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Conserved domains on  [gi|32474688|ref|NP_867682|]
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regulatory protein [Rhodopirellula baltica SH 1]

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List of domain hits

Name Accession Description Interval E-value
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
18-111 6.42e-19

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


:

Pssm-ID: 238017  Cd Length: 102  Bit Score: 82.82  E-value: 6.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688  18 MAHLTSSIDGNPSGTFQLDRD-EMQVGRHPDC-DIVVDAGAVSRYHAKITKKG-NEFAVEDAGSRNGTFVNGQLLSR--P 92
Cdd:cd00060   1 VPRLVVLSGDASGRRYYLDPGgTYTIGRDSDNcDIVLDDPSVSRRHAVIRYDGdGGVVLIDLGSTNGTFVNGQRVSPgeP 80
                        90
                ....*....|....*....
gi 32474688  93 HVLSEGDRIRISEVVLVFH 111
Cdd:cd00060  81 VRLRDGDVIRLGNTSISFR 99
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
387-586 9.06e-44

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


:

Pssm-ID: 254114  Cd Length: 192  Bit Score: 155.14  E-value: 9.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   387 PDGRLAVVVADVVGHGVAAAMYMAKLSAETRFCLASEPDLARAVERLNDRMSA-LEVQRFVTYLLVVIDPQSNELKIVNA 465
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRnLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   466 GHMPPIVRDAVSGQISEpgDEDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEALNAKEEEWGTDPLRQIVLKAVP 545
Cdd:pfam07228  81 GHPPPLLLRPDGGVVEL--LESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 32474688   546 skeddEPLAKVVKNeiVRQAFEHMGGAVQFDDMCMVIIERT 586
Cdd:pfam07228 159 -----LSPEELLDA--LLEDLLRLGGGELEDDITLLVLRVR 192
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
187-332 1.07e-12

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


:

Pssm-ID: 214500  Cd Length: 149  Bit Score: 65.87  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688    187 VDDVLPKVLSSLFQIFPsADRGFVVM--ETPDGALVPRWVQLRNKTDDTETIRISRTIIRQTMETGHTILSLDAMDDSRF 264
Cdd:smart00065   2 LEELLQTILEELRQLLG-ADRVLIYLvdENDRGELVLVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32474688    265 DSSESIADFSIRSMMCAPLHDeDGKAIGALQIDSTQGRGQFRDEDIDLLTGIAAQASVVINNARMHEQ 332
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
239-585 4.49e-47

Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / Transcription]


:

Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 170.28  E-value: 4.49e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 239 SRTIIRQTMETGHTILSLDAMDDSRFDSSESIADFSIRSMMCAPLHDEDGKAIGALQIDSTQGRGQFRDEDIdlltGIAA 318
Cdd:COG2208  28 GLYAQISAEPLTEMFFLQTEKGLRQAELLYEINDILERFLPVEVLLGVSGKLRALSEEIKHWRGGLPLVAEL----LVEI 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 319 QASVVINNARMHEQALRQQEVEQDLKLATEVQRAFLPAEAPQVPTYHLESFYQAANHIGGDYFDYVDLPDGRLAVVVADV 398
Cdd:COG2208 104 NRAVGLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVPASEVGGDYYDFIQLGEKRLRIGIGDV 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 399 VGHGVAAAMYMAK-LSAETRFCLASEPDLARAVERLNDRMSA-LEVQRFVTYLLVVIDPQSNELKIVNAGHMPPIVRDav 476
Cdd:COG2208 184 SGKGVPAALLMLMpKLALRLLLESGPLDPADVLETLNRVLKQnLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILS-- 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 477 SGQISEPGD-EDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEALNAKEEEWGTDPLRQIVLKAVPSKEDDeplak 555
Cdd:COG2208 262 ADGEIEVEDlTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERLLKILGRLLGQPAEE----- 336
                       330       340       350
                ....*....|....*....|....*....|
gi 32474688 556 vVKNEIVRQAFEHMGGAVQFDDMCMVIIER 585
Cdd:COG2208 337 -ILEAILESLEELQGDQIQDDDITLLVLKV 365
COG1716 COG1716
FOG: FHA domain [Signal transduction mechanisms]
42-130 6.78e-17

FOG: FHA domain [Signal transduction mechanisms]


:

Pssm-ID: 224630 [Multi-domain]  Cd Length: 191  Bit Score: 79.23  E-value: 6.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688  42 VGRHPDCDIVVDAGAVSRYHAKITKKGNEFAVEDAGSRNGTFVNGQLLSRPHVLSEGDRIRISEVVLVFHGdevPGFASG 121
Cdd:COG1716  93 IGRDPDNDIVLDDDVVSRRHAELRREGNEVFLEDLGSTNGTYVNGEKVRQRVLLQDGDVIRLGGTLAERLR---IILTEL 169

                ....*....
gi 32474688 122 GGSGEMTFD 130
Cdd:COG1716 170 EIDGVDPVA 178
 
Name Accession Description Interval E-value
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
18-111 6.42e-19

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017  Cd Length: 102  Bit Score: 82.82  E-value: 6.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688  18 MAHLTSSIDGNPSGTFQLDRD-EMQVGRHPDC-DIVVDAGAVSRYHAKITKKG-NEFAVEDAGSRNGTFVNGQLLSR--P 92
Cdd:cd00060   1 VPRLVVLSGDASGRRYYLDPGgTYTIGRDSDNcDIVLDDPSVSRRHAVIRYDGdGGVVLIDLGSTNGTFVNGQRVSPgeP 80
                        90
                ....*....|....*....
gi 32474688  93 HVLSEGDRIRISEVVLVFH 111
Cdd:cd00060  81 VRLRDGDVIRLGNTSISFR 99
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
387-586 9.06e-44

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 254114  Cd Length: 192  Bit Score: 155.14  E-value: 9.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   387 PDGRLAVVVADVVGHGVAAAMYMAKLSAETRFCLASEPDLARAVERLNDRMSA-LEVQRFVTYLLVVIDPQSNELKIVNA 465
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRnLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   466 GHMPPIVRDAVSGQISEpgDEDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEALNAKEEEWGTDPLRQIVLKAVP 545
Cdd:pfam07228  81 GHPPPLLLRPDGGVVEL--LESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 32474688   546 skeddEPLAKVVKNeiVRQAFEHMGGAVQFDDMCMVIIERT 586
Cdd:pfam07228 159 -----LSPEELLDA--LLEDLLRLGGGELEDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
369-567 1.08e-31

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 121.69  E-value: 1.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688    369 FYQAANHIGGDYFDYVDLPDGRLAVVVADVVGHGVAAAMYMAKLSAETRFCLASEPDLARAVERLNDRMSALEVQ-RFVT 447
Cdd:smart00331   9 YYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGEDgMFAT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688    448 YLLVVIDPQSNELKIVNAGHMPPIVRDAVSGQISEPgdEDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEALNAk 527
Cdd:smart00331  89 LFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDL--DDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEARNP- 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 32474688    528 eeEWGTDPLRQIVlkavpskeDDEPLAKVvkNEIVRQAFE 567
Cdd:smart00331 166 --ERLEELLEELL--------GSPPAEIA--QRILEELLE 193
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
42-104 1.35e-20

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


Pssm-ID: 249907  Cd Length: 67  Bit Score: 86.49  E-value: 1.35e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32474688    42 VGRHPDCDIVVDAGAVSRYHAKITKKGN-EFAVEDAGSRNGTFVNGQLLSR-PHVLSEGDRIRIS 104
Cdd:pfam00498   3 IGRSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGSTNGTFVNGQRLGPgPVRLRDGDVIRLG 67
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
187-332 1.07e-12

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


Pssm-ID: 214500  Cd Length: 149  Bit Score: 65.87  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688    187 VDDVLPKVLSSLFQIFPsADRGFVVM--ETPDGALVPRWVQLRNKTDDTETIRISRTIIRQTMETGHTILSLDAMDDSRF 264
Cdd:smart00065   2 LEELLQTILEELRQLLG-ADRVLIYLvdENDRGELVLVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32474688    265 DSSESIADFSIRSMMCAPLHDeDGKAIGALQIDSTQGRGQFRDEDIDLLTGIAAQASVVINNARMHEQ 332
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
186-324 1.31e-12

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


Pssm-ID: 250726  Cd Length: 146  Bit Score: 65.68  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   186 SVDDVLPKVLSSLFQIFPsADRGFVVMETPDGALVPRWVQLRNKTDDTETIRISR--TIIRQTMETGHTILSLDAMDDSR 263
Cdd:pfam01590   1 DLEELLQTILEELRELLG-ADRVAIYLADADGLLLYLVAGDGLSDIPLAARGLPLggGVVGEVIAGGNPIVVPDVQDDPR 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32474688   264 F--------DSSESIADFSIRSMMCAPLHDEdGKAIGALQIDSTQGRgQFRDEDIDLLTGIAAQASVVI 324
Cdd:pfam01590  80 FrdltalasDLPHFLRGLGIRSCLAVPLKGG-GELIGVLVLHSTSPR-AFTEEELELLQALADQVAIAL 146
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
171-338 7.77e-11

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 60.76  E-value: 7.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 171 LAALIAINSNLTGAISVDDVLPKVLSSLFQIFPsADRGFVVMETPDGALVPRWVQLRNKTDDTETIRISRTI-------I 243
Cdd:COG2203   3 EALLNELAAKIAQDLDLEEILQAALELLAELLG-ADRGLIYLLDEDGLLDGALVAEAAEAGLEQLIDELFGLvilpaclI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 244 RQTMETGHTILSLDAMDDSRFDSSESIADFS-IRSMMCAPLHDeDGKAIGALQIDSTQGRGQFRDEDIDLLTGIAAQASV 322
Cdd:COG2203  82 GIALREGRPVVVEDILQDPRFRDNPLVLLEPpIRSYLGVPLIA-QGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAI 160
                       170
                ....*....|....*.
gi 32474688 323 VINNARMhEQALRQQE 338
Cdd:COG2203 161 AIERARL-YEELQEAE 175
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
42-89 1.67e-10

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


Pssm-ID: 214578  Cd Length: 52  Bit Score: 57.57  E-value: 1.67e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 32474688     42 VGRHP-DCDIVVDAGAVSRYHAKITKK-GNEFAVEDAGSRNGTFVNGQLL 89
Cdd:smart00240   3 IGRSSeDCDIQLDGPSISRRHAVIVYDgGGRFYLIDLGSTNGTFVNGKRI 52
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
239-585 4.49e-47

Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / Transcription]


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 170.28  E-value: 4.49e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 239 SRTIIRQTMETGHTILSLDAMDDSRFDSSESIADFSIRSMMCAPLHDEDGKAIGALQIDSTQGRGQFRDEDIdlltGIAA 318
Cdd:COG2208  28 GLYAQISAEPLTEMFFLQTEKGLRQAELLYEINDILERFLPVEVLLGVSGKLRALSEEIKHWRGGLPLVAEL----LVEI 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 319 QASVVINNARMHEQALRQQEVEQDLKLATEVQRAFLPAEAPQVPTYHLESFYQAANHIGGDYFDYVDLPDGRLAVVVADV 398
Cdd:COG2208 104 NRAVGLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVPASEVGGDYYDFIQLGEKRLRIGIGDV 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 399 VGHGVAAAMYMAK-LSAETRFCLASEPDLARAVERLNDRMSA-LEVQRFVTYLLVVIDPQSNELKIVNAGHMPPIVRDav 476
Cdd:COG2208 184 SGKGVPAALLMLMpKLALRLLLESGPLDPADVLETLNRVLKQnLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILS-- 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 477 SGQISEPGD-EDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEALNAKEEEWGTDPLRQIVLKAVPSKEDDeplak 555
Cdd:COG2208 262 ADGEIEVEDlTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERLLKILGRLLGQPAEE----- 336
                       330       340       350
                ....*....|....*....|....*....|
gi 32474688 556 vVKNEIVRQAFEHMGGAVQFDDMCMVIIER 585
Cdd:COG2208 337 -ILEAILESLEELQGDQIQDDDITLLVLKV 365
COG1716 COG1716
FOG: FHA domain [Signal transduction mechanisms]
42-130 6.78e-17

FOG: FHA domain [Signal transduction mechanisms]


Pssm-ID: 224630 [Multi-domain]  Cd Length: 191  Bit Score: 79.23  E-value: 6.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688  42 VGRHPDCDIVVDAGAVSRYHAKITKKGNEFAVEDAGSRNGTFVNGQLLSRPHVLSEGDRIRISEVVLVFHGdevPGFASG 121
Cdd:COG1716  93 IGRDPDNDIVLDDDVVSRRHAELRREGNEVFLEDLGSTNGTYVNGEKVRQRVLLQDGDVIRLGGTLAERLR---IILTEL 169

                ....*....
gi 32474688 122 GGSGEMTFD 130
Cdd:COG1716 170 EIDGVDPVA 178
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
26-108 7.81e-11

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis].


Pssm-ID: 234178 [Multi-domain]  Cd Length: 396  Bit Score: 63.16  E-value: 7.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688    26 DGNPSGTFQLDRDEMQVGRHPDCDIVVD--AGAVSRYHAKITKKGNEFAVEDAgSRNGTFVNGQL--LSR--PHVLSEGD 99
Cdd:TIGR03354  12 TPGIAAQKTFGTNGGTIGRSEDCDWVLPdpERHVSGRHARIRYRDGAYLLTDL-STNGVFLNGSGspLGRgnPVRLEQGD 90

                  ....*....
gi 32474688   100 RIRISEVVL 108
Cdd:TIGR03354  91 RLRLGDYEI 99
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
313-582 1.69e-09

stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane spanning protein with two separable functions. It plays a role in the switch to polar cell division during sporulation. By means of it protein phosphatase activity, located in the C-terminal region, it activates sigma-F. All proteins that score above the trusted cutoff to this model are found in endospore-forming Gram-positive bacteria. Surprisingly, a sequence from the Cyanobacterium-like (and presumably non-spore-forming) photosynthesizer Heliobacillus mobilis is homologous, and scores between the trusted and noise cutoffs [Cellular processes, Sporulation and germination].


Pssm-ID: 234038 [Multi-domain]  Cd Length: 764  Bit Score: 59.32  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   313 LTGIAAQASVVINNARMHEQALRQQE-VEQDLKLATEVqrAFLPAEAPQVPTyHLESFYQAANHIGGDYFDYVDLPDGRL 391
Cdd:TIGR02865 505 GRGECEKKIAPIISEVTGELMCVKDErCSIDPKGRCHL--TFEETPKYHVST-GVARAAKDGELVSGDSYSFGKLSAGKY 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   392 AVVVADVVGHGV-AAAMYMAKLSAETRFcLASEPDLARAVERLNDRMSALEVQ-RFVTYLLVVIDPQSNELKIVNAGHMP 469
Cdd:TIGR02865 582 AVAISDGMGSGPeAAQESSACVRLLEKF-LESGFDREVAIKTVNSILSLRSTDeKFSTLDLSVIDLYTGQAEFVKVGAVP 660
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   470 PIV-RDAVSGQIsepgdEDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEAlnAKEEEWGTDPLRQIVlkavpsKE 548
Cdd:TIGR02865 661 SFIkRGAKVEVI-----RSSNLPIGILDEVDVELVRKKLKNGDLIVMVSDGVLEG--EKEVEGKVLWLVRKL------KE 727
                         250       260       270
                  ....*....|....*....|....*....|....
gi 32474688   549 DDEPLAKVVKNEIVRQAFEHMGGAVQfDDMCMVI 582
Cdd:TIGR02865 728 TNTNDPEEIAEYLLEKAKELRSGKIK-DDMTVIV 760
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
168-351 1.93e-03

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: 233584 [Multi-domain]  Cd Length: 534  Bit Score: 39.70  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   168 EAKLAALIAINSNLTGAISVDDVLPKVLSSLFQIFPSAdRGFVVMETPDG-ALVPRWVQLRNKTDDTETIRISRTIIRQT 246
Cdd:TIGR01817   1 DLQLAALYEISKILSAPTRLEKTLANVLNVLSNDLGMR-HGLITLSDSEGePLLVAAIGWSEEGFAPIRYRVGEGAIGQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   247 METGHTILSLDAMDDSRFDSSESIADFSIRSMMCAPLHdEDGKAIGALQIDSTQGRGQFRDEDIDLLTGIAAQASVVINN 326
Cdd:TIGR01817  80 VATGNSLVVPDVAAEPLFLDRLSLYDPGPVPFIGVPIK-ADSETIGVLAADRDFRSRERLEEEVRFLEMVANLIGQTVRL 158
                         170       180
                  ....*....|....*....|....*
gi 32474688   327 ARmHEQALRQQEVEQDLKLATEVQR 351
Cdd:TIGR01817 159 HR-LVAQRRERLIAEAVQLSKQLRD 182
PRK05022 PRK05022
anaerobic nitric oxide reductase transcription regulator; Provisional
279-357 2.75e-03

anaerobic nitric oxide reductase transcription regulator; Provisional


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 39.38  E-value: 2.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32474688  279 MCAPLHDeDGKAIGALQIDSTQGrGQFRDEDIDLLTGIAAQASVVINNARMHEQaLRQQEVEQDLKLATEVQRAFLPAE 357
Cdd:PRK05022 113 MGLPLFV-DGRLIGALTLDALDP-GQFDAFSDEELRALAALAAATLRNALLIEQ-LESQAELPQDVAEFLRQEALKEGE 188
 
Name Accession Description Interval E-value
FHA cd00060
Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative ...
18-111 6.42e-19

Forkhead associated domain (FHA); found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain. FHA domains may bind phosphothreonine, phosphoserine and sometimes phosphotyrosine. In eukaryotes, many FHA domain-containing proteins localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. Members of the FHA family include: Dun1, Rad53, Cds1, Mek1, KAPP(kinase-associated protein phosphatase),and Ki-67 (a human nuclear protein related to cell proliferation).


Pssm-ID: 238017  Cd Length: 102  Bit Score: 82.82  E-value: 6.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688  18 MAHLTSSIDGNPSGTFQLDRD-EMQVGRHPDC-DIVVDAGAVSRYHAKITKKG-NEFAVEDAGSRNGTFVNGQLLSR--P 92
Cdd:cd00060   1 VPRLVVLSGDASGRRYYLDPGgTYTIGRDSDNcDIVLDDPSVSRRHAVIRYDGdGGVVLIDLGSTNGTFVNGQRVSPgeP 80
                        90
                ....*....|....*....
gi 32474688  93 HVLSEGDRIRISEVVLVFH 111
Cdd:cd00060  81 VRLRDGDVIRLGNTSISFR 99
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
387-586 9.06e-44

Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II sporulation E proteins (EC:3.1.3.16). These are required for formation of a normal polar septum during sporulation. The N-terminal region is hydrophobic and is expected to contain up to 12 membrane-spanning segments.


Pssm-ID: 254114  Cd Length: 192  Bit Score: 155.14  E-value: 9.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   387 PDGRLAVVVADVVGHGVAAAMYMAKLSAETRFCLASEPDLARAVERLNDRMSA-LEVQRFVTYLLVVIDPQSNELKIVNA 465
Cdd:pfam07228   1 PDGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRnLEGERFATAVLAVYDPETGTLEYANA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   466 GHMPPIVRDAVSGQISEpgDEDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEALNAKEEEWGTDPLRQIVLKAVP 545
Cdd:pfam07228  81 GHPPPLLLRPDGGVVEL--LESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELFGLERLLALLAERHG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 32474688   546 skeddEPLAKVVKNeiVRQAFEHMGGAVQFDDMCMVIIERT 586
Cdd:pfam07228 159 -----LSPEELLDA--LLEDLLRLGGGELEDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
369-567 1.08e-31

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 121.69  E-value: 1.08e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688    369 FYQAANHIGGDYFDYVDLPDGRLAVVVADVVGHGVAAAMYMAKLSAETRFCLASEPDLARAVERLNDRMSALEVQ-RFVT 447
Cdd:smart00331   9 YYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGEDgMFAT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688    448 YLLVVIDPQSNELKIVNAGHMPPIVRDAVSGQISEPgdEDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEALNAk 527
Cdd:smart00331  89 LFLALYDFAGGTLSYANAGHSPPYLLRADGGLVEDL--DDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEARNP- 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 32474688    528 eeEWGTDPLRQIVlkavpskeDDEPLAKVvkNEIVRQAFE 567
Cdd:smart00331 166 --ERLEELLEELL--------GSPPAEIA--QRILEELLE 193
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
42-104 1.35e-20

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


Pssm-ID: 249907  Cd Length: 67  Bit Score: 86.49  E-value: 1.35e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32474688    42 VGRHPDCDIVVDAGAVSRYHAKITKKGN-EFAVEDAGSRNGTFVNGQLLSR-PHVLSEGDRIRIS 104
Cdd:pfam00498   3 IGRSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGSTNGTFVNGQRLGPgPVRLRDGDVIRLG 67
GAF smart00065
Domain present in phytochromes and cGMP-specific phosphodiesterases; Mutations within these ...
187-332 1.07e-12

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


Pssm-ID: 214500  Cd Length: 149  Bit Score: 65.87  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688    187 VDDVLPKVLSSLFQIFPsADRGFVVM--ETPDGALVPRWVQLRNKTDDTETIRISRTIIRQTMETGHTILSLDAMDDSRF 264
Cdd:smart00065   2 LEELLQTILEELRQLLG-ADRVLIYLvdENDRGELVLVAADGLTLPTLGIRFPLDEGLAGRVAETGRPLNIPDVEADPLF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32474688    265 DSSESIADFSIRSMMCAPLHDeDGKAIGALQIDSTQGRGQFRDEDIDLLTGIAAQASVVINNARMHEQ 332
Cdd:smart00065  81 AEDLLGRYQGVRSFLAVPLVA-DGELVGVLALHNKKSPRPFTEEDEELLQALANQLAIALANAQLYEE 147
GAF pfam01590
GAF domain; This domain is present in cGMP-specific phosphodiesterases, adenylyl and guanylyl ...
186-324 1.31e-12

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


Pssm-ID: 250726  Cd Length: 146  Bit Score: 65.68  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   186 SVDDVLPKVLSSLFQIFPsADRGFVVMETPDGALVPRWVQLRNKTDDTETIRISR--TIIRQTMETGHTILSLDAMDDSR 263
Cdd:pfam01590   1 DLEELLQTILEELRELLG-ADRVAIYLADADGLLLYLVAGDGLSDIPLAARGLPLggGVVGEVIAGGNPIVVPDVQDDPR 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32474688   264 F--------DSSESIADFSIRSMMCAPLHDEdGKAIGALQIDSTQGRgQFRDEDIDLLTGIAAQASVVI 324
Cdd:pfam01590  80 FrdltalasDLPHFLRGLGIRSCLAVPLKGG-GELIGVLVLHSTSPR-AFTEEELELLQALADQVAIAL 146
FhlA COG2203
FOG: GAF domain [Signal transduction mechanisms]
171-338 7.77e-11

FOG: GAF domain [Signal transduction mechanisms]


Pssm-ID: 225113  Cd Length: 175  Bit Score: 60.76  E-value: 7.77e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 171 LAALIAINSNLTGAISVDDVLPKVLSSLFQIFPsADRGFVVMETPDGALVPRWVQLRNKTDDTETIRISRTI-------I 243
Cdd:COG2203   3 EALLNELAAKIAQDLDLEEILQAALELLAELLG-ADRGLIYLLDEDGLLDGALVAEAAEAGLEQLIDELFGLvilpaclI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 244 RQTMETGHTILSLDAMDDSRFDSSESIADFS-IRSMMCAPLHDeDGKAIGALQIDSTQGRGQFRDEDIDLLTGIAAQASV 322
Cdd:COG2203  82 GIALREGRPVVVEDILQDPRFRDNPLVLLEPpIRSYLGVPLIA-QGELLGLLCVHDSEPRRQWSEEELELLEELAEQVAI 160
                       170
                ....*....|....*.
gi 32474688 323 VINNARMhEQALRQQE 338
Cdd:COG2203 161 AIERARL-YEELQEAE 175
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
42-89 1.67e-10

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


Pssm-ID: 214578  Cd Length: 52  Bit Score: 57.57  E-value: 1.67e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 32474688     42 VGRHP-DCDIVVDAGAVSRYHAKITKK-GNEFAVEDAGSRNGTFVNGQLL 89
Cdd:smart00240   3 IGRSSeDCDIQLDGPSISRRHAVIVYDgGGRFYLIDLGSTNGTFVNGKRI 52
GAF_3 pfam13492
GAF domain;
186-326 2.00e-09

GAF domain;


Pssm-ID: 257816  Cd Length: 129  Bit Score: 55.91  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   186 SVDDVLPKVLSSLFQIFPsADRGFVVMETPDGALVPRWVQLRNKTDDTETIRISRTIIRQTMETGHTILSLDAMDDSRFD 265
Cdd:pfam13492   1 DPDELLERALELLAELLG-ADRAALYLLDEDGLELRLVAGSGGEPRLSESLPEDSPLAQRALEKGEPVSVPAGDNRDLLP 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32474688   266 SsesiadfsiRSMMCAPLHDEdGKAIGALQIDSTQGRgQFRDEDIDLLTGIAAQASVVINN 326
Cdd:pfam13492  80 S---------ESLLAVPLRAG-GEVIGVLVLESTPEE-AFTPEDLELLELLASQIAIALEN 129
GAF_2 pfam13185
GAF domain;
184-324 8.82e-09

GAF domain;


Pssm-ID: 257553  Cd Length: 150  Bit Score: 54.14  E-value: 8.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   184 AISVDDVLPKVLSSLFQIFPSaDRGFVVMETPDGALVP-----------RWVQLRNKTDDTETIRISRTIIRQTMETGHT 252
Cdd:pfam13185   1 ALSLEELLEAILEALLELTGS-EAGFIGLLDEDGTLLLlaasggteellRELAALSGELGGPPAAGAVGLGEGALRTGKP 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32474688   253 ILSLDAMDDSRFDSSESIADFSIRSMMCAPLHDeDGKAIGALQIDSTQGRGqFRDEDIDLLTGIAAQASVVI 324
Cdd:pfam13185  80 VIINDVASDPSGAGGLPAGHEGLRSFLSVPLIS-GGRVIGVLALGSKEPGA-FDEEDLELLELLAEQIAIAI 149
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
239-585 4.49e-47

Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / Transcription]


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 170.28  E-value: 4.49e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 239 SRTIIRQTMETGHTILSLDAMDDSRFDSSESIADFSIRSMMCAPLHDEDGKAIGALQIDSTQGRGQFRDEDIdlltGIAA 318
Cdd:COG2208  28 GLYAQISAEPLTEMFFLQTEKGLRQAELLYEINDILERFLPVEVLLGVSGKLRALSEEIKHWRGGLPLVAEL----LVEI 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 319 QASVVINNARMHEQALRQQEVEQDLKLATEVQRAFLPAEAPQVPTYHLESFYQAANHIGGDYFDYVDLPDGRLAVVVADV 398
Cdd:COG2208 104 NRAVGLVSAHNELLLLEQNNISAELEVARQIQQNLLPKALPLFPGIDIEAILVPASEVGGDYYDFIQLGEKRLRIGIGDV 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 399 VGHGVAAAMYMAK-LSAETRFCLASEPDLARAVERLNDRMSA-LEVQRFVTYLLVVIDPQSNELKIVNAGHMPPIVRDav 476
Cdd:COG2208 184 SGKGVPAALLMLMpKLALRLLLESGPLDPADVLETLNRVLKQnLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILS-- 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 477 SGQISEPGD-EDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEALNAKEEEWGTDPLRQIVLKAVPSKEDDeplak 555
Cdd:COG2208 262 ADGEIEVEDlTALGLPIGLLPDYQYEVASLQLEPGDLLVLYTDGVTEARNSDGEFFGLERLLKILGRLLGQPAEE----- 336
                       330       340       350
                ....*....|....*....|....*....|
gi 32474688 556 vVKNEIVRQAFEHMGGAVQFDDMCMVIIER 585
Cdd:COG2208 337 -ILEAILESLEELQGDQIQDDDITLLVLKV 365
COG1716 COG1716
FOG: FHA domain [Signal transduction mechanisms]
42-130 6.78e-17

FOG: FHA domain [Signal transduction mechanisms]


Pssm-ID: 224630 [Multi-domain]  Cd Length: 191  Bit Score: 79.23  E-value: 6.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688  42 VGRHPDCDIVVDAGAVSRYHAKITKKGNEFAVEDAGSRNGTFVNGQLLSRPHVLSEGDRIRISEVVLVFHGdevPGFASG 121
Cdd:COG1716  93 IGRDPDNDIVLDDDVVSRRHAELRREGNEVFLEDLGSTNGTYVNGEKVRQRVLLQDGDVIRLGGTLAERLR---IILTEL 169

                ....*....
gi 32474688 122 GGSGEMTFD 130
Cdd:COG1716 170 EIDGVDPVA 178
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
26-108 7.81e-11

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis].


Pssm-ID: 234178 [Multi-domain]  Cd Length: 396  Bit Score: 63.16  E-value: 7.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688    26 DGNPSGTFQLDRDEMQVGRHPDCDIVVD--AGAVSRYHAKITKKGNEFAVEDAgSRNGTFVNGQL--LSR--PHVLSEGD 99
Cdd:TIGR03354  12 TPGIAAQKTFGTNGGTIGRSEDCDWVLPdpERHVSGRHARIRYRDGAYLLTDL-STNGVFLNGSGspLGRgnPVRLEQGD 90

                  ....*....
gi 32474688   100 RIRISEVVL 108
Cdd:TIGR03354  91 RLRLGDYEI 99
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
313-582 1.69e-09

stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane spanning protein with two separable functions. It plays a role in the switch to polar cell division during sporulation. By means of it protein phosphatase activity, located in the C-terminal region, it activates sigma-F. All proteins that score above the trusted cutoff to this model are found in endospore-forming Gram-positive bacteria. Surprisingly, a sequence from the Cyanobacterium-like (and presumably non-spore-forming) photosynthesizer Heliobacillus mobilis is homologous, and scores between the trusted and noise cutoffs [Cellular processes, Sporulation and germination].


Pssm-ID: 234038 [Multi-domain]  Cd Length: 764  Bit Score: 59.32  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   313 LTGIAAQASVVINNARMHEQALRQQE-VEQDLKLATEVqrAFLPAEAPQVPTyHLESFYQAANHIGGDYFDYVDLPDGRL 391
Cdd:TIGR02865 505 GRGECEKKIAPIISEVTGELMCVKDErCSIDPKGRCHL--TFEETPKYHVST-GVARAAKDGELVSGDSYSFGKLSAGKY 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   392 AVVVADVVGHGV-AAAMYMAKLSAETRFcLASEPDLARAVERLNDRMSALEVQ-RFVTYLLVVIDPQSNELKIVNAGHMP 469
Cdd:TIGR02865 582 AVAISDGMGSGPeAAQESSACVRLLEKF-LESGFDREVAIKTVNSILSLRSTDeKFSTLDLSVIDLYTGQAEFVKVGAVP 660
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   470 PIV-RDAVSGQIsepgdEDSGLPIAIDEGMEYAVTTVPMHAGDLALMYTDGFSEAlnAKEEEWGTDPLRQIVlkavpsKE 548
Cdd:TIGR02865 661 SFIkRGAKVEVI-----RSSNLPIGILDEVDVELVRKKLKNGDLIVMVSDGVLEG--EKEVEGKVLWLVRKL------KE 727
                         250       260       270
                  ....*....|....*....|....*....|....
gi 32474688   549 DDEPLAKVVKNEIVRQAFEHMGGAVQfDDMCMVI 582
Cdd:TIGR02865 728 TNTNDPEEIAEYLLEKAKELRSGKIK-DDMTVIV 760
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain ...
35-108 1.17e-05

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


Pssm-ID: 225987 [Multi-domain]  Cd Length: 430  Bit Score: 46.71  E-value: 1.17e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32474688  35 LDRDEMQVGRHPDCDIVVD--AGAVSRYHAKITKKGNEFAVEDAgSRNGTFVNGQLLSR---PHVLSEGDRIRISEVVL 108
Cdd:COG3456  23 FDRGGGVIGRSPDCDWQIDdpERFVSKQHCTISYRDGGFCLTDT-SNGGLLVNGSDLPLgegSARLQQGDEILIGRYII 100
FhlA COG3604
Transcriptional regulator containing GAF, AAA-type ATPase, and DNA binding domains ...
169-366 8.48e-05

Transcriptional regulator containing GAF, AAA-type ATPase, and DNA binding domains [Transcription / Signal transduction mechanisms]


Pssm-ID: 226132 [Multi-domain]  Cd Length: 550  Bit Score: 44.25  E-value: 8.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 169 AKLAALIAINSNLTGAISVDDVLPKVLSSLFQIFPS---ADRGFVVMETPDGaLVPRWVQ-------LRNKTDDTEtiri 238
Cdd:COG3604  27 LELLADIRILVELTNALLSPLRLERLLAEVAKELHSlfgCDASALLRLDSKN-LIPLATDglskdhlGREQRFVVE---- 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688 239 SRTIIRQTMETG-------HTILSLDAMDDSRFDSsesiADFSIRSMMCAPLHdEDGKAIGALQIDSTQgRGQFRDEDID 311
Cdd:COG3604 102 GHPLLEQILKAGrplvfhpADSLFPDPYDGLLPDT----EGNKKHACIGVPLK-SGDKLIGALTLDHTE-PDQFDEDLDE 175
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 32474688 312 LLTGIAAQASVVINNARMHEQALRQQEveqdlKLATEVQRAFLPAEAPQVPTYHL 366
Cdd:COG3604 176 ELRFLAALAALAVANALLHRELSSLKE-----RLEEENLALEEQLSEVVLEVGGI 225
nifA TIGR01817
Nif-specific regulatory protein; This model represents NifA, a DNA-binding regulatory protein ...
168-351 1.93e-03

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: 233584 [Multi-domain]  Cd Length: 534  Bit Score: 39.70  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   168 EAKLAALIAINSNLTGAISVDDVLPKVLSSLFQIFPSAdRGFVVMETPDG-ALVPRWVQLRNKTDDTETIRISRTIIRQT 246
Cdd:TIGR01817   1 DLQLAALYEISKILSAPTRLEKTLANVLNVLSNDLGMR-HGLITLSDSEGePLLVAAIGWSEEGFAPIRYRVGEGAIGQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32474688   247 METGHTILSLDAMDDSRFDSSESIADFSIRSMMCAPLHdEDGKAIGALQIDSTQGRGQFRDEDIDLLTGIAAQASVVINN 326
Cdd:TIGR01817  80 VATGNSLVVPDVAAEPLFLDRLSLYDPGPVPFIGVPIK-ADSETIGVLAADRDFRSRERLEEEVRFLEMVANLIGQTVRL 158
                         170       180
                  ....*....|....*....|....*
gi 32474688   327 ARmHEQALRQQEVEQDLKLATEVQR 351
Cdd:TIGR01817 159 HR-LVAQRRERLIAEAVQLSKQLRD 182
PRK05022 PRK05022
anaerobic nitric oxide reductase transcription regulator; Provisional
279-357 2.75e-03

anaerobic nitric oxide reductase transcription regulator; Provisional


Pssm-ID: 235331 [Multi-domain]  Cd Length: 509  Bit Score: 39.38  E-value: 2.75e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32474688  279 MCAPLHDeDGKAIGALQIDSTQGrGQFRDEDIDLLTGIAAQASVVINNARMHEQaLRQQEVEQDLKLATEVQRAFLPAE 357
Cdd:PRK05022 113 MGLPLFV-DGRLIGALTLDALDP-GQFDAFSDEELRALAALAAATLRNALLIEQ-LESQAELPQDVAEFLRQEALKEGE 188
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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