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Conserved domains on  [gi|398364465|ref|NP_012462|]
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Jem1p [Saccharomyces cerevisiae S288C]

Protein Classification

J domain-containing protein( domain architecture ID 11422315)

J domain-containing protein similar to molecular chaperone DnaJ, a protein that plays crucial roles in protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of Hsp70

CATH:  1.10.287.110
Gene Ontology:  GO:0006457
PubMed:  35729039|9644977|8016869|15170475
SCOP:  4000605

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 538-613 6.19e-27

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: 106.33  E-value: 6.19e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQesIHETMSQINEAYETLSDDDKRKEYDLSRSNPRR 613
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDR---NPGDPE--AEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL 71
 
Name Accession Description Interval E-value
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 538-613 6.19e-27

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: 106.33  E-value: 6.19e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQesIHETMSQINEAYETLSDDDKRKEYDLSRSNPRR 613
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDR---NPGDPE--AEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL 71
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 538-605 1.49e-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: 96.77  E-value: 1.49e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364465  538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhNDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 538-644 1.75e-22

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: 99.21  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465  538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhNDKQESiHETMSQINEAYETLSDDDKRKEYD-LSRSNPRRNTF 616
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDR-----NKDKEA-EEKFKEINEAYEVLSDPEKRAQYDqFGHAGFNGGGG 74

                          90       100
                  ....*....|....*....|....*...
gi 398364465  617 PQGpRQNNMFKNPGSGfPFGNGFKMNFG 644
Cdd:TIGR02349  75 GGG-GGFNGFDIGFFG-DFGDIFGDFFG 100
PRK14280 PRK14280
molecular chaperone DnaJ;
536-644 5.91e-21

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 95.17  E-value: 5.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYD-LSRSNPRRn 614
Cdd:PRK14280   3 KRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDI------NKEEGADEKFKEISEAYEVLSDDQKRAQYDqFGHAGPNQ- 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 398364465 615 TFPQGPRQNNMFknpGSGFPFGNGFKMNFG 644
Cdd:PRK14280  76 GFGGGGFGGGDF---GGGFGFEDIFSSFFG 102
DnaJ smart00271
DnaJ molecular chaperone homology domain;
537-600 3.96e-20

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 84.21  E-value: 3.96e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364465   537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanHNDKQESIHETMSQINEAYETLSDDDK 600
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDK----NPGDKEEAEEKFKEINEAYEVLSDPEK 60
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 538-597 1.72e-17

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: 76.43  E-value: 1.72e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhNDKQESIHETMSQINEAYETLSD 597
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDK-----NPDDPEAEEKFKEINEAYEVLSD 55
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
536-605 2.35e-15

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 78.71  E-value: 2.35e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:NF037946   4 KRDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDR------NKAPDAAEIFAEINEAYEVLSNPEKRANYD 67
 
Name Accession Description Interval E-value
DnaJ COG0484
DnaJ-class molecular chaperone with C-terminal Zn finger domain [Posttranslational ...
 538-613 6.19e-27

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: 106.33  E-value: 6.19e-27
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQesIHETMSQINEAYETLSDDDKRKEYDLSRSNPRR 613
Cdd:COG0484    1 DYYEILGVSRDASAEEIKKAYRKLAKKYHPDR---NPGDPE--AEEKFKEINEAYEVLSDPEKRAAYDRFGHAAEL 71
CbpA COG2214
Curved DNA-binding protein CbpA, contains a DnaJ-like domain [Transcription];
537-624 1.02e-24

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


Pssm-ID: 441816 [Multi-domain]  Cd Length: 91  Bit Score: 98.25  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanHNDKQESIHETMSQINEAYETLSDDDKRKEYDLSRSNPRRNTF 616
Cdd:COG2214    5 KDHYAVLGVPPDASLEEIRQAYRRLAKLLHPDR----GGELKALAEELFQRLNEAYEVLSDPERRAEYDRELGQSGKGSA 80


                 ....*...
gi 398364465 617 PQGPRQNN 624
Cdd:COG2214   81 SQPSAAAQ 88
DnaJ pfam00226
DnaJ domain; DnaJ domains (J-domains) are associated with hsp70 heat-shock system and it is ...
 538-605 1.49e-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: 96.77  E-value: 1.49e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364465  538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhNDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:pfam00226   1 DYYEILGVSPDASDEEIKKAYRKLALKYHPDK-----NPGDPEAEEKFKEINEAYEVLSDPEKRAIYD 63
DnaJ_bact TIGR02349
chaperone protein DnaJ; This model represents bacterial forms of DnaJ, part of the ...
 538-644 1.75e-22

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: 99.21  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465  538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhNDKQESiHETMSQINEAYETLSDDDKRKEYD-LSRSNPRRNTF 616
Cdd:TIGR02349   1 DYYEILGVSKDASEEEIKKAYRKLAKKYHPDR-----NKDKEA-EEKFKEINEAYEVLSDPEKRAQYDqFGHAGFNGGGG 74

                          90       100
                  ....*....|....*....|....*...
gi 398364465  617 PQGpRQNNMFKNPGSGfPFGNGFKMNFG 644
Cdd:TIGR02349  75 GGG-GGFNGFDIGFFG-DFGDIFGDFFG 100
PRK14280 PRK14280
molecular chaperone DnaJ;
536-644 5.91e-21

molecular chaperone DnaJ;


Pssm-ID: 237656 [Multi-domain]  Cd Length: 376  Bit Score: 95.17  E-value: 5.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYD-LSRSNPRRn 614
Cdd:PRK14280   3 KRDYYEVLGVSKSASKDEIKKAYRKLSKKYHPDI------NKEEGADEKFKEISEAYEVLSDDQKRAQYDqFGHAGPNQ- 75

                         90       100       110
                 ....*....|....*....|....*....|
gi 398364465 615 TFPQGPRQNNMFknpGSGFPFGNGFKMNFG 644
Cdd:PRK14280  76 GFGGGGFGGGDF---GGGFGFEDIFSSFFG 102
DnaJ smart00271
DnaJ molecular chaperone homology domain;
537-600 3.96e-20

DnaJ molecular chaperone homology domain;


Pssm-ID: 197617 [Multi-domain]  Cd Length: 60  Bit Score: 84.21  E-value: 3.96e-20
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 398364465   537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanHNDKQESIHETMSQINEAYETLSDDDK 600
Cdd:smart00271   1 TDYYEILGVPRDASLDEIKKAYRKLALKYHPDK----NPGDKEEAEEKFKEINEAYEVLSDPEK 60
PRK14277 PRK14277
chaperone protein DnaJ; Provisional
 535-644 5.42e-20

chaperone protein DnaJ; Provisional


Pssm-ID: 184599 [Multi-domain]  Cd Length: 386  Bit Score: 92.56  E-value: 5.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 535 PKKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDkikANHNDKQEsiHETMSQINEAYETLSDDDKRKEYD-LSRSNPRR 613
Cdd:PRK14277   3 AKKDYYEILGVDRNATEEEIKKAYRRLAKKYHPD---LNPGDKEA--EQKFKEINEAYEILSDPQKRAQYDqFGHAAFDP 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 398364465 614 NTFPQGPRQNNMFKNPGSGFPFGnGFKMNFG 644
Cdd:PRK14277  78 GGFGQGGFGQGGFGGGGFDFDFG-GFGDIFE 107
PRK14295 PRK14295
molecular chaperone DnaJ;
536-638 5.77e-20

molecular chaperone DnaJ;


Pssm-ID: 237665 [Multi-domain]  Cd Length: 389  Bit Score: 92.22  E-value: 5.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDkikANHNDKQESihETMSQINEAYETLSDDDKRKEYDLSRSNPRRNT 615
Cdd:PRK14295   8 EKDYYKVLGVPKDATEAEIKKAYRKLAREYHPD---ANKGDAKAE--ERFKEISEAYDVLSDEKKRKEYDEARSLFGNGG 82

                         90       100
                 ....*....|....*....|...
gi 398364465 616 FPQGPRqnnmfKNPGSGFPFGNG 638
Cdd:PRK14295  83 FRPGPG-----GGGGGGFNFDLG 100
PRK10767 PRK10767
chaperone protein DnaJ; Provisional
 536-605 2.04e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 236757 [Multi-domain]  Cd Length: 371  Bit Score: 90.59  E-value: 2.04e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQ-EsihETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK10767   3 KRDYYEVLGVSRNASEDEIKKAYRKLAMKYHPDR---NPGDKEaE---EKFKEIKEAYEVLSDPQKRAAYD 67
PRK14281 PRK14281
chaperone protein DnaJ; Provisional
 536-605 2.13e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237657 [Multi-domain]  Cd Length: 397  Bit Score: 90.64  E-value: 2.13e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQESIHetMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14281   2 KRDYYEVLGVSRSADKDEIKKAYRKLALKYHPDK---NPDNKEAEEH--FKEVNEAYEVLSNDDKRRRYD 66
SEC63 COG5407
Preprotein translocase subunit Sec63 [Intracellular trafficking, secretion, and vesicular ...
 538-603 2.61e-19

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


Pssm-ID: 444165 [Multi-domain]  Cd Length: 61  Bit Score: 81.97  E-value: 2.61e-19
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQesIHETMSQINEAYETLSDDDKRKE 603
Cdd:COG5407    1 DPYEVLGVAKTASADEIKKAYRKLAKKYHPDR---NKGDPK--AEERFKEINEAYELLSDAEKRAR 61
PRK14276 PRK14276
chaperone protein DnaJ; Provisional
 536-605 8.67e-19

chaperone protein DnaJ; Provisional


Pssm-ID: 237653 [Multi-domain]  Cd Length: 380  Bit Score: 88.61  E-value: 8.67e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDkikANHNDKQEsihETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14276   3 NTEYYDRLGVSKDASQDEIKKAYRKLSKKYHPD---INKEPGAE---EKYKEVQEAYETLSDPQKRAAYD 66
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
 536-605 3.32e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 87.13  E-value: 3.32e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14291   2 KKDYYEILGVSRNATQEEIKKAYRRLARKYHPDF------NKNPEAEEKFKEINEAYQVLSDPEKRKLYD 65
PRK14283 PRK14283
chaperone protein DnaJ; Provisional
 536-644 8.24e-18

chaperone protein DnaJ; Provisional


Pssm-ID: 184604 [Multi-domain]  Cd Length: 378  Bit Score: 85.65  E-value: 8.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDkikANHndkQESIHETMSQINEAYETLSDDDKRKEYDlsrsnprrnT 615
Cdd:PRK14283   4 KRDYYEVLGVDRNADKKEIKKAYRKLARKYHPD---VSE---EEGAEEKFKEISEAYAVLSDDEKRQRYD---------Q 68

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 398364465 616 FPQ----GPRQNNMFKN-------PGSGFPFGNGFKM-NFG 644
Cdd:PRK14283  69 FGHagmdGFSQEDIFNNinfedifQGFGFGIGNIFDMfGFG 109
PRK14282 PRK14282
chaperone protein DnaJ; Provisional
 536-605 1.17e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 184603 [Multi-domain]  Cd Length: 369  Bit Score: 85.23  E-value: 1.17e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQESiHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14282   3 KKDYYEILGVSRNATQEEIKRAYKRLVKEWHPDR---HPENRKEA-EQKFKEIQEAYEVLSDPQKRAMYD 68
DnaJ cd06257
DnaJ domain or J-domain. DnaJ/Hsp40 (heat shock protein 40) proteins are highly conserved and ...
 538-597 1.72e-17

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: 76.43  E-value: 1.72e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhNDKQESIHETMSQINEAYETLSD 597
Cdd:cd06257    1 DYYDILGVPPDASDEEIKKAYRKLALKYHPDK-----NPDDPEAEEKFKEINEAYEVLSD 55
PRK14298 PRK14298
chaperone protein DnaJ; Provisional
 536-644 7.28e-17

chaperone protein DnaJ; Provisional


Pssm-ID: 184612 [Multi-domain]  Cd Length: 377  Bit Score: 82.97  E-value: 7.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYDLSRSNPRRNT 615
Cdd:PRK14298   4 TRDYYEILGLSKDASVEDIKKAYRKLAMKYHPDK------NKEPDAEEKFKEISEAYAVLSDAEKRAQYDRFGHAGIDNQ 77

                         90       100
                 ....*....|....*....|....*....
gi 398364465 616 FpqgpRQNNMFKNPGSGfPFGNGFKMNFG 644
Cdd:PRK14298  78 Y----SAEDIFRGADFG-GFGDIFEMFFG 101
PRK14297 PRK14297
molecular chaperone DnaJ;
535-605 1.14e-16

molecular chaperone DnaJ;


Pssm-ID: 184611 [Multi-domain]  Cd Length: 380  Bit Score: 82.14  E-value: 1.14e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364465 535 PKKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQEsiHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14297   2 ASKDYYEVLGLEKGASDDEIKKAFRKLAIKYHPDK---NKGNKEA--EEKFKEINEAYQVLSDPQKKAQYD 67
PRK10266 PRK10266
curved DNA-binding protein;
537-618 1.47e-16

curved DNA-binding protein;


Pssm-ID: 182347 [Multi-domain]  Cd Length: 306  Bit Score: 81.02  E-value: 1.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKanHNDKQESIHEtmsqINEAYETLSDDDKRKEYD---LSRSNPRR 613
Cdd:PRK10266   4 KDYYAIMGVKPTDDLKTIKTAYRRLARKYHPDVSK--EPDAEARFKE----VAEAWEVLSDEQRRAEYDqlwQHRNDPQF 77


                 ....*
gi 398364465 614 NTFPQ 618
Cdd:PRK10266  78 NRQFQ 82
PRK14279 PRK14279
molecular chaperone DnaJ;
537-644 1.62e-16

molecular chaperone DnaJ;


Pssm-ID: 237655 [Multi-domain]  Cd Length: 392  Bit Score: 82.09  E-value: 1.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDkikANHNDKqeSIHETMSQINEAYETLSDDDKRKEYDLSRSNPRRNTF 616
Cdd:PRK14279   9 KDFYKELGVSSDASAEEIKKAYRKLARELHPD---ANPGDP--AAEERFKAVSEAHDVLSDPAKRKEYDETRRLFAGGGF 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 398364465 617 PQGprqnnmFKNPGSGF----PFGNGFKMNFG 644
Cdd:PRK14279  84 GGR------RFDGGGGFggfgTGGDGAEFNLN 109
PRK14290 PRK14290
chaperone protein DnaJ; Provisional
 537-605 1.94e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 172778 [Multi-domain]  Cd Length: 365  Bit Score: 81.52  E-value: 1.94e-16
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398364465 537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDkikANHNDKQESiHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14290   3 KDYYKILGVDRNASQEDIKKAFRELAKKWHPD---LHPGNKAEA-EEKFKEISEAYEVLSDPQKRRQYD 67
PRK14299 PRK14299
chaperone protein DnaJ; Provisional
 536-605 2.64e-16

chaperone protein DnaJ; Provisional


Pssm-ID: 237667 [Multi-domain]  Cd Length: 291  Bit Score: 79.98  E-value: 2.64e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14299   3 YKDYYAILGVPKNASQDEIKKAFKKLARKYHPDV------NKSPGAEEKFKEINEAYTVLSDPEKRRIYD 66
terminal_TopJ NF037946
terminal organelle assembly protein TopJ;
536-605 2.35e-15

terminal organelle assembly protein TopJ;


Pssm-ID: 468284 [Multi-domain]  Cd Length: 440  Bit Score: 78.71  E-value: 2.35e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:NF037946   4 KRDYYEVLGVDRDADDQEIKKAFRKLAKKYHPDR------NKAPDAAEIFAEINEAYEVLSNPEKRANYD 67
PRK14296 PRK14296
chaperone protein DnaJ; Provisional
 536-605 3.91e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237666 [Multi-domain]  Cd Length: 372  Bit Score: 77.68  E-value: 3.91e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14296   3 KKDYYEVLGVSKTASEQEIRQAYRKLAKQYHPDL------NKSPDAHDKMVEINEAADVLLDKDKRKQYD 66
DjlA COG1076
DnaJ domain-containing protein [Posttranslational modification, protein turnover, chaperones];
538-597 3.97e-15

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


Pssm-ID: 440694 [Multi-domain]  Cd Length: 75  Bit Score: 70.60  E-value: 3.97e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKANHNDK-QESIHETMSQINEAYETLSD 597
Cdd:COG1076    5 DAFELLGLPPDADDAELKRAYRKLQREHHPDRLAAGLPEEeQRLALQKAAAINEAYETLKD 65
PRK14292 PRK14292
chaperone protein DnaJ; Provisional
 538-644 5.35e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237662 [Multi-domain]  Cd Length: 371  Bit Score: 77.24  E-value: 5.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYDlsrsnpRRNTFP 617
Cdd:PRK14292   3 DYYELLGVSRTASADEIKSAYRKLALKYHPDR------NKEKGAAEKFAQINEAYAVLSDAEKRAHYD------RFGTAP 70

                         90       100
                 ....*....|....*....|....*...
gi 398364465 618 Q-GPRQNNMFKnpGSGFPFGNGFKMNFG 644
Cdd:PRK14292  71 GaGMPGGDPFG--GMGFDPMDIFEQLFG 96
PRK14294 PRK14294
chaperone protein DnaJ; Provisional
 536-605 6.59e-15

chaperone protein DnaJ; Provisional


Pssm-ID: 237664 [Multi-domain]  Cd Length: 366  Bit Score: 76.73  E-value: 6.59e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQEsiHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14294   3 KRDYYEILGVTRDASEEEIKKSYRKLAMKYHPDR---NPGDKEA--EELFKEAAEAYEVLSDPKKRGIYD 67
PRK14278 PRK14278
chaperone protein DnaJ; Provisional
 537-639 1.29e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237654 [Multi-domain]  Cd Length: 378  Bit Score: 75.86  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhNDKQESiHETMSQINEAYETLSDDDKRKEYDLSrSNPrrntf 616
Cdd:PRK14278   3 RDYYGLLGVSRNASDAEIKRAYRKLARELHPDV-----NPDEEA-QEKFKEISVAYEVLSDPEKRRIVDLG-GDP----- 70

                         90       100
                 ....*....|....*....|...
gi 398364465 617 pqgprqnnMFKNPGSGFPFGNGF 639
Cdd:PRK14278  71 --------LESAGGGGGGFGGGF 85
PRK14285 PRK14285
chaperone protein DnaJ; Provisional
 536-605 1.98e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172773 [Multi-domain]  Cd Length: 365  Bit Score: 75.41  E-value: 1.98e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKanHNDKQESIhetMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14285   2 KRDYYEILGLSKGASKDEIKKAYRKIAIKYHPDKNK--GNKEAESI---FKEATEAYEVLIDDNKRAQYD 66
PRK14293 PRK14293
molecular chaperone DnaJ;
538-605 2.05e-14

molecular chaperone DnaJ;


Pssm-ID: 237663 [Multi-domain]  Cd Length: 374  Bit Score: 75.41  E-value: 2.05e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14293   4 DYYEILGVSRDADKDELKRAYRRLARKYHPDV------NKEPGAEDRFKEINRAYEVLSDPETRARYD 65
PRK14300 PRK14300
chaperone protein DnaJ; Provisional
 537-605 2.93e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 172788 [Multi-domain]  Cd Length: 372  Bit Score: 74.67  E-value: 2.93e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398364465 537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKANHNDKQesihetMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14300   3 QDYYQILGVSKTASQADLKKAYLKLAKQYHPDTTDAKDAEKK------FKEINAAYDVLKDEQKRAAYD 65
PRK14284 PRK14284
chaperone protein DnaJ; Provisional
 538-605 3.10e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237658 [Multi-domain]  Cd Length: 391  Bit Score: 74.88  E-value: 3.10e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 398364465 538 DYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhNDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14284   2 DYYTILGVSKTASPEEIKKAYRKLAVKYHPDK-----NPGDAEAEKRFKEVSEAYEVLSDAQKRESYD 64
PRK14289 PRK14289
molecular chaperone DnaJ;
536-605 5.00e-14

molecular chaperone DnaJ;


Pssm-ID: 237660 [Multi-domain]  Cd Length: 386  Bit Score: 74.10  E-value: 5.00e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQEsiHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14289   4 KRDYYEVLGVSKTATVDEIKKAYRKKAIQYHPDK---NPGDKEA--EEKFKEAAEAYDVLSDPDKRSRYD 68
PRK14287 PRK14287
chaperone protein DnaJ; Provisional
 536-644 7.34e-14

chaperone protein DnaJ; Provisional


Pssm-ID: 237659 [Multi-domain]  Cd Length: 371  Bit Score: 73.50  E-value: 7.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhnDKQESIHETMSQINEAYETLSDDDKRKEYD-LSRSNPrrn 614
Cdd:PRK14287   3 KRDYYEVLGVDRNASVDEVKKAYRKLARKYHPDV------NKAPDAEDKFKEVKEAYDTLSDPQKKAHYDqFGHTDP--- 73

                         90       100       110
                 ....*....|....*....|....*....|..
gi 398364465 615 tfpqgprqNNMFKNPGSG-FP-FGNGFKMNFG 644
Cdd:PRK14287  74 --------NQGFGGGGAGdFGgFSDIFDMFFG 97
PRK14286 PRK14286
chaperone protein DnaJ; Provisional
 537-605 8.58e-13

chaperone protein DnaJ; Provisional


Pssm-ID: 172774 [Multi-domain]  Cd Length: 372  Bit Score: 70.40  E-value: 8.58e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398364465 537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKANhndkQESiHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14286   4 RSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGN----KES-EEKFKEATEAYEILRDPKKRQAYD 67
termin_org_DnaJ TIGR03835
terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ ...
 536-605 9.98e-13

terminal organelle assembly protein TopJ; This model describes TopJ (MG_200, CbpA), a DnaJ homolog and probable assembly protein of the Mycoplasma terminal organelle. The terminal organelle is involved in both cytadherence and gliding motility. [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274808 [Multi-domain]  Cd Length: 871  Bit Score: 71.38  E-value: 9.98e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465  536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQESIhetMSQINEAYETLSDDDKRKEYD 605
Cdd:TIGR03835   1 KRDYYEVLGIDRDADEQEIKKAFRKLAKKYHPDR---NKAPDAASI---FAEINEANDVLSNPKKRANYD 64
PRK14301 PRK14301
chaperone protein DnaJ; Provisional
 536-605 2.10e-12

chaperone protein DnaJ; Provisional


Pssm-ID: 237668 [Multi-domain]  Cd Length: 373  Bit Score: 69.00  E-value: 2.10e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDkikanHNDKQESIHETMSQINEAYETLSDDDKRKEYD 605
Cdd:PRK14301   3 QRDYYEVLGVSRDASEDEIKKAYRKLALQYHPD-----RNPDNPEAEQKFKEAAEAYEVLRDAEKRARYD 67
PTZ00037 PTZ00037
DnaJ_C chaperone protein; Provisional
 537-605 1.84e-10

DnaJ_C chaperone protein; Provisional


Pssm-ID: 240236 [Multi-domain]  Cd Length: 421  Bit Score: 63.30  E-value: 1.84e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 398364465 537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKikanhNDKQESIHEtmsqINEAYETLSDDDKRKEYD 605
Cdd:PTZ00037  28 EKLYEVLNLSKDCTTSEIKKAYRKLAIKHHPDK-----GGDPEKFKE----ISRAYEVLSDPEKRKIYD 87
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 535-605 7.17e-09

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 59.03  E-value: 7.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364465  535 PKKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKANhndkqESIHEtMSQINEAYETLSDDDKRKEYD 605
Cdd:PTZ00341  571 PDTLFYDILGVGVNADMKEISERYFKLAENYYPPKRSGN-----EGFHK-FKKINEAYQILGDIDKKKMYN 635
PRK14288 PRK14288
molecular chaperone DnaJ;
539-639 4.97e-07

molecular chaperone DnaJ;


Pssm-ID: 172776 [Multi-domain]  Cd Length: 369  Bit Score: 52.38  E-value: 4.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 539 YYKILGVSPSASSKEIRKAYLNLTKKYHPDKikaNHNDKQEsiHETMSQINEAYETLSDDDKRKEYD------LSRSNPR 612
Cdd:PRK14288   5 YYEILEVEKHSNQETIKKSYRKLALKYHPDR---NAGDKEA--EEKFKLINEAYGVLSDEKKRALYDrygkkgLNQAGAS 79

                         90       100
                 ....*....|....*....|....*..
gi 398364465 613 RNTFpqgprqNNMFKNPGSGFPFGNGF 639
Cdd:PRK14288  80 QSDF------SDFFEDLGSFFEDAFGF 100
djlA PRK09430
co-chaperone DjlA;
537-569 7.44e-07

co-chaperone DjlA;


Pssm-ID: 236512 [Multi-domain]  Cd Length: 267  Bit Score: 50.97  E-value: 7.44e-07
                         10        20        30
                 ....*....|....*....|....*....|...
gi 398364465 537 KDYYKILGVSPSASSKEIRKAYLNLTKKYHPDK 569
Cdd:PRK09430 200 EDAYKVLGVSESDDDQEIKRAYRKLMSEHHPDK 232
hscB TIGR00714
Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K ...
 552-610 8.92e-05

Fe-S protein assembly co-chaperone HscB; This model describes the small subunit, Hsc20 (20K heat shock cognate protein) of a pair of proteins Hsc66-Hsc20, related to the DnaK-DnaJ heat shock proteins, which also serve as molecular chaperones. Hsc20, unlike DnaJ, appears not to have chaperone activity on its own, but to act solely as a regulatory subunit for Hsc66 (i.e., to be a co-chaperone). The gene for Hsc20 in E. coli, hscB, is not induced by heat shock. [Protein fate, Protein folding and stabilization]


Pssm-ID: 211601 [Multi-domain]  Cd Length: 155  Bit Score: 43.33  E-value: 8.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 398364465  552 KEIRKAYLNLTKKYHPDKIKANHNDKQESihETMSQINEAYETLSDDDKRKEYDLSRSN 610
Cdd:TIGR00714   6 SRLRKRYRQLQAQYHPDASGMAQEQLAAS--QQSTTLNQAYHTLKDPLRRAEYMLKLLN 62
ZUO1 COG5269
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ...
 536-605 1.63e-04

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


Pssm-ID: 227594 [Multi-domain]  Cd Length: 379  Bit Score: 44.25  E-value: 1.63e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 398364465 536 KKDYYKILGVSP---SASSKEIRKAYLNLTKKYHPDKIKANHNDKQESIHETmsqINEAYETLSDDDKRKEYD 605
Cdd:COG5269   42 KVDLYALLGLSKyrtKAIPPQILKAHKKKVYKYHPDKTAAGGNKGCDEFFKL---IQKAREVLGDRKLRLQYD 111
hscB PRK01356
co-chaperone HscB; Provisional
 538-606 5.89e-04

co-chaperone HscB; Provisional


Pssm-ID: 167217 [Multi-domain]  Cd Length: 166  Bit Score: 41.02  E-value: 5.89e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 398364465 538 DYYKILGVSP--SASSKEIRKAYLNLTKKYHPDKIKANHNDKQESIheTMSQINEAYETLSDDDKRKEYDL 606
Cdd:PRK01356   3 NYFQLLGLPQeyNIDLKILEKQYFAMQVKYHPDKAKTLQEKEQNLI--IASELNNAYSTLKDALKRAEYML 71
hscB PRK05014
co-chaperone HscB; Provisional
 538-607 7.11e-04

co-chaperone HscB; Provisional


Pssm-ID: 179914 [Multi-domain]  Cd Length: 171  Bit Score: 40.66  E-value: 7.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 398364465 538 DYYKILGVSPSAsskEIRKA-----YLNLTKKYHPDKIkANHNDKQE--SIHETmSQINEAYETLSDDDKRKEYDLS 607
Cdd:PRK05014   2 DYFTLFGLPARY---DIDTQllasrYQELQRQFHPDKF-ANASERERllAVQQA-ATINDAYQTLKHPLKRAEYLLS 73
PTZ00100 PTZ00100
DnaJ chaperone protein; Provisional
 536-595 9.25e-03

DnaJ chaperone protein; Provisional


Pssm-ID: 240265  Cd Length: 116  Bit Score: 36.37  E-value: 9.25e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 398364465 536 KKDYYKILGVSPSASSKEIRKAYLNLTKKYHPDKIKANHndkqesiheTMSQINEAYETL 595
Cdd:PTZ00100  64 KSEAYKILNISPTASKERIREAHKQLMLRNHPDNGGSTY---------IASKVNEAKDLL 114
 
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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