNGLNMIQ-EMEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRSYSID 412
Cdd:PRK10923  397 MQPdswatllaqwadralrsgHQNLLSEAQpELERTLLTTALRHTQGHKQEAARLLGWGRNTLTRKLKELGME 469
PRK10820 PRK10820
transcriptional regulator TyrR;
56-414 6.22e-60

transcriptional regulator TyrR;


Pssm-ID: 236769 [Multi-domain]  Cd Length: 520  Bit Score: 202.99  E-value: 6.22e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  56 EGQFFIQD-----LGSRNGTYVN-GAQVLharLRhhDQVRMG-QTQILFSQRLGDLELKVLNSSKNAKWQAQLNRLpaiA 128
Cdd:PRK10820  153 NGQDFLMEitpvyLQDENDQHVLvGAVVM---LR--STARMGrQLQNLAVNDDSAFSQIVAVSPKMRQVVEQARKL---A 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 129 QSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNAARGGTLFL 208
Cdd:PRK10820  225 MLDAPLLITGDTGTGKDLLAYACHLRSPRGKKPFLALNCASIPDDVVESELFGHAPGAYPNALEGKKGFFEQANGGSVLL 304

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 209 DEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERMEDF 288
Cdd:PRK10820  305 DEIGEMSPRMQAKLLRFLNDGTFRRVGEDHEVHVDVRVICATQKNLVELVQKGEFREDLYYRLNVLTLNLPPLRDRPQDI 384

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 289 EELLAFFAQKY---------RVRFDLATIkeLKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPM-IVDQGLPISN-- 356
Cdd:PRK10820  385 MPLTELFVARFadeqgvprpKLAADLNTV--LTRYGWPGNVRQLKNAIYRALTQLEGYELRPQDILLpDYDAAVAVGEda 462

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2258821257 357 MDwfprpNGLNMIQEMEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIRSYSIDVK 414
Cdd:PRK10820  463 ME-----GSLDEITSRFERSVLTRLYRNYPSTRKLAKRLGVSHTAIANKLREYGLSQK 515
pspF PRK11608
phage shock protein operon transcriptional activator; Provisional
 121-397 9.92e-60

phage shock protein operon transcriptional activator; Provisional


Pssm-ID: 236936 [Multi-domain]  Cd Length: 326  Bit Score: 197.20  E-value: 9.92e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 121 LNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTKGSFTGATDNRKGAFNA 200
Cdd:PRK11608   19 LEQVSRLAPLDKPVLIIGERGTGKELIASRLHYLSSRWQGPFISLNCAALNENLLDSELFGHEAGAFTGAQKRHPGRFER 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 201 ARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPA 280
Cdd:PRK11608   99 ADGGTLFLDELATAPMLVQEKLLRVIEYGELERVGGSQPLQVNVRLVCATNADLPAMVAEGKFRADLLDRLAFDVVQLPP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 281 LSERMEDFEELLAFFA-QKYR-------VRFDLATIKELKAYSWPGNIRELRNAVARAaalVNGHAVQPNHIPMIV---- 348
Cdd:PRK11608  179 LRERQSDIMLMAEHFAiQMCRelglplfPGFTERARETLLNYRWPGNIRELKNVVERS---VYRHGTSEYPLDNIIidpf 255

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2258821257 349 ------DQGLPISNMDWFPRPNGLNMIQ-EMEKNLILELLEKNNGNQRKTARELGM 397
Cdd:PRK11608  256 krrpaeEAIAVSETTSLPTLPLDLREWQhQQEKELLQRSLQQAKFNQKRAAELLGL 311
RtcR COG4650
Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a ...
 119-333 3.09e-52

Sigma54-dependent transcription regulator containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 443688 [Multi-domain]  Cd Length: 534  Bit Score: 182.72  E-value: 3.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 119 AQLNRLpaIAQ-------SHLPVLISGPSGSGKEVVAQTLHKLSQRS---SGPLININCSALSESLVESELFGHTKGSFT 188
Cdd:COG4650   191 AAFNRL--IEQiervairSRAPILLTGPTGAGKSQLARRIYELKKARhqvSGRFVEVNCATLRGDGAMSALFGHVKGAFT 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 189 GATDNRKGAFNAARGGTLFLDEIGDLPINLQPKMLRALENNEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLF 268
Cdd:COG4650   269 GAVSDRAGLLRSADGGVLFLDEIGELGLDEQAMLLRAIEEKRFLPVGSDKEVSSDFQLIAGTNRDLRQEVAEGRFREDLL 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 269 YRLHVVEIRTPALSERMEDFE----ELLAFFAQKY--RVRFDlatiKELKA-Y---------SWPGNIRELRNAVARAAA 332
Cdd:COG4650   349 ARINLWTFRLPGLAERREDIEpnldYELARFAREQgrRVRFN----KEARArYlafatspeaLWSGNFRDLNASVTRMAT 424


                  .
gi 2258821257 333 L 333
Cdd:COG4650   425 L 425
PRK11388 PRK11388
DNA-binding transcriptional regulator DhaR; Provisional
 5-417 6.43e-51

DNA-binding transcriptional regulator DhaR; Provisional


Pssm-ID: 183114 [Multi-domain]  Cd Length: 638  Bit Score: 181.41  E-value: 6.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257   5 YNQRGFLTLVSEKTVRTVEIGQFASIGRSADNTL----VIQDDFASGR---HARV-LNKEGQFfIQDLGS----RNGTYV 72
Cdd:PRK11388  219 WDEQGNLQFLNAQAARLLRLDATASQGRAITELLtlpaVLQQAIKQAHplkHVEVtFESQGQF-IDAVITlkpiIEGQGT 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  73 NGAQVLHA--RLRHHDQVRMGQTQILFSQRLG-DLELK-VLNSSKNAkwqaqlnrlpaiAQSHLPVLISGPSGSGKEVVA 148
Cdd:PRK11388  298 SFILLLHPveQMRQLMTSQLGKVSHTFDHMPQdSPQMRrLIHFGRQA------------AKSSFPVLLCGEEGVGKALLA 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 149 QTLHKLSQRSSGPLININCSALSESLVESELFGhtkGSFTGATDNRKGAFNAARGGTLFLDEIGDLPINLQPKMLRALEN 228
Cdd:PRK11388  366 QAIHNESERAAGPYIAVNCQLYPDEALAEEFLG---SDRTDSENGRLSKFELAHGGTLFLEKVEYLSPELQSALLQVLKT 442

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 229 NEIKPVGSDTSVSTDVRIIAATHKNIRQKVKSGEFREDLFYRLHVVEIRTPALSERMEDFEEL----LAFFAQKYRVRF- 303
Cdd:PRK11388  443 GVITRLDSRRLIPVDVRVIATTTADLAMLVEQNRFSRQLYYALHAFEITIPPLRMRREDIPALvnnkLRSLEKRFSTRLk 522

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 304 -DLATIKELKAYSWPGNIRELRNAVARAAALVNGHAVQPNHIPMIVDQGLPISNMDWFPRPNGLNMiQEMEKNLILELLE 382
Cdd:PRK11388  523 iDDDALARLVSYRWPGNDFELRSVIENLALSSDNGRIRLSDLPEHLFTEQATDDVSATRLSTSLSL-AELEKEAIINAAQ 601

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 2258821257 383 KNNGNQRKTARELGMAKSTLHDRIRSYSIDVKVFK 417
Cdd:PRK11388  602 VCGGRIQEMAALLGIGRTTLWRKMKQHGIDAGQFK 636
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
29-97 2.17e-24

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 96.18  E-value: 2.17e-24
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLH-ARLRHHDQVRMGQTQILF 97
Cdd:COG1716    24 TIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQRVTEpAPLRDGDVIRLGKTELRF 93
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
 132-330 1.10e-23

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 103.65  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 132 LPVLISGPSGSGKEVVAQTLHKLSQRS-----SGPLININCSALSES--LVESELFGHTKGSFTGATDNRKGAFNAARGG 204
Cdd:COG1221   131 LHTLILGPTGVGKSFFAELMYEYAIEIgvlpeDAPFVVFNCADYANNpqLLMSQLFGYVKGAFTGADKDKEGLIEKADGG 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 205 TLFLDEIGDLPINLQPKMLRALENNEIKPVG-SDTSVSTDVRIIAATHKNI---------RqkvksgefredlfyRLHVV 274
Cdd:COG1221   211 ILFLDEVHRLPPEGQEMLFTFMDKGIYRRLGeTEKTRKANVRIIFATTEDPessllktflR--------------RIPMV 276

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258821257 275 eIRTPALSER--MEDFEELLAFFAQ-----KYRVRFDLATIKELKAYSWPGNIRELRNAV----ARA 330
Cdd:COG1221   277 -IKLPSLEERslEERLELIKHFFKEeakrlNKPIKVSKEVLKALLLYDCPGNIGQLKSDIqlacAKA 342
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 126-271 2.97e-22

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 92.21  E-value: 2.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 126 AIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESELFGHTkgsftgATDNRKGAFNAARGGT 205
Cdd:cd00009    14 LELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHF------LVRLLFELAEKAKPGV 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258821257 206 LFLDEIGDLPINLQPKMLRALENneikpVGSDTSVSTDVRIIAATHKNIrqkvkSGEFREDLFYRL 271
Cdd:cd00009    88 LFIDEIDSLSRGAQNALLRVLET-----LNDLRIDRENVRVIGATNRPL-----LGDLDRALYDRL 143
Sigma54_activ_2 pfam14532
Sigma-54 interaction domain;
113-281 1.02e-21

Sigma-54 interaction domain;


Pssm-ID: 434021 [Multi-domain]  Cd Length: 138  Bit Score: 90.48  E-value: 1.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 113 KNAKWQAQLNRLPAIAQSHLPVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVESelfghtkgsftgatd 192
Cdd:pfam14532   3 ASAAIQEIKRRLEQAAQSTLPVFLTGEPGSGKEFCARYLHNPSTPWVQPFDIEYLAHAPLELLEQ--------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 193 nrkgafnaARGGTLFLDEIGDLPINLQ---PKMLRALENNeikpvgsdtsvstDVRIIAATHKNIRQKVKSGEFREDLFY 269
Cdd:pfam14532  68 --------AKGGTLYLKDIADLSKALQkglLLLLAKAEGY-------------RVRLVCTSSKDLPQLAAAGLFDEQLYF 126

                         170
                  ....*....|..
gi 2258821257 270 RLHVVEIRTPAL 281
Cdd:pfam14532 127 ELSALRLHVPPL 138
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 29-98 2.46e-21

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 87.72  E-value: 2.46e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLH-ARLRHHDQVRMGQTQILFS 98
Cdd:cd00060    22 TIGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNGKRITPpVPLQDGDVIRLGDTTFRFE 92
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 28-93 5.03e-21

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438745 [Multi-domain]  Cd Length: 91  Bit Score: 86.97  E-value: 5.03e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258821257  28 ASIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHA-RLRHHDQVRMGQT 93
Cdd:cd22693    20 ITIGRADDNDLVLSDDFVSSRHARIYLQGSSWYLEDLGSTNGTFVNGNRVTQPvVVQPGDTIRIGAT 86
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 25-98 1.49e-15

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 77.88  E-value: 1.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  25 GQFASIGRSADNTLVIQDD--FASGRHARVLNKEGQFFIQDLgSRNGTYVNGAQV-LH----ARLRHHDQVRMGQTQILF 97
Cdd:COG3456    25 RGGGTIGRSADCDWVLPDPdrSVSRRHAEIRFRDGAFCLTDL-STNGTFLNGSDHpLGpgrpVRLRDGDRLRIGDYEIRV 103


                  .
gi 2258821257  98 S 98
Cdd:COG3456   104 E 104
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 29-90 1.94e-15

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 70.30  E-value: 1.94e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEG-QFFIQDLGSRNGTYVNGAQVLH--ARLRHHDQVRM 90
Cdd:pfam00498   2 TIGRSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGSTNGTFVNGQRLGPepVRLKDGDVIRL 66
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
 25-98 8.32e-15

forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438750 [Multi-domain]  Cd Length: 93  Bit Score: 69.75  E-value: 8.32e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258821257  25 GQFaSIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHARLRHHDQVRMGQTQILFS 98
Cdd:cd22698    21 DEF-TIGRSSNNDIRLNDHSVSRHHARIVRQGDKCNLTDLGSTNGTFLNGIRVGTHELKHGDRIQLGETIFRFI 93
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
 28-96 6.80e-14

forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438732 [Multi-domain]  Cd Length: 96  Bit Score: 66.98  E-value: 6.80e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258821257  28 ASIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLH--ARLRHHDQVRMGQTQIL 96
Cdd:cd22680    23 VSIGRDPENVIVIPDPFVSRNHARITVDSNEIYIEDLGSTNGTFVNDFKRIKgpAKLHPNDIIKLGRTTVL 93
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 11-92 1.28e-13

first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438746 [Multi-domain]  Cd Length: 93  Bit Score: 66.20  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  11 LTLVSEKTVRTVEIGQFASIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHARLRHHDQVRM 90
Cdd:cd22694     1 LTIRIPGGELRFDPGSSVRIGRDPDADVRLDDPRVSRRHALLEFDGDGWVYTDLGSRNGTYLNGRRVQQVKLSDGTRVRL 80


                  ..
gi 2258821257  91 GQ 92
Cdd:cd22694    81 GD 82
FHA_AGGF1 cd22686
forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 ...
 28-97 1.45e-12

forkhead associated (FHA) domain found in angiogenic factor with G patch and FHA domains 1 (AGGF1) and similar proteins; AGGF1, also called angiogenic factor VG5Q, or G patch domain-containing protein 7 (GPATC7), or vasculogenesis gene on 5q protein, is an angiogenic factor involved in vascular development, angiogenesis, specification of hemangioblasts, and differentiation of veins. It promotes angiogenesis and the proliferation of endothelial cells. It inhibits inflammatory effect and preserve vascular integrity in non-nervous system diseases. Mutated AGGF1 causes susceptibility to Klippel-Trenaunay syndrome, a vascular disorder. Increased AGGF1 expression is associated with tumor angiogenesis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438738 [Multi-domain]  Cd Length: 123  Bit Score: 64.23  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  28 ASIGRSADN--TLVIQDDFASGRHARVL--NKEGQFFIQDLGSRNGTYVNGAQVLHAR-------LRHHDQVRMGQTQIL 96
Cdd:cd22686    28 ATIGREKDHghTIRIPELGVSKFHAEIYydDDEQSYTIVDLGSQNGTYLNGVRISQPKeksdpypLTHGDELKIGETTLL 107


                  .
gi 2258821257  97 F 97
Cdd:cd22686   108 F 108
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 26-97 2.35e-12

second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 62.51  E-value: 2.35e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2258821257  26 QFASIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHARLRHHDQVRMGQTQILF 97
Cdd:cd22737    21 QAVRIGRASDNDIVIPEGSVSRHHATLVPTPGGTQIRDLRSTNGTFVNGLRVDAALLHDGDVVTIGDIDFVF 92
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 133-277 3.54e-11

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 60.85  E-value: 3.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  133 PVLISGPSGSGKEVVAQTLHKLSQRSSGPLININCSALSESLVES---ELFGHTKGSFTGATDNRKgAFNAARG---GTL 206
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQlllIIVGGKKASGSGELRLRL-ALALARKlkpDVL 82

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258821257  207 FLDEIGDLPINLQPKMLRALENNEikpVGSDTSVSTDVRIIAATHKniRQKVKSGEFREDLFYRLHVVEIR 277
Cdd:smart00382  83 ILDEITSLLDAEQEALLLLLEELR---LLLLLKSEKNLTVILTTND--EKDLGPALLRRRFDRRIVLLLIL 148
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 30-95 8.69e-11

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438720 [Multi-domain]  Cd Length: 91  Bit Score: 58.25  E-value: 8.69e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258821257  30 IGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQV-LHARLRHHDQVRMGQTQI 95
Cdd:cd22668    22 IGRGSDADFRLPDTGVSRRHAEIRWDGQVAHLTDLGSTNGTTVNNAPVtPEWRLADGDVITLGHSEI 88
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 29-77 3.08e-10

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 55.26  E-value: 3.08e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2258821257   29 SIGR-SADNTLVIQDDFASGRHARVLNKEG-QFFIQDLGSRNGTYVNGAQV 77
Cdd:smart00240   2 TIGRsSEDCDIQLDGPSISRRHAVIVYDGGgRFYLIDLGSTNGTFVNGKRI 52
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
 29-97 5.49e-10

forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438736 [Multi-domain]  Cd Length: 94  Bit Score: 55.85  E-value: 5.49e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHARLRHHDQVRMGQTQILF 97
Cdd:cd22684    24 TAGRHPESDIFLDDVTVSRRHAEFRRAEGGFVVRDVGSLNGTYVNRERIDSAVLRNGDEVQIGKFRLVF 92
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
 30-97 3.29e-09

forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.


Pssm-ID: 438734 [Multi-domain]  Cd Length: 96  Bit Score: 53.69  E-value: 3.29e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258821257  30 IGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNG---AQVLHARLRHHDQVRMGQTQILF 97
Cdd:cd22682    24 IGRSVESQVQIDDDSVSRYHAKLAVNPSAVSIIDLGSTNGTIVNGkkiPKLASCDLQNGDQIKIGNTIFKF 94
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
 30-109 6.24e-09

forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438717 [Multi-domain]  Cd Length: 97  Bit Score: 53.00  E-value: 6.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  30 IGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHARLRHhdQVRMGQtQILFsqrlGDLELKVL 109
Cdd:cd22665    25 IGRDPSCSVVLPDKSVSKQHACIEVDGGTHLIEDLGSTNGTRIGNKVRLKPNVRY--ELIDGD-LLLF----GDVKCQYV 97
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
 27-96 7.38e-09

forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438730 [Multi-domain]  Cd Length: 102  Bit Score: 53.13  E-value: 7.38e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258821257  27 FASIGRSADNTLVIQDDFASGRHARVL--NKEGQFFIQDLGSRNGTYVNGAQVLHA----RLRHHDQVRMG-QTQIL 96
Cdd:cd22678    24 PLTIGRIQRGDIALKDDEVSGKHARIEwnSTGSKWELVDLGSLNGTLVNGESISPNgrpvVLSSGDVITLGsETKIL 100
FHA_GarA-like cd22720
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ...
 29-97 3.09e-08

forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438772 [Multi-domain]  Cd Length: 100  Bit Score: 51.16  E-value: 3.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHARLRHHDQVRMGQTQILF 97
Cdd:cd22720    27 SAGRHPDSDIFLDDVTVSRRHAEFRLENNEFNVVDVGSLNGTYVNREPVDSAVLANGDEVQIGKFRLVF 95
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 30-97 9.34e-08

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 49.57  E-value: 9.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  30 IGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLH--ARLRHHDQVRMGQTQILF 97
Cdd:pfam16697  21 IGSDPDCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGSGNGTLVNGQRVTElgIALRPGDRIELGQTEFCL 90
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
 15-74 1.45e-07

forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438722 [Multi-domain]  Cd Length: 105  Bit Score: 49.53  E-value: 1.45e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2258821257  15 SEKTVRTVEIGQFASIGRSADNTLVIQDDFASGRHAR----VLNKEGQ--FFIQDLgSRNGTYVNG 74
Cdd:cd22670    11 STDIVLPIYKNQVITIGRSPSCDIVINDPFVSRTHCRiysvQFDESSAplVYVEDL-SSNGTYLNG 75
FHA_ZEP-like cd22702
forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar ...
 26-89 2.40e-07

forkhead associated (FHA) domain found in chloroplastic zeaxanthin epoxidase (ZEP) and similar proteins; ZEP, also called protein ABA DEFICIENT 1, ABA1, protein IMPAIRED IN BABA-INDUCED STERILITY 3, protein LOW EXPRESSION OF OSMOTIC STRESS-RESPONSIVE GENES 6, or protein NON-PHOTOCHEMICAL QUENCHING 2, plays an important role in the xanthophyll cycle and abscisic acid (ABA) biosynthesis. It converts zeaxanthin into antheraxanthin and subsequently violaxanthin. ZEP is required for resistance to osmotic and drought stresses, ABA-dependent stomatal closure, seed development and dormancy, modulation of defense gene expression, and disease resistance and non-photochemical quencing (NPQ). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438754 [Multi-domain]  Cd Length: 123  Bit Score: 49.35  E-value: 2.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258821257  26 QFASIGRSAD-----NTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHARLRHHDQVR 89
Cdd:cd22702    32 QPCIIGSDPHqaisgISVVIPSPQVSELHARITCKNGAFFLTDLGSEHGTWINDNEGRRYRAPPNFPVR 100
FHA_Slr1951-like cd22697
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ...
 11-99 5.39e-07

forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438749 [Multi-domain]  Cd Length: 102  Bit Score: 47.84  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  11 LTLVSEKTVRTVEIG-QFASIGRSADNTLVIQDDFASGRHARVLNK-----EGQFFIQDLG-----SRNGTYVNGAQVLH 79
Cdd:cd22697     2 LVELDGNVRREIRLDePIYTIGRHPGNDIQIPSQQISRRHATLRRKinpnlDISFWIIDGDlegaeSLNGLWVNGERILQ 81

                          90       100
                  ....*....|....*....|
gi 2258821257  80 ARLRHHDQVRMGQTQILFSQ 99
Cdd:cd22697    82 HELVNGDEIALGPKIVLRYQ 101
FHA_FHAD1 cd22700
forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 ...
 26-97 6.09e-07

forkhead associated (FHA) domain found in forkhead-associated domain-containing protein 1 (FHAD1) and similar proteins; FHAD1, also called FHA domain-containing protein 1, is an uncharacterized FHA domain-containing protein. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438752 [Multi-domain]  Cd Length: 96  Bit Score: 47.25  E-value: 6.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258821257  26 QFASIGR-SADntLVIQDDFASGRHArVLNK---EGQFFIQDLGSRNGTYVNGAQVLHA--RLRHHDQVRMGQTQILF 97
Cdd:cd22700    16 KVTTIGReGCD--LVLQSPGVEEQHA-VIEYseqENCFVLQDLNTAQGTYVNDCRIQNAavRLAPGDVLRFGFGGLPY 90
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 30-98 7.22e-07

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 47.21  E-value: 7.22e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258821257  30 IGRSADNTLVIQDDFASGRHARV-LNKEGQFFIQDLGSRNGTYVNGAQVLH-ARLRHHDQVRMGQTQILFS 98
Cdd:cd22673    25 FGRDLSCDIRIQLPGVSREHCRIeVDENGKAYLENLSTTNPTLVNGKAIEKsAELKDGDVITIGGRSFRFE 95
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 133-251 2.64e-06

AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 46.52  E-value: 2.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257 133 PVLISGPSGSGKEVVAQTL-HKLSQRSSGPLinincsALSESLVESELFGHTKgSFTGATDNRKGAF-NAAR-GGTLFLD 209
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLaAALSNRPVFYV------QLTRDTTEEDLFGRRN-IDPGGASWVDGPLvRAAReGEIAVLD 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2258821257 210 EIGDLPINLQPKMLRALENNEIKPVGSDTSVS---TDVRIIAATH 251
Cdd:pfam07728  74 EINRANPDVLNSLLSLLDERRLLLPDGGELVKaapDGFRLIATMN 118
FHA_Ct664-like cd22696
forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar ...
 22-96 3.27e-06

forkhead associated (FHA) domain found in Chlamydia trachomatis Ct664 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Chlamydia trachomatis Ct664 protein. Ct664 situates within the type III secretion system cluster that also encodes an STPK (CT673 in C. trachomatis), suggesting a role of CT664 in the chlamydial type III secretion system by mediating phosphorylation-dependent protein-protein interactions. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438748 [Multi-domain]  Cd Length: 97  Bit Score: 45.18  E-value: 3.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258821257  22 VEIGQFASIGRSADNT-LVIQDDFASGRHARV-LNKEGQFFIQDLGSRNGTYVNGAQVLH-ARLRHHDQVRMGQTQIL 96
Cdd:cd22696    17 LESGKTYFIGKDPTVCdIVLQDPSISRQHARLsIDQDNRVFIEDLSSKNGVLVNGKPIEGkEEISGSDVISLGTTSFL 94
HTH_8 pfam02954
Bacterial regulatory protein, Fis family;
371-407 7.18e-06

Bacterial regulatory protein, Fis family;


Pssm-ID: 427077 [Multi-domain]  Cd Length: 40  Bit Score: 42.77  E-value: 7.18e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2258821257 371 EMEKNLILELLEKNNGNQRKTARELGMAKSTLHDRIR 407
Cdd:pfam02954   3 EVEKELIEAALERTGGNKSKAARLLGISRRTLYRKLK 39
FHA_CHFR cd22672
forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains ...
 30-89 1.49e-05

forkhead associated (FHA) domain found in checkpoint with forkhead and RING finger domains protein (CHFR); CHFR, also called RING finger protein 196 (RNF196), is a checkpoint protein that delays entry into mitosis in response to stress. It functions as an E3 ubiquitin ligase that ubiquitinates and degrades its target proteins, such as Aurora-A, Plk1, Kif22 and PARP-1, which are critical for proper mitotic transitions. It also plays an important role in cell cycle progression and tumor suppression and is negatively regulated by SUMOylation-mediated proteasomal ubiquitylation. Moreover, CHFR is involved in the early stage of the DNA damage response, which mediates the crosstalk between ubiquitination and poly-ADP-ribosylation. CHFR contains a fork head associated-(FHA) domain and a RING-HC finger. The CHFR FHA domain has been crystallized as a segment-swapped dimer. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438724 [Multi-domain]  Cd Length: 108  Bit Score: 43.82  E-value: 1.49e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2258821257  30 IGRSADNTLVIQDD-FASGRHARVL-NKEGQFFIQDLgSRNGTYVNGAQVLH---ARLRHHDQVR 89
Cdd:cd22672    25 IGRAKDCDLSFPGNkLVSGDHCKIIrDEKGQVWLEDT-STNGTLVNKVKVVKgqkVELKHGDVIY 88
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
 29-97 1.51e-05

forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438735 [Multi-domain]  Cd Length: 96  Bit Score: 43.25  E-value: 1.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQV--LHARLRHHDQVRMGQTQILF 97
Cdd:cd22683    24 TIGRSRSCDLVLSDPSISRFHAELRLEQNGINVIDNNSANGTFINGKRIkgKTYILKNGDIIVFGKCSFLI 94
FHA_OdhI-like cd22721
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate ...
 29-97 1.72e-05

forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI) and similar proteins; OdhI is an essential component of the PknG signaling pathway. It regulates glutamate production under biotin non-limiting conditions. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438773 [Multi-domain]  Cd Length: 102  Bit Score: 43.54  E-value: 1.72e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHARLRHHDQVRMGQTQILF 97
Cdd:cd22721    32 TAGRHPESDIFLDDVTVSRRHAEFRINEGEFEVVDVGSLNGTYVNREPRNAQVMQTGDEIQIGKFRLVF 100
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
 20-74 3.30e-05

forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438731 [Multi-domain]  Cd Length: 126  Bit Score: 43.03  E-value: 3.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2258821257  20 RTVEIGQFASIGRS------ADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNG 74
Cdd:cd22679    18 RHIVLDEPVKIGRSvararpAANNAIFDCKVLSRNHALLWYDDGKFYLQDTKSSNGTFVNN 78
FHA_EmbR-like cd22669
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ...
 29-97 3.48e-05

forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438721 [Multi-domain]  Cd Length: 89  Bit Score: 42.02  E-value: 3.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHAR-LRHHDQVRMGQTQILF 97
Cdd:cd22669    19 RIGRLHDNDIVLDSANVSRHHAVIVDTGTNYVINDLRSSNGVHVQHERIRSAVtLNDGDHIRICDHEFTF 88
FHA_Cep170 cd22704
forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) ...
 30-97 2.42e-04

forkhead associated (FHA) domain found in the centrosomal protein of 170 kDa protein (Cep170) family; The Cep170 family includes Cep170 and Cep170B. Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). Cep170B, also called centrosomal protein 170B, plays a role in microtubule organization. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438756 [Multi-domain]  Cd Length: 102  Bit Score: 40.00  E-value: 2.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2258821257  30 IGRSaDNTLVIQDDFASGRHArVLN---KEGQFFIQDLGSRNGTYVNGAQV---LHARLRHHDQVRMGQTQILF 97
Cdd:cd22704    21 VGRE-DCDLILQSRSVDKQHA-VITydqIDNEFKIKDLGSLNGTFVNDSRIpeqTYITLKLGDSIRFGYDTNVY 92
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
 29-91 2.67e-04

forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438715 [Multi-domain]  Cd Length: 110  Bit Score: 40.03  E-value: 2.67e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  29 SIGRSADNTLVIQDD---FASGRHARV-LNKEGQFFIQDLGSRNGTYVNGAQV--LHARLRHH-DQVRMG 91
Cdd:cd22663    24 TVGRGLGVTYQLVSTcplMISRNHCVLkKNDEGQWTIKDNKSLNGVWVNGERIepLKPYPLNEgDLIQLG 93
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
 27-97 3.18e-04

forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438729 [Multi-domain]  Cd Length: 106  Bit Score: 39.85  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  27 FASIGRSADNTLVIQDDFASGRHA------RVLNKEGQFFIQDLGSRNGTYVNGAQV---LHARLRHHDQVRMGQTQILF 97
Cdd:cd22677    23 FYVFGRLPGCDVVLEHPSISRYHAvlqyrgDADDHDGGFYLYDLGSTHGTFLNKQRIppkQYYRLRVGHVLKFGGSTRLY 102
FHA_FKH1-like cd22701
forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 ...
 19-98 5.88e-04

forkhead associated (FHA) domain found in Saccharomyces cerevisiae fork head protein homolog 1 (FKH1), 2 (FKH2) and similar proteins; This family includes FKH1 and FKH2, as well as pre-rRNA-processing protein FHL1. FKH1 and FKH2 are forkhead transcription factors that regulate the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20, as well as SWI5 and ACE2. FKH1 and FKH2 are involved in HMRa silencing. They associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. They also function in controlling yeast cell morphology by preventing pseudohyphal growth and act as rate-limiting replication origin activators via their interaction with the origin recognition complex (ORC). FHL1 is a forkhead protein that controls the pre-rRNA processing machinery in conjunction with IFH1. It might act as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator. This family also includes AtFHA1 and AtFHA2, which may play a role in the control of plant organ development. AtFHA2 is specifically involved in the regulation of stamen development. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438753 [Multi-domain]  Cd Length: 106  Bit Score: 39.14  E-value: 5.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  19 VRTVEIgqfaSIGRSADNTLVIQD-----DFA-----SGRHARV-LNKE-GQFFIQDLGsRNGTYVNGAQVL----HARL 82
Cdd:cd22701    14 VQKLEV----VLGRNSKNSSSTAAdsvdiDLGpskkiSRRHARIfYDFTtQCFELSVLG-RNGVKVDGILVKpgspPVPL 88

                          90
                  ....*....|....*.
gi 2258821257  83 RHHDQVRMGQTQILFS 98
Cdd:cd22701    89 RSGSLIQIGGVLFYFL 104
FHA_SNIP1_DDL-like cd22676
forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA ...
 39-91 1.14e-03

forkhead associated (FHA) domain found in Smad nuclear-interacting protein 1 (SNIP1), FHA domain-containing protein DDL, and similar proteins; SNIP1 is an FHA domain-containing protein required for pre-mRNA splicing as a component of the spliceosome. It inhibits NF-kappaB signaling by competing for its binding to the C/H1 domain of CBP/p300 transcriptional co-activators. It is involved in microRNA (miRNA) biogenesis. SNIP1 is a regulator of the cell cycle and cyclin D1 expression and may be involved in cyclin-D1/CCND1 mRNA stability through the SNARP complex which associates with both the 3'end of the CCND1 gene and its mRNA. This family also includes Arabidopsis thaliana FHA domain-containing protein DDL and similar proteins. DDL, also called protein DAWDLE, is involved in the microRNA (miRNA) and short interfering RNA (siRNA) biogenesis. It may facilitate DCL1 to access or recognize primary miRNAs. DDL binds RNA non-specifically. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438728 [Multi-domain]  Cd Length: 111  Bit Score: 38.43  E-value: 1.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2258821257  39 VIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHAR---LRHHDQVRMG 91
Cdd:cd22676    47 VIQFREVEKRNEGDVIENIRPYIIDLGSTNGTFLNGEKIEPRRyyeLREKDVLKFG 102
BREX_3_BrxF NF033453
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ...
 134-176 1.25e-03

BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.


Pssm-ID: 468038  Cd Length: 149  Bit Score: 39.01  E-value: 1.25e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2258821257 134 VLISGPSGSGKEVVaqtLHKLSQRSSGPLININcSALSESLVE 176
Cdd:NF033453   19 ILLVGPPGSGKTAL---LRELAAKRGAPVINVN-LELSRRLLE 57
FHA_DMA-like cd22692
forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest ...
 21-91 1.67e-03

forkhead associated (FHA) domain found in Saccharomyces cerevisiae defective in mitotic arrest protein 1 (DMA1), 2 (DMA2) and similar proteins; DMA1 (also known as checkpoint forkhead associated with RING domains-containing protein 1, or CHF1) and DMA2 (also known as checkpoint forkhead associated with RING domains-containing protein 2, or CHF2) are E3 ubiquitin-protein ligases which function in cell cycle retarding in conjunction with the UBC4 and UBC13/MMS2 complex, two E2 ubiquitin conjugating enzymes. They are involved in nutritional control of the cell cycle and required for proper spindle positioning, likely regulating septin ring deposition at the bud neck. DMA1 targets the degradation of G1 cyclin PCL1. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438744 [Multi-domain]  Cd Length: 139  Bit Score: 38.70  E-value: 1.67e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2258821257  21 TVEIGQFASIGRSAD-NTLVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHA-------RLRHHDQVRMG 91
Cdd:cd22692    38 QIHIGRYTERVRQAIyHPVVFKSKVVSRTHGCIKVDEGNWYIKDVKSSSGTFLNHQRLSPAsrtskpyPLRDGDILQLG 116
PLN02927 PLN02927
antheraxanthin epoxidase/zeaxanthin epoxidase
 14-94 1.78e-03

antheraxanthin epoxidase/zeaxanthin epoxidase


Pssm-ID: 178515 [Multi-domain]  Cd Length: 668  Bit Score: 40.46  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  14 VSEKTVRTVEIGQFASIGRSADNT-----LVIQDDFASGRHARVLNKEGQFFIQDLGSRNGTYVNGAQ--------VLHA 80
Cdd:PLN02927  545 VSETLCLTKDEDQPCIVGSEPDQDfpgmrIVIPSSQVSKMHARVIYKDGAFFLMDLRSEHGTYVTDNEgrryratpNFPA 624

                          90
                  ....*....|....
gi 2258821257  81 RLRHHDQVRMGQTQ 94
Cdd:PLN02927  625 RFRSSDIIEFGSDK 638
FHA_Cep170A cd22724
forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar ...
 30-106 1.93e-03

forkhead associated (FHA) domain found in centrosomal protein of 170 kDa (Cep170) and similar proteins; Cep170, also called Cep170A, KARP-1-binding protein, or KARP1-binding protein, is a protein that localizes to centrosomes as well as spindle microtubules and plays a role in microtubule organization and microtubule assembly. It is required for centriole subdistal appendage assembly. Cep170 is phosphorylated during M phase and interacts with Polo-like kinase 1 (Plk1). The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438776 [Multi-domain]  Cd Length: 106  Bit Score: 37.64  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  30 IGRSaDNTLVIQDDFASGRHArVLNKEG---QFFIQDLGSRNGTYVNGAQVL---HARLRHHDQVRMGQTQILFSQRLGD 103
Cdd:cd22724    25 VGRD-DCELMLQSRSVDKQHA-VINYDAstdEHKVKDLGSLNGTFVNDVRIPeqtYITLKLDDKLRFGYDTNLFTVVRGE 102


                  ...
gi 2258821257 104 LEL 106
Cdd:cd22724   103 MRV 105
FHA_KIF28P cd22709
forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; ...
 30-91 2.07e-03

forkhead associated (FHA) domain found in kinesin-like protein KIF28P and similar proteins; KIF28P, also called kinesin-like protein 6 (KLP6), is a microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells. The FHA domain is a small phosphopeptide recognition module, but this group may lack the conserved residues that are required for binding phosphothreonine.


Pssm-ID: 438761 [Multi-domain]  Cd Length: 102  Bit Score: 37.58  E-value: 2.07e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2258821257  30 IGRSADNtlVIQDDFASG-----RHARVLNKEGQFFIQDLGSRNGTYVNGAQVLHAR-LRHHDQVRMG 91
Cdd:cd22709    27 IGRADAE--PEPDIVLSGlsiqkQHAVITNTDGKVTIEPVSPGAKVIVNGVPVTGETeLHHLDRVILG 92
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 29-98 4.05e-03

forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 36.92  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2258821257  29 SIGRSADNTLVIQDDFASGRHARV--------LNKEGQ---FFIQDLgSRNGTYVNGAQVLH---ARLRHHDQVRMGQTQ 94
Cdd:cd22667    23 TVGRKDCDIIIVDDSSISRKHATLtvlhpeanLSDPDTrpeLTLKDL-SKYGTFVNGEKLKGgseVTLKDGDVITFGVLG 101


                  ....
gi 2258821257  95 ILFS 98
Cdd:cd22667   102 SKFR 105
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 127-187 5.32e-03

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 37.76  E-value: 5.32e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2258821257 127 IAQSHLPVLISGPSGSGKEVVAQT-LHKLSQRSSGPLiNINCSALSES-----LVESELFGHTKGSF 187
Cdd:pfam12775  27 LLKNGKPVLLVGPTGTGKTVIIQNlLRKLDKEKYLPL-FINFSAQTTSnqtqdIIESKLEKRRKGVY 92
 
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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