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Conserved domains on  [gi|451929005|pdb|4IL3|A]
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Chain A, Ste24p

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 ...
 17-446 1.25e-179

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: 508.17  E-value: 1.25e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       17 LIISAFSIAQFSFESYLTYRQYQKLSETKLP-PVLEDEIDDETFHKSRNYSRAKAKFSIFSDIYNLAQKLVFIKYDFFPK 95
Cdd:cd07343   1 YIILLLLVLVYLFELYLSLRQLRHLKRKLPPpPELADVISQEEFEKAQAYSLDKSRFSIVSSLLSLLLLLLLLLFGLLPL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       96 IWHMAvtlsnavlpvRFHMVSTVAQSLCFLGLLSSMSTLVDLPLSYYSHFVLEEKFGFNKLTVKLWITDMIKSLTLAYAI 175
Cdd:cd07343  81 LDLLL----------RSLGGNEILQSLLFFLLLSLISTLLSLPFSLYSTFVIEEKFGFNKQTLGLFIKDLLKSLLLSLVL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      176 GGPILYLFLKIFDKFPTDFLWYIMVFLFVVQILAMTIIPVFIMPLFNKFTPLEDGELKKSIESLADRVGFPLDKIFVIDG 255
Cdd:cd07343 151 GGPLLALLLWIIKKFGKYWWLYAWLFVVVFSLLLMFIYPTLIAPLFNKFTPLEDGELKTKIEALAKRAGFPLKKVYVMDG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      256 SKRSSHSNAYFTGLpFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIVNMVIFSQLHTFLIFSLFTSIYRNSSFY 335
Cdd:cd07343 231 SKRSTHSNAYFTGF-GKNKRIVLFDTLLEQLTEDEILAVLAHELGHWKHGHILKGLILSQLLLFLGFYLFGLLLNNPSLY 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      336 NTFGFFVeksssgfvdpviTKEFPIIIGFMLFndlLTPLECAMQFIMSLISRTHEYQADAYAKKLGYKQNLCRALIDLQI 415
Cdd:cd07343 310 RAFGFFG------------PSDQPALIGFLLL---LSPLSFLLSPLMNALSRKFEYEADAFAVELGYGEALISALVKLSK 374

                       410       420       430
                ....*....|....*....|....*....|.
4IL3_A      416 KNLSTMNVDPLYSSYHYSHPTLAERLTALDY 446
Cdd:cd07343 375 DNLSNLTPDPLYSAFHYSHPPLLERIAALEK 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 ...
 17-446 1.25e-179

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: 508.17  E-value: 1.25e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       17 LIISAFSIAQFSFESYLTYRQYQKLSETKLP-PVLEDEIDDETFHKSRNYSRAKAKFSIFSDIYNLAQKLVFIKYDFFPK 95
Cdd:cd07343   1 YIILLLLVLVYLFELYLSLRQLRHLKRKLPPpPELADVISQEEFEKAQAYSLDKSRFSIVSSLLSLLLLLLLLLFGLLPL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       96 IWHMAvtlsnavlpvRFHMVSTVAQSLCFLGLLSSMSTLVDLPLSYYSHFVLEEKFGFNKLTVKLWITDMIKSLTLAYAI 175
Cdd:cd07343  81 LDLLL----------RSLGGNEILQSLLFFLLLSLISTLLSLPFSLYSTFVIEEKFGFNKQTLGLFIKDLLKSLLLSLVL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      176 GGPILYLFLKIFDKFPTDFLWYIMVFLFVVQILAMTIIPVFIMPLFNKFTPLEDGELKKSIESLADRVGFPLDKIFVIDG 255
Cdd:cd07343 151 GGPLLALLLWIIKKFGKYWWLYAWLFVVVFSLLLMFIYPTLIAPLFNKFTPLEDGELKTKIEALAKRAGFPLKKVYVMDG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      256 SKRSSHSNAYFTGLpFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIVNMVIFSQLHTFLIFSLFTSIYRNSSFY 335
Cdd:cd07343 231 SKRSTHSNAYFTGF-GKNKRIVLFDTLLEQLTEDEILAVLAHELGHWKHGHILKGLILSQLLLFLGFYLFGLLLNNPSLY 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      336 NTFGFFVeksssgfvdpviTKEFPIIIGFMLFndlLTPLECAMQFIMSLISRTHEYQADAYAKKLGYKQNLCRALIDLQI 415
Cdd:cd07343 310 RAFGFFG------------PSDQPALIGFLLL---LSPLSFLLSPLMNALSRKFEYEADAFAVELGYGEALISALVKLSK 374

                       410       420       430
                ....*....|....*....|....*....|.
4IL3_A      416 KNLSTMNVDPLYSSYHYSHPTLAERLTALDY 446
Cdd:cd07343 375 DNLSNLTPDPLYSAFHYSHPPLLERIAALEK 405
Peptidase_M48_N pfam16491
CAAX prenyl protease N-terminal, five membrane helices; The five N-terminal five transmembrane ...
 37-223 1.09e-71

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: 224.29  E-value: 1.09e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A         37 QYQKLSETK-LPPVLEDEIDDETFHKSRNYSRAKAKFSIFSDIYNLAQKLVFIKYDFFPKIWHMAVTLSnavlpvrfhMV 115
Cdd:pfam16491   1 QYRHLKRHRdVPEELADIIDQETFQKSQDYTLAKSRFSLVSSLFSLILLLAFLLFGGLPWLWNLSGSLL---------SE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A        116 STVAQSLCFLGLLSSMSTLVDLPLSYYSHFVLEEKFGFNKLTVKLWITDMIKSLTLAYAIGGPILYLFLKIFDKFPTDFL 195
Cdd:pfam16491  72 SEILQSLAFLLILSLISTLISLPFSLYSTFVIEEKFGFNKQTPKLFITDLLKSLLLSLVLGGPLLAAILWIIQKAGDYFW 151

                         170       180
                  ....*....|....*....|....*...
4IL3_A        196 WYIMVFLFVVQILAMTIIPVFIMPLFNK 223
Cdd:pfam16491 152 LYLWLFWLVFQLLLMTIYPTLIAPLFNK 179
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 229-445 1.37e-40

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 144.26  E-value: 1.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      229 DGELKKSIESLADRVGFPLDKIFVIDgskrSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIV 308
Cdd:COG0501   1 DPELYRLVEELAARAGIPMPEVYVMD----SPAPNAFATGRGPNNARIVVTDGLLELLDRDELEAVLAHELGHIKNGDIL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      309 NMVIFSqlhtfLIFSLFTSIYRnssfyntfgffvekssSGFVDPVITKEFPIIIGFMLFndLLTPLecAMQFIMSLISRT 388
Cdd:COG0501  77 LMTLAS-----GLLGLIGFLAR----------------LLPLAFGRDRDAGLLLGLLLG--ILAPF--LATLIQLALSRK 131

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4IL3_A      389 HEYQADAYAKKL-GYKQNLCRALIDLQIKNLST------------MNVDPL-YSSYHYSHPTLAERLTALD 445
Cdd:COG0501 132 REYEADRAAAELtGDPDALASALRKLAGGNLSIplrrafpaqahaFIINPLkLSSLFSTHPPLEERIARLR 202
PRK03982 PRK03982
heat shock protein HtpX; Provisional
 173-444 2.96e-07

heat shock protein HtpX; Provisional


Pssm-ID: 235186 [Multi-domain]  Cd Length: 288  Bit Score: 51.93  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       173 YAIGGPILYLFLKIFDKFPTDFLWY----IMVFLFVVQILamtiipvfimplfnkfTPLEDGELKKSIESLADRVGFPLD 248
Cdd:PRK03982  23 YLLGGSIGPIIAILLALIPNLISYYysdkIVLASYNARIV----------------SEEEAPELYRIVERLAERANIPKP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       249 KIFVIDgskrSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIVNMVI-------FSQLHTFLI 321
Cdd:PRK03982  87 KVAIVP----TQTPNAFATGRDPKHAVVAVTEGILNLLNEDELEGVIAHELTHIKNRDTLIQTIaatlagaIMYLAQWLS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       322 FSLFtsiyrnssfyntFGFFVEKSSSGfvdpvitkefPIIIGFMLFNdLLTPLecAMQFIMSLISRTHEYQADAYAKKL- 400
Cdd:PRK03982 163 WGLW------------FGGGGRDDRNG----------GNPIGSLLLI-ILAPI--AATLIQFAISRQREFSADEGGARLt 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
4IL3_A       401 GYKQNLCRALIDLQ--------------------IKNLSTMNVDPLYSsyhySHPTLAERLTAL 444
Cdd:PRK03982 218 GNPLALANALQKLEkgvryiplkngnpatahmfiINPFRGQFLANLFS----THPPTEERIERL 277
 
Name Accession Description Interval E-value
M48A_Zmpste24p_like cd07343
Peptidase M48 subfamily A, a type 1 CaaX endopeptidase; This family contains peptidase family ...
 17-446 1.25e-179

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: 508.17  E-value: 1.25e-179
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       17 LIISAFSIAQFSFESYLTYRQYQKLSETKLP-PVLEDEIDDETFHKSRNYSRAKAKFSIFSDIYNLAQKLVFIKYDFFPK 95
Cdd:cd07343   1 YIILLLLVLVYLFELYLSLRQLRHLKRKLPPpPELADVISQEEFEKAQAYSLDKSRFSIVSSLLSLLLLLLLLLFGLLPL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       96 IWHMAvtlsnavlpvRFHMVSTVAQSLCFLGLLSSMSTLVDLPLSYYSHFVLEEKFGFNKLTVKLWITDMIKSLTLAYAI 175
Cdd:cd07343  81 LDLLL----------RSLGGNEILQSLLFFLLLSLISTLLSLPFSLYSTFVIEEKFGFNKQTLGLFIKDLLKSLLLSLVL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      176 GGPILYLFLKIFDKFPTDFLWYIMVFLFVVQILAMTIIPVFIMPLFNKFTPLEDGELKKSIESLADRVGFPLDKIFVIDG 255
Cdd:cd07343 151 GGPLLALLLWIIKKFGKYWWLYAWLFVVVFSLLLMFIYPTLIAPLFNKFTPLEDGELKTKIEALAKRAGFPLKKVYVMDG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      256 SKRSSHSNAYFTGLpFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIVNMVIFSQLHTFLIFSLFTSIYRNSSFY 335
Cdd:cd07343 231 SKRSTHSNAYFTGF-GKNKRIVLFDTLLEQLTEDEILAVLAHELGHWKHGHILKGLILSQLLLFLGFYLFGLLLNNPSLY 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      336 NTFGFFVeksssgfvdpviTKEFPIIIGFMLFndlLTPLECAMQFIMSLISRTHEYQADAYAKKLGYKQNLCRALIDLQI 415
Cdd:cd07343 310 RAFGFFG------------PSDQPALIGFLLL---LSPLSFLLSPLMNALSRKFEYEADAFAVELGYGEALISALVKLSK 374

                       410       420       430
                ....*....|....*....|....*....|.
4IL3_A      416 KNLSTMNVDPLYSSYHYSHPTLAERLTALDY 446
Cdd:cd07343 375 DNLSNLTPDPLYSAFHYSHPPLLERIAALEK 405
Peptidase_M48_N pfam16491
CAAX prenyl protease N-terminal, five membrane helices; The five N-terminal five transmembrane ...
 37-223 1.09e-71

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: 224.29  E-value: 1.09e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A         37 QYQKLSETK-LPPVLEDEIDDETFHKSRNYSRAKAKFSIFSDIYNLAQKLVFIKYDFFPKIWHMAVTLSnavlpvrfhMV 115
Cdd:pfam16491   1 QYRHLKRHRdVPEELADIIDQETFQKSQDYTLAKSRFSLVSSLFSLILLLAFLLFGGLPWLWNLSGSLL---------SE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A        116 STVAQSLCFLGLLSSMSTLVDLPLSYYSHFVLEEKFGFNKLTVKLWITDMIKSLTLAYAIGGPILYLFLKIFDKFPTDFL 195
Cdd:pfam16491  72 SEILQSLAFLLILSLISTLISLPFSLYSTFVIEEKFGFNKQTPKLFITDLLKSLLLSLVLGGPLLAAILWIIQKAGDYFW 151

                         170       180
                  ....*....|....*....|....*...
4IL3_A        196 WYIMVFLFVVQILAMTIIPVFIMPLFNK 223
Cdd:pfam16491 152 LYLWLFWLVFQLLLMTIYPTLIAPLFNK 179
M48A_Ste24p cd07330
Peptidase M48 CaaX prenyl protease type 1, an integral membrane, Zn-dependent protein; This ...
 117-444 5.26e-49

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: 169.16  E-value: 5.26e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      117 TVAQSLCFLGLLSSMSTLVDLPLSYYSHFVLEEKFGFNKLTVKLWITDMIKSLTLAYAIGGPILYLFLKIFD--KFPTD- 193
Cdd:cd07330   2 PILAALVFLLVFTGLMVLVELPFGWVARFRVEERFGYMRETRSLWSKRTVALLTVGLLVALPVSALLLPFEEpgGGAWWl 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      194 -FLWYIMVFLFVVQILAmtiiPVFIMPLFNKFTPLEDGELKKSIESLADRVGFPLDKIFVIDGSKRS-SHSNAYFTGLPF 271
Cdd:cd07330  82 gEWLAWLFYLFWRWKLS----PFYAQFWKRRSRPLANGELRERIESMMNREGFGCAEILKVELSGGSmIHANAYFPGSGK 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      272 TSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIVNMVIFSQLHTFLIFSLFTSIYrnssfyntfgffveksssgfvd 351
Cdd:cd07330 158 RRRVVVFADALVSLMTPDELLAVIAHELGHVKHHHHLFRLAASQAVSFIVCALFILIY---------------------- 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      352 pvitkefpiiigfmlfndlltPLecamQFIMSLISRTHEYQADAYAKKLGYKQNLCRALIDLQIKNLSTMNVDPLYSSYH 431
Cdd:cd07330 216 ---------------------PL----RFLLNFFARRFEYQADAYAAKLAGADALISALVKLHRDNLTTLTPSRLYSLWH 270

                       330
                ....*....|...
4IL3_A      432 YSHPTLAERLTAL 444
Cdd:cd07330 271 YSHPHAAMRVAHL 283
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 226-446 1.11e-45

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: 157.59  E-value: 1.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A        226 PLEDGELKKSIESLADRVGFPLDKIFViDGSKRSSHSNAYFTGLpFTSKRIVLFDTLVNS-NSTDEITAVLAHEIGHWQK 304
Cdd:pfam01435   1 PLRNAELQRVVERLAAAAGLPLPPWYV-VVIKSSPVPNAFAYGL-LPGGRVVVTTGLLDLlETEDELAAVLGHEIGHIKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A        305 NHIVNMVIFSQLHTFLIFSLF-TSIYRNSSFYNTFGffveksssgfvdpvitkefpiiIGFMLFndlLTPLECAMQFIMS 383
Cdd:pfam01435  79 RHSVESLSIMGGLSLAQLFLAlLLLGAAASGFANFG----------------------IIFLLL---IGPLAALLTLLLL 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
4IL3_A        384 LISRTHEYQADAYAKKLGYKQNLC-RALIDLQ--IKNLSTMNVDPLYSSYHYSHPTLAERLTALDY 446
Cdd:pfam01435 134 PYSRAQEYEADRLGAELMARAGYDpRALIKLWgeIDNNGRASDGALYPELLSTHPSLVERIAALRE 199
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 229-445 1.37e-40

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 144.26  E-value: 1.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      229 DGELKKSIESLADRVGFPLDKIFVIDgskrSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIV 308
Cdd:COG0501   1 DPELYRLVEELAARAGIPMPEVYVMD----SPAPNAFATGRGPNNARIVVTDGLLELLDRDELEAVLAHELGHIKNGDIL 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      309 NMVIFSqlhtfLIFSLFTSIYRnssfyntfgffvekssSGFVDPVITKEFPIIIGFMLFndLLTPLecAMQFIMSLISRT 388
Cdd:COG0501  77 LMTLAS-----GLLGLIGFLAR----------------LLPLAFGRDRDAGLLLGLLLG--ILAPF--LATLIQLALSRK 131

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4IL3_A      389 HEYQADAYAKKL-GYKQNLCRALIDLQIKNLST------------MNVDPL-YSSYHYSHPTLAERLTALD 445
Cdd:COG0501 132 REYEADRAAAELtGDPDALASALRKLAGGNLSIplrrafpaqahaFIINPLkLSSLFSTHPPLEERIARLR 202
Peptidase_M48_M56 cd05843
Peptidases M48 (Ste24 endopeptidase or htpX homolog) and M56 (in MecR1 and BlaR1), integral ...
 232-304 1.16e-19

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: 83.65  E-value: 1.16e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
4IL3_A      232 LKKSIESLADRVG-FPLDKIFVIDGSkrssHSNAYFTGLPftSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQK 304
Cdd:cd05843   1 LKKIRQEILLSAGaFPLDKVVVVPGS----VPNAFFTGGA--NKRVVLTTALLELLSEEELAAVIAHELGHFKA 68
M48A_Ste24p-like cd07345
Peptidase M48 subfamily A-like, putative CaaX prenyl protease; This family contains peptidase ...
 96-444 3.25e-17

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: 82.71  E-value: 3.25e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       96 IWHMAVTLSNAVLPVRFHMVSTVAQSLCFLGLLSSMSTLVDL---PLSYYSHFVLEEKFGFNKLTVKL-------WItdm 165
Cdd:cd07345  11 IDIYALDLKYYLSFIPLFGSSPTLLALLFLLLFLLLLLLVWYaayPVYKKLFSGLESRRAYVLSNLRFllpillpWL--- 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      166 ikSLTLAYAIGGPILYLFLKIFDKFPTDFLWYIMVFLFVVQILAmtiiPVFIMPLFNKfTPLEDGELKKSIESLADRVGF 245
Cdd:cd07345  88 --LLSLLQDLLSLLPLAILKNLLSSSLGLLGFLLLFLLLLLLFP----PLLIRLIWGC-KPLPPGPLRDRLEAFCRRAGF 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      246 PLDKIFVIDgSKRSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIVNMVIFSQLHTFLIFSLF 325
Cdd:cd07345 161 KVADILVWP-LFEGRVATAGVMGILPRFRYILITDALLDSLSPEELEAVLAHEIGHVKKRHLLLYLLFFLGFILLLALLS 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      326 TSIYRNSSFYNTFGFFVEKSSSGFVDPVITKEFPIIIGFMLFndlltplecamQFIMSLISRTHEYQADAYAKKLGYK-Q 404
Cdd:cd07345 240 LLLSLLLLLLLPLLILLLGSSAEILLTLLLALPLLLLLVLYF-----------RFVFGFFSRNFERQADLYALRALGSaE 308

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
4IL3_A      405 NLCRALidLQIKNLSTMNVDPlySSYHysHPTLAERLTAL 444
Cdd:cd07345 309 PLISAL--EKIAELSGNSRDK--PSWH--HFSIAQRIAFL 342
M48B_HtpX_like cd07338
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 228-445 2.94e-16

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: 77.24  E-value: 2.94e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      228 EDGELKKSIESLADRVGFPLDKIFVIDGSkrssHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHI 307
Cdd:cd07338  31 EYPWLQEIVEEVARRAGIKPPKVGIAEDP----IPNAFAYGSPLTGARVAVTRGLLDILNRDELEAVIGHELGHIKHRDV 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      308 VNMVIFSqlhtfLIFSLFTSIYRNSSFYNTFGFFVEKSSSGFvdpvitkefpiIIGFMLFndlltplecAMQFIMSLI-- 385
Cdd:cd07338 107 AIMTAIG-----LIPSIIYYIGRSLLFSGGSSGGRNGGGALL-----------AVGIAAF---------AVYFLFQLLvl 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
4IL3_A      386 --SRTHEYQADAYAKKL-GYKQNLCRALIDLQIKNLSTMNVDplyssyhysHPTLAERLTALD 445
Cdd:cd07338 162 gfSRLREYYADAHSAKVtGNGRALQSALAKIAYGYLAEIFST---------HPLPAKRIQALE 215
M48B_HtpX_like cd07337
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 198-445 4.89e-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: 67.72  E-value: 4.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      198 IMVFLFVVQILAMTIiPVFIMPLFNKFTPLEDGELKKSIESLADRVGFPLD--KIFVIDgskrSSHSNAYFTGlpftSKR 275
Cdd:cd07337   8 IGISPFGESILRALS-GCRIRRGARKPTRRELEEINPELEDKARRLGPDPEkvKLFISD----DEYPNAFALG----RNT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      276 IVLFDTLVNSNSTDEITAVLAHEIGHWQ-KNHIVNMVIFsqlhtflIFSLFTSIYrnssfyntfgffveksssgfvdpvi 354
Cdd:cd07337  79 ICVTKGLLDLLDYEELKGILAHELGHLShKDTDYLLLIF-------VLLLLAAIW------------------------- 126

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      355 tkefpIIIGFMLFNDLLTPlecamqfIMSLISRTHEYQADAYAKKLGYKQNLCRALIDLQiknLSTMNVDPLYSSYHYSH 434
Cdd:cd07337 127 -----TKLGTLLIFVWIRL-------LVMFSSRKAEYRADAFAVKIGYGEGLRSALDQLR---EYEDAPKGFLAALYSTH 191

                       250
                ....*....|.
4IL3_A      435 PTLAERLTALD 445
Cdd:cd07337 192 PPTEKRIERLE 202
M48C_Oma1_like cd07332
Peptidase M48C Ste24p, integral membrane endopeptidase; This subfamily contains peptidase M48C ...
 229-444 8.11e-13

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: 67.60  E-value: 8.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      229 DGELKKSIESLADRVGFPLD-----KIFVIDGSKrssHSNAyFTgLPftSKRIVLFDTLVN-SNSTDEITAVLAHEIGHW 302
Cdd:cd07332  43 PAERQAALQQLFARLLAALPlpypyRLHFRDSGI---GANA-FA-LP--GGTIVVTDGLVElAESPEELAAVLAHEIGHV 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      303 QKNHIVNMVIFSQLhTFLIFSLFTSiyrnssfyntfgffvekSSSGFVDPVITkefpiiIGFMLFNdlltplecaMQFim 382
Cdd:cd07332 116 EHRHSLRQLIRSSG-LSLLVSLLTG-----------------DVSGLSDLLAG------LPALLLS---------LSY-- 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
4IL3_A      383 sliSRTHEYQADAYAKKLGYKQNLC-RALID----LQIKNLSTMNVDPLYSsyhySHPTLAERLTAL 444
Cdd:cd07332 161 ---SRDFEREADAFALELLKAAGISpEGLADfferLEEEHGDGGSLPEWLS----THPDTEERIEAI 220
M48B_HtpX_like cd07335
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This family contains ...
 231-444 6.38e-12

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: 65.30  E-value: 6.38e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      231 ELKKSIESLADRVGFPLDKIFVIDgskrSSHSNAYFTGlPFTSKRIVLFDT-LVNSNSTDEITAVLAHEIGHWQKNHIVN 309
Cdd:cd07335  35 WLVETVAELARKAGIKMPEVGIYP----SPDVNAFATG-PSRNNSLVAVSTgLLDNMSEDEVEAVLAHEISHIANGDMVT 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      310 MvifsqlhTFLifslftsiyrnSSFYNTFGFFVEKSSSGFVDPVITKE--FPIIIGFMLFNDLLTPLECAMQFIMSLISR 387
Cdd:cd07335 110 M-------TLL-----------QGVVNTFVIFLSRIIALIIDSFLSGDenGSGIGYFLVVIVLEIVLGILASLVVMWFSR 171

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
4IL3_A      388 THEYQADAYAKKLGYKQNLCRALIDLQ--------------IKNLSTMNVdplYSSYHYSHPTLAERLTAL 444
Cdd:cd07335 172 KREFRADAGGAKLTGKEKMIAALERLKqiserpeseddvaaAIKISRGSG---FLRLFSTHPPLEERIAAL 239
M48B_Htpx_like cd07340
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 225-445 3.02e-09

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: 57.51  E-value: 3.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      225 TPLEDGELKKSIESLADRVGFPLDKIFVIDgskrSSHSNAYFTGLpfTSKRIVLFDT--LVNSNSTDEITAVLAHEIGhw 302
Cdd:cd07340  24 TREDEPRLYNVVEELAIAAGLPMPKVYIID----DPAPNAFATGR--NPEHAVIAVTtgLLEKLNRDELEGVIAHELS-- 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      303 qknHIVN-----MVIFSQLhTFLIfSLFTSIYRNSSFYNTFGFFVEKSSSGFVDPVItkefpIIIGFMLFndLLTPLecA 377
Cdd:cd07340  96 ---HIKNydirlMTIAVVL-VGII-ALIADLALRSFFYGGGSRRRRRDGGGGGALIL-----LILGLVLI--ILAPI--F 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      378 MQFIMSLISRTHEYQADAYAKKL-GYKQNLCRALidLQIKNLSTMNVDPLYSSYHYS------------------HPTLA 438
Cdd:cd07340 162 AQLIQLAISRQREYLADASAVELtRNPEGLISAL--EKISGDSSPLKVANSATAHLNlyfpnpgkkssfsslfstHPPIE 239


                ....*..
4IL3_A      439 ERLTALD 445
Cdd:cd07340 240 ERIKRLR 246
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 237-444 1.06e-07

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: 52.07  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      237 ESLADRVGFPLDKIFVIDgskrSSHSNAYFTGLPFTSKRIV---LFDTLvnsnSTDEITAVLAHEIGHWQKNHIVNMVIF 313
Cdd:cd07329   1 DRLARQADVPPPRVYVVD----SDVPNAFAVGRSRGPTVVVttgLLDLL----DDDELEAVLAHELAHLKRRDVLVLLLF 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      314 SQLhTFLIFSLFTSIYRNSSFYNTFgffveksssgfvdpvitkeFPIIIGFMLFNDLLTPLECAMQFIMSLISRTHEyqa 393
Cdd:cd07329  73 DPL-LLLVVGLLLFLSLFIFELLGF-------------------FFQPLLFLAFFALLRLAELLADALAVARTSAAR--- 129

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
4IL3_A      394 daYAKKLGYKQNLCRALIDL---QIKNLSTMNVDPLYSS-----YHYSHPTLAERLTAL 444
Cdd:cd07329 130 --RARLTGLPAALASALEKIedaSDRALEAGLVLPALAAdasslEKTDHPPLEERVERL 186
PRK03982 PRK03982
heat shock protein HtpX; Provisional
 173-444 2.96e-07

heat shock protein HtpX; Provisional


Pssm-ID: 235186 [Multi-domain]  Cd Length: 288  Bit Score: 51.93  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       173 YAIGGPILYLFLKIFDKFPTDFLWY----IMVFLFVVQILamtiipvfimplfnkfTPLEDGELKKSIESLADRVGFPLD 248
Cdd:PRK03982  23 YLLGGSIGPIIAILLALIPNLISYYysdkIVLASYNARIV----------------SEEEAPELYRIVERLAERANIPKP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       249 KIFVIDgskrSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIVNMVI-------FSQLHTFLI 321
Cdd:PRK03982  87 KVAIVP----TQTPNAFATGRDPKHAVVAVTEGILNLLNEDELEGVIAHELTHIKNRDTLIQTIaatlagaIMYLAQWLS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       322 FSLFtsiyrnssfyntFGFFVEKSSSGfvdpvitkefPIIIGFMLFNdLLTPLecAMQFIMSLISRTHEYQADAYAKKL- 400
Cdd:PRK03982 163 WGLW------------FGGGGRDDRNG----------GNPIGSLLLI-ILAPI--AATLIQFAISRQREFSADEGGARLt 217

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
4IL3_A       401 GYKQNLCRALIDLQ--------------------IKNLSTMNVDPLYSsyhySHPTLAERLTAL 444
Cdd:PRK03982 218 GNPLALANALQKLEkgvryiplkngnpatahmfiINPFRGQFLANLFS----THPPTEERIERL 277
M48_Ste24p_like cd07328
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 236-444 3.71e-07

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: 49.86  E-value: 3.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      236 IESLADRVGFP-LDKIFVIDgskrssHSNAYFT--------------GLPftskrivlfdtLVNSNSTDEITAVLAHEIG 300
Cdd:cd07328  32 VDELAAALGAPpPDEVVLTA------DVNASVTelglllgrrglltlGLP-----------LLAALSPEELRAVLAHELG 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      301 HwqknhivnmviFSQLHTflifslftsiyrnssfynTFGFFVeksssgfvdpvitkefpiiigfmlfndlltplecamqf 380
Cdd:cd07328  95 H-----------FANGDT------------------RLGAWI-------------------------------------- 107

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
4IL3_A      381 imslISRTHEYQADAYAKKLGYKQNLCRALIDLQIKNLstmnvdplySSYHYSHPTLAERLTAL 444
Cdd:cd07328 108 ----LSRRAEYEADRVAARVAGSAAAASALRKLAARRP---------SSPDDTHPPLAERLAAL 158
PRK01345 PRK01345
heat shock protein HtpX; Provisional
 231-455 3.06e-06

heat shock protein HtpX; Provisional


Pssm-ID: 234944 [Multi-domain]  Cd Length: 317  Bit Score: 48.86  E-value: 3.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       231 ELKKSIESLADRVGFPLDKIFVIDgskrSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIVNM 310
Cdd:PRK01345  68 ELYRMVRDLARRAGLPMPKVYIID----NPQPNAFATGRNPENAAVAATTGLLQRLSPEEVAGVMAHELAHVKNRDTLTM 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       311 VIFSqlhtflifSLFTSIyrnsSFYNTFGFFVEKSSSGFVDPVItkefpiIIGfMLFNDLLTPLeCAMQFIMSlISRTHE 390
Cdd:PRK01345 144 TITA--------TLAGAI----SMLANFAFFFGGNRENNNGPLG------LVG-TLAAMIVAPL-AAMLVQMA-ISRTRE 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       391 YQADAY-AKKLGYKQNLCRALIDL-----QIKN-----------------LSTMNVDPLYSsyhySHPTLAERLTALDYV 447
Cdd:PRK01345 203 YAADRRgAEICGNPLWLASALGKIergahGVPNeeaernpatahmfiinpLSGEGMDNLFS----THPATENRIAALQRM 278


                 ....*...
4IL3_A       448 SEKKKNSG 455
Cdd:PRK01345 279 AGEMGGRS 286
M48B_HtpX_like cd07339
Peptidase M48 subfamily B HtpX-like membrane-bound metallopeptidase; This HtpX family of ...
 207-440 4.07e-06

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: 47.94  E-value: 4.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      207 ILAMTIIPVFIMPLFN--KFTPLEDGELKKSIESLADRVGFP-LDKIFVIDgskrSSHSNAYFTGLPFTSKrIVLFDTLV 283
Cdd:cd07339   3 LLSPRVSPRLILRLYGarPLSPGDAPELYRLLQELARRAGLPrPPLLYYVP----SRVLNAFAVGSRKDAA-IALTDGLL 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      284 NSNSTDEITAVLAHEIGHWQKNHIVnmvifsqlhtflIFSLFTSIYRNSSFYNTFGFFVekssSGFVDPVI-TKEFPI-- 360
Cdd:cd07339  78 RRLTLRELAGVLAHEVSHIRNGDLR------------VMGLADLISRLTSLLSLLGQLL----LLLNLPLLlLGEVTIsw 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      361 -IIGFMLFndllTPlecamqFIMSLI----SRTHEYQADAYAKKL-GYKQNLCRAL--IDLQIKNLSTMNVDPLY----S 428
Cdd:cd07339 142 lAILLLIL----AP------TLSTLLqlalSRTREFDADLDAARLtGDPEGLASALakLERYQGGWWERLLLPGRrvpeP 211

                       250
                ....*....|..
4IL3_A      429 SYHYSHPTLAER 440
Cdd:cd07339 212 SLLRTHPPTEER 223
M48B_HtpX_like cd07327
HtpX-like membrane-bound metallopeptidase; This family contains peptidase M48 subfamily B, ...
 225-314 7.48e-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: 46.48  E-value: 7.48e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      225 TPLEDGELKKSIESLADRVGFPLDKIFVIDGSKRsshsNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQK 304
Cdd:cd07327  19 SEEEAPELHAIVERLARRAGLPKPRVAIVDTPMP----NAFATGRNPKNAAVAVTTGLLQLLNEDELEAVLAHELSHIKN 94

                        90
                ....*....|
4IL3_A      305 NHIVNMVIFS 314
Cdd:cd07327  95 RDVLVMTLAS 104
PRK03001 PRK03001
zinc metalloprotease HtpX;
236-444 1.63e-05

zinc metalloprotease HtpX;


Pssm-ID: 179524 [Multi-domain]  Cd Length: 283  Bit Score: 46.56  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       236 IESLADRVGFPLDKIFVIDgskrSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIvnmvifsq 315
Cdd:PRK03001  73 VRELAQRAGLPMPKVYLIN----EDQPNAFATGRNPEHAAVAATTGILRVLSEREIRGVMAHELAHVKHRDI-------- 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       316 lhtfLIFSLFTSIYRN-SSFYNTFGFFVEKSSSG-FVDPVItkefpiiigfMLFNDLLTPLecAMQFIMSLISRTHEYQA 393
Cdd:PRK03001 141 ----LISTISATMAGAiSALANFAMFFGGRDENGrPVNPIA----------GIAVAILAPL--AASLIQMAISRAREFEA 204

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       394 DAYAKKL-GYKQNLCRAL---------IDLQIKNLST-----MNVDPL----YSSYHYSHPTLAERLTAL 444
Cdd:PRK03001 205 DRGGARIsGDPQALASALdkihryasgIPFQAAEAHPataqmMIINPLsgggLANLFSTHPSTEERIARL 274
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 231-308 4.17e-05

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


Pssm-ID: 320684 [Multi-domain]  Cd Length: 199  Bit Score: 44.52  E-value: 4.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A      231 ELKKSIESLADRVGFPLD-KIFVIdgskRSSHSNAYFTGlpFTSKR-IVLFDTLVNSNSTDEITAVLAHEIGHWQKNHIV 308
Cdd:cd07325  14 ELHALLVEACRILGLKKVpELYVY----QSPVLNAFALG--FEGRPfIVLNSGLVELLDDDELRFVIGHELGHIKSGHVL 87
M48C_Oma1-like cd07324
Oma1 peptidase-like, integral membrane metallopeptidase; This family contains peptidase M48 ...
 240-315 6.10e-05

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: 42.94  E-value: 6.10e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
4IL3_A      240 ADRVGFPLdKIFVIDGSKRsshsNAYFTGLPFtskrIVLFDTLVNS-NSTDEITAVLAHEIGHWQKNHIVNMVI-FSQ 315
Cdd:cd07324  13 SGRPDLPY-RFFVVDDPSI----NAFALPGGY----IFVTTGLLLLlESEDELAAVLAHEIGHVTLRHIARQLErYSR 81
PRK01265 PRK01265
heat shock protein HtpX; Provisional
 171-324 7.87e-04

heat shock protein HtpX; Provisional


Pssm-ID: 234931 [Multi-domain]  Cd Length: 324  Bit Score: 41.27  E-value: 7.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       171 LAYAIGGpilYLFLKIFDKfptdflwYIMVFLFVVqILAMTIIPVFIMPLF-------NKFTPLED--GELKKSIESLAD 241
Cdd:PRK01265  26 LAYAVAY---YAFGAQFGV-------GLILGILIF-VFFLNIIQWLFGPYMinaayrtVEVTPTDPvyGWLYSIVAEVAK 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       242 RVGFPLDKIFVIDgskrSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWqKNHIVNMVIFSQLHTFLI 321
Cdd:PRK01265  95 YNGIRVPKVYIAD----VPFPNAFAYGSPIAGKRIAITLPLLKILNRDEIKAVAGHELGHL-KHRDVELLMAIGLIPTLI 169


                 ...
4IL3_A       322 FSL 324
Cdd:PRK01265 170 YYL 172
PRK02870 PRK02870
heat shock protein HtpX; Provisional
 249-400 6.59e-03

heat shock protein HtpX; Provisional


Pssm-ID: 235081 [Multi-domain]  Cd Length: 336  Bit Score: 38.55  E-value: 6.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
4IL3_A       249 KIFVIDgskrSSHSNAYFTGLPFTSKRIVLFDTLVNSNSTDEITAVLAHEIGHWQKNHI-VNMVIfsqlhtfLIFSLFTS 327
Cdd:PRK02870 135 KVYIID----APYMNAFASGYSEKSAMVAITTGLLEKLDRDELQAVMAHELSHIRHGDIrLTLCV-------GVLSNIML 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
4IL3_A       328 IYRNSSFYNTFGffvEKSSSGfvdpvITKEFPIIIGFMLFNDLLTplecamQFIMSLISRTHEYQADAYAKKL 400
Cdd:PRK02870 204 IVADFLFYSFMG---NRRNSG-----ANRARMIILILRYVLPILT------VLLMLFLSRTREYMADAGAVEL 262
 
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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