NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|460394786|ref|XP_004242972|]
View 

uncharacterized protein LOC101266839 [Solanum lycopersicum]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 546-643 1.94e-44

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


:

Pssm-ID: 464360  Cd Length: 92  Bit Score: 154.43  E-value: 1.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786  546 ARRITCKKCGNFHVWVVTKKTKSKARWCQECKDFHPAKDGDGWVEQPSHPFFFgmllkvdnpVAYVCADSRIYNATEWYI 625
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLW---------RYYACMDGKVYDITEWAI 71

                          90       100
                  ....*....|....*....|.
gi 460394786  626 CQG---MRCPVNSHKPSFHVN 643
Cdd:pfam14901  72 CQGdslMHCRPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 436-500 2.60e-21

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


:

Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 87.91  E-value: 2.60e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460394786  436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:pfam00226   1 DYYEILGVSP--DASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
RfbX super family cl43657
Membrane protein involved in the export of O-antigen and teichoic acid [Cell wall/membrane ...
 239-359 2.02e-03

Membrane protein involved in the export of O-antigen and teichoic acid [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG2244:

Pssm-ID: 441845 [Multi-domain]  Cd Length: 366  Bit Score: 41.09  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 239 CMRMTSILSVIWCGVLSLIAAAKFKFLLILAVVAVIGLLtGFIITFLGVAAVSISYLWFYGRFWAAVLLVLSGGALyrlk 318
Cdd:COG2244   82 ALLLRLLLSLLLALLLLLLAPFIAALLGEPELALLLLLL-ALALLLSALSAVLLALLRGLERFKLLALINILSSLL---- 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 460394786 319 heRLAV---FVITSYSVF-CAWTYVGWIGLIFILNLSFISSDILI 359
Cdd:COG2244  157 --SLLLallLALLGLGLWgLVLKYSLPLLLSGLLGLLLTNLDRLL 199
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 546-643 1.94e-44

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 154.43  E-value: 1.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786  546 ARRITCKKCGNFHVWVVTKKTKSKARWCQECKDFHPAKDGDGWVEQPSHPFFFgmllkvdnpVAYVCADSRIYNATEWYI 625
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLW---------RYYACMDGKVYDITEWAI 71

                          90       100
                  ....*....|....*....|.
gi 460394786  626 CQG---MRCPVNSHKPSFHVN 643
Cdd:pfam14901  72 CQGdslMHCRPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 436-500 2.60e-21

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 87.91  E-value: 2.60e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460394786  436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:pfam00226   1 DYYEILGVSP--DASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 436-492 3.32e-17

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 76.04  E-value: 3.32e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLD 492
Cdd:cd06257    1 DYYDILGVPP--DASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 436-508 8.63e-17

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 77.44  E-value: 8.63e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYDDELRREEL 508
Cdd:COG0484    1 DYYEILGVSR--DASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL 71
DnaJ smart00271
DnaJ molecular chaperone homology domain;
435-495 6.11e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 72.27  E-value: 6.11e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 460394786   435 TNHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGN-EKAAEAFMKLQNAYEVLLDSFK 495
Cdd:smart00271   1 TDYYEILGVPR--DASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSDPEK 60
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 438-500 7.14e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 74.03  E-value: 7.14e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 460394786 438 YSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK10767   7 YEVLGVSR--NASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 438-532 3.16e-11

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 65.70  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786  438 YSALGLMRfqNTDASVLKREYRKKAMLVHPDKNmgNEKAAEAFMK-LQNAYEVLLDSFKRKAYDdelrreelvNYLHRF- 515
Cdd:TIGR02349   3 YEILGVSK--DASEEEIKKAYRKLAKKYHPDRN--KDKEAEEKFKeINEAYEVLSDPEKRAQYD---------QFGHAGf 69

                          90
                  ....*....|....*...
gi 460394786  516 -QSPSQKGRGYGFFTSGF 532
Cdd:TIGR02349  70 nGGGGGGGGGFNGFDIGF 87
RfbX COG2244
Membrane protein involved in the export of O-antigen and teichoic acid [Cell wall/membrane ...
 239-359 2.02e-03

Membrane protein involved in the export of O-antigen and teichoic acid [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441845 [Multi-domain]  Cd Length: 366  Bit Score: 41.09  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 239 CMRMTSILSVIWCGVLSLIAAAKFKFLLILAVVAVIGLLtGFIITFLGVAAVSISYLWFYGRFWAAVLLVLSGGALyrlk 318
Cdd:COG2244   82 ALLLRLLLSLLLALLLLLLAPFIAALLGEPELALLLLLL-ALALLLSALSAVLLALLRGLERFKLLALINILSSLL---- 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 460394786 319 heRLAV---FVITSYSVF-CAWTYVGWIGLIFILNLSFISSDILI 359
Cdd:COG2244  157 --SLLLallLALLGLGLWgLVLKYSLPLLLSGLLGLLLTNLDRLL 199
Trep_Strep pfam09605
Hypothetical bacterial integral membrane protein (Trep_Strep); This family consists of ...
 215-346 2.89e-03

Hypothetical bacterial integral membrane protein (Trep_Strep); This family consists of strongly hydrophobic proteins about 190 amino acids in length with a strongly basic motif near the C-terminus. It is found in rather few species, but in paralogous families of 12 members in the oral pathogenic spirochaete Treponema denticola and 2 in Streptococcus pneumoniae R6.


Pssm-ID: 430711  Cd Length: 185  Bit Score: 39.41  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786  215 FGNIMLLLSMVwldCALRGIESFLCMRMTSILSVIWCGVLSLIAAAKF-KFLLILAVVAVIGLLtgFIITflgvaavsis 293
Cdd:pfam09605  10 FTAIYFVVMFV---VGMLGMIGPVLMLLSPAIAALLAGIVYMLMVAKVpKFGAITIMGILLGLL--FFLT---------- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 460394786  294 ylwfyGRFWAAVLLVLSGGAL----YRLKHERLAVFVITSYSVFCAWTYVGWIGLIF 346
Cdd:pfam09605  75 -----GMGWPMLLTAIIGGLLaeliAKSGGYKSKKRNILAYAVFSLWMLGPYLPIWF 126
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
 241-380 4.12e-03

Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.


Pssm-ID: 349949 [Multi-domain]  Cd Length: 378  Bit Score: 40.10  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 241 RMTSILSVIWCGVLSLIAAAKFKFLLILAVVAVIGLLTGFIITFLGVAAVSisylWF--------YGRFWAAVLLVLSGG 312
Cdd:cd06174   61 RPVLLLGLLLFALGALLFAFAPSFWLLLLGRFLLGLGSGLIDPAVLALIAD----LFperergraLGLLQAFGSVGGILG 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 460394786 313 ALyrlkherLAVFVITSYSVfcAWTYVGWIGLIFILnLSFIssdILIFFLRNNVNEQRRAHTFPDQTT 380
Cdd:cd06174  137 PL-------LGGILASSLGF--GWRAVFLIAAALAL-LAAI---LLLLVVPDPPESARAKNEEASSKS 191
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 546-643 1.94e-44

Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes and in J-domain protein interacting with viral protein (Jiv) located in the N terminal region of the pestivirus viral polypeptide. The viral protein interacts stably with non structural (NS) protein NS2, causing a conformational change in NS2-NS3 and stimulates NS2-NS3 cleavage in trans. Cleavage of NS2-NS3 increases cytopathogenicity and consequently aids viral replication. Jiv therefore acts as a regulating cofactor for NS2 auto-protease. The efficient release of NS3 from the viral polypeptide by Jiv is considered crucial to the pestivirus cytopathogenicity. In eukaryotes, it usually lies 40 residues downstream of DnaJ family pfam00226. However, the function in eukaryotes is still unknown.


Pssm-ID: 464360  Cd Length: 92  Bit Score: 154.43  E-value: 1.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786  546 ARRITCKKCGNFHVWVVTKKTKSKARWCQECKDFHPAKDGDGWVEQPSHPFFFgmllkvdnpVAYVCADSRIYNATEWYI 625
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLLW---------RYYACMDGKVYDITEWAI 71

                          90       100
                  ....*....|....*....|.
gi 460394786  626 CQG---MRCPVNSHKPSFHVN 643
Cdd:pfam14901  72 CQGdslMHCRPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 436-500 2.60e-21

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 87.91  E-value: 2.60e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460394786  436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:pfam00226   1 DYYEILGVSP--DASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 436-492 3.32e-17

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 76.04  E-value: 3.32e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLD 492
Cdd:cd06257    1 DYYDILGVPP--DASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 436-508 8.63e-17

DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 77.44  E-value: 8.63e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYDDELRREEL 508
Cdd:COG0484    1 DYYEILGVSR--DASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL 71
DnaJ smart00271
DnaJ molecular chaperone homology domain;
435-495 6.11e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 72.27  E-value: 6.11e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 460394786   435 TNHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGN-EKAAEAFMKLQNAYEVLLDSFK 495
Cdd:smart00271   1 TDYYEILGVPR--DASLDEIKKAYRKLALKYHPDKNPGDkEEAEEKFKEINEAYEVLSDPEK 60
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 438-500 7.14e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 74.03  E-value: 7.14e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 460394786 438 YSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK10767   7 YEVLGVSR--NASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 436-498 2.94e-12

Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 61.94  E-value: 2.94e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKA 498
Cdd:COG5407    1 DPYEVLGVAK--TASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRAR 61
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 438-532 3.16e-11

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 65.70  E-value: 3.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786  438 YSALGLMRfqNTDASVLKREYRKKAMLVHPDKNmgNEKAAEAFMK-LQNAYEVLLDSFKRKAYDdelrreelvNYLHRF- 515
Cdd:TIGR02349   3 YEILGVSK--DASEEEIKKAYRKLAKKYHPDRN--KDKEAEEKFKeINEAYEVLSDPEKRAQYD---------QFGHAGf 69

                          90
                  ....*....|....*...
gi 460394786  516 -QSPSQKGRGYGFFTSGF 532
Cdd:TIGR02349  70 nGGGGGGGGGFNGFDIGF 87
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 436-533 5.71e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 65.01  E-value: 5.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 436 NHYSALGLMRFQNTDAsvLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYDdelrreelvnylhRF 515
Cdd:PRK14285   4 DYYEILGLSKGASKDE--IKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYD-------------RF 68

                         90
                 ....*....|....*....
gi 460394786 516 -QSPSQKGRGYGFFTSGFT 533
Cdd:PRK14285  69 gHTAFEGGGGFEGFSGGFS 87
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
435-505 6.42e-11

Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 59.35  E-value: 6.42e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 460394786 435 TNHYSALGLmrfqNTDASV--LKREYRKKAMLVHPDKNMGN-EKAAEAFMKLQNAYEVLLDSFKRKAYDDELRR 505
Cdd:COG2214    5 KDHYAVLGV----PPDASLeeIRQAYRRLAKLLHPDRGGELkALAEELFQRLNEAYEVLSDPERRAEYDRELGQ 74
PRK14279 PRK14279
molecular chaperone DnaJ;
436-505 1.67e-10

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 63.60  E-value: 1.67e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 460394786 436 NHYSALGLmrfqNTDASV--LKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYdDELRR 505
Cdd:PRK14279  10 DFYKELGV----SSDASAeeIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEY-DETRR 76
PRK14297 PRK14297
molecular chaperone DnaJ;
434-532 2.02e-10

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 63.26  E-value: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 434 STNHYSALGLMRFQNTDAsvLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYDdelrreelvnylh 513
Cdd:PRK14297   3 SKDYYEVLGLEKGASDDE--IKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYD------------- 67

                         90
                 ....*....|....*....
gi 460394786 514 RFQSPSQKGRGyGFFTSGF 532
Cdd:PRK14297  68 QFGTADFNGAG-GFGSGGF 85
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 437-500 2.18e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 63.24  E-value: 2.18e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 460394786 437 HYSALGLMRfqntDASV--LKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14294   6 YYEILGVTR----DASEeeIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYD 67
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 432-500 2.26e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 63.08  E-value: 2.26e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 460394786 432 LNSTNHYSALGLMRFQNTDAsvLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14286   1 MSERSYYDILGVSKSANDEE--IKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 436-500 3.26e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 62.90  E-value: 3.26e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460394786 436 NHYSALGLMRFQNTDAsvLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14281   4 DYYEVLGVSRSADKDE--IKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14289 PRK14289
molecular chaperone DnaJ;
436-500 4.97e-10

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 62.16  E-value: 4.97e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14289   6 DYYEVLGVSK--TATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYD 68
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 436-534 6.06e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 61.74  E-value: 6.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYDdelrreelvNYLHRF 515
Cdd:PRK14277   6 DYYEILGVDR--NATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYD---------QFGHAA 74

                         90
                 ....*....|....*....
gi 460394786 516 QSPSQKGRGyGFFTSGFTQ 534
Cdd:PRK14277  75 FDPGGFGQG-GFGQGGFGG 92
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 436-536 9.11e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 61.30  E-value: 9.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYDdelrreelvnylhRF 515
Cdd:PRK14301   5 DYYEVLGVSR--DASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYD-------------RF 69

                         90       100
                 ....*....|....*....|.
gi 460394786 516 QSPSQKGRGYGfftSGFTQTE 536
Cdd:PRK14301  70 GHAGVNGNGGF---GGFSSAE 87
PRK14295 PRK14295
molecular chaperone DnaJ;
436-539 1.87e-09

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 60.25  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 436 NHYSALGLMRfqntDASV--LKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYDDElrREELVNYLH 513
Cdd:PRK14295  10 DYYKVLGVPK----DATEaeIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDEA--RSLFGNGGF 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 460394786 514 RFQSPSQKGRGYGF-----FTSGFTQTEAAG 539
Cdd:PRK14295  84 RPGPGGGGGGGFNFdlgdlFGGGAQGGGGAG 114
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 435-500 2.47e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 59.86  E-value: 2.47e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 460394786 435 TNHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14284   1 MDYYTILGVSK--TASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 434-500 5.56e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 58.91  E-value: 5.56e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 460394786 434 STNHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNmGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14278   2 ARDYYGLLGVSR--NASDAEIKRAYRKLARELHPDVN-PDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 436-527 5.68e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 55.60  E-value: 5.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNmGNEKAAEAFMKLQNAYEVLLDSFKRKAYD-------DELRREEL 508
Cdd:PRK14283   6 DYYEVLGVDR--NADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDqfghagmDGFSQEDI 82

                         90       100
                 ....*....|....*....|..
gi 460394786 509 ---VNYLHRFQspsqkGRGYGF 527
Cdd:PRK14283  83 fnnINFEDIFQ-----GFGFGI 99
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 432-500 7.97e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 55.09  E-value: 7.97e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 460394786 432 LNSTNHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMgNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14276   1 MNNTEYYDRLGVSK--DASQDEIKKAYRKLSKKYHPDINK-EPGAEEKYKEVQEAYETLSDPQKRAAYD 66
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 436-500 1.02e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 54.90  E-value: 1.02e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMgNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14292   3 DYYELLGVSR--TASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 436-500 1.43e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 54.47  E-value: 1.43e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 460394786 436 NHYSALGLMRfqntDASV--LKREYRKKAMLVHPDKNmGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14298   6 DYYEILGLSK----DASVedIKKAYRKLAMKYHPDKN-KEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14280 PRK14280
molecular chaperone DnaJ;
436-532 4.16e-07

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 52.80  E-value: 4.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMgNEKAAEAFMKLQNAYEVLLDSFKRKAYDdelrreelvNYLHrf 515
Cdd:PRK14280   5 DYYEVLGVSK--SASKDEIKKAYRKLSKKYHPDINK-EEGADEKFKEISEAYEVLSDDQKRAQYD---------QFGH-- 70

                         90
                 ....*....|....*..
gi 460394786 516 QSPSQKGRGYGFFTSGF 532
Cdd:PRK14280  71 AGPNQGFGGGGFGGGDF 87
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 430-501 1.08e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 51.75  E-value: 1.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 460394786 430 RLLNSTNHYSALGLMrfQNTDASVLKREYRKKAMLVHPDKNMGNEKaaeaFMKLQNAYEVLLDSFKRKAYDD 501
Cdd:PTZ00037  23 REVDNEKLYEVLNLS--KDCTTSEIKKAYRKLAIKHHPDKGGDPEK----FKEISRAYEVLSDPEKRKIYDE 88
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 406-528 2.08e-06

Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 50.80  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 406 VDRDTGIPSTSGSDVEMTSEDevLRLLNSTNHYSALGL--MRFQNTDASVLKrEYRKKAMLVHPDKNM--GNEKAAEAFM 481
Cdd:COG5269   16 ARIHSEYFKGRNVLNLYTRED--FKNWKKVDLYALLGLskYRTKAIPPQILK-AHKKKVYKYHPDKTAagGNKGCDEFFK 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 460394786 482 KLQNAYEVLLDSFKRKAYDDELRREELvnylhrfqSPSQKGRGYGFF 528
Cdd:COG5269   93 LIQKAREVLGDRKLRLQYDSNDFDADV--------PPPRIYTPDEFF 131
PRK14288 PRK14288
molecular chaperone DnaJ;
447-500 2.30e-06

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 50.46  E-value: 2.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 460394786 447 QNTDASVLKREYRKKAMLVHPDKNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14288  13 KHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYD 66
PRK14293 PRK14293
molecular chaperone DnaJ;
438-500 4.27e-06

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 49.60  E-value: 4.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 460394786 438 YSALGLMRfqNTDASVLKREYRKKAMLVHPDKNmgNEKAAE-AFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14293   6 YEILGVSR--DADKDELKRAYRRLARKYHPDVN--KEPGAEdRFKEINRAYEVLSDPETRARYD 65
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
432-492 4.37e-06

DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 44.79  E-value: 4.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 460394786 432 LNSTNHYSALGLMRfqNTDASVLKREYRKKAMLVHPDK----------NMGNEKAAEafmkLQNAYEVLLD 492
Cdd:COG1076    1 MQLDDAFELLGLPP--DADDAELKRAYRKLQREHHPDRlaaglpeeeqRLALQKAAA----INEAYETLKD 65
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 436-501 5.33e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 49.16  E-value: 5.33e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNE-KAAEAFMKLQNAYEVLLDSFKRKAYDD 501
Cdd:PRK14290   4 DYYKILGVDR--NASQEDIKKAFRELAKKWHPDLHPGNKaEAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 436-500 5.52e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 49.38  E-value: 5.52e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMgNEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14291   4 DYYEILGVSR--NATQEEIKKAYRRLARKYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYD 65
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 434-532 3.06e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 46.93  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 434 STNHYSALGLMRFQNTdaSVLKREYRKKAMLVHPDkNMGNEKAAEAFMKLQNAYEVLLDSFKRKAYDdelrreelvNYLH 513
Cdd:PRK14300   2 SQDYYQILGVSKTASQ--ADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYD---------RFGH 69

                         90       100
                 ....*....|....*....|
gi 460394786 514 -RFQspSQKGRGYGFFTSGF 532
Cdd:PRK14300  70 dAFQ--NQQSRGGGGNHGGF 87
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 432-500 6.21e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 42.69  E-value: 6.21e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 460394786 432 LNSTNHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGnEKAAEAFMKLQNAYEVLLDSFKRKAYD 500
Cdd:PRK14287   1 MSKRDYYEVLGVDR--NASVDEVKKAYRKLARKYHPDVNKA-PDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 436-539 1.15e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 41.86  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 436 NHYSALGLMRfqNTDASVLKREYRKKAMLVHPDKNMGNEkAAEAFMKLQNAYEVLLDSFKRKAYDdelrreelvNYLHR- 514
Cdd:PRK14296   5 DYYEVLGVSK--TASEQEIRQAYRKLAKQYHPDLNKSPD-AHDKMVEINEAADVLLDKDKRKQYD---------QFGHAa 72

                         90       100
                 ....*....|....*....|....*
gi 460394786 515 FQSPSQKGRGYGFFTSGFTQTEAAG 539
Cdd:PRK14296  73 FDGSSGFSSNFGDFEDLFSNMGSSG 97
RfbX COG2244
Membrane protein involved in the export of O-antigen and teichoic acid [Cell wall/membrane ...
 239-359 2.02e-03

Membrane protein involved in the export of O-antigen and teichoic acid [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 441845 [Multi-domain]  Cd Length: 366  Bit Score: 41.09  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 239 CMRMTSILSVIWCGVLSLIAAAKFKFLLILAVVAVIGLLtGFIITFLGVAAVSISYLWFYGRFWAAVLLVLSGGALyrlk 318
Cdd:COG2244   82 ALLLRLLLSLLLALLLLLLAPFIAALLGEPELALLLLLL-ALALLLSALSAVLLALLRGLERFKLLALINILSSLL---- 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 460394786 319 heRLAV---FVITSYSVF-CAWTYVGWIGLIFILNLSFISSDILI 359
Cdd:COG2244  157 --SLLLallLALLGLGLWgLVLKYSLPLLLSGLLGLLLTNLDRLL 199
Trep_Strep pfam09605
Hypothetical bacterial integral membrane protein (Trep_Strep); This family consists of ...
 215-346 2.89e-03

Hypothetical bacterial integral membrane protein (Trep_Strep); This family consists of strongly hydrophobic proteins about 190 amino acids in length with a strongly basic motif near the C-terminus. It is found in rather few species, but in paralogous families of 12 members in the oral pathogenic spirochaete Treponema denticola and 2 in Streptococcus pneumoniae R6.


Pssm-ID: 430711  Cd Length: 185  Bit Score: 39.41  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786  215 FGNIMLLLSMVwldCALRGIESFLCMRMTSILSVIWCGVLSLIAAAKF-KFLLILAVVAVIGLLtgFIITflgvaavsis 293
Cdd:pfam09605  10 FTAIYFVVMFV---VGMLGMIGPVLMLLSPAIAALLAGIVYMLMVAKVpKFGAITIMGILLGLL--FFLT---------- 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 460394786  294 ylwfyGRFWAAVLLVLSGGAL----YRLKHERLAVFVITSYSVFCAWTYVGWIGLIF 346
Cdd:pfam09605  75 -----GMGWPMLLTAIIGGLLaeliAKSGGYKSKKRNILAYAVFSLWMLGPYLPIWF 126
Colicin_V pfam02674
Colicin V production protein; Colicin V production protein is required in E. Coli for colicin ...
 264-354 3.80e-03

Colicin V production protein; Colicin V production protein is required in E. Coli for colicin V production from plasmid pColV-K30. This protein is coded for in the purF operon.


Pssm-ID: 460647  Cd Length: 143  Bit Score: 38.27  E-value: 3.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786  264 FLLILAVVAVIGLLTGFIITFLGVAAVSISylwfygrFWAAVLLVLSGGALYRLKHERLAVFVITSYSV--FCAWTYVGW 341
Cdd:pfam02674   5 ILLILLLSALLGLRRGFVREVLSLLGWVVA-------FVVASLFYPPLAPLLASLILSPALAAAVAFILlfLVVLLIGSL 77

                          90
                  ....*....|....*
gi 460394786  342 IG--LIFILNLSFIS 354
Cdd:pfam02674  78 LGvlLRKLVRLTGLG 92
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
 241-380 4.12e-03

Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.


Pssm-ID: 349949 [Multi-domain]  Cd Length: 378  Bit Score: 40.10  E-value: 4.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 460394786 241 RMTSILSVIWCGVLSLIAAAKFKFLLILAVVAVIGLLTGFIITFLGVAAVSisylWF--------YGRFWAAVLLVLSGG 312
Cdd:cd06174   61 RPVLLLGLLLFALGALLFAFAPSFWLLLLGRFLLGLGSGLIDPAVLALIAD----LFperergraLGLLQAFGSVGGILG 136

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 460394786 313 ALyrlkherLAVFVITSYSVfcAWTYVGWIGLIFILnLSFIssdILIFFLRNNVNEQRRAHTFPDQTT 380
Cdd:cd06174  137 PL-------LGGILASSLGF--GWRAVFLIAAALAL-LAAI---LLLLVVPDPPESARAKNEEASSKS 191
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH