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Conserved domains on  [gi|1340987731|ref|XP_023775101|]
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dnaJ homolog subfamily C member 13 isoform X2 [Cyanistes caeruleus]

Protein Classification

J domain-containing protein( domain architecture ID 18340985)

J domain-containing protein similar to the N-terminal conserved domain (called J domain) of DnaJ-like proteins, which is involved in regulating the ATPase activity of heat shock protein 70 (Hsp70) by ATP hydrolysis

Gene Ontology:  GO:0006457

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RME-8_N pfam19432
DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in ...
24-843 0e+00

DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in Arabidopsis) is involved in membrane trafficking through early endosomes and in the regulation of endosomal membrane tubulation. It regulates the dynamics of SNX1 (sorting nexin 1) on the endosomal membrane. It coordinates the function of the WASH complex and the retromer SNX dimer through its interaction with FAM21 subunit in WASH complex. This is the N-terminal domain of RME-8, which is required for membrane association and interaction with FAM21 tail domain. It contains critical residues mediating phosphatidylinositol 3-phosphate (PI(3)P) binding, required for its association with endosomes.


:

Pssm-ID: 466078  Cd Length: 819  Bit Score: 1494.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731   24 CFYTTKHSWRGKYKRVFSVGTHAITTYNPNTLEVTNQWPYGDICSISPVGKGQG-TEFNLTFRKGsgKKSETLKFSTEHR 102
Cdd:pfam19432    1 CYLVTKHSWKGKYKRIFSIGTLGITTYNPSTLEVTNQWLYSDFISIKPSPKSGGpNEFIITTRKK--GKSDTMRFSSEYR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  103 TELLTEALRFRTDFSEGKI--TGRRYNCYKHHWSDTRKPVILEVTPGGIDQIDPATNKVLCSYDYRNIEGFVDITGYQGG 180
Cdd:pfam19432   79 AEILTDALRYRAKFADEYKdkLDQRFNAYKHHWSDRRIPVVLRVTPVGLEQLDPATGEVLASYLYKDIEGIILVSDYPGG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  181 FCILYGGFSRLHLFASEQREEIIKSAIEHAGNFIGISLRIRKESLEFEQYLNLRFGKYSNDESITSLAEFVVQKITPRHL 260
Cdd:pfam19432  159 FVILYGGFRRLHLFAVENRDELIKKIRENAAEYIGIPIKVAKEPITLDQFKLTRLGKYSSDEHLTSLAEFPVQKISPRHP 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  261 EPVKRVLALTEACLVERDPATYNIATLKPLGEVFAIVCDCENPQLFTIEFIKGQIRKYSSTERDSLLASLLDGVRASGNR 340
Cdd:pfam19432  239 DPVRRLLCLSETCLLERDPATYNVVTLRPLKDIFALVRDEEDPQRFSIEYKNGDVRSYTSTERDALLASLLDGVRASGNR 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  341 DVCVKMTSTHKGQRWGLLSMPVDEEVESLHLKFLAAPPNG-NFADAVFRFNANISYSGVLHAVTQDGLFSENKEKLINNA 419
Cdd:pfam19432  319 DVHVKMRRTDRGLRLGPLSVPVDEEVESQLLKFLISPPPGgSFADAVERFNANIPYSGLLHSVTQDGLFAENKEKLIVSA 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  420 ITALLSQEGDIAA-SNAELESQFQAVRRLVASKAGFLAFTQLPKFRERLGVKVVKALKRNNDGVTHASIDMLCALMCPMH 498
Cdd:pfam19432  399 LEALLEEEGDQDFiSPHELEAQFQALRRLFASKAGFSAFTAVPGFREKLGSKVVRALKRNDEAVSHAAVDMLCALMQPMH 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  499 DDYDLRQEQLNKASLLSSKKFLENLLEKFNSHVDHGTGALVISSLLDFLTFALCAPYSETTEGQQFDMLLEMVASNGRTL 578
Cdd:pfam19432  479 DNYDLRQEQLNKSSLLSSKKFLEHLLDMLVDHVERGTGALVVAAMLDFLTFALCAPYSETTDGKQFDSLLEMVADRGRSL 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  579 FKLFQHPSMAIVKGAGLVMKAIIEEGDKEIATKMQDLALSEGALPRHLHTAMFTISTDQRMLTNRQLSRHLVGLWTAENK 658
Cdd:pfam19432  559 FKLFQHPSLAIVKGAGLVMRAIIEEGDPEISARMQELALSEGALLRHLHTALFTTSRDLRLLTNRQLSRHLIALWITGNP 638
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  659 TAMNLLKRILPPGLLAYLDSTDPVPEKDADRMHVRDNLKIATDQYGKFNKVPEwqrlagkaakevEKFAKEKVDLVLMHW 738
Cdd:pfam19432  639 DAMDLLKRILPAGLLDYLDSTEEPPEDEEDLLNTRDNLKMATDHSEQKSGLKE------------QKTVEKHVEGLLQHW 706
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  739 RDRMGIAQKENIIQKPVILRKRRQRIKIEANWDLFYYRFVQDHARSNLIWNFKTREELRDTLESEMRAFNIDRELGSANV 818
Cdd:pfam19432  707 RLRIGLEFKKKFQQRPVVLRKRRQRVKSEANWPMFYYQFKKDHAKPDLIWNHKTREELREALENELRAFNQDKELAGDKV 786
                          810       820
                   ....*....|....*....|....*
gi 1340987731  819 ISWNHQEFEVKYECLSEEIKIGDYY 843
Cdd:pfam19432  787 ISWNHTEFEVRYPSLADEIKIGDYY 811
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
1313-1366 1.87e-16

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: 75.20  E-value: 1.87e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKN---PEGRDMFEKVNKAYEFLC 1366
Cdd:pfam00226    1 DYYEILGVSPDA---SDEEIKKAYRKLALKYHPDKNpgdPEAEEKFKEINEAYEVLS 54
GYF_2 pfam14237
GYF domain 2; This domain is found in bacteria, archaea and eukaryotes, and is approximately ...
988-1038 1.17e-15

GYF domain 2; This domain is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. It contains an evolutionary conserved signature W-X-Y-X6-11-GPF-X4-M-X2-W-X3-GYF, the site of interaction with proline-rich peptides. Family members include RME-8 (Required for receptor-mediated endocytosis 8), a DNAJC13 protein. RME-8 was first identified as a protein that is required for endocytosis in Caenorhabditis elegans. It coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation. Family members found in Arabidopsis include Arabidopsis trithorax-related3 (Atxr3), also known as set domain group 2 (Sdg2). It is the major enzyme responsible for H3K4me3 in Arabidopsis and SDG2-dependent H3K4m3 is critical for regulating gene expression and plant development. Another family member found in Arabidopsis is Tic56. It is an essential subunit of a 1-MDa protein complex at the inner chloroplast envelope membrane. Furthermore, Tic56 is important for rRNA processing and chloroplast ribosome assembly.


:

Pssm-ID: 464112  Cd Length: 50  Bit Score: 72.58  E-value: 1.17e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1340987731  988 WYFGNaDKERSGPYSFQEMQELWNNGNLTSKTRCWAQGMDGWRPLQVIPQL 1038
Cdd:pfam14237    1 WYYAV-NGQQQGPFSLEELRQLAASGEITPDTLVWREGMDDWKPASDVPEL 50
 
Name Accession Description Interval E-value
RME-8_N pfam19432
DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in ...
24-843 0e+00

DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in Arabidopsis) is involved in membrane trafficking through early endosomes and in the regulation of endosomal membrane tubulation. It regulates the dynamics of SNX1 (sorting nexin 1) on the endosomal membrane. It coordinates the function of the WASH complex and the retromer SNX dimer through its interaction with FAM21 subunit in WASH complex. This is the N-terminal domain of RME-8, which is required for membrane association and interaction with FAM21 tail domain. It contains critical residues mediating phosphatidylinositol 3-phosphate (PI(3)P) binding, required for its association with endosomes.


Pssm-ID: 466078  Cd Length: 819  Bit Score: 1494.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731   24 CFYTTKHSWRGKYKRVFSVGTHAITTYNPNTLEVTNQWPYGDICSISPVGKGQG-TEFNLTFRKGsgKKSETLKFSTEHR 102
Cdd:pfam19432    1 CYLVTKHSWKGKYKRIFSIGTLGITTYNPSTLEVTNQWLYSDFISIKPSPKSGGpNEFIITTRKK--GKSDTMRFSSEYR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  103 TELLTEALRFRTDFSEGKI--TGRRYNCYKHHWSDTRKPVILEVTPGGIDQIDPATNKVLCSYDYRNIEGFVDITGYQGG 180
Cdd:pfam19432   79 AEILTDALRYRAKFADEYKdkLDQRFNAYKHHWSDRRIPVVLRVTPVGLEQLDPATGEVLASYLYKDIEGIILVSDYPGG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  181 FCILYGGFSRLHLFASEQREEIIKSAIEHAGNFIGISLRIRKESLEFEQYLNLRFGKYSNDESITSLAEFVVQKITPRHL 260
Cdd:pfam19432  159 FVILYGGFRRLHLFAVENRDELIKKIRENAAEYIGIPIKVAKEPITLDQFKLTRLGKYSSDEHLTSLAEFPVQKISPRHP 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  261 EPVKRVLALTEACLVERDPATYNIATLKPLGEVFAIVCDCENPQLFTIEFIKGQIRKYSSTERDSLLASLLDGVRASGNR 340
Cdd:pfam19432  239 DPVRRLLCLSETCLLERDPATYNVVTLRPLKDIFALVRDEEDPQRFSIEYKNGDVRSYTSTERDALLASLLDGVRASGNR 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  341 DVCVKMTSTHKGQRWGLLSMPVDEEVESLHLKFLAAPPNG-NFADAVFRFNANISYSGVLHAVTQDGLFSENKEKLINNA 419
Cdd:pfam19432  319 DVHVKMRRTDRGLRLGPLSVPVDEEVESQLLKFLISPPPGgSFADAVERFNANIPYSGLLHSVTQDGLFAENKEKLIVSA 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  420 ITALLSQEGDIAA-SNAELESQFQAVRRLVASKAGFLAFTQLPKFRERLGVKVVKALKRNNDGVTHASIDMLCALMCPMH 498
Cdd:pfam19432  399 LEALLEEEGDQDFiSPHELEAQFQALRRLFASKAGFSAFTAVPGFREKLGSKVVRALKRNDEAVSHAAVDMLCALMQPMH 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  499 DDYDLRQEQLNKASLLSSKKFLENLLEKFNSHVDHGTGALVISSLLDFLTFALCAPYSETTEGQQFDMLLEMVASNGRTL 578
Cdd:pfam19432  479 DNYDLRQEQLNKSSLLSSKKFLEHLLDMLVDHVERGTGALVVAAMLDFLTFALCAPYSETTDGKQFDSLLEMVADRGRSL 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  579 FKLFQHPSMAIVKGAGLVMKAIIEEGDKEIATKMQDLALSEGALPRHLHTAMFTISTDQRMLTNRQLSRHLVGLWTAENK 658
Cdd:pfam19432  559 FKLFQHPSLAIVKGAGLVMRAIIEEGDPEISARMQELALSEGALLRHLHTALFTTSRDLRLLTNRQLSRHLIALWITGNP 638
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  659 TAMNLLKRILPPGLLAYLDSTDPVPEKDADRMHVRDNLKIATDQYGKFNKVPEwqrlagkaakevEKFAKEKVDLVLMHW 738
Cdd:pfam19432  639 DAMDLLKRILPAGLLDYLDSTEEPPEDEEDLLNTRDNLKMATDHSEQKSGLKE------------QKTVEKHVEGLLQHW 706
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  739 RDRMGIAQKENIIQKPVILRKRRQRIKIEANWDLFYYRFVQDHARSNLIWNFKTREELRDTLESEMRAFNIDRELGSANV 818
Cdd:pfam19432  707 RLRIGLEFKKKFQQRPVVLRKRRQRVKSEANWPMFYYQFKKDHAKPDLIWNHKTREELREALENELRAFNQDKELAGDKV 786
                          810       820
                   ....*....|....*....|....*
gi 1340987731  819 ISWNHQEFEVKYECLSEEIKIGDYY 843
Cdd:pfam19432  787 ISWNHTEFEVRYPSLADEIKIGDYY 811
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
1313-1366 1.87e-16

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: 75.20  E-value: 1.87e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKN---PEGRDMFEKVNKAYEFLC 1366
Cdd:pfam00226    1 DYYEILGVSPDA---SDEEIKKAYRKLALKYHPDKNpgdPEAEEKFKEINEAYEVLS 54
GYF_2 pfam14237
GYF domain 2; This domain is found in bacteria, archaea and eukaryotes, and is approximately ...
988-1038 1.17e-15

GYF domain 2; This domain is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. It contains an evolutionary conserved signature W-X-Y-X6-11-GPF-X4-M-X2-W-X3-GYF, the site of interaction with proline-rich peptides. Family members include RME-8 (Required for receptor-mediated endocytosis 8), a DNAJC13 protein. RME-8 was first identified as a protein that is required for endocytosis in Caenorhabditis elegans. It coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation. Family members found in Arabidopsis include Arabidopsis trithorax-related3 (Atxr3), also known as set domain group 2 (Sdg2). It is the major enzyme responsible for H3K4me3 in Arabidopsis and SDG2-dependent H3K4m3 is critical for regulating gene expression and plant development. Another family member found in Arabidopsis is Tic56. It is an essential subunit of a 1-MDa protein complex at the inner chloroplast envelope membrane. Furthermore, Tic56 is important for rRNA processing and chloroplast ribosome assembly.


Pssm-ID: 464112  Cd Length: 50  Bit Score: 72.58  E-value: 1.17e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1340987731  988 WYFGNaDKERSGPYSFQEMQELWNNGNLTSKTRCWAQGMDGWRPLQVIPQL 1038
Cdd:pfam14237    1 WYYAV-NGQQQGPFSLEELRQLAASGEITPDTLVWREGMDDWKPASDVPEL 50
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
1313-1366 6.51e-15

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: 70.65  E-value: 6.51e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFLC 1366
Cdd:cd06257      1 DYYDILGVPPDA---SDEEIKKAYRKLALKYHPDKNPddpEAEEKFKEINEAYEVLS 54
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1313-1366 1.07e-14

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 70.34  E-value: 1.07e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1340987731  1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKNP----EGRDMFEKVNKAYEFLC 1366
Cdd:smart00271    2 DYYEILGVPRDA---SLDEIKKAYRKLALKYHPDKNPgdkeEAEEKFKEINEAYEVLS 56
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
1313-1365 9.22e-13

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: 67.42  E-value: 9.22e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:COG0484      1 DYYEILGVSRDASAEE---IKKAYRKLAKKYHPDRNPgdpEAEEKFKEINEAYEVL 53
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
1309-1365 2.79e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 67.86  E-value: 2.79e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731 1309 MSIDDAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:PRK10767     1 MAKRDYYEVLGVSRNA---SEDEIKKAYRKLAMKYHPDRNPgdkEAEEKFKEIKEAYEVL 57
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
1313-1365 1.02e-08

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: 59.54  E-value: 1.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKN--PEGRDMFEKVNKAYEFL 1365
Cdd:TIGR02349    1 DYYEILGVSKDA---SEEEIKKAYRKLAKKYHPDRNkdKEAEEKFKEINEAYEVL 52
 
Name Accession Description Interval E-value
RME-8_N pfam19432
DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in ...
24-843 0e+00

DNAJ protein RME-8 N-terminal; DNAJ protein RME-8 (receptor-mediated endocytosis-8; Gvr2 in Arabidopsis) is involved in membrane trafficking through early endosomes and in the regulation of endosomal membrane tubulation. It regulates the dynamics of SNX1 (sorting nexin 1) on the endosomal membrane. It coordinates the function of the WASH complex and the retromer SNX dimer through its interaction with FAM21 subunit in WASH complex. This is the N-terminal domain of RME-8, which is required for membrane association and interaction with FAM21 tail domain. It contains critical residues mediating phosphatidylinositol 3-phosphate (PI(3)P) binding, required for its association with endosomes.


Pssm-ID: 466078  Cd Length: 819  Bit Score: 1494.42  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731   24 CFYTTKHSWRGKYKRVFSVGTHAITTYNPNTLEVTNQWPYGDICSISPVGKGQG-TEFNLTFRKGsgKKSETLKFSTEHR 102
Cdd:pfam19432    1 CYLVTKHSWKGKYKRIFSIGTLGITTYNPSTLEVTNQWLYSDFISIKPSPKSGGpNEFIITTRKK--GKSDTMRFSSEYR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  103 TELLTEALRFRTDFSEGKI--TGRRYNCYKHHWSDTRKPVILEVTPGGIDQIDPATNKVLCSYDYRNIEGFVDITGYQGG 180
Cdd:pfam19432   79 AEILTDALRYRAKFADEYKdkLDQRFNAYKHHWSDRRIPVVLRVTPVGLEQLDPATGEVLASYLYKDIEGIILVSDYPGG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  181 FCILYGGFSRLHLFASEQREEIIKSAIEHAGNFIGISLRIRKESLEFEQYLNLRFGKYSNDESITSLAEFVVQKITPRHL 260
Cdd:pfam19432  159 FVILYGGFRRLHLFAVENRDELIKKIRENAAEYIGIPIKVAKEPITLDQFKLTRLGKYSSDEHLTSLAEFPVQKISPRHP 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  261 EPVKRVLALTEACLVERDPATYNIATLKPLGEVFAIVCDCENPQLFTIEFIKGQIRKYSSTERDSLLASLLDGVRASGNR 340
Cdd:pfam19432  239 DPVRRLLCLSETCLLERDPATYNVVTLRPLKDIFALVRDEEDPQRFSIEYKNGDVRSYTSTERDALLASLLDGVRASGNR 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  341 DVCVKMTSTHKGQRWGLLSMPVDEEVESLHLKFLAAPPNG-NFADAVFRFNANISYSGVLHAVTQDGLFSENKEKLINNA 419
Cdd:pfam19432  319 DVHVKMRRTDRGLRLGPLSVPVDEEVESQLLKFLISPPPGgSFADAVERFNANIPYSGLLHSVTQDGLFAENKEKLIVSA 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  420 ITALLSQEGDIAA-SNAELESQFQAVRRLVASKAGFLAFTQLPKFRERLGVKVVKALKRNNDGVTHASIDMLCALMCPMH 498
Cdd:pfam19432  399 LEALLEEEGDQDFiSPHELEAQFQALRRLFASKAGFSAFTAVPGFREKLGSKVVRALKRNDEAVSHAAVDMLCALMQPMH 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  499 DDYDLRQEQLNKASLLSSKKFLENLLEKFNSHVDHGTGALVISSLLDFLTFALCAPYSETTEGQQFDMLLEMVASNGRTL 578
Cdd:pfam19432  479 DNYDLRQEQLNKSSLLSSKKFLEHLLDMLVDHVERGTGALVVAAMLDFLTFALCAPYSETTDGKQFDSLLEMVADRGRSL 558
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  579 FKLFQHPSMAIVKGAGLVMKAIIEEGDKEIATKMQDLALSEGALPRHLHTAMFTISTDQRMLTNRQLSRHLVGLWTAENK 658
Cdd:pfam19432  559 FKLFQHPSLAIVKGAGLVMRAIIEEGDPEISARMQELALSEGALLRHLHTALFTTSRDLRLLTNRQLSRHLIALWITGNP 638
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  659 TAMNLLKRILPPGLLAYLDSTDPVPEKDADRMHVRDNLKIATDQYGKFNKVPEwqrlagkaakevEKFAKEKVDLVLMHW 738
Cdd:pfam19432  639 DAMDLLKRILPAGLLDYLDSTEEPPEDEEDLLNTRDNLKMATDHSEQKSGLKE------------QKTVEKHVEGLLQHW 706
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731  739 RDRMGIAQKENIIQKPVILRKRRQRIKIEANWDLFYYRFVQDHARSNLIWNFKTREELRDTLESEMRAFNIDRELGSANV 818
Cdd:pfam19432  707 RLRIGLEFKKKFQQRPVVLRKRRQRVKSEANWPMFYYQFKKDHAKPDLIWNHKTREELREALENELRAFNQDKELAGDKV 786
                          810       820
                   ....*....|....*....|....*
gi 1340987731  819 ISWNHQEFEVKYECLSEEIKIGDYY 843
Cdd:pfam19432  787 ISWNHTEFEVRYPSLADEIKIGDYY 811
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
1313-1366 1.87e-16

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: 75.20  E-value: 1.87e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKN---PEGRDMFEKVNKAYEFLC 1366
Cdd:pfam00226    1 DYYEILGVSPDA---SDEEIKKAYRKLALKYHPDKNpgdPEAEEKFKEINEAYEVLS 54
GYF_2 pfam14237
GYF domain 2; This domain is found in bacteria, archaea and eukaryotes, and is approximately ...
988-1038 1.17e-15

GYF domain 2; This domain is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. It contains an evolutionary conserved signature W-X-Y-X6-11-GPF-X4-M-X2-W-X3-GYF, the site of interaction with proline-rich peptides. Family members include RME-8 (Required for receptor-mediated endocytosis 8), a DNAJC13 protein. RME-8 was first identified as a protein that is required for endocytosis in Caenorhabditis elegans. It coordinates the activity of the WASH complex with the function of the retromer SNX dimer to control endosomal tubulation. Family members found in Arabidopsis include Arabidopsis trithorax-related3 (Atxr3), also known as set domain group 2 (Sdg2). It is the major enzyme responsible for H3K4me3 in Arabidopsis and SDG2-dependent H3K4m3 is critical for regulating gene expression and plant development. Another family member found in Arabidopsis is Tic56. It is an essential subunit of a 1-MDa protein complex at the inner chloroplast envelope membrane. Furthermore, Tic56 is important for rRNA processing and chloroplast ribosome assembly.


Pssm-ID: 464112  Cd Length: 50  Bit Score: 72.58  E-value: 1.17e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1340987731  988 WYFGNaDKERSGPYSFQEMQELWNNGNLTSKTRCWAQGMDGWRPLQVIPQL 1038
Cdd:pfam14237    1 WYYAV-NGQQQGPFSLEELRQLAASGEITPDTLVWREGMDDWKPASDVPEL 50
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
1313-1366 6.51e-15

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: 70.65  E-value: 6.51e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFLC 1366
Cdd:cd06257      1 DYYDILGVPPDA---SDEEIKKAYRKLALKYHPDKNPddpEAEEKFKEINEAYEVLS 54
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1313-1366 1.07e-14

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 70.34  E-value: 1.07e-14
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1340987731  1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKNP----EGRDMFEKVNKAYEFLC 1366
Cdd:smart00271    2 DYYEILGVPRDA---SLDEIKKAYRKLALKYHPDKNPgdkeEAEEKFKEINEAYEVLS 56
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
1313-1365 9.22e-13

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: 67.42  E-value: 9.22e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:COG0484      1 DYYEILGVSRDASAEE---IKKAYRKLAKKYHPDRNPgdpEAEEKFKEINEAYEVL 53
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
1313-1365 6.41e-12

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 62.32  E-value: 6.41e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKN---PEGRDMFEKVNKAYEFL 1365
Cdd:COG5407      1 DPYEVLGVAKTASADE---IKKAYRKLAKKYHPDRNkgdPKAEERFKEINEAYELL 53
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
1309-1365 2.79e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 67.86  E-value: 2.79e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731 1309 MSIDDAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:PRK10767     1 MAKRDYYEVLGVSRNA---SEDEIKKAYRKLAMKYHPDRNPgdkEAEEKFKEIKEAYEVL 57
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1309-1367 1.33e-10

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 59.73  E-value: 1.33e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1340987731 1309 MSIDDAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKNPEGRD----MFEKVNKAYEFLCT 1367
Cdd:COG2214      2 PDLKDHYAVLGVPPDA---SLEEIRQAYRRLAKLLHPDRGGELKAlaeeLFQRLNEAYEVLSD 61
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
1313-1365 8.66e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 63.25  E-value: 8.66e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1340987731 1313 DAYEVLNLPRGQGQnDEskIRKAYFRLAQKYHPD--KNPEGRDMFEKVNKAYEFL 1365
Cdd:PRK14291     4 DYYEILGVSRNATQ-EE--IKKAYRRLARKYHPDfnKNPEAEEKFKEINEAYQVL 55
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
1313-1365 1.17e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 62.90  E-value: 1.17e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:PRK14277     6 DYYEILGVDRNATEEE---IKKAYRRLAKKYHPDLNPgdkEAEQKFKEINEAYEIL 58
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
1313-1365 2.18e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 62.13  E-value: 2.18e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:PRK14281     4 DYYEVLGVSRSA---DKDEIKKAYRKLALKYHPDKNPdnkEAEEHFKEVNEAYEVL 56
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1309-1377 8.16e-09

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 54.03  E-value: 8.16e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1340987731 1309 MSIDDAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDK-----NPEGRDMFEK----VNKAYEFLCTKSAKVIDGPD 1377
Cdd:COG1076      1 MQLDDAFELLGLPPDA---DDAELKRAYRKLQREHHPDRlaaglPEEEQRLALQkaaaINEAYETLKDPRGIDLAAPA 75
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
1313-1365 1.02e-08

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: 59.54  E-value: 1.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKN--PEGRDMFEKVNKAYEFL 1365
Cdd:TIGR02349    1 DYYEILGVSKDA---SEEEIKKAYRKLAKKYHPDRNkdKEAEEKFKEINEAYEVL 52
PRK14297 PRK14297
molecular chaperone DnaJ;
1309-1365 2.51e-08

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 58.64  E-value: 2.51e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731 1309 MSIDDAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:PRK14297     1 MASKDYYEVLGLEKGASDDE---IKKAFRKLAIKYHPDKNKgnkEAEEKFKEINEAYQVL 57
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
1309-1365 8.69e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 56.10  E-value: 8.69e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1340987731 1309 MSIDDAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPD--KNPEGRDMFEKVNKAYEFL 1365
Cdd:PRK14299     1 MAYKDYYAILGVPKNASQDE---IKKAFKKLARKYHPDvnKSPGAEEKFKEINEAYTVL 56
PRK14293 PRK14293
molecular chaperone DnaJ;
1313-1365 1.13e-07

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 56.54  E-value: 1.13e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPD--KNPEGRDMFEKVNKAYEFL 1365
Cdd:PRK14293     4 DYYEILGVSRDADKDE---LKRAYRRLARKYHPDvnKEPGAEDRFKEINRAYEVL 55
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
1309-1365 4.70e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 54.32  E-value: 4.70e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1340987731 1309 MSIDDAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKN--PEGRDMFEKVNKAYEFL 1365
Cdd:PRK14276     1 MNNTEYYDRLGVSKDASQDE---IKKAYRKLSKKYHPDINkePGAEEKYKEVQEAYETL 56
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
1309-1365 5.17e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 54.36  E-value: 5.17e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731 1309 MSIDDAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:PRK14301     1 MSQRDYYEVLGVSRDASEDE---IKKAYRKLALQYHPDRNPdnpEAEQKFKEAAEAYEVL 57
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
1313-1373 5.27e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 54.39  E-value: 5.27e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1340987731 1313 DAYEVLNLPRgqgQNDESKIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFLCTKSAKVI 1373
Cdd:PRK14294     5 DYYEILGVTR---DASEEEIKKSYRKLAMKYHPDRNPgdkEAEELFKEAAEAYEVLSDPKKRGI 65
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
1313-1365 5.65e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 54.08  E-value: 5.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKN--PEGRDMFEKVNKAYEFL 1365
Cdd:PRK14298     6 DYYEILGLSKDASVED---IKKAYRKLAMKYHPDKNkePDAEEKFKEISEAYAVL 57
PRK14280 PRK14280
molecular chaperone DnaJ;
1309-1365 9.77e-07

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 53.57  E-value: 9.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1340987731 1309 MSIDDAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNPE--GRDMFEKVNKAYEFL 1365
Cdd:PRK14280     1 MAKRDYYEVLGVSKSASKDE---IKKAYRKLSKKYHPDINKEegADEKFKEISEAYEVL 56
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
1313-1365 1.55e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 52.87  E-value: 1.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNPEGR----DMFEKVNKAYEFL 1365
Cdd:PRK14282     5 DYYEILGVSRNATQEE---IKRAYKRLVKEWHPDRHPENRkeaeQKFKEIQEAYEVL 58
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
1313-1365 1.55e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 52.90  E-value: 1.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKN--PEGRDMFEKVNKAYEFL 1365
Cdd:PRK14283     6 DYYEVLGVDRNA---DKKEIKKAYRKLARKYHPDVSeeEGAEEKFKEISEAYAVL 57
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
1313-1365 3.80e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 51.77  E-value: 3.80e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:PRK14284     2 DYYTILGVSKTASPEE---IKKAYRKLAVKYHPDKNPgdaEAEKRFKEVSEAYEVL 54
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
1315-1365 4.31e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 51.75  E-value: 4.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1340987731 1315 YEVLNLPRgqgQNDESKIRKAYFRLAQKYHPDK--NPEgrdMFEKVNKAYEFL 1365
Cdd:PTZ00037    31 YEVLNLSK---DCTTSEIKKAYRKLAIKHHPDKggDPE---KFKEISRAYEVL 77
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
1313-1378 4.66e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 51.21  E-value: 4.66e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNP--EGRDMFEKVNKAYEFLCTKSAK-VID-GPDP 1378
Cdd:PRK14278     4 DYYGLLGVSRNASDAE---IKRAYRKLARELHPDVNPdeEAQEKFKEISVAYEVLSDPEKRrIVDlGGDP 70
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
1309-1371 5.23e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 51.16  E-value: 5.23e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1340987731 1309 MSIDDAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPD--KNPEGRDMFEKVNKAYEFLCTKSAK 1371
Cdd:PRK14287     1 MSKRDYYEVLGVDRNASVDE---VKKAYRKLARKYHPDvnKAPDAEDKFKEVKEAYDTLSDPQKK 62
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
1313-1365 5.76e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 51.15  E-value: 5.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDK---NPEGRDMFEKVNKAYEFL 1365
Cdd:PRK14285     4 DYYEILGLSKGASKDE---IKKAYRKIAIKYHPDKnkgNKEAESIFKEATEAYEVL 56
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
1309-1365 2.44e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 49.22  E-value: 2.44e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731 1309 MSIDDAYEVLNLPRGQgqNDEsKIRKAYFRLAQKYHPDKN---PEGRDMFEKVNKAYEFL 1365
Cdd:PRK14286     1 MSERSYYDILGVSKSA--NDE-EIKSAYRKLAIKYHPDKNkgnKESEEKFKEATEAYEIL 57
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
1313-1365 3.24e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 48.73  E-value: 3.24e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1340987731 1313 DAYEVLNLPRGQgqnDESKIRKAYFRLAQKYHPDKNPE--GRDMFEKVNKAYEFL 1365
Cdd:PRK14292     3 DYYELLGVSRTA---SADEIKSAYRKLALKYHPDRNKEkgAAEKFAQINEAYAVL 54
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
1313-1365 4.58e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 48.00  E-value: 4.58e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNP----EGRDMFEKVNKAYEFL 1365
Cdd:PRK14290     4 DYYKILGVDRNASQED---IKKAFRELAKKWHPDLHPgnkaEAEEKFKEISEAYEVL 57
PRK14295 PRK14295
molecular chaperone DnaJ;
1313-1365 7.90e-05

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 47.54  E-value: 7.90e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340987731 1313 DAYEVLNLPRgqgQNDESKIRKAYFRLAQKYHPDKN---PEGRDMFEKVNKAYEFL 1365
Cdd:PRK14295    10 DYYKVLGVPK---DATEAEIKKAYRKLAREYHPDANkgdAKAEERFKEISEAYDVL 62
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
1284-1365 8.26e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 48.24  E-value: 8.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1340987731 1284 IKDPVKLLKDTLEAWKKEVEKKP---PTMSIDDA--YEVLnlprGQGQN-DESKIRKAYFRLAQKYHPDKNP--EGRDMF 1355
Cdd:PTZ00341   540 VEEEISTAEEHIEEPASDVQQDSeaaPTIEIPDTlfYDIL----GVGVNaDMKEISERYFKLAENYYPPKRSgnEGFHKF 615
                           90
                   ....*....|
gi 1340987731 1356 EKVNKAYEFL 1365
Cdd:PTZ00341   616 KKINEAYQIL 625
PRK14289 PRK14289
molecular chaperone DnaJ;
1313-1365 2.09e-04

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 45.98  E-value: 2.09e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1340987731 1313 DAYEVLNLPRgQGQNDEskIRKAYFRLAQKYHPDKNP---EGRDMFEKVNKAYEFL 1365
Cdd:PRK14289     6 DYYEVLGVSK-TATVDE--IKKAYRKKAIQYHPDKNPgdkEAEEKFKEAAEAYDVL 58
PRK10266 PRK10266
curved DNA-binding protein;
1309-1365 2.17e-04

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 45.58  E-value: 2.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1340987731 1309 MSIDDAYEVLNLprgQGQNDESKIRKAYFRLAQKYHPD--KNPEGRDMFEKVNKAYEFL 1365
Cdd:PRK10266     1 MELKDYYAIMGV---KPTDDLKTIKTAYRRLARKYHPDvsKEPDAEARFKEVAEAWEVL 56
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
1313-1365 1.38e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 43.46  E-value: 1.38e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1340987731 1313 DAYEVLNLPRGQGQNDeskIRKAYFRLAQKYHPDKNPEG--RDMFEKVNKAYEFL 1365
Cdd:PRK14300     4 DYYQILGVSKTASQAD---LKKAYLKLAKQYHPDTTDAKdaEKKFKEINAAYDVL 55
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
1309-1366 1.63e-03

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 40.22  E-value: 1.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1340987731 1309 MSIDDAYEVLNLPrgqGQNDESKIRKAYFRLAQKYHPDkNPEGRDMFEKVNKAYEFLC 1366
Cdd:PTZ00100    62 MSKSEAYKILNIS---PTASKERIREAHKQLMLRNHPD-NGGSTYIASKVNEAKDLLL 115
djlA PRK09430
co-chaperone DjlA;
1304-1368 4.14e-03

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 41.34  E-value: 4.14e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1340987731 1304 KKPPTMSIDDAYEVLNLprgQGQNDESKIRKAYFRLAQKYHPDK-----NPEgrDMFE-------KVNKAYEFLCTK 1368
Cdd:PRK09430   192 QAQRGPTLEDAYKVLGV---SESDDDQEIKRAYRKLMSEHHPDKlvakgLPP--EMMEmakekaqEIQAAYELIKKQ 263
 
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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