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Conserved domains on  [gi|190194391|ref|NP_084322|]
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dnaJ homolog subfamily C member 21 [Mus musculus]

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
 2-66 8.43e-28

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK10767:

Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 114.47  E-value: 8.43e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK10767   4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYD 67
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 4-267 2.51e-13

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: 71.60  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGV---RRDASEEELKKAYRKLALRWHPDKNLDNAA-EAAEQFKLIQAAYDVLSDPQERAWYDNHREallkgglDG 79
Cdd:COG5269   45 LYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNkGCDEFFKLIQKAREVLGDRKLRLQYDSNDF-------DA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  80 EYQDDSLdllhyftvtcysgYGDDErgFYAVYRVVFELIAKEELEcmsegdvEDFPTFGDSQSDYDTVvHPFYAHWQSFC 159
Cdd:COG5269  118 DVPPPRI-------------YTPDE--FFEVWEPVFEREARFSKK-------QPVPSLGPSDSSLKEV-EEFYEFWSNFD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391 160 TQKNFSWKEEYDTRQASNRWEKRAMEKENKKIRDRARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQnAEKARKAEEMR 239
Cdd:COG5269  175 SWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ-EKEMKKIRKWE 249

                        250       260
                 ....*....|....*....|....*...
gi 190194391 240 RQQKLKQAKLAEQYREQSWMTMANLEKE 267
Cdd:COG5269  250 REAGARLKALAALKGKAEAKNKAEIEAE 277
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 314-339 2.28e-09

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: 52.56  E-value: 2.28e-09
                          10        20
                  ....*....|....*....|....*.
gi 190194391  314 LYCPACDKSFKTEKAMKNHEKSKKHR 339
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
PTZ00121 super family cl31754
MAEBL; Provisional
 181-471 3.64e-04

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  181 KRAMEKENKKIRDRARKEKNELVRQLVAFIRKRD--KRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLAEQYREQSW 258
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK 1213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  259 MTMANLEKELQEMEARYEKEFGDGSDENEVEDQEPRNGLDGKDSEEAEEAELYQDLYCPACDKSFKTEKAMKNHEKSKKH 338
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  339 REMVALLKQQLEEEEEQF-SGVQMDENVLNANSEEEMEDTPKQKLSKKQKKKKQKSAQNFDDNFNENGTEEGGKIAPEKT 417
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 190194391  418 KSNEDNAKELENRPQENTCITETTEACEDPKSEAKSVPKSKGKKTKDVKKSVKA 471
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA 1427
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 2-66 8.43e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 114.47  E-value: 8.43e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK10767   4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 3-66 1.69e-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: 1.69e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190194391    3 CHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 5-108 1.35e-26

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: 110.77  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391    5 YEALGVRRDASEEELKKAYRKLALRWHPDKNLDnaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLDGEYQDD 84
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGGGF 80

                          90       100
                  ....*....|....*....|....
gi 190194391   85 SldllhYFTVTCYSGYGDDERGFY 108
Cdd:TIGR02349  81 N-----GFDIGFFGDFGDIFGDFF 99
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-73 8.12e-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: 97.08  E-value: 8.12e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL 73
Cdd:COG0484    2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAE 70
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-60 9.96e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 91.14  E-value: 9.96e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 190194391     2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQ 60
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPE 59
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 3-58 1.00e-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: 88.37  E-value: 1.00e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 190194391   3 CHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSD 58
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 4-267 2.51e-13

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 71.60  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGV---RRDASEEELKKAYRKLALRWHPDKNLDNAA-EAAEQFKLIQAAYDVLSDPQERAWYDNHREallkgglDG 79
Cdd:COG5269   45 LYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNkGCDEFFKLIQKAREVLGDRKLRLQYDSNDF-------DA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  80 EYQDDSLdllhyftvtcysgYGDDErgFYAVYRVVFELIAKEELEcmsegdvEDFPTFGDSQSDYDTVvHPFYAHWQSFC 159
Cdd:COG5269  118 DVPPPRI-------------YTPDE--FFEVWEPVFEREARFSKK-------QPVPSLGPSDSSLKEV-EEFYEFWSNFD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391 160 TQKNFSWKEEYDTRQASNRWEKRAMEKENKKIRDRARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQnAEKARKAEEMR 239
Cdd:COG5269  175 SWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ-EKEMKKIRKWE 249

                        250       260
                 ....*....|....*....|....*...
gi 190194391 240 RQQKLKQAKLAEQYREQSWMTMANLEKE 267
Cdd:COG5269  250 REAGARLKALAALKGKAEAKNKAEIEAE 277
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 314-339 2.28e-09

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: 52.56  E-value: 2.28e-09
                          10        20
                  ....*....|....*....|....*.
gi 190194391  314 LYCPACDKSFKTEKAMKNHEKSKKHR 339
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 313-343 1.65e-06

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: 44.55  E-value: 1.65e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 190194391   313 DLYCPACDKSFKTEKAMKNHEKSKKHREMVA 343
Cdd:smart00451   3 GFYCKLCNVTFTDEISVEAHLKGKKHKKNVK 33
PTZ00121 PTZ00121
MAEBL; Provisional
 181-471 3.64e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  181 KRAMEKENKKIRDRARKEKNELVRQLVAFIRKRD--KRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLAEQYREQSW 258
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK 1213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  259 MTMANLEKELQEMEARYEKEFGDGSDENEVEDQEPRNGLDGKDSEEAEEAELYQDLYCPACDKSFKTEKAMKNHEKSKKH 338
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  339 REMVALLKQQLEEEEEQF-SGVQMDENVLNANSEEEMEDTPKQKLSKKQKKKKQKSAQNFDDNFNENGTEEGGKIAPEKT 417
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 190194391  418 KSNEDNAKELENRPQENTCITETTEACEDPKSEAKSVPKSKGKKTKDVKKSVKA 471
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA 1427
PTZ00121 PTZ00121
MAEBL; Provisional
 167-340 2.48e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  167 KEEYDTRQASNRWEKRAMEKENKKIRDRARKEKNELVRQLVAFiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ 246
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  247 AKLAEQYR---------EQSWMTMANLEKELQEMEARYEKEFGDGSDENEVEDQEPRNGLDGKDSEE-----AEEAELYQ 312
Cdd:PTZ00121 1640 KKEAEEKKkaeelkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAE 1719

                         170       180
                  ....*....|....*....|....*...
gi 190194391  313 DLYCPACDKSFKTEKAMKNHEKSKKHRE 340
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 2-66 8.43e-28

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 114.47  E-value: 8.43e-28
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK10767   4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYD 67
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 3-66 1.69e-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: 1.69e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190194391    3 CHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 5-108 1.35e-26

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: 110.77  E-value: 1.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391    5 YEALGVRRDASEEELKKAYRKLALRWHPDKNLDnaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLDGEYQDD 84
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGGGF 80

                          90       100
                  ....*....|....*....|....
gi 190194391   85 SldllhYFTVTCYSGYGDDERGFY 108
Cdd:TIGR02349  81 N-----GFDIGFFGDFGDIFGDFF 99
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-73 8.12e-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: 97.08  E-value: 8.12e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL 73
Cdd:COG0484    2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAE 70
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-60 9.96e-23

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 91.14  E-value: 9.96e-23
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 190194391     2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQ 60
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPE 59
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 4-102 1.51e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 99.54  E-value: 1.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREAllkgGLDGEYQD 83
Cdd:PRK14298   7 YYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAE--EKFKEISEAYAVLSDAEKRAQYDRFGHA----GIDNQYSA 80

                         90
                 ....*....|....*....
gi 190194391  84 DSLdllhyFTVTCYSGYGD 102
Cdd:PRK14298  81 EDI-----FRGADFGGFGD 94
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 2-66 5.49e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 97.56  E-value: 5.49e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14282   4 KDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYD 68
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 3-58 1.00e-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: 88.37  E-value: 1.00e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 190194391   3 CHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSD 58
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
PRK14293 PRK14293
molecular chaperone DnaJ;
1-76 1.53e-21

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 96.21  E-value: 1.53e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190194391   1 MKCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGG 76
Cdd:PRK14293   2 AADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAE--DRFKEINRAYEVLSDPETRARYDQFGEAGVSGA 75
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 5-79 3.40e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 95.54  E-value: 3.40e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   5 YEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLDG 79
Cdd:PRK14276   7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAE--EKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFGG 79
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 2-92 6.56e-21

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 94.42  E-value: 6.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLDGEY 81
Cdd:PRK14301   4 RDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN-PEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVNGNGGFGG 82

                         90
                 ....*....|.
gi 190194391  82 QDDSLDLLHYF 92
Cdd:PRK14301  83 FSSAEDIFSHF 93
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
4-66 6.97e-21

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 87.08  E-value: 6.97e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:COG2214    7 HYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 2-75 1.32e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 93.29  E-value: 1.32e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKG 75
Cdd:PRK14294   4 RDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGD-KEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSG 76
PRK14279 PRK14279
molecular chaperone DnaJ;
2-83 3.55e-20

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 92.49  E-value: 3.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAeAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLDGEY 81
Cdd:PRK14279   9 KDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPA-AEERFKAVSEAHDVLSDPAKRKEYDETRRLFAGGGFGGRR 87


                 ..
gi 190194391  82 QD 83
Cdd:PRK14279  88 FD 89
PRK14297 PRK14297
molecular chaperone DnaJ;
2-76 4.44e-20

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 92.15  E-value: 4.44e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGG 76
Cdd:PRK14297   4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGN-KEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNGA 77
PRK14295 PRK14295
molecular chaperone DnaJ;
2-76 5.53e-20

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 91.83  E-value: 5.53e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAeAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGG 76
Cdd:PRK14295   9 KDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAK-AEERFKEISEAYDVLSDEKKRKEYDEARSLFGNGG 82
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 4-66 7.62e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 91.27  E-value: 7.62e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaaEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14278   5 YYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDE--EAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 2-66 3.27e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 89.22  E-value: 3.27e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14290   3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 2-66 3.60e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 89.47  E-value: 3.60e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14277   5 KDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGD-KEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14280 PRK14280
molecular chaperone DnaJ;
4-66 4.51e-19

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 89.01  E-value: 4.51e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14280   6 YYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN--KEEGADEKFKEISEAYEVLSDDQKRAQYD 66
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 2-83 5.17e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 89.06  E-value: 5.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLdGEY 81
Cdd:PRK14291   3 KDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAE--EKFKEINEAYQVLSDPEKRKLYDQFGHAAFSGSG-QQQ 79


                 ..
gi 190194391  82 QD 83
Cdd:PRK14291  80 QG 81
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 4-66 2.94e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 86.79  E-value: 2.94e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14281   5 YYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDN-KEAEEHFKEVNEAYEVLSNDDKRRRYD 66
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 5-63 3.01e-18

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 78.50  E-value: 3.01e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 190194391   5 YEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAeAAEQFKLIQAAYDVLSDPQERA 63
Cdd:COG5407    3 YEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPK-AEERFKEINEAYELLSDAEKRA 60
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 2-79 5.59e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 85.81  E-value: 5.59e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLDG 79
Cdd:PRK14286   4 RSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGN-KESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGG 80
PRK14289 PRK14289
molecular chaperone DnaJ;
4-80 7.34e-18

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 85.65  E-value: 7.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNlDNAAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK-----GGLD 78
Cdd:PRK14289   7 YYEVLGVSKTATVDEIKKAYRKKAIQYHPDKN-PGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGgaaggGGFS 85


                 ..
gi 190194391  79 GE 80
Cdd:PRK14289  86 GE 87
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 2-79 1.00e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 83.83  E-value: 1.00e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLDG 79
Cdd:PRK14299   4 KDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAE--EKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQG 79
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 4-84 2.28e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 83.72  E-value: 2.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaaEAAEQFKLIQAAYDVLSDPQERAWYDNHREAllkgGLDGEYQD 83
Cdd:PRK14283   7 YYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEE--GAEEKFKEISEAYAVLSDDEKRQRYDQFGHA----GMDGFSQE 80


                 .
gi 190194391  84 D 84
Cdd:PRK14283  81 D 81
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 4-75 4.25e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 83.35  E-value: 4.25e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNH-REALLKG 75
Cdd:PRK14284   3 YYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGD-AEAEKRFKEVSEAYEVLSDAQKRESYDRYgKDGPFAG 74
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 4-80 4.30e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 83.01  E-value: 4.30e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDnaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLDGE 80
Cdd:PRK14292   4 YYELLGVSRTASADEIKSAYRKLALKYHPDRNKE--KGAAEKFAQINEAYAVLSDAEKRAHYDRFGTAPGAGMPGGD 78
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 5-89 1.56e-16

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 81.79  E-value: 1.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   5 YEALGVRRDASEEELKKAYRKLALRWHPDKNLDnaaeaAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGLDGEYQDD 84
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD-----PEKFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQPADASD 105


                 ....*
gi 190194391  85 SLDLL 89
Cdd:PTZ00037 106 LFDLI 110
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 4-66 3.77e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 76.97  E-value: 3.77e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14287   6 YYEVLGVDRNASVDEVKKAYRKLARKYHPDVN--KAPDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 4-76 9.22e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 75.80  E-value: 9.22e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGG 76
Cdd:PRK14285   5 YYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGN-KEAESIFKEATEAYEVLIDDNKRAQYDRFGHTAFEGG 76
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 4-92 1.29e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 72.35  E-value: 1.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYD-------NHREALLKGG 76
Cdd:PRK14300   5 YYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQKRAAYDrfghdafQNQQSRGGGG 82

                         90
                 ....*....|....*.
gi 190194391  77 LDGEYQDDSLDLLHYF 92
Cdd:PRK14300  83 NHGGFHPDINDIFGDF 98
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 4-267 2.51e-13

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 71.60  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGV---RRDASEEELKKAYRKLALRWHPDKNLDNAA-EAAEQFKLIQAAYDVLSDPQERAWYDNHREallkgglDG 79
Cdd:COG5269   45 LYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNkGCDEFFKLIQKAREVLGDRKLRLQYDSNDF-------DA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  80 EYQDDSLdllhyftvtcysgYGDDErgFYAVYRVVFELIAKEELEcmsegdvEDFPTFGDSQSDYDTVvHPFYAHWQSFC 159
Cdd:COG5269  118 DVPPPRI-------------YTPDE--FFEVWEPVFEREARFSKK-------QPVPSLGPSDSSLKEV-EEFYEFWSNFD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391 160 TQKNFSWKEEYDTRQASNRWEKRAMEKENKKIRDRARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQnAEKARKAEEMR 239
Cdd:COG5269  175 SWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ-EKEMKKIRKWE 249

                        250       260
                 ....*....|....*....|....*...
gi 190194391 240 RQQKLKQAKLAEQYREQSWMTMANLEKE 267
Cdd:COG5269  250 REAGARLKALAALKGKAEAKNKAEIEAE 277
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1-60 1.13e-11

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 60.58  E-value: 1.13e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190194391   1 MKCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAE-----AAEQFKLIQAAYDVLSDPQ 60
Cdd:COG1076    3 LDDAFELLGLPPDADDAELKRAYRKLQREHHPDRLAAGLPEeeqrlALQKAAAINEAYETLKDPR 67
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 2-75 2.07e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 65.74  E-value: 2.07e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 190194391   2 KCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKG 75
Cdd:PRK14296   4 KDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAH--DKMVEINEAADVLLDKDKRKQYDQFGHAAFDG 75
PRK10266 PRK10266
curved DNA-binding protein;
1-70 3.77e-11

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 64.07  E-value: 3.77e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   1 MKCHYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNAAEAaeQFKLIQAAYDVLSDPQERAWYDNHRE 70
Cdd:PRK10266   3 LKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEA--RFKEVAEAWEVLSDEQRRAEYDQLWQ 70
PRK14288 PRK14288
molecular chaperone DnaJ;
4-92 5.31e-11

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 64.33  E-value: 5.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391   4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK--GGLDGEY 81
Cdd:PRK14288   5 YYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGD-KEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNqaGASQSDF 83

                         90
                 ....*....|.
gi 190194391  82 QDDSLDLLHYF 92
Cdd:PRK14288  84 SDFFEDLGSFF 94
zf-C2H2_jaz pfam12171
Zinc-finger double-stranded RNA-binding; This domain family is found in archaea and eukaryotes, ...
 314-339 2.28e-09

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: 52.56  E-value: 2.28e-09
                          10        20
                  ....*....|....*....|....*.
gi 190194391  314 LYCPACDKSFKTEKAMKNHEKSKKHR 339
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
djlA PRK09430
co-chaperone DjlA;
5-56 1.72e-07

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 52.51  E-value: 1.72e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190194391   5 YEALGVRRDASEEELKKAYRKLALRWHPDK-----------NLdnAAEAAEQfklIQAAYDVL 56
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDKlvakglppemmEM--AKEKAQE---IQAAYELI 260
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 313-343 1.65e-06

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: 44.55  E-value: 1.65e-06
                           10        20        30
                   ....*....|....*....|....*....|.
gi 190194391   313 DLYCPACDKSFKTEKAMKNHEKSKKHREMVA 343
Cdd:smart00451   3 GFYCKLCNVTFTDEISVEAHLKGKKHKKNVK 33
zf-met pfam12874
Zinc-finger of C2H2 type; This is a zinc-finger domain with the CxxCx(12)Hx(6)H motif, found ...
 314-338 1.92e-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: 1.92e-06
                          10        20
                  ....*....|....*....|....*
gi 190194391  314 LYCPACDKSFKTEKAMKNHEKSKKH 338
Cdd:pfam12874   1 FYCELCNVTFNSESQLKSHLQGKKH 25
PTZ00121 PTZ00121
MAEBL; Provisional
 181-471 3.64e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.59  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  181 KRAMEKENKKIRDRARKEKNELVRQLVAFIRKRD--KRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLAEQYREQSW 258
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK 1213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  259 MTMANLEKELQEMEARYEKEFGDGSDENEVEDQEPRNGLDGKDSEEAEEAELYQDLYCPACDKSFKTEKAMKNHEKSKKH 338
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  339 REMVALLKQQLEEEEEQF-SGVQMDENVLNANSEEEMEDTPKQKLSKKQKKKKQKSAQNFDDNFNENGTEEGGKIAPEKT 417
Cdd:PTZ00121 1294 EAKKAEEKKKADEAKKKAeEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK 1373

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 190194391  418 KSNEDNAKELENRPQENTCITETTEACEDPKSEAKSVPKSKGKKTKDVKKSVKA 471
Cdd:PTZ00121 1374 EEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKA 1427
PTZ00121 PTZ00121
MAEBL; Provisional
 167-340 2.48e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  167 KEEYDTRQASNRWEKRAMEKENKKIRDRARKEKNELVRQLVAFiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ 246
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  247 AKLAEQYR---------EQSWMTMANLEKELQEMEARYEKEFGDGSDENEVEDQEPRNGLDGKDSEE-----AEEAELYQ 312
Cdd:PTZ00121 1640 KKEAEEKKkaeelkkaeEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAE 1719

                         170       180
                  ....*....|....*....|....*...
gi 190194391  313 DLYCPACDKSFKTEKAMKNHEKSKKHRE 340
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 4-79 3.71e-03

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 40.15  E-value: 3.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190194391    4 HYEALGVRRDASEEELKKAYRKLALRWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYDnhreallKGGLDG 79
Cdd:PTZ00341  575 FYDILGVGVNADMKEISERYFKLAENYYPPKR--SGNEGFHKFKKINEAYQILGDIDKKKMYN-------KFGYDG 641
PTZ00121 PTZ00121
MAEBL; Provisional
 167-471 8.48e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 8.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  167 KEEYDTRQASNRWEKRAMEKENKKIRDRARKEKNELvrqlvafirkrDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ 246
Cdd:PTZ00121 1467 EEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEA-----------KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKK 1535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  247 AKLAEQYREQSWMTMANLEKELQEMEARYEKEfgdgsdenEVEDQEPRNGLDGKDSEEA---EEAELYQDLYCPACDKSF 323
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKKAEEKKKAE--------EAKKAEEDKNMALRKAEEAkkaEEARIEEVMKLYEEEKKM 1607

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190194391  324 KTEKAMKNHEKSKKHREMVALLKQQLEEEEEQFSGVQMDENVLNANSEEEMEDTPKQKLSKKQkkkkqksaqnfddnfne 403
Cdd:PTZ00121 1608 KAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA----------------- 1670

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190194391  404 ngtEEGGKIAPEKTKSNEDNAKELENRPQENtciTETTEACEDPKSEAKSVPKSKGKKTKDVKKSVKA 471
Cdd:PTZ00121 1671 ---EEDKKKAEEAKKAEEDEKKAAEALKKEA---EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKA 1732
 
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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