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Conserved domains on  [gi|334182627|ref|NP_173112|]
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Chaperone DnaJ-domain superfamily protein [Arabidopsis thaliana]

Protein Classification

DnaJ homolog subfamily C member 14( domain architecture ID 10446388)

DnaJ homolog subfamily C member 14 (DNAJC14) regulates the export of target proteins, such as dopamine D1 receptor (DRD1), from the endoplasmic reticulum to the cell surface

CATH:  1.10.287.110
Gene Ontology:  GO:0015031|GO:0050780
PubMed:  35729039|9644977|8016869|15170475|9585179|10542335
SCOP:  4000605

Graphical summary

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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 ...
 388-484 1.67e-47

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: 160.21  E-value: 1.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627  388 SRRIHCTKCGNSHIWVCTNRSKAKARWCQECGQYHQAKDGDGWVEHKGTLVFekahkieiPRAFVCAEGKVFDVSEWAIC 467
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLL--------WRYYACMDGKVYDITEWAIC 72

                          90       100
                  ....*....|....*....|
gi 334182627  468 QG---MACRPNTHRPSFHVN 484
Cdd:pfam14901  73 QGdslMHCRPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 291-355 1.93e-23

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: 93.31  E-value: 1.93e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182627  291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:pfam00226   1 DYYEILGVS--PDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
PTZ00341 super family cl31759
Ring-infected erythrocyte surface antigen; Provisional
 213-356 1.89e-05

Ring-infected erythrocyte surface antigen; Provisional


The actual alignment was detected with superfamily member PTZ00341:

Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 47.86  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627  213 VEEPTKPETVIDEEFPGEFEYSSVPAEEAEKKVHEDKSSTKPASS------STVVSNMKE-ISTVKvvkiETDSADEMKR 285
Cdd:PTZ00341  494 VEEPTVADIVEQETVDEHVEEPAVDENEEQQTADEHVEEPTIAEEhveeeiSTAEEHIEEpASDVQ----QDSEAAPTIE 569

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182627  286 ILDSLnHYEALGLPLfkKIDAALLKKDYRKKAMLVHPDKNMGSPlASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PTZ00341  570 IPDTL-FYDILGVGV--NADMKEISERYFKLAENYYPPKRSGNE-GFHKFKKINEAYQILGDIDKKKMYNK 636
NorM super family cl43171
Na+-driven multidrug efflux pump, DinF/NorM/MATE family [Defense mechanisms];
105-203 8.92e-03

Na+-driven multidrug efflux pump, DinF/NorM/MATE family [Defense mechanisms];


The actual alignment was detected with superfamily member COG0534:

Pssm-ID: 440300 [Multi-domain]  Cd Length: 427  Bit Score: 38.59  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627 105 LGMGAAGAVVLYLGRTPgifIVGLF---------GILILWMYA-NFWITGTLFIVGGYLFSLNHARVVVLMATMyAMYCV 174
Cdd:COG0534  316 LGIGLLLALLLFLFPEP---IIGLFtddpevialAATYLRIAAlFQPFDGLQFVLSGALRGAGDTRFPMIISLL-RLWLV 391

                         90       100       110
                 ....*....|....*....|....*....|....
gi 334182627 175 KVRLGWPGVILSMNL-----AFLSNDIFICLLQW 203
Cdd:COG0534  392 RLPLAYLLAFLGLGLtgvwlALPIGEVLRALLLL 425
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 388-484 1.67e-47

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: 160.21  E-value: 1.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627  388 SRRIHCTKCGNSHIWVCTNRSKAKARWCQECGQYHQAKDGDGWVEHKGTLVFekahkieiPRAFVCAEGKVFDVSEWAIC 467
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLL--------WRYYACMDGKVYDITEWAIC 72

                          90       100
                  ....*....|....*....|
gi 334182627  468 QG---MACRPNTHRPSFHVN 484
Cdd:pfam14901  73 QGdslMHCRPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 291-355 1.93e-23

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: 93.31  E-value: 1.93e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182627  291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:pfam00226   1 DYYEILGVS--PDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 291-390 3.92e-20

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: 86.68  E-value: 3.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDELLKKEESRTKIVCQ 370
Cdd:COG0484    1 DYYEILGVS--RDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELA 78

                         90       100
                 ....*....|....*....|
gi 334182627 371 SSHASSHQNSAAYRSEESRR 390
Cdd:COG0484   79 ESAAAEAAAAEAKEEAAEAG 98
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 291-347 1.56e-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: 76.43  E-value: 1.56e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSD 347
Cdd:cd06257    1 DYYDILGVP--PDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
291-350 7.77e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.58  E-value: 7.77e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182627   291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSP-LASESFKKLQSAYEVLSDSVK 350
Cdd:smart00271   2 DYYEILGVP--RDASLDEIKKAYRKLALKYHPDKNPGDKeEAEEKFKEINEAYEVLSDPEK 60
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 283-355 6.30e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 79.42  E-value: 6.30e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334182627 283 MKRildslNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK10767   2 AKR-----DYYEVLGVS--RNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 293-356 7.36e-14

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: 73.02  E-value: 7.36e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182627  293 YEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNmGSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:TIGR02349   3 YEILGVS--KDASEEEIKKAYRKLAKKYHPDRN-KDKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 213-356 1.89e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 47.86  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627  213 VEEPTKPETVIDEEFPGEFEYSSVPAEEAEKKVHEDKSSTKPASS------STVVSNMKE-ISTVKvvkiETDSADEMKR 285
Cdd:PTZ00341  494 VEEPTVADIVEQETVDEHVEEPAVDENEEQQTADEHVEEPTIAEEhveeeiSTAEEHIEEpASDVQ----QDSEAAPTIE 569

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182627  286 ILDSLnHYEALGLPLfkKIDAALLKKDYRKKAMLVHPDKNMGSPlASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PTZ00341  570 IPDTL-FYDILGVGV--NADMKEISERYFKLAENYYPPKRSGNE-GFHKFKKINEAYQILGDIDKKKMYNK 636
NorM COG0534
Na+-driven multidrug efflux pump, DinF/NorM/MATE family [Defense mechanisms];
105-203 8.92e-03

Na+-driven multidrug efflux pump, DinF/NorM/MATE family [Defense mechanisms];


Pssm-ID: 440300 [Multi-domain]  Cd Length: 427  Bit Score: 38.59  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627 105 LGMGAAGAVVLYLGRTPgifIVGLF---------GILILWMYA-NFWITGTLFIVGGYLFSLNHARVVVLMATMyAMYCV 174
Cdd:COG0534  316 LGIGLLLALLLFLFPEP---IIGLFtddpevialAATYLRIAAlFQPFDGLQFVLSGALRGAGDTRFPMIISLL-RLWLV 391

                         90       100       110
                 ....*....|....*....|....*....|....
gi 334182627 175 KVRLGWPGVILSMNL-----AFLSNDIFICLLQW 203
Cdd:COG0534  392 RLPLAYLLAFLGLGLtgvwlALPIGEVLRALLLL 425
 
Name Accession Description Interval E-value
Jiv90 pfam14901
Cleavage inducing molecular chaperone; Jiv90 is a fragment of the DnaJ protein in eukaryotes ...
 388-484 1.67e-47

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: 160.21  E-value: 1.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627  388 SRRIHCTKCGNSHIWVCTNRSKAKARWCQECGQYHQAKDGDGWVEHKGTLVFekahkieiPRAFVCAEGKVFDVSEWAIC 467
Cdd:pfam14901   1 ANTIRCTKCGNRHKRICTDRPKYAARWCQECKIFHSAKDGDIWVESSMLGLL--------WRYYACMDGKVYDITEWAIC 72

                          90       100
                  ....*....|....*....|
gi 334182627  468 QG---MACRPNTHRPSFHVN 484
Cdd:pfam14901  73 QGdslMHCRPNTHRVQYRIN 92
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 291-355 1.93e-23

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: 93.31  E-value: 1.93e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182627  291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:pfam00226   1 DYYEILGVS--PDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 291-390 3.92e-20

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: 86.68  E-value: 3.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDELLKKEESRTKIVCQ 370
Cdd:COG0484    1 DYYEILGVS--RDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELA 78

                         90       100
                 ....*....|....*....|
gi 334182627 371 SSHASSHQNSAAYRSEESRR 390
Cdd:COG0484   79 ESAAAEAAAAEAKEEAAEAG 98
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 291-347 1.56e-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: 76.43  E-value: 1.56e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSD 347
Cdd:cd06257    1 DYYDILGVP--PDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
291-350 7.77e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.58  E-value: 7.77e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182627   291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSP-LASESFKKLQSAYEVLSDSVK 350
Cdd:smart00271   2 DYYEILGVP--RDASLDEIKKAYRKLALKYHPDKNPGDKeEAEEKFKEINEAYEVLSDPEK 60
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 283-355 6.30e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 79.42  E-value: 6.30e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334182627 283 MKRildslNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK10767   2 AKR-----DYYEVLGVS--RNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 293-356 7.36e-14

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: 73.02  E-value: 7.36e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182627  293 YEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNmGSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:TIGR02349   3 YEILGVS--KDASEEEIKKAYRKLAKKYHPDRN-KDKEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 291-352 1.49e-13

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 65.41  E-value: 1.49e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRR 352
Cdd:COG5407    1 DPYEVLGVA--KTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRA 60
PRK14295 PRK14295
molecular chaperone DnaJ;
291-356 5.20e-13

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 70.65  E-value: 5.20e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14295  10 DYYKVLGVP--KDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDE 73
PRK14289 PRK14289
molecular chaperone DnaJ;
291-357 9.11e-13

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 69.86  E-value: 9.11e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDEL 357
Cdd:PRK14289   6 DYYEVLGVS--KTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQF 70
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
291-359 1.06e-12

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 63.97  E-value: 1.06e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334182627 291 NHYEALGLPL---FKKIDAAllkkdYRKKAMLVHPDKNMGSP-LASESFKKLQSAYEVLSDSVKRRDYDELLK 359
Cdd:COG2214    6 DHYAVLGVPPdasLEEIRQA-----YRRLAKLLHPDRGGELKaLAEELFQRLNEAYEVLSDPERRAEYDRELG 73
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 283-356 1.09e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 69.84  E-value: 1.09e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182627 283 MKRildslNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14281   1 MKR-----DYYEVLGVS--RSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQ 67
PRK14279 PRK14279
molecular chaperone DnaJ;
291-357 3.68e-12

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 68.22  E-value: 3.68e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDEL 357
Cdd:PRK14279  10 DFYKELGVS--SDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDET 74
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 292-356 1.02e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 66.71  E-value: 1.02e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182627 292 HYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14294   6 YYEILGVT--RDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQ 68
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 291-355 1.09e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 66.41  E-value: 1.09e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNmGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK14298   6 DYYEILGLS--KDASVEDIKKAYRKLAMKYHPDKN-KEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 291-356 2.59e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 65.59  E-value: 2.59e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14277   6 DYYEILGVD--RNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQ 69
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 290-355 4.97e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 64.48  E-value: 4.97e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 290 LNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK14284   1 MDYYTILGVS--KTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14297 PRK14297
molecular chaperone DnaJ;
291-356 6.16e-11

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 64.42  E-value: 6.16e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14297   5 DYYEVLGLE--KGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQ 68
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 287-355 1.77e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 62.84  E-value: 1.77e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334182627 287 LDSLNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK14301   1 MSQRDYYEVLGVS--RDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYD 67
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 283-356 1.82e-10

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 62.92  E-value: 1.82e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 283 MKRILDSLNHYEALGLplfkKIDAAL--LKKDYRKKAMLVHPDKNmGSPlasESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PTZ00037  21 RKREVDNEKLYEVLNL----SKDCTTseIKKAYRKLAIKHHPDKG-GDP---EKFKEISRAYEVLSDPEKRKIYDE 88
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 290-355 1.06e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 60.29  E-value: 1.06e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 290 LNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMgSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK14292   2 MDYYELLGVS--RTASADEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 286-356 1.47e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 59.84  E-value: 1.47e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182627 286 ILDSLNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNmGSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14283   1 MAEKRDYYEVLGVD--RNADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDQ 68
PRK14280 PRK14280
molecular chaperone DnaJ;
291-356 1.52e-09

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 59.74  E-value: 1.52e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMgSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14280   5 DYYEVLGVS--KSASKDEIKKAYRKLSKKYHPDINK-EEGADEKFKEISEAYEVLSDDQKRAQYDQ 67
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 292-359 1.72e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 59.62  E-value: 1.72e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334182627 292 HYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDELLK 359
Cdd:PRK14286   6 YYDILGVS--KSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGK 71
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 283-355 4.06e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 58.46  E-value: 4.06e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334182627 283 MKRildslNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK14285   1 MKR-----DYYEILGLS--KGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 293-356 4.53e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 58.56  E-value: 4.53e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334182627 293 YEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMgSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14276   7 YDRLGVS--KDASQDEIKKAYRKLSKKYHPDINK-EPGAEEKYKEVQEAYETLSDPQKRAAYDQ 67
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 291-356 1.18e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 57.09  E-value: 1.18e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMgSPLASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14291   4 DYYEILGVS--RNATQEEIKKAYRRLARKYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYDQ 66
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 309-355 1.56e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 56.60  E-value: 1.56e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 334182627 309 LKKDYRKKAMLVHPDKNmGSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK14278  20 IKRAYRKLARELHPDVN-PDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 291-355 2.32e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 55.72  E-value: 2.32e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMgSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK14299   5 DYYAILGVP--KNASQDEIKKAFKKLARKYHPDVNK-SPGAEEKFKEINEAYTVLSDPEKRRIYD 66
PRK14293 PRK14293
molecular chaperone DnaJ;
293-355 9.53e-08

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 54.23  E-value: 9.53e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334182627 293 YEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMgSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK14293   6 YEILGVS--RDADKDELKRAYRRLARKYHPDVNK-EPGAEDRFKEINRAYEVLSDPETRARYD 65
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 291-355 1.06e-07

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 54.27  E-value: 1.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334182627 291 NHYEALGLPLFK-KIDAALLKKDYRKKAMLVHPDKNM--GSPLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:COG5269   44 DLYALLGLSKYRtKAIPPQILKAHKKKVYKYHPDKTAagGNKGCDEFFKLIQKAREVLGDRKLRLQYD 111
PRK14288 PRK14288
molecular chaperone DnaJ;
290-360 1.57e-07

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 53.54  E-value: 1.57e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182627 290 LNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSPLASESFKKLQSAYEVLSDSVKRRDYDELLKK 360
Cdd:PRK14288   3 LSYYEILEVE--KHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKK 71
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
291-347 5.98e-07

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 47.10  E-value: 5.98e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGSplASESFKKL--------QSAYEVLSD 347
Cdd:COG1076    5 DAFELLGLP--PDADDAELKRAYRKLQREHHPDRLAAG--LPEEEQRLalqkaaaiNEAYETLKD 65
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 291-355 7.75e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 51.33  E-value: 7.75e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMGS-PLASESFKKLQSAYEVLSDSVKRRDYD 355
Cdd:PRK14282   5 DYYEILGVS--RNATQEEIKRAYKRLVKEWHPDRHPENrKEAEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 309-356 1.11e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 51.09  E-value: 1.11e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 334182627 309 LKKDYRKKAMLVHPDKNMGSPL-ASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PRK14290  20 IKKAFRELAKKWHPDLHPGNKAeAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 289-357 1.17e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 50.78  E-value: 1.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334182627 289 SLNHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDkNMGSPLASESFKKLQSAYEVLSDSVKRRDYDEL 357
Cdd:PRK14300   2 SQDYYQILGVS--KTASQADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYDRF 67
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 291-357 1.98e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 50.01  E-value: 1.98e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182627 291 NHYEALGLPLFKKIDAalLKKDYRKKAMLVHPDKNMgSPLASESFKKLQSAYEVLSDSVKRRDYDEL 357
Cdd:PRK14287   5 DYYEVLGVDRNASVDE--VKKAYRKLARKYHPDVNK-APDAEDKFKEVKEAYDTLSDPQKKAHYDQF 68
PRK10266 PRK10266
curved DNA-binding protein;
305-357 8.95e-06

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 47.89  E-value: 8.95e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 334182627 305 DAALLKKDYRKKAMLVHPDKNMgSPLASESFKKLQSAYEVLSDSVKRRDYDEL 357
Cdd:PRK10266  17 DLKTIKTAYRRLARKYHPDVSK-EPDAEARFKEVAEAWEVLSDEQRRAEYDQL 68
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 213-356 1.89e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 47.86  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627  213 VEEPTKPETVIDEEFPGEFEYSSVPAEEAEKKVHEDKSSTKPASS------STVVSNMKE-ISTVKvvkiETDSADEMKR 285
Cdd:PTZ00341  494 VEEPTVADIVEQETVDEHVEEPAVDENEEQQTADEHVEEPTIAEEhveeeiSTAEEHIEEpASDVQ----QDSEAAPTIE 569

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334182627  286 ILDSLnHYEALGLPLfkKIDAALLKKDYRKKAMLVHPDKNMGSPlASESFKKLQSAYEVLSDSVKRRDYDE 356
Cdd:PTZ00341  570 IPDTL-FYDILGVGV--NADMKEISERYFKLAENYYPPKRSGNE-GFHKFKKINEAYQILGDIDKKKMYNK 636
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 291-357 8.53e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 44.94  E-value: 8.53e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334182627 291 NHYEALGLPlfKKIDAALLKKDYRKKAMLVHPDKNMgSPLASESFKKLQSAYEVLSDSVKRRDYDEL 357
Cdd:PRK14296   5 DYYEVLGVS--KTASEQEIRQAYRKLAKQYHPDLNK-SPDAHDKMVEINEAADVLLDKDKRKQYDQF 68
PHA03102 PHA03102
Small T antigen; Reviewed
 294-353 2.70e-04

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 41.58  E-value: 2.70e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627 294 EALGLPLFKKIDAALLKKDYRKKAMLVHPDKNmGSPlasESFKKLQSAYEVLSDSVKRRD 353
Cdd:PHA03102   9 DLLGLPRSAWGNLPLMRKAYLRKCLEFHPDKG-GDE---EKMKELNTLYKKFRESVKSLR 64
PHA02624 PHA02624
large T antigen; Provisional
 294-351 3.75e-04

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 43.43  E-value: 3.75e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 334182627 294 EALGLPLFKKIDAALLKKDYRKKAMLVHPDKNmGSPlasESFKKLQSAYEVLSDSVKR 351
Cdd:PHA02624  15 DLLGLPMAAWGNLPLMRKAYLRKCKEYHPDKG-GDE---EKMKRLNSLYKKLQEGVKS 68
hscB PRK01356
co-chaperone HscB; Provisional
 291-359 5.50e-03

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 37.93  E-value: 5.50e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334182627 291 NHYEALGLPLFKKIDAALLKKDYRKKAMLVHPD-------KNMGSPLASEsfkkLQSAYEVLSDSVKRRDYDELLK 359
Cdd:PRK01356   3 NYFQLLGLPQEYNIDLKILEKQYFAMQVKYHPDkaktlqeKEQNLIIASE----LNNAYSTLKDALKRAEYMLLLQ 74
NorM COG0534
Na+-driven multidrug efflux pump, DinF/NorM/MATE family [Defense mechanisms];
105-203 8.92e-03

Na+-driven multidrug efflux pump, DinF/NorM/MATE family [Defense mechanisms];


Pssm-ID: 440300 [Multi-domain]  Cd Length: 427  Bit Score: 38.59  E-value: 8.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334182627 105 LGMGAAGAVVLYLGRTPgifIVGLF---------GILILWMYA-NFWITGTLFIVGGYLFSLNHARVVVLMATMyAMYCV 174
Cdd:COG0534  316 LGIGLLLALLLFLFPEP---IIGLFtddpevialAATYLRIAAlFQPFDGLQFVLSGALRGAGDTRFPMIISLL-RLWLV 391

                         90       100       110
                 ....*....|....*....|....*....|....
gi 334182627 175 KVRLGWPGVILSMNL-----AFLSNDIFICLLQW 203
Cdd:COG0534  392 RLPLAYLLAFLGLGLtgvwlALPIGEVLRALLLL 425
 
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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