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Conserved domains on  [gi|1034643595|ref|XP_005248307|]
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dnaJ homolog subfamily C member 21 isoform X4 [Homo sapiens]

Protein Classification

CbpA and DnaJ domain-containing protein; DnaJ and zf-C2H2_jaz domain-containing protein( domain architecture ID 13466669)

protein containing domains CbpA, DnaJ, and zf-C2H2_jaz; 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
 87-166 3.50e-29

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK10767:

Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 118.71  E-value: 3.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  87 AMKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK----- 161
Cdd:PRK10767    2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEqgggg 80


                  ....*
gi 1034643595 162 GGFDG 166
Cdd:PRK10767   81 GGFGG 85
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 91-354 6.10e-15

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: 76.61  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGV---RRDASEEELKKAYRKLALKWHPDKNLDNAA-EAAEQFKLIQAAYDVLSDPQERAWYDNHreallkgGFDG 166
Cdd:COG5269    45 LYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNkGCDEFFKLIQKAREVLGDRKLRLQYDSN-------DFDA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 167 EYQDDSLdllryftvtcysgYGDDEkgFYTVYRNVFEMIAKEELESVleeevddFPTFGDSQSDYDTVvHPFYAYWQSFC 246
Cdd:COG5269   118 DVPPPRI-------------YTPDE--FFEVWEPVFEREARFSKKQP-------VPSLGPSDSSLKEV-EEFYEFWSNFD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 247 TQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQnAEKARKAEEMR 326
Cdd:COG5269   175 SWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ-EKEMKKIRKWE 249

                         250       260
                  ....*....|....*....|....*...
gi 1034643595 327 RQQKLKQAKLVEQYREQSWMTMANLEKE 354
Cdd:COG5269   250 REAGARLKALAALKGKAEAKNKAEIEAE 277
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 401-426 9.83e-10

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: 53.71  E-value: 9.83e-10
                          10        20
                  ....*....|....*....|....*.
gi 1034643595 401 LYCPACDKSFKTEKAMKNHEKSKKHR 426
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-166 3.50e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 118.71  E-value: 3.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  87 AMKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK----- 161
Cdd:PRK10767    2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEqgggg 80


                  ....*
gi 1034643595 162 GGFDG 166
Cdd:PRK10767   81 GGFGG 85
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 92-179 8.11e-28

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: 114.62  E-value: 8.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  92 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDnaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEYQDD 171
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGGGF 80


                  ....*...
gi 1034643595 172 SLDLLRYF 179
Cdd:TIGR02349  81 NGFDIGFF 88
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 90-153 1.91e-27

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: 104.86  E-value: 1.91e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034643595  90 CHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 153
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 91-160 1.04e-23

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: 97.08  E-value: 1.04e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL 160
Cdd:COG0484     2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAE 70
DnaJ smart00271
DnaJ molecular chaperone homology domain;
89-147 7.85e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 91.53  E-value: 7.85e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034643595   89 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQ 147
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPE 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 90-145 1.81e-21

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: 87.60  E-value: 1.81e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034643595  90 CHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSD 145
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 91-354 6.10e-15

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 76.61  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGV---RRDASEEELKKAYRKLALKWHPDKNLDNAA-EAAEQFKLIQAAYDVLSDPQERAWYDNHreallkgGFDG 166
Cdd:COG5269    45 LYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNkGCDEFFKLIQKAREVLGDRKLRLQYDSN-------DFDA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 167 EYQDDSLdllryftvtcysgYGDDEkgFYTVYRNVFEMIAKEELESVleeevddFPTFGDSQSDYDTVvHPFYAYWQSFC 246
Cdd:COG5269   118 DVPPPRI-------------YTPDE--FFEVWEPVFEREARFSKKQP-------VPSLGPSDSSLKEV-EEFYEFWSNFD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 247 TQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQnAEKARKAEEMR 326
Cdd:COG5269   175 SWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ-EKEMKKIRKWE 249

                         250       260
                  ....*....|....*....|....*...
gi 1034643595 327 RQQKLKQAKLVEQYREQSWMTMANLEKE 354
Cdd:COG5269   250 REAGARLKALAALKGKAEAKNKAEIEAE 277
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 401-426 9.83e-10

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: 53.71  E-value: 9.83e-10
                          10        20
                  ....*....|....*....|....*.
gi 1034643595 401 LYCPACDKSFKTEKAMKNHEKSKKHR 426
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 400-432 3.65e-07

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: 46.48  E-value: 3.65e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034643595  400 DLYCPACDKSFKTEKAMKNHEKSKKHREMVALL 432
Cdd:smart00451   3 GFYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
PTZ00121 PTZ00121
MAEBL; Provisional
 254-427 2.94e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  254 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQ----- 328
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKveqlk 1639

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  329 ----QKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDE-----AEDAELYD 399
Cdd:PTZ00121  1640 kkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAE 1719

                          170       180
                   ....*....|....*....|....*...
gi 1034643595  400 DLYCPACDKSFKTEKAMKNHEKSKKHRE 427
Cdd:PTZ00121  1720 ELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 267-385 2.38e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 267 EKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLVEQYREQswm 346
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--- 243

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034643595 347 tMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEED 385
Cdd:pfam13868 244 -QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEA 281
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-166 3.50e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 118.71  E-value: 3.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  87 AMKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK----- 161
Cdd:PRK10767    2 AKRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEqgggg 80


                  ....*
gi 1034643595 162 GGFDG 166
Cdd:PRK10767   81 GGFGG 85
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 92-179 8.11e-28

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: 114.62  E-value: 8.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  92 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDnaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEYQDD 171
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGGGF 80


                  ....*...
gi 1034643595 172 SLDLLRYF 179
Cdd:TIGR02349  81 NGFDIGFF 88
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 90-153 1.91e-27

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: 104.86  E-value: 1.91e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034643595  90 CHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 153
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 91-160 1.04e-23

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: 97.08  E-value: 1.04e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL 160
Cdd:COG0484     2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAE 70
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 91-205 5.77e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 100.69  E-value: 5.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREAllkgGFDGEYQD 170
Cdd:PRK14298    7 YYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAE--EKFKEISEAYAVLSDAEKRAQYDRFGHA----GIDNQYSA 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034643595 171 DSLdllryFTVTCYSGYGDdekgfytvyrnVFEMI 205
Cdd:PRK14298   81 EDI-----FRGADFGGFGD-----------IFEMF 99
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 92-166 7.15e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 100.55  E-value: 7.15e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034643595  92 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 166
Cdd:PRK14276    7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAE--EKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFGG 79
DnaJ smart00271
DnaJ molecular chaperone homology domain;
89-147 7.85e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 91.53  E-value: 7.85e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034643595   89 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQ 147
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPE 59
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 86-153 1.10e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 99.87  E-value: 1.10e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034643595  86 RAMKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYD 153
Cdd:PRK14282    1 REKKDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK14293 PRK14293
molecular chaperone DnaJ;
88-163 3.74e-22

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 98.14  E-value: 3.74e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034643595  88 MKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGG 163
Cdd:PRK14293    2 AADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAE--DRFKEINRAYEVLSDPETRARYDQFGEAGVSGA 75
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 89-166 1.69e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 96.37  E-value: 1.69e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034643595  89 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKG-GFDG 166
Cdd:PRK14294    4 RDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGD-KEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGtGFSG 81
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 90-145 1.81e-21

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: 87.60  E-value: 1.81e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034643595  90 CHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSD 145
Cdd:cd06257     1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 89-166 2.01e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 95.96  E-value: 2.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  89 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL--KGGFDG 166
Cdd:PRK14301    4 RDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN-PEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVngNGGFGG 82
PRK14297 PRK14297
molecular chaperone DnaJ;
87-166 2.82e-21

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 95.62  E-value: 2.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  87 AMKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK--GGF 164
Cdd:PRK14297    2 ASKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGN-KEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNgaGGF 80


                  ..
gi 1034643595 165 DG 166
Cdd:PRK14297   81 GS 82
PRK14279 PRK14279
molecular chaperone DnaJ;
89-170 2.90e-21

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 95.95  E-value: 2.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  89 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAeAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEY 168
Cdd:PRK14279    9 KDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPA-AEERFKAVSEAHDVLSDPAKRKEYDETRRLFAGGGFGGRR 87


                  ..
gi 1034643595 169 QD 170
Cdd:PRK14279   88 FD 89
PRK14295 PRK14295
molecular chaperone DnaJ;
89-164 4.12e-21

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 95.30  E-value: 4.12e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034643595  89 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAeAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGF 164
Cdd:PRK14295    9 KDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAK-AEERFKEISEAYDVLSDEKKRKEYDEARSLFGNGGF 83
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
91-153 9.80e-21

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 86.70  E-value: 9.80e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYD 153
Cdd:COG2214     7 HYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14280 PRK14280
molecular chaperone DnaJ;
91-166 2.58e-20

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 92.86  E-value: 2.58e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 166
Cdd:PRK14280    6 YYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN--KEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGG 79
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 91-153 2.61e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 92.81  E-value: 2.61e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaaEAAEQFKLIQAAYDVLSDPQERAWYD 153
Cdd:PRK14278    5 YYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDE--EAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 89-166 1.44e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 90.63  E-value: 1.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  89 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL------KG 162
Cdd:PRK14277    5 KDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGD-KEAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFdpggfgQG 83


                  ....
gi 1034643595 163 GFDG 166
Cdd:PRK14277   84 GFGQ 87
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 89-153 1.69e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 90.38  E-value: 1.69e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034643595  89 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYD 153
Cdd:PRK14290    3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYD 67
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 87-170 1.78e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 90.60  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  87 AMKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREAllkgGFDG 166
Cdd:PRK14291    1 AKKDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAE--EKFKEINEAYQVLSDPEKRKLYDQFGHA----AFSG 74


                  ....
gi 1034643595 167 EYQD 170
Cdd:PRK14291   75 SGQQ 78
PRK14289 PRK14289
molecular chaperone DnaJ;
91-167 5.27e-19

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 89.12  E-value: 5.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNlDNAAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK-----GGFD 165
Cdd:PRK14289    7 YYEVLGVSKTATVDEIKKAYRKKAIQYHPDKN-PGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGgaaggGGFS 85


                  ..
gi 1034643595 166 GE 167
Cdd:PRK14289   86 GE 87
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 91-153 8.78e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 88.71  E-value: 8.78e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 153
Cdd:PRK14281    5 YYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDN-KEAEEHFKEVNEAYEVLSNDDKRRRYD 66
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 92-150 1.00e-18

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 80.04  E-value: 1.00e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034643595  92 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAeAAEQFKLIQAAYDVLSDPQERA 150
Cdd:COG5407     3 YEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPK-AEERFKEINEAYELLSDAEKRA 60
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 91-179 1.12e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 87.98  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNH-REALLK--GGFDGE 167
Cdd:PRK14284    3 YYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGD-AEAEKRFKEVSEAYEVLSDAQKRESYDRYgKDGPFAgaGGFGGA 81

                          90
                  ....*....|..
gi 1034643595 168 YQDDSLDLLRYF 179
Cdd:PRK14284   82 GMGNMEDALRTF 93
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 89-166 2.34e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 86.97  E-value: 2.34e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034643595  89 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 166
Cdd:PRK14286    4 RSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGN-KESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGG 80
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 87-166 2.59e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 85.38  E-value: 2.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  87 AMKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 166
Cdd:PRK14299    2 AYKDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAE--EKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQG 79
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 91-204 7.97e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 85.26  E-value: 7.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaaEAAEQFKLIQAAYDVLSDPQERAWYDNHREAllkgGFDGEYQD 170
Cdd:PRK14283    7 YYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEE--GAEEKFKEISEAYAVLSDDEKRQRYDQFGHA----GMDGFSQE 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1034643595 171 DSLDLLRYFTVtcYSGYGDDekgfytvYRNVFEM 204
Cdd:PRK14283   81 DIFNNINFEDI--FQGFGFG-------IGNIFDM 105
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 91-153 1.54e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 84.56  E-value: 1.54e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDnaAEAAEQFKLIQAAYDVLSDPQERAWYD 153
Cdd:PRK14292    4 YYELLGVSRTASADEIKSAYRKLALKYHPDRNKE--KGAAEKFAQINEAYAVLSDAEKRAHYD 64
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 92-176 4.64e-17

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 83.33  E-value: 4.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  92 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDnaaeaAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEYQDD 171
Cdd:PTZ00037   31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD-----PEKFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQPADASD 105


                  ....*
gi 1034643595 172 SLDLL 176
Cdd:PTZ00037  106 LFDLI 110
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 91-166 4.35e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 80.05  E-value: 4.35e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 166
Cdd:PRK14287    6 YYEVLGVDRNASVDEVKKAYRKLARKYHPDVN--KAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPNQGFGG 79
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 91-166 2.59e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 77.72  E-value: 2.59e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGG--FDG 166
Cdd:PRK14285    5 YYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGN-KEAESIFKEATEAYEVLIDDNKRAQYDRFGHTAFEGGggFEG 81
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 91-354 6.10e-15

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 76.61  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGV---RRDASEEELKKAYRKLALKWHPDKNLDNAA-EAAEQFKLIQAAYDVLSDPQERAWYDNHreallkgGFDG 166
Cdd:COG5269    45 LYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNkGCDEFFKLIQKAREVLGDRKLRLQYDSN-------DFDA 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 167 EYQDDSLdllryftvtcysgYGDDEkgFYTVYRNVFEMIAKEELESVleeevddFPTFGDSQSDYDTVvHPFYAYWQSFC 246
Cdd:COG5269   118 DVPPPRI-------------YTPDE--FFEVWEPVFEREARFSKKQP-------VPSLGPSDSSLKEV-EEFYEFWSNFD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 247 TQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQnAEKARKAEEMR 326
Cdd:COG5269   175 SWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ-EKEMKKIRKWE 249

                         250       260
                  ....*....|....*....|....*...
gi 1034643595 327 RQQKLKQAKLVEQYREQSWMTMANLEKE 354
Cdd:COG5269   250 REAGARLKALAALKGKAEAKNKAEIEAE 277
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 91-179 6.12e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 73.51  E-value: 6.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYD-------NHREALLKGG 163
Cdd:PRK14300    5 YYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQKRAAYDrfghdafQNQQSRGGGG 82

                          90
                  ....*....|....*.
gi 1034643595 164 FDGEYQDDSLDLLRYF 179
Cdd:PRK14300   83 NHGGFHPDINDIFGDF 98
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 87-170 3.00e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 68.43  E-value: 3.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  87 AMKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKG--GF 164
Cdd:PRK14296    2 KKKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAH--DKMVEINEAADVLLDKDKRKQYDQFGHAAFDGssGF 79


                  ....*.
gi 1034643595 165 DGEYQD 170
Cdd:PRK14296   80 SSNFGD 85
PRK10266 PRK10266
curved DNA-binding protein;
88-157 1.52e-11

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 65.61  E-value: 1.52e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  88 MKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAaeQFKLIQAAYDVLSDPQERAWYDNHRE 157
Cdd:PRK10266    3 LKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEA--RFKEVAEAWEVLSDEQRRAEYDQLWQ 70
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
88-147 2.14e-11

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 59.81  E-value: 2.14e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034643595  88 MKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAE-----AAEQFKLIQAAYDVLSDPQ 147
Cdd:COG1076     3 LDDAFELLGLPPDADDAELKRAYRKLQREHHPDRLAAGLPEeeqrlALQKAAAINEAYETLKDPR 67
PRK14288 PRK14288
molecular chaperone DnaJ;
91-179 2.22e-11

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 65.48  E-value: 2.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK--GGFDGEY 168
Cdd:PRK14288    5 YYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGD-KEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNqaGASQSDF 83

                          90
                  ....*....|.
gi 1034643595 169 QDDSLDLLRYF 179
Cdd:PRK14288   84 SDFFEDLGSFF 94
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 401-426 9.83e-10

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: 53.71  E-value: 9.83e-10
                          10        20
                  ....*....|....*....|....*.
gi 1034643595 401 LYCPACDKSFKTEKAMKNHEKSKKHR 426
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 400-432 3.65e-07

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: 46.48  E-value: 3.65e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1034643595  400 DLYCPACDKSFKTEKAMKNHEKSKKHREMVALL 432
Cdd:smart00451   3 GFYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
zf-met pfam12874
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ...
 401-425 6.55e-07

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: 45.56  E-value: 6.55e-07
                          10        20
                  ....*....|....*....|....*
gi 1034643595 401 LYCPACDKSFKTEKAMKNHEKSKKH 425
Cdd:pfam12874   1 FYCELCNVTFNSESQLKSHLQGKKH 25
djlA PRK09430
co-chaperone DjlA;
92-143 8.55e-07

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 50.58  E-value: 8.55e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034643595  92 YEALGVRRDASEEELKKAYRKLALKWHPDK-----------NLdnAAEAAEQfklIQAAYDVL 143
Cdd:PRK09430  203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakglppemmEM--AKEKAQE---IQAAYELI 260
PTZ00121 PTZ00121
MAEBL; Provisional
 254-468 8.89e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 8.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  254 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQlvafiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ 333
Cdd:PTZ00121  1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  334 AKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKdsDEAEDAELYDDLYCPACDKSFKTE 413
Cdd:PTZ00121  1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEA 1643

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1034643595  414 KAMKNHEKSKKHREMVALLKQQLEEEEENFSRpQIDENPLDDNSEEEMEDAPKQK 468
Cdd:PTZ00121  1644 EEKKKAEELKKAEEENKIKAAEEAKKAEEDKK-KAEEAKKAEEDEKKAAEALKKE 1697
PTZ00121 PTZ00121
MAEBL; Provisional
 254-427 2.94e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  254 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQ----- 328
Cdd:PTZ00121  1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKveqlk 1639

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  329 ----QKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDE-----AEDAELYD 399
Cdd:PTZ00121  1640 kkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAE 1719

                          170       180
                   ....*....|....*....|....*...
gi 1034643595  400 DLYCPACDKSFKTEKAMKNHEKSKKHRE 427
Cdd:PTZ00121  1720 ELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 91-166 3.74e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 43.62  E-value: 3.74e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034643595   91 HYEALGVRRDASEEELKKAYRKLALKWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYDnhreallKGGFDG 166
Cdd:PTZ00341   575 FYDILGVGVNADMKEISERYFKLAENYYPPKR--SGNEGFHKFKKINEAYQILGDIDKKKMYN-------KFGYDG 641
PTZ00121 PTZ00121
MAEBL; Provisional
 254-423 5.16e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  254 KEEYDTRQASNRWEKRAMEKENKKIRDKARK----EKNELVRQLVAFIRKRD-------KRVQAHRKLVEEQNAEKARKA 322
Cdd:PTZ00121  1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeaRKAEDARKAEEARKAEDakrveiaRKAEDARKAEEARKAEDAKKA 1178

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  323 EEMRRQQKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDLY 402
Cdd:PTZ00121  1179 EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258

                          170       180
                   ....*....|....*....|.
gi 1034643595  403 CPACDKSFKTEKAMKNHEKSK 423
Cdd:PTZ00121  1259 EARMAHFARRQAAIKAEEARK 1279
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 267-463 1.99e-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: 40.88  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 267 EKRAMEKENK--KIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKL----KQAKLVEQY 340
Cdd:pfam17380 340 ERMAMEREREleRIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKIleeeRQRKIQQQK 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 341 REQSWMTMANLEKELQEMEaRYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAElyddlycpacdKSFKTEKAMKNHE 420
Cdd:pfam17380 420 VEMEQIRAEQEEARQREVR-RLEEERAREMERVRLEEQERQQQVERLRQQEEERKR-----------KKLELEKEKRDRK 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034643595 421 KSKKHREMValLKQQLEEEEenfsRPQIDENPLDDNSEEEMED 463
Cdd:pfam17380 488 RAEEQRRKI--LEKELEERK----QAMIEEERKRKLLEKEMEE 524
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 267-385 2.38e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 267 EKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLVEQYREQswm 346
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--- 243

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1034643595 347 tMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEED 385
Cdd:pfam13868 244 -QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEA 281
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 254-446 2.73e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.73  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  254 KEEYDTRQASNRWEKRAMEKENKKIRDK----------ARKEKNELVRQLVAFIRKRDK--RVQAHRKLVEEQNAEKARK 321
Cdd:pfam02463  302 LLKLERRKVDDEEKLKESEKEKKKAEKElkkekeeieeLEKELKELEIKREAEEEEEEEleKLQEKLEQLEEELLAKKKL 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  322 AEEMR-RQQKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDD 400
Cdd:pfam02463  382 ESERLsSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLL 461

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1034643595  401 LYCPACDKSFKTEKAMKNHEKSKKHREMVALLKQQLEEEEENFSRP 446
Cdd:pfam02463  462 KDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
269-401 3.54e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 269 RAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ--AKLVEQYREQSWM 346
Cdd:PRK03918  506 KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEelAELLKELEELGFE 585

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034643595 347 TMANLEKELQEMEARYEK--EFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDL 401
Cdd:PRK03918  586 SVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
PTZ00121 PTZ00121
MAEBL; Provisional
 254-428 5.33e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 5.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  254 KEEYDTRQASNRWEKRAMEKENKKIRDKA--RKEKNELVRQLVAFIRKRDkrvQAHRKLVEEQNAEKARKAEEMRRQQKL 331
Cdd:PTZ00121  1451 KKAEEAKKAEEAKKKAEEAKKADEAKKKAeeAKKADEAKKKAEEAKKKAD---EAKKAAEAKKKADEAKKAEEAKKADEA 1527

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595  332 KQAklvEQYREQSWMTMANLEKELQEM----EARYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDLYCPACD 407
Cdd:PTZ00121  1528 KKA---EEAKKADEAKKAEEKKKADELkkaeELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEE 1604

                          170       180
                   ....*....|....*....|.
gi 1034643595  408 KSFKTEKAMKNHEKSKKHREM 428
Cdd:PTZ00121  1605 KKMKAEEAKKAEEAKIKAEEL 1625
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 254-391 9.99e-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: 38.95  E-value: 9.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034643595 254 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQlvafirkrDKRVQAHRKLVEEQNAEKARKAEEMRR---QQK 330
Cdd:pfam17380 429 QEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQ--------QEEERKRKKLELEKEKRDRKRAEEQRRkilEKE 500

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034643595 331 LKQAK--LVEQYREQSWmtmanLEKELQEME-ARYEKEFGDGSDEN-----EMEEHELKDEEDGKDSDE 391
Cdd:pfam17380 501 LEERKqaMIEEERKRKL-----LEKEMEERQkAIYEEERRREAEEErrkqqEMEERRRIQEQMRKATEE 564
 
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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