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Conserved domains on  [gi|169825695|ref|YP_001695853|]
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stage II sporulation protein E [Lysinibacillus sphaericus C3-41]

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
591-777 3.20e-25

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: 104.29  E-value: 3.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  591 PGLFAILLSDGMGQSKEAQHESRKLIHLMRECLNYNMNPETAMHTLHYVMSLKQQDDMYATLDFALVDLQHGDLWSWKAG 670
Cdd:pfam07228   2 DGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  671 GMSTYILR--GKEIIKVESNAAPVGFLSISAVEAEKRKLKAGDVILMHSDGLFSSVADWDEQ--EETFLAYAQqvASTNN 746
Cdd:pfam07228  82 HPPPLLLRpdGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELfgLERLLALLA--ERHGL 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 169825695  747 TIQEKLTTIMQSFQDY--FEIEDDCTVLMLEVT 777
Cdd:pfam07228 160 SPEELLDALLEDLLRLggGELEDDITLLVLRVR 192
Voltage_gated_ClC super family cl02915
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
177-298 2.58e-04

CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function.


The actual alignment was detected with superfamily member pfam00654:

Pssm-ID: 261508  Cd Length: 345  Bit Score: 42.54  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  177 LVVFAAMLTGMQAVVFSYFSL----------PIFLLQLFICFGALVGsvPLATVIGAVLGTLIGVAKLSFTGMLSVATL- 245
Cdd:pfam00654 163 LFILLGILCGLLGALFVRLLLkverlfrrlkKKPPILRPALGGLLVG--LLGLFLPEVLGGGYGLIQLLLSGNTLSLLLl 240
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169825695  246 ----------TGLCAGMGAKGGRF------GVAIGSILPSVFFLFYDATLPLDSVYftsIAIGSVLFLT 298
Cdd:pfam00654 241 llllllkllaTALSLGSGAPGGIFapslfiGAALGRLLGLLLALLFPGIAPSPGAF---ALLGMAAFLA 306
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
29-776 3.68e-71

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: 249.61  E-value: 3.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   29 LFFLTSFFLAQSVVFEAAVPFSVPFWAIIRTKYR--EYAKFVLFGSLAGCFFLGFGQVV---ILALQIIMYECIMRFRYw 103
Cdd:TIGR02865   2 IFFVIAFLLGRAVIVSPMAPFGIAFLAAVLLAKKggDKAFFSALGVLLGAISIQPKHSLkylLLVAVIILLSYVLKNLT- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  104 rlPQSIAVSLAVLL--------VQFMWQGAMYQGLPPVLVQFYVGCEAALALIMTLFMQVLFVNSY-EWFTShwtyEKLG 174
Cdd:TIGR02865  81 --DKKKTVVPPIVVfleaavyaIFGYLQNKLVTPLDFILSIVEASLSFVLYYIFNYSIPCLKNGRTkHLLTN----EEIV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  175 SGLVVFAAMLTGMQAVVFSYFSLPIFLLQLFICFGALVGSVPLATVIGAVLGTLIGVAKLSFTGMLSVATLTGLCAGMGA 254
Cdd:TIGR02865 155 SLIILIASVLTGLRGLSIWGLSLENIIARLAVLLISYIGGSGAGAAGGVVIGVILGLANNANLYQIGVFGFAGLLGGIFK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  255 KGGRFGVAIGSILPSVFFLFYDATLPLDSVYFTSIAIGSVLFLTIPRKYSDKVRDKLFPQREEVLIARQ--NWLTEHVTY 332
Cdd:TIGR02865 235 ELGKIGTGIGYLVGFLILAFYTQGSVAFSLALYEALIATLLFLLIPNKIYKKLERYLDGERKQPDLQEDymRKVREIAAE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  333 KLEHF-----------QHFVQFMKELVFERFMTAPVEEAKEvspmNTCLSCFRYDHCWGAQNNGMDKLMTD-WFHMKGvg 400
Cdd:TIGR02865 315 KLEEFsevfrelsntfVEALASNEKLTMKRKSSYLLENLAE----RVCQSCNMKHRCWKREFDYTYSAMEElIENLEE-- 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  401 KESAIHRVEEQMRYKCVKSTKIFEELDTELYRERINGQY----FHGKKMIALQLRDMSNHLNQLIAEMKEDTVSFVSVEK 476
Cdd:TIGR02865 389 KKDPNSKLPDEFERKCIKRKELINTTEDILNNYIINEMWrkrlEEGRRLVAEQLKGVAESVEDIAKEINLEIVFHQLLEE 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  477 DIIERLKDAHIECFQLDVLNNKPGarKIVCALAPARVDWEKDttlAERMILPILYEIFNEPFEIEKVVACEIPFRHIQIC 556
Cdd:TIGR02865 469 KIIRALNKNGIPYEDVLAYNTEGG--NIDVELTIAACGGRGE---CEKKIAPIISEVTGELMCVKDERCSIDPKGRCHLT 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  557 FRSAISFEVEYDIYSMSKDATLYSGDSHALFQLHPGLFAILLSDGMGQSKEAQHESRKLIHLMRECLNYNMNPETAMHTL 636
Cdd:TIGR02865 544 FEETPKYHVSTGVARAAKDGELVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGFDREVAIKTV 623
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  637 HYVMSLKQQDDMYATLDFALVDLQHGDLWSWKAGGMSTYILRGKEIIKVESNAAPVGFLSISAVEAEKRKLKAGDVILMH 716
Cdd:TIGR02865 624 NSILSLRSTDEKFSTLDLSVIDLYTGQAEFVKVGAVPSFIKRGAKVEVIRSSNLPIGILDEVDVELVRKKLKNGDLIVMV 703
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  717 SDGLFssvaDWDEQEETFLAYAQQVASTNNTIQEklttimQSFQDYF----------EIEDDCTVLMLEV 776
Cdd:TIGR02865 704 SDGVL----EGEKEVEGKVLWLVRKLKETNTNDP------EEIAEYLlekakelrsgKIKDDMTVIVAKV 763
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
591-777 3.20e-25

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: 104.29  E-value: 3.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  591 PGLFAILLSDGMGQSKEAQHESRKLIHLMRECLNYNMNPETAMHTLHYVMSLKQQDDMYATLDFALVDLQHGDLWSWKAG 670
Cdd:pfam07228   2 DGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  671 GMSTYILR--GKEIIKVESNAAPVGFLSISAVEAEKRKLKAGDVILMHSDGLFSSVADWDEQ--EETFLAYAQqvASTNN 746
Cdd:pfam07228  82 HPPPLLLRpdGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELfgLERLLALLA--ERHGL 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 169825695  747 TIQEKLTTIMQSFQDY--FEIEDDCTVLMLEVT 777
Cdd:pfam07228 160 SPEELLDALLEDLLRLggGELEDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
568-758 2.31e-24

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 101.66  E-value: 2.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   568 DIYSMSKDATLYSGDSHALFQLHPGLFAILLSDGMGQSKEAQHESRKLIHLMRECLNYNMNPETAMHTLHYVMSLKQQDD 647
Cdd:smart00331   5 LIAQYYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGEDG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   648 MYATLDFALVDLQHGDLWSWKAGGMSTYILR--GKEIIKVESNAAPVGFLSISAVEAEKRKLKAGDVILMHSDGLFSSVA 725
Cdd:smart00331  85 MFATLFLALYDFAGGTLSYANAGHSPPYLLRadGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEARN 164
                          170       180       190
                   ....*....|....*....|....*....|...
gi 169825695   726 dwDEQEETFLAyaqqvASTNNTIQEKLTTIMQS 758
Cdd:smart00331 165 --PERLEELLE-----ELLGSPPAEIAQRILEE 190
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
177-298 2.58e-04

Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.


Pssm-ID: 250034  Cd Length: 345  Bit Score: 42.54  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  177 LVVFAAMLTGMQAVVFSYFSL----------PIFLLQLFICFGALVGsvPLATVIGAVLGTLIGVAKLSFTGMLSVATL- 245
Cdd:pfam00654 163 LFILLGILCGLLGALFVRLLLkverlfrrlkKKPPILRPALGGLLVG--LLGLFLPEVLGGGYGLIQLLLSGNTLSLLLl 240
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169825695  246 ----------TGLCAGMGAKGGRF------GVAIGSILPSVFFLFYDATLPLDSVYftsIAIGSVLFLT 298
Cdd:pfam00654 241 llllllkllaTALSLGSGAPGGIFapslfiGAALGRLLGLLLALLFPGIAPSPGAF---ALLGMAAFLA 306
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
146-295 4.09e-03

CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function.


Pssm-ID: 238233  Cd Length: 383  Bit Score: 38.70  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 146 ALIMTLFM--QVLFVNSYEWFTSHWTYeklgsGLVVFAAMLTGMQAVVFSYF---------SLPIFLLQLFICFGALVGS 214
Cdd:cd00400  180 ALVSRLLFgaEPAFGVPLYDPLSLLEL-----PLYLLLGLLAGLVGVLFVRLlykierlfrRLPIPPWLRPALGGLLLGL 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 215 vpLATVIGAVLGTLIGVAKLSFTGMLSVATL----------TGLCAGMGAKGGRF------GVAIGSILPSVFFLFYdAT 278
Cdd:cd00400  255 --LGLFLPQVLGSGYGAILLALAGELSLLLLllllllkllaTALTLGSGFPGGVFapslfiGAALGAAFGLLLPALF-PG 331
                        170
                 ....*....|....*..
gi 169825695 279 LPLDSVYFTSIAIGSVL 295
Cdd:cd00400  332 LVASPGAYALVGMAALL 348
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
29-776 3.68e-71

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: 249.61  E-value: 3.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   29 LFFLTSFFLAQSVVFEAAVPFSVPFWAIIRTKYR--EYAKFVLFGSLAGCFFLGFGQVV---ILALQIIMYECIMRFRYw 103
Cdd:TIGR02865   2 IFFVIAFLLGRAVIVSPMAPFGIAFLAAVLLAKKggDKAFFSALGVLLGAISIQPKHSLkylLLVAVIILLSYVLKNLT- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  104 rlPQSIAVSLAVLL--------VQFMWQGAMYQGLPPVLVQFYVGCEAALALIMTLFMQVLFVNSY-EWFTShwtyEKLG 174
Cdd:TIGR02865  81 --DKKKTVVPPIVVfleaavyaIFGYLQNKLVTPLDFILSIVEASLSFVLYYIFNYSIPCLKNGRTkHLLTN----EEIV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  175 SGLVVFAAMLTGMQAVVFSYFSLPIFLLQLFICFGALVGSVPLATVIGAVLGTLIGVAKLSFTGMLSVATLTGLCAGMGA 254
Cdd:TIGR02865 155 SLIILIASVLTGLRGLSIWGLSLENIIARLAVLLISYIGGSGAGAAGGVVIGVILGLANNANLYQIGVFGFAGLLGGIFK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  255 KGGRFGVAIGSILPSVFFLFYDATLPLDSVYFTSIAIGSVLFLTIPRKYSDKVRDKLFPQREEVLIARQ--NWLTEHVTY 332
Cdd:TIGR02865 235 ELGKIGTGIGYLVGFLILAFYTQGSVAFSLALYEALIATLLFLLIPNKIYKKLERYLDGERKQPDLQEDymRKVREIAAE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  333 KLEHF-----------QHFVQFMKELVFERFMTAPVEEAKEvspmNTCLSCFRYDHCWGAQNNGMDKLMTD-WFHMKGvg 400
Cdd:TIGR02865 315 KLEEFsevfrelsntfVEALASNEKLTMKRKSSYLLENLAE----RVCQSCNMKHRCWKREFDYTYSAMEElIENLEE-- 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  401 KESAIHRVEEQMRYKCVKSTKIFEELDTELYRERINGQY----FHGKKMIALQLRDMSNHLNQLIAEMKEDTVSFVSVEK 476
Cdd:TIGR02865 389 KKDPNSKLPDEFERKCIKRKELINTTEDILNNYIINEMWrkrlEEGRRLVAEQLKGVAESVEDIAKEINLEIVFHQLLEE 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  477 DIIERLKDAHIECFQLDVLNNKPGarKIVCALAPARVDWEKDttlAERMILPILYEIFNEPFEIEKVVACEIPFRHIQIC 556
Cdd:TIGR02865 469 KIIRALNKNGIPYEDVLAYNTEGG--NIDVELTIAACGGRGE---CEKKIAPIISEVTGELMCVKDERCSIDPKGRCHLT 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  557 FRSAISFEVEYDIYSMSKDATLYSGDSHALFQLHPGLFAILLSDGMGQSKEAQHESRKLIHLMRECLNYNMNPETAMHTL 636
Cdd:TIGR02865 544 FEETPKYHVSTGVARAAKDGELVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGFDREVAIKTV 623
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  637 HYVMSLKQQDDMYATLDFALVDLQHGDLWSWKAGGMSTYILRGKEIIKVESNAAPVGFLSISAVEAEKRKLKAGDVILMH 716
Cdd:TIGR02865 624 NSILSLRSTDEKFSTLDLSVIDLYTGQAEFVKVGAVPSFIKRGAKVEVIRSSNLPIGILDEVDVELVRKKLKNGDLIVMV 703
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  717 SDGLFssvaDWDEQEETFLAYAQQVASTNNTIQEklttimQSFQDYF----------EIEDDCTVLMLEV 776
Cdd:TIGR02865 704 SDGVL----EGEKEVEGKVLWLVRKLKETNTNDP------EEIAEYLlekakelrsgKIKDDMTVIVAKV 763
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
505-778 3.13e-14

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 73.98  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 505 VCALAPARVDWEKDTTLAERMILPILYEifnepFEIEKVVACEIPFRHIQICFRSAISFEVEYDIYS------------- 571
Cdd:COG2208   71 VLLGVSGKLRALSEEIKHWRGGLPLVAE-----LLVEINRAVGLVSAHNELLLLEQNNISAELEVARqiqqnllpkalpl 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 572 ---MSKDATLY-----SGDSHALFQLHPGLFAILLSDGMGQSKEAQHESRKLIhLMRECLNYN--MNPETAMHTLHYVMS 641
Cdd:COG2208  146 fpgIDIEAILVpasevGGDYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPK-LALRLLLESgpLDPADVLETLNRVLK 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 642 LKQQDDMYATLDFALVDLQHGDLWSWKAGGMSTYILRGKEIIKVE---SNAAPVGFLSISAVEAEKRKLKAGDVILMHSD 718
Cdd:COG2208  225 QNLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILSADGEIEVEdltALGLPIGLLPDYQYEVASLQLEPGDLLVLYTD 304
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169825695 719 GLF---SSVAD-WDEQE--ETFLAYAQQVAstnntiQEKLTTIMQS---FQDYFEIEDDCTVLMLEVTH 778
Cdd:COG2208  305 GVTearNSDGEfFGLERllKILGRLLGQPA------EEILEAILESleeLQGDQIQDDDITLLVLKVKK 367
DUF4401 pfam14351
Domain of unknown function (DUF4401); This family of proteins is found in bacteria. Proteins ...
24-281 1.91e-07

Domain of unknown function (DUF4401); This family of proteins is found in bacteria. Proteins in this family are typically between 357 and 735 amino acids in length. The family is found in association with pfam09925. There is a single completely conserved residue K that may be functionally important.


Pssm-ID: 258524 [Multi-domain]  Cd Length: 321  Bit Score: 52.24  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   24 IFIGSLFFLTSFFLAQSVVFE------AAVPFSVPFWAIIRTKYREYA-KFVLFGSLAGCFFLGFG--------QVVILA 88
Cdd:pfam14351  12 GWLAALFLLGFLALAFNLAFDeggalvVGLILIAIAVALLRKLPSLFLrQLALALSLAGQLLLAFGlfdlldesVLAALL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   89 LQIIMYECImrfrYWRLPQSIAVSLAVLLVQFMWQGAMYQGLPPVLVQFYVGceAALALIMTLFMQVLFVNSYEWFTS-H 167
Cdd:pfam14351  92 LLALILALL----YFLMPDRLLRFLSAAAGVLALLGLLAELLLSGLAYLLLP--LAPLLLVALFVFLLLNLILGRLRRrH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  168 WTYEKLGSGLVVF----AAMLTGMQAVVFSYF-------SLPIFLLQLFICFGALVGSVPLATVIGAVLG-------TLI 229
Cdd:pfam14351 166 ALLEPLAYGLLLSllalLLVLSGNSLILGAPFllaswlkALLTLLLLVGLALLLISILWRRRQPLTSKLQavvllalLLL 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 169825695  230 GVAKLSFTGMLSVATLTGLCAGMGAKGGrFGVAIGSILPSVFFLFYDATLPL 281
Cdd:pfam14351 246 ALLSLPAPGLGAALLLLLLGFYRGSRVL-LGLGLLALLLYLSWYYYSLGITL 296
 
Name Accession Description Interval E-value
SpoIIE pfam07228
Stage II sporulation protein E (SpoIIE); This family contains a number of bacterial stage II ...
591-777 3.20e-25

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: 104.29  E-value: 3.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  591 PGLFAILLSDGMGQSKEAQHESRKLIHLMRECLNYNMNPETAMHTLHYVMSLKQQDDMYATLDFALVDLQHGDLWSWKAG 670
Cdd:pfam07228   2 DGRVALVIGDVMGHGLPAALLMGMLRTALRALALEGLDPAEVLERLNRALQRNLEGERFATAVLAVYDPETGTLEYANAG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  671 GMSTYILR--GKEIIKVESNAAPVGFLSISAVEAEKRKLKAGDVILMHSDGLFSSVADWDEQ--EETFLAYAQqvASTNN 746
Cdd:pfam07228  82 HPPPLLLRpdGGVVELLESPGLPLGVLPDAPYETAEFPLEPGDTLLLYTDGLTEARDPDGELfgLERLLALLA--ERHGL 159
                         170       180       190
                  ....*....|....*....|....*....|...
gi 169825695  747 TIQEKLTTIMQSFQDY--FEIEDDCTVLMLEVT 777
Cdd:pfam07228 160 SPEELLDALLEDLLRLggGELEDDITLLVLRVR 192
PP2C_SIG smart00331
Sigma factor PP2C-like phosphatases;
568-758 2.31e-24

Sigma factor PP2C-like phosphatases;


Pssm-ID: 214624  Cd Length: 193  Bit Score: 101.66  E-value: 2.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   568 DIYSMSKDATLYSGDSHALFQLHPGLFAILLSDGMGQSKEAQHESRKLIHLMRECLNYNMNPETAMHTLHYVMSLKQQDD 647
Cdd:smart00331   5 LIAQYYEDATQVGGDFYDVVKLPEGRLLIAIADVMGKGLAAALAMSMARSALRTLLSEGISLSQILERLNRAIYENGEDG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   648 MYATLDFALVDLQHGDLWSWKAGGMSTYILR--GKEIIKVESNAAPVGFLSISAVEAEKRKLKAGDVILMHSDGLFSSVA 725
Cdd:smart00331  85 MFATLFLALYDFAGGTLSYANAGHSPPYLLRadGGLVEDLDDLGAPLGLEPDVEVDVRELTLEPGDLLLLYTDGLTEARN 164
                          170       180       190
                   ....*....|....*....|....*....|...
gi 169825695   726 dwDEQEETFLAyaqqvASTNNTIQEKLTTIMQS 758
Cdd:smart00331 165 --PERLEELLE-----ELLGSPPAEIAQRILEE 190
Voltage_CLC pfam00654
Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane ...
177-298 2.58e-04

Voltage gated chloride channel; This family of ion channels contains 10 or 12 transmembrane helices. Each protein forms a single pore. It has been shown that some members of this family form homodimers. In terms of primary structure, they are unrelated to known cation channels or other types of anion channels. Three ClC subfamilies are found in animals. ClC-1 is involved in setting and restoring the resting membrane potential of skeletal muscle, while other channels play important parts in solute concentration mechanisms in the kidney. These proteins contain two pfam00571 domains.


Pssm-ID: 250034  Cd Length: 345  Bit Score: 42.54  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  177 LVVFAAMLTGMQAVVFSYFSL----------PIFLLQLFICFGALVGsvPLATVIGAVLGTLIGVAKLSFTGMLSVATL- 245
Cdd:pfam00654 163 LFILLGILCGLLGALFVRLLLkverlfrrlkKKPPILRPALGGLLVG--LLGLFLPEVLGGGYGLIQLLLSGNTLSLLLl 240
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169825695  246 ----------TGLCAGMGAKGGRF------GVAIGSILPSVFFLFYDATLPLDSVYftsIAIGSVLFLT 298
Cdd:pfam00654 241 llllllkllaTALSLGSGAPGGIFapslfiGAALGRLLGLLLALLFPGIAPSPGAF---ALLGMAAFLA 306
Voltage_gated_ClC cd00400
CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of ...
146-295 4.09e-03

CLC voltage-gated chloride channel. The ClC chloride channels catalyse the selective flow of Cl- ions across cell membranes, thereby regulating electrical excitation in skeletal muscle and the flow of salt and water across epithelial barriers. This domain is found in the halogen ions (Cl-, Br- and I-) transport proteins of the ClC family. The ClC channels are found in all three kingdoms of life and perform a variety of functions including cellular excitability regulation, cell volume regulation, membrane potential stabilization, acidification of intracellular organelles, signal transduction, transepithelial transport in animals, and the extreme acid resistance response in eubacteria. They lack any structural or sequence similarity to other known ion channels and exhibit unique properties of ion permeation and gating. Unlike cation-selective ion channels, which form oligomers containing a single pore along the axis of symmetry, the ClC channels form two-pore homodimers with one pore per subunit without axial symmetry. Although lacking the typical voltage-sensor found in cation channels, all studied ClC channels are gated (opened and closed) by transmembrane voltage. The gating is conferred by the permeating ion itself, acting as the gating charge. In addition, eukaryotic and some prokaryotic ClC channels have two additional C-terminal CBS (cystathionine beta synthase) domains of putative regulatory function.


Pssm-ID: 238233  Cd Length: 383  Bit Score: 38.70  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 146 ALIMTLFM--QVLFVNSYEWFTSHWTYeklgsGLVVFAAMLTGMQAVVFSYF---------SLPIFLLQLFICFGALVGS 214
Cdd:cd00400  180 ALVSRLLFgaEPAFGVPLYDPLSLLEL-----PLYLLLGLLAGLVGVLFVRLlykierlfrRLPIPPWLRPALGGLLLGL 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 215 vpLATVIGAVLGTLIGVAKLSFTGMLSVATL----------TGLCAGMGAKGGRF------GVAIGSILPSVFFLFYdAT 278
Cdd:cd00400  255 --LGLFLPQVLGSGYGAILLALAGELSLLLLllllllkllaTALTLGSGFPGGVFapslfiGAALGAAFGLLLPALF-PG 331
                        170
                 ....*....|....*..
gi 169825695 279 LPLDSVYFTSIAIGSVL 295
Cdd:cd00400  332 LVASPGAYALVGMAALL 348
spore_II_E TIGR02865
stage II sporulation protein E; Stage II sporulation protein E (SpoIIE) is a multiple membrane ...
29-776 3.68e-71

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: 249.61  E-value: 3.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   29 LFFLTSFFLAQSVVFEAAVPFSVPFWAIIRTKYR--EYAKFVLFGSLAGCFFLGFGQVV---ILALQIIMYECIMRFRYw 103
Cdd:TIGR02865   2 IFFVIAFLLGRAVIVSPMAPFGIAFLAAVLLAKKggDKAFFSALGVLLGAISIQPKHSLkylLLVAVIILLSYVLKNLT- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  104 rlPQSIAVSLAVLL--------VQFMWQGAMYQGLPPVLVQFYVGCEAALALIMTLFMQVLFVNSY-EWFTShwtyEKLG 174
Cdd:TIGR02865  81 --DKKKTVVPPIVVfleaavyaIFGYLQNKLVTPLDFILSIVEASLSFVLYYIFNYSIPCLKNGRTkHLLTN----EEIV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  175 SGLVVFAAMLTGMQAVVFSYFSLPIFLLQLFICFGALVGSVPLATVIGAVLGTLIGVAKLSFTGMLSVATLTGLCAGMGA 254
Cdd:TIGR02865 155 SLIILIASVLTGLRGLSIWGLSLENIIARLAVLLISYIGGSGAGAAGGVVIGVILGLANNANLYQIGVFGFAGLLGGIFK 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  255 KGGRFGVAIGSILPSVFFLFYDATLPLDSVYFTSIAIGSVLFLTIPRKYSDKVRDKLFPQREEVLIARQ--NWLTEHVTY 332
Cdd:TIGR02865 235 ELGKIGTGIGYLVGFLILAFYTQGSVAFSLALYEALIATLLFLLIPNKIYKKLERYLDGERKQPDLQEDymRKVREIAAE 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  333 KLEHF-----------QHFVQFMKELVFERFMTAPVEEAKEvspmNTCLSCFRYDHCWGAQNNGMDKLMTD-WFHMKGvg 400
Cdd:TIGR02865 315 KLEEFsevfrelsntfVEALASNEKLTMKRKSSYLLENLAE----RVCQSCNMKHRCWKREFDYTYSAMEElIENLEE-- 388
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  401 KESAIHRVEEQMRYKCVKSTKIFEELDTELYRERINGQY----FHGKKMIALQLRDMSNHLNQLIAEMKEDTVSFVSVEK 476
Cdd:TIGR02865 389 KKDPNSKLPDEFERKCIKRKELINTTEDILNNYIINEMWrkrlEEGRRLVAEQLKGVAESVEDIAKEINLEIVFHQLLEE 468
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  477 DIIERLKDAHIECFQLDVLNNKPGarKIVCALAPARVDWEKDttlAERMILPILYEIFNEPFEIEKVVACEIPFRHIQIC 556
Cdd:TIGR02865 469 KIIRALNKNGIPYEDVLAYNTEGG--NIDVELTIAACGGRGE---CEKKIAPIISEVTGELMCVKDERCSIDPKGRCHLT 543
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  557 FRSAISFEVEYDIYSMSKDATLYSGDSHALFQLHPGLFAILLSDGMGQSKEAQHESRKLIHLMRECLNYNMNPETAMHTL 636
Cdd:TIGR02865 544 FEETPKYHVSTGVARAAKDGELVSGDSYSFGKLSAGKYAVAISDGMGSGPEAAQESSACVRLLEKFLESGFDREVAIKTV 623
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  637 HYVMSLKQQDDMYATLDFALVDLQHGDLWSWKAGGMSTYILRGKEIIKVESNAAPVGFLSISAVEAEKRKLKAGDVILMH 716
Cdd:TIGR02865 624 NSILSLRSTDEKFSTLDLSVIDLYTGQAEFVKVGAVPSFIKRGAKVEVIRSSNLPIGILDEVDVELVRKKLKNGDLIVMV 703
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  717 SDGLFssvaDWDEQEETFLAYAQQVASTNNTIQEklttimQSFQDYF----------EIEDDCTVLMLEV 776
Cdd:TIGR02865 704 SDGVL----EGEKEVEGKVLWLVRKLKETNTNDP------EEIAEYLlekakelrsgKIKDDMTVIVAKV 763
RsbU COG2208
Serine phosphatase RsbU, regulator of sigma subunit [Signal transduction mechanisms / ...
505-778 3.13e-14

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


Pssm-ID: 225118 [Multi-domain]  Cd Length: 367  Bit Score: 73.98  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 505 VCALAPARVDWEKDTTLAERMILPILYEifnepFEIEKVVACEIPFRHIQICFRSAISFEVEYDIYS------------- 571
Cdd:COG2208   71 VLLGVSGKLRALSEEIKHWRGGLPLVAE-----LLVEINRAVGLVSAHNELLLLEQNNISAELEVARqiqqnllpkalpl 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 572 ---MSKDATLY-----SGDSHALFQLHPGLFAILLSDGMGQSKEAQHESRKLIhLMRECLNYN--MNPETAMHTLHYVMS 641
Cdd:COG2208  146 fpgIDIEAILVpasevGGDYYDFIQLGEKRLRIGIGDVSGKGVPAALLMLMPK-LALRLLLESgpLDPADVLETLNRVLK 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695 642 LKQQDDMYATLDFALVDLQHGDLWSWKAGGMSTYILRGKEIIKVE---SNAAPVGFLSISAVEAEKRKLKAGDVILMHSD 718
Cdd:COG2208  225 QNLEEDMFVTLFLGVYDLDSGELTYSNAGHEPALILSADGEIEVEdltALGLPIGLLPDYQYEVASLQLEPGDLLVLYTD 304
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169825695 719 GLF---SSVAD-WDEQE--ETFLAYAQQVAstnntiQEKLTTIMQS---FQDYFEIEDDCTVLMLEVTH 778
Cdd:COG2208  305 GVTearNSDGEfFGLERllKILGRLLGQPA------EEILEAILESleeLQGDQIQDDDITLLVLKVKK 367
DUF4401 pfam14351
Domain of unknown function (DUF4401); This family of proteins is found in bacteria. Proteins ...
24-281 1.91e-07

Domain of unknown function (DUF4401); This family of proteins is found in bacteria. Proteins in this family are typically between 357 and 735 amino acids in length. The family is found in association with pfam09925. There is a single completely conserved residue K that may be functionally important.


Pssm-ID: 258524 [Multi-domain]  Cd Length: 321  Bit Score: 52.24  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   24 IFIGSLFFLTSFFLAQSVVFE------AAVPFSVPFWAIIRTKYREYA-KFVLFGSLAGCFFLGFG--------QVVILA 88
Cdd:pfam14351  12 GWLAALFLLGFLALAFNLAFDeggalvVGLILIAIAVALLRKLPSLFLrQLALALSLAGQLLLAFGlfdlldesVLAALL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695   89 LQIIMYECImrfrYWRLPQSIAVSLAVLLVQFMWQGAMYQGLPPVLVQFYVGceAALALIMTLFMQVLFVNSYEWFTS-H 167
Cdd:pfam14351  92 LLALILALL----YFLMPDRLLRFLSAAAGVLALLGLLAELLLSGLAYLLLP--LAPLLLVALFVFLLLNLILGRLRRrH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  168 WTYEKLGSGLVVF----AAMLTGMQAVVFSYF-------SLPIFLLQLFICFGALVGSVPLATVIGAVLG-------TLI 229
Cdd:pfam14351 166 ALLEPLAYGLLLSllalLLVLSGNSLILGAPFllaswlkALLTLLLLVGLALLLISILWRRRQPLTSKLQavvllalLLL 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 169825695  230 GVAKLSFTGMLSVATLTGLCAGMGAKGGrFGVAIGSILPSVFFLFYDATLPL 281
Cdd:pfam14351 246 ALLSLPAPGLGAALLLLLLGFYRGSRVL-LGLGLLALLLYLSWYYYSLGITL 296
AcrB COG0841
Cation/multidrug efflux pump [Defense mechanisms]
127-248 2.99e-03

Cation/multidrug efflux pump [Defense mechanisms]


Pssm-ID: 223911 [Multi-domain]  Cd Length: 1009  Bit Score: 39.90  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169825695  127 YQGLPPVLVQFYVGCEAALALIMTLFMQVLFVN------SYEWFTSHWTYEKLGSGLVV-FAAMLTGMQAVV---FSYFS 196
Cdd:COG0841   795 YNGLPSVTISGNLAPGVSSGDAMAAMEKLAAELplpsgyTYEWSGESEQEKEAGGQALLlFALALLVVFLVLaaqYESFS 874
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 169825695  197 LPIfllqlficfgALVGSVPLAtVIGAVLGTLIGVAKLSFTGMLSVATLTGL 248
Cdd:COG0841   875 IPF----------IVMLTVPLG-LLGALLALLLTGLPLDVYAQIGLITLIGL 915
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.12
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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