NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|21361912|ref|NP_071760|]
View 

dnaJ homolog subfamily C member 1 precursor [Homo sapiens]

Protein Classification

DnaJ homolog subfamily C member 1( domain architecture ID 10446272)

DnaJ homolog subfamily C member 1 (DNAJC1) may modulate protein synthesis

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
65-126 9.60e-24

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: 94.46  E-value: 9.60e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361912    65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKN-KDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
496-543 8.40e-07

'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: 45.64  E-value: 8.40e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21361912 496 PWTQNQQKLLELALQQYPRGssdRWDKIARCVPSKSKEDCIARYKLLV 543
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
329-375 2.53e-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: 36.01  E-value: 2.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21361912 329 EWTEEDLSQLTRSMVKFPggtPGRWEKIAHELG-RSVTDVTTKAKQLK 375
Cdd:cd00167   1 PWTEEEDELLLEAVKKYG---KNNWEKIAKELPgRTPKQCRERWRNLL 45
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
65-126 9.60e-24

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: 94.46  E-value: 9.60e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361912    65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKN-KDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
66-126 1.79e-20

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 93.05  E-value: 1.79e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361912    66 FYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:TIGR02349   2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYD 62
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
65-184 8.20e-20

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: 85.91  E-value: 8.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361912  65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYDDILINGLPDWRQPVFYY 143
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21361912 144 RRVRKMSNAELALLLFIILTVGHYAVVWSIYLEKQLDELLS 184
Cdd:COG0484  81 AAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLL 121
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
65-126 1.37e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 87.60  E-value: 1.37e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
65-118 8.10e-18

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: 77.20  E-value: 8.10e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21361912  65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKD-ENAETQFRQLVAIYEVLKD 118
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
DnaJ smart00271
DnaJ molecular chaperone homology domain;
65-121 5.26e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.96  E-value: 5.26e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 21361912     65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKD--ENAETQFRQLVAIYEVLKDDER 121
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
65-126 1.93e-15

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 78.71  E-value: 1.93e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYD 67
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
496-543 8.40e-07

'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: 45.64  E-value: 8.40e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21361912 496 PWTQNQQKLLELALQQYPRGssdRWDKIARCVPSKSKEDCIARYKLLV 543
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
495-544 6.17e-06

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 43.37  E-value: 6.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 21361912    495 EPWTQNQQKLLELALQQYPRGssdRWDKIARCVPSKSKEDCIARYKLLVE 544
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLK 48
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
494-539 8.20e-05

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: 40.18  E-value: 8.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 21361912   494 EEPWTQNQQKLLELALQQYPrgssDRWDKIARCVPSKSKEDCIARY 539
Cdd:pfam00249   1 RGPWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRW 42
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
475-539 1.88e-04

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 44.11  E-value: 1.88e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361912 475 EQNESSDEESLRKERARSAEEPWT-QNQQKLLElALQQYprgsSDRWDKIARCVPSKSKEDCIARY 539
Cdd:COG5259 260 PSEFTSSDFKPVTISLLIRDKNWSrQELLLLLE-GIEMY----GDDWDKVARHVGTKTKEQCILHF 320
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
329-375 2.53e-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: 36.01  E-value: 2.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21361912 329 EWTEEDLSQLTRSMVKFPggtPGRWEKIAHELG-RSVTDVTTKAKQLK 375
Cdd:cd00167   1 PWTEEEDELLLEAVKKYG---KNNWEKIAKELPgRTPKQCRERWRNLL 45
 
Name Accession Description Interval E-value
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
65-126 9.60e-24

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: 94.46  E-value: 9.60e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361912    65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKN-KDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDKNpGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
66-126 1.79e-20

chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the DnaK-DnaJ-GrpE chaperone system. The three components typically are encoded by consecutive genes. DnaJ homologs occur in many genomes, typically not near DnaK and GrpE-like genes; most such genes are not included by this family. Eukaryotic (mitochondrial and chloroplast) forms are not included in the scope of this family.


Pssm-ID: 274090 [Multi-domain]  Cd Length: 354  Bit Score: 93.05  E-value: 1.79e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361912    66 FYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:TIGR02349   2 YYEILGVSKDASEEEIKKAYRKLAKKYHPDRNKDKEAEEKFKEINEAYEVLSDPEKRAQYD 62
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
65-184 8.20e-20

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: 85.91  E-value: 8.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361912  65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYDDILINGLPDWRQPVFYY 143
Cdd:COG0484   1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDRNPgDPEAEEKFKEINEAYEVLSDPEKRAAYDRFGHAAELLLATELAES 80
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 21361912 144 RRVRKMSNAELALLLFIILTVGHYAVVWSIYLEKQLDELLS 184
Cdd:COG0484  81 AAAEAAAAEAKEEAAEAGASEYEAIAEEASQLRLASLLLLL 121
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
65-126 1.37e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 87.60  E-value: 1.37e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14298   6 DYYEILGLSKDASVEDIKKAYRKLAMKYHPDKNKEPDAEEKFKEISEAYAVLSDAEKRAQYD 67
PRK14280 PRK14280
molecular chaperone DnaJ;
65-126 5.14e-18

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 85.93  E-value: 5.14e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14280   5 DYYEVLGVSKSASKDEIKKAYRKLSKKYHPDINKEEGADEKFKEISEAYEVLSDDQKRAQYD 66
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
65-118 8.10e-18

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: 77.20  E-value: 8.10e-18
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21361912  65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKD-ENAETQFRQLVAIYEVLKD 118
Cdd:cd06257   1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDKNPDdPEAEEKFKEINEAYEVLSD 55
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
63-126 9.87e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 84.81  E-value: 9.87e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361912   63 QLNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK10767   3 KRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDRNPgDKEAEEKFKEIKEAYEVLSDPQKRAAYD 67
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
65-126 4.33e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 83.34  E-value: 4.33e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14283   6 DYYEVLGVDRNADKKEIKKAYRKLARKYHPDVSEEEGAEEKFKEISEAYAVLSDDEKRQRYD 67
DnaJ smart00271
DnaJ molecular chaperone homology domain;
65-121 5.26e-17

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 74.96  E-value: 5.26e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 21361912     65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKD--ENAETQFRQLVAIYEVLKDDER 121
Cdd:smart00271   2 DYYEILGVPRDASLDEIKKAYRKLALKYHPDKNPGdkEEAEEKFKEINEAYEVLSDPEK 60
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
63-126 1.70e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 81.29  E-value: 1.70e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361912   63 QLNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14276   3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPDINKEPGAEEKYKEVQEAYETLSDPQKRAAYD 66
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
65-124 1.77e-16

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 73.50  E-value: 1.77e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21361912  65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDE-NAETQFRQLVAIYEVLKDDERRQR 124
Cdd:COG5407   1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDRNKGDpKAEERFKEINEAYELLSDAEKRAR 61
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
65-126 3.30e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 80.48  E-value: 3.30e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14278   4 DYYGLLGVSRNASDAEIKRAYRKLARELHPDVNPDEEAQEKFKEISVAYEVLSDPEKRRIVD 65
PRK14293 PRK14293
molecular chaperone DnaJ;
65-126 3.72e-16

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 80.42  E-value: 3.72e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14293   4 DYYEILGVSRDADKDELKRAYRRLARKYHPDVNKEPGAEDRFKEINRAYEVLSDPETRARYD 65
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
62-126 4.70e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 79.79  E-value: 4.70e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361912   62 VQLNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDE-NAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14301   2 SQRDYYEVLGVSRDASEDEIKKAYRKLALQYHPDRNPDNpEAEQKFKEAAEAYEVLRDAEKRARYD 67
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
65-126 5.97e-16

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 73.21  E-value: 5.97e-16
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361912  65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDEN--AETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:COG2214   6 DHYAVLGVPPDASLEEIRQAYRRLAKLLHPDRGGELKalAEELFQRLNEAYEVLSDPERRAEYD 69
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
64-126 8.49e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 79.16  E-value: 8.49e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361912   64 LNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14292   2 MDYYELLGVSRTASADEIKSAYRKLALKYHPDRNKEKGAAEKFAQINEAYAVLSDAEKRAHYD 64
PRK14295 PRK14295
molecular chaperone DnaJ;
57-127 9.85e-16

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 79.12  E-value: 9.85e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   57 DLVEEvqlNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYDD 127
Cdd:PRK14295   5 DYIEK---DYYKVLGVPKDATEAEIKKAYRKLAREYHPDANKgDAKAEERFKEISEAYDVLSDEKKRKEYDE 73
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
65-126 1.29e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 78.70  E-value: 1.29e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKD-ENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14281   4 DYYEVLGVSRSADKDEIKKAYRKLALKYHPDKNPDnKEAEEHFKEVNEAYEVLSNDDKRRRYD 66
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
65-126 1.93e-15

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 78.71  E-value: 1.93e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:NF037946   6 DYYEVLGVDRDADDQEIKKAFRKLAKKYHPDRNKAPDAAEIFAEINEAYEVLSNPEKRANYD 67
PRK14279 PRK14279
molecular chaperone DnaJ;
60-127 8.70e-15

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 76.31  E-value: 8.70e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21361912   60 EEVQLNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYDD 127
Cdd:PRK14279   5 EWVEKDFYKELGVSSDASAEEIKKAYRKLARELHPDANPgDPAAEERFKAVSEAHDVLSDPAKRKEYDE 73
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
66-126 1.58e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 75.19  E-value: 1.58e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   66 FYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14294   6 YYEILGVTRDASEEEIKKSYRKLAMKYHPDRNPgDKEAEELFKEAAEAYEVLSDPKKRGIYD 67
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
65-126 1.88e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 75.05  E-value: 1.88e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14300   4 DYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKKFKEINAAYDVLKDEQKRAAYD 65
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
64-126 2.20e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 74.88  E-value: 2.20e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361912   64 LNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14284   1 MDYYTILGVSKTASPEEIKKAYRKLAVKYHPDKNPgDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
66-126 2.84e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 74.64  E-value: 2.84e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   66 FYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14286   6 YYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKgNKESEEKFKEATEAYEILRDPKKRQAYD 67
PRK14297 PRK14297
molecular chaperone DnaJ;
65-126 3.23e-14

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 74.43  E-value: 3.23e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14297   5 DYYEVLGLEKGASDDEIKKAFRKLAIKYHPDKNKgNKEAEEKFKEINEAYQVLSDPQKKAQYD 67
PRK14289 PRK14289
molecular chaperone DnaJ;
65-126 1.47e-13

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 72.56  E-value: 1.47e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14289   6 DYYEVLGVSKTATVDEIKKAYRKKAIQYHPDKNPgDKEAEEKFKEAAEAYDVLSDPDKRSRYD 68
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
65-126 1.87e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 71.95  E-value: 1.87e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKD-ENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14285   4 DYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNKGnKEAESIFKEATEAYEVLIDDNKRAQYD 66
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
65-126 2.46e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 71.76  E-value: 2.46e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14277   6 DYYEILGVDRNATEEEIKKAYRRLAKKYHPDLNPgDKEAEQKFKEINEAYEILSDPQKRAQYD 68
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
65-126 3.89e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 70.95  E-value: 3.89e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14291   4 DYYEILGVSRNATQEEIKKAYRRLARKYHPDFNKNPEAEEKFKEINEAYQVLSDPEKRKLYD 65
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
65-126 4.96e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 70.81  E-value: 4.96e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14287   5 DYYEVLGVDRNASVDEVKKAYRKLARKYHPDVNKAPDAEDKFKEVKEAYDTLSDPQKKAHYD 66
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
65-126 8.16e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 69.20  E-value: 8.16e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14299   5 DYYAILGVPKNASQDEIKKAFKKLARKYHPDVNKSPGAEEKFKEINEAYTVLSDPEKRRIYD 66
PRK10266 PRK10266
curved DNA-binding protein;
65-128 5.24e-12

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 66.77  E-value: 5.24e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDI 128
Cdd:PRK10266   5 DYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSKEPDAEARFKEVAEAWEVLSDEQRRAEYDQL 68
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
66-139 2.43e-11

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 65.61  E-value: 2.43e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21361912   66 FYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENaetQFRQLVAIYEVLKDDERRQRYDDILINGLPDWRQP 139
Cdd:PTZ00037  30 LYEVLNLSKDCTTSEIKKAYRKLAIKHHPDKGGDPE---KFKEISRAYEVLSDPEKRKIYDEYGEEGLEGGEQP 100
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
65-127 2.70e-11

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 65.34  E-value: 2.70e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKD--ENAETQFRQLVAIYEVLKDDERRQRYDD 127
Cdd:PRK14290   4 DYYKILGVDRNASQEDIKKAFRELAKKWHPDLHPGnkAEAEEKFKEISEAYEVLSDPQKRRQYDQ 68
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
65-126 1.25e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 63.27  E-value: 1.25e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDK---NKDEnAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14282   5 DYYEILGVSRNATQEEIKRAYKRLVKEWHPDRhpeNRKE-AEQKFKEIQEAYEVLSDPQKRAMYD 68
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
65-126 3.54e-10

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 61.89  E-value: 3.54e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21361912   65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14296   5 DYYEVLGVSKTASEQEIRQAYRKLAKQYHPDLNKSPDAHDKMVEINEAADVLLDKDKRKQYD 66
PRK14288 PRK14288
molecular chaperone DnaJ;
62-126 8.29e-08

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 54.31  E-value: 8.29e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361912   62 VQLNFYQFLGVQQDASSADIRKAYRKLSLTLHPDKNK-DENAETQFRQLVAIYEVLKDDERRQRYD 126
Cdd:PRK14288   1 MELSYYEILEVEKHSNQETIKKSYRKLALKYHPDRNAgDKEAEEKFKLINEAYGVLSDEKKRALYD 66
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
496-543 8.40e-07

'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: 45.64  E-value: 8.40e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21361912 496 PWTQNQQKLLELALQQYPRGssdRWDKIARCVPSKSKEDCIARYKLLV 543
Cdd:cd00167   1 PWTEEEDELLLEAVKKYGKN---NWEKIAKELPGRTPKQCRERWRNLL 45
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
65-96 1.25e-06

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 46.33  E-value: 1.25e-06
                        10        20        30
                ....*....|....*....|....*....|..
gi 21361912  65 NFYQFLGVQQDASSADIRKAYRKLSLTLHPDK 96
Cdd:COG1076   5 DAFELLGLPPDADDAELKRAYRKLQREHHPDR 36
SANT smart00717
SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains;
495-544 6.17e-06

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


Pssm-ID: 197842 [Multi-domain]  Cd Length: 49  Bit Score: 43.37  E-value: 6.17e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 21361912    495 EPWTQNQQKLLELALQQYPRGssdRWDKIARCVPSKSKEDCIARYKLLVE 544
Cdd:smart00717   2 GEWTEEEDELLIELVKKYGKN---NWEKIAKELPGRTAEQCRERWRNLLK 48
Myb_DNA-binding pfam00249
Myb-like DNA-binding domain; This family contains the DNA binding domains from Myb proteins, ...
494-539 8.20e-05

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: 40.18  E-value: 8.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 21361912   494 EEPWTQNQQKLLELALQQYPrgssDRWDKIARCVPSKSKEDCIARY 539
Cdd:pfam00249   1 RGPWTPEEDELLLEAVEKLG----NRWKKIAKLLPGRTDNQCKNRW 42
RSC8 COG5259
RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / ...
475-539 1.88e-04

RSC chromatin remodeling complex subunit RSC8 [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227584 [Multi-domain]  Cd Length: 531  Bit Score: 44.11  E-value: 1.88e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21361912 475 EQNESSDEESLRKERARSAEEPWT-QNQQKLLElALQQYprgsSDRWDKIARCVPSKSKEDCIARY 539
Cdd:COG5259 260 PSEFTSSDFKPVTISLLIRDKNWSrQELLLLLE-GIEMY----GDDWDKVARHVGTKTKEQCILHF 320
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
66-143 4.72e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 43.24  E-value: 4.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21361912    66 FYQFLGVQQDASSADIRKAYRKLSLTLHPDKNKDENAETQFRQLVAIYEVLKDDERRQRYDDILINGLP--DWRQPVFYY 143
Cdd:PTZ00341  575 FYDILGVGVNADMKEISERYFKLAENYYPPKRSGNEGFHKFKKINEAYQILGDIDKKKMYNKFGYDGIKgvNFIHPSIFY 654
djlA PRK09430
co-chaperone DjlA;
67-96 6.55e-04

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 41.72  E-value: 6.55e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 21361912   67 YQFLGVQQDASSADIRKAYRKLSLTLHPDK 96
Cdd:PRK09430 203 YKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
PHA02624 PHA02624
large T antigen; Provisional
79-138 1.78e-03

large T antigen; Provisional


Pssm-ID: 222912 [Multi-domain]  Cd Length: 647  Bit Score: 41.12  E-value: 1.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21361912   79 ADIRKAYRKLSLTLHPDKNKDENaetQFRQLVAIYEVLKDDERRQR-------YDDILINGLPDWRQ 138
Cdd:PHA02624  28 PLMRKAYLRKCKEYHPDKGGDEE---KMKRLNSLYKKLQEGVKSARqsfgtqdSSEIPTYGTPEWEQ 91
SANT cd00167
'SWI3, ADA2, N-CoR and TFIIIB' DNA-binding domains. Tandem copies of the domain bind telomeric ...
329-375 2.53e-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: 36.01  E-value: 2.53e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 21361912 329 EWTEEDLSQLTRSMVKFPggtPGRWEKIAHELG-RSVTDVTTKAKQLK 375
Cdd:cd00167   1 PWTEEEDELLLEAVKKYG---KNNWEKIAKELPgRTPKQCRERWRNLL 45
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH