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Conserved domains on  [gi|488892999|ref|WP_002804144|]
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MULTISPECIES: LexA family transcriptional regulator [Campylobacter]

Protein Classification

HTH_XRE and S24_LexA-like domain-containing protein( domain architecture ID 11715193)

HTH_XRE and S24_LexA-like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 81-207 1.86e-24

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


:

Pssm-ID: 442176  Cd Length: 121  Bit Score: 93.49  E-value: 1.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999  81 DVAAAAGYGAINsklEYTEIViskkfacEALGLPPLT--RLDIIKVIGDSMEPFIHNGDVIAVDVSKNKlelVKNGDIVV 158
Cdd:COG2932    5 DGEASAGGGAFN---EVEEPV-------DKLEFPGLPpdNLFAVRVSGDSMEPTIRDGDIVLVDPSDTE---IRDGGIYV 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488892999 159 INLDGEIYCKKLLKQPfVNEIVLSSMNSFYKDIVVNIDQISCAEIIGVV 207
Cdd:COG2932   72 VRTDGELLVKRLQRRP-DGKLRLISDNPAYPPIEIPPEDADEIEIIGRV 119
HTH_XRE super family cl22854
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 6-66 3.27e-09

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


The actual alignment was detected with superfamily member pfam07022:

Pssm-ID: 473980  Cd Length: 65  Bit Score: 51.56  E-value: 3.27e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488892999    6 DILNRVYAILNITDDKEFCGIYEIKPNTLSTWRTRNTIPYELLLKISKEQNISLDSIFFGK 66
Cdd:pfam07022   1 AVIERLMKAYGFKSRQELADHLGVSKSTLSTWYTRDSFPAELVVRCALETGVSLEWLATGD 61
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 81-207 1.86e-24

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 93.49  E-value: 1.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999  81 DVAAAAGYGAINsklEYTEIViskkfacEALGLPPLT--RLDIIKVIGDSMEPFIHNGDVIAVDVSKNKlelVKNGDIVV 158
Cdd:COG2932    5 DGEASAGGGAFN---EVEEPV-------DKLEFPGLPpdNLFAVRVSGDSMEPTIRDGDIVLVDPSDTE---IRDGGIYV 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488892999 159 INLDGEIYCKKLLKQPfVNEIVLSSMNSFYKDIVVNIDQISCAEIIGVV 207
Cdd:COG2932   72 VRTDGELLVKRLQRRP-DGKLRLISDNPAYPPIEIPPEDADEIEIIGRV 119
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 121-207 7.25e-21

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 82.99  E-value: 7.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999 121 IIKVIGDSMEPFIHNGDVIAVDVSKNklelVKNGDIVVINLDGEIYCKKLLKQPFvNEIVLSSMNSFYKDIVVNIDQIsc 200
Cdd:cd06529    2 ALRVKGDSMEPTIPDGDLVLVDPSDT----PRDGDIVVARLDGELTVKRLQRRGG-GRLRLISDNPAYPPIEIDEEEL-- 74


                 ....*..
gi 488892999 201 aEIIGVV 207
Cdd:cd06529   75 -EIVGVV 80
Peptidase_S24 pfam00717
Peptidase S24-like;
121-208 1.66e-20

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 83.02  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999  121 IIKVIGDSMEPFIHNGDVIAVDVSKNklelVKNGDIVVINLDGEIYCKKLLKQPfvNEIVLSSMNSFYKDIVVNIDQIsc 200
Cdd:pfam00717  37 ALRVKGDSMEPGIPDGDLVLVDPSRE----ARNGDIVVARLDGEATVKRLYRDG--GGIRLISLNPEYPPIELPAEDD-- 108


                  ....*...
gi 488892999  201 AEIIGVVC 208
Cdd:pfam00717 109 VEIIGRVV 116
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
122-207 2.61e-10

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 56.73  E-value: 2.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999 122 IKVIGDSM-EPFIHNGDVIAVDVSKNklelVKNGDIVVINLDGEIYCKKLLKQPFVNeivLSSMNSFYKDIVVNIDqiSC 200
Cdd:PRK10276  54 VKASGDSMiDAGISDGDLLIVDSAIT----ASHGDIVIAAVDGEFTVKKLQLRPTVQ---LIPMNSAYSPITISSE--DT 124


                 ....*..
gi 488892999 201 AEIIGVV 207
Cdd:PRK10276 125 LDVFGVV 131
Phage_CI_repr pfam07022
Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI ...
 6-66 3.27e-09

Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI repressor proteins and related bacterial sequences. The CI repressor is known to function as a transcriptional switch, determining whether transcription is lytic or lysogenic.


Pssm-ID: 311152  Cd Length: 65  Bit Score: 51.56  E-value: 3.27e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488892999    6 DILNRVYAILNITDDKEFCGIYEIKPNTLSTWRTRNTIPYELLLKISKEQNISLDSIFFGK 66
Cdd:pfam07022   1 AVIERLMKAYGFKSRQELADHLGVSKSTLSTWYTRDSFPAELVVRCALETGVSLEWLATGD 61
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 121-207 5.47e-07

SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA. [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 273106 [Multi-domain]  Cd Length: 199  Bit Score: 48.17  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999  121 IIKVIGDSM-EPFIHNGDVIAVdvskNKLELVKNGDIVVINLDGEIYCKKLLKQPfvNEIVLSSMNSFYKDIVVNidqIS 199
Cdd:TIGR00498 113 LLKVMGDSMvDAGICDGDLLIV----RSQKDARNGEIVAAMIDGEVTVKRFYKDG--TKVELKPENPEFDPIVLN---AE 183


                  ....*...
gi 488892999  200 CAEIIGVV 207
Cdd:TIGR00498 184 DVTILGKV 191
 
Name Accession Description Interval E-value
COG2932 COG2932
Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: ...
 81-207 1.86e-24

Phage repressor protein C, contains Cro/C1-type HTH and peptisase s24 domains [Mobilome: prophages, transposons];


Pssm-ID: 442176  Cd Length: 121  Bit Score: 93.49  E-value: 1.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999  81 DVAAAAGYGAINsklEYTEIViskkfacEALGLPPLT--RLDIIKVIGDSMEPFIHNGDVIAVDVSKNKlelVKNGDIVV 158
Cdd:COG2932    5 DGEASAGGGAFN---EVEEPV-------DKLEFPGLPpdNLFAVRVSGDSMEPTIRDGDIVLVDPSDTE---IRDGGIYV 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488892999 159 INLDGEIYCKKLLKQPfVNEIVLSSMNSFYKDIVVNIDQISCAEIIGVV 207
Cdd:COG2932   72 VRTDGELLVKRLQRRP-DGKLRLISDNPAYPPIEIPPEDADEIEIIGRV 119
S24_LexA-like cd06529
Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of ...
 121-207 7.25e-21

Peptidase S24 LexA-like proteins are involved in the SOS response leading to the repair of single-stranded DNA within the bacterial cell. This family includes: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The LexA-like proteins contain two-domains: an N-terminal DNA binding domain and a C-terminal domain (CTD) that provides LexA dimerization as well as cleavage activity. They undergo autolysis, cleaving at an Ala-Gly or a Cys-Gly bond, separating the DNA-binding domain from the rest of the protein. In the presence of single-stranded DNA, the LexA, UmuD and MucA proteins interact with RecA, activating self cleavage, thus either derepressing transcription in the case of LexA or activating the lesion-bypass polymerase in the case of UmuD and MucA. The LexA proteins are serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases. LexA sequence homologs are found in almost all of the bacterial genomes sequenced to date, covering a large number of phyla, suggesting both, an ancient origin and a widespread distribution of lexA and the SOS response.


Pssm-ID: 119397 [Multi-domain]  Cd Length: 81  Bit Score: 82.99  E-value: 7.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999 121 IIKVIGDSMEPFIHNGDVIAVDVSKNklelVKNGDIVVINLDGEIYCKKLLKQPFvNEIVLSSMNSFYKDIVVNIDQIsc 200
Cdd:cd06529    2 ALRVKGDSMEPTIPDGDLVLVDPSDT----PRDGDIVVARLDGELTVKRLQRRGG-GRLRLISDNPAYPPIEIDEEEL-- 74


                 ....*..
gi 488892999 201 aEIIGVV 207
Cdd:cd06529   75 -EIVGVV 80
Peptidase_S24 pfam00717
Peptidase S24-like;
121-208 1.66e-20

Peptidase S24-like;


Pssm-ID: 425835  Cd Length: 116  Bit Score: 83.02  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999  121 IIKVIGDSMEPFIHNGDVIAVDVSKNklelVKNGDIVVINLDGEIYCKKLLKQPfvNEIVLSSMNSFYKDIVVNIDQIsc 200
Cdd:pfam00717  37 ALRVKGDSMEPGIPDGDLVLVDPSRE----ARNGDIVVARLDGEATVKRLYRDG--GGIRLISLNPEYPPIELPAEDD-- 108


                  ....*...
gi 488892999  201 AEIIGVVC 208
Cdd:pfam00717 109 VEIIGRVV 116
LexA COG1974
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ...
 121-211 8.21e-18

SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];


Pssm-ID: 441577 [Multi-domain]  Cd Length: 199  Bit Score: 78.03  E-value: 8.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999 121 IIKVIGDSM-EPFIHNGDVIAVDVSKNklelVKNGDIVVINLDGEIYCKKLLKQPfvNEIVLSSMNSFYKDIVVNIDQIs 199
Cdd:COG1974  114 ALRVKGDSMiDAGILDGDLVIVDRQLE----AENGDIVVALIDGEATVKRLYKEG--GRVRLQPENPAYPPIIIEGDDV- 186

                         90
                 ....*....|..
gi 488892999 200 caEIIGVVCKAI 211
Cdd:COG1974  187 --EILGVVVGVI 196
Peptidase_S24_S26 cd06462
The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal ...
 121-207 1.68e-16

The S24, S26 LexA/signal peptidase superfamily contains LexA-related and type I signal peptidase families. The S24 LexA protein domains include: the lambda repressor CI/C2 family and related bacterial prophage repressor proteins; LexA (EC 3.4.21.88), the repressor of genes in the cellular SOS response to DNA damage; MucA and the related UmuD proteins, which are lesion-bypass DNA polymerases, induced in response to mitogenic DNA damage; RulA, a component of the rulAB locus that confers resistance to UV, and RuvA, which is a component of the RuvABC resolvasome that catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. The S26 type I signal peptidase (SPase) family also includes mitochondrial inner membrane protease (IMP)-like members. SPases are essential membrane-bound proteases which function to cleave away the amino-terminal signal peptide from the translocated pre-protein, thus playing a crucial role in the transport of proteins across membranes in all living organisms. All members in this superfamily are unique serine proteases that carry out catalysis using a serine/lysine dyad instead of the prototypical serine/histidine/aspartic acid triad found in most serine proteases.


Pssm-ID: 119396 [Multi-domain]  Cd Length: 84  Bit Score: 71.53  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999 121 IIKVIGDSMEPFIHNGDVIAVDVSKNKlelVKNGDIVVINLDG-EIYCKKLLKQPFVNEIVLSSMNSFYKDIVVNIDQIs 199
Cdd:cd06462    2 ALRVEGDSMEPTIPDGDLVLVDKSSYE---PKRGDIVVFRLPGgELTVKRVIGLPGEGHYFLLGDNPNSPDSRIDGPPE- 77


                 ....*...
gi 488892999 200 cAEIIGVV 207
Cdd:cd06462   78 -LDIVGVV 84
PRK10276 PRK10276
translesion error-prone DNA polymerase V autoproteolytic subunit;
122-207 2.61e-10

translesion error-prone DNA polymerase V autoproteolytic subunit;


Pssm-ID: 182350  Cd Length: 139  Bit Score: 56.73  E-value: 2.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999 122 IKVIGDSM-EPFIHNGDVIAVDVSKNklelVKNGDIVVINLDGEIYCKKLLKQPFVNeivLSSMNSFYKDIVVNIDqiSC 200
Cdd:PRK10276  54 VKASGDSMiDAGISDGDLLIVDSAIT----ASHGDIVIAAVDGEFTVKKLQLRPTVQ---LIPMNSAYSPITISSE--DT 124


                 ....*..
gi 488892999 201 AEIIGVV 207
Cdd:PRK10276 125 LDVFGVV 131
Phage_CI_repr pfam07022
Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI ...
 6-66 3.27e-09

Bacteriophage CI repressor helix-turn-helix domain; This family consists of several phage CI repressor proteins and related bacterial sequences. The CI repressor is known to function as a transcriptional switch, determining whether transcription is lytic or lysogenic.


Pssm-ID: 311152  Cd Length: 65  Bit Score: 51.56  E-value: 3.27e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488892999    6 DILNRVYAILNITDDKEFCGIYEIKPNTLSTWRTRNTIPYELLLKISKEQNISLDSIFFGK 66
Cdd:pfam07022   1 AVIERLMKAYGFKSRQELADHLGVSKSTLSTWYTRDSFPAELVVRCALETGVSLEWLATGD 61
lexA TIGR00498
SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in ...
 121-207 5.47e-07

SOS regulatory protein LexA; LexA acts as a homodimer to repress a number of genes involved in the response to DNA damage (SOS response), including itself and RecA. RecA, in the presence of single-stranded DNA, acts as a co-protease to activate a latent autolytic protease activity (EC 3.4.21.88) of LexA, where the active site Ser is part of LexA. The autolytic cleavage site is an Ala-Gly bond in LexA (at position 84-85 in E. coli LexA; this sequence is replaced by Gly-Gly in Synechocystis). The cleavage leads to derepression of the SOS regulon and eventually to DNA repair. LexA in Bacillus subtilis is called DinR. LexA is much less broadly distributed than RecA. [DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 273106 [Multi-domain]  Cd Length: 199  Bit Score: 48.17  E-value: 5.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488892999  121 IIKVIGDSM-EPFIHNGDVIAVdvskNKLELVKNGDIVVINLDGEIYCKKLLKQPfvNEIVLSSMNSFYKDIVVNidqIS 199
Cdd:TIGR00498 113 LLKVMGDSMvDAGICDGDLLIV----RSQKDARNGEIVAAMIDGEVTVKRFYKDG--TKVELKPENPEFDPIVLN---AE 183


                  ....*...
gi 488892999  200 CAEIIGVV 207
Cdd:TIGR00498 184 DVTILGKV 191
S26_SPase_I cd06530
The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4. ...
 121-168 9.03e-06

The S26 Type I signal peptidase (SPase; LepB; leader peptidase B; leader peptidase I; EC 3.4.21.89) family members are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidase I, which is the most intensively studied, has two N-terminal transmembrane segments inserted in the plasma membrane and a hydrophilic, C-terminal catalytic region that is located in the periplasmic space. Although the bacterial signal peptidase I is monomeric, signal peptidases of eukaryotic cells commonly function as oligomeric complexes containing two divergent copies of the catalytic monomer. These are the IMP1 and IMP2 signal peptidases of the mitochondrial inner membrane that remove leader peptides from nuclear- and mitochondrial-encoded proteins. Also, two components of the endoplasmic reticulum signal peptidase in mammals (18-kDa and 21-kDa) belong to this family and they process many proteins that enter the ER for retention or for export to the Golgi apparatus, secretory vesicles, plasma membranes or vacuole. An atypical member of the S26 SPase type I family is the TraF peptidase which has the remarkable activity of producing a cyclic protein of the Pseudomonas pilin system. The type I signal peptidases are unique serine proteases that utilize a serine/lysine catalytic dyad mechanism in place of the classical serine/histidine/aspartic acid catalytic triad mechanism.


Pssm-ID: 119398 [Multi-domain]  Cd Length: 85  Bit Score: 42.57  E-value: 9.03e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488892999 121 IIKVIGDSMEPFIHNGDVIAVDVSKNKLELVKNGDIVVINLDG---EIYCK 168
Cdd:cd06530    2 PVVVPGGSMEPTLQPGDLVLVNKLSYGFREPKRGDVVVFKSPGdpgKPIIK 52
LepB COG0681
Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];
123-160 4.23e-03

Signal peptidase I [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440445 [Multi-domain]  Cd Length: 189  Bit Score: 36.75  E-value: 4.23e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 488892999 123 KVIGDSMEPFIHNGDVIAVDVSKNKLELVKNGDIVVIN 160
Cdd:COG0681   37 VIPSGSMEPTLLVGDRLLVNKLSYGFGEPKRGDIVVFK 74
sigpep_I_bact TIGR02227
signal peptidase I, bacterial type; This model represents signal peptidase I from most ...
 119-174 5.34e-03

signal peptidase I, bacterial type; This model represents signal peptidase I from most bacteria. Eukaryotic sequences are likely organellar. Several bacteria have multiple paralogs, but these represent isozymes of signal peptidase I. Virtually all known bacteria may be presumed to A related model finds a simlar protein in many archaea and a few bacteria, as well as a microsomal (endoplasmic reticulum) protein in eukaryotes. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 274044 [Multi-domain]  Cd Length: 142  Bit Score: 36.05  E-value: 5.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488892999  119 LDIIKVIGDSMEPFIHNGDVIAVDVSKNKLELVKNGDIVVINLD---GEIYCKKLLKQP 174
Cdd:TIGR02227   3 FFPYKIPGGSMEPTLKEGDRILVNKFAYRTSDPKRGDIVVFKDPdtnKNIYVKRIIGLP 61
 
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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