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Conserved domains on  [gi|6324103|ref|NP_014172|]
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Jjj1p [Saccharomyces cerevisiae S288C]

Protein Classification

DnaJ and zf-C2H2_jaz domain-containing protein( domain architecture ID 13425065)

protein containing domains DnaJ, ZUO1, and zf-C2H2_jaz

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10767 super family cl35946
chaperone protein DnaJ; Provisional
 1-67 1.89e-28

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK10767:

Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 116.78  E-value: 1.89e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK10767   2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYD 67
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 6-275 1.44e-08

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


The actual alignment was detected with superfamily member COG5269:

Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 56.96  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103    6 YELLGVE---THASDLELKKAYRKKALQYHPDKNPDNVEEATQK-FAVIRAAYEVLSDPQERAWYDSHKEqilNDTPPST 81
Cdd:COG5269  46 YALLGLSkyrTKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEfFKLIQKAREVLGDRKLRLQYDSNDF---DADVPPP 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103   82 DDYYDYEvdatvtgvttdelllffnsalytkidnsaagIYQIAGKIFaklakdeilsgKRLGKFSEYQDdvfeqdinsig 161
Cdd:COG5269 123 RIYTPDE-------------------------------FFEVWEPVF-----------EREARFSKKQP----------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103  162 ylkacdnfinktdkllYPLFGYSPTDYEYLKHFYKTWSAFNTLKSFSWKDEYMYSKNYDRRTKREVNRRNEKARQQARNE 241
Cdd:COG5269 150 ----------------VPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQ 213

                       250       260       270
                ....*....|....*....|....*....|....
gi 6324103  242 YNKTVKRFVVFIKKLDKRMKegaKIAEEQRKLKE 275
Cdd:COG5269 214 DNARLKRLVQIAKKRDPRIK---SFKEQEKEMKK 244
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 338-363 5.54e-08

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


:

Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 48.71  E-value: 5.54e-08
                          10        20
                  ....*....|....*....|....*.
gi 6324103    338 YECFICNKTFKSEKQLKNHINTKLHK 363
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 1-67 1.89e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 116.78  E-value: 1.89e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK10767   2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 4-67 6.43e-26

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: 100.63  E-value: 6.43e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324103      4 CYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 5-83 1.85e-24

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: 99.39  E-value: 1.85e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324103    5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYDSHKEQILNDTPPSTDD 83
Cdd:COG0484   2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAE 79
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 5-67 1.55e-23

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: 102.29  E-value: 1.55e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103      5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:TIGR02349   2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYD 62
DnaJ smart00271
DnaJ molecular chaperone homology domain;
3-61 1.30e-21

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 88.45  E-value: 1.30e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 6324103       3 TCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNVEEATQKFAVIRAAYEVLSDPQ 61
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPE 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 4-59 2.83e-20

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: 84.52  E-value: 2.83e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6324103    4 CYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSD 59
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
5-69 7.16e-16

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 80.25  E-value: 7.16e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYDSH 69
Cdd:NF037946   7 YYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKA--PDAAEIFAEINEAYEVLSNPEKRANYDKY 69
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 6-275 1.44e-08

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 56.96  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103    6 YELLGVE---THASDLELKKAYRKKALQYHPDKNPDNVEEATQK-FAVIRAAYEVLSDPQERAWYDSHKEqilNDTPPST 81
Cdd:COG5269  46 YALLGLSkyrTKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEfFKLIQKAREVLGDRKLRLQYDSNDF---DADVPPP 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103   82 DDYYDYEvdatvtgvttdelllffnsalytkidnsaagIYQIAGKIFaklakdeilsgKRLGKFSEYQDdvfeqdinsig 161
Cdd:COG5269 123 RIYTPDE-------------------------------FFEVWEPVF-----------EREARFSKKQP----------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103  162 ylkacdnfinktdkllYPLFGYSPTDYEYLKHFYKTWSAFNTLKSFSWKDEYMYSKNYDRRTKREVNRRNEKARQQARNE 241
Cdd:COG5269 150 ----------------VPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQ 213

                       250       260       270
                ....*....|....*....|....*....|....
gi 6324103  242 YNKTVKRFVVFIKKLDKRMKegaKIAEEQRKLKE 275
Cdd:COG5269 214 DNARLKRLVQIAKKRDPRIK---SFKEQEKEMKK 244
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 338-363 5.54e-08

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 48.71  E-value: 5.54e-08
                          10        20
                  ....*....|....*....|....*.
gi 6324103    338 YECFICNKTFKSEKQLKNHINTKLHK 363
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 338-365 1.40e-03

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 36.46  E-value: 1.40e-03
                           10        20
                   ....*....|....*....|....*...
gi 6324103     338 YECFICNKTFKSEKQLKNHINTKLHKKN 365
Cdd:smart00451   4 FYCKLCNVTFTDEISVEAHLKGKKHKKN 31
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 1-67 1.89e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 116.78  E-value: 1.89e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK10767   2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 4-67 6.43e-26

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: 100.63  E-value: 6.43e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6324103      4 CYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 5-83 1.85e-24

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: 99.39  E-value: 1.85e-24
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6324103    5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYDSHKEQILNDTPPSTDD 83
Cdd:COG0484   2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAE 79
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 5-67 1.55e-23

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: 102.29  E-value: 1.55e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103      5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:TIGR02349   2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYD 62
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 1-67 8.29e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 100.59  E-value: 8.29e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14301   2 SQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN-PEAEQKFKEAAEAYEVLRDAEKRARYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 1-67 4.91e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 98.33  E-value: 4.91e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14277   3 AKKDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGD-KEAEQKFKEINEAYEILSDPQKRAQYD 68
DnaJ smart00271
DnaJ molecular chaperone homology domain;
3-61 1.30e-21

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 88.45  E-value: 1.30e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 6324103       3 TCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNVEEATQKFAVIRAAYEVLSDPQ 61
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPE 59
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
5-67 2.49e-21

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 88.62  E-value: 2.49e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103    5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNVEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:COG2214   7 HYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 2-77 2.68e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 95.99  E-value: 2.68e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324103     2 KTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYDSHKEQILNDT 77
Cdd:PRK14294   3 KRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGD-KEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGT 77
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 1-67 3.30e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 95.89  E-value: 3.30e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14278   1 MARDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPD--EEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14289 PRK14289
molecular chaperone DnaJ;
5-67 3.54e-21

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 95.67  E-value: 3.54e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14289   7 YYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPGD-KEAEEKFKEAAEAYDVLSDPDKRSRYD 68
PRK14297 PRK14297
molecular chaperone DnaJ;
5-67 8.46e-21

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 94.46  E-value: 8.46e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14297   6 YYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGN-KEAEEKFKEINEAYQVLSDPQKKAQYD 67
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 4-59 2.83e-20

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: 84.52  E-value: 2.83e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 6324103    4 CYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSD 59
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 1-67 4.48e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 92.56  E-value: 4.48e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14281   1 MKRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDN-KEAEEHFKEVNEAYEVLSNDDKRRRYD 66
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 5-67 8.48e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 91.39  E-value: 8.48e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNVEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14282   6 YYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 1-102 1.40e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 87.90  E-value: 1.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYDSHKEQILNdtpPS 80
Cdd:PRK14291   1 AKKDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKN--PEAEEKFKEINEAYQVLSDPEKRKLYDQFGHAAFS---GS 75

                         90       100
                 ....*....|....*....|..
gi 6324103    81 TDDYYDYEVDATVTGVTTDELL 102
Cdd:PRK14291  76 GQQQQGQEGFSDFGGGNIEDIL 97
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 5-67 2.02e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 87.21  E-value: 2.02e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14298   7 YYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKE--PDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 5-67 2.48e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 87.21  E-value: 2.48e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNVeEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14284   3 YYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGDA-EAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14280 PRK14280
molecular chaperone DnaJ;
5-67 5.29e-18

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 85.93  E-value: 5.29e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14280   6 YYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKE--EGADEKFKEISEAYEVLSDDQKRAQYD 66
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 5-67 1.14e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 84.94  E-value: 1.14e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14292   4 YYELLGVSRTASADEIKSAYRKLALKYHPDRNKE--KGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 1-67 1.71e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 84.21  E-value: 1.71e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNVEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14290   1 MAKDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYD 67
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 5-64 1.91e-17

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 76.58  E-value: 1.91e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103    5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERA 64
Cdd:COG5407   2 PYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGD-PKAEERFKEINEAYELLSDAEKRA 60
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 5-67 3.52e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 83.60  E-value: 3.52e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14276   6 YYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKE--PGAEEKYKEVQEAYETLSDPQKRAAYD 66
PRK14293 PRK14293
molecular chaperone DnaJ;
1-67 3.57e-17

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 83.50  E-value: 3.57e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14293   1 MAADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKE--PGAEDRFKEINRAYEVLSDPETRARYD 65
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 5-67 1.32e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 81.96  E-value: 1.32e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14286   6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGN-KESEEKFKEATEAYEILRDPKKRQAYD 67
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
5-69 7.16e-16

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 80.25  E-value: 7.16e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYDSH 69
Cdd:NF037946   7 YYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKA--PDAAEIFAEINEAYEVLSNPEKRANYDKY 69
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 5-67 1.51e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 78.71  E-value: 1.51e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14283   7 YYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEE--EGAEEKFKEISEAYAVLSDDEKRQRYD 67
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 5-69 1.97e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 77.29  E-value: 1.97e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnvEEATQKFAVIRAAYEVLSDPQERAWYDSH 69
Cdd:PRK14299   6 YYAILGVPKNASQDEIKKAFKKLARKYHPDVNKS--PGAEEKFKEINEAYTVLSDPEKRRIYDTY 68
PRK14295 PRK14295
molecular chaperone DnaJ;
5-67 3.21e-15

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 77.58  E-value: 3.21e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNVeEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14295  11 YYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDA-KAEERFKEISEAYDVLSDEKKRKEYD 72
PRK14288 PRK14288
molecular chaperone DnaJ;
1-90 1.34e-14

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 75.50  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYDSHKEQILNDTPPS 80
Cdd:PRK14288   1 MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGD-KEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNQAGAS 79

                         90
                 ....*....|
gi 6324103    81 TDDYYDYEVD 90
Cdd:PRK14288  80 QSDFSDFFED 89
PRK14279 PRK14279
molecular chaperone DnaJ;
5-67 1.36e-14

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 75.92  E-value: 1.36e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14279  11 FYKELGVSSDASAEEIKKAYRKLARELHPDANPGD-PAAEERFKAVSEAHDVLSDPAKRKEYD 72
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
5-61 1.38e-14

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 68.67  E-value: 1.38e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324103    5 YYELLGVETHASDLELKKAYRKKALQYHPDK-----NPDNVEEATQKFAVIRAAYEVLSDPQ 61
Cdd:COG1076   6 AFELLGLPPDADDAELKRAYRKLQREHHPDRlaaglPEEEQRLALQKAAAINEAYETLKDPR 67
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 1-67 4.05e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 74.26  E-value: 4.05e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNvEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14285   1 MKRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGN-KEAESIFKEATEAYEVLIDDNKRAQYD 66
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 5-87 4.43e-14

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 74.47  E-value: 4.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNPDnveeaTQKFAVIRAAYEVLSDPQERAWYDSHKEQILNDTPPSTD-- 82
Cdd:PTZ00037  30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD-----PEKFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQPADas 104


                 ....*
gi 6324103    83 DYYDY 87
Cdd:PTZ00037 105 DLFDL 109
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 5-67 4.79e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 73.89  E-value: 4.79e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPDKNpdNVEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14287   6 YYEVLGVDRNASVDEVKKAYRKLARKYHPDVN--KAPDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 1-67 1.76e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 72.35  E-value: 1.76e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103     1 MKTCYYELLGVETHASDLELKKAYRKKALQYHPDKNpdNVEEATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK14300   1 MSQDYYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQKRAAYD 65
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
 5-69 2.27e-11

terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274808 [Multi-domain]  Cd Length: 871  Bit Score: 66.76  E-value: 2.27e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324103      5 YYELLGVETHASDLELKKAYRKKALQYHPDKNpdNVEEATQKFAVIRAAYEVLSDPQERAWYDSH 69
Cdd:TIGR03835   4 YYEVLGIDRDADEQEIKKAFRKLAKKYHPDRN--KAPDAASIFAEINEANDVLSNPKKRANYDKY 66
PRK10266 PRK10266
curved DNA-binding protein;
5-67 1.02e-10

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 62.92  E-value: 1.02e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324103     5 YYELLGVETHASDLELKKAYRKKALQYHPD--KNPDnveeATQKFAVIRAAYEVLSDPQERAWYD 67
Cdd:PRK10266   6 YYAIMGVKPTDDLKTIKTAYRRLARKYHPDvsKEPD----AEARFKEVAEAWEVLSDEQRRAEYD 66
djlA PRK09430
co-chaperone DjlA;
6-57 6.07e-10

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 60.21  E-value: 6.07e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6324103     6 YELLGVETHASDLELKKAYRKKALQYHPDK------NPDNVEEATQKFAVIRAAYEVL 57
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakglPPEMMEMAKEKAQEIQAAYELI 260
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 2-88 8.68e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 57.65  E-value: 8.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103     2 KTCYYELLGVETHASDLELKKAYRKKALQYHPDKNPDNveEATQKFAVIRAAYEVLSDPQERAWYDSHKEQILNDTPPST 81
Cdd:PRK14296   3 KKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSP--DAHDKMVEINEAADVLLDKDKRKQYDQFGHAAFDGSSGFS 80


                 ....*..
gi 6324103    82 DDYYDYE 88
Cdd:PRK14296  81 SNFGDFE 87
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 6-275 1.44e-08

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 56.96  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103    6 YELLGVE---THASDLELKKAYRKKALQYHPDKNPDNVEEATQK-FAVIRAAYEVLSDPQERAWYDSHKEqilNDTPPST 81
Cdd:COG5269  46 YALLGLSkyrTKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEfFKLIQKAREVLGDRKLRLQYDSNDF---DADVPPP 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103   82 DDYYDYEvdatvtgvttdelllffnsalytkidnsaagIYQIAGKIFaklakdeilsgKRLGKFSEYQDdvfeqdinsig 161
Cdd:COG5269 123 RIYTPDE-------------------------------FFEVWEPVF-----------EREARFSKKQP----------- 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324103  162 ylkacdnfinktdkllYPLFGYSPTDYEYLKHFYKTWSAFNTLKSFSWKDEYMYSKNYDRRTKREVNRRNEKARQQARNE 241
Cdd:COG5269 150 ----------------VPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQ 213

                       250       260       270
                ....*....|....*....|....*....|....
gi 6324103  242 YNKTVKRFVVFIKKLDKRMKegaKIAEEQRKLKE 275
Cdd:COG5269 214 DNARLKRLVQIAKKRDPRIK---SFKEQEKEMKK 244
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 338-363 5.54e-08

Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, and is approximately 30 amino acids in length. The mammalian members of this group occur multiple times along the protein, joined by flexible linkers, and are referred to as JAZ - dsRNA-binding ZF protein - zinc-fingers. The JAZ proteins are expressed in all tissues tested and localize in the nucleus, particularly the nucleolus. JAZ preferentially binds to double-stranded (ds) RNA or RNA/DNA hybrids rather than DNA. In addition to binding double-stranded RNA, these zinc-fingers are required for nucleolar localization.


Pssm-ID: 432381 [Multi-domain]  Cd Length: 27  Bit Score: 48.71  E-value: 5.54e-08
                          10        20
                  ....*....|....*....|....*.
gi 6324103    338 YECFICNKTFKSEKQLKNHINTKLHK 363
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
zf-met pfam12874
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ...
 338-362 2.19e-06

Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found in multiple copies in a wide range of proteins from plants to metazoans. Some member proteins, particularly those from plants, are annotated as being RNA-binding.


Pssm-ID: 463736 [Multi-domain]  Cd Length: 25  Bit Score: 44.02  E-value: 2.19e-06
                          10        20
                  ....*....|....*....|....*
gi 6324103    338 YECFICNKTFKSEKQLKNHINTKLH 362
Cdd:pfam12874   1 FYCELCNVTFNSESQLKSHLQGKKH 25
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 3-69 7.54e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.93  E-value: 7.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324103      3 TCYYELLGVETHASDLELKKAYRKKALQYHPDKNpdNVEEATQKFAVIRAAYEVLSDPQERAWYDSH 69
Cdd:PTZ00341  573 TLFYDILGVGVNADMKEISERYFKLAENYYPPKR--SGNEGFHKFKKINEAYQILGDIDKKKMYNKF 637
PHA03102 PHA03102
Small T antigen; Reviewed
 7-77 2.77e-04

Small T antigen; Reviewed


Pssm-ID: 222986 [Multi-domain]  Cd Length: 153  Bit Score: 41.58  E-value: 2.77e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324103     7 ELLGVETHA-SDLEL-KKAYRKKALQYHPDK--NPDNVEEATQKFAVIRAAYEVLSDPQERAWYDSHKEQILNDT 77
Cdd:PHA03102   9 DLLGLPRSAwGNLPLmRKAYLRKCLEFHPDKggDEEKMKELNTLYKKFRESVKSLRDLDGEEDSSSEEEDVPSGY 83
zf-C2H2 pfam00096
Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two ...
 338-359 5.54e-04

Zinc finger, C2H2 type; The C2H2 zinc finger is the classical zinc finger domain. The two conserved cysteines and histidines co-ordinate a zinc ion. The following pattern describes the zinc finger. #-X-C-X(1-5)-C-X3-#-X5-#-X2-H-X(3-6)-[H/C] Where X can be any amino acid, and numbers in brackets indicate the number of residues. The positions marked # are those that are important for the stable fold of the zinc finger. The final position can be either his or cys. The C2H2 zinc finger is composed of two short beta strands followed by an alpha helix. The amino terminal part of the helix binds the major groove in DNA binding zinc fingers. The accepted consensus binding sequence for Sp1 is usually defined by the asymmetric hexanucleotide core GGGCGG but this sequence does not include, among others, the GAG (=CTC) repeat that constitutes a high-affinity site for Sp1 binding to the wt1 promoter.


Pssm-ID: 395048 [Multi-domain]  Cd Length: 23  Bit Score: 37.28  E-value: 5.54e-04
                          10        20
                  ....*....|....*....|..
gi 6324103    338 YECFICNKTFKSEKQLKNHINT 359
Cdd:pfam00096   1 YKCPDCGKSFSRKSNLKRHLRT 22
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 338-365 1.40e-03

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 36.46  E-value: 1.40e-03
                           10        20
                   ....*....|....*....|....*...
gi 6324103     338 YECFICNKTFKSEKQLKNHINTKLHKKN 365
Cdd:smart00451   4 FYCKLCNVTFTDEISVEAHLKGKKHKKN 31
PHA02624 PHA02624
large T antigen; Provisional
 7-46 4.16e-03

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 39.97  E-value: 4.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 6324103     7 ELLGVETHA-SDLEL-KKAYRKKALQYHPDKNPDnvEEATQK 46
Cdd:PHA02624  15 DLLGLPMAAwGNLPLmRKAYLRKCKEYHPDKGGD--EEKMKR 54
zf-C2H2_4 pfam13894
C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.
 338-359 9.43e-03

C2H2-type zinc finger; This family contains a number of divergent C2H2 type zinc fingers.


Pssm-ID: 464025  Cd Length: 24  Bit Score: 34.16  E-value: 9.43e-03
                          10        20
                  ....*....|....*....|..
gi 6324103    338 YECFICNKTFKSEKQLKNHINT 359
Cdd:pfam13894   1 FKCPICGKSFSSKKSLKRHLKT 22
 
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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