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Conserved domains on  [gi|499976638|ref|WP_011657356|]
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MULTISPECIES: site-2 protease family protein [Burkholderia]

Protein Classification

site-2 protease family protein( domain architecture ID 10150298)

Site-2 protease (S2P) homolog is a zinc metalloprotease which cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms, including processes as sporulation, cell division, stress response, and cell differentiation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 9-193 4.78e-65

Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains.


:

Pssm-ID: 100079  Cd Length: 181  Bit Score: 198.92  E-value: 4.78e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638   9 IAVYALPVIFAITLHEAAHGYAARLLGDNTAYMMGRVSFNPMRHIDPLGTIAIPLAMyfltggAFLFGYAKPVPVSFGNL 88
Cdd:cd06158    1 ILIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLL------PFLFGWAKPVPVNPRNF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  89 RNPRWGSLWVALAGPACNFVQALIWGVLTIVLPA-AGVDEPFFTRMAYAGVSANLVLGVLNLFPLPPLDGGRILAALLPP 167
Cdd:cd06158   75 KNPRRGMLLVSLAGPLSNLLLALLFALLLRLLPAfGGVVASFLFLMLAYGVLINLVLAVFNLLPIPPLDGSKILAALLPR 154

                        170       180
                 ....*....|....*....|....*.
gi 499976638 168 KQSIALSRIEPYGFIIVLALVATGVL 193
Cdd:cd06158  155 RLAEAYARLEPYGFLILLALLFTGIL 180
 
Name Accession Description Interval E-value
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 9-193 4.78e-65

Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains.


Pssm-ID: 100079  Cd Length: 181  Bit Score: 198.92  E-value: 4.78e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638   9 IAVYALPVIFAITLHEAAHGYAARLLGDNTAYMMGRVSFNPMRHIDPLGTIAIPLAMyfltggAFLFGYAKPVPVSFGNL 88
Cdd:cd06158    1 ILIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLL------PFLFGWAKPVPVNPRNF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  89 RNPRWGSLWVALAGPACNFVQALIWGVLTIVLPA-AGVDEPFFTRMAYAGVSANLVLGVLNLFPLPPLDGGRILAALLPP 167
Cdd:cd06158   75 KNPRRGMLLVSLAGPLSNLLLALLFALLLRLLPAfGGVVASFLFLMLAYGVLINLVLAVFNLLPIPPLDGSKILAALLPR 154

                        170       180
                 ....*....|....*....|....*.
gi 499976638 168 KQSIALSRIEPYGFIIVLALVATGVL 193
Cdd:cd06158  155 RLAEAYARLEPYGFLILLALLFTGIL 180
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 5-204 7.36e-41

Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441597  Cd Length: 175  Bit Score: 137.26  E-value: 7.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638   5 LIQTIAVYALPVIFAITLHEAAHGYAARLLGDNTAymmgRVSFNPmrhidplgtiaiplamyfltggaFLFGYAKPVpvs 84
Cdd:COG1994    7 LHPSILIFALALFLSVLLHELAHALVARRLGDPTA----KITLNP-----------------------LKGGWAKIN--- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  85 fGNLRNPrWGSLWVALAGPACNFVQALIWGVLTIVLPAAGVdePFFTRMAYAGVSANLVLGVLNLFPLPPLDGGRILAAL 164
Cdd:COG1994   57 -RNFRNP-RDEALVALAGPLANLLLALLFALLLRLLPALGL--GPLALLLGYLALINLVLAVFNLLPIPPLDGGRILRAL 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 499976638 165 LPPKQSIALSRIEPYGFIIVLALVATGVLT-NFWLRPLVNA 204
Cdd:COG1994  133 LPRRTARRATRLEPYGFLILLLLIFLGLLLgNIWLSPLLNL 173
Peptidase_M50 pfam02163
Peptidase family M50;
56-188 1.69e-04

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 41.71  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638   56 LGTIAIPLAMYFLTGGAFLFGYAK-PVPVSFGNLRNPRWGSLWVALAGPACNFVQALIWGVLTIVLPAAGVdepfftrma 134
Cdd:pfam02163 169 IGIGPVYVKYGLLEALGFALEKTVnLVTLTLKALGKLITGVSLKNLGGPIGIAGQAAEAGLIAFLYFLALI--------- 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499976638  135 yagvsaNLVLGVLNLFPLPPLDGGRILAALLPPKQSIALS-RIEPYGFIIVLALV 188
Cdd:pfam02163 240 ------NLNLGIFNLLPVPPLDGGHILRALLEAIRGKPLSeRAEEIALRVGLALL 288
 
Name Accession Description Interval E-value
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 9-193 4.78e-65

Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with a minimal core protein and no PDZ domains.


Pssm-ID: 100079  Cd Length: 181  Bit Score: 198.92  E-value: 4.78e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638   9 IAVYALPVIFAITLHEAAHGYAARLLGDNTAYMMGRVSFNPMRHIDPLGTIAIPLAMyfltggAFLFGYAKPVPVSFGNL 88
Cdd:cd06158    1 ILIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLL------PFLFGWAKPVPVNPRNF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  89 RNPRWGSLWVALAGPACNFVQALIWGVLTIVLPA-AGVDEPFFTRMAYAGVSANLVLGVLNLFPLPPLDGGRILAALLPP 167
Cdd:cd06158   75 KNPRRGMLLVSLAGPLSNLLLALLFALLLRLLPAfGGVVASFLFLMLAYGVLINLVLAVFNLLPIPPLDGSKILAALLPR 154

                        170       180
                 ....*....|....*....|....*.
gi 499976638 168 KQSIALSRIEPYGFIIVLALVATGVL 193
Cdd:cd06158  155 RLAEAYARLEPYGFLILLALLFTGIL 180
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 10-193 4.26e-41

Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of this family use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. The domain core structure appears to contain at least three transmembrane helices with a catalytic zinc atom coordinated by three conserved residues contained within the consensus sequence HExxH, together with a conserved aspartate residue. The S2P/M50 family of RIP proteases is widely distributed; in eukaryotic cells, they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum (ER) stress responses. In sterol-depleted mammalian cells, a two-step proteolytic process releases the N-terminal domains of sterol regulatory element-binding proteins (SREBPs) from membranes of the ER. These domains translocate into the nucleus, where they activate genes of cholesterol and fatty acid biosynthesis. It is the second proteolytic step that is carried out by the SREBP Site-2 protease (S2P) which is present in this CD superfamily. Prokaryotic S2P/M50 homologs have been shown to regulate stress responses, sporulation, cell division, and cell differentiation. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses, and in Bacillus subtilis, the S2P homolog SpoIVFB is involved in the pro-sigmaK pathway of spore formation. Some of the subfamilies within this hierarchy contain one or two PDZ domain insertions, with putative regulatory roles, such as the inhibition of substrate cleavage as seen by the RseP PDZ domain.


Pssm-ID: 100078 [Multi-domain]  Cd Length: 180  Bit Score: 138.14  E-value: 4.26e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  10 AVYALPVIFAITLHEAAHGYAARLLGDNTAYMMGRVSFNPMRHIDPLGTIAIPLamyfltggaflFGYAKPVPVSFGNLR 89
Cdd:cd05709    1 LAFILALLISVTVHELGHALVARRLGVKVARFSGGFTLNPLKHGDPYGIILIPL-----------GGYAKPVGENPRAFK 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  90 NPRWGSLWVALAGPACNFVQALIWGVLTIVLPAAGVDEP------FFTRMAYAGVSANLVLGVLNLFPLPPLDGGRILAA 163
Cdd:cd05709   70 KPRWQRLLVALAGPLANLLLALLLLLLLLLLGGLPPAPVgqaassGLANLLAFLALINLNLAVFNLLPIPPLDGGRILRA 149

                        170       180       190
                 ....*....|....*....|....*....|
gi 499976638 164 LLPPKQSIALSRIEPYGFIIVLALVATGVL 193
Cdd:cd05709  150 LLEAIRGRVEERLEAYGFAILLGLLLLLLL 179
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 5-204 7.36e-41

Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441597  Cd Length: 175  Bit Score: 137.26  E-value: 7.36e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638   5 LIQTIAVYALPVIFAITLHEAAHGYAARLLGDNTAymmgRVSFNPmrhidplgtiaiplamyfltggaFLFGYAKPVpvs 84
Cdd:COG1994    7 LHPSILIFALALFLSVLLHELAHALVARRLGDPTA----KITLNP-----------------------LKGGWAKIN--- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  85 fGNLRNPrWGSLWVALAGPACNFVQALIWGVLTIVLPAAGVdePFFTRMAYAGVSANLVLGVLNLFPLPPLDGGRILAAL 164
Cdd:COG1994   57 -RNFRNP-RDEALVALAGPLANLLLALLFALLLRLLPALGL--GPLALLLGYLALINLVLAVFNLLPIPPLDGGRILRAL 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 499976638 165 LPPKQSIALSRIEPYGFIIVLALVATGVLT-NFWLRPLVNA 204
Cdd:COG1994  133 LPRRTARRATRLEPYGFLILLLLIFLGLLLgNIWLSPLLNL 173
S2P-M50_SpoIVFB cd06161
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 90-198 4.93e-10

SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB.


Pssm-ID: 100082 [Multi-domain]  Cd Length: 208  Bit Score: 57.17  E-value: 4.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  90 NPRWGSLWVALAGPACNFVQALIWGVLTIVLPAAGVDEPFFTRMAYAgvsaNLVLGVLNLFPLPPLDGGRILAALLPP-- 167
Cdd:cd06161   78 ETPKEEFVIALAGPLVSLLLAGLFYLLYLLLPGGGPLSSLLEFLAQV----NLILGLFNLLPALPLDGGRVLRALLWRrt 153

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499976638 168 ------KQSIALSRIEPYGFIIVLALVATGVLTNFWL 198
Cdd:cd06161  154 gyrratRIAARIGQLFAILLVVLGLFLLFLGLGNLWL 190
S2P-M50_PDZ_RseP-like cd06163
RseP-like Site-2 proteases (S2P), zinc metalloproteases (MEROPS family M50A), cleave ...
 82-189 1.46e-09

RseP-like Site-2 proteases (S2P), zinc metalloproteases (MEROPS family M50A), cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. In Escherichia coli, the S2P homolog RseP is involved in the sigmaE pathway of extracytoplasmic stress responses. Also included in this group are such homologs as Bacillus subtilis YluC, Mycobacterium tuberculosis Rv2869c S2P, and Bordetella bronchiseptica HurP. Rv2869c S2P appears to have a role in the regulation of prokaryotic lipid biosynthesis and membrane composition and YluC of Bacillus has a role in transducing membrane stress. This group includes bacterial and eukaryotic S2P/M50s homologs with either one or two PDZ domains present. PDZ domains are believed to have a regulatory role. The RseP PDZ domain is required for the inhibitory reaction that prevents cleavage of its substrate, RseA.


Pssm-ID: 100084 [Multi-domain]  Cd Length: 182  Bit Score: 55.11  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  82 PVSFGNLrnPRWGSLWVALAGPACNFVQALIwgVLTIVLpaagvdepFFTrmayAGVSANLvlGVLNLFPLPPLDGGRIL 161
Cdd:cd06163   79 PRSFNSK--PVWQRILIVFAGPLANFLLAIV--LFAVLL--------SFL----ALLSINL--GILNLLPIPALDGGHLL 140

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 499976638 162 AAL--------LPPKQSIALSRIepyGFIIVLALVA 189
Cdd:cd06163  141 FLLieairgrpLSEKVEEIIQTI---GFALLLGLML 173
S2P-M50_SpoIVFB_CBS cd06164
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 93-165 1.25e-08

SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates intramembrane proteolysis (RIP), and is involved in the pro-sigmaK pathway of bacterial spore formation. In this subgroup, SpoIVFB (sporulation protein, stage IV cell wall formation, F locus, promoter-distal B) contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain. SpoIVFB is one of 4 proteins involved in endospore formation; the others are SpoIVFA (sporulation protein, stage IV cell wall formation, F locus, promoter-proximal A), BofA (bypass-of-forespore A), and SpoIVB (sporulation protein, stage IV cell wall formation, B locus). SpoIVFB is negatively regulated by SpoIVFA and BofA and activated by SpoIVB. It is thought that SpoIVFB, SpoIVFA, and BofA are located in the mother-cell membrane that surrounds the forespore and that SpoIVB is secreted from the forespore into the space between the two where it activates SpoIVFB. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown.


Pssm-ID: 100085  Cd Length: 227  Bit Score: 53.31  E-value: 1.25e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499976638  93 WGSLWVALAGPACNFVQALIWGVLTIVLPAAGVDEP--FFTRMAYAgvsaNLVLGVLNLFPLPPLDGGRILAALL 165
Cdd:cd06164   96 GQEFVIAIAGPLVSLVLALLFLLLSLALPGSGAGPLgvLLGYLALI----NLLLAVFNLLPAFPLDGGRVLRALL 166
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 136-189 8.83e-06

Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, protein turnover, chaperones, Transcription];


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 45.46  E-value: 8.83e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 499976638 136 AGVSANLvlGVLNLFPLPPLDGGRILAAL--------LPPKQSIALSRIepyGFIIVLALVA 189
Cdd:COG0750  282 ALLSINL--GVLNLLPIPALDGGHLLFLLieairgrpVSEKVQEPIQRI---GFALLLGLMV 338
S2P-M50_like_2 cd06160
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 12-198 1.36e-04

Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) which cleave transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms. Members of the S2P/M50 family of RIP proteases use proteolytic activity within the membrane to transfer information across membranes to integrate gene expression with physiologic stresses occurring in another cellular compartment. In eukaryotic cells they regulate such processes as sterol and lipid metabolism, and endoplasmic reticulum stress responses. In prokaryotes they regulate such processes as sporulation, cell division, stress response, and cell differentiation. This group includes bacterial, eukaryotic, and Archaeal S2P/M50s homologs with additional putative N- and C-terminal transmembrane spanning regions, relative to the core protein, and no PDZ domains.


Pssm-ID: 100081  Cd Length: 183  Bit Score: 41.06  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  12 YALPVIFAITLHEAAHGYAARLLGDNTAYMMgrvsFNPMRHIDPLGTIAIplamyfltggaflfgyakpvpvsFGNLRNP 91
Cdd:cd06160   36 FALALLAILGIHEMGHYLAARRHGVKASLPY----FIPFPFIGTFGAFIR-----------------------MRSPIPN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638  92 RWGSLWVALAGPACNFVQALIWGVLTIVLpaagvdepfftrmayaGVSANLVLGVLNLFPLPPLDGGRILAALLPPKQSI 171
Cdd:cd06160   89 RKALFDIALAGPLAGLLLALPVLIIGLAV----------------AGWVGLLVTALNLLPVGQLDGGHIVRALFGRRVAA 152

                        170       180
                 ....*....|....*....|....*..
gi 499976638 172 ALSriepYGFIIVLALVATGVLTNFWL 198
Cdd:cd06160  153 LIG----IGLLVALGLLALYLSFSIWL 175
Peptidase_M50 pfam02163
Peptidase family M50;
56-188 1.69e-04

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 41.71  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499976638   56 LGTIAIPLAMYFLTGGAFLFGYAK-PVPVSFGNLRNPRWGSLWVALAGPACNFVQALIWGVLTIVLPAAGVdepfftrma 134
Cdd:pfam02163 169 IGIGPVYVKYGLLEALGFALEKTVnLVTLTLKALGKLITGVSLKNLGGPIGIAGQAAEAGLIAFLYFLALI--------- 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 499976638  135 yagvsaNLVLGVLNLFPLPPLDGGRILAALLPPKQSIALS-RIEPYGFIIVLALV 188
Cdd:pfam02163 240 ------NLNLGIFNLLPVPPLDGGHILRALLEAIRGKPLSeRAEEIALRVGLALL 288
 
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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