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M50 family metallopeptidase [Acidithiobacillus marinus]

Protein Classification

M50 family metallopeptidase( domain architecture ID 10145855)

M50 family metallopeptidase that cleaves transmembrane domains of substrate proteins, regulating intramembrane proteolysis (RIP) of diverse signal transduction mechanisms; belongs to the site-2 protease (S2P) class of zinc metalloproteases

EC:  3.4.24.-
Gene Ontology:  GO:0016020|GO:0008233|GO:0004222|GO:0046872|GO:0006508
MEROPS:  M50
PubMed:  16322567|16731018|24099006|27889944|24099002

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 15-184 3.95e-18

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: 77.66  E-value: 3.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  15 LVTLGLFVISFLLHELGHALVVALLRGKAAVQEIRAGSLTFYRGRVLRVGILPIWGYVRFAEE-----GVPPSDWRLIFV 89
Cdd:cd05709     1 LAFILALLISVTVHELGHALVARRLGVKVARFSGGFTLNPLKHGDPYGIILIPLGGYAKPVGEnprafKKPRWQRLLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  90 AGPAASLFTAYLFLVLHHFSSLLGFPEN-------WHQVFDIMAMANFALAGFNLIPIPPLDGWKIVESWLPlfGIRLSK 162
Cdd:cd05709    81 AGPLANLLLALLLLLLLLLLGGLPPAPVgqaassgLANLLAFLALINLNLAVFNLLPIPPLDGGRILRALLE--AIRGRV 158

                         170       180
                  ....*....|....*....|..
gi 1325632681 163 ESRAQMNKWGMVFIMIVSFGFV 184
Cdd:cd05709   159 EERLEAYGFAILLGLLLLLLLN 180
 
Name Accession Description Interval E-value
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 15-184 3.95e-18

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: 77.66  E-value: 3.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  15 LVTLGLFVISFLLHELGHALVVALLRGKAAVQEIRAGSLTFYRGRVLRVGILPIWGYVRFAEE-----GVPPSDWRLIFV 89
Cdd:cd05709     1 LAFILALLISVTVHELGHALVARRLGVKVARFSGGFTLNPLKHGDPYGIILIPLGGYAKPVGEnprafKKPRWQRLLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  90 AGPAASLFTAYLFLVLHHFSSLLGFPEN-------WHQVFDIMAMANFALAGFNLIPIPPLDGWKIVESWLPlfGIRLSK 162
Cdd:cd05709    81 AGPLANLLLALLLLLLLLLLGGLPPAPVgqaassgLANLLAFLALINLNLAVFNLLPIPPLDGGRILRALLE--AIRGRV 158

                         170       180
                  ....*....|....*....|..
gi 1325632681 163 ESRAQMNKWGMVFIMIVSFGFV 184
Cdd:cd05709   159 EERLEAYGFAILLGLLLLLLLN 180
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 14-189 9.66e-18

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


Pssm-ID: 441597  Cd Length: 175  Bit Score: 76.40  E-value: 9.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  14 ILVTLGLFVISFLLHELGHALVvALLRGkaavqeIRAGSLTFYrgrvLRVGilpiwGYVRFAEEGVPPSDWRLIFVAGPA 93
Cdd:COG1994    11 ILIFALALFLSVLLHELAHALV-ARRLG------DPTAKITLN----PLKG-----GWAKINRNFRNPRDEALVALAGPL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  94 ASLFTAYLFLVLHHFSSLLGFPeNWHQVFDIMAMANFALAGFNLIPIPPLDGWKIVESWLPlfgiRLSKESRAQMNKWGM 173
Cdd:COG1994    75 ANLLLALLFALLLRLLPALGLG-PLALLLGYLALINLVLAVFNLLPIPPLDGGRILRALLP----RRTARRATRLEPYGF 149

                         170
                  ....*....|....*.
gi 1325632681 174 VFIMIVSFGFVAIHGF 189
Cdd:COG1994   150 LILLLLIFLGLLLGNI 165
Peptidase_M50 pfam02163
Peptidase family M50;
20-110 4.74e-06

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 45.56  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  20 LFVISFLLHELGHALVvallrGKAAVQEIRAGSLTFYRgrvlrVGILPIWGYVRFAEEGVPPSDW--RLIFVAGPAASLF 97
Cdd:pfam02163   5 ALGILVVVHELGHFLV-----ARRFGVKVERFSIGFYR-----IALIPLGGYVKMADEFKSKSPWqrLAIALAGPLANFI 74

                          90
                  ....*....|...
gi 1325632681  98 TAYLFLVLHHFSS 110
Cdd:pfam02163  75 LAIILFAVLLFLS 87
 
Name Accession Description Interval E-value
S2P-M50 cd05709
Site-2 protease (S2P) class of zinc metalloproteases (MEROPS family M50) cleaves transmembrane ...
 15-184 3.95e-18

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: 77.66  E-value: 3.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  15 LVTLGLFVISFLLHELGHALVVALLRGKAAVQEIRAGSLTFYRGRVLRVGILPIWGYVRFAEE-----GVPPSDWRLIFV 89
Cdd:cd05709     1 LAFILALLISVTVHELGHALVARRLGVKVARFSGGFTLNPLKHGDPYGIILIPLGGYAKPVGEnprafKKPRWQRLLVAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  90 AGPAASLFTAYLFLVLHHFSSLLGFPEN-------WHQVFDIMAMANFALAGFNLIPIPPLDGWKIVESWLPlfGIRLSK 162
Cdd:cd05709    81 AGPLANLLLALLLLLLLLLLGGLPPAPVgqaassgLANLLAFLALINLNLAVFNLLPIPPLDGGRILRALLE--AIRGRV 158

                         170       180
                  ....*....|....*....|..
gi 1325632681 163 ESRAQMNKWGMVFIMIVSFGFV 184
Cdd:cd05709   159 EERLEAYGFAILLGLLLLLLLN 180
SpoIVFB COG1994
Zn-dependent protease (includes sporulation protein SpoIVFB) [Posttranslational modification, ...
 14-189 9.66e-18

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


Pssm-ID: 441597  Cd Length: 175  Bit Score: 76.40  E-value: 9.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  14 ILVTLGLFVISFLLHELGHALVvALLRGkaavqeIRAGSLTFYrgrvLRVGilpiwGYVRFAEEGVPPSDWRLIFVAGPA 93
Cdd:COG1994    11 ILIFALALFLSVLLHELAHALV-ARRLG------DPTAKITLN----PLKG-----GWAKINRNFRNPRDEALVALAGPL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  94 ASLFTAYLFLVLHHFSSLLGFPeNWHQVFDIMAMANFALAGFNLIPIPPLDGWKIVESWLPlfgiRLSKESRAQMNKWGM 173
Cdd:COG1994    75 ANLLLALLFALLLRLLPALGLG-PLALLLGYLALINLVLAVFNLLPIPPLDGGRILRALLP----RRTARRATRLEPYGF 149

                         170
                  ....*....|....*.
gi 1325632681 174 VFIMIVSFGFVAIHGF 189
Cdd:COG1994   150 LILLLLIFLGLLLGNI 165
S2P-M50_like_1 cd06158
Uncharacterized homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS family M50) ...
 14-184 1.80e-12

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: 62.56  E-value: 1.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  14 ILVTLGLFVISFLLHELGHALVVALLRGKAAvqeIRAGSLTF-------YRGRVLRVGILPI---WG---YVRFAEEGVP 80
Cdd:cd06158     1 ILIVIIAVLLAITLHEFAHAYVAYRLGDPTA---RRAGRLTLnplahidPIGTIILPLLLPFlfgWAkpvPVNPRNFKNP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  81 PSDWRLIFVAGPAASLFTAYLFLVLhhFSSLLGFPENWHQVFDIMAMA----NFALAGFNLIPIPPLDGWKIVESWLPLF 156
Cdd:cd06158    78 RRGMLLVSLAGPLSNLLLALLFALL--LRLLPAFGGVVASFLFLMLAYgvliNLVLAVFNLLPIPPLDGSKILAALLPRR 155

                         170       180
                  ....*....|....*....|....*...
gi 1325632681 157 GIRLSkesrAQMNKWGMVFIMIVSFGFV 184
Cdd:cd06158   156 LAEAY----ARLEPYGFLILLALLFTGI 179
S2P-M50_SpoIVFB_CBS cd06164
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 10-153 4.34e-12

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: 62.17  E-value: 4.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  10 FLLAILVTLGLFViSFLLHELGHALVVallrgkaavqeiragslTFYRGRVLRVGILPIWGYVRFAEEGVPPSDWRLIFV 89
Cdd:cd06164    42 WLLGLAAALLLFA-SVLLHELGHSLVA-----------------RRYGIPVRSITLFLFGGVARLEREPETPGQEFVIAI 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1325632681  90 AGPAASLFTAYLFLVLHHFSSLLGFPENWHqVFDIMAMANFALAGFNLIPIPPLDGWKIVESWL 153
Cdd:cd06164   104 AGPLVSLVLALLFLLLSLALPGSGAGPLGV-LLGYLALINLLLAVFNLLPAFPLDGGRVLRALL 166
S2P-M50_SpoIVFB cd06161
SpoIVFB Site-2 protease (S2P), a zinc metalloprotease (MEROPS family M50B), regulates ...
 10-153 1.17e-11

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: 61.02  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  10 FLLAILVTLGLFViSFLLHELGHALVVAllrgkaavqeiragsltFYRGRVLRVGILPIWGYVRFAEEGVPPSDWRLIFV 89
Cdd:cd06161    27 WLLGLLEALLLFL-SVLLHELGHALVAR-----------------RYGIRVRSITLLPFGGVAELEEEPETPKEEFVIAL 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1325632681  90 AGPAASLFtayLFLVLHHFSSLLGFPENWHQVFDIMAMANFALAGFNLIPIPPLDGWKIVESWL 153
Cdd:cd06161    89 AGPLVSLL---LAGLFYLLYLLLPGGGPLSSLLEFLAQVNLILGLFNLLPALPLDGGRVLRALL 149
S2P-M50_PDZ_RseP-like cd06163
RseP-like Site-2 proteases (S2P), zinc metalloproteases (MEROPS family M50A), cleave ...
 14-178 1.53e-10

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: 57.42  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  14 ILVTLGLFVISFLLHELGHaLVVALLRGkAAVQEIragSLTF--------YRGRVLRVGILPIWGYVRFAEEGVPPSD-- 83
Cdd:cd06163     1 ILAFILVLGILIFVHELGH-FLVAKLFG-VKVEEF---SIGFgpklfsfkKGETEYSISAIPLGGYVKMLGEDPEEEAdp 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  84 ------------WR--LIFVAGPAASLFTAYLFlvlhhFSSLLGFpenwhqvfdiMAMANFALAGFNLIPIPPLDGWKIV 149
Cdd:cd06163    76 eddprsfnskpvWQriLIVFAGPLANFLLAIVL-----FAVLLSF----------LALLSINLGILNLLPIPALDGGHLL 140

                         170       180       190
                  ....*....|....*....|....*....|
gi 1325632681 150 ESWLP-LFGIRLSKESRAQMNKWGMVFIMI 178
Cdd:cd06163   141 FLLIEaIRGRPLSEKVEEIIQTIGFALLLG 170
Peptidase_M50 pfam02163
Peptidase family M50;
20-110 4.74e-06

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 45.56  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  20 LFVISFLLHELGHALVvallrGKAAVQEIRAGSLTFYRgrvlrVGILPIWGYVRFAEEGVPPSDW--RLIFVAGPAASLF 97
Cdd:pfam02163   5 ALGILVVVHELGHFLV-----ARRFGVKVERFSIGFYR-----IALIPLGGYVKMADEFKSKSPWqrLAIALAGPLANFI 74

                          90
                  ....*....|...
gi 1325632681  98 TAYLFLVLHHFSS 110
Cdd:pfam02163  75 LAIILFAVLLFLS 87
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 8-105 3.14e-04

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 40.46  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681   8 LNFLLAILVTLGLFVISFLLHELGHaLVVALLRGkaavqeIRAG--SLTFyrGRVL----------RVGILPIWGYVRFA 75
Cdd:COG0750     1 MSFLLTILAFILVLGVLVFVHELGH-FLVARLFG------VKVEefSIGF--GPKLfskkrgeteyGIRAIPLGGYVKMA 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1325632681  76 ----EEGVPPSD----------WR--LIFVAGPAASLFTAYLFLVL 105
Cdd:COG0750    72 gmdpESEVAPEDdprafnskpvWQrlIIVLAGPLANFLLAIVLFAV 117
S2P-M50_PDZ_Arch cd06159
Uncharacterized Archaeal homologs of Site-2 protease (S2P), zinc metalloproteases (MEROPS ...
 21-186 4.84e-04

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: 39.59  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  21 FVISFLLHELGHALVvallrgkAAVQEIRAGSLtfyrgrVLRVGILPIWGYVRFAEE---GVPPSDWRLIFVAGPAASLF 97
Cdd:cd06159   117 LVVGVVVHELSHGIL-------ARVEGIKVKSG------GLLLLIIPPGAFVEPDEEelnKADRRIRLRIFAAGVTANFV 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681  98 TAYLFLVLhhfssllgFPENWhqvfdiMAMANFALAGFNLIPIPPLDGWKIVESWLPLFGIRLSKESRAQMNKWGM-VFI 176
Cdd:cd06159   184 VALIAFAL--------FFLYW------IFWINFLLGLFNCLPAIPLDGGHVFRDLLEALLRRFPSEKAERVVNAITyYLS 249

                         170
                  ....*....|
gi 1325632681 177 MIVSFGFVAI 186
Cdd:cd06159   250 SLVLLSLLFM 259
Peptidase_M50 pfam02163
Peptidase family M50;
121-179 5.03e-04

Peptidase family M50;


Pssm-ID: 426630 [Multi-domain]  Cd Length: 291  Bit Score: 39.78  E-value: 5.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1325632681 121 VFDIMAMANFALAGFNLIPIPPLDGWKIVESWLP-LFGIRLSKESRAQMNKWGMVFIMIV 179
Cdd:pfam02163 232 FLYFLALINLNLGIFNLLPVPPLDGGHILRALLEaIRGKPLSERAEEIALRVGLALLLLL 291
RseP COG0750
Membrane-associated protease RseP, regulator of RpoE activity [Posttranslational modification, ...
 117-177 8.88e-04

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


Pssm-ID: 440513 [Multi-domain]  Cd Length: 349  Bit Score: 38.91  E-value: 8.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1325632681 117 NWHQVFDIMAMANFALAGFNLIPIPPLDGWKIV----ESwlpLFGIRLSKESRAQMNKWGMVFIM 177
Cdd:COG0750   273 GLASFLSFLALLSINLGVLNLLPIPALDGGHLLflliEA---IRGRPVSEKVQEPIQRIGFALLL 334
 
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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