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Conserved domains on  [gi|389616158|ref|NP_001254504|]
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dnaJ homolog subfamily C member 17 [Gallus gallus]

Protein Classification

DnaJ homolog subfamily C member 17( domain architecture ID 11087556)

DnaJ homolog subfamily C member 17 (DNAJC17) may play a role in splicing-related processes

CATH:  1.10.287.110
Gene Ontology:  GO:0006457|GO:0000390|GO:0006357|GO:0003723
PubMed:  15170475|35729039|9644977|8016869|9585179|10542335
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RRM_DNAJC17 cd12429
RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD ...
 172-248 9.61e-35

RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD corresponds to the RRM of some eukaryotic DnaJ homolog subfamily C member 17 and similar proteins. 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. Members in this family contains an N-terminal DnaJ domain or J-domain, which mediates the interaction with Hsp70. They also contains a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), at the C-terminus, which may play an essential role in RNA binding.


:

Pssm-ID: 409863 [Multi-domain]  Cd Length: 74  Bit Score: 120.84  E-value: 9.61e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158 172 PKLKLKWKCRKEdetGGGYSKEVLLRILQKYGDVLNLLISSRKAGSAVVEFATVKAAEMAVKNEVGLTDNPLKISWL 248
Cdd:cd12429    1 PRLKVKWKSKKG---NGGYSEEELRKIFSKYGPVSDVVISSKKKGSAIVEFATVVAADAAVENEVGLPDNPLLVSWL 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 18-73 2.53e-18

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: 77.51  E-value: 2.53e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 389616158   18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYD 73
Cdd:pfam00226   8 VSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 18-134 2.03e-15

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: 72.04  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDKVRKAkKQAAERTQKLDEKRKKVK 97
Cdd:COG0484    8 VSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHA-AELLLATELAESAAAEAA 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 389616158  98 LDLEAREREAQARDNEEEEIRITRTLEQEIIRLREEG 134
Cdd:COG0484   87 AAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLAL 123
 
Name Accession Description Interval E-value
RRM_DNAJC17 cd12429
RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD ...
 172-248 9.61e-35

RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD corresponds to the RRM of some eukaryotic DnaJ homolog subfamily C member 17 and similar proteins. 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. Members in this family contains an N-terminal DnaJ domain or J-domain, which mediates the interaction with Hsp70. They also contains a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), at the C-terminus, which may play an essential role in RNA binding.


Pssm-ID: 409863 [Multi-domain]  Cd Length: 74  Bit Score: 120.84  E-value: 9.61e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158 172 PKLKLKWKCRKEdetGGGYSKEVLLRILQKYGDVLNLLISSRKAGSAVVEFATVKAAEMAVKNEVGLTDNPLKISWL 248
Cdd:cd12429    1 PRLKVKWKSKKG---NGGYSEEELRKIFSKYGPVSDVVISSKKKGSAIVEFATVVAADAAVENEVGLPDNPLLVSWL 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 18-73 2.53e-18

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: 77.51  E-value: 2.53e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 389616158   18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYD 73
Cdd:pfam00226   8 VSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 18-134 2.03e-15

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: 72.04  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDKVRKAkKQAAERTQKLDEKRKKVK 97
Cdd:COG0484    8 VSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHA-AELLLATELAESAAAEAA 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 389616158  98 LDLEAREREAQARDNEEEEIRITRTLEQEIIRLREEG 134
Cdd:COG0484   87 AAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLAL 123
PRK14279 PRK14279
molecular chaperone DnaJ;
18-77 2.73e-15

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 75.54  E-value: 2.73e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDKVRK 77
Cdd:PRK14279  17 VSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDETRR 76
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 18-65 2.22e-14

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: 66.41  E-value: 2.22e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTD 65
Cdd:cd06257    8 VPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 18-74 9.97e-13

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: 67.63  E-value: 9.97e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158   18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:TIGR02349   8 VSKDASEEEIKKAYRKLAKKYHPDRNKD-KEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
18-65 7.00e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 56.86  E-value: 7.00e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 389616158    18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEV-FHQLSQALAVLTD 65
Cdd:smart00271   9 VPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEkFKEINEAYEVLSD 57
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
22-82 1.82e-10

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 56.65  E-value: 1.82e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 389616158  22 ASEKEVKKAYRQKALTCHPDKNPDNPQ-AAEVFHQLSQALAVLTDAAARAAYDKVRKAKKQA 82
Cdd:COG2214   17 ASLEEIRQAYRRLAKLLHPDRGGELKAlAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKG 78
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 75-158 9.97e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.50  E-value: 9.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  75 VRKAKKQAAERTQKLDEkrkkVKLDLEAREREAqardneEEEIRITRTLEQEIIRLREEGSRQLEEQQRlIREQIQLERQ 154
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNE----LIASLEELEREL------EQKAEEAEALLKEAEKLKEELEEKKEKLQE-EEDKLLEEAE 572


                 ....
gi 389616158 155 QRIQ 158
Cdd:PRK00409 573 KEAQ 576
 
Name Accession Description Interval E-value
RRM_DNAJC17 cd12429
RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD ...
 172-248 9.61e-35

RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD corresponds to the RRM of some eukaryotic DnaJ homolog subfamily C member 17 and similar proteins. 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. Members in this family contains an N-terminal DnaJ domain or J-domain, which mediates the interaction with Hsp70. They also contains a RNA recognition motif (RRM), also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), at the C-terminus, which may play an essential role in RNA binding.


Pssm-ID: 409863 [Multi-domain]  Cd Length: 74  Bit Score: 120.84  E-value: 9.61e-35
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158 172 PKLKLKWKCRKEdetGGGYSKEVLLRILQKYGDVLNLLISSRKAGSAVVEFATVKAAEMAVKNEVGLTDNPLKISWL 248
Cdd:cd12429    1 PRLKVKWKSKKG---NGGYSEEELRKIFSKYGPVSDVVISSKKKGSAIVEFATVVAADAAVENEVGLPDNPLLVSWL 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 18-73 2.53e-18

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: 77.51  E-value: 2.53e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 389616158   18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYD 73
Cdd:pfam00226   8 VSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 18-134 2.03e-15

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: 72.04  E-value: 2.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDKVRKAkKQAAERTQKLDEKRKKVK 97
Cdd:COG0484    8 VSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHA-AELLLATELAESAAAEAA 86

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 389616158  98 LDLEAREREAQARDNEEEEIRITRTLEQEIIRLREEG 134
Cdd:COG0484   87 AAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLAL 123
PRK14279 PRK14279
molecular chaperone DnaJ;
18-77 2.73e-15

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 75.54  E-value: 2.73e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDKVRK 77
Cdd:PRK14279  17 VSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDETRR 76
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 18-73 2.97e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 75.18  E-value: 2.97e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYD 73
Cdd:PRK10767  12 VSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 18-74 1.71e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 73.24  E-value: 1.71e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14301  12 VSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDR 68
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 18-65 2.22e-14

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: 66.41  E-value: 2.22e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTD 65
Cdd:cd06257    8 VPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 18-74 9.97e-13

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: 67.63  E-value: 9.97e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158   18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:TIGR02349   8 VSKDASEEEIKKAYRKLAKKYHPDRNKD-KEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 18-74 2.12e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 66.80  E-value: 2.12e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14298  13 LSKDASVEDIKKAYRKLAMKYHPDKNKE-PDAEEKFKEISEAYAVLSDAEKRAQYDR 68
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 18-74 2.15e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 66.71  E-value: 2.15e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14294  12 VTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQ 68
PRK14289 PRK14289
molecular chaperone DnaJ;
18-74 1.03e-11

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 64.85  E-value: 1.03e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14289  13 VSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQ 69
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 18-74 1.33e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 64.44  E-value: 1.33e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14281  11 VSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQ 67
PRK14295 PRK14295
molecular chaperone DnaJ;
18-76 2.11e-11

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 64.10  E-value: 2.11e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDKVR 76
Cdd:PRK14295  17 VPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDEAR 75
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 18-74 5.68e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 62.60  E-value: 5.68e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14292  10 VSRTASADEIKSAYRKLALKYHPDRNKE-KGAAEKFAQINEAYAVLSDAEKRAHYDR 65
PRK14297 PRK14297
molecular chaperone DnaJ;
22-74 6.84e-11

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 62.49  E-value: 6.84e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 389616158  22 ASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14297  16 ASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQ 68
DnaJ smart00271
DnaJ molecular chaperone homology domain;
18-65 7.00e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 56.86  E-value: 7.00e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 389616158    18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEV-FHQLSQALAVLTD 65
Cdd:smart00271   9 VPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEkFKEINEAYEVLSD 57
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 18-77 7.62e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 62.17  E-value: 7.62e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDKVRK 77
Cdd:PRK14284   9 VSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGK 68
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 22-74 1.73e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 61.16  E-value: 1.73e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 389616158  22 ASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14285  15 ASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDR 67
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
22-82 1.82e-10

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 56.65  E-value: 1.82e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 389616158  22 ASEKEVKKAYRQKALTCHPDKNPDNPQ-AAEVFHQLSQALAVLTDAAARAAYDKVRKAKKQA 82
Cdd:COG2214   17 ASLEEIRQAYRRLAKLLHPDRGGELKAlAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKG 78
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 18-74 1.98e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 60.99  E-value: 1.98e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNpDNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14283  13 VDRNADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDQ 68
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 18-71 3.41e-10

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 55.01  E-value: 3.41e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAA 71
Cdd:COG5407    8 VAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRAR 61
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 18-78 4.18e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 60.00  E-value: 4.18e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDKVRKA 78
Cdd:PRK14286  12 VSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKA 72
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 18-73 6.32e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 59.30  E-value: 6.32e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYD 73
Cdd:PRK14278  11 VSRNASDAEIKRAYRKLARELHPDVNPD-EEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 18-74 8.25e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 59.04  E-value: 8.25e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14277  13 VDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQ 69
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 18-74 4.28e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 57.02  E-value: 4.28e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14276  12 VSKDASQDEIKKAYRKLSKKYHPDINKE-PGAEEKYKEVQEAYETLSDPQKRAAYDQ 67
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 18-74 1.37e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 55.32  E-value: 1.37e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQ-AAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14290  11 VDRNASQEDIKKAFRELAKKWHPDLHPGNKAeAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 18-74 1.48e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 55.16  E-value: 1.48e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPdNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14291  11 VSRNATQEEIKKAYRRLARKYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYDQ 66
PRK14280 PRK14280
molecular chaperone DnaJ;
18-74 4.88e-08

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 53.57  E-value: 4.88e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14280  12 VSKSASKDEIKKAYRKLSKKYHPDINKE-EGADEKFKEISEAYEVLSDDQKRAQYDQ 67
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 18-74 3.43e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 50.71  E-value: 3.43e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14299  12 VPKNASQDEIKKAFKKLARKYHPDVNKS-PGAEEKFKEINEAYTVLSDPEKRRIYDT 67
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 18-74 4.97e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 50.56  E-value: 4.97e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDNPQAAEV-FHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14282  12 VSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQkFKEIQEAYEVLSDPQKRAMYDR 69
PRK14293 PRK14293
molecular chaperone DnaJ;
18-74 9.06e-07

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 49.99  E-value: 9.06e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14293  11 VSRDADKDELKRAYRRLARKYHPDVNKE-PGAEDRFKEINRAYEVLSDPETRARYDQ 66
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 18-74 1.40e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 49.17  E-value: 1.40e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14296  12 VSKTASEQEIRQAYRKLAKQYHPDLNKS-PDAHDKMVEINEAADVLLDKDKRKQYDQ 67
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 18-74 3.17e-06

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 48.28  E-value: 3.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnpqaAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PTZ00037  36 LSKDCTTSEIKKAYRKLAIKHHPDKGGD----PEKFKEISRAYEVLSDPEKRKIYDE 88
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 189-246 1.38e-05

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 42.27  E-value: 1.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 389616158 189 GYSKEVLLRILQKYGDVLNLLI----SSRKAGSAVVEFATVKAAEMAVK--NEVGLTDNPLKIS 246
Cdd:cd00590    9 DTTEEDLRELFSKFGEVVSVRIvrdrDGKSKGFAFVEFESPEDAEKALEalNGTELGGRPLKVS 72
PRK14288 PRK14288
molecular chaperone DnaJ;
20-87 1.41e-05

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 46.22  E-value: 1.41e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 389616158  20 EKASEKE-VKKAYRQKALTCHPDKNPDNPQAAEVFHQLSQALAVLTDAAARAAYDKVRKAKKQAAERTQ 87
Cdd:PRK14288  12 EKHSNQEtIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQ 80
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 18-74 4.04e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 44.61  E-value: 4.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14287  12 VDRNASVDEVKKAYRKLARKYHPDVNKA-PDAEDKFKEVKEAYDTLSDPQKKAHYDQ 67
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 18-74 6.24e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 44.23  E-value: 6.24e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 389616158  18 VGEKASEKEVKKAYRQKALTCHPDkNPDNPQAAEVFHQLSQALAVLTDAAARAAYDK 74
Cdd:PRK14300  11 VSKTASQADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYDR 66
PRK10266 PRK10266
curved DNA-binding protein;
25-76 2.92e-04

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 41.73  E-value: 2.92e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 389616158  25 KEVKKAYRQKALTCHPDKNPDnPQAAEVFHQLSQALAVLTDAAARAAYDKVR 76
Cdd:PRK10266  19 KTIKTAYRRLARKYHPDVSKE-PDAEARFKEVAEAWEVLSDEQRRAEYDQLW 69
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-158 1.41e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  48 QAAEVFHQLSQALAVLTDAAARAAYDKVRKAKKQAAERTQKLDEKRKKVKLDLEAREREAQARDNEEEEIRITRTLEQEI 127
Cdd:COG1196  210 EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE 289

                         90       100       110
                 ....*....|....*....|....*....|.
gi 389616158 128 IRLREEGSRQLEEQQRLIREQIQLERQQRIQ 158
Cdd:COG1196  290 EYELLAELARLEQDIARLEERRRELEERLEE 320
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-156 1.42e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  48 QAAEVFHQLSQALAVLTDAAARAAyDKVRKAKKQAAERTQKLDEKRKKVKLDLEAREREAQARDNEEEEIRITRTLEQEI 127
Cdd:COG1196  338 ELEELEEELEEAEEELEEAEAELA-EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL 416

                         90       100
                 ....*....|....*....|....*....
gi 389616158 128 IRLREEGSRQLEEQQRLIREQIQLERQQR 156
Cdd:COG1196  417 ERLEEELEELEEALAELEEEEEEEEEALE 445
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 63-158 3.10e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  63 LTDAAARAAYDKVRKAKKQAAERTQKLDEKRKKVKLDLEAREREAQARDNEEEEIRITRTLEQEIIRLREEGSRQLEEQQ 142
Cdd:COG1196  314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                         90
                 ....*....|....*.
gi 389616158 143 RLIREQIQLERQQRIQ 158
Cdd:COG1196  394 AAAELAAQLEELEEAE 409
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 75-158 9.97e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 37.50  E-value: 9.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389616158  75 VRKAKKQAAERTQKLDEkrkkVKLDLEAREREAqardneEEEIRITRTLEQEIIRLREEGSRQLEEQQRlIREQIQLERQ 154
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNE----LIASLEELEREL------EQKAEEAEALLKEAEKLKEELEEKKEKLQE-EEDKLLEEAE 572


                 ....
gi 389616158 155 QRIQ 158
Cdd:PRK00409 573 KEAQ 576
 
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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