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Conserved domains on  [gi|30689058|ref|NP_197749|]
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DNAJ heat shock N-terminal domain-containing protein [Arabidopsis thaliana]

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 ...
 173-245 4.55e-24

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: 92.72  E-value: 4.55e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30689058 173 RMLKVSW--EKSGEGYTAGRLREVFSEFGEVEDVVIRStKKKCSALIVMATKDGAVAATRTLCGNLSNPLLVVPL 245
Cdd:cd12429   1 PRLKVKWksKKGNGGYSEEELRKIFSKYGPVSDVVISS-KKKGSAIVEFATVVAADAAVENEVGLPDNPLLVSWL 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 6-73 3.78e-17

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: 74.05  E-value: 3.78e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058     6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:pfam00226   1 DYYEILGVSPDA-----SDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
 
Name Accession Description Interval E-value
RRM_DNAJC17 cd12429
RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD ...
 173-245 4.55e-24

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: 92.72  E-value: 4.55e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30689058 173 RMLKVSW--EKSGEGYTAGRLREVFSEFGEVEDVVIRStKKKCSALIVMATKDGAVAATRTLCGNLSNPLLVVPL 245
Cdd:cd12429   1 PRLKVKWksKKGNGGYSEEELRKIFSKYGPVSDVVISS-KKKGSAIVEFATVVAADAAVENEVGLPDNPLLVSWL 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 6-73 3.78e-17

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: 74.05  E-value: 3.78e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058     6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:pfam00226   1 DYYEILGVSPDA-----SDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 6-140 7.29e-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: 70.12  E-value: 7.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689058   6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFDDLLRIQREkqHK 85
Cdd:COG0484   1 DYYEILGVSRDA-----SAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL--LL 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30689058  86 KSQVDSKRRKMMSDLEERERSAFSPNPSARAYDEEERIARKLKEEIDRIRARHAK 140
Cdd:COG0484  74 ATELAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELAL 128
PRK14279 PRK14279
molecular chaperone DnaJ;
6-78 4.03e-13

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 68.99  E-value: 4.03e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30689058    6 DHYIVLGLASgeealKLTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFDDLLRI 78
Cdd:PRK14279  10 DFYKELGVSS-----DASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDETRRL 77
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 6-65 6.72e-13

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: 62.18  E-value: 6.72e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689058   6 DHYIVLGLASGeealkLTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKD 65
Cdd:cd06257   1 DYYDILGVPPD-----ASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 6-73 5.32e-12

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: 65.31  E-value: 5.32e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058     6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDdPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:TIGR02349   1 DYYEILGVSKDA-----SEEEIKKAYRKLAKKYHPDRNKD-KEAEEKFKEINEAYEVLSDPEKRAQYD 62
DnaJ smart00271
DnaJ molecular chaperone homology domain;
5-67 1.72e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 58.40  E-value: 1.72e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30689058      5 VDHYIVLGLASGeealkLTEKEIAKAYKLKALDLHPDKRPDDP-DAHEKFQRLKTSYEVLKDEK 67
Cdd:smart00271   1 TDYYEILGVPRD-----ASLDEIKKAYRKLALKYHPDKNPGDKeEAEEKFKEINEAYEVLSDPE 59
RRM smart00360
RNA recognition motif;
191-228 4.31e-04

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 37.96  E-value: 4.31e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 30689058    191 LREVFSEFGEVEDVVIRSTKK----KCSALIVMATKDGAVAA 228
Cdd:smart00360  16 LRELFSKFGKVESVRLVRDKEtgksKGFAFVEFESEEDAEKA 57
RRM COG0724
RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];
191-232 5.77e-04

RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440488 [Multi-domain]  Cd Length: 85  Bit Score: 38.16  E-value: 5.77e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30689058 191 LREVFSEFGEVEDVVI---RSTKK-KCSALIVMATKDGAVAATRTL 232
Cdd:COG0724  18 LRELFSEYGEVTSVKLitdRETGRsRGFGFVEMPDDEEAQAAIEAL 63
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 191-232 8.42e-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: 34.52  E-value: 8.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 30689058   191 LREVFSEFGEVE--DVVIRSTKK-KCSALIVMATKDGAVAATRTL 232
Cdd:pfam00076  15 LKDLFSKFGPIKsiRLVRDETGRsKGFAFVEFEDEEDAEKAIEAL 59
 
Name Accession Description Interval E-value
RRM_DNAJC17 cd12429
RNA recognition motif (RRM) found in the DnaJ homolog subfamily C member 17; The CD ...
 173-245 4.55e-24

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: 92.72  E-value: 4.55e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30689058 173 RMLKVSW--EKSGEGYTAGRLREVFSEFGEVEDVVIRStKKKCSALIVMATKDGAVAATRTLCGNLSNPLLVVPL 245
Cdd:cd12429   1 PRLKVKWksKKGNGGYSEEELRKIFSKYGPVSDVVISS-KKKGSAIVEFATVVAADAAVENEVGLPDNPLLVSWL 74
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 6-73 3.78e-17

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: 74.05  E-value: 3.78e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058     6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:pfam00226   1 DYYEILGVSPDA-----SDEEIKKAYRKLALKYHPDKNPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 6-140 7.29e-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: 70.12  E-value: 7.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689058   6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFDDLLRIQREkqHK 85
Cdd:COG0484   1 DYYEILGVSRDA-----SAEEIKKAYRKLAKKYHPDRNPGDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL--LL 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30689058  86 KSQVDSKRRKMMSDLEERERSAFSPNPSARAYDEEERIARKLKEEIDRIRARHAK 140
Cdd:COG0484  74 ATELAESAAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLLALLELAL 128
PRK14279 PRK14279
molecular chaperone DnaJ;
6-78 4.03e-13

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 68.99  E-value: 4.03e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30689058    6 DHYIVLGLASgeealKLTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFDDLLRI 78
Cdd:PRK14279  10 DFYKELGVSS-----DASAEEIKKAYRKLARELHPDANPGDPAAEERFKAVSEAHDVLSDPAKRKEYDETRRL 77
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 6-73 5.86e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 68.25  E-value: 5.86e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK10767   5 DYYEVLGVSRNA-----SEDEIKKAYRKLAMKYHPDRNPGDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 6-65 6.72e-13

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: 62.18  E-value: 6.72e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689058   6 DHYIVLGLASGeealkLTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKD 65
Cdd:cd06257   1 DYYDILGVPPD-----ASDEEIKKAYRKLALKYHPDKNPDDPEAEEKFKEINEAYEVLSD 55
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 6-73 5.32e-12

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: 65.31  E-value: 5.32e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058     6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDdPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:TIGR02349   1 DYYEILGVSKDA-----SEEEIKKAYRKLAKKYHPDRNKD-KEAEEKFKEINEAYEVLSDPEKRAQYD 62
DnaJ smart00271
DnaJ molecular chaperone homology domain;
5-67 1.72e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 58.40  E-value: 1.72e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30689058      5 VDHYIVLGLASGeealkLTEKEIAKAYKLKALDLHPDKRPDDP-DAHEKFQRLKTSYEVLKDEK 67
Cdd:smart00271   1 TDYYEILGVPRD-----ASLDEIKKAYRKLALKYHPDKNPGDKeEAEEKFKEINEAYEVLSDPE 59
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 6-73 2.34e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 63.61  E-value: 2.34e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLAsgEEAlklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14301   5 DYYEVLGVS--RDA---SEDEIKKAYRKLALQYHPDRNPDNPEAEQKFKEAAEAYEVLRDAEKRARYD 67
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
1-73 4.02e-11

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 58.58  E-value: 4.02e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30689058   1 MEGFVDHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPD-AHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:COG2214   1 MPDLKDHYAVLGVPPDA-----SLEEIRQAYRRLAKLLHPDRGGELKAlAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 6-73 4.18e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 62.94  E-value: 4.18e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14284   2 DYYTILGVSKTA-----SPEEIKKAYRKLAVKYHPDKNPGDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 6-73 6.52e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 62.52  E-value: 6.52e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14281   4 DYYEVLGVSRSA-----DKDEIKKAYRKLALKYHPDKNPDNKEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14295 PRK14295
molecular chaperone DnaJ;
6-74 1.28e-10

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 61.40  E-value: 1.28e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30689058    6 DHYIVLGLASgeealKLTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFDD 74
Cdd:PRK14295  10 DYYKVLGVPK-----DATEAEIKKAYRKLAREYHPDANKGDAKAEERFKEISEAYDVLSDEKKRKEYDE 73
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 6-70 1.72e-10

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 55.78  E-value: 1.72e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30689058   6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARK 70
Cdd:COG5407   1 DPYEVLGVAKTA-----SADEIKKAYRKLAKKYHPDRNKGDPKAEERFKEINEAYELLSDAEKRA 60
PRK14289 PRK14289
molecular chaperone DnaJ;
6-75 1.78e-10

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 61.00  E-value: 1.78e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689058    6 DHYIVLGLASgeealKLTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFDDL 75
Cdd:PRK14289   6 DYYEVLGVSK-----TATVDEIKKAYRKKAIQYHPDKNPGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQF 70
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 6-73 5.02e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 59.68  E-value: 5.02e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDdPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14278   4 DYYGLLGVSRNA-----SDAEIKRAYRKLARELHPDVNPD-EEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 6-73 2.50e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 57.47  E-value: 2.50e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASgeealKLTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14294   5 DYYEILGVTR-----DASEEEIKKSYRKLAMKYHPDRNPGDKEAEELFKEAAEAYEVLSDPKKRGIYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 1-73 3.05e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 57.12  E-value: 3.05e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30689058    1 MEGFVDHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14277   1 MAAKKDYYEILGVDRNA-----TEEEIKKAYRRLAKKYHPDLNPGDKEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14297 PRK14297
molecular chaperone DnaJ;
6-73 3.93e-09

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 56.72  E-value: 3.93e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14297   5 DYYEVLGLEKGA-----SDDEIKKAFRKLAIKYHPDKNKGNKEAEEKFKEINEAYQVLSDPQKKAQYD 67
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 6-73 5.23e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 56.37  E-value: 5.23e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEEalkltEKEIAKAYKLKALDLHPDKRpDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14283   6 DYYEVLGVDRNAD-----KKEIKKAYRKLARKYHPDVS-EEEGAEEKFKEISEAYAVLSDDEKRQRYD 67
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 6-73 8.02e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 56.01  E-value: 8.02e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEEAlklteKEIAKAYKLKALDLHPDKRpDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14298   6 DYYEILGLSKDASV-----EDIKKAYRKLAMKYHPDKN-KEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 6-73 1.30e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 55.16  E-value: 1.30e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDdPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14291   4 DYYEILGVSRNA-----TQEEIKKAYRRLARKYHPDFNKN-PEAEEKFKEINEAYQVLSDPEKRKLYD 65
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 7-73 1.60e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 55.00  E-value: 1.60e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30689058    7 HYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14286   6 YYDILGVSKSA-----NDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14280 PRK14280
molecular chaperone DnaJ;
6-73 2.10e-07

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 51.65  E-value: 2.10e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRpDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14280   5 DYYEVLGVSKSA-----SKDEIKKAYRKLSKKYHPDIN-KEEGADEKFKEISEAYEVLSDDQKRAQYD 66
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 6-74 2.15e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 51.47  E-value: 2.15e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDD-PDAHEKFQRLKTSYEVLKDEKARKLFDD 74
Cdd:PRK14290   4 DYYKILGVDRNA-----SQEDIKKAFRELAKKWHPDLHPGNkAEAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 6-73 4.66e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 50.38  E-value: 4.66e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14285   4 DYYEILGLSKGA-----SKDEIKKAYRKIAIKYHPDKNKGNKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 6-73 5.44e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 49.94  E-value: 5.44e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRpDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14299   5 DYYAILGVPKNA-----SQDEIKKAFKKLARKYHPDVN-KSPGAEEKFKEINEAYTVLSDPEKRRIYD 66
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 23-74 8.54e-07

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 49.82  E-value: 8.54e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 30689058   23 TEKEIAKAYKLKALDLHPDKRPDDpdahEKFQRLKTSYEVLKDEKARKLFDD 74
Cdd:PTZ00037  41 TTSEIKKAYRKLAIKHHPDKGGDP----EKFKEISRAYEVLSDPEKRKIYDE 88
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 6-73 1.57e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 49.02  E-value: 1.57e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRPDD-PDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14282   5 DYYEILGVSRNA-----TQEEIKRAYKRLVKEWHPDRHPENrKEAEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK10266 PRK10266
curved DNA-binding protein;
1-129 1.63e-06

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 48.66  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30689058    1 MEgFVDHYIVLGLASGEEAlklteKEIAKAYKLKALDLHPDKRpDDPDAHEKFQRLKTSYEVLKDEKARKLFDDLL---- 76
Cdd:PRK10266   1 ME-LKDYYAIMGVKPTDDL-----KTIKTAYRRLARKYHPDVS-KEPDAEARFKEVAEAWEVLSDEQRRAEYDQLWqhrn 73

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 30689058   77 --RIQREKQHKKSQVDSKR--RKMMSDLEERERSAFSPNPSARAYDEEERIARKLKE 129
Cdd:PRK10266  74 dpQFNRQFQHGDGQSFNAEdfDDIFSSIFGQHARQSRQRPAARGHDIEIEVAVFLEE 130
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 5-73 2.05e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 48.73  E-value: 2.05e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30689058    5 VDHYIVLGLASGEEAlklteKEIAKAYKLKALDLHPDKRPdDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14292   2 MDYYELLGVSRTASA-----DEIKSAYRKLALKYHPDRNK-EKGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 6-73 4.08e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 47.78  E-value: 4.08e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLAsgEEAlklTEKEIAKAYKLKALDLHPDKRpDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14276   5 EYYDRLGVS--KDA---SQDEIKKAYRKLSKKYHPDIN-KEPGAEEKYKEVQEAYETLSDPQKRAAYD 66
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 6-73 7.91e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 46.93  E-value: 7.91e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASgeealKLTEKEIAKAYKLKALDLHPDKrPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14300   4 DYYQILGVSK-----TASQADLKKAYLKLAKQYHPDT-TDAKDAEKKFKEINAAYDVLKDEQKRAAYD 65
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 6-73 2.55e-05

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 45.32  E-value: 2.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEealklTEKEIAKAYKLKALDLHPDKRpDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14296   5 DYYEVLGVSKTA-----SEQEIRQAYRKLAKQYHPDLN-KSPDAHDKMVEINEAADVLLDKDKRKQYD 66
PRK14288 PRK14288
molecular chaperone DnaJ;
24-73 4.80e-05

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 44.29  E-value: 4.80e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 30689058   24 EKEIAKAYKLKALDLHPDKRPDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14288  17 QETIKKSYRKLALKYHPDRNAGDKEAEEKFKLINEAYGVLSDEKKRALYD 66
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
 191-228 7.90e-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: 40.34  E-value: 7.90e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 30689058 191 LREVFSEFGEVEDVVI---RSTKKKCSALIVMATKDGAVAA 228
Cdd:cd00590  15 LRELFSKFGEVVSVRIvrdRDGKSKGFAFVEFESPEDAEKA 55
RRM1_U1A_like cd12246
RNA recognition motif 1 (RRM1) found in the U1A/U2B"/SNF protein family; This subfamily ...
 191-234 2.71e-04

RNA recognition motif 1 (RRM1) found in the U1A/U2B"/SNF protein family; This subfamily corresponds to the RRM1 of U1A/U2B"/SNF protein family which contains Drosophila sex determination protein SNF and its two mammalian counterparts, U1 small nuclear ribonucleoprotein A (U1 snRNP A or U1-A or U1A) and U2 small nuclear ribonucleoprotein B" (U2 snRNP B" or U2B"), all of which consist of two RNA recognition motifs (RRMs), connected by a variable, flexible linker. SNF is an RNA-binding protein found in the U1 and U2 snRNPs of Drosophila where it is essential in sex determination and possesses a novel dual RNA binding specificity. SNF binds with high affinity to both Drosophila U1 snRNA stem-loop II (SLII) and U2 snRNA stem-loop IV (SLIV). It can also bind to poly(U) RNA tracts flanking the alternatively spliced Sex-lethal (Sxl) exon, as does Drosophila Sex-lethal protein (SXL). U1A is an RNA-binding protein associated with the U1 snRNP, a small RNA-protein complex involved in pre-mRNA splicing. U1A binds with high affinity and specificity to stem-loop II (SLII) of U1 snRNA. It is predominantly a nuclear protein that shuttles between the nucleus and the cytoplasm independently of interactions with U1 snRNA. Moreover, U1A may be involved in RNA 3'-end processing, specifically cleavage, splicing and polyadenylation, through interacting with a large number of non-snRNP proteins. U2B", initially identified to bind to stem-loop IV (SLIV) at the 3' end of U2 snRNA, is a unique protein that comprises of the U2 snRNP. Additional research indicates U2B" binds to U1 snRNA stem-loop II (SLII) as well and shows no preference for SLIV or SLII on the basis of binding affinity. Moreover, U2B" does not require an auxiliary protein for binding to RNA, and its nuclear transport is independent of U2 snRNA binding.


Pssm-ID: 409692 [Multi-domain]  Cd Length: 78  Bit Score: 38.67  E-value: 2.71e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 30689058 191 LREVFSEFGEVEDVVIRSTKK-KCSALIVMATKDGAVAATRTLCG 234
Cdd:cd12246  20 LYALFSQFGPVLDIVASKSLKmRGQAFVVFKDVESATNALRALQG 64
RRM smart00360
RNA recognition motif;
191-228 4.31e-04

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 37.96  E-value: 4.31e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 30689058    191 LREVFSEFGEVEDVVIRSTKK----KCSALIVMATKDGAVAA 228
Cdd:smart00360  16 LRELFSKFGKVESVRLVRDKEtgksKGFAFVEFESEEDAEKA 57
RRM2_NsCP33_like cd21608
RNA recognition motif 2 (RRM2) found in Nicotiana sylvestris chloroplastic 33 kDa ...
 187-234 4.38e-04

RNA recognition motif 2 (RRM2) found in Nicotiana sylvestris chloroplastic 33 kDa ribonucleoprotein (NsCP33) and similar proteins; The family includes NsCP33, Arabidopsis thaliana chloroplastic 31 kDa ribonucleoprotein (CP31A) and mitochondrial glycine-rich RNA-binding protein 2 (AtGR-RBP2). NsCP33 may be involved in splicing and/or processing of chloroplast RNA's. AtCP31A, also called RNA-binding protein 1/2/3 (AtRBP33), or RNA-binding protein CP31A, or RNA-binding protein RNP-T, or RNA-binding protein cp31, is required for specific RNA editing events in chloroplasts and stabilizes specific chloroplast mRNAs, as well as for normal chloroplast development under cold stress conditions by stabilizing transcripts of numerous mRNAs under these conditions. CP31A may modulate telomere replication through RNA binding domains. AtGR-RBP2, also called AtRBG2, or glycine-rich protein 2 (AtGRP2), or mitochondrial RNA-binding protein 1a (At-mRBP1a), plays a role in RNA transcription or processing during stress. It binds RNAs and DNAs sequence with a preference to single-stranded nucleic acids. AtGR-RBP2 displays strong affinity to poly(U) sequence. It exerts cold and freezing tolerance, probably by exhibiting an RNA chaperone activity during the cold and freezing adaptation process. Some members in this family contain two RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). The model corresponds to the second RRM motif.


Pssm-ID: 410187 [Multi-domain]  Cd Length: 76  Bit Score: 38.30  E-value: 4.38e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 30689058 187 TAGRLREVFSEFGEVEDVVI---RST-KKKCSALIVMATKDGAVAATRTLCG 234
Cdd:cd21608  12 TEDDLRDLFSEFGEVESAKVitdRETgRSRGFGFVTFSTAEAAEAAIDALNG 63
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 6-73 4.69e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 41.15  E-value: 4.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEEAlklteKEIAKAYKLKALDLHPDKRpDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14287   5 DYYEVLGVDRNASV-----DEVKKAYRKLARKYHPDVN-KAPDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PRK14293 PRK14293
molecular chaperone DnaJ;
6-73 4.81e-04

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 41.13  E-value: 4.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30689058    6 DHYIVLGLASGEEAlklteKEIAKAYKLKALDLHPDKRpDDPDAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:PRK14293   4 DYYEILGVSRDADK-----DELKRAYRRLARKYHPDVN-KEPGAEDRFKEINRAYEVLSDPETRARYD 65
RRM COG0724
RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];
191-232 5.77e-04

RNA recognition motif (RRM) domain [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440488 [Multi-domain]  Cd Length: 85  Bit Score: 38.16  E-value: 5.77e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 30689058 191 LREVFSEFGEVEDVVI---RSTKK-KCSALIVMATKDGAVAATRTL 232
Cdd:COG0724  18 LRELFSEYGEVTSVKLitdRETGRsRGFGFVEMPDDEEAQAAIEAL 63
RRM1_Prp24 cd12296
RNA recognition motif 1 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar ...
 184-231 1.00e-03

RNA recognition motif 1 in fungal pre-messenger RNA splicing protein 24 (Prp24) and similar proteins; This subfamily corresponds to the RRM1 of Prp24, also termed U4/U6 snRNA-associated-splicing factor PRP24 (U4/U6 snRNP), an RNA-binding protein with four well conserved RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains). It facilitates U6 RNA base-pairing with U4 RNA during spliceosome assembly. Prp24 specifically binds free U6 RNA primarily with RRMs 1 and 2 and facilitates pairing of U6 RNA bases with U4 RNA bases. Additionally, it may also be involved in dissociation of the U4/U6 complex during spliceosome activation.


Pssm-ID: 409737 [Multi-domain]  Cd Length: 71  Bit Score: 36.86  E-value: 1.00e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 30689058 184 EGYTAGRLREVFSEFGEVEDVVIRSTKKKCSALIVMATKDGAVAA-TRT 231
Cdd:cd12296  10 KSITENKIRQFFKDCGEIREVKILESGNGLVAVIEFETEDEALAAlTKD 58
PHA03102 PHA03102
Small T antigen; Reviewed
 27-69 1.08e-03

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 38.88  E-value: 1.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 30689058   27 IAKAYKLKALDLHPDKRPDdpdaHEKFQRLKTSYEVLKDEKAR 69
Cdd:PHA03102  24 MRKAYLRKCLEFHPDKGGD----EEKMKELNTLYKKFRESVKS 62
PHA02624 PHA02624
large T antigen; Provisional
 27-74 1.58e-03

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 39.97  E-value: 1.58e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 30689058   27 IAKAYKLKALDLHPDKRPDdpdaHEKFQRLKTSYEVLKDE--KARKLFDD 74
Cdd:PHA02624  30 MRKAYLRKCKEYHPDKGGD----EEKMKRLNSLYKKLQEGvkSARQSFGT 75
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 3-73 2.68e-03

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 38.86  E-value: 2.68e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30689058   3 GFVDHYIVLGLAsgEEALKLTEKEIAKAYKLKALDLHPDKRPDDP--DAHEKFQRLKTSYEVLKDEKARKLFD 73
Cdd:COG5269  41 KKVDLYALLGLS--KYRTKAIPPQILKAHKKKVYKYHPDKTAAGGnkGCDEFFKLIQKAREVLGDRKLRLQYD 111
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
6-71 5.12e-03

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 35.16  E-value: 5.12e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30689058   6 DHYIVLGLASGeealkLTEKEIAKAYKLKALDLHPDK----RPDD--PDAHEKFQRLKTSYEVLKDEKARKL 71
Cdd:COG1076   5 DAFELLGLPPD-----ADDAELKRAYRKLQREHHPDRlaagLPEEeqRLALQKAAAINEAYETLKDPRGIDL 71
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
 191-232 8.42e-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: 34.52  E-value: 8.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 30689058   191 LREVFSEFGEVE--DVVIRSTKK-KCSALIVMATKDGAVAATRTL 232
Cdd:pfam00076  15 LKDLFSKFGPIKsiRLVRDETGRsKGFAFVEFEDEEDAEKAIEAL 59
RRM_TRA2 cd12363
RNA recognition motif (RRM) found in transformer-2 protein homolog TRA2-alpha, TRA2-beta and ...
 186-234 9.82e-03

RNA recognition motif (RRM) found in transformer-2 protein homolog TRA2-alpha, TRA2-beta and similar proteins; This subfamily corresponds to the RRM of two mammalian homologs of Drosophila transformer-2 (Tra2), TRA2-alpha, TRA2-beta (also termed SFRS10), and similar proteins found in eukaryotes. TRA2-alpha is a 40-kDa serine/arginine-rich (SR) protein that specifically binds to gonadotropin-releasing hormone (GnRH) exonic splicing enhancer on exon 4 (ESE4) and is necessary for enhanced GnRH pre-mRNA splicing. It strongly stimulates GnRH intron A excision in a dose-dependent manner. In addition, TRA2-alpha can interact with either 9G8 or SRp30c, which may also be crucial for ESE-dependent GnRH pre-mRNA splicing. TRA2-beta is a serine/arginine-rich (SR) protein that controls the pre-mRNA alternative splicing of the calcitonin/calcitonin gene-related peptide (CGRP), the survival motor neuron 1 (SMN1) protein and the tau protein. Both, TRA2-alpha and TRA2-beta, contains a well conserved RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), flanked by the N- and C-terminal arginine/serine (RS)-rich regions.


Pssm-ID: 409798 [Multi-domain]  Cd Length: 80  Bit Score: 34.51  E-value: 9.82e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 30689058 186 YTAGR-LREVFSEFGEVEDVVI----RSTKKKCSALIVMATKDGAVAATRTLCG 234
Cdd:cd12363  12 YTTERdLREVFSRYGPIEKVQVvydqQTGRSRGFGFVYFESVEDAKEAKERLNG 65
 
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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