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Conserved domains on  [gi|495965884|ref|WP_008690463|]
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MULTISPECIES: site-2 protease family protein [Longicatena]

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) ...
 13-195 1.20e-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: 200.47  E-value: 1.20e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  13 MIYLIPAVAIALSFHEFAHAFVSYKLGDYTQKERGRLTLNPLKHLDPIGTLCLLFFQ---FGWAKPVEVDPYYYRNKKEG 89
Cdd:cd06158    1 ILIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLLpflFGWAKPVPVNPRNFKNPRRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  90 MIWTALAGPLMNMLIGFICVFLCYLMIRFNfysnysGAVADYLFQLSYMTALINIGLGIFNLIPLPPLDGSKILMGVLSE 169
Cdd:cd06158   81 MLLVSLAGPLSNLLLALLFALLLRLLPAFG------GVVASFLFLMLAYGVLINLVLAVFNLLPIPPLDGSKILAALLPR 154

                        170       180
                 ....*....|....*....|....*.
gi 495965884 170 ETYFNLMRYEMYLSFALILVLVSGVL 195
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) ...
 13-195 1.20e-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: 200.47  E-value: 1.20e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  13 MIYLIPAVAIALSFHEFAHAFVSYKLGDYTQKERGRLTLNPLKHLDPIGTLCLLFFQ---FGWAKPVEVDPYYYRNKKEG 89
Cdd:cd06158    1 ILIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLLpflFGWAKPVPVNPRNFKNPRRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  90 MIWTALAGPLMNMLIGFICVFLCYLMIRFNfysnysGAVADYLFQLSYMTALINIGLGIFNLIPLPPLDGSKILMGVLSE 169
Cdd:cd06158   81 MLLVSLAGPLSNLLLALLFALLLRLLPAFG------GVVASFLFLMLAYGVLINLVLAVFNLLPIPPLDGSKILAALLPR 154

                        170       180
                 ....*....|....*....|....*.
gi 495965884 170 ETYFNLMRYEMYLSFALILVLVSGVL 195
Cdd:cd06158  155 RLAEAYARLEPYGFLILLALLFTGIL 180
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 13-200 2.46e-34

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


Pssm-ID: 441597  Cd Length: 175  Bit Score: 120.31  E-value: 2.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  13 MIYLIPAVAIALSFHEFAHAFVSYKLGDYTQkergRLTLNPLKhldpigtlcllffqFGWAKpveVDpYYYRNKKeGMIW 92
Cdd:COG1994   11 ILIFALALFLSVLLHELAHALVARRLGDPTA----KITLNPLK--------------GGWAK---IN-RNFRNPR-DEAL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  93 TALAGPLMNMLIGFICVFLCYLMIRFNFysnysgavaDYLFQLSYMTALINIGLGIFNLIPLPPLDGSKILMGVLSEETY 172
Cdd:COG1994   68 VALAGPLANLLLALLFALLLRLLPALGL---------GPLALLLGYLALINLVLAVFNLLPIPPLDGGRILRALLPRRTA 138

                        170       180
                 ....*....|....*....|....*...
gi 495965884 173 FNLMRYEMYLSFALILVLVSGVLDGPLF 200
Cdd:COG1994  139 RRATRLEPYGFLILLLLIFLGLLLGNIW 166
Peptidase_M50 pfam02163
Peptidase family M50;
137-190 2.69e-07

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 49.80  E-value: 2.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495965884  137 YMTALINIGLGIFNLIPLPPLDGSKILMGVLSEET----YFNLMRYEMYLSFALILVL 190
Cdd:pfam02163 234 YFLALINLNLGIFNLLPVPPLDGGHILRALLEAIRgkplSERAEEIALRVGLALLLLL 291
PRK10779 PRK10779
sigma E protease regulator RseP;
125-163 1.17e-03

sigma E protease regulator RseP;


Pssm-ID: 182723 [Multi-domain]  Cd Length: 449  Bit Score: 39.28  E-value: 1.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 495965884 125 SGAVADYLFQLSYM-TALINIGLGIFNLIPLPPLDGSKIL 163
Cdd:PRK10779 367 AGMSAEYGLVYYLMfLALISVNLGIINLFPLPVLDGGHLL 406
TIGR00054 TIGR00054
RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are ...
 125-163 9.77e-03

RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by a match to the full length of the seed alignment; the model also detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 272878 [Multi-domain]  Cd Length: 419  Bit Score: 36.34  E-value: 9.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 495965884  125 SGAVadYLFQLSymtALINIGLGIFNLIPLPPLDGSKIL 163
Cdd:TIGR00054 343 SGIV--YLLQFG---AFLSINLGIMNLLPIPALDGGQLL 376
 
Name Accession Description Interval E-value
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 13-195 1.20e-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: 200.47  E-value: 1.20e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  13 MIYLIPAVAIALSFHEFAHAFVSYKLGDYTQKERGRLTLNPLKHLDPIGTLCLLFFQ---FGWAKPVEVDPYYYRNKKEG 89
Cdd:cd06158    1 ILIVIIAVLLAITLHEFAHAYVAYRLGDPTARRAGRLTLNPLAHIDPIGTIILPLLLpflFGWAKPVPVNPRNFKNPRRG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  90 MIWTALAGPLMNMLIGFICVFLCYLMIRFNfysnysGAVADYLFQLSYMTALINIGLGIFNLIPLPPLDGSKILMGVLSE 169
Cdd:cd06158   81 MLLVSLAGPLSNLLLALLFALLLRLLPAFG------GVVASFLFLMLAYGVLINLVLAVFNLLPIPPLDGSKILAALLPR 154

                        170       180
                 ....*....|....*....|....*.
gi 495965884 170 ETYFNLMRYEMYLSFALILVLVSGVL 195
Cdd:cd06158  155 RLAEAYARLEPYGFLILLALLFTGIL 180
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 14-195 7.89e-44

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: 145.07  E-value: 7.89e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  14 IYLIPAVAIALSFHEFAHAFVSYKLGDYTQKERGRLTLNPLKHLDPIGTLCLLFFqfGWAKPVEVDPYYYRNKKEGMIWT 93
Cdd:cd05709    1 LAFILALLISVTVHELGHALVARRLGVKVARFSGGFTLNPLKHGDPYGIILIPLG--GYAKPVGENPRAFKKPRWQRLLV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  94 ALAGPLMNMLIGFICVFLcYLMIRFNFYSNYSGAVADYLFQLSYMTALINIGLGIFNLIPLPPLDGSKILMGVLSEETYF 173
Cdd:cd05709   79 ALAGPLANLLLALLLLLL-LLLLGGLPPAPVGQAASSGLANLLAFLALINLNLAVFNLLPIPPLDGGRILRALLEAIRGR 157

                        170       180
                 ....*....|....*....|..
gi 495965884 174 NLMRYEMYLSFALILVLVSGVL 195
Cdd:cd05709  158 VEERLEAYGFAILLGLLLLLLL 179
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 13-200 2.46e-34

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


Pssm-ID: 441597  Cd Length: 175  Bit Score: 120.31  E-value: 2.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  13 MIYLIPAVAIALSFHEFAHAFVSYKLGDYTQkergRLTLNPLKhldpigtlcllffqFGWAKpveVDpYYYRNKKeGMIW 92
Cdd:COG1994   11 ILIFALALFLSVLLHELAHALVARRLGDPTA----KITLNPLK--------------GGWAK---IN-RNFRNPR-DEAL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  93 TALAGPLMNMLIGFICVFLCYLMIRFNFysnysgavaDYLFQLSYMTALINIGLGIFNLIPLPPLDGSKILMGVLSEETY 172
Cdd:COG1994   68 VALAGPLANLLLALLFALLLRLLPALGL---------GPLALLLGYLALINLVLAVFNLLPIPPLDGGRILRALLPRRTA 138

                        170       180
                 ....*....|....*....|....*...
gi 495965884 173 FNLMRYEMYLSFALILVLVSGVLDGPLF 200
Cdd:COG1994  139 RRATRLEPYGFLILLLLIFLGLLLGNIW 166
S2P-M50_PDZ_RseP-like cd06163
RseP-like Site-2 proteases (S2P), zinc metalloproteases (MEROPS family M50A), cleave ...
 91-195 1.51e-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: 1.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  91 IWTALAGPLMNMLIGFICVFLcylmirfnfysnysgavadylfqLSYMTALINIGLGIFNLIPLPPLDGSKILM------ 164
Cdd:cd06163   91 ILIVFAGPLANFLLAIVLFAV-----------------------LLSFLALLSINLGILNLLPIPALDGGHLLFllieai 147

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495965884 165 --GVLSEETyfnlMRYEMYLSFALILVLVSGVL 195
Cdd:cd06163  148 rgRPLSEKV----EEIIQTIGFALLLGLMLFVT 176
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 124-190 1.78e-08

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 53.55  E-value: 1.78e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495965884 124 YSGAVADY-LFQLSYMTALINIGLGIFNLIPLPPLDGSKILMGV--------LSEETyfnlMRYEMYLSFALILVL 190
Cdd:COG0750  265 IAGEAASSgLASFLSFLALLSINLGVLNLLPIPALDGGHLLFLLieairgrpVSEKV----QEPIQRIGFALLLGL 336
S2P-M50_SpoIVFB_CBS cd06164
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 89-163 8.07e-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: 51.00  E-value: 8.07e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495965884  89 GMIWTALAGPLMNMLIGFICVFLCYLMIrfnfySNYSGAVADYLFQLsymtALINIGLGIFNLIPLPPLDGSKIL 163
Cdd:cd06164   97 QEFVIAIAGPLVSLVLALLFLLLSLALP-----GSGAGPLGVLLGYL----ALINLLLAVFNLLPAFPLDGGRVL 162
Peptidase_M50 pfam02163
Peptidase family M50;
137-190 2.69e-07

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 49.80  E-value: 2.69e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495965884  137 YMTALINIGLGIFNLIPLPPLDGSKILMGVLSEET----YFNLMRYEMYLSFALILVL 190
Cdd:pfam02163 234 YFLALINLNLGIFNLLPVPPLDGGHILRALLEAIRgkplSERAEEIALRVGLALLLLL 291
S2P-M50_SpoIVFB cd06161
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 15-168 7.91e-07

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: 47.92  E-value: 7.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  15 YLIPAVAIALS--FHEFAHAFVSYKLGdytqKERGRLTLNPlkhldpigtlcllffqFGWAkpVEVDPYYYRNKKEGMIw 92
Cdd:cd06161   30 GLLEALLLFLSvlLHELGHALVARRYG----IRVRSITLLP----------------FGGV--AELEEEPETPKEEFVI- 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495965884  93 tALAGPLMNMLIGFICVFLCYlmirfnfYSNYSGAVADYLFQLsymtALINIGLGIFNLIPLPPLDGSKILMGVLS 168
Cdd:cd06161   87 -ALAGPLVSLLLAGLFYLLYL-------LLPGGGPLSSLLEFL----AQVNLILGLFNLLPALPLDGGRVLRALLW 150
S2P-M50_PDZ_Arch cd06159
Uncharacterized Archaeal homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS ...
 14-163 3.05e-05

Uncharacterized Archaeal 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 appears to be limited to Archaeal S2P/M50s homologs with additional putative N-terminal transmembrane spanning regions, relative to the core protein, and either one or two PDZ domains present.


Pssm-ID: 100080 [Multi-domain]  Cd Length: 263  Bit Score: 43.83  E-value: 3.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  14 IYLIPAVAIALSFHEFAHAFVSyklgdytqkergrlTLNPLKhLDPIGTLCLLFFQFGWAKPVEvdPYYYRNKKEGMIWT 93
Cdd:cd06159  111 PYGIIALVVGVVVHELSHGILA--------------RVEGIK-VKSGGLLLLIIPPGAFVEPDE--EELNKADRRIRLRI 173

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495965884  94 ALAGPLMNMLIGFICVFLCYLmirfnfysnysgavadylfqlsYMTALINIGLGIFNLIPLPPLDGSKIL 163
Cdd:cd06159  174 FAAGVTANFVVALIAFALFFL----------------------YWIFWINFLLGLFNCLPAIPLDGGHVF 221
PRK10779 PRK10779
sigma E protease regulator RseP;
125-163 1.17e-03

sigma E protease regulator RseP;


Pssm-ID: 182723 [Multi-domain]  Cd Length: 449  Bit Score: 39.28  E-value: 1.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 495965884 125 SGAVADYLFQLSYM-TALINIGLGIFNLIPLPPLDGSKIL 163
Cdd:PRK10779 367 AGMSAEYGLVYYLMfLALISVNLGIINLFPLPVLDGGHLL 406
TIGR00054 TIGR00054
RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are ...
 125-163 9.77e-03

RIP metalloprotease RseP; Members of this nearly universal bacterial protein family are regulated intramembrane proteolysis (RIP) proteases. Older and synonymous gene symbols include yaeL in E. coli, mmpA in Caulobacter crescentus, etc. This family includes a region that hits the PDZ domain, found in a number of proteins targeted to the membrane by binding to a peptide ligand. The N-terminal region of this family contains a perfectly conserved motif HEXGH as found in a number of metalloproteinases, where the Glu is the active site and the His residues coordinate the metal cation. Membership in this family is determined by a match to the full length of the seed alignment; the model also detects fragments as well matches a number of members of the PEPTIDASE FAMILY S2C. The region of match appears not to overlap the active site domain. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 272878 [Multi-domain]  Cd Length: 419  Bit Score: 36.34  E-value: 9.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 495965884  125 SGAVadYLFQLSymtALINIGLGIFNLIPLPPLDGSKIL 163
Cdd:TIGR00054 343 SGIV--YLLQFG---AFLSINLGIMNLLPIPALDGGQLL 376
 
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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