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Conserved domains on  [gi|193788632|ref|NP_001123359|]
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dnaJ homolog subfamily C member 2 isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ZUO1 super family cl34965
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-361 1.50e-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: 212.97  E-value: 1.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  75 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269   31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 155 RAFNSVDptFDNSVPS-KSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269  108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 234 EKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAK---- 309
Cdd:COG5269  186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAAlkgk 265

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193788632 310 -EKQRQAELEAARLAKEKEEEevrqqallaKKEKDIQKKAIKKERQKLRNSCK 361
Cdd:COG5269  266 aEAKNKAEIEAEALASATAVK---------KKAKEVMKKALKMEKKAIKNAAK 309
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 500-547 2.40e-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: 2.40e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 193788632 500 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELV 547
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
zuotin_NTD super family cl48853
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-49 8.70e-04

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


The actual alignment was detected with superfamily member cd23953:

Pssm-ID: 467935  Cd Length: 38  Bit Score: 37.10  E-value: 8.70e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 193788632  13 TAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASAS 49
Cdd:cd23953    2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRTFS 38
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 400-453 1.03e-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: 37.17  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193788632 400 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 453
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-361 1.50e-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: 212.97  E-value: 1.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  75 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269   31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 155 RAFNSVDptFDNSVPS-KSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269  108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 234 EKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAK---- 309
Cdd:COG5269  186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAAlkgk 265

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193788632 310 -EKQRQAELEAARLAKEKEEEevrqqallaKKEKDIQKKAIKKERQKLRNSCK 361
Cdd:COG5269  266 aEAKNKAEIEAEALASATAVK---------KKAKEVMKKALKMEKKAIKNAAK 309
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 88-158 4.20e-14

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 67.11  E-value: 4.20e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193788632   88 DHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
87-153 1.13e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 59.94  E-value: 1.13e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193788632    87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 153
Cdd:smart00271   1 TDYYEILGVPR---DASLDEIKKAYRKLALKYHPDKNPGD----KEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 88-150 1.62e-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: 59.48  E-value: 1.62e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193788632  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257    1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-157 2.32e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 62.47  E-value: 2.32e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193788632  87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:PRK10767   4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 500-547 2.40e-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: 2.40e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 193788632 500 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELV 547
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
498-549 1.05e-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: 1.05e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 193788632   498 FTPWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELVEM 549
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, ...
 500-546 2.94e-08

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


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 49.81  E-value: 2.94e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 193788632  500 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMKRYKEL 546
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-49 8.70e-04

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


Pssm-ID: 467935  Cd Length: 38  Bit Score: 37.10  E-value: 8.70e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 193788632  13 TAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASAS 49
Cdd:cd23953    2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRTFS 38
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 400-453 1.03e-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: 37.17  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193788632 400 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 453
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
399-455 2.79e-03

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 2.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 193788632   399 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSLQK 455
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
HpsJ_fam NF038305
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ...
 306-398 4.26e-03

HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.


Pssm-ID: 468465 [Multi-domain]  Cd Length: 230  Bit Score: 39.10  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 306 QEAKEKQRQAELEAARLAKEKEE----EEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKIEEINE-QIRKEKEEAEarm 380
Cdd:NF038305 120 QETQLQQQLNQLQAQTSPQQLNQllksEQKQGQALASGQLPEEQKEQLQQFKSNPQALDKFLAQQLtQIRTQAEEAE--- 196

                         90
                 ....*....|....*...
gi 193788632 381 RQASKNTEKSTGGGGNGS 398
Cdd:NF038305 197 KQARLEALKSSLRIGLGS 214
 
Name Accession Description Interval E-value
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 75-361 1.50e-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: 212.97  E-value: 1.50e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  75 MLKTLDPKDWKNQDHYAVLGLGHVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEpikEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:COG5269   31 LYTREDFKNWKKVDLYALLGLSKYRTKAIPPQILKAHKKKVYKYHPDKTAAGGN---KGCDEFFKLIQKAREVLGDRKLR 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 155 RAFNSVDptFDNSVPS-KSEAKDNFFEVFTPVFERNSRWSNKKNVPKLGDMNSSFEDVDIFYSFWYNFDSWREFSYLDEE 233
Cdd:COG5269  108 LQYDSND--FDADVPPpRIYTPDEFFEVWEPVFEREARFSKKQPVPSLGPSDSSLKEVEEFYEFWSNFDSWRTFEPLDED 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 234 EKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRTLVDNAYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAK---- 309
Cdd:COG5269  186 YPDDMEERDRKRYSEAKNREKRAKLKNQDNARLKRLVQIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAAlkgk 265

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193788632 310 -EKQRQAELEAARLAKEKEEEevrqqallaKKEKDIQKKAIKKERQKLRNSCK 361
Cdd:COG5269  266 aEAKNKAEIEAEALASATAVK---------KKAKEVMKKALKMEKKAIKNAAK 309
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 88-158 4.20e-14

DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is thought that this domain mediates the interaction. DnaJ-domain is therefore part of a chaperone (protein folding) system. The T-antigens, although not in Prosite are confirmed as DnaJ containing domains from literature.


Pssm-ID: 395170 [Multi-domain]  Cd Length: 63  Bit Score: 67.11  E-value: 4.20e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193788632   88 DHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaagEPIKEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:pfam00226   1 DYYEILGVSP---DASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ smart00271
DnaJ molecular chaperone homology domain;
87-153 1.13e-11

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 59.94  E-value: 1.13e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193788632    87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAgepiKEGDNDYFTCITKAYEMLSDPVK 153
Cdd:smart00271   1 TDYYEILGVPR---DASLDEIKKAYRKLALKYHPDKNPGD----KEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 88-150 1.62e-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: 59.48  E-value: 1.62e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193788632  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRkaagePIKEGDNDYFTCITKAYEMLSD 150
Cdd:cd06257    1 DYYDILG---VPPDASDEEIKKAYRKLALKYHPDKN-----PDDPEAEEKFKEINEAYEVLSD 55
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
87-157 3.27e-11

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 59.73  E-value: 3.27e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193788632  87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaaGEPIKEGDNDYFTCITKAYEMLSDPVKRRAF 157
Cdd:COG2214    5 KDHYAVLGVPP---DASLEEIRQAYRRLAKLLHPDR----GGELKALAEELFQRLNEAYEVLSDPERRAEY 68
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 88-157 6.83e-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: 60.49  E-value: 6.83e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193788632  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:COG0484    1 DYYEILG---VSRDASAEEIKKAYRKLAKKYHPDRNpgdPEAEEKFKE--------INEAYEVLSDPEKRAAY 62
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 87-157 2.32e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 62.47  E-value: 2.32e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 193788632  87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAF 157
Cdd:PRK10767   4 RDYYEVLG---VSRNASEDEIKKAYRKLAMKYHPDRNpgdKEAEEKFKE--------IKEAYEVLSDPQKRAAY 66
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 500-547 2.40e-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: 2.40e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 193788632 500 PWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELV 547
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 87-209 3.26e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 62.12  E-value: 3.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDK----RKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDP 162
Cdd:PRK14282   4 KDYYEILG---VSRNATQEEIKRAYKRLVKEWHPDRhpenRKEAEQKFKE--------IQEAYEVLSDPQKRAMYDRFGY 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193788632 163 TFDNSVPSKSEAKDNFFE-------------VFTPVFERNSRWSNKKNVPKLG-DMNSSFE 209
Cdd:PRK14282  73 VGEQPPYQETESGGGFFEdifkdfenifnrdIFDIFFGERRTQEEQREYARRGeDIRYEIE 133
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
498-549 1.05e-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: 1.05e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 193788632   498 FTPWTTEEQKLLEQALKTYPVNtpeRWEKIAEAVPGRTKKDCMKRYKELVEM 549
Cdd:smart00717   1 KGEWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLKP 49
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 87-217 1.08e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 57.47  E-value: 1.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFNSvdptF 164
Cdd:PRK14291   3 KDYYEILG---VSRNATQEEIKKAYRRLARKYHPDfnKNPEAEEKFKE--------INEAYQVLSDPEKRKLYDQ----F 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 193788632 165 DNSVPSKSEAKDNFFEVFTPVFERNsrwsnkknvpkLGDMnssFEDVDIFYSF 217
Cdd:PRK14291  68 GHAAFSGSGQQQQGQEGFSDFGGGN-----------IEDI---LEDVFDIFGF 106
PRK14295 PRK14295
molecular chaperone DnaJ;
82-167 2.08e-08

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 56.40  E-value: 2.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  82 KDWKNQDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKaaGEPIKEgdnDYFTCITKAYEMLSDPVKRRAFNSVD 161
Cdd:PRK14295   4 KDYIEKDYYKVLG---VPKDATEAEIKKAYRKLAREYHPDANK--GDAKAE---ERFKEISEAYDVLSDEKKRKEYDEAR 75


                 ....*.
gi 193788632 162 PTFDNS 167
Cdd:PRK14295  76 SLFGNG 81
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 86-210 2.57e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 56.25  E-value: 2.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  86 NQDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRRAFNSVDPT 163
Cdd:PRK14276   3 NTEYYDRLG---VSKDASQDEIKKAYRKLSKKYHPDINKEPGaeEKYKE--------VQEAYETLSDPQKRAAYDQYGAA 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193788632 164 ---------------FDNsvpskSEAKDNFFEVFTPVFERNSRWSNkKNVPKLGD-----MNSSFED 210
Cdd:PRK14276  72 ganggfgggaggfggFDG-----SGGFGGFEDIFSSFFGGGGARRN-PNAPRQGDdlqyrVNLDFEE 132
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
 500-546 2.94e-08

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


Pssm-ID: 459731 [Multi-domain]  Cd Length: 46  Bit Score: 49.81  E-value: 2.94e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 193788632  500 PWTTEEQKLLEQALKTYPvntpERWEKIAEAVPGRTKKDCMKRYKEL 546
Cdd:pfam00249   3 PWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRWQNY 45
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 87-159 3.39e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 55.33  E-value: 3.39e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193788632  87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKegdndyFTCITKAYEMLSDPVKRRAFNS 159
Cdd:PRK14299   4 KDYYAILG---VPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEK------FKEINEAYTVLSDPEKRRIYDT 67
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 86-158 3.77e-08

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 55.98  E-value: 3.77e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193788632  86 NQDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKrkaagepikEGDNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PTZ00037  27 NEKLYEVLNLSK---DCTTSEIKKAYRKLAIKHHPDK---------GGDPEKFKEISRAYEVLSDPEKRKIYD 87
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 88-155 5.27e-08

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 55.06  E-value: 5.27e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPD--KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRR 155
Cdd:PRK14278   4 DYYGLLG---VSRNASDAEIKRAYRKLARELHPDvnPDEEAQEKFKE--------ISVAYEVLSDPEKRR 62
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 86-158 1.15e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 54.23  E-value: 1.15e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 193788632  86 NQDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14286   3 ERSYYDILG---VSKSANDEEIKSAYRKLAIKYHPDKNKGNKES-----EEKFKEATEAYEILRDPKKRQAYD 67
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 87-158 3.17e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 52.54  E-value: 3.17e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193788632  87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAGEpikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14298   5 RDYYEILGLSK---DASVEDIKKAYRKLAMKYHPDKNKEPDA------EEKFKEISEAYAVLSDAEKRAQYD 67
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 87-158 3.77e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 52.50  E-value: 3.77e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193788632  87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14277   5 KDYYEILG---VDRNATEEEIKKAYRRLAKKYHPDLNpgdKEAEQKFKE--------INEAYEILSDPQKRAQYD 68
PRK14297 PRK14297
molecular chaperone DnaJ;
86-154 4.84e-07

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 52.09  E-value: 4.84e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193788632  86 NQDHYAVLGLghvRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKR 154
Cdd:PRK14297   3 SKDYYEVLGL---EKGASDDEIKKAFRKLAIKYHPDKNkgnKEAEEKFKE--------INEAYQVLSDPQKK 63
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 87-187 5.14e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 52.07  E-value: 5.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEGdndyftciTKAYEMLSDPVKRRAFNSVDPT 163
Cdd:PRK14294   4 RDYYEILG---VTRDASEEEIKKSYRKLAMKYHPDRNpgdKEAEELFKEA--------AEAYEVLSDPKKRGIYDQYGHE 72

                         90       100
                 ....*....|....*....|....*
gi 193788632 164 -FDNSVPSKSEAKDNFFEVFTPVFE 187
Cdd:PRK14294  73 gLSGTGFSGFSGFDDIFSSFGDIFE 97
PRK14280 PRK14280
molecular chaperone DnaJ;
87-210 7.56e-07

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 51.65  E-value: 7.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAG--EPIKEgdndyftcITKAYEMLSDPVKRR---AFNSVD 161
Cdd:PRK14280   4 RDYYEVLGVSK---SASKDEIKKAYRKLSKKYHPDINKEEGadEKFKE--------ISEAYEVLSDDQKRAqydQFGHAG 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 193788632 162 P--TFDNSVPSKSEAKDNF-FE-VFTPVFERNSRwSNKKNVPKLGD-----MNSSFED 210
Cdd:PRK14280  73 PnqGFGGGGFGGGDFGGGFgFEdIFSSFFGGGGR-RRDPNAPRQGAdlqytMTLTFEE 129
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 88-158 9.84e-07

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 51.38  E-value: 9.84e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193788632  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKAAGEPIKEgdndyFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14284   2 DYYTILG---VSKTASPEEIKKAYRKLAVKYHPDKNPGDAEAEKR-----FKEVSEAYEVLSDAQKRESYD 64
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 87-158 1.69e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 50.58  E-value: 1.69e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193788632  87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14281   3 RDYYEVLGVSR---SADKDEIKKAYRKLALKYHPDKNpdnKEAEEHFKE--------VNEAYEVLSNDDKRRRYD 66
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 87-158 1.97e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 50.31  E-value: 1.97e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 193788632  87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPD----KRKAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14290   3 KDYYKILG---VDRNASQEDIKKAFRELAKKWHPDlhpgNKAEAEEKFKE--------ISEAYEVLSDPQKRRQYD 67
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 88-154 3.72e-06

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 49.50  E-value: 3.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193788632  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKaagepiKEGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14292   3 DYYELLG---VSRTASADEIKSAYRKLALKYHPDRNK------EKGAAEKFAQINEAYAVLSDAEKR 60
PRK14293 PRK14293
molecular chaperone DnaJ;
88-154 1.08e-05

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 47.68  E-value: 1.08e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193788632  88 DHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKRKaagEPikeGDNDYFTCITKAYEMLSDPVKR 154
Cdd:PRK14293   4 DYYEILG---VSRDADKDELKRAYRRLARKYHPDVNK---EP---GAEDRFKEINRAYEVLSDPETR 61
PRK14289 PRK14289
molecular chaperone DnaJ;
87-158 1.87e-05

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 47.13  E-value: 1.87e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 193788632  87 QDHYAVLGlghVRYKATQRQIKAAHKAMVLKHHPDKR---KAAGEPIKEgdndyftcITKAYEMLSDPVKRRAFN 158
Cdd:PRK14289   5 RDYYEVLG---VSKTATVDEIKKAYRKKAIQYHPDKNpgdKEAEEKFKE--------AAEAYDVLSDPDKRSRYD 68
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
87-151 8.16e-05

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 40.94  E-value: 8.16e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 193788632  87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDkRKAAGEP--IKEGDNDYFTCITKAYEMLSDP 151
Cdd:COG1076    4 DDAFELLGLPP---DADDAELKRAYRKLQREHHPD-RLAAGLPeeEQRLALQKAAAINEAYETLKDP 66
SANT_CDC5_II cd11659
SANT/myb-like DNA-binding domain of Cell Division Cycle 5-Like Protein repeat II; In humans, ...
 494-548 1.44e-04

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


Pssm-ID: 212557 [Multi-domain]  Cd Length: 53  Bit Score: 39.60  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 193788632 494 PYTDFTPWTTEEQKLLEQALKTYpvntPERWEKIAEAVpGRTKKDCMKRYKELVE 548
Cdd:cd11659    1 PSIKKTEWTREEDEKLLHLAKLL----PTQWRTIAPIV-GRTAQQCLERYNKLLD 50
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 87-158 1.90e-04

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 43.83  E-value: 1.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 193788632  87 QDHYAVLGLGHvryKATQRQIKAAHKAMVLKHHPDKRKAAGEPikegdNDYFTCITKAYEMLSDPVKRRAFN 158
Cdd:PRK14285   3 RDYYEILGLSK---GASKDEIKKAYRKIAIKYHPDKNKGNKEA-----ESIFKEATEAYEVLIDDNKRAQYD 66
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
306-379 4.11e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 42.94  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 306 QEAKEKQRQAELE---AARLAKEKEEEEVRQQALLAKKEKDI---QKKAIKKERQKLRNSCKIEEINEQIRKEKEEAEAR 379
Cdd:COG2268  251 AEERREAETARAEaeaAYEIAEANAEREVQRQLEIAEREREIelqEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAE 330
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 230-379 5.69e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 5.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  230 LDEEEKEKAECRDERRWIEKQNRATRAqrkkeEMNRIRTLvdnaYSCDPRIKKFKEEEKAKKEAEKKAKAEAKRKEQE-A 308
Cdd:pfam17380 301 LRQEKEEKAREVERRRKLEEAEKARQA-----EMDRQAAI----YAEQERMAMERERELERIRQEERKRELERIRQEEiA 371

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 193788632  309 KEKQRQAELEAARLAKEKEEEEVRQQALLAKKEkdiqkKAIKKERQKLRNSCKIEEinEQIRKEKEEAEAR 379
Cdd:pfam17380 372 MEISRMRELERLQMERQQKNERVRQELEAARKV-----KILEEERQRKIQQQKVEM--EQIRAEQEEARQR 435
zuotin_NTD cd23953
N-terminal domain of fungal ribosome associated J-protein zuotin and similar proteins; Zuotin, ...
 13-49 8.70e-04

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


Pssm-ID: 467935  Cd Length: 38  Bit Score: 37.10  E-value: 8.70e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 193788632  13 TAITHALTSASTLCQVEPVGRWFEAFVKRRNRNASAS 49
Cdd:cd23953    2 SAVVHASLSAPVTRKLEPVGPAFLAHARRKLHNRTFS 38
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
 400-453 1.03e-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: 37.17  E-value: 1.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 193788632 400 NWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSL 453
Cdd:cd00167    1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELP-------GRTPKQCRERWRNL 44
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 306-385 1.60e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 1.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 306 QEAKEKQRQAELEAARL---AKEKEEEEVRQQALLAKK-EKDIQKKAIKKERQKLRNSCKIEEINEQIRKEKEEAEARMR 381
Cdd:PRK09510 125 KQAALKQKQAEEAAAKAaaaAKAKAEAEAKRAAAAAKKaAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAE 204


                 ....
gi 193788632 382 QASK 385
Cdd:PRK09510 205 AEAK 208
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 306-389 1.82e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 306 QEAKEKQRQAELEAARLAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKIEEINEQIRKEKEEAEARMRQASK 385
Cdd:PRK09510  95 KQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAE 174


                 ....
gi 193788632 386 NTEK 389
Cdd:PRK09510 175 AAKK 178
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
399-455 2.79e-03

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 2.79e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 193788632   399 KNWSEDDLQLLIKAVNLFPAGtnsRWEVIANYMNihsssgvKRTAKDVIGKAKSLQK 455
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELP-------GRTAEQCRERWRNLLK 48
HpsJ_fam NF038305
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ...
 306-398 4.26e-03

HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.


Pssm-ID: 468465 [Multi-domain]  Cd Length: 230  Bit Score: 39.10  E-value: 4.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632 306 QEAKEKQRQAELEAARLAKEKEE----EEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKIEEINE-QIRKEKEEAEarm 380
Cdd:NF038305 120 QETQLQQQLNQLQAQTSPQQLNQllksEQKQGQALASGQLPEEQKEQLQQFKSNPQALDKFLAQQLtQIRTQAEEAE--- 196

                         90
                 ....*....|....*...
gi 193788632 381 RQASKNTEKSTGGGGNGS 398
Cdd:NF038305 197 KQARLEALKSSLRIGLGS 214
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 306-385 5.66e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 37.71  E-value: 5.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  306 QEAKEKQRQAELEAARLAKE---KEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKieEINEQIRKEKEEAEARMRQ 382
Cdd:pfam05672  35 LEKEEEERLRKEELRRRAEEeraRREEEARRLEEERRREEEERQRKAEEEAEEREQREQ--EEQERLQKQKEEAEAKARE 112


                  ...
gi 193788632  383 ASK 385
Cdd:pfam05672 113 EAE 115
PTZ00121 PTZ00121
MAEBL; Provisional
 230-386 6.55e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 6.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  230 LDEEEKEKAECRDERRWIEKQNRATRAQRKKEEMNRIRtlvdnayscdprikkfkeeEKAKKEAEKKAKAEAKRKEQEAK 309
Cdd:PTZ00121 1625 LKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIK-------------------AAEEAKKAEEDKKKAEEAKKAEE 1685

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 193788632  310 EKQRQAEleaarlAKEKEEEEVRQQALLAKKEKDIQKKAIKKERQKLRNSCKIEEINEQIRKEKEEA-EARMRQASKN 386
Cdd:PTZ00121 1686 DEKKAAE------ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAeEAKKDEEEKK 1757
PTZ00121 PTZ00121
MAEBL; Provisional
 236-389 7.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 7.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  236 EKAECRDERRWIEKQNRATRAQRKKEEMNRIRTlvdnayscdpRIKKFKEEEKAKKEAEKKAKAEAKRKEQEAKEKQRQA 315
Cdd:PTZ00121 1590 EEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA----------EELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN 1659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 193788632  316 ELEAARLAKEKEEEevRQQALLAKKEKDIQKKAIKKERQKLRNSCKIEEIN----------EQIRKEKEEAEARMRQASK 385
Cdd:PTZ00121 1660 KIKAAEEAKKAEED--KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKkkeaeekkkaEELKKAEEENKIKAEEAKK 1737


                  ....
gi 193788632  386 NTEK 389
Cdd:PTZ00121 1738 EAEE 1741
 
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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