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Conserved domains on  [gi|16197949|gb|AAL13745|]
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LD21896p [Drosophila melanogaster]

Protein Classification

J domain-containing protein( domain architecture ID 11155597)

J domain-containing protein similar to Drosophila melanogaster wurst that is essential for airway clearance and respiratory-tube size control

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  35729039|9644977|8016869|15170475|9585179|10542335|19372762
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 331-393 7.67e-21

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: 85.22  E-value: 7.67e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16197949   331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIKsnRRR 393
Cdd:pfam00226   3 YEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD---PEAEEKFKEINEAYEVLSDPE--KRA 60
TM2 pfam05154
TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a ...
 47-97 2.24e-11

TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a short linker. The function of this domain is unknown, however it occurs in a wide range or protein contexts.


:

Pssm-ID: 428337  Cd Length: 50  Bit Score: 58.27  E-value: 2.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16197949    47 PQKSVVIAYLCWLFGGIFGLHHLYLHRDRHAFIWWCTLGGyMGIGWMGELF 97
Cdd:pfam05154   1 SGKSKLIAYLLWLFLGGFGVHRFYLGKTGTGILYLLTFGG-LGIWWLIDLI 50
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 331-393 7.67e-21

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: 85.22  E-value: 7.67e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16197949   331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIKsnRRR 393
Cdd:pfam00226   3 YEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD---PEAEEKFKEINEAYEVLSDPE--KRA 60
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 331-402 7.98e-21

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: 87.84  E-value: 7.98e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949 331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIKsnRRRKNKQYQEEE 402
Cdd:COG0484   3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD---PEAEEKFKEINEAYEVLSDPE--KRAAYDRFGHAA 69
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 329-385 3.56e-20

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 83.36  E-value: 3.56e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16197949 329 NSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDeglRAQAHQRFIEIQQAYSVLS 385
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPD---DPEAEEKFKEINEAYEVLS 54
DnaJ smart00271
DnaJ molecular chaperone homology domain;
331-389 1.78e-19

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 81.51  E-value: 1.78e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16197949    331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglRAQAHQRFIEIQQAYSVLSKIKS 389
Cdd:smart00271   4 YEILGVPRDASLDEIKKAYRKLALKYHPDKNPGD--KEEAEEKFKEINEAYEVLSDPEK 60
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 331-385 1.05e-17

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: 83.80  E-value: 1.05e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16197949   331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDeglrAQAHQRFIEIQQAYSVLS 385
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD----KEAEEKFKEINEAYEVLS 53
PRK14295 PRK14295
molecular chaperone DnaJ;
327-404 1.82e-17

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 83.36  E-value: 1.82e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIKsnrrrKNKQYQEEEAI 404
Cdd:PRK14295   8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGD---AKAEERFKEISEAYDVLSDEK-----KRKEYDEARSL 77
TM2 pfam05154
TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a ...
 47-97 2.24e-11

TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a short linker. The function of this domain is unknown, however it occurs in a wide range or protein contexts.


Pssm-ID: 428337  Cd Length: 50  Bit Score: 58.27  E-value: 2.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16197949    47 PQKSVVIAYLCWLFGGIFGLHHLYLHRDRHAFIWWCTLGGyMGIGWMGELF 97
Cdd:pfam05154   1 SGKSKLIAYLLWLFLGGFGVHRFYLGKTGTGILYLLTFGG-LGIWWLIDLI 50
TM2 COG2314
Uncharacterized membrane protein YozV, TM2 domain, contains pTyr [General function prediction ...
 42-100 7.26e-09

Uncharacterized membrane protein YozV, TM2 domain, contains pTyr [General function prediction only];


Pssm-ID: 441888  Cd Length: 79  Bit Score: 52.22  E-value: 7.26e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16197949  42 MNALPPQKSVVIAYLCWLFGGIFGLHHLYLHRDRHAFIWWCTLG-GYMGIGWMGELFLIP 100
Cdd:COG2314   1 AELPKSEKSKLVAGLLAIFLGGFGIHRFYLGKTGTGIIYLLFFWtGIPGIIGLIDGILYL 60
PHA01886 PHA01886
TM2 domain-containing protein
 49-107 1.08e-05

TM2 domain-containing protein


Pssm-ID: 222840  Cd Length: 78  Bit Score: 43.42  E-value: 1.08e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16197949   49 KSVVIAYLCWLFGGIFGLHHLYLHRDRHAFIWWCTlGGYMGIGWMGELFLIPEYVRDAN 107
Cdd:PHA01886   2 KSTAIAYVLWFFLGFFGIHRFYTGNIATGIIWLFT-GGLFGIGWFIDLFLTAGLVQSSN 59
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 331-393 7.67e-21

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: 85.22  E-value: 7.67e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16197949   331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIKsnRRR 393
Cdd:pfam00226   3 YEILGVSPDASDEEIKKAYRKLALKYHPDKNPGD---PEAEEKFKEINEAYEVLSDPE--KRA 60
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 331-402 7.98e-21

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: 87.84  E-value: 7.98e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949 331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIKsnRRRKNKQYQEEE 402
Cdd:COG0484   3 YEILGVSRDASAEEIKKAYRKLAKKYHPDRNPGD---PEAEEKFKEINEAYEVLSDPE--KRAAYDRFGHAA 69
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 329-385 3.56e-20

DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonine family. Hsp40 proteins are characterized by the presence of a J domain, which mediates the interaction with Hsp70. They may contain other domains as well, and the architectures provide a means of classification.


Pssm-ID: 99751 [Multi-domain]  Cd Length: 55  Bit Score: 83.36  E-value: 3.56e-20
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 16197949 329 NSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDeglRAQAHQRFIEIQQAYSVLS 385
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPD---DPEAEEKFKEINEAYEVLS 54
DnaJ smart00271
DnaJ molecular chaperone homology domain;
331-389 1.78e-19

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 81.51  E-value: 1.78e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 16197949    331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglRAQAHQRFIEIQQAYSVLSKIKS 389
Cdd:smart00271   4 YEILGVPRDASLDEIKKAYRKLALKYHPDKNPGD--KEEAEEKFKEINEAYEVLSDPEK 60
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 329-392 3.23e-18

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 78.12  E-value: 3.23e-18
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16197949 329 NSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDeglRAQAHQRFIEIQQAYSVLSKIKSNRR 392
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKG---DPKAEERFKEINEAYELLSDAEKRAR 61
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 331-385 1.05e-17

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: 83.80  E-value: 1.05e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 16197949   331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDeglrAQAHQRFIEIQQAYSVLS 385
Cdd:TIGR02349   3 YEILGVSKDASEEEIKKAYRKLAKKYHPDRNKD----KEAEEKFKEINEAYEVLS 53
PRK14295 PRK14295
molecular chaperone DnaJ;
327-404 1.82e-17

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 83.36  E-value: 1.82e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIKsnrrrKNKQYQEEEAI 404
Cdd:PRK14295   8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKGD---AKAEERFKEISEAYDVLSDEK-----KRKEYDEARSL 77
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
331-393 2.78e-16

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 73.60  E-value: 2.78e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16197949 331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglRAQAHQRFIEIQQAYSVLSkiKSNRRR 393
Cdd:COG2214   8 YAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGEL--KALAEELFQRLNEAYEVLS--DPERRA 66
PRK14280 PRK14280
molecular chaperone DnaJ;
328-398 9.87e-16

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 78.22  E-value: 9.87e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16197949  328 RNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlraqAHQRFIEIQQAYSVLSkiKSNRRRKNKQY 398
Cdd:PRK14280   4 RDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEG----ADEKFKEISEAYEVLS--DDQKRAQYDQF 68
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
326-386 1.67e-15

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 70.98  E-value: 1.67e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16197949 326 GERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKV---KDEGLRAQAHQRFIEIQQAYSVLSK 386
Cdd:COG1076   2 QLDDAFELLGLPPDADDAELKRAYRKLQREHHPDRLaagLPEEEQRLALQKAAAINEAYETLKD 65
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 327-398 3.04e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 76.67  E-value: 3.04e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlraqAHQRFIEIQQAYSVLSkiKSNRRRKNKQY 398
Cdd:PRK14276   3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPG----AEEKYKEVQEAYETLS--DPQKRAAYDQY 68
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 327-385 2.78e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 73.64  E-value: 2.78e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLS 385
Cdd:PRK10767   3 KRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPGD---KEAEEKFKEIKEAYEVLS 58
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 327-401 1.88e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 71.34  E-value: 1.88e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlraqAHQRFIEIQQAYSVLSkiKSNRRRKNKQYQEE 401
Cdd:PRK14291   2 KKDYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPE----AEEKFKEINEAYQVLS--DPEKRKLYDQFGHA 70
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 331-385 2.25e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 70.98  E-value: 2.25e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16197949  331 YKVLGVSATASQAEITAAYRKLSKEYHPDkvKDEGLRAQAHQRFIEIQQAYSVLS 385
Cdd:PRK14282   7 YEILGVSRNATQEEIKRAYKRLVKEWHPD--RHPENRKEAEQKFKEIQEAYEVLS 59
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 327-398 2.30e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 70.75  E-value: 2.30e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlraqAHQRFIEIQQAYSVLskIKSNRRRKNKQY 398
Cdd:PRK14296   3 KKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPD----AHDKMVEINEAADVL--LDKDKRKQYDQF 68
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 328-385 2.38e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 70.85  E-value: 2.38e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16197949  328 RNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlrAQAhqRFIEIQQAYSVLS 385
Cdd:PRK14278   3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEE--AQE--KFKEISVAYEVLS 56
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 328-385 3.98e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 70.26  E-value: 3.98e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16197949  328 RNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlraqAHQRFIEIQQAYSVLS 385
Cdd:PRK14298   5 RDYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPD----AEEKFKEISEAYAVLS 58
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 327-398 1.19e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 68.68  E-value: 1.19e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSkiKSNRRRKNKQY 398
Cdd:PRK14281   2 KRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDN---KEAEEHFKEVNEAYEVLS--NDDKRRRYDQF 68
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 331-385 1.67e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 68.38  E-value: 1.67e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16197949  331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlraqAHQRFIEIQQAYSVLS 385
Cdd:PRK14292   5 YELLGVSRTASADEIKSAYRKLALKYHPDRNKEKG----AAEKFAQINEAYAVLS 55
PRK14279 PRK14279
molecular chaperone DnaJ;
327-400 1.85e-12

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 68.22  E-value: 1.85e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIKsnrrrKNKQYQE 400
Cdd:PRK14279   8 EKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPGD---PAAEERFKAVSEAHDVLSDPA-----KRKEYDE 73
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 327-392 2.32e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 67.93  E-value: 2.32e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlraqAHQRFIEIQQAYSVLSKIKSNRR 392
Cdd:PRK14283   4 KRDYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEG----AEEKFKEISEAYAVLSDDEKRQR 65
djlA PRK09430
co-chaperone DjlA;
331-394 4.32e-12

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 65.99  E-value: 4.32e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16197949  331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGLRAQ----AHQRFIEIQQAYSVlskIKSNRRRK 394
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDKLVAKGLPPEmmemAKEKAQEIQAAYEL---IKKQKGFK 267
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 328-403 4.84e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 66.12  E-value: 4.84e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16197949  328 RNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlraqAHQRFIEIQQAYSVLSkiKSNRRRKNKQYQEEEA 403
Cdd:PRK14299   4 KDYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPG----AEEKFKEINEAYTVLS--DPEKRRIYDTYGTTAA 73
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 326-398 7.04e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 66.36  E-value: 7.04e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16197949  326 GERNSYKVLGVSATASQAEITAAYRKLSKEYHPDkvKDEGLRAqAHQRFIEIQQAYSVLSkiKSNRRRKNKQY 398
Cdd:PRK14277   3 AKKDYYEILGVDRNATEEEIKKAYRRLAKKYHPD--LNPGDKE-AEQKFKEINEAYEILS--DPQKRAQYDQF 70
PRK14293 PRK14293
molecular chaperone DnaJ;
328-385 1.49e-11

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 65.40  E-value: 1.49e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16197949  328 RNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEGlraqAHQRFIEIQQAYSVLS 385
Cdd:PRK14293   3 ADYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPG----AEDRFKEINRAYEVLS 56
TM2 pfam05154
TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a ...
 47-97 2.24e-11

TM2 domain; This family is composed of a pair of transmembrane alpha helices connected by a short linker. The function of this domain is unknown, however it occurs in a wide range or protein contexts.


Pssm-ID: 428337  Cd Length: 50  Bit Score: 58.27  E-value: 2.24e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 16197949    47 PQKSVVIAYLCWLFGGIFGLHHLYLHRDRHAFIWWCTLGGyMGIGWMGELF 97
Cdd:pfam05154   1 SGKSKLIAYLLWLFLGGFGVHRFYLGKTGTGILYLLTFGG-LGIWWLIDLI 50
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 331-385 4.00e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 64.09  E-value: 4.00e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16197949  331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLS 385
Cdd:PRK14284   4 YTILGVSKTASPEEIKKAYRKLAVKYHPDKNPGD---AEAEKRFKEVSEAYEVLS 55
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 327-384 5.38e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 63.61  E-value: 5.38e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVL 384
Cdd:PRK14301   3 QRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDN---PEAEQKFKEAAEAYEVL 57
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 327-398 1.98e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 61.93  E-value: 1.98e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIKsnRRRKNKQY 398
Cdd:PRK14286   3 ERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGN---KESEEKFKEATEAYEILRDPK--KRQAYDQF 69
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 328-400 2.11e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 61.87  E-value: 2.11e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16197949  328 RNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglRAQAHQRFIEIQQAYSVLSKiksnrRRKNKQYQE 400
Cdd:PRK14290   3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGN--KAEAEEKFKEISEAYEVLSD-----PQKRRQYDQ 68
PRK14289 PRK14289
molecular chaperone DnaJ;
327-398 4.01e-10

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 61.00  E-value: 4.01e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDkvKDEGLRaQAHQRFIEIQQAYSVLSKIksNRRRKNKQY 398
Cdd:PRK14289   4 KRDYYEVLGVSKTATVDEIKKAYRKKAIQYHPD--KNPGDK-EAEEKFKEAAEAYDVLSDP--DKRSRYDQF 70
PRK14297 PRK14297
molecular chaperone DnaJ;
328-385 4.03e-10

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 60.95  E-value: 4.03e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 16197949  328 RNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLS 385
Cdd:PRK14297   4 KDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKGN---KEAEEKFKEINEAYQVLS 58
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 328-393 6.65e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 60.41  E-value: 6.65e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16197949  328 RNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglraQAHQRFIEIQQAYSVLskiKSNRRR 393
Cdd:PRK14300   3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAK----DAEKKFKEINAAYDVL---KDEQKR 61
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 321-401 1.21e-09

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 59.83  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16197949  321 SMDVDGERnSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglraqahQRFIEIQQAYSVLSkiKSNRRRKNKQYQE 400
Cdd:PTZ00037  22 KREVDNEK-LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDP-------EKFKEISRAYEVLS--DPEKRKIYDEYGE 91


                 .
gi 16197949  401 E 401
Cdd:PTZ00037  92 E 92
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 326-401 3.08e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 58.24  E-value: 3.08e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16197949  326 GERNSYKVLGVSATASQAEITAAYRKLSKEYHPDkvKDEGLRaQAHQRFIEIQQAYSVLSKIKsnRRRKNKQYQEE 401
Cdd:PRK14294   2 VKRDYYEILGVTRDASEEEIKKSYRKLAMKYHPD--RNPGDK-EAEELFKEAAEAYEVLSDPK--KRGIYDQYGHE 72
TM2 COG2314
Uncharacterized membrane protein YozV, TM2 domain, contains pTyr [General function prediction ...
 42-100 7.26e-09

Uncharacterized membrane protein YozV, TM2 domain, contains pTyr [General function prediction only];


Pssm-ID: 441888  Cd Length: 79  Bit Score: 52.22  E-value: 7.26e-09
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16197949  42 MNALPPQKSVVIAYLCWLFGGIFGLHHLYLHRDRHAFIWWCTLG-GYMGIGWMGELFLIP 100
Cdd:COG2314   1 AELPKSEKSKLVAGLLAIFLGGFGIHRFYLGKTGTGIIYLLFFWtGIPGIIGLIDGILYL 60
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 327-385 8.62e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 56.94  E-value: 8.62e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglraQAHQRFIEIQQAYSVLS 385
Cdd:PRK14287   3 KRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAP----DAEDKFKEVKEAYDTLS 57
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 327-398 1.04e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 56.54  E-value: 1.04e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLskIKSNRRRKNKQY 398
Cdd:PRK14285   2 KRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGN---KEAESIFKEATEAYEVL--IDDNKRAQYDRF 68
PRK10266 PRK10266
curved DNA-binding protein;
331-392 2.64e-08

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 54.83  E-value: 2.64e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949  331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVKDeglrAQAHQRFIEIQQAYSVLSkiKSNRR 392
Cdd:PRK10266   7 YAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKE----PDAEARFKEVAEAWEVLS--DEQRR 62
PHA01886 PHA01886
TM2 domain-containing protein
 49-107 1.08e-05

TM2 domain-containing protein


Pssm-ID: 222840  Cd Length: 78  Bit Score: 43.42  E-value: 1.08e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 16197949   49 KSVVIAYLCWLFGGIFGLHHLYLHRDRHAFIWWCTlGGYMGIGWMGELFLIPEYVRDAN 107
Cdd:PHA01886   2 KSTAIAYVLWFFLGFFGIHRFYTGNIATGIIWLFT-GGLFGIGWFIDLFLTAGLVQSSN 59
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 331-396 4.95e-05

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 45.55  E-value: 4.95e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16197949   331 YKVLGVSATASQAEITAAYRKLSKEYHPDKVK-DEGLraqahQRFIEIQQAYSVLSKIkSNRRRKNK 396
Cdd:PTZ00341  576 YDILGVGVNADMKEISERYFKLAENYYPPKRSgNEGF-----HKFKKINEAYQILGDI-DKKKMYNK 636
PRK14288 PRK14288
molecular chaperone DnaJ;
327-388 1.49e-04

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 43.52  E-value: 1.49e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16197949  327 ERNSYKVLGVSATASQAEITAAYRKLSKEYHPDKVKDEglrAQAHQRFIEIQQAYSVLSKIK 388
Cdd:PRK14288   2 ELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAGD---KEAEEKFKLINEAYGVLSDEK 60
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 339-384 1.68e-03

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 38.71  E-value: 1.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 16197949   339 TASQAEITAAYRKLSKEYHPDKVKDEGLRAQAHQRFIEIQQAYSVL 384
Cdd:TIGR00714   2 QLDQSRLRKRYRQLQAQYHPDASGMAQEQLAASQQSTTLNQAYHTL 47
 
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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