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Conserved domains on  [gi|1391667040|ref|WP_109491938|]
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MULTISPECIES: M56 family metallopeptidase [Streptomyces]

Protein Classification

M56 family metallopeptidase( domain architecture ID 11574413)

M56 family metallopeptidase is an integral membrane metallopeptidase, containing a zinc-binding HEXXH motif; it allows bacteria to respond to presence of beta-lactam antibiotics by expression of beta-lactamases and penicillin-binding proteins; includes transmembrane proteins BlaR1 and MecR1

Gene Ontology:  GO:0008233|GO:0046872|GO:0016020
MEROPS:  M56
PubMed:  11239156

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 103-254 4.56e-26

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


:

Pssm-ID: 320685 [Multi-domain]  Cd Length: 165  Bit Score: 101.23  E-value: 4.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 103 AAWHHHRVRRDAARALAGLRRTSVAVLPDAVPYAYALPGGRGRIVASTSLLDCLEPAERRALFAHERAHLAGSHHRFLLT 182
Cdd:cd07326     6 RRRRLRRLLLLLLRELRARGGGGVRVVDHDAPLAFCLGGRRPRIVLSTGLLELLSPEELRAVLAHERAHLRRRDPLLLLL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391667040 183 VRLAARASPFL---RPLRTAVAYTAERWADEDAAAATGNrRVVARAIGKAALLSRGAPAATLAHFAAPGPVPRRV 254
Cdd:cd07326    86 ASALARALPFLpllRRLAAAYRLLRELAADDAAARRVGP-RALASALLKLARAGAPAAPAGALAFAGAAVNEARI 159
 
Name Accession Description Interval E-value
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 103-254 4.56e-26

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


Pssm-ID: 320685 [Multi-domain]  Cd Length: 165  Bit Score: 101.23  E-value: 4.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 103 AAWHHHRVRRDAARALAGLRRTSVAVLPDAVPYAYALPGGRGRIVASTSLLDCLEPAERRALFAHERAHLAGSHHRFLLT 182
Cdd:cd07326     6 RRRRLRRLLLLLLRELRARGGGGVRVVDHDAPLAFCLGGRRPRIVLSTGLLELLSPEELRAVLAHERAHLRRRDPLLLLL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391667040 183 VRLAARASPFL---RPLRTAVAYTAERWADEDAAAATGNrRVVARAIGKAALLSRGAPAATLAHFAAPGPVPRRV 254
Cdd:cd07326    86 ASALARALPFLpllRRLAAAYRLLRELAADDAAARRVGP-RALASALLKLARAGAPAAPAGALAFAGAAVNEARI 159
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 103-254 1.59e-13

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: 68.23  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 103 AAWHHHRVRRDAARA-LAGLRRTSVAVLPDAVPYAYALPGGRG-RIVASTSLLDCLE-PAERRALFAHERAHLAGSHHRF 179
Cdd:pfam01435   4 NAELQRVVERLAAAAgLPLPPWYVVVIKSSPVPNAFAYGLLPGgRVVVTTGLLDLLEtEDELAAVLGHEIGHIKARHSVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 180 -----------------------------------LLTVRLAARASPFLRPLRTAVAYTAERWADEDAAAATGNRRVVAR 224
Cdd:pfam01435  84 slsimgglslaqlflallllgaaasgfanfgiiflLLIGPLAALLTLLLLPYSRAQEYEADRLGAELMARAGYDPRALIK 163

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1391667040 225 AIGKAALLSRGAPAATLAHFAAPGP-VPRRV 254
Cdd:pfam01435 164 LWGEIDNNGRASDGALYPELLSTHPsLVERI 194
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 107-237 5.72e-07

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 49.11  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 107 HHRVRRDAARAlaGLRRTSVAVLPDAVPYAYALpgGRG----RIVASTSLLDCLEPAERRALFAHERAHLAGSH------ 176
Cdd:COG0501     5 YRLVEELAARA--GIPMPEVYVMDSPAPNAFAT--GRGpnnaRIVVTDGLLELLDRDELEAVLAHELGHIKNGDillmtl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 177 ------------------------HRFLLTVRLAARASPFLRPLRTAVAYTAERWADEDAAAATGNRRVVARAIGKAALL 232
Cdd:COG0501    81 asgllgligflarllplafgrdrdAGLLLGLLLGILAPFLATLIQLALSRKREYEADRAAAELTGDPDALASALRKLAGG 160


                  ....*
gi 1391667040 233 SRGAP 237
Cdd:COG0501   161 NLSIP 165
PRK02391 PRK02391
heat shock protein HtpX; Provisional
 117-187 8.91e-03

heat shock protein HtpX; Provisional


Pssm-ID: 179418 [Multi-domain]  Cd Length: 296  Bit Score: 37.22  E-value: 8.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391667040 117 ALAGLRRTSVAVLPDAVPYAYALpgGRGR----IVASTSLLDCLEPAERRALFAHERAHLAgshHRFLLTVRLAA 187
Cdd:PRK02391   87 ALADLPKPRVAVADSDVPNAFAT--GRSPknavVCVTTGLMRRLDPDELEAVLAHELSHVK---NRDVAVMTIAS 156
 
Name Accession Description Interval E-value
M56_BlaR1_MecR1_like cd07326
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 103-254 4.56e-26

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


Pssm-ID: 320685 [Multi-domain]  Cd Length: 165  Bit Score: 101.23  E-value: 4.56e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 103 AAWHHHRVRRDAARALAGLRRTSVAVLPDAVPYAYALPGGRGRIVASTSLLDCLEPAERRALFAHERAHLAGSHHRFLLT 182
Cdd:cd07326     6 RRRRLRRLLLLLLRELRARGGGGVRVVDHDAPLAFCLGGRRPRIVLSTGLLELLSPEELRAVLAHERAHLRRRDPLLLLL 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391667040 183 VRLAARASPFL---RPLRTAVAYTAERWADEDAAAATGNrRVVARAIGKAALLSRGAPAATLAHFAAPGPVPRRV 254
Cdd:cd07326    86 ASALARALPFLpllRRLAAAYRLLRELAADDAAARRVGP-RALASALLKLARAGAPAAPAGALAFAGAAVNEARI 159
Peptidase_M48 pfam01435
Peptidase family M48; Peptidase_M48 is the largely extracellular catalytic region of CAAX ...
 103-254 1.59e-13

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: 68.23  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 103 AAWHHHRVRRDAARA-LAGLRRTSVAVLPDAVPYAYALPGGRG-RIVASTSLLDCLE-PAERRALFAHERAHLAGSHHRF 179
Cdd:pfam01435   4 NAELQRVVERLAAAAgLPLPPWYVVVIKSSPVPNAFAYGLLPGgRVVVTTGLLDLLEtEDELAAVLGHEIGHIKARHSVE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 180 -----------------------------------LLTVRLAARASPFLRPLRTAVAYTAERWADEDAAAATGNRRVVAR 224
Cdd:pfam01435  84 slsimgglslaqlflallllgaaasgfanfgiiflLLIGPLAALLTLLLLPYSRAQEYEADRLGAELMARAGYDPRALIK 163

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1391667040 225 AIGKAALLSRGAPAATLAHFAAPGP-VPRRV 254
Cdd:pfam01435 164 LWGEIDNNGRASDGALYPELLSTHPsLVERI 194
M48_Ste24p_like cd07325
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 108-234 1.75e-08

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: 53.77  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 108 HRVRRDAARALaGLRRT-SVAVLPDAVPYAYAL-PGGRGRIVASTSLLDCLEPAERRALFAHERAHLAGSH---HRFLLT 182
Cdd:cd07325    16 HALLVEACRIL-GLKKVpELYVYQSPVLNAFALgFEGRPFIVLNSGLVELLDDDELRFVIGHELGHIKSGHvlyRTLLLL 94

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1391667040 183 VRLAARASPFLRPLRTAVA----------YTAERWadedAAAATGNRRVVARAIGKAALLSR 234
Cdd:cd07325    95 LLLLGELIGILLLSSALPLallawsraaeYSADRA----GLLVCQDPEAAIRALMKLAGGSK 152
HtpX COG0501
Zn-dependent protease with chaperone function [Posttranslational modification, protein ...
 107-237 5.72e-07

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


Pssm-ID: 440267 [Multi-domain]  Cd Length: 210  Bit Score: 49.11  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 107 HHRVRRDAARAlaGLRRTSVAVLPDAVPYAYALpgGRG----RIVASTSLLDCLEPAERRALFAHERAHLAGSH------ 176
Cdd:COG0501     5 YRLVEELAARA--GIPMPEVYVMDSPAPNAFAT--GRGpnnaRIVVTDGLLELLDRDELEAVLAHELGHIKNGDillmtl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 177 ------------------------HRFLLTVRLAARASPFLRPLRTAVAYTAERWADEDAAAATGNRRVVARAIGKAALL 232
Cdd:COG0501    81 asgllgligflarllplafgrdrdAGLLLGLLLGILAPFLATLIQLALSRKREYEADRAAAELTGDPDALASALRKLAGG 160


                  ....*
gi 1391667040 233 SRGAP 237
Cdd:COG0501   161 NLSIP 165
M56_like cd07329
Peptidase M56-like, integral membrane metallopeptidase in bacteria; This family contains ...
 117-254 4.42e-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: 46.29  E-value: 4.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 117 ALAGLRRTSVAVLPDAVPYAYALPGGRGR-IVASTSLLDCLEPAERRALFAHERAHLAGSHHRFLLTVRLAARA------ 189
Cdd:cd07329     5 RQADVPPPRVYVVDSDVPNAFAVGRSRGPtVVVTTGLLDLLDDDELEAVLAHELAHLKRRDVLVLLLFDPLLLLvvglll 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 190 --------------SPFLRPLRTAVAYTAERWADEDAAAATGNRRVVARAIGKAAL------LSRGAPAATLAHFAAPGP 249
Cdd:cd07329    85 flslfifellgfffQPLLFLAFFALLRLAELLADALAVARTSAARRARLTGLPAALasalekIEDASDRALEAGLVLPAL 164


                  ....*
gi 1391667040 250 VPRRV 254
Cdd:cd07329   165 AADAS 169
MecR1 COG4219
Signal transducer regulating beta-lactamase production, contains metallopeptidase domain ...
 93-240 2.92e-04

Signal transducer regulating beta-lactamase production, contains metallopeptidase domain [Signal transduction mechanisms];


Pssm-ID: 443363 [Multi-domain]  Cd Length: 337  Bit Score: 41.96  E-value: 2.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040  93 LAAVLVACSAAAWHHHRVRR-----------------DAARALAGLRRTSVAVLPDAVPYAYALPGGRGRIVASTSLLDc 155
Cdd:COG4219     2 LAGVLLLLLRLLISLLRLRRllrrarpvtdeellellERLARRLGIRRPVRLLESDRITSPFSFGLLRPVILLPAGLEE- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 156 LEPAERRALFAHERAHLAGSHHRFLLTVRLAARA---SPFLRPLRTAVAYTAERWADEDAAAATGNRRVVARAIGKAALL 232
Cdd:COG4219    81 LSEEELEAILAHELAHIRRRDLLDNLLAELLLALfwfNPLVWLARRRLRLDRELACDAAVLKAGGDRKAYAETLLKLAER 160


                  ....*...
gi 1391667040 233 SRGAPAAT 240
Cdd:COG4219   161 RSQPALAL 168
M48_Ste24p_like cd07328
M48 Ste24 endopeptidase-like, integral membrane metallopeptidase; This family contains ...
 112-240 6.69e-04

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: 39.46  E-value: 6.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 112 RDAARALAGLRRTSVAVLPD---AVPYAYALPGGRGRIVASTSLLDCLEPAERRALFAHERAHLAGSHHRflLTVRLAAR 188
Cdd:cd07328    33 DELAAALGAPPPDEVVLTADvnaSVTELGLLLGRRGLLTLGLPLLAALSPEELRAVLAHELGHFANGDTR--LGAWILSR 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1391667040 189 AspflrplrtavaytAERWADEDAAAATGnRRVVARAIGKAALLSRGAPAAT 240
Cdd:cd07328   111 R--------------AEYEADRVAARVAG-SAAAASALRKLAARRPSSPDDT 147
M56_BlaR1_MecR1_like cd07341
Peptidase M56-like including those in BlaR1 and MecR1, integral membrane metallopeptidase; ...
 93-253 6.17e-03

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


Pssm-ID: 320700 [Multi-domain]  Cd Length: 187  Bit Score: 36.92  E-value: 6.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040  93 LAAVLVACSAAAWHHHRVRRDAARALA----------GLRRTSVAVLPDAVPYAYALPGGRGRIVASTSLLDcLEPAERR 162
Cdd:cd07341     6 ALLLLLRLLRGLLRLRRLRRRAEPVPDslllelarrlGLRRSVRLSVSALVASPMVVGLFRPVILLPEGLLE-GSPEELR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1391667040 163 ALFAHERAHLAGSHHRFLLTVRLAARA---SPFLRPLRTAVAYTAERWADEDAAAATGNRRVVARAIGKAALLSRGAPAA 239
Cdd:cd07341    85 AILLHELAHIRRRDLLVNLLQRLLEALfwfNPLVWLLSRRLRLERELACDEAVLAALGDKEDYAEALLRLAERRSQPPPA 164

                         170
                  ....*....|....
gi 1391667040 240 TLAHFAAPGPVPRR 253
Cdd:cd07341   165 LALALAGSKSLLKR 178
PRK02391 PRK02391
heat shock protein HtpX; Provisional
 117-187 8.91e-03

heat shock protein HtpX; Provisional


Pssm-ID: 179418 [Multi-domain]  Cd Length: 296  Bit Score: 37.22  E-value: 8.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1391667040 117 ALAGLRRTSVAVLPDAVPYAYALpgGRGR----IVASTSLLDCLEPAERRALFAHERAHLAgshHRFLLTVRLAA 187
Cdd:PRK02391   87 ALADLPKPRVAVADSDVPNAFAT--GRSPknavVCVTTGLMRRLDPDELEAVLAHELSHVK---NRDVAVMTIAS 156
 
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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