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Conserved domains on  [gi|25151010|ref|NP_492222|]
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J domain-containing protein [Caenorhabditis elegans]

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
PubMed:  9585179|23894646|15170475|9644977

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 ...
 13-846 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: 1414.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010     13 CYLVTKHSWKGKYKRVFSIGTLAITTYNPNTLEITNQWLYEDFLSVKPLRNGGSndskQDEYKIHVRNRGKNNDMRFSSD 92
Cdd:pfam19432    1 CYLVTKHSWKGKYKRIFSIGTLGITTYNPSTLEVTNQWLYSDFISIKPSPKSGG----PNEFIITTRKKGKSDTMRFSSE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010     93 YTTDILTHCLQFSTKFADKNFEPLT--VTAFKQSWSDRRIPVTLRANASCLEQID-NRGVVVQSYPYKNIRSIGKVSDCP 169
Cdd:pfam19432   77 YRAEILTDALRYRAKFADEYKDKLDqrFNAYKHHWSDRRIPVVLRVTPVGLEQLDpATGEVLASYLYKDIEGIILVSDYP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    170 GGFVVDVGEHRRRHMFASSNNEELVKEIRRLASDNIGIIVPIAKEQLTLEDFMRTRLGLCSRDEELTSYAEFKISKITRR 249
Cdd:pfam19432  157 GGFVILYGGFRRLHLFAVENRDELIKKIRENAAEYIGIPIKVAKEPITLDQFKLTRLGKYSSDEHLTSLAEFPVQKISPR 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    250 NEMPVRRLLCLSETCIIERDLATYAVICATPLKHIVCLVRSEKDPQQFIVEYENGDGRAYVAAERDLILASLLDGIRASG 329
Cdd:pfam19432  237 HPDPVRRLLCLSETCLLERDPATYNVVTLRPLKDIFALVRDEEDPQRFSIEYKNGDVRSYTSTERDALLASLLDGVRASG 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    330 NNEVFVCGHRFERNLRVIPFSTNLDEDSESQCMKHIIAPPPGLRRCDLIRRFNANVPYSGLRFSKSHEGFFSENKGKVIV 409
Cdd:pfam19432  317 NRDVHVKMRRTDRGLRLGPLSVPVDEEVESQLLKFLISPPPGGSFADAVERFNANIPYSGLLHSVTQDGLFAENKEKLIV 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    410 NAIEAVLMENYTkDDKEYKHKTEAQLQCLRRLFASKSGFQAFTEVNGVREKLGSLVVRVLSWKSESIDHSTVEALCALMY 489
Cdd:pfam19432  397 SALEALLEEEGD-QDFISPHELEAQFQALRRLFASKAGFSAFTAVPGFREKLGSKVVRALKRNDEAVSHAAVDMLCALMQ 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    490 PMHDQYELRIEQLNKQSLMSSPKFVENLLDLIVLHVDRSTGWLVIASMLNFLTFSVCSPYSETTAGDTFDHILKLVSLRG 569
Cdd:pfam19432  476 PMHDNYDLRQEQLNKSSLLSSKKFLEHLLDMLVDHVERGTGALVVAAMLDFLTFALCAPYSETTDGKQFDSLLEMVADRG 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    570 RSFFRLFQCPSMTIVKGAGMVMRAIIEEADVETSKSMQMLALSEGAFLTHLFMSLLSTGKDLRVMTNKQLSGHLISLWIA 649
Cdd:pfam19432  556 RSLFKLFQHPSLAIVKGAGLVMRAIIEEGDPEISARMQELALSEGALLRHLHTALFTTSRDLRLLTNRQLSRHLIALWIT 635

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    650 DNQQANDLLIRCLPRGLLNYMESDEKVPVNEKDLLIVRNNFDAASNETKQ-NAMKEKfdqlrVTAEAGLERFVQHWDLEQ 728
Cdd:pfam19432  636 GNPDAMDLLKRILPAGLLDYLDSTEEPPEDEEDLLNTRDNLKMATDHSEQkSGLKEQ-----KTVEKHVEGLLQHWRLRI 710

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    729 KLNFlpkrvideKQQQRQQPVVLRKRRNRVRPNVNWKLFAYQFSKDHSQADLIWNEKTREEFRHAMDTETRALISEKEQA 808
Cdd:pfam19432  711 GLEF--------KKKFQQRPVVLRKRRQRVKSEANWPMFYYQFKKDHAKPDLIWNHKTREELREALENELRAFNQDKELA 782

                          810       820       830
                   ....*....|....*....|....*....|....*...
gi 25151010    809 PTGLpIAWNHTEFQIRYPSLLEEIKIGDYYLRLLLIEA 846
Cdd:pfam19432  783 GDKV-ISWNHTEFEVRYPSLADEIKIGDYYLRLLLEED 819
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 1324-1378 7.43e-13

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: 65.19  E-value: 7.43e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010   1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKN---PEGREMFERINAAYELLSSET 1378
Cdd:pfam00226    4 EILGVspDASDEE------IKKAYRKLALKYHPDKNpgdPEAEEKFKEINEAYEVLSDPE 57
GYF_2 pfam14237
GYF domain 2; This domain is found in bacteria, archaea and eukaryotes, and is approximately ...
 983-1033 2.29e-11

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: 60.64  E-value: 2.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 25151010    983 WYYHDKDaKQVGPLSFEKMKSLYTEKTIFEKSQIWAAGMDKWMSLAAVPQF 1033
Cdd:pfam14237    1 WYYAVNG-QQQGPFSLEELRQLAASGEITPDTLVWREGMDDWKPASDVPEL 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 ...
 13-846 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: 1414.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010     13 CYLVTKHSWKGKYKRVFSIGTLAITTYNPNTLEITNQWLYEDFLSVKPLRNGGSndskQDEYKIHVRNRGKNNDMRFSSD 92
Cdd:pfam19432    1 CYLVTKHSWKGKYKRIFSIGTLGITTYNPSTLEVTNQWLYSDFISIKPSPKSGG----PNEFIITTRKKGKSDTMRFSSE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010     93 YTTDILTHCLQFSTKFADKNFEPLT--VTAFKQSWSDRRIPVTLRANASCLEQID-NRGVVVQSYPYKNIRSIGKVSDCP 169
Cdd:pfam19432   77 YRAEILTDALRYRAKFADEYKDKLDqrFNAYKHHWSDRRIPVVLRVTPVGLEQLDpATGEVLASYLYKDIEGIILVSDYP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    170 GGFVVDVGEHRRRHMFASSNNEELVKEIRRLASDNIGIIVPIAKEQLTLEDFMRTRLGLCSRDEELTSYAEFKISKITRR 249
Cdd:pfam19432  157 GGFVILYGGFRRLHLFAVENRDELIKKIRENAAEYIGIPIKVAKEPITLDQFKLTRLGKYSSDEHLTSLAEFPVQKISPR 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    250 NEMPVRRLLCLSETCIIERDLATYAVICATPLKHIVCLVRSEKDPQQFIVEYENGDGRAYVAAERDLILASLLDGIRASG 329
Cdd:pfam19432  237 HPDPVRRLLCLSETCLLERDPATYNVVTLRPLKDIFALVRDEEDPQRFSIEYKNGDVRSYTSTERDALLASLLDGVRASG 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    330 NNEVFVCGHRFERNLRVIPFSTNLDEDSESQCMKHIIAPPPGLRRCDLIRRFNANVPYSGLRFSKSHEGFFSENKGKVIV 409
Cdd:pfam19432  317 NRDVHVKMRRTDRGLRLGPLSVPVDEEVESQLLKFLISPPPGGSFADAVERFNANIPYSGLLHSVTQDGLFAENKEKLIV 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    410 NAIEAVLMENYTkDDKEYKHKTEAQLQCLRRLFASKSGFQAFTEVNGVREKLGSLVVRVLSWKSESIDHSTVEALCALMY 489
Cdd:pfam19432  397 SALEALLEEEGD-QDFISPHELEAQFQALRRLFASKAGFSAFTAVPGFREKLGSKVVRALKRNDEAVSHAAVDMLCALMQ 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    490 PMHDQYELRIEQLNKQSLMSSPKFVENLLDLIVLHVDRSTGWLVIASMLNFLTFSVCSPYSETTAGDTFDHILKLVSLRG 569
Cdd:pfam19432  476 PMHDNYDLRQEQLNKSSLLSSKKFLEHLLDMLVDHVERGTGALVVAAMLDFLTFALCAPYSETTDGKQFDSLLEMVADRG 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    570 RSFFRLFQCPSMTIVKGAGMVMRAIIEEADVETSKSMQMLALSEGAFLTHLFMSLLSTGKDLRVMTNKQLSGHLISLWIA 649
Cdd:pfam19432  556 RSLFKLFQHPSLAIVKGAGLVMRAIIEEGDPEISARMQELALSEGALLRHLHTALFTTSRDLRLLTNRQLSRHLIALWIT 635

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    650 DNQQANDLLIRCLPRGLLNYMESDEKVPVNEKDLLIVRNNFDAASNETKQ-NAMKEKfdqlrVTAEAGLERFVQHWDLEQ 728
Cdd:pfam19432  636 GNPDAMDLLKRILPAGLLDYLDSTEEPPEDEEDLLNTRDNLKMATDHSEQkSGLKEQ-----KTVEKHVEGLLQHWRLRI 710

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    729 KLNFlpkrvideKQQQRQQPVVLRKRRNRVRPNVNWKLFAYQFSKDHSQADLIWNEKTREEFRHAMDTETRALISEKEQA 808
Cdd:pfam19432  711 GLEF--------KKKFQQRPVVLRKRRQRVKSEANWPMFYYQFKKDHAKPDLIWNHKTREELREALENELRAFNQDKELA 782

                          810       820       830
                   ....*....|....*....|....*....|....*...
gi 25151010    809 PTGLpIAWNHTEFQIRYPSLLEEIKIGDYYLRLLLIEA 846
Cdd:pfam19432  783 GDKV-ISWNHTEFEVRYPSLADEIKIGDYYLRLLLEED 819
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 1324-1378 7.43e-13

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: 65.19  E-value: 7.43e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010   1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKN---PEGREMFERINAAYELLSSET 1378
Cdd:pfam00226    4 EILGVspDASDEE------IKKAYRKLALKYHPDKNpgdPEAEEKFKEINEAYEVLSDPE 57
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1324-1378 1.03e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 61.87  E-value: 1.03e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25151010    1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKNP----EGREMFERINAAYELLSSET 1378
Cdd:smart00271    5 EILGVprDASLDE------IKKAYRKLALKYHPDKNPgdkeEAEEKFKEINEAYEVLSDPE 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 1324-1375 1.76e-11

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: 61.02  E-value: 1.76e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151010 1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLS 1375
Cdd:cd06257    4 DILGVppDASDEE------IKKAYRKLALKYHPDKNPddpEAEEKFKEINEAYEVLS 54
GYF_2 pfam14237
GYF domain 2; This domain is found in bacteria, archaea and eukaryotes, and is approximately ...
 983-1033 2.29e-11

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: 60.64  E-value: 2.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 25151010    983 WYYHDKDaKQVGPLSFEKMKSLYTEKTIFEKSQIWAAGMDKWMSLAAVPQF 1033
Cdd:pfam14237    1 WYYAVNG-QQQGPFSLEELRQLAASGEITPDTLVWREGMDDWKPASDVPEL 50
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 1324-1377 7.36e-11

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: 62.03  E-value: 7.36e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 25151010 1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLSSE 1377
Cdd:COG0484    4 EILGVsrDASAEE------IKKAYRKLAKKYHPDRNPgdpEAEEKFKEINEAYEVLSDP 56
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 1341-1377 3.39e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 55.20  E-value: 3.39e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 25151010  1341 IRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLSSE 1377
Cdd:PRK14281   20 IKKAYRKLALKYHPDKNPdnkEAEEHFKEVNEAYEVLSND 59
 
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 ...
 13-846 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: 1414.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010     13 CYLVTKHSWKGKYKRVFSIGTLAITTYNPNTLEITNQWLYEDFLSVKPLRNGGSndskQDEYKIHVRNRGKNNDMRFSSD 92
Cdd:pfam19432    1 CYLVTKHSWKGKYKRIFSIGTLGITTYNPSTLEVTNQWLYSDFISIKPSPKSGG----PNEFIITTRKKGKSDTMRFSSE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010     93 YTTDILTHCLQFSTKFADKNFEPLT--VTAFKQSWSDRRIPVTLRANASCLEQID-NRGVVVQSYPYKNIRSIGKVSDCP 169
Cdd:pfam19432   77 YRAEILTDALRYRAKFADEYKDKLDqrFNAYKHHWSDRRIPVVLRVTPVGLEQLDpATGEVLASYLYKDIEGIILVSDYP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    170 GGFVVDVGEHRRRHMFASSNNEELVKEIRRLASDNIGIIVPIAKEQLTLEDFMRTRLGLCSRDEELTSYAEFKISKITRR 249
Cdd:pfam19432  157 GGFVILYGGFRRLHLFAVENRDELIKKIRENAAEYIGIPIKVAKEPITLDQFKLTRLGKYSSDEHLTSLAEFPVQKISPR 236

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    250 NEMPVRRLLCLSETCIIERDLATYAVICATPLKHIVCLVRSEKDPQQFIVEYENGDGRAYVAAERDLILASLLDGIRASG 329
Cdd:pfam19432  237 HPDPVRRLLCLSETCLLERDPATYNVVTLRPLKDIFALVRDEEDPQRFSIEYKNGDVRSYTSTERDALLASLLDGVRASG 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    330 NNEVFVCGHRFERNLRVIPFSTNLDEDSESQCMKHIIAPPPGLRRCDLIRRFNANVPYSGLRFSKSHEGFFSENKGKVIV 409
Cdd:pfam19432  317 NRDVHVKMRRTDRGLRLGPLSVPVDEEVESQLLKFLISPPPGGSFADAVERFNANIPYSGLLHSVTQDGLFAENKEKLIV 396

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    410 NAIEAVLMENYTkDDKEYKHKTEAQLQCLRRLFASKSGFQAFTEVNGVREKLGSLVVRVLSWKSESIDHSTVEALCALMY 489
Cdd:pfam19432  397 SALEALLEEEGD-QDFISPHELEAQFQALRRLFASKAGFSAFTAVPGFREKLGSKVVRALKRNDEAVSHAAVDMLCALMQ 475

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    490 PMHDQYELRIEQLNKQSLMSSPKFVENLLDLIVLHVDRSTGWLVIASMLNFLTFSVCSPYSETTAGDTFDHILKLVSLRG 569
Cdd:pfam19432  476 PMHDNYDLRQEQLNKSSLLSSKKFLEHLLDMLVDHVERGTGALVVAAMLDFLTFALCAPYSETTDGKQFDSLLEMVADRG 555

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    570 RSFFRLFQCPSMTIVKGAGMVMRAIIEEADVETSKSMQMLALSEGAFLTHLFMSLLSTGKDLRVMTNKQLSGHLISLWIA 649
Cdd:pfam19432  556 RSLFKLFQHPSLAIVKGAGLVMRAIIEEGDPEISARMQELALSEGALLRHLHTALFTTSRDLRLLTNRQLSRHLIALWIT 635

                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    650 DNQQANDLLIRCLPRGLLNYMESDEKVPVNEKDLLIVRNNFDAASNETKQ-NAMKEKfdqlrVTAEAGLERFVQHWDLEQ 728
Cdd:pfam19432  636 GNPDAMDLLKRILPAGLLDYLDSTEEPPEDEEDLLNTRDNLKMATDHSEQkSGLKEQ-----KTVEKHVEGLLQHWRLRI 710

                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010    729 KLNFlpkrvideKQQQRQQPVVLRKRRNRVRPNVNWKLFAYQFSKDHSQADLIWNEKTREEFRHAMDTETRALISEKEQA 808
Cdd:pfam19432  711 GLEF--------KKKFQQRPVVLRKRRQRVKSEANWPMFYYQFKKDHAKPDLIWNHKTREELREALENELRAFNQDKELA 782

                          810       820       830
                   ....*....|....*....|....*....|....*...
gi 25151010    809 PTGLpIAWNHTEFQIRYPSLLEEIKIGDYYLRLLLIEA 846
Cdd:pfam19432  783 GDKV-ISWNHTEFEVRYPSLADEIKIGDYYLRLLLEED 819
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 1324-1378 7.43e-13

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: 65.19  E-value: 7.43e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151010   1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKN---PEGREMFERINAAYELLSSET 1378
Cdd:pfam00226    4 EILGVspDASDEE------IKKAYRKLALKYHPDKNpgdPEAEEKFKEINEAYEVLSDPE 57
DnaJ smart00271
DnaJ molecular chaperone homology domain;
1324-1378 1.03e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 61.87  E-value: 1.03e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25151010    1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKNP----EGREMFERINAAYELLSSET 1378
Cdd:smart00271    5 EILGVprDASLDE------IKKAYRKLALKYHPDKNPgdkeEAEEKFKEINEAYEVLSDPE 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 1324-1375 1.76e-11

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: 61.02  E-value: 1.76e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151010 1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLS 1375
Cdd:cd06257    4 DILGVppDASDEE------IKKAYRKLALKYHPDKNPddpEAEEKFKEINEAYEVLS 54
GYF_2 pfam14237
GYF domain 2; This domain is found in bacteria, archaea and eukaryotes, and is approximately ...
 983-1033 2.29e-11

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: 60.64  E-value: 2.29e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 25151010    983 WYYHDKDaKQVGPLSFEKMKSLYTEKTIFEKSQIWAAGMDKWMSLAAVPQF 1033
Cdd:pfam14237    1 WYYAVNG-QQQGPFSLEELRQLAASGEITPDTLVWREGMDDWKPASDVPEL 50
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 1324-1377 7.36e-11

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: 62.03  E-value: 7.36e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 25151010 1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLSSE 1377
Cdd:COG0484    4 EILGVsrDASAEE------IKKAYRKLAKKYHPDRNPgdpEAEEKFKEINEAYEVLSDP 56
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 1341-1377 3.39e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 55.20  E-value: 3.39e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 25151010  1341 IRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLSSE 1377
Cdd:PRK14281   20 IKKAYRKLALKYHPDKNPdnkEAEEHFKEVNEAYEVLSND 59
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 1324-1377 5.35e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 54.39  E-value: 5.35e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 25151010  1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPD--KNPEGREMFERINAAYELLSSE 1377
Cdd:PRK14291    7 EILGVsrNATQEE------IKKAYRRLARKYHPDfnKNPEAEEKFKEINEAYQVLSDP 58
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 1324-1375 7.92e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 53.61  E-value: 7.92e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 25151010  1324 EILSVDLTNEEhrkpAFIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLS 1375
Cdd:PRK10767    8 EVLGVSRNASE----DEIKKAYRKLAMKYHPDRNPgdkEAEEKFKEIKEAYEVLS 58
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 1341-1391 1.25e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 53.13  E-value: 1.25e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 25151010  1341 IRRQYYKLAAKYHPDKNP--EGREMFERINAAYELLSSetannsgmPDSHRIV 1391
Cdd:PRK14278   20 IKRAYRKLARELHPDVNPdeEAQEKFKEISVAYEVLSD--------PEKRRIV 64
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1322-1377 1.33e-06

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 48.56  E-value: 1.33e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 25151010 1322 AREIL--SVDLTNEEhrkpafIRRQYYKLAAKYHPDKNPEGR----EMFERINAAYELLSSE 1377
Cdd:COG2214    7 HYAVLgvPPDASLEE------IRQAYRRLAKLLHPDRGGELKalaeELFQRLNEAYEVLSDP 62
PRK14297 PRK14297
molecular chaperone DnaJ;
1341-1375 4.74e-06

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 51.32  E-value: 4.74e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 25151010  1341 IRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLS 1375
Cdd:PRK14297   21 IKKAFRKLAIKYHPDKNKgnkEAEEKFKEINEAYQVLS 58
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1326-1377 5.22e-06

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 46.33  E-value: 5.22e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 25151010 1326 LSVDLTNEEhrkpafIRRQYYKLAAKYHPDK-----NPEGREMFE----RINAAYELLSSE 1377
Cdd:COG1076   12 LPPDADDAE------LKRAYRKLQREHHPDRlaaglPEEEQRLALqkaaAINEAYETLKDP 66
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 1324-1375 9.89e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 50.15  E-value: 9.89e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151010  1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLS 1375
Cdd:PRK14294    8 EILGVtrDASEEE------IKKSYRKLAMKYHPDRNPgdkEAEELFKEAAEAYEVLS 58
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 1324-1375 1.64e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 49.41  E-value: 1.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 25151010  1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKNPEGR----EMFERINAAYELLS 1375
Cdd:PRK14282    8 EILGVsrNATQEE------IKRAYKRLVKEWHPDRHPENRkeaeQKFKEIQEAYEVLS 59
PRK14293 PRK14293
molecular chaperone DnaJ;
1324-1375 2.12e-05

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 49.22  E-value: 2.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 25151010  1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPD--KNPEGREMFERINAAYELLS 1375
Cdd:PRK14293    7 EILGVsrDADKDE------LKRAYRRLARKYHPDvnKEPGAEDRFKEINRAYEVLS 56
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 1341-1385 2.62e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 49.12  E-value: 2.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151010  1341 IRRQYYKLAAKYHPDKNPE--GREMFERINAAYELLSSE----------TANNSGMP 1385
Cdd:PRK14292   19 IKSAYRKLALKYHPDRNKEkgAAEKFAQINEAYAVLSDAekrahydrfgTAPGAGMP 75
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 1341-1375 2.98e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 48.40  E-value: 2.98e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 25151010  1341 IRRQYYKLAAKYHPD--KNPEGREMFERINAAYELLS 1375
Cdd:PRK14299   21 IKKAFKKLARKYHPDvnKSPGAEEKFKEINEAYTVLS 57
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 1338-1377 3.01e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 48.69  E-value: 3.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 25151010  1338 PAFIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLSSE 1377
Cdd:PRK14284   15 PEEIKKAYRKLAVKYHPDKNPgdaEAEKRFKEVSEAYEVLSDA 57
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 1324-1377 3.44e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 48.69  E-value: 3.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 25151010  1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKN--PEGREMFERINAAYELLSSE 1377
Cdd:PRK14298    9 EILGLskDASVED------IKKAYRKLAMKYHPDKNkePDAEEKFKEISEAYAVLSDA 60
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 1341-1377 3.54e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 48.55  E-value: 3.54e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 25151010  1341 IRRQYYKLAAKYHPDKN--PEGREMFERINAAYELLSSE 1377
Cdd:PRK14276   21 IKKAYRKLSKKYHPDINkePGAEEKYKEVQEAYETLSDP 59
PRK14288 PRK14288
molecular chaperone DnaJ;
1324-1377 6.85e-05

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 47.76  E-value: 6.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151010  1324 EILSVdltnEEHRKPAFIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLSSE 1377
Cdd:PRK14288    7 EILEV----EKHSNQETIKKSYRKLALKYHPDRNAgdkEAEEKFKLINEAYGVLSDE 59
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 1324-1377 7.59e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 47.51  E-value: 7.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 25151010  1324 EILSVDLTNEEHRkpafIRRQYYKLAAKYHPDKN--PEGREMFERINAAYELLSSE 1377
Cdd:PRK14283    9 EVLGVDRNADKKE----IKKAYRKLARKYHPDVSeeEGAEEKFKEISEAYAVLSDD 60
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 1324-1374 5.99e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 44.73  E-value: 5.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 25151010  1324 EILSV--DLTNEEhrkpafIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELL 1374
Cdd:PRK14301    8 EVLGVsrDASEDE------IKKAYRKLALQYHPDRNPdnpEAEQKFKEAAEAYEVL 57
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 1326-1377 7.99e-04

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 44.43  E-value: 7.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 25151010  1326 LSVDLTNEEhrkpafIRRQYYKLAAKYHPDKNPEgREMFERINAAYELLSSE 1377
Cdd:PTZ00037   36 LSKDCTTSE------IKKAYRKLAIKHHPDKGGD-PEKFKEISRAYEVLSDP 80
PRK14289 PRK14289
molecular chaperone DnaJ;
1324-1375 1.30e-03

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 43.67  E-value: 1.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 25151010  1324 EILSVD--LTNEEhrkpafIRRQYYKLAAKYHPDKNP---EGREMFERINAAYELLS 1375
Cdd:PRK14289    9 EVLGVSktATVDE------IKKAYRKKAIQYHPDKNPgdkEAEEKFKEAAEAYDVLS 59
PRK14295 PRK14295
molecular chaperone DnaJ;
1341-1377 2.01e-03

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 42.91  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 25151010  1341 IRRQYYKLAAKYHPDKN---PEGREMFERINAAYELLSSE 1377
Cdd:PRK14295   26 IKKAYRKLAREYHPDANkgdAKAEERFKEISEAYDVLSDE 65
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 1325-1375 2.03e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 43.00  E-value: 2.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 25151010  1325 ILSVDLTNEEHRkpafIRRQYYKLAAKYHPDKNP----EGREMFERINAAYELLS 1375
Cdd:PRK14290    8 ILGVDRNASQED----IKKAFRELAKKWHPDLHPgnkaEAEEKFKEISEAYEVLS 58
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 1324-1374 5.85e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 41.47  E-value: 5.85e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 25151010  1324 EILSVDLTNEEHRkpafIRRQYYKLAAKYHPD--KNPEGREMFERINAAYELL 1374
Cdd:PRK14296    8 EVLGVSKTASEQE----IRQAYRKLAKQYHPDlnKSPDAHDKMVEINEAADVL 56
 
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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