NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|6677659|ref|NP_033610|]
View 

dnaJ homolog subfamily C member 2 isoform 1 [Mus musculus]

Protein Classification

DnaJ homolog subfamily C member 2( domain architecture ID 20367907)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 2.68e-63

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: 213.74  E-value: 2.68e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659   75 MLKTLDPKDWKNQDHYAVLGLGHVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269  31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659  155 RAFNSVDptFDNSVPS-KSEAKDNFFQVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659  234 EKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEARRKEQEAKEKQR 313
Cdd:COG5269 186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAALKGK 265

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6677659  314 QAEleavrlaKEKEEEEVRQQALLA---KKEKDIQKKAIKKERQKLRNSCKSWNHFSD 368
Cdd:COG5269 266 AEA-------KNKAEIEAEALASATavkKKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
 344-420 3.27e-17

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


:

Pssm-ID: 435537  Cd Length: 87  Bit Score: 76.92  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    344 IQKKAIKKERQKLRNSCKSWNHFSDNEADRVKM----MEEVEKLCDRLELASLQGLNEILASST-REVGKAALEKQIEEV 418
Cdd:pfam16717   1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80


                  ..
gi 6677659    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 2.78e-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: 2.78e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6677659  553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMRRYKELV 600
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 453-506 2.22e-04

'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: 39.10  E-value: 2.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 6677659  453 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVISKAKSL 506
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
zuotin_NTD super family cl48853
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-47 3.63e-03

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.


The actual alignment was detected with superfamily member cd23953:

Pssm-ID: 467935  Cd Length: 38  Bit Score: 35.56  E-value: 3.63e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6677659   13 TAITHALTSASSVCQVEPVGRWFEAFV--KRRNRNAS 47
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHArrKLHNRTFS 38
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-368 2.68e-63

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 213.74  E-value: 2.68e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659   75 MLKTLDPKDWKNQDHYAVLGLGHVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269  31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659  155 RAFNSVDptFDNSVPS-KSEAKDNFFQVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659  234 EKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEARRKEQEAKEKQR 313
Cdd:COG5269 186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAALKGK 265

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6677659  314 QAEleavrlaKEKEEEEVRQQALLA---KKEKDIQKKAIKKERQKLRNSCKSWNHFSD 368
Cdd:COG5269 266 AEA-------KNKAEIEAEALASATavkKKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
 344-420 3.27e-17

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


Pssm-ID: 435537  Cd Length: 87  Bit Score: 76.92  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    344 IQKKAIKKERQKLRNSCKSWNHFSDNEADRVKM----MEEVEKLCDRLELASLQGLNEILASST-REVGKAALEKQIEEV 418
Cdd:pfam16717   1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80


                  ..
gi 6677659    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 1.32e-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: 68.65  E-value: 1.32e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6677659     88 DHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
87-153 4.88e-12

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 61.10  E-value: 4.88e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6677659      87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 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 7.59e-12

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: 60.64  E-value: 7.59e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6677659   88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257   1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-157 2.48e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 65.55  E-value: 2.48e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6677659    87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---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 2.78e-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: 2.78e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6677659  553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMRRYKELV 600
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
552-602 1.23e-09

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 54.15  E-value: 1.23e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 6677659     552 TPWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMRRYKELVEM 602
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLKP 49
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 553-599 2.49e-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: 50.19  E-value: 2.49e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6677659    553 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMRRYKEL 599
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 453-506 2.22e-04

'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: 39.10  E-value: 2.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 6677659  453 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVISKAKSL 506
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
452-508 5.50e-04

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 37.97  E-value: 5.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6677659     452 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVISKAKSLQK 508
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-47 3.63e-03

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: 35.56  E-value: 3.63e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6677659   13 TAITHALTSASSVCQVEPVGRWFEAFV--KRRNRNAS 47
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHArrKLHNRTFS 38
PRK12704 PRK12704
phosphodiesterase; Provisional
 297-442 3.98e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659   297 AKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKDIQKK--AIKKERQKLRNSCKSWNHfsdneadRV 374
Cdd:PRK12704  51 AEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKleLLEKREEELEKKEKELEQ-------KQ 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6677659   375 KMMEEVEKLCDRLELASLQGLNEIlASSTREVGKAALekqIEEVNEQMRRE------KEEADARMrQASKNAEK 442
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELERI-SGLTAEEAKEIL---LEKVEEEARHEaavlikEIEEEAKE-EADKKAKE 192
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-368 2.68e-63

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 213.74  E-value: 2.68e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659   75 MLKTLDPKDWKNQDHYAVLGLGHVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269  31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659  155 RAFNSVDptFDNSVPS-KSEAKDNFFQVFSPVFERNSRWSNKKNVPKLGDMNSSFEDVDAFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269 108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659  234 EKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEARRKEQEAKEKQR 313
Cdd:COG5269 186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAALKGK 265

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 6677659  314 QAEleavrlaKEKEEEEVRQQALLA---KKEKDIQKKAIKKERQKLRNSCKSWNHFSD 368
Cdd:COG5269 266 AEA-------KNKAEIEAEALASATavkKKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
 344-420 3.27e-17

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


Pssm-ID: 435537  Cd Length: 87  Bit Score: 76.92  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    344 IQKKAIKKERQKLRNSCKSWNHFSDNEADRVKM----MEEVEKLCDRLELASLQGLNEILASST-REVGKAALEKQIEEV 418
Cdd:pfam16717   1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80


                  ..
gi 6677659    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 1.32e-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: 68.65  E-value: 1.32e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6677659     88 DHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
87-153 4.88e-12

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 61.10  E-value: 4.88e-12
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6677659      87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 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 7.59e-12

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: 60.64  E-value: 7.59e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6677659   88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257   1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
87-157 1.82e-11

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 60.50  E-value: 1.82e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6677659   87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKrkaaGEPIKEGDNDYFTCITKAYEMLSDPVKRRAF 157
Cdd:COG2214   5 KDHYAVLGVPP---DASLEEIRQAYRRLAKLLHPDR----GGELKALAEELFQRLNEAYEVLSDPERRAEY 68
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-157 2.48e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 65.55  E-value: 2.48e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6677659    87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:PRK10767   4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 88-157 3.11e-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: 61.64  E-value: 3.11e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6677659   88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:COG0484   1 DYYEILG---VSRDASAEEIKKAYRKLAKKYHPDRNpgdPEAEEKFKE--------INEAYEVLSDPEKRAAY 62
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 553-600 2.78e-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: 2.78e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 6677659  553 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMRRYKELV 600
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 87-209 4.73e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 61.73  E-value: 4.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDK----RKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDP 162
Cdd:PRK14282   4 KDYYEILG---VSRNATQEEIKRAYKRLVKEWHPDRhpenRKEAEQKFKE--------IQEAYEVLSDPQKRAMYDRFGY 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6677659   163 TFDNSVPSKSEAKDNFFQ-------------VFSPVFERNSRWSNKKNVPKLG-DMNSSFE 209
Cdd:PRK14282  73 VGEQPPYQETESGGGFFEdifkdfenifnrdIFDIFFGERRTQEEQREYARRGeDIRYEIE 133
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
552-602 1.23e-09

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 54.15  E-value: 1.23e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 6677659     552 TPWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMRRYKELVEM 602
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLKP 49
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 87-217 5.24e-09

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 58.63  E-value: 5.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSvdptF 164
Cdd:PRK14291   3 KDYYEILG---VSRNATQEEIKKAYRRLARKYHPDfnKNPEAEEKFKE--------INEAYQVLSDPEKRKLYDQ----F 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6677659   165 DNSVPSKSEAKDNFFQVFSPVFERNsrwsnkknvpkLGDMnssFEDVDAFYSF 217
Cdd:PRK14291  68 GHAAFSGSGQQQQGQEGFSDFGGGN-----------IEDI---LEDVFDIFGF 106
PRK14295 PRK14295
molecular chaperone DnaJ;
82-167 7.05e-09

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 58.32  E-value: 7.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    82 KDWKNQDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKaaGEPIKEgdnDYFTCITKAYEMLSDPVKRRAFNSVD 161
Cdd:PRK14295   4 KDYIEKDYYKVLG---VPKDATEAEIKKAYRKLAREYHPDANK--GDAKAE---ERFKEISEAYDVLSDEKKRKEYDEAR 75


                 ....*.
gi 6677659   162 PTFDNS 167
Cdd:PRK14295  76 SLFGNG 81
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 86-210 1.23e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 57.41  E-value: 1.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    86 NQDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDPT 163
Cdd:PRK14276   3 NTEYYDRLG---VSKDASQDEIKKAYRKLSKKYHPDINKEPGaeEKYKE--------VQEAYETLSDPQKRAAYDQYGAA 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6677659   164 ---------------FDNsvpskSEAKDNFFQVFSPVFERNSRWSNkKNVPKLGD-----MNSSFED 210
Cdd:PRK14276  72 ganggfgggaggfggFDG-----SGGFGGFEDIFSSFFGGGGARRN-PNAPRQGDdlqyrVNLDFEE 132
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 87-159 1.70e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 56.10  E-value: 1.70e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6677659    87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRRAFNS 159
Cdd:PRK14299   4 KDYYAILG---VPKNASQDEIKKAFKKLARKYHPDVNKSPGaeEKFKE--------INEAYTVLSDPEKRRIYDT 67
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 553-599 2.49e-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: 50.19  E-value: 2.49e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6677659    553 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMRRYKEL 599
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 86-158 3.35e-08

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 55.98  E-value: 3.35e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6677659    86 NQDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKrkaagepikEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PTZ00037  27 NEKLYEVLNLSK---DCTTSEIKKAYRKLAIKHHPDK---------GGDPEKFKEISRAYEVLSDPEKRKIYD 87
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 88-155 8.95e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 54.67  E-value: 8.95e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRR 155
Cdd:PRK14278   4 DYYGLLG---VSRNASDAEIKRAYRKLARELHPDvnPDEEAQEKFKE--------ISVAYEVLSDPEKRR 62
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 86-158 9.30e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 54.61  E-value: 9.30e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6677659    86 NQDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14286   3 ERSYYDILG---VSKSANDEEIKSAYRKLAIKYHPDKNKGNKES-----EEKFKEATEAYEILRDPKKRQAYD 67
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 88-158 1.61e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 53.69  E-value: 1.61e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6677659    88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEgdndyFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14284   2 DYYTILG---VSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKR-----FKEVSEAYEVLSDAQKRESYD 64
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 87-158 1.69e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 53.65  E-value: 1.69e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6677659    87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14277   5 KDYYEILG---VDRNATEEEIKKAYRRLAKKYHPDLNpgdKEAEQKFKE--------INEAYEILSDPQKRAQYD 68
PRK14297 PRK14297
molecular chaperone DnaJ;
86-154 2.27e-07

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 53.25  E-value: 2.27e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6677659    86 NQDHYAVLGLghvRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKR 154
Cdd:PRK14297   3 SKDYYEVLGL---EKGASDDEIKKAFRKLAIKYHPDKNkgnKEAEEKFKE--------INEAYQVLSDPQKK 63
PRK14280 PRK14280
molecular chaperone DnaJ;
87-210 2.62e-07

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 53.19  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRR---AFNSVD 161
Cdd:PRK14280   4 RDYYEVLGVSK---SASKDEIKKAYRKLSKKYHPDINKEEGadEKFKE--------ISEAYEVLSDDQKRAqydQFGHAG 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6677659   162 P--TFDNSVPSKSEAKDNF-FQ-VFSPVFERNSRwSNKKNVPKLGD-----MNSSFED 210
Cdd:PRK14280  73 PnqGFGGGGFGGGDFGGGFgFEdIFSSFFGGGGR-RRDPNAPRQGAdlqytMTLTFEE 129
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 87-187 2.84e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 52.84  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEGdndyftciTKAYEMLSDPVKRRAFNSVDPT 163
Cdd:PRK14294   4 RDYYEILG---VTRDASEEEIKKSYRKLAMKYHPDRNpgdKEAEELFKEA--------AEAYEVLSDPKKRGIYDQYGHE 72

                         90       100
                 ....*....|....*....|....*
gi 6677659   164 -FDNSVPSKSEAKDNFFQVFSPVFE 187
Cdd:PRK14294  73 gLSGTGFSGFSGFDDIFSSFGDIFE 97
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 87-187 3.97e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 52.54  E-value: 3.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAGEpikegdNDYFTCITKAYEMLSDPVKRRAFNSvdptFDN 166
Cdd:PRK14298   5 RDYYEILGLSK---DASVEDIKKAYRKLAMKYHPDKNKEPDA------EEKFKEISEAYAVLSDAEKRAQYDR----FGH 71

                         90       100
                 ....*....|....*....|....*.
gi 6677659   167 S-VPSKSEAKDNF----FQVFSPVFE 187
Cdd:PRK14298  72 AgIDNQYSAEDIFrgadFGGFGDIFE 97
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 88-154 4.98e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 52.20  E-value: 4.98e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6677659    88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKaagepiKEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14292   3 DYYELLG---VSRTASADEIKSAYRKLALKYHPDRNK------EKGAAEKFAQINEAYAVLSDAEKR 60
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 87-158 5.06e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 52.50  E-value: 5.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6677659    87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14281   3 RDYYEVLGVSR---SADKDEIKKAYRKLALKYHPDKNpdnKEAEEHFKE--------VNEAYEVLSNDDKRRRYD 66
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 87-158 1.30e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 51.09  E-value: 1.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6677659    87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPD----KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14290   3 KDYYKILG---VDRNASQEDIKKAFRELAKKWHPDlhpgNKAEAEEKFKE--------ISEAYEVLSDPQKRRQYD 67
PRK14289 PRK14289
molecular chaperone DnaJ;
87-158 3.73e-06

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 49.44  E-value: 3.73e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6677659    87 QDHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14289   5 RDYYEVLG---VSKTATVDEIKKAYRKKAIQYHPDKNpgdKEAEEKFKE--------AAEAYDVLSDPDKRSRYD 68
PRK14293 PRK14293
molecular chaperone DnaJ;
88-154 1.20e-05

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 48.06  E-value: 1.20e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6677659    88 DHYAVLGlghVRYTATQRQIKAAHKAMVLKHHPDKRKaagEPikeGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14293   4 DYYEILG---VSRDADKDELKRAYRRLARKYHPDVNK---EP---GAEDRFKEINRAYEVLSDPETR 61
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
87-151 5.12e-05

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 41.71  E-value: 5.12e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6677659   87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDkRKAAGEPIKEGD--NDYFTCITKAYEMLSDP 151
Cdd:COG1076   4 DDAFELLGLPP---DADDAELKRAYRKLQREHHPD-RLAAGLPEEEQRlaLQKAAAINEAYETLKDP 66
PTZ00121 PTZ00121
MAEBL; Provisional
 233-621 8.94e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 8.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    233 EEKEKAecrDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEARRKEQEAKEKQ 312
Cdd:PTZ00121 1287 EEKKKA---DEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAE 1363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    313 RQAELEAVRLAKEKEE-EEVRQQALLAKKEKDIQKKA----IKKERQKLRNSCKSWNHFSDNEADRVKMMEEVEKLCDRL 387
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKaDAAKKKAEEKKKADEAKKKAeedkKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEA 1443

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    388 ELASLQGLNEILASSTREVGKAALEKQIEEVNEQMRREKEEADARMRQASKNAEKSTGGSGSGSKNWSEDDLQlliKAVN 467
Cdd:PTZ00121 1444 KKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK---KAEE 1520

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    468 LFPAGTNSRWEvianymnihsssgvKRTAKDVISKAKSLQKLDPHQKDDINKKAFDKFKKEHGVASQADSAAPSERFEgp 547
Cdd:PTZ00121 1521 AKKADEAKKAE--------------EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAE-- 1584

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6677659    548 cidstPWTTEEQKLLEQALKTYPVNTPERWEKIAEAVPGRTKKDCMRRYKELVEMV-KAKKAAQEQVLNASRARK 621
Cdd:PTZ00121 1585 -----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVeQLKKKEAEEKKKAEELKK 1654
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 87-187 1.01e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 44.98  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    87 QDHYAVLGLGHvryTATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFNSvdptFDN 166
Cdd:PRK14285   3 RDYYEILGLSK---GASKDEIKKAYRKIAIKYHPDKNKGNKEA-----ESIFKEATEAYEVLIDDNKRAQYDR----FGH 70

                         90       100
                 ....*....|....*....|....
gi 6677659   167 SVPSKSEAKDNF---FQVFSPVFE 187
Cdd:PRK14285  71 TAFEGGGGFEGFsggFSGFSDIFE 94
SANT_CDC5_II cd11659
SANT/myb-like DNA-binding domain of Cell Division Cycle 5-Like Protein repeat II; In humans, ...
 547-601 1.03e-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: 40.37  E-value: 1.03e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 6677659  547 PCIDSTPWTTEEQKLLEQALKTYpvntPERWEKIAEAVpGRTKKDCMRRYKELVE 601
Cdd:cd11659   1 PSIKKTEWTREEDEKLLHLAKLL----PTQWRTIAPIV-GRTAQQCLERYNKLLD 50
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 453-506 2.22e-04

'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: 39.10  E-value: 2.22e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 6677659  453 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVISKAKSL 506
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 306-462 2.80e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.80e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659  306 QEAKEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKSWNHFSDNEADRVKMMEEVEKLCD 385
Cdd:COG1196 303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6677659  386 RLELASLQGLNEILASSTREVGKAALEKQIEEVNEQMRREKEEADARMRQASKNAEKSTGGSGSGSKNWSEDDLQLL 462
Cdd:COG1196 383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEE 459
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
452-508 5.50e-04

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 37.97  E-value: 5.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6677659     452 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVISKAKSLQK 508
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
PTZ00121 PTZ00121
MAEBL; Provisional
 232-442 2.70e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    232 EEEKEKAEcrDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEARRKEQEAKEK 311
Cdd:PTZ00121 1374 EEAKKKAD--AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKK 1451

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    312 QRQAELEAVRLAKEKEE----EEVRQQALLAKKEKDIQKKA--IKKERQKLRNSCKSWNHFSD-NEADRVKMMEEVEKLC 384
Cdd:PTZ00121 1452 KAEEAKKAEEAKKKAEEakkaDEAKKKAEEAKKADEAKKKAeeAKKKADEAKKAAEAKKKADEaKKAEEAKKADEAKKAE 1531

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6677659    385 DRLELASLQGLNEIlaSSTREVGKAALEKQIEEVN--EQMRREKEEADARMRQA--SKNAEK 442
Cdd:PTZ00121 1532 EAKKADEAKKAEEK--KKADELKKAEELKKAEEKKkaEEAKKAEEDKNMALRKAeeAKKAEE 1591
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-47 3.63e-03

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: 35.56  E-value: 3.63e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6677659   13 TAITHALTSASSVCQVEPVGRWFEAFV--KRRNRNAS 47
Cdd:cd23953   2 SAVVHASLSAPVTRKLEPVGPAFLAHArrKLHNRTFS 38
PRK12704 PRK12704
phosphodiesterase; Provisional
 297-442 3.98e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659   297 AKAEARRKEQEAKEKQRQAELEAVRLAKEKEEEEVRQQALLAKKEKDIQKK--AIKKERQKLRNSCKSWNHfsdneadRV 374
Cdd:PRK12704  51 AEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKleLLEKREEELEKKEKELEQ-------KQ 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6677659   375 KMMEEVEKLCDRLELASLQGLNEIlASSTREVGKAALekqIEEVNEQMRRE------KEEADARMrQASKNAEK 442
Cdd:PRK12704 124 QELEKKEEELEELIEEQLQELERI-SGLTAEEAKEIL---LEKVEEEARHEaavlikEIEEEAKE-EADKKAKE 192
PTZ00121 PTZ00121
MAEBL; Provisional
 230-428 4.66e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    230 LDEEEKEKAECRDERKWIEKQNRATRAQRKKEEMNRIRtlvdnayscdprikkfkeeEKAKKEAEKKAKAEARRKEQEAK 309
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK-------------------AAEEAKKAEEDKKKAEEAKKAEE 1685

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    310 EKQRQAEleavrlAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKSWNHFSDNEADRVKMMEEVEKLCDRLEL 389
Cdd:PTZ00121 1686 DEKKAAE------ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKI 1759

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 6677659    390 ASLQGLNEILASSTREVGKAALEKQIEEVNEQMRREKEE 428
Cdd:PTZ00121 1760 AHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
PTZ00121 PTZ00121
MAEBL; Provisional
 233-452 9.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    233 EEKEKAEcrDERKWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEARRKEQEAKEKQ 312
Cdd:PTZ00121 1454 EEAKKAE--EAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAE 1531

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6677659    313 RQAELEAVRLAKEKEE-EEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKSWNHFSDNEADRVKMMEEVEKLCDRLELAS 391
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKaDELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEE 1611

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6677659    392 LQGLNEIL--------ASSTREVGKAALEKQIEEVN--EQMRREKEEADARMRQASKNAEKSTGGSGSGSK 452
Cdd:PTZ00121 1612 AKKAEEAKikaeelkkAEEEKKKVEQLKKKEAEEKKkaEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH