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Conserved domains on  [gi|300795475|ref|NP_001178669|]
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dnaJ homolog subfamily C member 17 [Rattus norvegicus]

Protein Classification

J domain-containing protein( domain architecture ID 11087556)

J domain-containing protein containing a similar domain as DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70.

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 ...
 184-247 9.19e-26

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: 97.34  E-value: 9.19e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475 184 ESQGGYSRDILLRLLQKYGEVLNLVLSKKKAGNAIVEFATVRAAELAVRNEVGLADNPLKVSWL 247
Cdd:cd12429   11 KGNGGYSEEELRKIFSKYGPVSDVVISSKKKGSAIVEFATVVAADAAVENEVGLPDNPLLVSWL 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 11-73 5.39e-23

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


:

Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 89.84  E-value: 5.39e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475   11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYD 73
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-159 3.91e-03

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475  48 RAAELFHQLSQALEVLtDAAARAAYDKVRKARKQAAERT---------------QRLDEKRKKVKLDLEARERQAQAQGT 112
Cdd:COG1196  210 EKAERYRELKEELKEL-EAELLLLKLRELEAELEELEAEleeleaeleeleaelAELEAELEELRLELEELELELEEAQA 288

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 300795475 113 EEEEESRSTTTLEQEIARLREEGSRQLEEQQRLIQEQIRQDREQRLR 159
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
 
Name Accession Description Interval E-value
RRM_DNAJC17 cd12429
RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD ...
 184-247 9.19e-26

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: 97.34  E-value: 9.19e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475 184 ESQGGYSRDILLRLLQKYGEVLNLVLSKKKAGNAIVEFATVRAAELAVRNEVGLADNPLKVSWL 247
Cdd:cd12429   11 KGNGGYSEEELRKIFSKYGPVSDVVISSKKKGSAIVEFATVVAADAAVENEVGLPDNPLLVSWL 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 11-73 5.39e-23

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


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 89.84  E-value: 5.39e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475   11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYD 73
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 11-65 7.17e-19

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: 78.36  E-value: 7.17e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTD 65
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 11-73 1.13e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 85.20  E-value: 1.13e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYD 73
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 11-135 2.18e-17

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


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 77.05  E-value: 2.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDKVRKARkqAAERTQRLD 90
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAA--ELLLATELA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 300795475  91 EKRKKVKLDLEARERQAQAQGTEEEEESRSTTTLEQEIARLREEG 135
Cdd:COG0484   79 ESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLAL 123
DnaJ smart00271
DnaJ molecular chaperone homology domain;
10-65 6.81e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 70.73  E-value: 6.81e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795475    10 MDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPR-AAELFHQLSQALEVLTD 65
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEeAEEKFKEINEAYEVLSD 57
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 11-74 1.21e-15

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: 76.10  E-value: 1.21e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475   11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD-KEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 188-233 1.39e-03

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 36.44  E-value: 1.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 300795475  188 GYSRDILLRLLQKYGEVLNLVLSKKKAGN----AIVEFATVRAAELAVRN 233
Cdd:pfam00076   9 DTTEEDLKDLFSKFGPIKSIRLVRDETGRskgfAFVEFEDEEDAEKAIEA 58
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-159 3.91e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475  48 RAAELFHQLSQALEVLtDAAARAAYDKVRKARKQAAERT---------------QRLDEKRKKVKLDLEARERQAQAQGT 112
Cdd:COG1196  210 EKAERYRELKEELKEL-EAELLLLKLRELEAELEELEAEleeleaeleeleaelAELEAELEELRLELEELELELEEAQA 288

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 300795475 113 EEEEESRSTTTLEQEIARLREEGSRQLEEQQRLIQEQIRQDREQRLR 159
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 73-163 7.27e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 37.80  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475   73 DKVRKARKQAAERTQRLDEKRKKVKLDLEARERQAQAQGTEEEEESRSTTTLEQ-EIARLREEGSRQL-----EEQQRLI 146
Cdd:pfam17380 381 ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAREMervrlEEQERQQ 460

                          90
                  ....*....|....*...
gi 300795475  147 Q-EQIRQDREQRLRGRTE 163
Cdd:pfam17380 461 QvERLRQQEEERKRKKLE 478
 
Name Accession Description Interval E-value
RRM_DNAJC17 cd12429
RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD ...
 184-247 9.19e-26

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: 97.34  E-value: 9.19e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475 184 ESQGGYSRDILLRLLQKYGEVLNLVLSKKKAGNAIVEFATVRAAELAVRNEVGLADNPLKVSWL 247
Cdd:cd12429   11 KGNGGYSEEELRKIFSKYGPVSDVVISSKKKGSAIVEFATVVAADAAVENEVGLPDNPLLVSWL 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 11-73 5.39e-23

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


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 89.84  E-value: 5.39e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475   11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYD 73
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 11-65 7.17e-19

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: 78.36  E-value: 7.17e-19
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTD 65
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 11-73 1.13e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 85.20  E-value: 1.13e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYD 73
Cdd:PRK10767   5 DYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
PRK14279 PRK14279
molecular chaperone DnaJ;
5-77 1.47e-17

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 82.09  E-value: 1.47e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475   5 KELLQMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDKVRK 77
Cdd:PRK14279   4 REWVEKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDETRR 76
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 11-135 2.18e-17

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


Pssm-ID: 440252 [Multi-domain]  Cd Length: 139  Bit Score: 77.05  E-value: 2.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDKVRKARkqAAERTQRLD 90
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAA--ELLLATELA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 300795475  91 EKRKKVKLDLEARERQAQAQGTEEEEESRSTTTLEQEIARLREEG 135
Cdd:COG0484   79 ESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLAL 123
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 9-74 6.77e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 80.17  E-value: 6.77e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795475   9 QMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14301   3 QRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYDR 68
DnaJ smart00271
DnaJ molecular chaperone homology domain;
10-65 6.81e-16

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 70.73  E-value: 6.81e-16
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795475    10 MDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPR-AAELFHQLSQALEVLTD 65
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEeAEEKFKEINEAYEVLSD 57
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 11-74 1.21e-15

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: 76.10  E-value: 1.21e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475   11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD-KEAEEKFKEINEAYEVLSDPEKRAQYDQ 63
PRK14297 PRK14297
molecular chaperone DnaJ;
11-74 1.93e-15

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 75.98  E-value: 1.93e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYDQ 68
PRK14295 PRK14295
molecular chaperone DnaJ;
4-76 2.84e-15

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 75.27  E-value: 2.84e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475   4 TKELLQMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDKVR 76
Cdd:PRK14295   3 TKDYIEKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDEAR 75
PRK14289 PRK14289
molecular chaperone DnaJ;
11-74 2.86e-15

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 75.25  E-value: 2.86e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQ 69
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 11-74 2.89e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 75.19  E-value: 2.89e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14294   5 DYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYDQ 68
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 10-77 1.09e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 73.72  E-value: 1.09e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300795475  10 MDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDKVRK 77
Cdd:PRK14284   1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYDRYGK 68
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 1-74 1.21e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 73.34  E-value: 1.21e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475   1 MAVTKellqmDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14298   1 MATTR-----DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE-PDAEEKFKEISEAYAVLSDAEKRAQYDR 68
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 11-73 1.45e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 73.16  E-value: 1.45e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYD 73
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPD-EEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 11-74 3.56e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 72.14  E-value: 3.56e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYDQ 69
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 8-74 5.03e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 71.56  E-value: 5.03e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795475   8 LQMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14285   1 MKRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYDR 67
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 11-74 5.38e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 71.76  E-value: 5.38e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYDQ 67
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 11-71 2.40e-13

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 63.87  E-value: 2.40e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAA 71
Cdd:COG5407    1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRAR 61
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 13-78 3.54e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 69.25  E-value: 3.54e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795475  13 YALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDKVRKA 78
Cdd:PRK14286   7 YDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKA 72
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
11-82 4.30e-13

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 63.97  E-value: 4.30e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPR-AAELFHQLSQALEVLTDAAARAAYDKVRKARKQA 82
Cdd:COG2214    6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKAlAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKG 78
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 10-74 4.91e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 68.76  E-value: 4.91e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795475  10 MDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKE-KGAAEKFAQINEAYAVLSDAEKRAHYDR 65
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 9-74 2.01e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 67.04  E-value: 2.01e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795475   9 QMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14276   3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKE-PGAEEKYKEVQEAYETLSDPQKRAAYDQ 67
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 11-74 2.08e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 66.88  E-value: 2.08e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDN-PRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNkAEAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 11-74 7.93e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 65.23  E-value: 7.93e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNpDNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYDQ 68
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 11-74 4.22e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 62.89  E-value: 4.22e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAE-LFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEqKFKEIQEAYEVLSDPQKRAMYDR 69
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 9-74 1.03e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 61.71  E-value: 1.03e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795475   9 QMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPdNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14291   2 KKDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNK-NPEAEEKFKEINEAYQVLSDPEKRKLYDQ 66
PRK14280 PRK14280
molecular chaperone DnaJ;
11-74 1.07e-10

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 61.66  E-value: 1.07e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE-EGADEKFKEISEAYEVLSDDQKRAQYDQ 67
PRK14293 PRK14293
molecular chaperone DnaJ;
11-74 4.60e-10

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 59.62  E-value: 4.60e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14293   4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKE-PGAEDRFKEINRAYEVLSDPETRARYDQ 66
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 12-74 5.20e-09

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 56.75  E-value: 5.20e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300795475  12 LYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnpraAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PTZ00037  30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD----PEKFKEISRAYEVLSDPEKRKIYDE 88
PRK10266 PRK10266
curved DNA-binding protein;
11-79 7.03e-09

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 55.98  E-value: 7.03e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDKVRKAR 79
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKE-PDAEARFKEVAEAWEVLSDEQRRAEYDQLWQHR 72
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 11-74 1.18e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 55.34  E-value: 1.18e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKS-PDAHDKMVEINEAADVLLDKDKRKQYDQ 67
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 11-74 1.29e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 54.94  E-value: 1.29e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKS-PGAEEKFKEINEAYTVLSDPEKRRIYDT 67
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 11-74 6.92e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 53.09  E-value: 6.92e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDnPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKA-PDAEDKFKEVKEAYDTLSDPQKKAHYDQ 67
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 8-74 9.66e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 52.71  E-value: 9.66e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300795475   8 LQMDLYALLGIEEKAADKEVKKAYRQKALSCHPDkNPDNPRAAELFHQLSQALEVLTDAAARAAYDK 74
Cdd:PRK14300   1 MSQDYYQILGVSKTASQADLKKAYLKLAKQYHPD-TTDAKDAEKKFKEINAAYDVLKDEQKRAAYDR 66
PRK14288 PRK14288
molecular chaperone DnaJ;
8-87 6.67e-07

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 50.07  E-value: 6.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475   8 LQMDLYALLGIEEKAADKEVKKAYRQKALSCHPDKNPDNPRAAELFHQLSQALEVLTDAAARAAYDKVRKARKQAAERTQ 87
Cdd:PRK14288   1 MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGASQ 80
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 188-245 7.93e-07

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: 45.74  E-value: 7.93e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300795475 188 GYSRDILLRLLQKYGEVLNLVLSKKKAGN----AIVEFATVRAAELAVR--NEVGLADNPLKVS 245
Cdd:cd00590    9 DTTEEDLRELFSKFGEVVSVRIVRDRDGKskgfAFVEFESPEDAEKALEalNGTELGGRPLKVS 72
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
9-86 8.97e-06

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 42.86  E-value: 8.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475   9 QMDLYALLGIEEKAADKEVKKAYRQKALSCHPDK--NPDNPRAAELFHQLSQALevltdaaaRAAYDKVRKARKQAAERT 86
Cdd:COG1076    3 LDDAFELLGLPPDADDAELKRAYRKLQREHHPDRlaAGLPEEEQRLALQKAAAI--------NEAYETLKDPRGIDLAAP 74
djlA PRK09430
co-chaperone DjlA;
11-80 1.37e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 42.49  E-value: 1.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795475  11 DLYALLGIEEKAADKEVKKAYRqKALS-CHPDK-----NPdnPRAAELFHQLSQALevltdaaaRAAYDKVRKARK 80
Cdd:PRK09430 201 DAYKVLGVSESDDDQEIKRAYR-KLMSeHHPDKlvakgLP--PEMMEMAKEKAQEI--------QAAYELIKKQKG 265
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 5-75 1.44e-04

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 43.10  E-value: 1.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300795475   5 KELLQMDLYALLGIEE---KAADKEVKKAYRQKALSCHPDKNP--DNPRAAELFHQLSQALEVLTDAAARAAYDKV 75
Cdd:COG5269   38 KNWKKVDLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAagGNKGCDEFFKLIQKAREVLGDRKLRLQYDSN 113
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 188-233 1.39e-03

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 36.44  E-value: 1.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 300795475  188 GYSRDILLRLLQKYGEVLNLVLSKKKAGN----AIVEFATVRAAELAVRN 233
Cdd:pfam00076   9 DTTEEDLKDLFSKFGPIKSIRLVRDETGRskgfAFVEFEDEEDAEKAIEA 58
RRM2_MEI2_EAR1_like cd12276
RNA recognition motif 2 (RRM2) found in Mei2-like proteins and terminal EAR1-like proteins; ...
 190-244 2.95e-03

RNA recognition motif 2 (RRM2) found in Mei2-like proteins and terminal EAR1-like proteins; This subfamily corresponds to the RRM2 of Mei2-like proteins from plant and fungi, terminal EAR1-like proteins from plant, and other eukaryotic homologs. Mei2-like proteins represent an ancient eukaryotic RNA-binding proteins family whose corresponding Mei2-like genes appear to have arisen early in eukaryote evolution, been lost from some lineages such as Saccharomyces cerevisiae and metazoans, and diversified in the plant lineage. The plant Mei2-like genes may function in cell fate specification during development, rather than as stimulators of meiosis. In the fission yeast Schizosaccharomyces pombe, the Mei2 protein is an essential component of the switch from mitotic to meiotic growth. S. pombe Mei2 stimulates meiosis in the nucleus upon binding a specific non-coding RNA. The terminal EAR1-like protein 1 and 2 (TEL1 and TEL2) are mainly found in land plants. They may play a role in the regulation of leaf initiation. All members in this family are putative RNA-binding proteins carrying three RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). In addition to the RRMs, the terminal EAR1-like proteins also contain TEL characteristic motifs that allow sequence and putative functional discrimination between them and Mei2-like proteins.


Pssm-ID: 409718 [Multi-domain]  Cd Length: 71  Bit Score: 35.69  E-value: 2.95e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 300795475 190 SRDILLRLLQKYGEVLNLVLSKKKAGNAIVEFATVRAAELAVR--NEVGLADNPLKV 244
Cdd:cd12276   14 SNDELKSLFSKFGEIKEIRPTPDKPSQKFVEFYDVRDAEAALDglNGRELLGGKLKV 70
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-159 3.91e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 3.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475  48 RAAELFHQLSQALEVLtDAAARAAYDKVRKARKQAAERT---------------QRLDEKRKKVKLDLEARERQAQAQGT 112
Cdd:COG1196  210 EKAERYRELKEELKEL-EAELLLLKLRELEAELEELEAEleeleaeleeleaelAELEAELEELRLELEELELELEEAQA 288

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 300795475 113 EEEEESRSTTTLEQEIARLREEGSRQLEEQQRLIQEQIRQDREQRLR 159
Cdd:COG1196  289 EEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL 335
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 73-163 7.27e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 37.80  E-value: 7.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475   73 DKVRKARKQAAERTQRLDEKRKKVKLDLEARERQAQAQGTEEEEESRSTTTLEQ-EIARLREEGSRQL-----EEQQRLI 146
Cdd:pfam17380 381 ERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQrEVRRLEEERAREMervrlEEQERQQ 460

                          90
                  ....*....|....*...
gi 300795475  147 Q-EQIRQDREQRLRGRTE 163
Cdd:pfam17380 461 QvERLRQQEEERKRKKLE 478
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 48-166 8.61e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.61  E-value: 8.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300795475  48 RAAELFHQLSQALEVLTDAAARAAydKVRKARKQAAERTQRLDEKRKKVKLDLEARERQAQAQGTEEEEESRSTTTLEQE 127
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELE--EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA 408

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 300795475 128 IARLREEGSRQLEEQQRLIQEQIRQDREQRLRGRTENTE 166
Cdd:COG1196  409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
 
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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