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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 264 GISWEVLVVNEPIVNAFCLPAGKIVVFTGLLNHFKSDAEVATVIGHEVGHAVARHVAEGITKNLWFAILQLVL------- 336
Cdd:cd07331   21 GWDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSAERMSQQKLLQLLLLLLlaalgas 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 337 YQFVMPDLVNTMSALFLRLPFSRKMEIEADYIGLLLLASAGYDPRVAPTVYEKLGKL-GGDALGDYLSTHPSGKKR---- 411
Cdd:cd07331  101 LAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKAGYDPRAAVTFWEKMAAAeGGGKPPEFLSTHPSSETRieal 180

                 ....*..
gi 332008738 412 SKLLAQA 418
Cdd:cd07331  181 EELLPEA 187

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 264 GISWEVLVVNEPIVNAFCLPAGKIVVFTGLLNHFKSDAEVATVIGHEVGHAVARHVAEGITKNLWFAILQLVL------- 336
Cdd:cd07331   21 GWDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSAERMSQQKLLQLLLLLLlaalgas 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 337 YQFVMPDLVNTMSALFLRLPFSRKMEIEADYIGLLLLASAGYDPRVAPTVYEKLGKL-GGDALGDYLSTHPSGKKR---- 411
Cdd:cd07331  101 LAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKAGYDPRAAVTFWEKMAAAeGGGKPPEFLSTHPSSETRieal 180

                 ....*..
gi 332008738 412 SKLLAQA 418
Cdd:cd07331  181 EELLPEA 187

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738  240 LDDQWIQksRKKDSKAHAATSHLEGisWEVLVVNE-PIVNAFC---LPAGKIVVFTGLLNHFKSDAEVATVIGHEVGHAV 315
Cdd:pfam01435   2 LRNAELQ--RVVERLAAAAGLPLPP--WYVVVIKSsPVPNAFAyglLPGGRVVVTTGLLDLLETEDELAAVLGHEIGHIK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738  316 ARHVAEG--ITKNLWFAILQLVLYQF-------------VMPDLVNTMSAL-FLRLPFSRKMEIEADYIGLLLLASAGYD 379
Cdd:pfam01435  78 ARHSVESlsIMGGLSLAQLFLALLLLgaaasgfanfgiiFLLLIGPLAALLtLLLLPYSRAQEYEADRLGAELMARAGYD 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 332008738  380 PRVAPTV---YEKLGKLGGDAL-GDYLSTHPSGKKR 411
Cdd:pfam01435 158 PRALIKLwgeIDNNGRASDGALyPELLSTHPSLVER 193

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 264 GISWEVLVVNEPIVNAFCLPAGKIVVFTGLLNHFKSDAEVATVIGHEVGHAVARHVAEGITKNLWFAILQLVL------- 336
Cdd:cd07331   21 GWDWEVHVIDSPEVNAFVLPGGKIFVFTGLLPVAKNDDELAAVLGHEIAHALARHSAERMSQQKLLQLLLLLLlaalgas 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 337 YQFVMPDLVNTMSALFLRLPFSRKMEIEADYIGLLLLASAGYDPRVAPTVYEKLGKL-GGDALGDYLSTHPSGKKR---- 411
Cdd:cd07331  101 LAGLALGLLGLGAQLGLLLPYSRKQELEADRIGLQLMAKAGYDPRAAVTFWEKMAAAeGGGKPPEFLSTHPSSETRieal 180

                 ....*..
gi 332008738 412 SKLLAQA 418
Cdd:cd07331  181 EELLPEA 187

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 267 WEVLVVNEPIVNAFCLPAGKIVVFTGLLNHFKSDAEVATVIGHEVGHAVARHVAEGITKNlwfailqlvlyqfvmpdlvn 346
Cdd:cd07333   47 YRFFVVNDDSINAFATPGGYIYVNTGLILAADNEAELAGVLAHEIGHVVARHIAKQIEKS-------------------- 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 332008738 347 tmsalflrlpFSRKMEIEADYIGLLLLASAGYDPRVAPTVYEKL---GKLGGDALGDYLSTHPSGKKR 411
Cdd:cd07333  107 ----------YSREDEREADQLGLQYLTKAGYDPRGMVSFFKKLrrkEWFGGSSIPTYLSTHPAPAER 164

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 263 EGISWEVLVVN-EPIVNAFCLPAGKIVVFTGLLNHFKSDAEVATVIGHEVGHAVARHVAEGITKNLwfaILQLVLYQFV- 340
Cdd:cd07332   63 LPYPYRLHFRDsGIGANAFALPGGTIVVTDGLVELAESPEELAAVLAHEIGHVEHRHSLRQLIRSS---GLSLLVSLLTg 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 341 ----MPDLVNTMSALFLRLPFSRKMEIEADYIGLLLLASAGYDPRVAPTVYEKLGKLGGD--ALGDYLSTHPSGKKRSKL 414
Cdd:cd07332  140 dvsgLSDLLAGLPALLLSLSYSRDFEREADAFALELLKAAGISPEGLADFFERLEEEHGDggSLPEWLSTHPDTEERIEA 219

                 ...
gi 332008738 415 LAQ 417
Cdd:cd07332  220 IRE 222

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 268 EVLVVNEPIVNAFClpAGKIV-VFTGLLNHFKSDAEVATVIGHEVGHAVARHvaegITKNLWFAILQLVLYQFVmpdlvn 346
Cdd:cd07342   22 RVELGNSDGVNAYA--DGRRVqITSGMMDFAQDDDELALVVAHELAHNILGH----RDRLRANGVAGGLLDGFG------ 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 332008738 347 tmsalfLRLPFSRKMEIEADYIGLLLLASAGYDPRVAPTVYEKLGKLGGDALGdYLSTHPSGKKRSKLLAQA 418
Cdd:cd07342   90 ------GNAAYSREFEIEADYLGLYLMARAGYDIDGAADFWRRLGASHPVGIG-RAATHPSTAERFAALEKA 154

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 268 EVLVVNEPIVNAFCLPAGK---IVVFTGLLNHFkSDAEVATVIGHEVGHAVARHVaegitknLWFAILQLVLYQFVMPDL 344
Cdd:cd07325   33 ELYVYQSPVLNAFALGFEGrpfIVLNSGLVELL-DDDELRFVIGHELGHIKSGHV-------LYRTLLLLLLLLGELIGI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 345 VNTMSAL-FLRLPFSRKMEIEADYIGLLLLAsagyDPRVAPTVyekLGKLGGdalgdylsthpsGKKRSKllaqaNVMEE 423
Cdd:cd07325  105 LLLSSALpLALLAWSRAAEYSADRAGLLVCQ----DPEAAIRA---LMKLAG------------GSKLLK-----DVNNI 160

                        170
                 ....*....|....
gi 332008738 424 ALMIYREVQAGRTG 437
Cdd:cd07325  161 EYFLEEEAQADALD 174

Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; 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 ?-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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 269 VLVVNEPIVNAFCLP--AGKIVVFTGLLNHFkSDAEVATVIGHEVGHAVARHvaegitkNLWFAILQLvlyqfvmpdlvn 346
Cdd:cd07326   29 VRVVDHDAPLAFCLGgrRPRIVLSTGLLELL-SPEELRAVLAHERAHLRRRD-------PLLLLLASA------------ 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 332008738 347 tMSALFLRLPFSRK--------MEIEAD-----YIGLLLLASA 376
Cdd:cd07326   89 -LARALPFLPLLRRlaaayrllRELAADdaaarRVGPRALASA 130

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 268 EVLVVNEPIVNAFC---LPAGKIVVFT-GLLNHFKSDaEVATVIGHEVGHAVARHVAEGitknLWFAILQLVLYQFVMPD 343
Cdd:cd07338   52 KVGIAEDPIPNAFAygsPLTGARVAVTrGLLDILNRD-ELEAVIGHELGHIKHRDVAIM----TAIGLIPSIIYYIGRSL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 344 LVNTMSALFLR-----------------------LPFSRKMEIEADYIGLLL------LASAgydprvaptvyekLGKLG 394
Cdd:cd07338  127 LFSGGSSGGRNgggallavgiaafavyflfqllvLGFSRLREYYADAHSAKVtgngraLQSA-------------LAKIA 193

                        170       180
                 ....*....|....*....|.
gi 332008738 395 GDALGDYLSTHPSGKKRSKLL 415
Cdd:cd07338  194 YGYLAEIFSTHPLPAKRIQAL 214

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.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 332008738 269 VLVVNEPIVNAFCLP--AGKIVVFTGLLNHFkSDAEVATVIGHEVGHAVAR 317
Cdd:cd05843   20 VVVVPGSVPNAFFTGgaNKRVVLTTALLELL-SEEELAAVIAHELGHFKAH 69

HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, also known as HtpX, which consists of proteins smaller than Ste24p, with homology restricted to the C-terminal half of Ste24p. HtpX, an integral membrane (IM) metallopeptidase, is widespread in bacteria and archaea, and plays a central role in protein quality control by preventing the accumulation of misfolded proteins in the membrane. Its 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 eliminating them by collaborating with FtsH, a membrane-bound and ATP-dependent protease. HtpX contains the zinc binding 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. Mutation studies of HtpX-like M48 metalloprotease from Leptospira interrogans (LA4131) has been shown to result in altered expression of a subset of metal toxicity and stress response genes.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 269 VLVVNEPIVNAFCL---PAGK-IVVFTGLLNHFkSDAEVATVIGHEVGHAVARHVaegitknlwfailqlvlyqfvmpdL 344
Cdd:cd07327   44 VAIVDTPMPNAFATgrnPKNAaVAVTTGLLQLL-NEDELEAVLAHELSHIKNRDV------------------------L 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 345 VNTMSALflrlpfSRKMEIEADYIGLLL------LASA-------------GYDPRVAPTVYEKLGKLGGDALGDYLSTH 405
Cdd:cd07327   99 VMTLASL------SRYREFAADRGSAKLtgdplaLASAlmkisgsmqripkRDLRQVEASAFFIIPPLSGGSLAELFSTH 172

                        170
                 ....*....|
gi 332008738 406 PSGKKRSKLL 415
Cdd:cd07327  173 PPTEKRIERL 182

Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase family M48 subfamily A-like CaaX prenyl protease 1, most of which are uncharacterized. Some of these contain tetratricopeptide (TPR) repeats at the C-terminus. Proteins in this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be possibly associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. These proteins putatively remove the C-terminal three residues of farnesylated proteins proteolytically.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 266 SWEVLvvNEPIVNAF---CLPAGKIVVFT-GLLNHFkSDAEVATVIGHEVGHAVARH-------------VAEGITKNLW 328
Cdd:cd07345  167 VWPLF--EGRVATAGvmgILPRFRYILITdALLDSL-SPEELEAVLAHEIGHVKKRHlllyllfflgfilLLALLSLLLS 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 332008738 329 FAILQLVLYQFVMPD-----LVNTMSALFLRLP-----------FSRKMEIEADyiglLLLASAGYDPRVAPTVYEKLGK 392
Cdd:cd07345  244 LLLLLLLPLLILLLGssaeiLLTLLLALPLLLLlvlyfrfvfgfFSRNFERQAD----LYALRALGSAEPLISALEKIAE 319

                        170       180
                 ....*....|....*....|....*.
gi 332008738 393 LGGDALGDYLSTHPSGKKRSKLLAQA 418
Cdd:cd07345  320 LSGNSRDKPSWHHFSIAQRIAFLEKC 345