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Conserved domains on  [gi|502306620|ref|WP_012758340|]
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DUF2799 domain-containing protein [Rhizobium leguminosarum]

Protein Classification

DUF2799 domain-containing protein( domain architecture ID 10567071)

DUF2799 domain-containing protein similar to Escherichia coli YfiL

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF2799 pfam10973
Protein of unknown function (DUF2799); Some members in this family of proteins are annotated ...
 33-119 5.13e-22

Protein of unknown function (DUF2799); Some members in this family of proteins are annotated as yfiL which has no known function.


:

Pssm-ID: 431568  Cd Length: 86  Bit Score: 85.45  E-value: 5.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620   33 DWRVIGESDGAAGHePQQRFAAHAKSCERVKIVPDQTIWFQGYQTGLVRYCTPLSGLARGQAGSGYANVCPPQTAPGFLR 112
Cdd:pfam10973   1 DWYQIGYEDGMAGK-TASRLERLREACADVGVTPDAAAYLKGYQKGLEEYCTPDNGYALGLSGKSYPGVCPGDLNAEFLK 79


                  ....*..
gi 502306620  113 GFGLGSK 119
Cdd:pfam10973  80 GYQKGRD 86
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 122-196 5.19e-06

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 5.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620   122 GLQARLSSMQNDYSSKETSIDELSDKLRDAK-------------DGDRSELRRRIEDLEDDMHDIRRDQRDVQDELDRVN 188
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASrkigeiekeieqlEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764


                   ....*...
gi 502306620   189 EDVEWFQR 196
Cdd:TIGR02169  765 ARIEELEE 772
 
Name Accession Description Interval E-value
DUF2799 pfam10973
Protein of unknown function (DUF2799); Some members in this family of proteins are annotated ...
 33-119 5.13e-22

Protein of unknown function (DUF2799); Some members in this family of proteins are annotated as yfiL which has no known function.


Pssm-ID: 431568  Cd Length: 86  Bit Score: 85.45  E-value: 5.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620   33 DWRVIGESDGAAGHePQQRFAAHAKSCERVKIVPDQTIWFQGYQTGLVRYCTPLSGLARGQAGSGYANVCPPQTAPGFLR 112
Cdd:pfam10973   1 DWYQIGYEDGMAGK-TASRLERLREACADVGVTPDAAAYLKGYQKGLEEYCTPDNGYALGLSGKSYPGVCPGDLNAEFLK 79


                  ....*..
gi 502306620  113 GFGLGSK 119
Cdd:pfam10973  80 GYQKGRD 86
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 122-196 5.19e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 5.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620   122 GLQARLSSMQNDYSSKETSIDELSDKLRDAK-------------DGDRSELRRRIEDLEDDMHDIRRDQRDVQDELDRVN 188
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASrkigeiekeieqlEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764


                   ....*...
gi 502306620   189 EDVEWFQR 196
Cdd:TIGR02169  765 ARIEELEE 772
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 123-185 2.47e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 40.30  E-value: 2.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502306620  123 LQARLSSMQNDYSSKETSIDELSDKLRDAKDgDRSELRRRIEDLEDDMHDIRRDQRDVQDELD 185
Cdd:pfam08614  76 LAQRLVDLNEELQELEKKLREDERRLAALEA-ERAQLEEKLKDREEELREKRKLNQDLQDELV 137
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 136-185 8.59e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.16  E-value: 8.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 502306620 136 SKETSIDELSDKLRDAKDgDRSELRRRIEDLEDDMHDIRRDQRDVQDELD 185
Cdd:cd22887    1 ELESELQELEKRLAELEA-ELASLEEEIKDLEEELKEKNKANEILNDELI 49
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
123-186 1.86e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 1.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502306620 123 LQARLSSMQNDYSSKETSIDELSDKLRDAKDGDRSELR---------RRIEDLEDDMHDIRRDQRDVQDELDR 186
Cdd:COG2433  425 LEAEVEELEAELEEKDERIERLERELSEARSEERREIRkdreisrldREIERLERELEEERERIEELKRKLER 497
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 123-186 4.17e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 36.02  E-value: 4.17e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502306620   123 LQARLSSMQNDYSSKETSIDELSDKL-RDAKDGDRSELRRRIEDLEDDMHDIRRDQRDVQDELDR 186
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLqKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQK 87
 
Name Accession Description Interval E-value
DUF2799 pfam10973
Protein of unknown function (DUF2799); Some members in this family of proteins are annotated ...
 33-119 5.13e-22

Protein of unknown function (DUF2799); Some members in this family of proteins are annotated as yfiL which has no known function.


Pssm-ID: 431568  Cd Length: 86  Bit Score: 85.45  E-value: 5.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620   33 DWRVIGESDGAAGHePQQRFAAHAKSCERVKIVPDQTIWFQGYQTGLVRYCTPLSGLARGQAGSGYANVCPPQTAPGFLR 112
Cdd:pfam10973   1 DWYQIGYEDGMAGK-TASRLERLREACADVGVTPDAAAYLKGYQKGLEEYCTPDNGYALGLSGKSYPGVCPGDLNAEFLK 79


                  ....*..
gi 502306620  113 GFGLGSK 119
Cdd:pfam10973  80 GYQKGRD 86
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 122-196 5.19e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 5.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620   122 GLQARLSSMQNDYSSKETSIDELSDKLRDAK-------------DGDRSELRRRIEDLEDDMHDIRRDQRDVQDELDRVN 188
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRLDELSQELSDASrkigeiekeieqlEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELE 764


                   ....*...
gi 502306620   189 EDVEWFQR 196
Cdd:TIGR02169  765 ARIEELEE 772
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 123-192 1.90e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.59  E-value: 1.90e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620   123 LQARLSSMQNDYSSKETSIDELSDKLRDAKDgDRSELRRRIEDLEDDMHDIRRDQRDVQDELDRVNEDVE 192
Cdd:TIGR02169  355 LTEEYAELKEELEDLRAELEEVDKEFAETRD-ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELA 423
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 123-185 2.47e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 40.30  E-value: 2.47e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502306620  123 LQARLSSMQNDYSSKETSIDELSDKLRDAKDgDRSELRRRIEDLEDDMHDIRRDQRDVQDELD 185
Cdd:pfam08614  76 LAQRLVDLNEELQELEKKLREDERRLAALEA-ERAQLEEKLKDREEELREKRKLNQDLQDELV 137
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 123-192 4.57e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 4.57e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620   123 LQARLSSMQNDYSSKETSIDELSDKLRDAKDgDRSELRRRIEDLEDDMHDIRRDQRDVQDELDRVNEDVE 192
Cdd:TIGR02168  787 LEAQIEQLKEELKALREALDELRAELTLLNE-EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 136-185 8.59e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.16  E-value: 8.59e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 502306620 136 SKETSIDELSDKLRDAKDgDRSELRRRIEDLEDDMHDIRRDQRDVQDELD 185
Cdd:cd22887    1 ELESELQELEKRLAELEA-ELASLEEEIKDLEEELKEKNKANEILNDELI 49
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
123-186 1.86e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 1.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502306620 123 LQARLSSMQNDYSSKETSIDELSDKLRDAKDGDRSELR---------RRIEDLEDDMHDIRRDQRDVQDELDR 186
Cdd:COG2433  425 LEAEVEELEAELEEKDERIERLERELSEARSEERREIRkdreisrldREIERLERELEEERERIEELKRKLER 497
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
123-192 2.09e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 2.09e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620 123 LQARLSSMQNDYSSKETSIDELSDKLRDAKDGDRSELRRRIEDLEDDMHDIRRDQRDVQDELDRVNEDVE 192
Cdd:COG4717  161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 121-197 2.38e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 37.72  E-value: 2.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620 121 HGLQARLSSMQNDYSSKETSIDELSdklrdakdGDRSELRRRIEDLEDDMHDIRRDQRDVQDELD----RVNEDVEWFQR 196
Cdd:cd07596  113 ADALLTLQSLKKDLASKKAQLEKLK--------AAPGIKPAKVEELEEELEEAESALEEARKRYEeiseRLKEELKRFHE 184


                 .
gi 502306620 197 N 197
Cdd:cd07596  185 E 185
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 122-203 2.90e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 37.73  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502306620 122 GLQARLSSMQNDYSS--KETSIDELSDKLRDAKDGDRSELRRRIEDLEDDMHDIRRDQRD---VQDELDRVNEDVEWFQR 196
Cdd:cd22656  160 TLEKALKDLLTDEGGaiARKEIKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAalrLIADLTAADTDLDNLLA 239


                 ....*..
gi 502306620 197 NPNAALP 203
Cdd:cd22656  240 LIGPAIP 246
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 123-186 4.17e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 36.02  E-value: 4.17e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502306620   123 LQARLSSMQNDYSSKETSIDELSDKL-RDAKDGDRSELRRRIEDLEDDMHDIRRDQRDVQDELDR 186
Cdd:smart00935  23 LEKEFKKRQAELEKLEKELQKLKEKLqKDAATLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQK 87
 
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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