NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907156973|ref|XP_036020249|]
View 

metalloendopeptidase OMA1, mitochondrial isoform X3 [Mus musculus]

Protein Classification

M48 family metallopeptidase( domain architecture ID 11574487)

M48 family metallopeptidase is a Zn-dependent protease family protein, such as metalloendopeptidase OMA1 that is part of the quality control system in the inner membrane of mitochondria

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
M48C_Oma1_like cd07331
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 265-402 1.61e-55

Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.


:

Pssm-ID: 320690 [Multi-domain]  Cd Length: 187  Bit Score: 183.16  E-value: 1.61e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 265 HLTQCNRDVPGISET-NWVVHVVDSPAVNAFVLPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKASLVHLL 343
Cdd:cd07331     7 RLIAAAGDDPPQSAGwDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSAERMSQQKLL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156973 344 DFLGMIFLTMIWAicprdSLAVLGQWIQSKLQEYMFDRPYSRTLEAEADKVGLQLAAKA 402
Cdd:cd07331    87 QLLLLLLLAALGA-----SLAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKA 140
 
Name Accession Description Interval E-value
M48C_Oma1_like cd07331
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 265-402 1.61e-55

Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.


Pssm-ID: 320690 [Multi-domain]  Cd Length: 187  Bit Score: 183.16  E-value: 1.61e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 265 HLTQCNRDVPGISET-NWVVHVVDSPAVNAFVLPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKASLVHLL 343
Cdd:cd07331     7 RLIAAAGDDPPQSAGwDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSAERMSQQKLL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156973 344 DFLGMIFLTMIWAicprdSLAVLGQWIQSKLQEYMFDRPYSRTLEAEADKVGLQLAAKA 402
Cdd:cd07331    87 QLLLLLLLAALGA-----SLAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKA 140
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 281-402 1.57e-21

Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX prenyl protease homologs such as Human FACE-1 protease. These are metallopeptidases, with the characteriztic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit.


Pssm-ID: 426263 [Multi-domain]  Cd Length: 201  Bit Score: 92.11  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 281 WVVHVVDSPAVNAFV---LPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKASLVHLLDFLgMIFLTMIWAI 357
Cdd:pfam01435  26 YVVVIKSSPVPNAFAyglLPGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARHSVESLSIMGGLSLA-QLFLALLLLG 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907156973 358 CPRDSLAVLGQWIQSKL-----QEYMFDRPYSRTLEAEADKVGLQLAAKA 402
Cdd:pfam01435 105 AAASGFANFGIIFLLLIgplaaLLTLLLLPYSRAQEYEADRLGAELMARA 154
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
277-402 9.13e-15

Putative Zn-dependent protease [General function prediction only];


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 76.47  E-value: 9.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 277 SETNWVVHVVDSPAVNAFVLPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKASLVHlldfLGMIFLTMIwa 356
Cdd:COG4784    85 PDLPYTFTVLDSPVVNAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARHAVQRQSRAT----AAQIGLGRV-- 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907156973 357 ICPRDSLAVLGQWIQSKLQEYMfdRPYSRTLEAEADKVGLQLAAKA 402
Cdd:COG4784   159 LSPVLGSAQAGQLAGAGAQLLL--ASFSRDQELEADRLGVRYLARA 202
 
Name Accession Description Interval E-value
M48C_Oma1_like cd07331
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 265-402 1.61e-55

Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.


Pssm-ID: 320690 [Multi-domain]  Cd Length: 187  Bit Score: 183.16  E-value: 1.61e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 265 HLTQCNRDVPGISET-NWVVHVVDSPAVNAFVLPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKASLVHLL 343
Cdd:cd07331     7 RLIAAAGDDPPQSAGwDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSAERMSQQKLL 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907156973 344 DFLGMIFLTMIWAicprdSLAVLGQWIQSKLQEYMFDRPYSRTLEAEADKVGLQLAAKA 402
Cdd:cd07331    87 QLLLLLLLAALGA-----SLAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKA 140
M48C_Oma1-like cd07324
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ...
 275-402 1.96e-24

Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 subfamily C (also known as Oma1 peptidase or mitochondrial metalloendopeptidase OMA1), including similar peptidases containing tetratricopeptide (TPR) repeats, as well as uncharacterized proteins such as E. coli bepA (formerly yfgC), ycaL and loiP (formerly yggG), considered to be putative metallopeptidases. Oma1 peptidase is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Homologs of Oma1 are present in higher eukaryotes, eubacteria and archaebacteria, suggesting that Oma1 is the founding member of a conserved family of membrane-embedded metallopeptidases, all containing the zinc metalloprotease motif (HEXXH). M48 peptidases proteolytically remove the C-terminal three residues of farnesylated proteins.


Pssm-ID: 320683 [Multi-domain]  Cd Length: 142  Bit Score: 98.41  E-value: 1.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 275 GISETNWVVHVVDSPAVNAFVLPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKASLvhlldflgmifltmi 354
Cdd:cd07324    14 GRPDLPYRFFVVDDPSINAFALPGGYIFVTTGLLLLLESEDELAAVLAHEIGHVTLRHIARQLER--------------- 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1907156973 355 waicprdslavlgqwiqsklqeymfdrpYSRTLEAEADKVGLQLAAKA 402
Cdd:cd07324    79 ----------------------------YSRDQEREADRLGLQLLARA 98
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 281-402 1.57e-21

Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX prenyl protease homologs such as Human FACE-1 protease. These are metallopeptidases, with the characteriztic HExxH motif giving the two histidine-zinc-ligands and an adjacent glutamate on the next helix being the third. The whole molecule folds to form a deep groove/cleft into which the substrate can fit.


Pssm-ID: 426263 [Multi-domain]  Cd Length: 201  Bit Score: 92.11  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 281 WVVHVVDSPAVNAFV---LPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKASLVHLLDFLgMIFLTMIWAI 357
Cdd:pfam01435  26 YVVVIKSSPVPNAFAyglLPGGRVVVTTGLLDLLETEDELAAVLGHEIGHIKARHSVESLSIMGGLSLA-QLFLALLLLG 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907156973 358 CPRDSLAVLGQWIQSKL-----QEYMFDRPYSRTLEAEADKVGLQLAAKA 402
Cdd:pfam01435 105 AAASGFANFGIIFLLLIgplaaLLTLLLLPYSRAQEYEADRLGAELMARA 154
M48C_bepA_like cd07333
Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase ...
 280-402 1.27e-17

Peptidase M48C Ste24p bepA-like, integral membrane protein; This family contains peptidase M48C Ste24p protease bepA (formerly yfgC)-like proteins considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Several members of this family also contain tetratricopeptide (TPR) repeat motifs, which are involved in a variety of functions including protein-protein interactions. BepA has been shown to possess protease activity and is responsible for the degradation of incorrectly folded LptD, an essential outer-membrane protein (OMP) involved in OM transport and assembly of lipopolysaccharide. Overexpression of the bepA protease causes abnormal biofilm architecture.


Pssm-ID: 320692 [Multi-domain]  Cd Length: 174  Bit Score: 80.23  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 280 NWVVHVVDSPAVNAFVLPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEkaslvhlldflgmifltmiwaicp 359
Cdd:cd07333    46 PYRFFVVNDDSINAFATPGGYIYVNTGLILAADNEAELAGVLAHEIGHVVARHIAK------------------------ 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1907156973 360 rdslavlgQWIQSklqeymfdrpYSRTLEAEADKVGLQLAAKA 402
Cdd:cd07333   102 --------QIEKS----------YSREDEREADQLGLQYLTKA 126
COG4784 COG4784
Putative Zn-dependent protease [General function prediction only];
277-402 9.13e-15

Putative Zn-dependent protease [General function prediction only];


Pssm-ID: 443814 [Multi-domain]  Cd Length: 488  Bit Score: 76.47  E-value: 9.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 277 SETNWVVHVVDSPAVNAFVLPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKASLVHlldfLGMIFLTMIwa 356
Cdd:COG4784    85 PDLPYTFTVLDSPVVNAFALPGGYVYVTRGLLALANDEAELAAVLGHEIGHVTARHAVQRQSRAT----AAQIGLGRV-- 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907156973 357 ICPRDSLAVLGQWIQSKLQEYMfdRPYSRTLEAEADKVGLQLAAKA 402
Cdd:COG4784   159 LSPVLGSAQAGQLAGAGAQLLL--ASFSRDQELEADRLGVRYLARA 202
M48C_Oma1_like cd07332
Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C ...
 283-402 7.41e-14

Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.


Pssm-ID: 320691 [Multi-domain]  Cd Length: 222  Bit Score: 70.68  E-value: 7.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 283 VHVVDSPA-VNAFVLPNGQVFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHaaekaSLVHLLDFLGM-IFLTMIWAicpr 360
Cdd:cd07332    69 LHFRDSGIgANAFALPGGTIVVTDGLVELAESPEELAAVLAHEIGHVEHRH-----SLRQLIRSSGLsLLVSLLTG---- 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907156973 361 DSLAVLGQWIQskLQEYMFDRPYSRTLEAEADKVGLQLAAKA 402
Cdd:cd07332   140 DVSGLSDLLAG--LPALLLSLSYSRDFEREADAFALELLKAA 179
M48C_Oma1_like cd07342
M48C peptidase, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 283-402 2.75e-10

M48C peptidase, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 (also called mitochondrial metalloendopeptidase OMA1) protease homologs that are mostly uncharacterized. Oma1 is part of the quality control system in the inner membrane of mitochondria, with its catalytic site facing the matrix space. It cleaves and thereby promotes the turnover of mistranslated or misfolded membrane proteins. Oma1 can cleave the misfolded multi-pass membrane protein Oxa1, thus exerting a function similar to the ATP-dependent m-AAA protease for quality control of inner membrane proteins; it cleaves a misfolded polytopic membrane protein at multiple sites. It has been proposed that in the absence of m-AAA protease, proteolysis of Oxa1 is mediated by Oma1 in an ATP-independent manner. Oma1 is part of highly conserved mitochondrial metallopeptidases, with homologs present in higher eukaryotes, eubacteria and archaebacteria, all containing the zinc binding motif (HEXXH). It forms a high molecular mass complex in the inner membrane, possibly a homo-hexamer.


Pssm-ID: 320701 [Multi-domain]  Cd Length: 158  Bit Score: 58.81  E-value: 2.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 283 VHVVDSPAVNAFVlpNGQ-VFIFTGLLNSVTDVHQLSFLLGHEIAHAVLGHAAEKaslvhlldflgmifltmiwaicprD 361
Cdd:cd07342    23 VELGNSDGVNAYA--DGRrVQITSGMMDFAQDDDELALVVAHELAHNILGHRDRL------------------------R 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1907156973 362 SLAVLGQWIQSKLQeymfDRPYSRTLEAEADKVGLQLAAKA 402
Cdd:cd07342    77 ANGVAGGLLDGFGG----NAAYSREFEIEADYLGLYLMARA 113
M48C_loiP_like cd07334
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ...
 288-398 4.73e-10

Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase M48 Ste24p protease loiP (formerly yggG)-like family are mostly uncharacterized proteins that include E. coli loiP and ycaLG, considered to be putative metallopeptidases, containing a zinc-binding motif, HEXXH, and a COOH-terminal ER retrieval signal (KKXX). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. LoiP has been shown to be a metallopeptidase that cleaves its targets preferentially between Phe-Phe residues. It is upregulated when bacteria are subjected to media of low osmolarity, thus yggG was named LoiP (low osmolarity induced protease). Proper membrane localization of LoiP may depend on YfgC, another putative metalloprotease in this subfamily.


Pssm-ID: 320693 [Multi-domain]  Cd Length: 215  Bit Score: 59.14  E-value: 4.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 288 SPAVNAFVLPNGQVFIFTGLLNSVTDvHQLSFLLGHEIAHAVLGHAAEKASLVHLLDFLgmifltmiwaicpRDSLA--- 364
Cdd:cd07334    66 TPDVNAFAMADGSVRVYSGLMDMMTD-DELLGVIGHEIGHVKLGHSKKAMKTAYLTSAA-------------RKAAAsas 131

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1907156973 365 -VLGQWIQS---KLQEYMFDRPYSRTLEAEADKVGLQL 398
Cdd:cd07334   132 gTVGALSDSqlgALAEKLINAQFSQKQESEADDYGYKF 169
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 283-405 2.45e-08

Zn-dependent protease with chaperone function [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 54.12  E-value: 2.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 283 VHVVDSPAVNAFV----LPNGQVFIFTGLLNSVTDvHQLSFLLGHEIAHAVLGHAAEK---ASLVHLLDFLGMiFLTMIW 355
Cdd:COG0501    22 VYVMDSPAPNAFAtgrgPNNARIVVTDGLLELLDR-DELEAVLAHELGHIKNGDILLMtlaSGLLGLIGFLAR-LLPLAF 99

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 356 AICPRDSLAV----------LGQWIQSKLqeymfdrpySRTLEAEADKVGLQLAAKALKL 405
Cdd:COG0501   100 GRDRDAGLLLglllgilapfLATLIQLAL---------SRKREYEADRAAAELTGDPDAL 150
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 285-381 2.57e-05

M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 family Ste24p-like proteins that are as yet uncharacterized, but probably function as intracellular, membrane-associated zinc metalloproteases; they all contain the HEXXH Zn-binding motif, which is critical for Ste24p activity. They likely remove the C-terminal three residues of farnesylated proteins proteolytically and are possibly associated with the endoplasmic reticulum and golgi. Some members also contain ankyrin domains which occur in very diverse families of proteins and mediate protein-protein interactions.


Pssm-ID: 320684 [Multi-domain]  Cd Length: 199  Bit Score: 44.91  E-value: 2.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 285 VVDSPAVNAFVL-PNGQVFI--FTGLLNSVTDVhQLSFLLGHEIAHAVLGHAaekasLVHLLDFLGMIFLTMIWAICPRD 361
Cdd:cd07325    36 VYQSPVLNAFALgFEGRPFIvlNSGLVELLDDD-ELRFVIGHELGHIKSGHV-----LYRTLLLLLLLLGELIGILLLSS 109

                          90       100
                  ....*....|....*....|.
gi 1907156973 362 SLAVLGQ-WiqSKLQEYMFDR 381
Cdd:cd07325   110 ALPLALLaW--SRAAEYSADR 128
Peptidase_M48_M56 cd05843
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 282-336 4.55e-04

Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral membrane metallopeptidases; This family contains peptidase M48 (also known as Ste24 peptidase, Ste24p, Ste24 endopeptidase, a-factor converting enzyme, AFC1), M56 (also known as BlaR1 peptidase) as well as a novel family called minigluzincins. Peptidase M48 belongs to Ste24 endopeptidase family. Members of this family include Ste24 protease (peptidase M48A), protease htpX homolog (peptidase M48B), or CAAX prenyl protease 1, and mitochondrial metalloendopeptidase OMA1 (peptidase M48C). They proteolytically remove the C-terminal three residues of farnesylated proteins. They are integral membrane proteins associated with the endoplasmic reticulum and golgi, binding one zinc ion per subunit. In eukaryotes, Ste24p is required for the first NH2-terminal proteolytic processing event within the a-factor precursor, which takes place after COOH-terminal CAAX modification (C is cysteine; A is usually aliphatic; X is one of several amino acids) is complete. The Ste24p contains multiple membrane spans, a zinc metalloprotease motif (HEXXH), and a COOH-terminal ER retrieval signal (KKXX). Mutation studies have shown that the HEXXH protease motif, which is extracellular but adjacent to a transmembrane domain and therefore close to the membrane surface, is critical for Ste24p activity. Ste24p has limited homology to HtpX family of prokaryotic proteins; HtpX proteins, also part of the M48 peptidase family, are smaller and homology is restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins; HtpX then undergoes self-degradation and collaborates with FtsH to eliminate these misfolded proteins. Peptidase M56 includes zinc metalloprotease domain in MecR1 and BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain beta-lactam antibiotics in MRSA. Also included are a novel family of related proteins that consist of the soluble minimal scaffold similar to the catalytic domains of the integral-membrane metallopeptidase M48 and M56, thus called minigluzincins.


Pssm-ID: 320682 [Multi-domain]  Cd Length: 94  Bit Score: 39.36  E-value: 4.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156973 282 VVHVVDSPAVNAFVLP--NGQVFIFTGLLNSVTDvHQLSFLLGHEIAHAVL-GHAAEK 336
Cdd:cd05843    19 KVVVVPGSVPNAFFTGgaNKRVVLTTALLELLSE-EELAAVIAHELGHFKAhEYQADN 75
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 275-393 6.69e-04

Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of peptidase M48 subfamily B includes uncharacterized HtpX homologs and consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX expression is controlled by the Cpx stress response system, which senses abnormal membrane proteins. HtpX participates in the proteolytic quality control of these misfolded proteins by undergoing self-degradation and collaborating with FtsH, a membrane-bound and ATP-dependent protease, to eliminate them. HtpX, a zinc metalloprotease with an active site motif HEXXH, has an FtsH-like topology, and is capable of introducing endoproteolytic cleavages into SecY (also an FtsH substrate). However, HtpX does not have an ATPase activity and will only act against cytoplasmic regions of a target membrane protein. Thus, HtpX and FtsH have overlapping and/or complementary functions, which are especially important at high temperature; in E. coli and Xylella fastidiosa, HtpX is heat-inducible, while in Streptococcus gordonii it is not.


Pssm-ID: 320696 [Multi-domain]  Cd Length: 203  Bit Score: 40.76  E-value: 6.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 275 GISETNWVVHVVDSPAVNAFVLPNGQVFIFTGLLNSvTDVHQLSFLLGHEiahavLGHAAEKASLVHLLDFLgMIFLTMI 354
Cdd:cd07337    53 GPDPEKVKLFISDDEYPNAFALGRNTICVTKGLLDL-LDYEELKGILAHE-----LGHLSHKDTDYLLLIFV-LLLLAAI 125

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907156973 355 WAicprdSLAVLGQWIQSKLQeYMFDrpySRTLEAEADK 393
Cdd:cd07337   126 WT-----KLGTLLIFVWIRLL-VMFS---SRKAEYRADA 155
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 282-361 3.91e-03

Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains peptidase M56, which includes zinc metalloprotease domain in MecR1 as well as BlaR1. MecR1 is a transmembrane beta-lactam sensor/signal transducer protein that regulates the expression of an altered penicillin-binding protein PBP2a, which resists inactivation by beta-lactam antibiotics, in methicillin-resistant Staphylococcus aureus (MRSA). BlaR1 regulates the inducible expression of a class A beta-lactamase that hydrolytically destroys certain beta-lactam antibiotics in MRSA. Both, MecR1 and BlaR1, are transmembrane proteins that consist of four transmembrane helices, a cytoplasmic zinc protease domain, and the soluble C-terminal extracellular sensor domain, and are highly similar in sequence and function. The signal for protein expression is transmitted by site-specific proteolytic cleavage of both the transducer, which auto-activates, and the repressor, which is inactivated, unblocking gene transcription. All members contain the zinc metalloprotease motif (HEXXH). Homologs of this peptidase domain are also found in a number of other bacterial genome sequences, most of which are as yet uncharacterized.


Pssm-ID: 320688 [Multi-domain]  Cd Length: 188  Bit Score: 38.59  E-value: 3.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156973 282 VVHVVDSPAVNAFVL---PNGQVFIFTGLLNSVTDvHQLSFLLGHEIAHAVLGHAAEKASLVHLLDFLGMIFLTMIWAIC 358
Cdd:cd07329    13 RVYVVDSDVPNAFAVgrsRGPTVVVTTGLLDLLDD-DELEAVLAHELAHLKRRDVLVLLLFDPLLLLVVGLLLFLSLFIF 91


                  ...
gi 1907156973 359 PRD 361
Cdd:cd07329    92 ELL 94
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH