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Conserved domains on  [gi|81912958|sp|Q80Z32|]
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RecName: Full=Origin recognition complex subunit 1

Protein Classification

BAH_Orc1p_animal and Cdc6_C domain-containing protein( domain architecture ID 12939703)

protein containing domains BAH_Orc1p_animal, rne, P-loop containing Nucleoside Triphosphate Hydrolases, and Cdc6_C

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 43-169 4.21e-51

BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces cerevisiae Orc1p. Orc1 is part of the Yeast Sir1-origin recognition complex. The Orc1p BAH doman functions in epigenetic silencing. In vertebrates, a similar ORC protein complex exists, which has been shown essential for DNA replication in Xenopus laevis. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


:

Pssm-ID: 240070  Cd Length: 128  Bit Score: 174.87  E-value: 4.21e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  43 EIHIKVGQFVLIQGEDNQKPYVAKLIELFENGSEVPPKKYARVQWFVRFCEIPIPKRHLLGRRPSAQEIFWYDCSDCDND 122
Cdd:cd04719   1 ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDND 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 81912958 123 IHVETIIGPVQVVALAPEDEIP-VNQKSEETLFVKLSWNKKNFAPLPP 169
Cdd:cd04719  81 IDAETIIGKVRVEPVEPKTDLPeTKKKTGGPLFVKRYWDTKTFRSLDS 128
PTZ00112 super family cl36513
origin recognition complex 1 protein; Provisional
 482-773 4.54e-50

origin recognition complex 1 protein; Provisional


The actual alignment was detected with superfamily member PTZ00112:

Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 191.36  E-value: 4.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   482 LHVSAVPDSLPCREQEFQDIYSFVESKL-LDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAQTNDVPPFEYVEVNGMKL 560
Cdd:PTZ00112  748 MQLDVVPKYLPCREKEIKEVHGFLESGIkQSGSNQILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMNV 827

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   561 TEPHQVYvQILQKLTGQKATAN--HAAELLAKQFC-SRGSQKETTVLLVDELDLLWTHKQDVLYNLFDWPTHKGARLVVL 637
Cdd:PTZ00112  828 VHPNAAY-QVLYKQLFNKKPPNalNSFKILDRLFNqNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVLI 906

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   638 TIANTMDLPERiMMNRVASRLGLTRMSFQPYSHSQLKQILVSRLKHLKAFED-DAVQLVARKVAALSGDARRCLDICRRA 716
Cdd:PTZ00112  907 AISNTMDLPER-LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRKA 985

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 81912958   717 TEicevsHQRGDSqclVTVAHLMEAIDEMFSSSYITAIKNSSVLEQSFLRAIIAEFR 773
Cdd:PTZ00112  986 FE-----NKRGQK---IVPRDITEATNQLFDSPLTNAINYLPWPFKMFLTCLIVELR 1034
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 765-844 1.89e-19

CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix fold, with a five alpha-helical bundle (alpha15-alpha19) structure, backed on one side by three beta strands (beta6-beta8). It has been shown that this domain acts as a DNA-localization factor, however its exact function is, as yet, unknown. Putative functions include: (1) mediation of protein-protein interactions and (2) regulation of nucleotide binding and hydrolysis. Mutagenesis studies have shown that this domain is essential for appropriate Cdc6 activity.


:

Pssm-ID: 462672  Cd Length: 84  Bit Score: 83.41  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   765 LRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRILLVEPS----RNDLLLRVRLNVSQND 840
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 81912958   841 VLYA 844
Cdd:pfam09079  81 VLEA 84
COG3899 super family cl28481
Predicted ATPase [General function prediction only];
426-536 1.09e-03

Predicted ATPase [General function prediction only];


The actual alignment was detected with superfamily member COG3899:

Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.92  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  426 QSRTRRTASKPSSQTPSKSPKKTFRPRPPLHATPQIRDRNLAVQEPASVLEEARLRLHVSAVPDSLPCREQEFQDIYSFV 505
Cdd:COG3899  224 AAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAAL 303

                         90       100       110
                 ....*....|....*....|....*....|.
gi 81912958  506 ESkLLDGTGGCMYISGVPGTGKTATVHEVIR 536
Cdd:COG3899  304 ER-ARAGRGELVLVSGEAGIGKSRLVRELAR 333
 
Name Accession Description Interval E-value
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 43-169 4.21e-51

BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces cerevisiae Orc1p. Orc1 is part of the Yeast Sir1-origin recognition complex. The Orc1p BAH doman functions in epigenetic silencing. In vertebrates, a similar ORC protein complex exists, which has been shown essential for DNA replication in Xenopus laevis. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240070  Cd Length: 128  Bit Score: 174.87  E-value: 4.21e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  43 EIHIKVGQFVLIQGEDNQKPYVAKLIELFENGSEVPPKKYARVQWFVRFCEIPIPKRHLLGRRPSAQEIFWYDCSDCDND 122
Cdd:cd04719   1 ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDND 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 81912958 123 IHVETIIGPVQVVALAPEDEIP-VNQKSEETLFVKLSWNKKNFAPLPP 169
Cdd:cd04719  81 IDAETIIGKVRVEPVEPKTDLPeTKKKTGGPLFVKRYWDTKTFRSLDS 128
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 482-773 4.54e-50

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 191.36  E-value: 4.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   482 LHVSAVPDSLPCREQEFQDIYSFVESKL-LDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAQTNDVPPFEYVEVNGMKL 560
Cdd:PTZ00112  748 MQLDVVPKYLPCREKEIKEVHGFLESGIkQSGSNQILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMNV 827

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   561 TEPHQVYvQILQKLTGQKATAN--HAAELLAKQFC-SRGSQKETTVLLVDELDLLWTHKQDVLYNLFDWPTHKGARLVVL 637
Cdd:PTZ00112  828 VHPNAAY-QVLYKQLFNKKPPNalNSFKILDRLFNqNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVLI 906

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   638 TIANTMDLPERiMMNRVASRLGLTRMSFQPYSHSQLKQILVSRLKHLKAFED-DAVQLVARKVAALSGDARRCLDICRRA 716
Cdd:PTZ00112  907 AISNTMDLPER-LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRKA 985

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 81912958   717 TEicevsHQRGDSqclVTVAHLMEAIDEMFSSSYITAIKNSSVLEQSFLRAIIAEFR 773
Cdd:PTZ00112  986 FE-----NKRGQK---IVPRDITEATNQLFDSPLTNAINYLPWPFKMFLTCLIVELR 1034
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
482-798 3.95e-37

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 143.84  E-value: 3.95e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 482 LHVSAVPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAQTNDVpPFEYVEVNGMKLT 561
Cdd:COG1474  19 LSPDYVPDRLPHREEEIEELASALRPALRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGV-DVRVVYVNCRQAS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 562 EPHQVYVQILQKLTGQK---ATANHAAELLaKQFCSRGSQKETT-----------VLlvdeldllwTHKQDVLYNLFDWP 627
Cdd:COG1474  98 TRYRVLSRILEELGSGEdipSTGLSTDELF-DRLYEALDERDGVlvvvldeidylVD---------DEGDDLLYQLLRAN 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 628 T-HKGARLVVLTIANTMDLPERiMMNRVASRLGLTRMSFQPYSHSQLKQILVSRLKHlkAFEDDAV-----QLVARKVAA 701
Cdd:COG1474 168 EeLEGARVGVIGISNDLEFLEN-LDPRVKSSLGEEEIVFPPYDADELRDILEDRAEL--AFYDGVLsdeviPLIAALAAQ 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 702 LSGDARRCLDICRRATEICEvshQRGDSQclVTVAHLMEAIDEMFSSSYITAIKNSSVLEQSFLRAiIAEFRRSGLEEAT 781
Cdd:COG1474 245 EHGDARKAIDLLRVAGEIAE---REGSDR--VTEEHVREAREKIERDRLLEVLRGLPTHEKLVLLA-IAELLKDGEDPVR 318

                       330
                ....*....|....*..
gi 81912958 782 FQQIYSQHVALCRMEGL 798
Cdd:COG1474 319 TGEVYEAYEELCEELGV 335
BAH smart00439
Bromo adjacent homology domain;
45-168 1.15e-22

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 93.90  E-value: 1.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958     45 HIKVGQFVLIQGEDNQKPY-VAKLIELFENGSEVPpKKYARVQWFVRFCEIPIPKRHLLGRRpsaqEIFWydcSDCDNDI 123
Cdd:smart00439   1 TISVGDFVLVEPDDADEPYyIGRIEEIFETKKNSE-SKMVRVRWFYRPEETVLEKAALFDKN----EVFL---SDEYDTV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 81912958    124 HVETIIGPVQVVALAPEDEIPVNQKS--EETLFVKLSWN--KKNFAPLP 168
Cdd:smart00439  73 PLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDpeKGSFKKLP 121
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 482-814 2.73e-21

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 96.55  E-value: 2.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   482 LHVSAVPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAQTNDVpPFEYVEVNGMKLT 561
Cdd:TIGR02928   8 LEPDYVPDRIVHRDEQIEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAEDRDV-RVVTVYVNCQILD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   562 EPHQVYVQILQKLTG---QKATANHAAELLAKQFCSR-GSQKETTVLLVDELDLLWTHKQDVLYNL---FDWPTHKGARL 634
Cdd:TIGR02928  87 TLYQVLVELANQLRGsgeEVPTTGLSTSEVFRRLYKElNERGDSLIIVLDEIDYLVGDDDDLLYQLsraRSNGDLDNAKV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   635 VVLTIANTMDLPERIMMnRVASRLGLTRMSFQPYSHSQLKQILVSRLKhlKAF-----EDDAVQLVARKVAALSGDARRC 709
Cdd:TIGR02928 167 GVIGISNDLKFRENLDP-RVKSSLCEEEIIFPPYDAEELRDILENRAE--KAFydgvlDDGVIPLCAALAAQEHGDARKA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   710 LDICRRATEICEvshQRGDSqcLVTVAHLMEAIDEMFSSSYITAIKNSSVLEQSFLRAIIAEFRRSGlEEATFQQIYSQH 789
Cdd:TIGR02928 244 IDLLRVAGEIAE---REGAE--RVTEDHVEKAQEKIEKDRLLELIRGLPTHSKLVLLAIANLAANDE-DPFRTGEVYEVY 317

                         330       340
                  ....*....|....*....|....*...
gi 81912958   790 VALCR---MEGLPYPTMSETMAVCSRLG 814
Cdd:TIGR02928 318 KEVCEdigVDPLTQRRISDLLNELDMLG 345
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 765-844 1.89e-19

CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix fold, with a five alpha-helical bundle (alpha15-alpha19) structure, backed on one side by three beta strands (beta6-beta8). It has been shown that this domain acts as a DNA-localization factor, however its exact function is, as yet, unknown. Putative functions include: (1) mediation of protein-protein interactions and (2) regulation of nucleotide binding and hydrolysis. Mutagenesis studies have shown that this domain is essential for appropriate Cdc6 activity.


Pssm-ID: 462672  Cd Length: 84  Bit Score: 83.41  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   765 LRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRILLVEPS----RNDLLLRVRLNVSQND 840
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 81912958   841 VLYA 844
Cdd:pfam09079  81 VLEA 84
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 44-168 2.54e-19

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 84.28  E-value: 2.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958    44 IHIKVGQFVLIQGED-NQKPYVAKLIELFENGSEvpPKKYARVQWFVRFCEipIPKRHLLGRRPsaQEIFWYDCSDCDNd 122
Cdd:pfam01426   1 ETYSVGDFVLVEPDDaDEPYYVARIEELFEDTKN--GKKMVRVQWFYRPEE--TVHRAGKAFNK--DELFLSDEEDDVP- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 81912958   123 ihVETIIGPVQVVALAP-EDEIPVNQKSEETLFVKLSWN--KKNFAPLP 168
Cdd:pfam01426  74 --LSAIIGKCSVLHKSDlESLDPYKIKEPDDFFCELLYDpkTKSFKKLP 120
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 758-841 2.63e-19

Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), which mediates DNA binding; This model characterizes the winged-helix, C-terminal domain of the Cell division control protein (Cdc6_C). Cdc6 (also known as Cell division cycle 6 or Cdc18) functions as a regulator at the early stages of DNA replication, by helping to recruit and load the Minichromosome Maintenance Complex (MCM) onto DNA and may have additional roles in the control of mitotic entry. Precise duplication of chromosomal DNA is required for genomic stability during replication. Cdc6 has an essential role in DNA replication and irregular expression of Cdc6 may lead to genomic instability. Cdc6 over-expression is observed in many cancerous lesions. DNA replication begins when an origin recognition complex (ORC) binds to a replication origin site on the chromatin. Studies indicate that Cdc6 interacts with ORC through the Orc1 subunit, and that this association increases the specificity of the ORC-origins interaction. Further studies suggest that hydrolysis of Cdc6-bound ATP promotes the association of the replication licensing factor Cdt1 with origins through an interaction with Orc6 and this in turn promotes the loading of MCM2-7 helicase onto chromatin. The MCM2-7 complex promotes the unwinding of DNA origins, and the binding of additional factors to initiate the DNA replication. S-Cdk (S-phase cyclin and cyclin-dependent kinase complex) prevents rereplication by causing the Cdc6 protein to dissociate from ORC and prevents the Cdc6 and MCM proteins from reassembling at any origin. By phosphorylating Cdc6, S-Cdk also triggers Cdc6's ubiquitination. The Cdc6 protein is composed of three domains, an N-terminal AAA+ domain with Walker A and B, and Sensor-1 and -2 motifs. The central region contains a conserved nucleotide binding/ATPase domain and is a member of the ATPase superfamily. The C-terminal domain (Cdc6_C) is a conserved winged-helix domain that possibly mediates protein-protein interactions or direct DNA interactions. Cdc6 is conserved in eukaryotes, and related genes are found in Archaea. The winged helix fold structure of Cdc6_C is similar to the structures of other eukaryotic replication initiators without apparent sequence similarity.


Pssm-ID: 176573 [Multi-domain]  Cd Length: 87  Bit Score: 83.05  E-value: 2.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 758 SVLEQSFLRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRILLVEPSRNDL---LLRVRL 834
Cdd:cd08768   1 PLHQKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISL 80


                ....*..
gi 81912958 835 NVSQNDV 841
Cdd:cd08768  81 NVDPDDV 87
Cdc6_C smart01074
CDC6, C terminal; The C terminal domain of CDC6 assumes a winged helix fold, with a five ...
 765-845 4.64e-17

CDC6, C terminal; The C terminal domain of CDC6 assumes a winged helix fold, with a five alpha-helical bundle (alpha15-alpha19) structure, backed on one side by three beta strands (beta6-beta8). It has been shown that this domain acts as a DNA-localisation factor, however its exact function is, as yet, unknown. Putative functions include: (1) mediation of protein-protein interactions and (2) regulation of nucleotide binding and hydrolysis. Mutagenesis studies have shown that this domain is essential for appropriate Cdc6 activity.


Pssm-ID: 215013 [Multi-domain]  Cd Length: 84  Bit Score: 76.52  E-value: 4.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958    765 LRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRILLVEPS---RNDLLLRVRLNVSQNDV 841
Cdd:smart01074   1 LLAIVLLLTRGGKEEVTTGEVYEVYKELCKELGVDPLTYTRIYDLLNELEMLGIIELRVSnrgRRGRTREISLNVDPDDV 80


                   ....
gi 81912958    842 LYAL 845
Cdd:smart01074  81 LEAL 84
AAA_lid_10 pfam17872
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 689-721 4.16e-09

AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 407729 [Multi-domain]  Cd Length: 99  Bit Score: 54.44  E-value: 4.16e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 81912958   689 DDAVQLVARKVAALSGDARRCLDICRRATEICE 721
Cdd:pfam17872  47 DDAIEIASRKVASVSGDARRALKICKRAAEIAE 79
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 497-660 7.78e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 40.98  E-value: 7.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 497 EFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQqaaqtndVPPFEYVEVNGMKLTEPHQVYVQILQKLTG 576
Cdd:cd00009   2 GQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF-------RPGAPFLYLNASDLLEGLVVAELFGHFLVR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 577 QKATANHAA--------ELlakQFCSRGSQKEttvllvdeldllwthKQDVLYNLFDWPTHKGARLVVLTianTMDLPER 648
Cdd:cd00009  75 LLFELAEKAkpgvlfidEI---DSLSRGAQNA---------------LLRVLETLNDLRIDRENVRVIGA---TNRPLLG 133

                       170
                ....*....|..
gi 81912958 649 IMMNRVASRLGL 660
Cdd:cd00009 134 DLDRALYDRLDI 145
COG3899 COG3899
Predicted ATPase [General function prediction only];
426-536 1.09e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.92  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  426 QSRTRRTASKPSSQTPSKSPKKTFRPRPPLHATPQIRDRNLAVQEPASVLEEARLRLHVSAVPDSLPCREQEFQDIYSFV 505
Cdd:COG3899  224 AAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAAL 303

                         90       100       110
                 ....*....|....*....|....*....|.
gi 81912958  506 ESkLLDGTGGCMYISGVPGTGKTATVHEVIR 536
Cdd:COG3899  304 ER-ARAGRGELVLVSGEAGIGKSRLVRELAR 333
 
Name Accession Description Interval E-value
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 43-169 4.21e-51

BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces cerevisiae Orc1p. Orc1 is part of the Yeast Sir1-origin recognition complex. The Orc1p BAH doman functions in epigenetic silencing. In vertebrates, a similar ORC protein complex exists, which has been shown essential for DNA replication in Xenopus laevis. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240070  Cd Length: 128  Bit Score: 174.87  E-value: 4.21e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  43 EIHIKVGQFVLIQGEDNQKPYVAKLIELFENGSEVPPKKYARVQWFVRFCEIPIPKRHLLGRRPSAQEIFWYDCSDCDND 122
Cdd:cd04719   1 ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDND 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 81912958 123 IHVETIIGPVQVVALAPEDEIP-VNQKSEETLFVKLSWNKKNFAPLPP 169
Cdd:cd04719  81 IDAETIIGKVRVEPVEPKTDLPeTKKKTGGPLFVKRYWDTKTFRSLDS 128
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 482-773 4.54e-50

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 191.36  E-value: 4.54e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   482 LHVSAVPDSLPCREQEFQDIYSFVESKL-LDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAQTNDVPPFEYVEVNGMKL 560
Cdd:PTZ00112  748 MQLDVVPKYLPCREKEIKEVHGFLESGIkQSGSNQILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMNV 827

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   561 TEPHQVYvQILQKLTGQKATAN--HAAELLAKQFC-SRGSQKETTVLLVDELDLLWTHKQDVLYNLFDWPTHKGARLVVL 637
Cdd:PTZ00112  828 VHPNAAY-QVLYKQLFNKKPPNalNSFKILDRLFNqNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVLI 906

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   638 TIANTMDLPERiMMNRVASRLGLTRMSFQPYSHSQLKQILVSRLKHLKAFED-DAVQLVARKVAALSGDARRCLDICRRA 716
Cdd:PTZ00112  907 AISNTMDLPER-LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRKA 985

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 81912958   717 TEicevsHQRGDSqclVTVAHLMEAIDEMFSSSYITAIKNSSVLEQSFLRAIIAEFR 773
Cdd:PTZ00112  986 FE-----NKRGQK---IVPRDITEATNQLFDSPLTNAINYLPWPFKMFLTCLIVELR 1034
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
482-798 3.95e-37

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 143.84  E-value: 3.95e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 482 LHVSAVPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAQTNDVpPFEYVEVNGMKLT 561
Cdd:COG1474  19 LSPDYVPDRLPHREEEIEELASALRPALRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGV-DVRVVYVNCRQAS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 562 EPHQVYVQILQKLTGQK---ATANHAAELLaKQFCSRGSQKETT-----------VLlvdeldllwTHKQDVLYNLFDWP 627
Cdd:COG1474  98 TRYRVLSRILEELGSGEdipSTGLSTDELF-DRLYEALDERDGVlvvvldeidylVD---------DEGDDLLYQLLRAN 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 628 T-HKGARLVVLTIANTMDLPERiMMNRVASRLGLTRMSFQPYSHSQLKQILVSRLKHlkAFEDDAV-----QLVARKVAA 701
Cdd:COG1474 168 EeLEGARVGVIGISNDLEFLEN-LDPRVKSSLGEEEIVFPPYDADELRDILEDRAEL--AFYDGVLsdeviPLIAALAAQ 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 702 LSGDARRCLDICRRATEICEvshQRGDSQclVTVAHLMEAIDEMFSSSYITAIKNSSVLEQSFLRAiIAEFRRSGLEEAT 781
Cdd:COG1474 245 EHGDARKAIDLLRVAGEIAE---REGSDR--VTEEHVREAREKIERDRLLEVLRGLPTHEKLVLLA-IAELLKDGEDPVR 318

                       330
                ....*....|....*..
gi 81912958 782 FQQIYSQHVALCRMEGL 798
Cdd:COG1474 319 TGEVYEAYEELCEELGV 335
cdc6 PRK00411
ORC1-type DNA replication protein;
487-798 2.84e-24

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 106.09  E-value: 2.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  487 VPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAQtndvpPFEYVEVNGMKLTEPHQV 566
Cdd:PRK00411  28 VPENLPHREEQIEELAFALRPALRGSRPLNVLIYGPPGTGKTTTVKKVFEELEEIAV-----KVVYVYINCQIDRTRYAI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  567 YVQILQKLTGQkatanhaaellakQFCSRG-SQKETTVLLVDELDLL---------------WTHKQDVLYNLFDWPT-H 629
Cdd:PRK00411 103 FSEIARQLFGH-------------PPPSSGlSFDELFDKIAEYLDERdrvlivalddinylfEKEGNDVLYSLLRAHEeY 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  630 KGARLVVLTIANTMDLPERIMMnRVASRLGLTRMSFQPYSHSQLKQILVSRLKHlkAF-----EDDAVQLVARKVAALSG 704
Cdd:PRK00411 170 PGARIGVIGISSDLTFLYILDP-RVKSVFRPEEIYFPPYTADEIFDILKDRVEE--GFypgvvDDEVLDLIADLTAREHG 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  705 DARRCLDICRRATEICEvshQRGDSQclVTVAHLMEAIDEMFSSSYITAIKNSSVLEQSFLRAIIaEFRRSGLEEATFQQ 784
Cdd:PRK00411 247 DARVAIDLLRRAGLIAE---REGSRK--VTEEDVRKAYEKSEIVHLSEVLRTLPLHEKLLLRAIV-RLLKKGGDEVTTGE 320

                        330
                 ....*....|....
gi 81912958  785 IYSQHVALCRMEGL 798
Cdd:PRK00411 321 VYEEYKELCEELGY 334
BAH smart00439
Bromo adjacent homology domain;
45-168 1.15e-22

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 93.90  E-value: 1.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958     45 HIKVGQFVLIQGEDNQKPY-VAKLIELFENGSEVPpKKYARVQWFVRFCEIPIPKRHLLGRRpsaqEIFWydcSDCDNDI 123
Cdd:smart00439   1 TISVGDFVLVEPDDADEPYyIGRIEEIFETKKNSE-SKMVRVRWFYRPEETVLEKAALFDKN----EVFL---SDEYDTV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 81912958    124 HVETIIGPVQVVALAPEDEIPVNQKS--EETLFVKLSWN--KKNFAPLP 168
Cdd:smart00439  73 PLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDpeKGSFKKLP 121
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 482-814 2.73e-21

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 96.55  E-value: 2.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   482 LHVSAVPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAQTNDVpPFEYVEVNGMKLT 561
Cdd:TIGR02928   8 LEPDYVPDRIVHRDEQIEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAEDRDV-RVVTVYVNCQILD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   562 EPHQVYVQILQKLTG---QKATANHAAELLAKQFCSR-GSQKETTVLLVDELDLLWTHKQDVLYNL---FDWPTHKGARL 634
Cdd:TIGR02928  87 TLYQVLVELANQLRGsgeEVPTTGLSTSEVFRRLYKElNERGDSLIIVLDEIDYLVGDDDDLLYQLsraRSNGDLDNAKV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   635 VVLTIANTMDLPERIMMnRVASRLGLTRMSFQPYSHSQLKQILVSRLKhlKAF-----EDDAVQLVARKVAALSGDARRC 709
Cdd:TIGR02928 167 GVIGISNDLKFRENLDP-RVKSSLCEEEIIFPPYDAEELRDILENRAE--KAFydgvlDDGVIPLCAALAAQEHGDARKA 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   710 LDICRRATEICEvshQRGDSqcLVTVAHLMEAIDEMFSSSYITAIKNSSVLEQSFLRAIIAEFRRSGlEEATFQQIYSQH 789
Cdd:TIGR02928 244 IDLLRVAGEIAE---REGAE--RVTEDHVEKAQEKIEKDRLLELIRGLPTHSKLVLLAIANLAANDE-DPFRTGEVYEVY 317

                         330       340
                  ....*....|....*....|....*...
gi 81912958   790 VALCR---MEGLPYPTMSETMAVCSRLG 814
Cdd:TIGR02928 318 KEVCEdigVDPLTQRRISDLLNELDMLG 345
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 765-844 1.89e-19

CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix fold, with a five alpha-helical bundle (alpha15-alpha19) structure, backed on one side by three beta strands (beta6-beta8). It has been shown that this domain acts as a DNA-localization factor, however its exact function is, as yet, unknown. Putative functions include: (1) mediation of protein-protein interactions and (2) regulation of nucleotide binding and hydrolysis. Mutagenesis studies have shown that this domain is essential for appropriate Cdc6 activity.


Pssm-ID: 462672  Cd Length: 84  Bit Score: 83.41  E-value: 1.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   765 LRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRILLVEPS----RNDLLLRVRLNVSQND 840
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 81912958   841 VLYA 844
Cdd:pfam09079  81 VLEA 84
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 44-168 2.54e-19

BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been called ELM1 and BAM (Bromo adjacent motif) domain. The function of this domain is unknown but may be involved in protein-protein interaction.


Pssm-ID: 460207  Cd Length: 120  Bit Score: 84.28  E-value: 2.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958    44 IHIKVGQFVLIQGED-NQKPYVAKLIELFENGSEvpPKKYARVQWFVRFCEipIPKRHLLGRRPsaQEIFWYDCSDCDNd 122
Cdd:pfam01426   1 ETYSVGDFVLVEPDDaDEPYYVARIEELFEDTKN--GKKMVRVQWFYRPEE--TVHRAGKAFNK--DELFLSDEEDDVP- 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 81912958   123 ihVETIIGPVQVVALAP-EDEIPVNQKSEETLFVKLSWN--KKNFAPLP 168
Cdd:pfam01426  74 --LSAIIGKCSVLHKSDlESLDPYKIKEPDDFFCELLYDpkTKSFKKLP 120
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 758-841 2.63e-19

Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), which mediates DNA binding; This model characterizes the winged-helix, C-terminal domain of the Cell division control protein (Cdc6_C). Cdc6 (also known as Cell division cycle 6 or Cdc18) functions as a regulator at the early stages of DNA replication, by helping to recruit and load the Minichromosome Maintenance Complex (MCM) onto DNA and may have additional roles in the control of mitotic entry. Precise duplication of chromosomal DNA is required for genomic stability during replication. Cdc6 has an essential role in DNA replication and irregular expression of Cdc6 may lead to genomic instability. Cdc6 over-expression is observed in many cancerous lesions. DNA replication begins when an origin recognition complex (ORC) binds to a replication origin site on the chromatin. Studies indicate that Cdc6 interacts with ORC through the Orc1 subunit, and that this association increases the specificity of the ORC-origins interaction. Further studies suggest that hydrolysis of Cdc6-bound ATP promotes the association of the replication licensing factor Cdt1 with origins through an interaction with Orc6 and this in turn promotes the loading of MCM2-7 helicase onto chromatin. The MCM2-7 complex promotes the unwinding of DNA origins, and the binding of additional factors to initiate the DNA replication. S-Cdk (S-phase cyclin and cyclin-dependent kinase complex) prevents rereplication by causing the Cdc6 protein to dissociate from ORC and prevents the Cdc6 and MCM proteins from reassembling at any origin. By phosphorylating Cdc6, S-Cdk also triggers Cdc6's ubiquitination. The Cdc6 protein is composed of three domains, an N-terminal AAA+ domain with Walker A and B, and Sensor-1 and -2 motifs. The central region contains a conserved nucleotide binding/ATPase domain and is a member of the ATPase superfamily. The C-terminal domain (Cdc6_C) is a conserved winged-helix domain that possibly mediates protein-protein interactions or direct DNA interactions. Cdc6 is conserved in eukaryotes, and related genes are found in Archaea. The winged helix fold structure of Cdc6_C is similar to the structures of other eukaryotic replication initiators without apparent sequence similarity.


Pssm-ID: 176573 [Multi-domain]  Cd Length: 87  Bit Score: 83.05  E-value: 2.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 758 SVLEQSFLRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRILLVEPSRNDL---LLRVRL 834
Cdd:cd08768   1 PLHQKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISL 80


                ....*..
gi 81912958 835 NVSQNDV 841
Cdd:cd08768  81 NVDPDDV 87
Cdc6_C smart01074
CDC6, C terminal; The C terminal domain of CDC6 assumes a winged helix fold, with a five ...
 765-845 4.64e-17

CDC6, C terminal; The C terminal domain of CDC6 assumes a winged helix fold, with a five alpha-helical bundle (alpha15-alpha19) structure, backed on one side by three beta strands (beta6-beta8). It has been shown that this domain acts as a DNA-localisation factor, however its exact function is, as yet, unknown. Putative functions include: (1) mediation of protein-protein interactions and (2) regulation of nucleotide binding and hydrolysis. Mutagenesis studies have shown that this domain is essential for appropriate Cdc6 activity.


Pssm-ID: 215013 [Multi-domain]  Cd Length: 84  Bit Score: 76.52  E-value: 4.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958    765 LRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRILLVEPS---RNDLLLRVRLNVSQNDV 841
Cdd:smart01074   1 LLAIVLLLTRGGKEEVTTGEVYEVYKELCKELGVDPLTYTRIYDLLNELEMLGIIELRVSnrgRRGRTREISLNVDPDDV 80


                   ....
gi 81912958    842 LYAL 845
Cdd:smart01074  81 LEAL 84
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 43-160 1.49e-10

BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). BAH domains have first been described as domains found in the polybromo protein and Yeast Rsc1/Rsc2 (Remodeling of the Structure of Chromatin). They also occur in mammalian DNA methyltransferases and the MTA1 subunits of histone deacetylase complexes. A BAH domain is also found in Yeast Sir3p and in the origin receptor complex protein 1 (Orc1p), where it was found to interact with the N-terminal lobe of the silence information regulator 1 protein (Sir1p), confirming the initial hypothesis that BAH plays a role in protein-protein interactions.


Pssm-ID: 239835 [Multi-domain]  Cd Length: 123  Bit Score: 59.33  E-value: 1.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  43 EIHIKVGQFVLIQGED---NQKPYVAKLIELFENGSEVppkKYARVQWFVRFCEIPIPKRHLLGRRpsaqEIFWYDcsDC 119
Cdd:cd04370   1 GITYEVGDSVYVEPDDsikSDPPYIARIEELWEDTNGS---KQVKVRWFYRPEETPKGLSPFALRR----ELFLSD--HL 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 81912958 120 DnDIHVETIIGPVQVVALAPEDEI--PVNQKSEETLFVKLSWN 160
Cdd:cd04370  72 D-EIPVESIIGKCKVLFVSEFEGLkqRPNKIDTDDFFCRLAYD 113
AAA_lid_10 pfam17872
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 689-721 4.16e-09

AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the C-terminus of AAA domains.


Pssm-ID: 407729 [Multi-domain]  Cd Length: 99  Bit Score: 54.44  E-value: 4.16e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 81912958   689 DDAVQLVARKVAALSGDARRCLDICRRATEICE 721
Cdd:pfam17872  47 DDAIEIASRKVASVSGDARRALKICKRAAEIAE 79
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 517-662 3.13e-08

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 52.98  E-value: 3.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   517 MYISGVPGTGKTATVHEVirclqqAAQTNdvppFEYVEVNGMKLTEPH--QVYVQILQKLTGQKATANHA-----AELLA 589
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAV------AKELG----APFIEISGSELVSKYvgESEKRLRELFEAAKKLAPCVifideIDALA 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81912958   590 KqfcSRGSQKETTVLLVdeldllwthkQDVLYNLFDWPTHKGARLVVLTIANTMDLPERIMMNRVASRLGLTR 662
Cdd:pfam00004  71 G---SRGSGGDSESRRV----------VNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 44-150 2.80e-06

BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5)-methyltransferases (DCM) from plants. DNA methylation, or the covalent addition of a methyl group to cytosine within the context of the CpG dinucleotide, has profound effects on the genome. These effects include transcriptional repression via inhibition of transcription factor binding, the recruitment of methyl-binding proteins and their associated chromatin remodeling factors, X chromosome inactivation, imprinting, and the suppression of parasitic DNA sequences. DNA methylation is also essential for proper embryonic development and is an important player in both DNA repair and genome stability. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240067  Cd Length: 122  Bit Score: 47.05  E-value: 2.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  44 IHIKVGQFVLIQGEDNQKPYVAKLIELFENgseVPPKKYARVQWFVRFCEIPIpKRHLLGRRPsaQEIFWydcSDCDNDI 123
Cdd:cd04716   2 ITYNLGDDAYVQGGEGEEPFICKITEFFEG---TDGKTYFTAQWFYRAEDTVI-ERQATNHDK--KRVFY---SEIKNDN 72

                        90       100       110
                ....*....|....*....|....*....|.
gi 81912958 124 HVETIIGPVQVVALAP----EDEIPVNQKSE 150
Cdd:cd04716  73 PLDCLISKVKILQVPPnvgtKRKKPNSEKCD 103
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 491-536 2.53e-05

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 45.57  E-value: 2.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 81912958   491 LPCREQEFQDIYSFVEsKLLDGTGGCMYISGVPGTGKTATVHEVIR 536
Cdd:pfam13191   2 LVGREEELEQLLDALD-RVRSGRPPSVLLTGEAGTGKTTLLRELLR 46
AAA_22 pfam13401
AAA domain;
510-589 1.78e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 42.33  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958   510 LDGTGGCMYISGVPGTGKTatvheviRCLQQAAQTNDVPPFEYVEVNGMKLTEPHQVYVQILQKLTGQKATANHAAELLA 589
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKT-------TLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLA 73
BAH_Orc1p_like cd04715
BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of ...
 16-144 4.75e-04

BAH, or Bromo Adjacent Homology domain, as present in the Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae Orc1p and similar proteins. Orc1 is part of the Yeast Sir1-origin recognition complex, the Orc1p BAH doman functions in epigenetic silencing. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240066  Cd Length: 159  Bit Score: 41.72  E-value: 4.75e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  16 WVGRPLPNRK-QFYQMYKeicmkINGcseIHIKVGQFVLIqGEDNQKPYVAKLIELFENgSEVPPKKYARVQWFVRFCEI 94
Cdd:cd04715   7 KRGEGGKKKDgQFYRSFT-----YDG---VEYRLYDDVYV-HNGDSEPYIGKIIKIYET-AIDSGKKKVKVIWFFRPSEI 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81912958  95 -----PIPKRHllgrrpsAQEIFwYDCSDCDN--DIH-VETIIGPVQVVALA-------PEDEIP 144
Cdd:cd04715  77 rmelkGEPKRH-------INEVF-LACGRGEGlaNINlLESIIGKCNVVCISedfrnpqPSDGIP 133
BAH_BAHCC1 cd04714
BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. ...
 46-168 7.44e-04

BAH, or Bromo Adjacent Homology domain, as present in mammalian BAHCC1 and similar proteins. BAHCC1 stands for BAH domain and coiled-coil containing 1. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240065  Cd Length: 121  Bit Score: 40.08  E-value: 7.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  46 IKVGQFVLIQ-GEDNQKPYVAKLIELFEN-GSEVppkkYARVQWFVRfceipiPKRHLLGRRPS--AQEIFWYDCSDcDN 121
Cdd:cd04714   4 IRVGDCVLFKsPGRPSLPYVARIESLWEDpEGNM----VVRVKWYYR------PEETKGGRKPNhgEKELFASDHQD-EN 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 81912958 122 DihVETIIGPVQVVALA----PEDEIPVNQKSEETLFVKLSWNKKNFAPLP 168
Cdd:cd04714  73 S--VQTIEHKCYVLTFAeyerLARVKKKPQDGVDFYYCAGTYNPDTGMLKC 121
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 497-660 7.78e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 40.98  E-value: 7.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 497 EFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQqaaqtndVPPFEYVEVNGMKLTEPHQVYVQILQKLTG 576
Cdd:cd00009   2 GQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF-------RPGAPFLYLNASDLLEGLVVAELFGHFLVR 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958 577 QKATANHAA--------ELlakQFCSRGSQKEttvllvdeldllwthKQDVLYNLFDWPTHKGARLVVLTianTMDLPER 648
Cdd:cd00009  75 LLFELAEKAkpgvlfidEI---DSLSRGAQNA---------------LLRVLETLNDLRIDRENVRVIGA---TNRPLLG 133

                       170
                ....*....|..
gi 81912958 649 IMMNRVASRLGL 660
Cdd:cd00009 134 DLDRALYDRLDI 145
BAH_plant_3 cd04713
BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH ...
 46-94 1.04e-03

BAH, or Bromo Adjacent Homology domain, plant-specific sub-family with unknown function. BAH domains are found in a variety of proteins playing roles in transcriptional silencing and the remodeling of chromatin. It is assumed that in most or all of these instances the BAH domain mediates protein-protein interactions.


Pssm-ID: 240064  Cd Length: 146  Bit Score: 40.14  E-value: 1.04e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 81912958  46 IKVGQFVLIQGEDNQKPYVA--KLIELFENGSevpPKkyARVQWFVRFCEI 94
Cdd:cd04713  21 YRLEDCVLLVPEDDQKPYIAiiKDIYKQEEGS---LK--LEVQWLYRPEEI 66
COG3899 COG3899
Predicted ATPase [General function prediction only];
426-536 1.09e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 42.92  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81912958  426 QSRTRRTASKPSSQTPSKSPKKTFRPRPPLHATPQIRDRNLAVQEPASVLEEARLRLHVSAVPDSLPCREQEFQDIYSFV 505
Cdd:COG3899  224 AAAAPAAPVVLVAALLLALAALLALLLLAARLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAAL 303

                         90       100       110
                 ....*....|....*....|....*....|.
gi 81912958  506 ESkLLDGTGGCMYISGVPGTGKTATVHEVIR 536
Cdd:COG3899  304 ER-ARAGRGELVLVSGEAGIGKSRLVRELAR 333
 
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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