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Conserved domains on  [gi|1380941522|ref|NP_001349596|]
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dnaJ homolog subfamily C member 2 isoform 3 [Homo sapiens]

Protein Classification

DnaJ homolog subfamily C member 2( domain architecture ID 13425069)

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

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 / ...
1-294 1.12e-65

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: 218.36  E-value: 1.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522   1 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 80
Cdd:COG5269    31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522  81 RAFNSVDptFDNSVPS-KSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEE 159
Cdd:COG5269   108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 160 EKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAK---- 235
Cdd:COG5269   186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAAlkgk 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 236 -EKQRQAELEAARLAKEKEEEevrqqallaKKEKDIQKKAIKKERQKLRNSCKTWNHFSD 294
Cdd:COG5269   266 aEAKNKAEIEAEALASATAVK---------KKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
270-346 7.49e-18

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


:

Pssm-ID: 435537  Cd Length: 87  Bit Score: 78.46  E-value: 7.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 270 IQKKAIKKERQKLRNSCKTWNHFSDNEAERVKM----MEEVEKLCDRLELASLQCLNETLTSCT-KEVGKAALEKQIEEI 344
Cdd:pfam16717   1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80

                  ..
gi 1380941522 345 NE 346
Cdd:pfam16717  81 VD 82
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
479-526 5.10e-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: 54.89  E-value: 5.10e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1380941522 479 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELV 526
Cdd:cd00167     1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
379-432 1.86e-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: 36.40  E-value: 1.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1380941522 379 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 432
Cdd:cd00167     1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
1-294 1.12e-65

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 218.36  E-value: 1.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522   1 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 80
Cdd:COG5269    31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522  81 RAFNSVDptFDNSVPS-KSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEE 159
Cdd:COG5269   108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 160 EKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAK---- 235
Cdd:COG5269   186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAAlkgk 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 236 -EKQRQAELEAARLAKEKEEEevrqqallaKKEKDIQKKAIKKERQKLRNSCKTWNHFSD 294
Cdd:COG5269   266 aEAKNKAEIEAEALASATAVK---------KKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
270-346 7.49e-18

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


Pssm-ID: 435537  Cd Length: 87  Bit Score: 78.46  E-value: 7.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 270 IQKKAIKKERQKLRNSCKTWNHFSDNEAERVKM----MEEVEKLCDRLELASLQCLNETLTSCT-KEVGKAALEKQIEEI 344
Cdd:pfam16717   1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80

                  ..
gi 1380941522 345 NE 346
Cdd:pfam16717  81 VD 82
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
14-84 6.65e-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: 66.34  E-value: 6.65e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1380941522  14 DHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 84
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
13-79 1.87e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 59.17  E-value: 1.87e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1380941522   13 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 79
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 ...
14-76 2.29e-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: 59.10  E-value: 2.29e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1380941522  14 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 76
Cdd:cd06257     1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
13-83 2.16e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 62.47  E-value: 2.16e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1380941522  13 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 83
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 ...
479-526 5.10e-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: 54.89  E-value: 5.10e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1380941522 479 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELV 526
Cdd:cd00167     1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
477-528 2.26e-09

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 53.00  E-value: 2.26e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1380941522  477 FTPWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELVEM 528
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, ...
479-525 4.90e-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: 49.04  E-value: 4.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1380941522 479 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMKRYKEL 525
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
232-362 4.81e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 232 QEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCD 311
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1380941522 312 RLELASLQCLNETLTSCTKEVGKAALEKQIEEINEQIRKEKEEAEARMRQA 362
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
flgK PRK08471
flagellar hook-associated protein FlgK; Validated
249-362 1.56e-03

flagellar hook-associated protein FlgK; Validated


Pssm-ID: 236270 [Multi-domain]  Cd Length: 613  Bit Score: 41.19  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 249 AKEKEEEEVRQQAL--LAKKEKDIQKKAIKKERQKLRNScktWNHFSDN---EAERVKMMEEVEKLCDRLE-----LASL 318
Cdd:PRK08471   82 STELEYTDYEFSTLqeASQYFPDLDDTGILKDLQDYFNA---WNDFASNpkdSAQKQALAQKTETLTNNIKdtrerLDTL 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1380941522 319 Q-CLNETLTSCTKEVGKaaLEKQIEEINEQIrkEKEEAEARMRQA 362
Cdd:PRK08471  159 QkKVNEELKVTVDEINS--LGKQIAEINKQI--KEVEAGKTLKHA 199
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
379-432 1.86e-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: 36.40  E-value: 1.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1380941522 379 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 432
Cdd:cd00167     1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
378-434 5.10e-03

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 35.28  E-value: 5.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1380941522  378 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSLQK 434
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
1-294 1.12e-65

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 218.36  E-value: 1.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522   1 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 80
Cdd:COG5269    31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522  81 RAFNSVDptFDNSVPS-KSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEE 159
Cdd:COG5269   108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 160 EKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAK---- 235
Cdd:COG5269   186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAAlkgk 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 236 -EKQRQAELEAARLAKEKEEEevrqqallaKKEKDIQKKAIKKERQKLRNSCKTWNHFSD 294
Cdd:COG5269   266 aEAKNKAEIEAEALASATAVK---------KKAKEVMKKALKMEKKAIKNAAKDADYFGD 316
RAC_head pfam16717
Ribosome-associated complex head domain; The RAC head domain is involved in ribosome binding.
270-346 7.49e-18

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


Pssm-ID: 435537  Cd Length: 87  Bit Score: 78.46  E-value: 7.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 270 IQKKAIKKERQKLRNSCKTWNHFSDNEAERVKM----MEEVEKLCDRLELASLQCLNETLTSCT-KEVGKAALEKQIEEI 344
Cdd:pfam16717   1 AAKKALKKNKRVLRGSVKDANYFADGEAEKAAVidgvLADVDLLCEKLDDEELAELAEKLEGAKdAEAVKAVFEEEVKEL 80

                  ..
gi 1380941522 345 NE 346
Cdd:pfam16717  81 VD 82
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
14-84 6.65e-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: 66.34  E-value: 6.65e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1380941522  14 DHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 84
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
13-79 1.87e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 59.17  E-value: 1.87e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1380941522   13 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 79
Cdd:smart00271   1 TDYYEILGVPR---DASLDEIKKAYRKLALKYHPDKNPGD----KEEAEEKFKEINEAYEVLSDPEK 60
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
13-83 2.04e-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: 2.04e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1380941522  13 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaaGEPIKEGDNDYFTCITKAYEMLSDPVKRRAF 83
Cdd:COG2214     5 KDHYAVLGVPP---DASLEEIRQAYRRLAKLLHPDR----GGELKALAEELFQRLNEAYEVLSDPERRAEY 68
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
14-76 2.29e-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: 59.10  E-value: 2.29e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1380941522  14 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 76
Cdd:cd06257     1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
14-83 4.62e-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: 60.87  E-value: 4.62e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1380941522  14 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 83
Cdd:COG0484     1 DYYEILG---VSRDASAEEIKKAYRKLAKKYHPDRNpgdPEAEEKFKE--------INEAYEVLSDPEKRAAY 62
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
13-83 2.16e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 62.47  E-value: 2.16e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1380941522  13 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 83
Cdd:PRK10767    4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
13-135 3.45e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 61.73  E-value: 3.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522  13 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDK----RKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDP 88
Cdd:PRK14282    4 KDYYEILG---VSRNATQEEIKRAYKRLVKEWHPDRhpenRKEAEQKFKE--------IQEAYEVLSDPQKRAMYDRFGY 72
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1380941522  89 TFDNSVPSKSEAKDNFFE-------------VFTPVFERNSRWSNKKNVPKLG-DMNSSFE 135
Cdd:PRK14282   73 VGEQPPYQETESGGGFFEdifkdfenifnrdIFDIFFGERRTQEEQREYARRGeDIRYEIE 133
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
479-526 5.10e-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: 54.89  E-value: 5.10e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1380941522 479 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELV 526
Cdd:cd00167     1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
477-528 2.26e-09

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 53.00  E-value: 2.26e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1380941522  477 FTPWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELVEM 528
Cdd:smart00717   1 KGEWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLKP 49
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
13-143 1.27e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 57.09  E-value: 1.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522  13 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSvdptF 90
Cdd:PRK14291    3 KDYYEILG---VSRNATQEEIKKAYRRLARKYHPDfnKNPEAEEKFKE--------INEAYQVLSDPEKRKLYDQ----F 67
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1380941522  91 DNSVPSKSEAKDNFFEVFTPVFERNsrwsnkknvpkLGDMnssFEDVDIFYSF 143
Cdd:PRK14291   68 GHAAFSGSGQQQQGQEGFSDFGGGN-----------IEDI---LEDVFDIFGF 106
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
13-85 1.95e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 55.72  E-value: 1.95e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1380941522  13 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKegdndyFTCITKAYEMLSDPVKRRAFNS 85
Cdd:PRK14299    4 KDYYAILG---VPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEK------FKEINEAYTVLSDPEKRRIYDT 67
PRK14295 PRK14295
molecular chaperone DnaJ;
8-93 1.96e-08

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 56.40  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522   8 KDWKNQDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKaaGEPIKEgdnDYFTCITKAYEMLSDPVKRRAFNSVD 87
Cdd:PRK14295    4 KDYIEKDYYKVLG---VPKDATEAEIKKAYRKLAREYHPDANK--GDAKAE---ERFKEISEAYDVLSDEKKRKEYDEAR 75

                  ....*.
gi 1380941522  88 PTFDNS 93
Cdd:PRK14295   76 SLFGNG 81
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
12-136 2.43e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 56.25  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522  12 NQDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDPT 89
Cdd:PRK14276    3 NTEYYDRLG---VSKDASQDEIKKAYRKLSKKYHPDINKEPGaeEKYKE--------VQEAYETLSDPQKRAAYDQYGAA 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1380941522  90 ---------------FDNsvpskSEAKDNFFEVFTPVFERNSRWSNkKNVPKLGD-----MNSSFED 136
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, ...
479-525 4.90e-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: 49.04  E-value: 4.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1380941522 479 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMKRYKEL 525
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
14-81 4.97e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 55.06  E-value: 4.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522  14 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRR 81
Cdd:PRK14278    4 DYYGLLG---VSRNASDAEIKRAYRKLARELHPDvnPDEEAQEKFKE--------ISVAYEVLSDPEKRR 62
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
12-84 5.56e-08

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 55.21  E-value: 5.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1380941522  12 NQDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaagepikEGDNDYFTCITKAYEMLSDPVKRRAFN 84
Cdd:PTZ00037   27 NEKLYEVLNLSK---DCTTSEIKKAYRKLAIKHHPDK---------GGDPEKFKEISRAYEVLSDPEKRKIYD 87
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
12-84 1.09e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 54.23  E-value: 1.09e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1380941522  12 NQDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFN 84
Cdd:PRK14286    3 ERSYYDILG---VSKSANDEEIKSAYRKLAIKYHPDKNKGNKES-----EEKFKEATEAYEILRDPKKRQAYD 67
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
13-84 2.99e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 52.54  E-value: 2.99e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1380941522  13 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAGEpikegdNDYFTCITKAYEMLSDPVKRRAFN 84
Cdd:PRK14298    5 RDYYEILGLSK---DASVEDIKKAYRKLAMKYHPDKNKEPDA------EEKFKEISEAYAVLSDAEKRAQYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
13-84 3.26e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 52.50  E-value: 3.26e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1380941522  13 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 84
Cdd:PRK14277    5 KDYYEILG---VDRNATEEEIKKAYRRLAKKYHPDLNpgdKEAEQKFKE--------INEAYEILSDPQKRAQYD 68
PRK14297 PRK14297
molecular chaperone DnaJ;
12-80 4.34e-07

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 52.09  E-value: 4.34e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1380941522  12 NQDHYAVLGLghvRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKR 80
Cdd:PRK14297    3 SKDYYEVLGL---EKGASDDEIKKAFRKLAIKYHPDKNkgnKEAEEKFKE--------INEAYQVLSDPQKK 63
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
13-113 4.65e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 52.07  E-value: 4.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522  13 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEGdndyftciTKAYEMLSDPVKRRAFNSVDPT 89
Cdd:PRK14294    4 RDYYEILG---VTRDASEEEIKKSYRKLAMKYHPDRNpgdKEAEELFKEA--------AEAYEVLSDPKKRGIYDQYGHE 72
                          90       100
                  ....*....|....*....|....*
gi 1380941522  90 -FDNSVPSKSEAKDNFFEVFTPVFE 113
Cdd:PRK14294   73 gLSGTGFSGFSGFDDIFSSFGDIFE 97
PRK14280 PRK14280
molecular chaperone DnaJ;
13-136 7.94e-07

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 51.26  E-value: 7.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522  13 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRR---AFNSVD 87
Cdd:PRK14280    4 RDYYEVLGVSK---SASKDEIKKAYRKLSKKYHPDINKEEGadEKFKE--------ISEAYEVLSDDQKRAqydQFGHAG 72
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1380941522  88 P--TFDNSVPSKSEAKDNF-FE-VFTPVFERNSRwSNKKNVPKLGD-----MNSSFED 136
Cdd:PRK14280   73 PnqGFGGGGFGGGDFGGGFgFEdIFSSFFGGGGR-RRDPNAPRQGAdlqytMTLTFEE 129
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
14-84 8.91e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 51.38  E-value: 8.91e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1380941522  14 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEgdndyFTCITKAYEMLSDPVKRRAFN 84
Cdd:PRK14284    2 DYYTILG---VSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKR-----FKEVSEAYEVLSDAQKRESYD 64
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
13-84 1.60e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 50.58  E-value: 1.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1380941522  13 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 84
Cdd:PRK14281    3 RDYYEVLGVSR---SADKDEIKKAYRKLALKYHPDKNpdnKEAEEHFKE--------VNEAYEVLSNDDKRRRYD 66
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
13-84 2.27e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 49.93  E-value: 2.27e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1380941522  13 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPD----KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 84
Cdd:PRK14290    3 KDYYKILG---VDRNASQEDIKKAFRELAKKWHPDlhpgNKAEAEEKFKE--------ISEAYEVLSDPQKRRQYD 67
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
14-80 2.90e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 49.50  E-value: 2.90e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1380941522  14 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKaagepiKEGDNDYFTCITKAYEMLSDPVKR 80
Cdd:PRK14292    3 DYYELLG---VSRTASADEIKSAYRKLALKYHPDRNK------EKGAAEKFAQINEAYAVLSDAEKR 60
PRK14293 PRK14293
molecular chaperone DnaJ;
14-80 1.02e-05

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 47.68  E-value: 1.02e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1380941522  14 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKaagEPikeGDNDYFTCITKAYEMLSDPVKR 80
Cdd:PRK14293    4 DYYEILG---VSRDADKDELKRAYRRLARKYHPDVNK---EP---GAEDRFKEINRAYEVLSDPETR 61
PRK14289 PRK14289
molecular chaperone DnaJ;
13-84 2.11e-05

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 46.75  E-value: 2.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1380941522  13 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 84
Cdd:PRK14289    5 RDYYEVLG---VSKTATVDEIKKAYRKKAIQYHPDKNpgdKEAEEKFKE--------AAEAYDVLSDPDKRSRYD 68
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
13-77 5.96e-05

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 41.32  E-value: 5.96e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1380941522  13 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDkRKAAGEPIKEGD--NDYFTCITKAYEMLSDP 77
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, ...
473-527 2.20e-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: 39.21  E-value: 2.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1380941522 473 PYTDFTPWTTEEQKLLEQALKTYpvntPERWEKIAEAVpGRTKKDCMKRYKELVE 527
Cdd:cd11659     1 PSIKKTEWTREEDEKLLHLAKLL----PTQWRTIAPIV-GRTAQQCLERYNKLLD 50
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
13-84 2.31e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 43.44  E-value: 2.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1380941522  13 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFN 84
Cdd:PRK14285    3 RDYYEILGLSK---GASKDEIKKAYRKIAIKYHPDKNKGNKEA-----ESIFKEATEAYEVLIDDNKRAQYD 66
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
232-362 4.81e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 232 QEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCD 311
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1380941522 312 RLELASLQCLNETLTSCTKEVGKAALEKQIEEINEQIRKEKEEAEARMRQA 362
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEL 433
flgK PRK08471
flagellar hook-associated protein FlgK; Validated
249-362 1.56e-03

flagellar hook-associated protein FlgK; Validated


Pssm-ID: 236270 [Multi-domain]  Cd Length: 613  Bit Score: 41.19  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 249 AKEKEEEEVRQQAL--LAKKEKDIQKKAIKKERQKLRNScktWNHFSDN---EAERVKMMEEVEKLCDRLE-----LASL 318
Cdd:PRK08471   82 STELEYTDYEFSTLqeASQYFPDLDDTGILKDLQDYFNA---WNDFASNpkdSAQKQALAQKTETLTNNIKdtrerLDTL 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1380941522 319 Q-CLNETLTSCTKEVGKaaLEKQIEEINEQIrkEKEEAEARMRQA 362
Cdd:PRK08471  159 QkKVNEELKVTVDEINS--LGKQIAEINKQI--KEVEAGKTLKHA 199
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
379-432 1.86e-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: 36.40  E-value: 1.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1380941522 379 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 432
Cdd:cd00167     1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
234-368 2.27e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 234 AKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKE--RQKLRNSCKTWNHFSDNEAERVKMMEEVEKLCD 311
Cdd:COG4717    91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEalEAELAELPERLEELEERLEELRELEEELEELEA 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1380941522 312 RLELASLQClnETLTSCTKEVGKAALEKQIEEINE------QIRKEKEEAEARMRQASKNTEK 368
Cdd:COG4717   171 ELAELQEEL--EELLEQLSLATEEELQDLAEELEElqqrlaELEEELEEAQEELEELEEELEQ 231
PRK12704 PRK12704
phosphodiesterase; Provisional
224-366 3.93e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 224 KAEAKRKEQEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKK--AIKKERQKLRNSCKTWNHfsdneaeRVK 301
Cdd:PRK12704   52 EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKleLLEKREEELEKKEKELEQ-------KQQ 124
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 302 MMEEVEKLCDRLELASLQCLnETLTSCTKEVGKAALEKQIE-----EINEQIRKEKEEAEARMRQASKNT 366
Cdd:PRK12704  125 ELEKKEEELEELIEEQLQEL-ERISGLTAEEAKEILLEKVEeearhEAAVLIKEIEEEAKEEADKKAKEI 193
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
378-434 5.10e-03

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 35.28  E-value: 5.10e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1380941522  378 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSLQK 434
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
232-377 5.19e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 39.47  E-value: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1380941522 232 QEAKEKQRQAELE---AARLAKEKEEEEVRQQALLAKKEKDI--QKKAIKKERQKLRnscKTWNHFSDNEAERVKMMEEV 306
Cdd:COG2268   251 AEERREAETARAEaeaAYEIAEANAEREVQRQLEIAEREREIelQEKEAEREEAELE---ADVRKPAEAEKQAAEAEAEA 327
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1380941522 307 EKLCDRLEL----ASLQCLNETLtsctKEVGKAALEKQIEEINEQIRKEKEEAearMRQASKNTEKSTGGGGNGS 377
Cdd:COG2268   328 EAEAIRAKGlaeaEGKRALAEAW----NKLGDAAILLMLIEKLPEIAEAAAKP---LEKIDKITIIDGGNGGNGA 395
 
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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