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Conserved domains on  [gi|296434479|sp|Q5F1R6|]
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RecName: Full=DnaJ homolog subfamily C member 21; AltName: Full=DnaJ homolog subfamily A member 5; AltName: Full=Protein GS3

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
 2-79 4.21e-29

chaperone protein DnaJ; Provisional


The actual alignment was detected with superfamily member PRK10767:

Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 118.32  E-value: 4.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK-----GG 76
Cdd:PRK10767   4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEqggggGG 82


                 ...
gi 296434479  77 FDG 79
Cdd:PRK10767  83 FGG 85
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 4-267 1.42e-14

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: 75.45  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGV---RRDASEEELKKAYRKLALKWHPDKNLDNAA-EAAEQFKLIQAAYDVLSDPQERAWYDNHreallkgGFDG 79
Cdd:COG5269   45 LYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNkGCDEFFKLIQKAREVLGDRKLRLQYDSN-------DFDA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  80 EYQDDSLdllryftvtcysgYGDDEkgFYTVYRNVFEMIAKEELESVleeevddFPTFGDSQSDYDTVvHPFYAYWQSFC 159
Cdd:COG5269  118 DVPPPRI-------------YTPDE--FFEVWEPVFEREARFSKKQP-------VPSLGPSDSSLKEV-EEFYEFWSNFD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479 160 TQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQnAEKARKAEEMR 239
Cdd:COG5269  175 SWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ-EKEMKKIRKWE 249

                        250       260
                 ....*....|....*....|....*...
gi 296434479 240 RQQKLKQAKLVEQYREQSWMTMANLEKE 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 2.30e-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: 2.30e-09
                          10        20
                  ....*....|....*....|....*.
gi 296434479  314 LYCPACDKSFKTEKAMKNHEKSKKHR 339
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 2-79 4.21e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 118.32  E-value: 4.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK-----GG 76
Cdd:PRK10767   4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEqggggGG 82


                 ...
gi 296434479  77 FDG 79
Cdd:PRK10767  83 FGG 85
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 5-92 5.29e-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: 115.01  E-value: 5.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479    5 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDnaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEYQDD 84
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGGGF 80


                  ....*...
gi 296434479   85 SLDLLRYF 92
Cdd:TIGR02349  81 NGFDIGFF 88
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 3-66 2.81e-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: 104.09  E-value: 2.81e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296434479    3 CHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-73 4.25e-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: 97.85  E-value: 4.25e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL 73
Cdd:COG0484    2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAE 70
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-60 1.34e-22

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 90.76  E-value: 1.34e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 296434479     2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQ 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 2.55e-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: 87.22  E-value: 2.55e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296434479   3 CHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSD 58
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 4-267 1.42e-14

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 75.45  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGV---RRDASEEELKKAYRKLALKWHPDKNLDNAA-EAAEQFKLIQAAYDVLSDPQERAWYDNHreallkgGFDG 79
Cdd:COG5269   45 LYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNkGCDEFFKLIQKAREVLGDRKLRLQYDSN-------DFDA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  80 EYQDDSLdllryftvtcysgYGDDEkgFYTVYRNVFEMIAKEELESVleeevddFPTFGDSQSDYDTVvHPFYAYWQSFC 159
Cdd:COG5269  118 DVPPPRI-------------YTPDE--FFEVWEPVFEREARFSKKQP-------VPSLGPSDSSLKEV-EEFYEFWSNFD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479 160 TQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQnAEKARKAEEMR 239
Cdd:COG5269  175 SWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ-EKEMKKIRKWE 249

                        250       260
                 ....*....|....*....|....*...
gi 296434479 240 RQQKLKQAKLVEQYREQSWMTMANLEKE 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 2.30e-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: 2.30e-09
                          10        20
                  ....*....|....*....|....*.
gi 296434479  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 ...
 313-345 6.56e-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: 45.71  E-value: 6.56e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 296434479   313 DLYCPACDKSFKTEKAMKNHEKSKKHREMVALL 345
Cdd:smart00451   3 GFYCKLCNVTFTDEISVEAHLKGKKHKKNVKKR 35
PTZ00121 PTZ00121
MAEBL; Provisional
 167-349 3.51e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  167 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQlvafiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ 246
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  247 AKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKdsDEAEDAELYDDLYCPACDKSFKTE 326
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEA 1643

                         170       180
                  ....*....|....*....|...
gi 296434479  327 KAMKNHEKSKKHREMVALLKQQL 349
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEE 1666
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 180-298 1.76e-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: 40.67  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  180 EKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLVEQYREQswm 259
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--- 243

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 296434479  260 tMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEED 298
Cdd:pfam13868 244 -QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEA 281
 
Name Accession Description Interval E-value
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 2-79 4.21e-29

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 118.32  E-value: 4.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK-----GG 76
Cdd:PRK10767   4 RDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD-KEAEEKFKEIKEAYEVLSDPQKRAAYDQYGHAAFEqggggGG 82


                 ...
gi 296434479  77 FDG 79
Cdd:PRK10767  83 FGG 85
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 5-92 5.29e-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: 115.01  E-value: 5.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479    5 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDnaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEYQDD 84
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD--KEAEEKFKEINEAYEVLSDPEKRAQYDQFGHAGFNGGGGGGGGGF 80


                  ....*...
gi 296434479   85 SLDLLRYF 92
Cdd:TIGR02349  81 NGFDIGFF 88
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 3-66 2.81e-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: 104.09  E-value: 2.81e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296434479    3 CHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD-PEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 4-73 4.25e-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: 97.85  E-value: 4.25e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL 73
Cdd:COG0484    2 YYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD-PEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAE 70
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 4-118 4.07e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 101.08  E-value: 4.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREAllkgGFDGEYQD 83
Cdd:PRK14298   7 YYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAE--EKFKEISEAYAVLSDAEKRAQYDRFGHA----GIDNQYSA 80

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 296434479  84 DSLdllryFTVTCYSGYGDdekgfytvyrnVFEMI 118
Cdd:PRK14298  81 EDI-----FRGADFGGFGD-----------IFEMF 99
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 5-79 5.48e-23

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 100.93  E-value: 5.48e-23
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296434479   5 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 79
Cdd:PRK14276   7 YDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAE--EKYKEVQEAYETLSDPQKRAAYDQYGAAGANGGFGG 79
DnaJ smart00271
DnaJ molecular chaperone homology domain;
2-60 1.34e-22

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 90.76  E-value: 1.34e-22
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 296434479     2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQ 60
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGDKEEAEEKFKEINEAYEVLSDPE 59
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 2-66 2.26e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 98.71  E-value: 2.26e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14282   4 KDYYEILGVSRNATQEEIKRAYKRLVKEWHPDRHPENRKEAEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK14293 PRK14293
molecular chaperone DnaJ;
1-76 3.36e-22

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 98.14  E-value: 3.36e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296434479   1 MKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGG 76
Cdd:PRK14293   2 AADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAE--DRFKEINRAYEVLSDPETRARYDQFGEAGVSGA 75
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 2-79 6.76e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 97.14  E-value: 6.76e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKG-GFDG 79
Cdd:PRK14294   4 RDYYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPGD-KEAEELFKEAAEAYEVLSDPKKRGIYDQYGHEGLSGtGFSG 81
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 2-79 9.80e-22

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 97.12  E-value: 9.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL--KGGFDG 79
Cdd:PRK14301   4 RDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN-PEAEQKFKEAAEAYEVLRDAEKRARYDRFGHAGVngNGGFGG 82
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 3-58 2.55e-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: 87.22  E-value: 2.55e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 296434479   3 CHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSD 58
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDD-PEAEEKFKEINEAYEVLSD 55
PRK14279 PRK14279
molecular chaperone DnaJ;
2-83 2.61e-21

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 95.95  E-value: 2.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAeAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEY 81
Cdd:PRK14279   9 KDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGDPA-AEERFKAVSEAHDVLSDPAKRKEYDETRRLFAGGGFGGRR 87


                 ..
gi 296434479  82 QD 83
Cdd:PRK14279  88 FD 89
PRK14295 PRK14295
molecular chaperone DnaJ;
2-77 3.72e-21

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 95.30  E-value: 3.72e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAeAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGF 77
Cdd:PRK14295   9 KDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGDAK-AEERFKEISEAYDVLSDEKKRKEYDEARSLFGNGGF 83
PRK14297 PRK14297
molecular chaperone DnaJ;
2-79 4.98e-21

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 94.85  E-value: 4.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK--GGFDG 79
Cdd:PRK14297   4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGN-KEAEEKFKEINEAYQVLSDPQKKAQYDQFGTADFNgaGGFGS 82
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
4-66 5.25e-21

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 87.47  E-value: 5.25e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:COG2214    7 HYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKALAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14280 PRK14280
molecular chaperone DnaJ;
4-79 2.26e-20

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 92.86  E-value: 2.26e-20
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 79
Cdd:PRK14280   6 YYEVLGVSKSASKDEIKKAYRKLSKKYHPDIN--KEEGADEKFKEISEAYEVLSDDQKRAQYDQFGHAGPNQGFGG 79
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 4-66 2.37e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 92.81  E-value: 2.37e-20
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaaEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14278   5 YYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDE--EAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 2-79 8.18e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 91.40  E-value: 8.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALL------KG 75
Cdd:PRK14277   5 KDYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPGD-KEAEQKFKEINEAYEILSDPQKRAQYDQFGHAAFdpggfgQG 83


                 ....
gi 296434479  76 GFDG 79
Cdd:PRK14277  84 GFGQ 87
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 2-66 1.53e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 90.38  E-value: 1.53e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14290   3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGNKAEAEEKFKEISEAYEVLSDPQKRRQYD 67
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 2-83 1.67e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 90.21  E-value: 1.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREAllkgGFDGEY 81
Cdd:PRK14291   3 KDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAE--EKFKEINEAYQVLSDPEKRKLYDQFGHA----AFSGSG 76


                 ..
gi 296434479  82 QD 83
Cdd:PRK14291  77 QQ 78
PRK14289 PRK14289
molecular chaperone DnaJ;
4-80 5.19e-19

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 89.12  E-value: 5.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNlDNAAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK-----GGFD 78
Cdd:PRK14289   7 YYEVLGVSKTATVDEIKKAYRKKAIQYHPDKN-PGDKEAEEKFKEAAEAYDVLSDPDKRSRYDQFGHAGVGgaaggGGFS 85


                 ..
gi 296434479  79 GE 80
Cdd:PRK14289  86 GE 87
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 4-92 7.03e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 88.75  E-value: 7.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNH-REALLK--GGFDGE 80
Cdd:PRK14284   3 YYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGD-AEAEKRFKEVSEAYEVLSDAQKRESYDRYgKDGPFAgaGGFGGA 81

                         90
                 ....*....|..
gi 296434479  81 YQDDSLDLLRYF 92
Cdd:PRK14284  82 GMGNMEDALRTF 93
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 4-66 7.87e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 88.71  E-value: 7.87e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14281   5 YYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDN-KEAEEHFKEVNEAYEVLSNDDKRRRYD 66
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 5-63 1.18e-18

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 79.66  E-value: 1.18e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 296434479   5 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAeAAEQFKLIQAAYDVLSDPQERA 63
Cdd:COG5407    3 YEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDPK-AEERFKEINEAYELLSDAEKRA 60
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 2-79 1.96e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 86.97  E-value: 1.96e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 79
Cdd:PRK14286   4 RSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGN-KESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVNAGAGG 80
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 2-79 3.78e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 84.99  E-value: 3.78e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 79
Cdd:PRK14299   4 KDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAE--EKFKEINEAYTVLSDPEKRRIYDTYGTTAASAGWQG 79
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 4-66 7.61e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 85.33  E-value: 7.61e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDnaAEAAEQFKLIQAAYDVLSDPQERAWYD 66
Cdd:PRK14292   4 YYELLGVSRTASADEIKSAYRKLALKYHPDRNKE--KGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 4-117 9.30e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 85.26  E-value: 9.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaaEAAEQFKLIQAAYDVLSDPQERAWYDNHREAllkgGFDGEYQD 83
Cdd:PRK14283   7 YYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEE--GAEEKFKEISEAYAVLSDDEKRQRYDQFGHA----GMDGFSQE 80

                         90       100       110
                 ....*....|....*....|....*....|....
gi 296434479  84 DSLDLLRYFTVtcYSGYGDDekgfytvYRNVFEM 117
Cdd:PRK14283  81 DIFNNINFEDI--FQGFGFG-------IGNIFDM 105
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 5-89 6.74e-17

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 82.95  E-value: 6.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   5 YEALGVRRDASEEELKKAYRKLALKWHPDKNLDnaaeaAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDGEYQDD 84
Cdd:PTZ00037  31 YEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGD-----PEKFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQPADASD 105


                 ....*
gi 296434479  85 SLDLL 89
Cdd:PTZ00037 106 LFDLI 110
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 4-79 3.61e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 80.05  E-value: 3.61e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGGFDG 79
Cdd:PRK14287   6 YYEVLGVDRNASVDEVKKAYRKLARKYHPDVN--KAPDAEDKFKEVKEAYDTLSDPQKKAHYDQFGHTDPNQGFGG 79
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 4-79 3.39e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 77.34  E-value: 3.39e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLKGG--FDG 79
Cdd:PRK14285   5 YYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGN-KEAESIFKEATEAYEVLIDDNKRAQYDRFGHTAFEGGggFEG 81
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 4-267 1.42e-14

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 75.45  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGV---RRDASEEELKKAYRKLALKWHPDKNLDNAA-EAAEQFKLIQAAYDVLSDPQERAWYDNHreallkgGFDG 79
Cdd:COG5269   45 LYALLGLskyRTKAIPPQILKAHKKKVYKYHPDKTAAGGNkGCDEFFKLIQKAREVLGDRKLRLQYDSN-------DFDA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  80 EYQDDSLdllryftvtcysgYGDDEkgFYTVYRNVFEMIAKEELESVleeevddFPTFGDSQSDYDTVvHPFYAYWQSFC 159
Cdd:COG5269  118 DVPPPRI-------------YTPDE--FFEVWEPVFEREARFSKKQP-------VPSLGPSDSSLKEV-EEFYEFWSNFD 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479 160 TQKNFAWKEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVqahrKLVEEQnAEKARKAEEMR 239
Cdd:COG5269  175 SWRTFEPLDEDYPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRI----KSFKEQ-EKEMKKIRKWE 249

                        250       260
                 ....*....|....*....|....*...
gi 296434479 240 RQQKLKQAKLVEQYREQSWMTMANLEKE 267
Cdd:COG5269  250 REAGARLKALAALKGKAEAKNKAEIEAE 277
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 4-92 7.13e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 73.12  E-value: 7.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYD-------NHREALLKGG 76
Cdd:PRK14300   5 YYQILGVSKTASQADLKKAYLKLAKQYHPDTT--DAKDAEKKFKEINAAYDVLKDEQKRAAYDrfghdafQNQQSRGGGG 82

                         90
                 ....*....|....*.
gi 296434479  77 FDGEYQDDSLDLLRYF 92
Cdd:PRK14300  83 NHGGFHPDINDIFGDF 98
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 2-83 6.16e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 67.28  E-value: 6.16e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   2 KCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEaaEQFKLIQAAYDVLSDPQERAWYDNHREALLKG--GFDG 79
Cdd:PRK14296   4 KDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAH--DKMVEINEAADVLLDKDKRKQYDQFGHAAFDGssGFSS 81


                 ....
gi 296434479  80 EYQD 83
Cdd:PRK14296  82 NFGD 85
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
1-60 1.41e-11

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 60.20  E-value: 1.41e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296434479   1 MKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAE-----AAEQFKLIQAAYDVLSDPQ 60
Cdd:COG1076    3 LDDAFELLGLPPDADDAELKRAYRKLQREHHPDRLAAGLPEeeqrlALQKAAAINEAYETLKDPR 67
PRK10266 PRK10266
curved DNA-binding protein;
1-70 1.57e-11

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 65.23  E-value: 1.57e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   1 MKCHYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNAAEAaeQFKLIQAAYDVLSDPQERAWYDNHRE 70
Cdd:PRK10266   3 LKDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEA--RFKEVAEAWEVLSDEQRRAEYDQLWQ 70
PRK14288 PRK14288
molecular chaperone DnaJ;
4-92 2.25e-11

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 65.48  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479   4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNLDNaAEAAEQFKLIQAAYDVLSDPQERAWYDNHREALLK--GGFDGEY 81
Cdd:PRK14288   5 YYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGD-KEAEEKFKLINEAYGVLSDEKKRALYDRYGKKGLNqaGASQSDF 83

                         90
                 ....*....|.
gi 296434479  82 QDDSLDLLRYF 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 2.30e-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: 2.30e-09
                          10        20
                  ....*....|....*....|....*.
gi 296434479  314 LYCPACDKSFKTEKAMKNHEKSKKHR 339
Cdd:pfam12171   2 FYCVLCDKYFKSENALQNHLKSKKHK 27
djlA PRK09430
co-chaperone DjlA;
5-56 4.99e-07

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 51.35  E-value: 4.99e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296434479   5 YEALGVRRDASEEELKKAYRKLALKWHPDK-----------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 ...
 313-345 6.56e-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: 45.71  E-value: 6.56e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 296434479   313 DLYCPACDKSFKTEKAMKNHEKSKKHREMVALL 345
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 ...
 314-338 1.23e-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: 44.79  E-value: 1.23e-06
                          10        20
                  ....*....|....*....|....*
gi 296434479  314 LYCPACDKSFKTEKAMKNHEKSKKH 338
Cdd:pfam12874   1 FYCELCNVTFNSESQLKSHLQGKKH 25
PTZ00121 PTZ00121
MAEBL; Provisional
 167-349 3.51e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  167 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQlvafiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ 246
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK-----AEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKK 1565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  247 AKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKdsDEAEDAELYDDLYCPACDKSFKTE 326
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK--IKAEELKKAEEEKKKVEQLKKKEA 1643

                         170       180
                  ....*....|....*....|...
gi 296434479  327 KAMKNHEKSKKHREMVALLKQQL 349
Cdd:PTZ00121 1644 EEKKKAEELKKAEEENKIKAAEE 1666
PTZ00121 PTZ00121
MAEBL; Provisional
 167-340 6.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  167 KEEYDTRQASNRWEKRAMEKENKKIRDKARKEKNELVRQLVAFiRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQ----- 241
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEE-EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKveqlk 1639

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  242 ----QKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDE-----AEDAELYD 312
Cdd:PTZ00121 1640 kkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAE 1719

                         170       180
                  ....*....|....*....|....*...
gi 296434479  313 DLYCPACDKSFKTEKAMKNHEKSKKHRE 340
Cdd:PTZ00121 1720 ELKKAEEENKIKAEEAKKEAEEDKKKAE 1747
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 4-79 8.37e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 42.47  E-value: 8.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296434479    4 HYEALGVRRDASEEELKKAYRKLALKWHPDKNldNAAEAAEQFKLIQAAYDVLSDPQERAWYDnhreallKGGFDG 79
Cdd:PTZ00341  575 FYDILGVGVNADMKEISERYFKLAENYYPPKR--SGNEGFHKFKKINEAYQILGDIDKKKMYN-------KFGYDG 641
PTZ00121 PTZ00121
MAEBL; Provisional
 167-336 9.00e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 9.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  167 KEEYDTRQASNRWEKRAMEKENKKIRDKARK----EKNELVRQLVAFIRKRD-------KRVQAHRKLVEEQNAEKARKA 235
Cdd:PTZ00121 1099 KAEEAKKTETGKAEEARKAEEAKKKAEDARKaeeaRKAEDARKAEEARKAEDakrveiaRKAEDARKAEEARKAEDAKKA 1178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  236 EEMRRQQKLKQAKLVEQYREQSWMTMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDLY 315
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFE 1258

                         170       180
                  ....*....|....*....|.
gi 296434479  316 CPACDKSFKTEKAMKNHEKSK 336
Cdd:PTZ00121 1259 EARMAHFARRQAAIKAEEARK 1279
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 180-298 1.76e-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: 40.67  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  180 EKRAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQAKLVEQYREQswm 259
Cdd:pfam13868 167 REEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--- 243

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 296434479  260 tMANLEKELQEMEARYEKEFGDGSDENEMEEHELKDEED 298
Cdd:pfam13868 244 -QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEA 281
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 180-376 2.39e-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: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  180 EKRAMEKENK--KIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKL----KQAKLVEQY 253
Cdd:pfam17380 340 ERMAMEREREleRIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKIleeeRQRKIQQQK 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479  254 REQSWMTMANLEKELQEMEaRYEKEFGDGSDENEMEEHELKDEEDGKDSDEAEDAElyddlycpacdKSFKTEKAMKNHE 333
Cdd:pfam17380 420 VEMEQIRAEQEEARQREVR-RLEEERAREMERVRLEEQERQQQVERLRQQEEERKR-----------KKLELEKEKRDRK 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 296434479  334 KSKKHREMValLKQQLEEEEenfsRPQIDENPLDDNSEEEMED 376
Cdd:pfam17380 488 RAEEQRRKI--LEKELEERK----QAMIEEERKRKLLEKEMEE 524
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
182-314 4.79e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296434479 182 RAMEKENKKIRDKARKEKNELVRQLVAFIRKRDKRVQAHRKLVEEQNAEKARKAEEMRRQQKLKQ--AKLVEQYREQSWM 259
Cdd:PRK03918 506 KELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEelAELLKELEELGFE 585

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 296434479 260 TMANLEKELQEMEARYEK--EFGDGSDENEMEEHELKDEEDGKDSDEAEDAELYDDL 314
Cdd:PRK03918 586 SVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
 
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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