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Conserved domains on  [gi|568928945|ref|XP_006503082|]
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CAAX prenyl protease 1 homolog isoform X1 [Mus musculus]

Protein Classification

M48 family metallopeptidase( domain architecture ID 11574938)

M48 family metallopeptidase similar to CAAX prenyl protease 1 which proteolytically removes the C-terminal three residues of farnesylated A-factor mating pheromone

CATH:  3.30.2010.10
EC:  3.4.24.-
Gene Ontology:  GO:0004222|GO:0046872|GO:0006508
PubMed:  26527717|7583637|8860988
SCOP:  4004609

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M48A_Zmpste24p_like cd07343
Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family ...
 22-490 0e+00

Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family M48 subfamily A which includes a number of well-characterized genes such as those found in humans (ZMPSTE24, also known as farnesylated protein-converting enzyme 1 or FACE-1 or Hs Ste24), Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24) and yeast (Ste24p). Ste24p contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. Ste24p is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes, while mutations in this gene or in that encoding its substrate, prelamin A, result in a series of human inherited diseases known as laminopathies, the most severe of which are Hutchinson Gilford progeria syndrome (HGPS) and restrictive dermopathy (RD) which arise due to unsuccessful maturation of prelamin A. Two forms of mandibuloacral dysplasia, a condition that causes a variety of abnormalities involving bone development, skin pigmentation, and fat distribution, are caused by mutations in two different genes; mutations in the LMNA gene, which normally provides instructions for making lamin A and lamin C, cause mandibuloacral dysplasia with A-type lipodystrophy (MAD-A), and mutations in the ZMPSTE24 gene cause mandibuloacral dysplasia with B-type lipodystrophy (MAD-B). Within cells, these genes are involved in maintaining the structure of the nucleus and may play a role in many cellular processes. Certain HIV protease inhibitors have been shown to inhibit the enzymatic activity of ZMPSTE24, but not enzymes involved in prelamin A processing.


:

Pssm-ID: 320702 [Multi-domain]  Cd Length: 405  Bit Score: 519.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945  22 AVLLFSWTVYLWETFLAQRQRRIYKTTTRVPAELEQIMDSDTFEKSRLYQLDKSTFSFWSGLYSEVEgtdssfpdhrrse 101
Cdd:cd07343    2 IILLLLVLVYLFELYLSLRQLRHLKRKLPPPPELADVISQEEFEKAQAYSLDKSRFSIVSSLLSLLL------------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 102 spilfhSLFILLFGGIPYLWRLsgqfcssAGFGPEYEIIQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNHQTLEF 181
Cdd:cd07343   69 ------LLLLLLFGLLPLLDLL-------LRSLGGNEILQSLLFFLLLSLISTLLSLPFSLYSTFVIEEKFGFNKQTLGL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 182 FMKDAIKKFIVTQCILLPVSALLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKQEIEVMA 261
Cdd:cd07343  136 FIKDLLKSLLLSLVLGGPLLALLLWIIKKFGKYWWLYAWLFVVVFSLLLMFIYPTLIAPLFNKFTPLEDGELKTKIEALA 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 262 KSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSvpnkdnqeesgmearnegegdseevkakvknkkq 341
Cdd:cd07343  216 KRAGFPLKKVYVMDGSKRSTHSNAYFTGFGKNKRIVLFDTLLEQLT---------------------------------- 261

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 342 gckNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRRELFAAFGFydSQPTLIGLLIIFQFIFSPYNEV 421
Cdd:cd07343  262 ---EDEILAVLAHELGHWKHGHILKGLILSQLLLFLGFYLFGLLLNNPSLYRAFGF--FGPSDQPALIGFLLLLSPLSFL 336

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568928945 422 LSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSTWHYSHPPLLERLQALKN 490
Cdd:cd07343  337 LSPLMNALSRKFEYEADAFAVELGYGEALISALVKLSKDNLSNLTPDPLYSAFHYSHPPLLERIAALEK 405
 
Name Accession Description Interval E-value
M48A_Zmpste24p_like cd07343
Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family ...
 22-490 0e+00

Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family M48 subfamily A which includes a number of well-characterized genes such as those found in humans (ZMPSTE24, also known as farnesylated protein-converting enzyme 1 or FACE-1 or Hs Ste24), Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24) and yeast (Ste24p). Ste24p contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. Ste24p is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes, while mutations in this gene or in that encoding its substrate, prelamin A, result in a series of human inherited diseases known as laminopathies, the most severe of which are Hutchinson Gilford progeria syndrome (HGPS) and restrictive dermopathy (RD) which arise due to unsuccessful maturation of prelamin A. Two forms of mandibuloacral dysplasia, a condition that causes a variety of abnormalities involving bone development, skin pigmentation, and fat distribution, are caused by mutations in two different genes; mutations in the LMNA gene, which normally provides instructions for making lamin A and lamin C, cause mandibuloacral dysplasia with A-type lipodystrophy (MAD-A), and mutations in the ZMPSTE24 gene cause mandibuloacral dysplasia with B-type lipodystrophy (MAD-B). Within cells, these genes are involved in maintaining the structure of the nucleus and may play a role in many cellular processes. Certain HIV protease inhibitors have been shown to inhibit the enzymatic activity of ZMPSTE24, but not enzymes involved in prelamin A processing.


Pssm-ID: 320702 [Multi-domain]  Cd Length: 405  Bit Score: 519.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945  22 AVLLFSWTVYLWETFLAQRQRRIYKTTTRVPAELEQIMDSDTFEKSRLYQLDKSTFSFWSGLYSEVEgtdssfpdhrrse 101
Cdd:cd07343    2 IILLLLVLVYLFELYLSLRQLRHLKRKLPPPPELADVISQEEFEKAQAYSLDKSRFSIVSSLLSLLL------------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 102 spilfhSLFILLFGGIPYLWRLsgqfcssAGFGPEYEIIQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNHQTLEF 181
Cdd:cd07343   69 ------LLLLLLFGLLPLLDLL-------LRSLGGNEILQSLLFFLLLSLISTLLSLPFSLYSTFVIEEKFGFNKQTLGL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 182 FMKDAIKKFIVTQCILLPVSALLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKQEIEVMA 261
Cdd:cd07343  136 FIKDLLKSLLLSLVLGGPLLALLLWIIKKFGKYWWLYAWLFVVVFSLLLMFIYPTLIAPLFNKFTPLEDGELKTKIEALA 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 262 KSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSvpnkdnqeesgmearnegegdseevkakvknkkq 341
Cdd:cd07343  216 KRAGFPLKKVYVMDGSKRSTHSNAYFTGFGKNKRIVLFDTLLEQLT---------------------------------- 261

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 342 gckNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRRELFAAFGFydSQPTLIGLLIIFQFIFSPYNEV 421
Cdd:cd07343  262 ---EDEILAVLAHELGHWKHGHILKGLILSQLLLFLGFYLFGLLLNNPSLYRAFGF--FGPSDQPALIGFLLLLSPLSFL 336

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568928945 422 LSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSTWHYSHPPLLERLQALKN 490
Cdd:cd07343  337 LSPLMNALSRKFEYEADAFAVELGYGEALISALVKLSKDNLSNLTPDPLYSAFHYSHPPLLERIAALEK 405
Peptidase_M48_N pfam16491
CAAX prenyl protease N-terminal, five membrane helices; The five N-terminal five transmembrane ...
 41-244 2.75e-67

CAAX prenyl protease N-terminal, five membrane helices; The five N-terminal five transmembrane alpha-helices of peptidase_M48 family proteins including the CAAX prenyl proteases reside completely within the membrane of the endoplasmic reticulum.


Pssm-ID: 465138  Cd Length: 179  Bit Score: 213.89  E-value: 2.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945   41 QRRIYKTTTRVPAELEQIMDSDTFEKSRLYQLDKSTFSFWSGLYSEVEgtdssfpdhrrsespilfhSLFILLFGGIPYL 120
Cdd:pfam16491   1 QYRHLKRHRDVPEELADIIDQETFQKSQDYTLAKSRFSLVSSLFSLIL-------------------LLAFLLFGGLPWL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945  121 WRLSGQFcssagfGPEYEIIQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNHQTLEFFMKDAIKKFIVTQCILLPV 200
Cdd:pfam16491  62 WNLSGSL------LSESEILQSLAFLLILSLISTLISLPFSLYSTFVIEEKFGFNKQTPKLFITDLLKSLLLSLVLGGPL 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568928945  201 SALLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDK 244
Cdd:pfam16491 136 LAAILWIIQKAGDYFWLYLWLFWLVFQLLLMTIYPTLIAPLFNK 179
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 250-490 1.75e-38

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 139.25  E-value: 1.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 250 EGKLKQEIEVMAKSIDFPLTKVYVVegskRSSHSNAYFYGFFK-NKRIVLFDTLLEEYSVpnkdnqeesgmearnegegd 328
Cdd:COG0501    1 DPELYRLVEELAARAGIPMPEVYVM----DSPAPNAFATGRGPnNARIVVTDGLLELLDR-------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 329 seevkakvknkkqgcknEEVLAVLGHELGHWKLGHTVKNIIISQMNSFlcFFLFAVLIGrrelfAAFGFYDSQPTLIGLL 408
Cdd:COG0501   57 -----------------DELEAVLAHELGHIKNGDILLMTLASGLLGL--IGFLARLLP-----LAFGRDRDAGLLLGLL 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 409 --IIFQFIFSPyneVLSFcltvLSRRFEFQADAFAKKL-GKAKDLYSALIKLNKDNLGFP-------------VSDWLFS 472
Cdd:COG0501  113 lgILAPFLATL---IQLA----LSRKREYEADRAAAELtGDPDALASALRKLAGGNLSIPlrrafpaqahafiINPLKLS 185

                        250
                 ....*....|....*...
gi 568928945 473 TWHYSHPPLLERLQALKN 490
Cdd:COG0501  186 SLFSTHPPLEERIARLRE 203
PRK02391 PRK02391
heat shock protein HtpX; Provisional
 346-488 2.48e-05

heat shock protein HtpX; Provisional


Pssm-ID: 179418 [Multi-domain]  Cd Length: 296  Bit Score: 46.08  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHwklghtVKN--IIISQMNSFLCffLFAVLIGRRELFAA-FGFYDSQPTLIGLLIIfqFIFSPYNEVL 422
Cdd:PRK02391 131 DELEAVLAHELSH------VKNrdVAVMTIASFLS--TIAFLIVRWGFYFGgFGGRGGGGGGGGILVV--ILVSLVVWAI 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 423 SFCLT-VLSRRFEFQADAFAKKL-GKAKDLYSALIKLN-------KDNL----------------GFPVSDwLFSTwhys 477
Cdd:PRK02391 201 SFLLIrALSRYREFAADRGAAIItGRPSALASALMKISgrmdrvpTEDLreaegmnaffiipalsGGSLGR-LFST---- 275

                        170
                 ....*....|.
gi 568928945 478 HPPLLERLQAL 488
Cdd:PRK02391 276 HPPLEKRIAQL 286
 
Name Accession Description Interval E-value
M48A_Zmpste24p_like cd07343
Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family ...
 22-490 0e+00

Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family M48 subfamily A which includes a number of well-characterized genes such as those found in humans (ZMPSTE24, also known as farnesylated protein-converting enzyme 1 or FACE-1 or Hs Ste24), Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24) and yeast (Ste24p). Ste24p contains the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. It is thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether its genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. Ste24p is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes, while mutations in this gene or in that encoding its substrate, prelamin A, result in a series of human inherited diseases known as laminopathies, the most severe of which are Hutchinson Gilford progeria syndrome (HGPS) and restrictive dermopathy (RD) which arise due to unsuccessful maturation of prelamin A. Two forms of mandibuloacral dysplasia, a condition that causes a variety of abnormalities involving bone development, skin pigmentation, and fat distribution, are caused by mutations in two different genes; mutations in the LMNA gene, which normally provides instructions for making lamin A and lamin C, cause mandibuloacral dysplasia with A-type lipodystrophy (MAD-A), and mutations in the ZMPSTE24 gene cause mandibuloacral dysplasia with B-type lipodystrophy (MAD-B). Within cells, these genes are involved in maintaining the structure of the nucleus and may play a role in many cellular processes. Certain HIV protease inhibitors have been shown to inhibit the enzymatic activity of ZMPSTE24, but not enzymes involved in prelamin A processing.


Pssm-ID: 320702 [Multi-domain]  Cd Length: 405  Bit Score: 519.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945  22 AVLLFSWTVYLWETFLAQRQRRIYKTTTRVPAELEQIMDSDTFEKSRLYQLDKSTFSFWSGLYSEVEgtdssfpdhrrse 101
Cdd:cd07343    2 IILLLLVLVYLFELYLSLRQLRHLKRKLPPPPELADVISQEEFEKAQAYSLDKSRFSIVSSLLSLLL------------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 102 spilfhSLFILLFGGIPYLWRLsgqfcssAGFGPEYEIIQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNHQTLEF 181
Cdd:cd07343   69 ------LLLLLLFGLLPLLDLL-------LRSLGGNEILQSLLFFLLLSLISTLLSLPFSLYSTFVIEEKFGFNKQTLGL 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 182 FMKDAIKKFIVTQCILLPVSALLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDKFTPLPEGKLKQEIEVMA 261
Cdd:cd07343  136 FIKDLLKSLLLSLVLGGPLLALLLWIIKKFGKYWWLYAWLFVVVFSLLLMFIYPTLIAPLFNKFTPLEDGELKTKIEALA 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 262 KSIDFPLTKVYVVEGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSvpnkdnqeesgmearnegegdseevkakvknkkq 341
Cdd:cd07343  216 KRAGFPLKKVYVMDGSKRSTHSNAYFTGFGKNKRIVLFDTLLEQLT---------------------------------- 261

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 342 gckNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLFAVLIGRRELFAAFGFydSQPTLIGLLIIFQFIFSPYNEV 421
Cdd:cd07343  262 ---EDEILAVLAHELGHWKHGHILKGLILSQLLLFLGFYLFGLLLNNPSLYRAFGF--FGPSDQPALIGFLLLLSPLSFL 336

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568928945 422 LSFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLGFPVSDWLFSTWHYSHPPLLERLQALKN 490
Cdd:cd07343  337 LSPLMNALSRKFEYEADAFAVELGYGEALISALVKLSKDNLSNLTPDPLYSAFHYSHPPLLERIAALEK 405
M48A_Ste24p cd07330
Peptidase M48 CaaX prenyl protease type 1, an integral membrane, Zn-dependent protein; This ...
 137-489 2.39e-100

Peptidase M48 CaaX prenyl protease type 1, an integral membrane, Zn-dependent protein; This family of M48 CaaX prenyl protease 1-like family includes a number of well characterized genes such as those found in Taenia solium metacestode (TsSte24p), Arabidopsis (AtSte24), yeast Ste24p and human (Hs Ste24p) as well as several uncharacterized genes such as YhfN, some of which also containing tetratricopeptide (TPR) repeats. All members of this family contain the zinc metalloprotease motif (HEXXH), likely exposed on the cytoplasmic side. They are thought to be intimately associated with the endoplasmic reticulum (ER), regardless of whether their genes possess the conventional signal motif (KKXX) in the C-terminal. Proteins in this family proteolytically remove the C-terminal three residues of farnesylated proteins. The gene ZmpSte24, also known as FACE-1 in humans, a member of this family, is involved in the post-translational processing of prelamin A to mature lamin A, a major component of the nuclear envelope. ZmpSte24 deficiency causes an accumulation of prelamin A leading to lipodystrophy and other disease phenotypes while mutations in the protein lead to diseases of lamin processing (laminopathies), such as premature aging disease progeria and metabolic disorders. Some of these mutations map to the peptide-binding site.


Pssm-ID: 320689 [Multi-domain]  Cd Length: 285  Bit Score: 302.83  E-value: 2.39e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 137 YEIIQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNHQTLEFFMKDAIKKFIVTQCILLPVSALLLYIIKIGG---D 213
Cdd:cd07330    1 YPILAALVFLLVFTGLMVLVELPFGWVARFRVEERFGYMRETRSLWSKRTVALLTVGLLVALPVSALLLPFEEPGGgawW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 214 YFFIYAWLFTLVVSLVLVTIYADYIAPLFDkftPLPEGKLKQEIEVMAKSIDF---PLTKVYVVEGSKRssHSNAYFYGF 290
Cdd:cd07330   81 LGEWLAWLFYLFWRWKLSPFYAQFWKRRSR---PLANGELRERIESMMNREGFgcaEILKVELSGGSMI--HANAYFPGS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 291 FKNKRIVLFDTLLEEYsvpnkdnqeesgmearnegegdseevkakvknkkqgCKNEEVLAVLGHELGHWKLGHTVKNIII 370
Cdd:cd07330  156 GKRRRVVVFADALVSL------------------------------------MTPDELLAVIAHELGHVKHHHHLFRLAA 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 371 SQMNSFLCFFLFavligrrelfaafgfydsqptliglliifqfifsPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDL 450
Cdd:cd07330  200 SQAVSFIVCALF----------------------------------ILIYPLRFLLNFFARRFEYQADAYAAKLAGADAL 245

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 568928945 451 YSALIKLNKDNLGFPVSDWLFSTWHYSHPPLLERLQALK 489
Cdd:cd07330  246 ISALVKLHRDNLTTLTPSRLYSLWHYSHPHAAMRVAHLL 284
Peptidase_M48_N pfam16491
CAAX prenyl protease N-terminal, five membrane helices; The five N-terminal five transmembrane ...
 41-244 2.75e-67

CAAX prenyl protease N-terminal, five membrane helices; The five N-terminal five transmembrane alpha-helices of peptidase_M48 family proteins including the CAAX prenyl proteases reside completely within the membrane of the endoplasmic reticulum.


Pssm-ID: 465138  Cd Length: 179  Bit Score: 213.89  E-value: 2.75e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945   41 QRRIYKTTTRVPAELEQIMDSDTFEKSRLYQLDKSTFSFWSGLYSEVEgtdssfpdhrrsespilfhSLFILLFGGIPYL 120
Cdd:pfam16491   1 QYRHLKRHRDVPEELADIIDQETFQKSQDYTLAKSRFSLVSSLFSLIL-------------------LLAFLLFGGLPWL 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945  121 WRLSGQFcssagfGPEYEIIQSLVFLLLATLFSALTGLPWSLYNTFVIEEKHGFNHQTLEFFMKDAIKKFIVTQCILLPV 200
Cdd:pfam16491  62 WNLSGSL------LSESEILQSLAFLLILSLISTLISLPFSLYSTFVIEEKFGFNKQTPKLFITDLLKSLLLSLVLGGPL 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568928945  201 SALLLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYADYIAPLFDK 244
Cdd:pfam16491 136 LAAILWIIQKAGDYFWLYLWLFWLVFQLLLMTIYPTLIAPLFNK 179
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 247-490 1.03e-59

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: 194.96  E-value: 1.03e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945  247 PLPEGKLKQEIEVMAKSIDFPLTKVYVVeGSKRSSHSNAYFYGFFKNKRIVLFDTLLEEYSvpnkdnqeesgmearnege 326
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYVV-VIKSSPVPNAFAYGLLPGGRVVVTTGLLDLLE------------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945  327 gdseevkakvknkkqgcKNEEVLAVLGHELGHWKLGHTVKNIIISQMNSFLCFFLF-AVLIGRRELFAAFGfydsqptli 405
Cdd:pfam01435  61 -----------------TEDELAAVLGHEIGHIKARHSVESLSIMGGLSLAQLFLAlLLLGAAASGFANFG--------- 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945  406 gllIIFQFIFSPYNEVLSFCLTVLSRRFEFQADAFAKKLGKAKDLY-SALIKLN--KDNLGFPVSDWLFSTWHYSHPPLL 482
Cdd:pfam01435 115 ---IIFLLLIGPLAALLTLLLLPYSRAQEYEADRLGAELMARAGYDpRALIKLWgeIDNNGRASDGALYPELLSTHPSLV 191


                  ....*...
gi 568928945  483 ERLQALKN 490
Cdd:pfam01435 192 ERIAALRE 199
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 250-490 1.75e-38

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 139.25  E-value: 1.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 250 EGKLKQEIEVMAKSIDFPLTKVYVVegskRSSHSNAYFYGFFK-NKRIVLFDTLLEEYSVpnkdnqeesgmearnegegd 328
Cdd:COG0501    1 DPELYRLVEELAARAGIPMPEVYVM----DSPAPNAFATGRGPnNARIVVTDGLLELLDR-------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 329 seevkakvknkkqgcknEEVLAVLGHELGHWKLGHTVKNIIISQMNSFlcFFLFAVLIGrrelfAAFGFYDSQPTLIGLL 408
Cdd:COG0501   57 -----------------DELEAVLAHELGHIKNGDILLMTLASGLLGL--IGFLARLLP-----LAFGRDRDAGLLLGLL 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 409 --IIFQFIFSPyneVLSFcltvLSRRFEFQADAFAKKL-GKAKDLYSALIKLNKDNLGFP-------------VSDWLFS 472
Cdd:COG0501  113 lgILAPFLATL---IQLA----LSRKREYEADRAAAELtGDPDALASALRKLAGGNLSIPlrrafpaqahafiINPLKLS 185

                        250
                 ....*....|....*...
gi 568928945 473 TWHYSHPPLLERLQALKN 490
Cdd:COG0501  186 SLFSTHPPLEERIARLRE 203
M48A_Ste24p-like cd07345
Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase ...
 111-491 1.04e-14

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.


Pssm-ID: 320704 [Multi-domain]  Cd Length: 346  Bit Score: 75.39  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 111 ILLFGGIPYLWRLSGQFCSSAGFGPeyeiIQSLVFLLLATLFSALTGLPWSLYntFVIEEKHGFNHQTLEFFMKDAIKKF 190
Cdd:cd07345    6 LLLFAIDIYALDLKYYLSFIPLFGS----SPTLLALLFLLLFLLLLLLVWYAA--YPVYKKLFSGLESRRAYVLSNLRFL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 191 IVtqcILLP---VSAL--LLYIIKIGGDYFFIYAWLFTLVVSLVLVTIYAdYIAPLFDKF----TPLPEGKLKQEIEVMA 261
Cdd:cd07345   80 LP---ILLPwllLSLLqdLLSLLPLAILKNLLSSSLGLLGFLLLFLLLLL-LFPPLLIRLiwgcKPLPPGPLRDRLEAFC 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 262 KSIDFPLTKVYVVEgSKRSSHSNAYFYGFFKNKRIVLF-DTLLEEYSVpnkdnqeesgmearnegegdseevkakvknkk 340
Cdd:cd07345  156 RRAGFKVADILVWP-LFEGRVATAGVMGILPRFRYILItDALLDSLSP-------------------------------- 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 341 qgcknEEVLAVLGHELGHWKLGHTVKNIIIsqmnsFLCFFLFAVLIG--RRELFAAFGFYDSQPTLIGLLIIFQFIFSpy 418
Cdd:cd07345  203 -----EELEAVLAHEIGHVKKRHLLLYLLF-----FLGFILLLALLSllLSLLLLLLLPLLILLLGSSAEILLTLLLA-- 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 419 neVLSFCLTVL---------SRRFEFQADAFA-KKLGKAKDLYSALIKLNKDNLGfpvsDWLFSTWHysHPPLLERLQAL 488
Cdd:cd07345  271 --LPLLLLLVLyfrfvfgffSRNFERQADLYAlRALGSAEPLISALEKIAELSGN----SRDKPSWH--HFSIAQRIAFL 342


                 ...
gi 568928945 489 KNA 491
Cdd:cd07345  343 EKC 345
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 346-490 1.08e-13

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: 69.65  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHWKLGHTVKNIIIsqmnsflcfFLFAVLIgrrelfAAFgfydsqpTLIGLLIIFQFIFspynevlsfc 425
Cdd:cd07337   92 EELKGILAHELGHLSHKDTDYLLLI---------FVLLLLA------AIW-------TKLGTLLIFVWIR---------- 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568928945 426 LTVL--SRRFEFQADAFAKKLGKAKDLYSALIKLNKDNlgfPVSDWLFSTWHYSHPPLLERLQALKN 490
Cdd:cd07337  140 LLVMfsSRKAEYRADAFAVKIGYGEGLRSALDQLREYE---DAPKGFLAALYSTHPPTEKRIERLEE 203
M48B_HtpX_like cd07335
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains ...
 345-489 2.72e-13

Peptidase M48 subfamily B 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.


Pssm-ID: 320694 [Multi-domain]  Cd Length: 240  Bit Score: 69.53  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 345 NEEVLAVLGHELGHWKLGHTVKNIII-SQMNSFLcfFLFAVLIGRRELFAAFGFYDSQPTLIGLL-IIFQFIFSpynEVL 422
Cdd:cd07335   88 EDEVEAVLAHEISHIANGDMVTMTLLqGVVNTFV--IFLSRIIALIIDSFLSGDENGSGIGYFLVvIVLEIVLG---ILA 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 423 SFCLTVLSRRFEFQADAFAKKLGKAKDLYSALIKLN-------------KDNLGFPVSDW--LFSTwhysHPPLLERLQA 487
Cdd:cd07335  163 SLVVMWFSRKREFRADAGGAKLTGKEKMIAALERLKqiserpeseddvaAAIKISRGSGFlrLFST----HPPLEERIAA 238


                 ..
gi 568928945 488 LK 489
Cdd:cd07335  239 LE 240
Peptidase_M48_M56 cd05843
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 253-458 3.15e-13

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: 65.55  E-value: 3.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 253 LKQEIEVMAKSID-FPLTKVYVVEGSkrssHSNAYFYGFFkNKRIVLFDTLLEEYSvpnkdnqeesgmearnegegdsee 331
Cdd:cd05843    1 LKKIRQEILLSAGaFPLDKVVVVPGS----VPNAFFTGGA-NKRVVLTTALLELLS------------------------ 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 332 vkakvknkkqgckNEEVLAVLGHELGHWKLghtvkniiisqmnsflcfflfavligrrelfaafgfydsqptliglliif 411
Cdd:cd05843   52 -------------EEELAAVIAHELGHFKA-------------------------------------------------- 68

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 568928945 412 qfifspynevlsfcltvlsrrFEFQADAFAKKLGKAKDLYSALIKLN 458
Cdd:cd05843   69 ---------------------HEYQADNVGARLFGKNELDAALLKLI 94
M48C_Oma1_like cd07332
Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C ...
 346-490 3.53e-10

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: 59.89  E-value: 3.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHWKLGHTVKNIIisqmNSFLCFFLFAVLIGRrelfaAFGFYDSQPTLIGLLIifqfifspyneVLSFc 425
Cdd:cd07332  102 EELAAVLAHEIGHVEHRHSLRQLI----RSSGLSLLVSLLTGD-----VSGLSDLLAGLPALLL-----------SLSY- 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568928945 426 ltvlSRRFEFQADAFA-KKLGKA----KDLYSALIKLNKDNLGFP-VSDWLfSTwhysHPPLLERLQALKN 490
Cdd:cd07332  161 ----SRDFEREADAFAlELLKAAgispEGLADFFERLEEEHGDGGsLPEWL-ST----HPDTEERIEAIRE 222
M48B_HtpX_like cd07338
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 346-488 1.83e-08

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: 320697 [Multi-domain]  Cd Length: 216  Bit Score: 54.89  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHWKlgHtvKNIIISQMNSFL---CFFLFAVLI--GRRELFAAFGFYDsqpTLIGL-LIIFQFIFspYN 419
Cdd:cd07338   88 DELEAVIGHELGHIK--H--RDVAIMTAIGLIpsiIYYIGRSLLfsGGSSGGRNGGGAL---LAVGIaAFAVYFLF--QL 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 420 EVLSFcltvlSRRFEFQADAFAKKL-GKAKDLYSALIKLnkdNLGFPVSdwLFSTwhysHPPLLERLQAL 488
Cdd:cd07338  159 LVLGF-----SRLREYYADAHSAKVtGNGRALQSALAKI---AYGYLAE--IFST----HPLPAKRIQAL 214
M48B_Htpx_like cd07340
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 346-489 2.44e-08

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: 320699 [Multi-domain]  Cd Length: 246  Bit Score: 54.81  E-value: 2.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHWKLGHTVKNIIISqmnSFLCFFLFAVLIGRRELFAAFGFYDS--------QPTLIGLLIIFQfIFSP 417
Cdd:cd07340   84 DELEGVIAHELSHIKNYDIRLMTIAV---VLVGIIALIADLALRSFFYGGGSRRRrrdgggggALILLILGLVLI-ILAP 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 418 ynevlsFCLTV----LSRRFEFQADAFAKKLGKAKD-LYSALIKLNKD--------------NLGFPVSDW------LFS 472
Cdd:cd07340  160 ------IFAQLiqlaISRQREYLADASAVELTRNPEgLISALEKISGDssplkvansatahlNLYFPNPGKkssfssLFS 233

                        170
                 ....*....|....*..
gi 568928945 473 TwhysHPPLLERLQALK 489
Cdd:cd07340  234 T----HPPIEERIKRLR 246
M48C_loiP_like cd07334
Peptidase M48C Ste24p loiP-like, integral membrane protein; This subfamily contains peptidase ...
 346-491 9.63e-08

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: 52.59  E-value: 9.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHWKLGHTVKNIIISQMNSFLcfflfavligRRELFAAFG----FYDSQ-PTLIGLLIIFQFifspyne 420
Cdd:cd07334   92 DELLGVIGHEIGHVKLGHSKKAMKTAYLTSAA----------RKAAASASGtvgaLSDSQlGALAEKLINAQF------- 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568928945 421 vlsfcltvlSRRFEFQADAFA----KKLGK-AKDLYSALIKLNKDNLGFPVSdwLFStwhySHPPLLERLQALKNA 491
Cdd:cd07334  155 ---------SQKQESEADDYGykflKKNGYnPQAAVSALEKLAALSGGGKSS--LFS----SHPDPAKRAERIRAR 215
M48B_HtpX_like cd07339
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 347-488 1.39e-07

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: 320698 [Multi-domain]  Cd Length: 229  Bit Score: 52.18  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 347 EVLAVLGHELGHwkLGH---TVKNI--IISQMNSFLCFFLFAVLIGRRELFAAFGfyDSQPTLIGLLIIFqfifSPyneV 421
Cdd:cd07339   84 ELAGVLAHEVSH--IRNgdlRVMGLadLISRLTSLLSLLGQLLLLLNLPLLLLGE--VTISWLAILLLIL----AP---T 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568928945 422 LSFCLT-VLSRRFEFQADAFAKKL-GKAKDLYSALIKLNKDNlGFPVSDWLFSTWHY-------SHPPLLERLQAL 488
Cdd:cd07339  153 LSTLLQlALSRTREFDADLDAARLtGDPEGLASALAKLERYQ-GGWWERLLLPGRRVpepsllrTHPPTEERIRRL 227
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 271-490 3.29e-07

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: 50.69  E-value: 3.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 271 VYVVEgskrSSHSNAYFYGFFKNKRIVLFDTLLEEYSvpnkdnqeesgmearnegegdseevkakvknkkqgckNEEVLA 350
Cdd:cd07325   34 LYVYQ----SPVLNAFALGFEGRPFIVLNSGLVELLD-------------------------------------DDELRF 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 351 VLGHELGHWKLGHTVKNIIISQMnsflcfFLFAVLIGRRELFAAfgfydsqptliglliiFQFIFSPYnevlsfcltvlS 430
Cdd:cd07325   73 VIGHELGHIKSGHVLYRTLLLLL------LLLGELIGILLLSSA----------------LPLALLAW-----------S 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 431 RRFEFQADAFAkkL---GKAKDLYSALIKL--------NKDNLGF--------PVSDWLF---STWHYSHPPLLERLQAL 488
Cdd:cd07325  120 RAAEYSADRAG--LlvcQDPEAAIRALMKLaggskllkDVNNIEYfleeeaqaDALDGFFkwlSELLSTHPFLVKRAAEL 197


                 ..
gi 568928945 489 KN 490
Cdd:cd07325  198 LR 199
M48B_HtpX_like cd07336
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 346-490 8.13e-07

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: 320695 [Multi-domain]  Cd Length: 266  Bit Score: 50.57  E-value: 8.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHwklghtVKN--IIISQMN-------SFLCFFLFAVLIgrrelFAAFGFYDSQPTLIGLLIIfqFIFS 416
Cdd:cd07336  110 DELEGVLAHELAH------IKNrdILISTIAatiagaiSMLANMAQWGAI-----FGGRGGRDRGGNPIGALLL--AILA 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 417 PyneVLSFCL-TVLSRRFEFQADAFAKKL-GKAKDLYSALIKLNKDNLGFPVSDW--------------------LFSTw 474
Cdd:cd07336  177 P---IAATLIqLAISRSREYLADETGARIsGNPLALASALEKLERGAQRHPPMEAnpatahlfivnplsggglakLFST- 252

                        170
                 ....*....|....*.
gi 568928945 475 hysHPPLLERLQALKN 490
Cdd:cd07336  253 ---HPPTEERIARLRA 265
M48B_HtpX_like cd07327
HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, ...
 346-489 1.16e-06

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.


Pssm-ID: 320686 [Multi-domain]  Cd Length: 183  Bit Score: 48.79  E-value: 1.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHwklghtVKNiiisqmnsflcfflfavligrrelfaafgfYDsqptliglliifqfifspyneVLSFC 425
Cdd:cd07327   79 DELEAVLAHELSH------IKN------------------------------RD---------------------VLVMT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 426 LTVLSRRFEFQADAFAKKL-GKAKDLYSALIKL--------------NKDNLGFPVSD-------WLFSTwhysHPPLLE 483
Cdd:cd07327  102 LASLSRYREFAADRGSAKLtGDPLALASALMKIsgsmqripkrdlrqVEASAFFIIPPlsggslaELFST----HPPTEK 177


                 ....*.
gi 568928945 484 RLQALK 489
Cdd:cd07327  178 RIERLR 183
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 346-488 1.43e-06

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: 48.60  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHWKLGHTVKNIIISQmnsflcffLFAVLIGRRELFAAFGFYDSQPTLIGLLIIFQFIFSPYNEVLSFc 425
Cdd:cd07329   48 DELEAVLAHELAHLKRRDVLVLLLFDP--------LLLLVVGLLLFLSLFIFELLGFFFQPLLFLAFFALLRLAELLAD- 118

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568928945 426 ltVLSRRFEFQADAfAKKLGKAKDLYSALIKL--------NKDNLGFPVSDWLFSTWHYSHPPLLERLQAL 488
Cdd:cd07329  119 --ALAVARTSAARR-ARLTGLPAALASALEKIedasdralEAGLVLPALAADASSLEKTDHPPLEERVERL 186
M48_Ste24p_like cd07328
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 346-489 2.59e-06

M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains peptidase M48-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.


Pssm-ID: 320687 [Multi-domain]  Cd Length: 160  Bit Score: 47.55  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHWKLGHTvkniiisqmnsflcfflfavligrrelfaAFGFYdsqptliglliifqfifspynevlsfc 425
Cdd:cd07328   83 EELRAVLAHELGHFANGDT-----------------------------RLGAW--------------------------- 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568928945 426 ltVLSRRFEFQADAFAKKLGKAKDLYSALIKLNKDNLgfpvsdwlfSTWHYSHPPLLERLQALK 489
Cdd:cd07328  107 --ILSRRAEYEADRVAARVAGSAAAASALRKLAARRP---------SSPDDTHPPLAERLAALG 159
PRK02391 PRK02391
heat shock protein HtpX; Provisional
 346-488 2.48e-05

heat shock protein HtpX; Provisional


Pssm-ID: 179418 [Multi-domain]  Cd Length: 296  Bit Score: 46.08  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHwklghtVKN--IIISQMNSFLCffLFAVLIGRRELFAA-FGFYDSQPTLIGLLIIfqFIFSPYNEVL 422
Cdd:PRK02391 131 DELEAVLAHELSH------VKNrdVAVMTIASFLS--TIAFLIVRWGFYFGgFGGRGGGGGGGGILVV--ILVSLVVWAI 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 423 SFCLT-VLSRRFEFQADAFAKKL-GKAKDLYSALIKLN-------KDNL----------------GFPVSDwLFSTwhys 477
Cdd:PRK02391 201 SFLLIrALSRYREFAADRGAAIItGRPSALASALMKISgrmdrvpTEDLreaegmnaffiipalsGGSLGR-LFST---- 275

                        170
                 ....*....|.
gi 568928945 478 HPPLLERLQAL 488
Cdd:PRK02391 276 HPPLEKRIAQL 286
M48C_Oma1_like cd07331
Peptidase M48C, integral membrane endopeptidase; This subfamily contains peptidase M48C Oma1 ...
 343-490 5.14e-05

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: 44.10  E-value: 5.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 343 CKNEEVLA-VLGHELGHWKLGHTVKNIiisqmnSFLCFFLFAVLIGrreLFAAFGFYDSQPTLIGLLIIFQFIFSPYnev 421
Cdd:cd07331   54 AKNDDELAaVLGHEIAHALARHSAERM------SQQKLLQLLLLLL---LAALGASLAGLALGLLGLGAQLGLLLPY--- 121

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568928945 422 lsfcltvlSRRFEFQADafakKLG---KAK---DLYSALI---KLNKDNLGFPVSDWLfSTwhysHPPLLERLQALKN 490
Cdd:cd07331  122 --------SRKQELEAD----RIGlqlMAKagyDPRAAVTfweKMAAAEGGGKPPEFL-ST----HPSSETRIEALEE 182
PRK03982 PRK03982
heat shock protein HtpX; Provisional
 346-489 1.27e-03

heat shock protein HtpX; Provisional


Pssm-ID: 235186 [Multi-domain]  Cd Length: 288  Bit Score: 40.76  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 346 EEVLAVLGHELGHWK----LGHTVKNII---ISQMNSFLCFFLFAVLIGRRElfaafgfyDSQPTLIGLLIIfqFIFSPY 418
Cdd:PRK03982 123 DELEGVIAHELTHIKnrdtLIQTIAATLagaIMYLAQWLSWGLWFGGGGRDD--------RNGGNPIGSLLL--IILAPI 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 419 NE-VLSFcltVLSRRFEFQADAFAKKL-GKAKDLYSALIKLNK---------DNLGF--------PVSDW---LFSTwhy 476
Cdd:PRK03982 193 AAtLIQF---AISRQREFSADEGGARLtGNPLALANALQKLEKgvryiplknGNPATahmfiinpFRGQFlanLFST--- 266

                        170
                 ....*....|...
gi 568928945 477 sHPPLLERLQALK 489
Cdd:PRK03982 267 -HPPTEERIERLL 278
M48C_Oma1-like cd07324
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ...
 343-490 2.22e-03

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: 38.31  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568928945 343 CKNEEVLA-VLGHELGHWKLGHTVKniiisQMNSFlcfflfavligrrelfaafgfydsqptliglliifqfifspynev 421
Cdd:cd07324   50 LESEDELAaVLAHEIGHVTLRHIAR-----QLERY--------------------------------------------- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568928945 422 lsfcltvlSRRFEFQADAFAKKL--------GKAKDLYSALIKLNKDNLGFPVSdwLFSTwhysHPPLLERLQALKN 490
Cdd:cd07324   80 --------SRDQEREADRLGLQLlaragydpRGMARFFERLARQEGLSGSRLPE--FLST----HPLTAERIAALRA 142
 
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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