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Conserved domains on  [gi|94538370|ref|NP_055192|]
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dnaJ homolog subfamily C member 2 isoform 1 [Homo sapiens]

Protein Classification

DnaJ homolog subfamily C member 2( domain architecture ID 19233869)

DnaJ homolog subfamily C member 2 (DNAJC2) acts both as a chaperone in the cytosol and as a chromatin regulator in the nucleus

EC:  1.8.4.-
Gene Ontology:  GO:0006325|GO:0051083|GO:0006260|GO:2000279|GO:0045893
PubMed:  16952052

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-368 2.50e-66

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: 221.83  E-value: 2.50e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370  75 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269  31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 155 RAFNSVDptFDNSVPS-KSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 234 EKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAK---- 309
Cdd:COG5269 186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAAlkgk 265

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 310 -EKQRQAELEAARLAKEKEEEevrqqallaKKEKDIQKKAIKKERQKLRNSCKTWNHFSD 368
Cdd:COG5269 266 aEAKNKAEIEAEALASATAVK---------KKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
 344-420 2.89e-18

Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.


:

Pssm-ID: 435537  Cd Length: 87  Bit Score: 79.62  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   344 IQKKAIKKERQKLRNSCKTWNHFSDNEAERVKM----MEEVEKLCDRLELASLQCLNETLTSCT-KEVGKAALEKQIEEI 418
Cdd:pfam16717   1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80


                  ..
gi 94538370   419 NE 420
Cdd:pfam16717  81 VD 82
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 553-600 3.13e-10

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


:

Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 55.66  E-value: 3.13e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 94538370 553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELV 600
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-49 7.51e-04

N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, also known as DnaJ-related protein ZUO1, J protein ZUO1, or heat shock protein 40 homolog ZUO1, is a component of the ribosome-associated complex (RAC), which is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. The RAC chaperone complex plays a role in regulating accurate translation termination and folding or maintaining nascent polypeptides in a folding-competent state. The ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain is stimulated by the RAC chaperone complex. ZUO1 acts as a J-protein for SSB1/SSB2 only when it is associated with SSZ1. The N-terminal domain (NTD) of ZUO1 is responsible for its interaction with SSZ1, and it contains a conserved LP-motif that binds to the SSZ1 C-terminal SBD (substrate binding domain) beta-lid domain in the same way as canonical Hsp70s bind to their substrates.


:

Pssm-ID: 467935  Cd Length: 38  Bit Score: 37.48  E-value: 7.51e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 94538370  13 TAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASAS 49
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRTFS 38
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 453-506 1.28e-03

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


:

Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 36.78  E-value: 1.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 94538370 453 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 506
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-368 2.50e-66

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 221.83  E-value: 2.50e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370  75 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269  31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 155 RAFNSVDptFDNSVPS-KSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 234 EKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAK---- 309
Cdd:COG5269 186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAAlkgk 265

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 310 -EKQRQAELEAARLAKEKEEEevrqqallaKKEKDIQKKAIKKERQKLRNSCKTWNHFSD 368
Cdd:COG5269 266 aEAKNKAEIEAEALASATAVK---------KKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
 344-420 2.89e-18

Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.


Pssm-ID: 435537  Cd Length: 87  Bit Score: 79.62  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   344 IQKKAIKKERQKLRNSCKTWNHFSDNEAERVKM----MEEVEKLCDRLELASLQCLNETLTSCT-KEVGKAALEKQIEEI 418
Cdd:pfam16717   1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80


                  ..
gi 94538370   419 NE 420
Cdd:pfam16717  81 VD 82
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 88-158 2.97e-14

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: 67.50  E-value: 2.97e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94538370    88 DHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
87-153 9.39e-12

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 60.33  E-value: 9.39e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94538370     87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 153
Cdd:smart00271   1 TDYYEILGVPR---DASLDEIKKAYRKLALKYHPDKNPGD----KEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 88-150 1.30e-11

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: 59.87  E-value: 1.30e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538370  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257   1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-157 2.29e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 62.85  E-value: 2.29e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94538370   87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:PRK10767   4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 553-600 3.13e-10

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 55.66  E-value: 3.13e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 94538370 553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELV 600
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
551-602 1.31e-09

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 53.77  E-value: 1.31e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 94538370    551 FTPWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELVEM 602
Cdd:smart00717   1 KGEWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLKP 49
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 553-599 3.38e-08

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 49.81  E-value: 3.38e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 94538370   553 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMKRYKEL 599
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 306-436 4.88e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 4.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 306 QEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCD 385
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 94538370 386 RLELASLQCLNETLTSCTKEVGKAALEKQIEEINEQIRKEKEEAEARMRQA 436
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-49 7.51e-04

N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, also known as DnaJ-related protein ZUO1, J protein ZUO1, or heat shock protein 40 homolog ZUO1, is a component of the ribosome-associated complex (RAC), which is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. The RAC chaperone complex plays a role in regulating accurate translation termination and folding or maintaining nascent polypeptides in a folding-competent state. The ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain is stimulated by the RAC chaperone complex. ZUO1 acts as a J-protein for SSB1/SSB2 only when it is associated with SSZ1. The N-terminal domain (NTD) of ZUO1 is responsible for its interaction with SSZ1, and it contains a conserved LP-motif that binds to the SSZ1 C-terminal SBD (substrate binding domain) beta-lid domain in the same way as canonical Hsp70s bind to their substrates.


Pssm-ID: 467935  Cd Length: 38  Bit Score: 37.48  E-value: 7.51e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 94538370  13 TAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASAS 49
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRTFS 38
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 453-506 1.28e-03

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 36.78  E-value: 1.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 94538370 453 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 506
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
flgK PRK08471
flagellar hook-associated protein FlgK; Validated
 323-436 1.29e-03

flagellar hook-associated protein FlgK; Validated


Pssm-ID: 236270 [Multi-domain]  Cd Length: 613  Bit Score: 41.96  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370  323 AKEKEEEEVRQQAL--LAKKEKDIQKKAIKKERQKLRNScktWNHFSDN---EAERVKMMEEVEKLCDRLE-----LASL 392
Cdd:PRK08471  82 STELEYTDYEFSTLqeASQYFPDLDDTGILKDLQDYFNA---WNDFASNpkdSAQKQALAQKTETLTNNIKdtrerLDTL 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 94538370  393 Q-CLNETLTSCTKEVGKaaLEKQIEEINEQIrkEKEEAEARMRQA 436
Cdd:PRK08471 159 QkKVNEELKVTVDEINS--LGKQIAEINKQI--KEVEAGKTLKHA 199
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
452-508 3.31e-03

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 3.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 94538370    452 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSLQK 508
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-368 2.50e-66

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 221.83  E-value: 2.50e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370  75 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269  31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 155 RAFNSVDptFDNSVPS-KSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 234 EKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAK---- 309
Cdd:COG5269 186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAAlkgk 265

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 310 -EKQRQAELEAARLAKEKEEEevrqqallaKKEKDIQKKAIKKERQKLRNSCKTWNHFSD 368
Cdd:COG5269 266 aEAKNKAEIEAEALASATAVK---------KKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
 344-420 2.89e-18

Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.


Pssm-ID: 435537  Cd Length: 87  Bit Score: 79.62  E-value: 2.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   344 IQKKAIKKERQKLRNSCKTWNHFSDNEAERVKM----MEEVEKLCDRLELASLQCLNETLTSCT-KEVGKAALEKQIEEI 418
Cdd:pfam16717   1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80


                  ..
gi 94538370   419 NE 420
Cdd:pfam16717  81 VD 82
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 88-158 2.97e-14

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: 67.50  E-value: 2.97e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94538370    88 DHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
87-153 9.39e-12

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 60.33  E-value: 9.39e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94538370     87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 153
Cdd:smart00271   1 TDYYEILGVPR---DASLDEIKKAYRKLALKYHPDKNPGD----KEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 88-150 1.30e-11

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: 59.87  E-value: 1.30e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538370  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257   1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
87-157 2.32e-11

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 60.12  E-value: 2.32e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94538370  87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaaGEPIKEGDNDYFTCITKAYEMLSDPVKRRAF 157
Cdd:COG2214   5 KDHYAVLGVPP---DASLEEIRQAYRRLAKLLHPDR----GGELKALAEELFQRLNEAYEVLSDPERRAEY 68
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 88-157 3.46e-11

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: 61.26  E-value: 3.46e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538370  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:COG0484   1 DYYEILG---VSRDASAEEIKKAYRKLAKKYHPDRNpgdPEAEEKFKE--------INEAYEVLSDPEKRAAY 62
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-157 2.29e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 62.85  E-value: 2.29e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 94538370   87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:PRK10767   4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 87-209 2.49e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 62.50  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDK----RKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDP 162
Cdd:PRK14282   4 KDYYEILG---VSRNATQEEIKRAYKRLVKEWHPDRhpenRKEAEQKFKE--------IQEAYEVLSDPQKRAMYDRFGY 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94538370  163 TFDNSVPSKSEAKDNFFE-------------VFTPVFERNSRWSNKKNVPKLG-DMNSSFE 209
Cdd:PRK14282  73 VGEQPPYQETESGGGFFEdifkdfenifnrdIFDIFFGERRTQEEQREYARRGeDIRYEIE 133
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 553-600 3.13e-10

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 55.66  E-value: 3.13e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 94538370 553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELV 600
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
551-602 1.31e-09

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 53.77  E-value: 1.31e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 94538370    551 FTPWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELVEM 602
Cdd:smart00717   1 KGEWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLKP 49
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 87-217 8.98e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 57.86  E-value: 8.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSvdptF 164
Cdd:PRK14291   3 KDYYEILG---VSRNATQEEIKKAYRRLARKYHPDfnKNPEAEEKFKE--------INEAYQVLSDPEKRKLYDQ----F 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 94538370  165 DNSVPSKSEAKDNFFEVFTPVFERNsrwsnkknvpkLGDMnssFEDVDIFYSF 217
Cdd:PRK14291  68 GHAAFSGSGQQQQGQEGFSDFGGGN-----------IEDI---LEDVFDIFGF 106
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 87-159 2.29e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 55.72  E-value: 2.29e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94538370   87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRRAFNS 159
Cdd:PRK14299   4 KDYYAILG---VPKNASQDEIKKAFKKLARKYHPDVNKSPGaeEKFKE--------INEAYTVLSDPEKRRIYDT 67
PRK14295 PRK14295
molecular chaperone DnaJ;
82-167 2.38e-08

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 56.40  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   82 KDWKNQDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKaaGEPIKEgdnDYFTCITKAYEMLSDPVKRRAFNSVD 161
Cdd:PRK14295   4 KDYIEKDYYKVLG---VPKDATEAEIKKAYRKLAREYHPDANK--GDAKAE---ERFKEISEAYDVLSDEKKRKEYDEAR 75


                 ....*.
gi 94538370  162 PTFDNS 167
Cdd:PRK14295  76 SLFGNG 81
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 86-210 2.94e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 56.25  E-value: 2.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   86 NQDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDPT 163
Cdd:PRK14276   3 NTEYYDRLG---VSKDASQDEIKKAYRKLSKKYHPDINKEPGaeEKYKE--------VQEAYETLSDPQKRAAYDQYGAA 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94538370  164 ---------------FDNsvpskSEAKDNFFEVFTPVFERNSRWSNkKNVPKLGD-----MNSSFED 210
Cdd:PRK14276  72 ganggfgggaggfggFDG-----SGGFGGFEDIFSSFFGGGGARRN-PNAPRQGDdlqyrVNLDFEE 132
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 553-599 3.38e-08

Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, as well as the SANT domain family.


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 49.81  E-value: 3.38e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 94538370   553 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMKRYKEL 599
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 86-158 3.92e-08

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 55.98  E-value: 3.92e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538370   86 NQDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaagepikEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PTZ00037  27 NEKLYEVLNLSK---DCTTSEIKKAYRKLAIKHHPDK---------GGDPEKFKEISRAYEVLSDPEKRKIYD 87
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 88-155 6.02e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 55.06  E-value: 6.02e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRR 155
Cdd:PRK14278   4 DYYGLLG---VSRNASDAEIKRAYRKLARELHPDvnPDEEAQEKFKE--------ISVAYEVLSDPEKRR 62
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 86-158 1.31e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 54.23  E-value: 1.31e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538370   86 NQDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14286   3 ERSYYDILG---VSKSANDEEIKSAYRKLAIKYHPDKNKGNKES-----EEKFKEATEAYEILRDPKKRQAYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 87-158 3.19e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 52.88  E-value: 3.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94538370   87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14277   5 KDYYEILG---VDRNATEEEIKKAYRRLAKKYHPDLNpgdKEAEQKFKE--------INEAYEILSDPQKRAQYD 68
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 87-158 3.61e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 52.54  E-value: 3.61e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94538370   87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAGEpikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14298   5 RDYYEILGLSK---DASVEDIKKAYRKLAMKYHPDKNKEPDA------EEKFKEISEAYAVLSDAEKRAQYD 67
PRK14297 PRK14297
molecular chaperone DnaJ;
86-154 3.74e-07

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 52.86  E-value: 3.74e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94538370   86 NQDHYAVLGLghvRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKR 154
Cdd:PRK14297   3 SKDYYEVLGL---EKGASDDEIKKAFRKLAIKYHPDKNkgnKEAEEKFKE--------INEAYQVLSDPQKK 63
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 87-187 5.30e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 52.07  E-value: 5.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEGdndyftciTKAYEMLSDPVKRRAFNSVDPT 163
Cdd:PRK14294   4 RDYYEILG---VTRDASEEEIKKSYRKLAMKYHPDRNpgdKEAEELFKEA--------AEAYEVLSDPKKRGIYDQYGHE 72

                         90       100
                 ....*....|....*....|....*
gi 94538370  164 -FDNSVPSKSEAKDNFFEVFTPVFE 187
Cdd:PRK14294  73 gLSGTGFSGFSGFDDIFSSFGDIFE 97
PRK14280 PRK14280
molecular chaperone DnaJ;
87-210 6.49e-07

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 52.03  E-value: 6.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRR---AFNSVD 161
Cdd:PRK14280   4 RDYYEVLGVSK---SASKDEIKKAYRKLSKKYHPDINKEEGadEKFKE--------ISEAYEVLSDDQKRAqydQFGHAG 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 94538370  162 P--TFDNSVPSKSEAKDNF-FE-VFTPVFERNSRwSNKKNVPKLGD-----MNSSFED 210
Cdd:PRK14280  73 PnqGFGGGGFGGGDFGGGFgFEdIFSSFFGGGGR-RRDPNAPRQGAdlqytMTLTFEE 129
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 88-158 9.73e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 51.38  E-value: 9.73e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 94538370   88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEgdndyFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14284   2 DYYTILG---VSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKR-----FKEVSEAYEVLSDAQKRESYD 64
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 87-158 1.53e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 50.96  E-value: 1.53e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94538370   87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14281   3 RDYYEVLGVSR---SADKDEIKKAYRKLALKYHPDKNpdnKEAEEHFKE--------VNEAYEVLSNDDKRRRYD 66
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 87-158 1.81e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 50.31  E-value: 1.81e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 94538370   87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPD----KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14290   3 KDYYKILG---VDRNASQEDIKKAFRELAKKWHPDlhpgNKAEAEEKFKE--------ISEAYEVLSDPQKRRQYD 67
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 88-154 3.67e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 49.50  E-value: 3.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94538370   88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKaagepiKEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14292   3 DYYELLG---VSRTASADEIKSAYRKLALKYHPDRNK------EKGAAEKFAQINEAYAVLSDAEKR 60
PRK14293 PRK14293
molecular chaperone DnaJ;
88-154 1.22e-05

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 47.68  E-value: 1.22e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94538370   88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKaagEPikeGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14293   4 DYYEILG---VSRDADKDELKRAYRRLARKYHPDVNK---EP---GAEDRFKEINRAYEVLSDPETR 61
PRK14289 PRK14289
molecular chaperone DnaJ;
87-158 1.97e-05

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 47.13  E-value: 1.97e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94538370   87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14289   5 RDYYEVLG---VSKTATVDEIKKAYRKKAIQYHPDKNpgdKEAEEKFKE--------AAEAYDVLSDPDKRSRYD 68
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
87-151 6.81e-05

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 41.32  E-value: 6.81e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 94538370  87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDkRKAAGEPIKEGD--NDYFTCITKAYEMLSDP 151
Cdd:COG1076   4 DDAFELLGLPP---DADDAELKRAYRKLQREHHPD-RLAAGLPEEEQRlaLQKAAAINEAYETLKDP 66
SANT_CDC5_II cd11659
SANT/myb-like DNA-binding domain of Cell Division Cycle 5-Like Protein repeat II; In humans, ...
 547-601 1.67e-04

SANT/myb-like DNA-binding domain of Cell Division Cycle 5-Like Protein repeat II; In humans, cell division cycle 5-like protein (CDC5) functions in pre-mRNA splicing in cell cycle control. The DNA-binding, myb-like domain of CDC5 is a member of the SANT/myb group. SANT is named after 'SWI3, ADA2, N-CoR and TFIIIB', several factors that share this domain. The SANT domain resembles the 3 alpha-helix bundle of DNA-binding Myb domains and is found in a diverse set of proteins.


Pssm-ID: 212557 [Multi-domain]  Cd Length: 53  Bit Score: 39.60  E-value: 1.67e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 94538370 547 PYTDFTPWTTEEQKLLEQALKTYpvntPERWEKIAEAVpGRTKKDCMKRYKELVE 601
Cdd:cd11659   1 PSIKKTEWTREEDEKLLHLAKLL----PTQWRTIAPIV-GRTAQQCLERYNKLLD 50
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 87-158 1.88e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 44.21  E-value: 1.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 94538370   87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14285   3 RDYYEILGLSK---GASKDEIKKAYRKIAIKYHPDKNKGNKEA-----ESIFKEATEAYEVLIDDNKRAQYD 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 306-436 4.88e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 4.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 306 QEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCD 385
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 94538370 386 RLELASLQCLNETLTSCTKEVGKAALEKQIEEINEQIRKEKEEAEARMRQA 436
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-49 7.51e-04

N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, also known as DnaJ-related protein ZUO1, J protein ZUO1, or heat shock protein 40 homolog ZUO1, is a component of the ribosome-associated complex (RAC), which is a heterodimer of the Hsp70/DnaK-type chaperone SSZ1 and the Hsp40/DnaJ-type chaperone ZUO1. The RAC chaperone complex plays a role in regulating accurate translation termination and folding or maintaining nascent polypeptides in a folding-competent state. The ATPase activity of the ribosome-associated pool of Hsp70-type chaperones SSB1/SSB2 that bind to the nascent polypeptide chain is stimulated by the RAC chaperone complex. ZUO1 acts as a J-protein for SSB1/SSB2 only when it is associated with SSZ1. The N-terminal domain (NTD) of ZUO1 is responsible for its interaction with SSZ1, and it contains a conserved LP-motif that binds to the SSZ1 C-terminal SBD (substrate binding domain) beta-lid domain in the same way as canonical Hsp70s bind to their substrates.


Pssm-ID: 467935  Cd Length: 38  Bit Score: 37.48  E-value: 7.51e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 94538370  13 TAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASAS 49
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRTFS 38
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 453-506 1.28e-03

'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric DNA tandem repeatsas part of the capping complex. Binding is sequence dependent for repeats which contain the G/C rich motif [C2-3 A (CA)1-6]. The domain is also found in regulatory transcriptional repressor complexes where it also binds DNA.


Pssm-ID: 238096 [Multi-domain]  Cd Length: 45  Bit Score: 36.78  E-value: 1.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 94538370 453 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 506
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
flgK PRK08471
flagellar hook-associated protein FlgK; Validated
 323-436 1.29e-03

flagellar hook-associated protein FlgK; Validated


Pssm-ID: 236270 [Multi-domain]  Cd Length: 613  Bit Score: 41.96  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370  323 AKEKEEEEVRQQAL--LAKKEKDIQKKAIKKERQKLRNScktWNHFSDN---EAERVKMMEEVEKLCDRLE-----LASL 392
Cdd:PRK08471  82 STELEYTDYEFSTLqeASQYFPDLDDTGILKDLQDYFNA---WNDFASNpkdSAQKQALAQKTETLTNNIKdtrerLDTL 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 94538370  393 Q-CLNETLTSCTKEVGKaaLEKQIEEINEQIrkEKEEAEARMRQA 436
Cdd:PRK08471 159 QkKVNEELKVTVDEINS--LGKQIAEINKQI--KEVEAGKTLKHA 199
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
308-442 1.94e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 1.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 308 AKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKE--RQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCD 385
Cdd:COG4717  91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEalEAELAELPERLEELEERLEELRELEEELEELEA 170

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 94538370 386 RLELASLQClnETLTSCTKEVGKAALEKQIEEINE------QIRKEKEEAEARMRQASKNTEK 442
Cdd:COG4717 171 ELAELQEEL--EELLEQLSLATEEELQDLAEELEElqqrlaELEEELEEAQEELEELEEELEQ 231
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
452-508 3.31e-03

SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 3.31e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 94538370    452 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSLQK 508
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
PRK12704 PRK12704
phosphodiesterase; Provisional
 298-440 3.56e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 3.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370  298 KAEAKRKEQEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKK--AIKKERQKLRNSCKTWNHfsdneaeRVK 375
Cdd:PRK12704  52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKleLLEKREEELEKKEKELEQ-------KQQ 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370  376 MMEEVEKLCDRLELASLQCLnETLTSCTKEVGKAALEKQIE-----EINEQIRKEKEEAEARMRQASKNT 440
Cdd:PRK12704 125 ELEKKEEELEELIEEQLQEL-ERISGLTAEEAKEILLEKVEeearhEAAVLIKEIEEEAKEEADKKAKEI 193
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
306-451 4.49e-03

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.86  E-value: 4.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370 306 QEAKEKQRQAELE---AARLAKEKEEEEVRQQALLAKKEKDI--QKKAIKKERQKLRnscKTWNHFSDNEAERVKMMEEV 380
Cdd:COG2268 251 AEERREAETARAEaeaAYEIAEANAEREVQRQLEIAEREREIelQEKEAEREEAELE---ADVRKPAEAEKQAAEAEAEA 327

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 94538370 381 EKLCDRLEL----ASLQCLNETLtsctKEVGKAALEKQIEEINEQIRKEKEEAearMRQASKNTEKSTGGGGNGS 451
Cdd:COG2268 328 EAEAIRAKGlaeaEGKRALAEAW----NKLGDAAILLMLIEKLPEIAEAAAKP---LEKIDKITIIDGGNGGNGA 395
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 230-436 9.23e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 38.95  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   230 LDEEEKEKAECRDERRWIEKQNRATRAqrkkeEMNRIRTLvdnaYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQE-A 308
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQA-----EMDRQAAI----YAEQERMAMERERELERIRQEERKRELERIRQEEiA 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 94538370   309 KEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKTWNHFSDNEAERVKMME-----EVEKL 383
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEeerarEMERV 451

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 94538370   384 cdRLELASLQCLNETLTSCTKEVGKAALEKQIEE-----INEQIRKEKEEAEARMRQA 436
Cdd:pfam17380 452 --RLEEQERQQQVERLRQQEEERKRKKLELEKEKrdrkrAEEQRRKILEKELEERKQA 507
 
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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