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Conserved domains on  [gi|1411078766|ref|XP_025247039|]
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origin recognition complex subunit 1 [Theropithecus gelada]

Protein Classification

BAH_Orc1p_animal and Cdc6_C domain-containing protein( domain architecture ID 12939701)

protein containing domains BAH_Orc1p_animal, 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 ...
 44-170 1.21e-63

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: 209.54  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  44 EIHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPHKKRARVQWFVRFCEVPACKRHLLGRKPGAQEIFWYDYPACDNN 123
Cdd:cd04719     1 ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDND 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1411078766 124 INAETIIGLVRVIPLAPKDVVP-TNLKNEKTLFVKLSWNEKKFRPLSS 170
Cdd:cd04719    81 IDAETIIGKVRVEPVEPKTDLPeTKKKTGGPLFVKRYWDTKTFRSLDS 128
PTZ00112 super family cl36513
origin recognition complex 1 protein; Provisional
 494-742 7.68e-46

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: 178.65  E-value: 7.68e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  494 LHVSAVPESLPCREQEFQDIYNFVESKLlDRTGG--CMYISGVPGTGKTATVHEVMRCLQQAAQANDVPPFQYIEVNGMK 571
Cdd:PTZ00112   748 MQLDVVPKYLPCREKEIKEVHGFLESGI-KQSGSnqILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMN 826

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  572 LTEPHQVYvQILQKLTGQKATAN--HAAELLAKRFC-TRGSPQETTVLLVDELDLLWTHKQDIMYNLFDWPTHKEARLVV 648
Cdd:PTZ00112   827 VVHPNAAY-QVLYKQLFNKKPPNalNSFKILDRLFNqNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVL 905

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  649 LTIANTMDLPERiMLNRVSSRLGLTRMSFQPYTYSQLQQILRSRLKQLKAFED-DAIQLVARKVAALSGDARRCLDICRR 727
Cdd:PTZ00112   906 IAISNTMDLPER-LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRK 984

                          250       260
                   ....*....|....*....|....*.
gi 1411078766  728 ATE-----------ICEFSQQKPDSP 742
Cdd:PTZ00112   985 AFEnkrgqkivprdITEATNQLFDSP 1010
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 770-853 1.43e-17

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: 78.05  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 770 SVLEQSFLRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLSYPTVSETMAVCSHLGSCRLLLVEPSRNDL---LLRVRL 846
Cdd:cd08768     1 PLHQKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISL 80


                  ....*..
gi 1411078766 847 NVSQDDV 853
Cdd:cd08768    81 NVDPDDV 87
 
Name Accession Description Interval E-value
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 44-170 1.21e-63

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: 209.54  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  44 EIHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPHKKRARVQWFVRFCEVPACKRHLLGRKPGAQEIFWYDYPACDNN 123
Cdd:cd04719     1 ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDND 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1411078766 124 INAETIIGLVRVIPLAPKDVVP-TNLKNEKTLFVKLSWNEKKFRPLSS 170
Cdd:cd04719    81 IDAETIIGKVRVEPVEPKTDLPeTKKKTGGPLFVKRYWDTKTFRSLDS 128
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 494-742 7.68e-46

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 178.65  E-value: 7.68e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  494 LHVSAVPESLPCREQEFQDIYNFVESKLlDRTGG--CMYISGVPGTGKTATVHEVMRCLQQAAQANDVPPFQYIEVNGMK 571
Cdd:PTZ00112   748 MQLDVVPKYLPCREKEIKEVHGFLESGI-KQSGSnqILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMN 826

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  572 LTEPHQVYvQILQKLTGQKATAN--HAAELLAKRFC-TRGSPQETTVLLVDELDLLWTHKQDIMYNLFDWPTHKEARLVV 648
Cdd:PTZ00112   827 VVHPNAAY-QVLYKQLFNKKPPNalNSFKILDRLFNqNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVL 905

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  649 LTIANTMDLPERiMLNRVSSRLGLTRMSFQPYTYSQLQQILRSRLKQLKAFED-DAIQLVARKVAALSGDARRCLDICRR 727
Cdd:PTZ00112   906 IAISNTMDLPER-LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRK 984

                          250       260
                   ....*....|....*....|....*.
gi 1411078766  728 ATE-----------ICEFSQQKPDSP 742
Cdd:PTZ00112   985 AFEnkrgqkivprdITEATNQLFDSP 1010
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
494-817 8.48e-36

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 139.98  E-value: 8.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 494 LHVSAVPESLPCREQEFQDIYNFVESKLLDRTGGCMYISGVPGTGKTATVHEVMRCLQQAAQANDVPpFQYIEVNGMKLT 573
Cdd:COG1474    19 LSPDYVPDRLPHREEEIEELASALRPALRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGVD-VRVVYVNCRQAS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 574 EPHQVYVQILQKLTGQK---ATANHAAEL---LAKRFCTRGSP-----------QETtvllvdeldllwtHKQDIMYNLF 636
Cdd:COG1474    98 TRYRVLSRILEELGSGEdipSTGLSTDELfdrLYEALDERDGVlvvvldeidylVDD-------------EGDDLLYQLL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 637 DWPT-HKEARLVVLTIANTMDLPERimLN-RVSSRLGLTRMSFQPYTYSQLQQILRSRLKQlkAF-----EDDAIQLVAR 709
Cdd:COG1474   165 RANEeLEGARVGVIGISNDLEFLEN--LDpRVKSSLGEEEIVFPPYDADELRDILEDRAEL--AFydgvlSDEVIPLIAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 710 KVAALSGDARRCLDICRRATEICEFSQQKpdspgLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAIlAEFRRSGL 789
Cdd:COG1474   241 LAAQEHGDARKAIDLLRVAGEIAEREGSD-----RVTEEHVREAREKIERDRLLEVLRGLPTHEKLVLLAI-AELLKDGE 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1411078766 790 EEATFQQIYSQHVALCRMEG---LSYPTVSE 817
Cdd:COG1474   315 DPVRTGEVYEAYEELCEELGvdpLSYRRVRD 345
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 45-169 2.26e-24

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: 98.92  E-value: 2.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  45 IHIQIGQFVLIEGDD-DENPYVAKLLELFEDDSDppHKKRARVQWFVRFCEVPacKRHLLGRKPGaqEIFWYDYPACdnn 123
Cdd:pfam01426   1 ETYSVGDFVLVEPDDaDEPYYVARIEELFEDTKN--GKKMVRVQWFYRPEETV--HRAGKAFNKD--ELFLSDEEDD--- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1411078766 124 INAETIIGLVRVIPLAP-KDVVPTNLKNEKTLFVKLSWNE--KKFRPLS 169
Cdd:pfam01426  72 VPLSAIIGKCSVLHKSDlESLDPYKIKEPDDFFCELLYDPktKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
46-169 3.85e-24

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 98.13  E-value: 3.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766   46 HIQIGQFVLIEGDD-DENPYVAKLLELFEDDSDPpHKKRARVQWFVRFCEVPACKRHLLGRkpgaQEIFWYDypaCDNNI 124
Cdd:smart00439   1 TISVGDFVLVEPDDaDEPYYIGRIEEIFETKKNS-ESKMVRVRWFYRPEETVLEKAALFDK----NEVFLSD---EYDTV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1411078766  125 NAETIIGLVRVIPLAPKDVVPTNLKN--EKTLFVKLSWNEKKFRPLS 169
Cdd:smart00439  73 PLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSFKK 119
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 494-826 1.85e-22

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: 100.01  E-value: 1.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 494 LHVSAVPESLPCREQEFQDIYNFVESKLLDRTGGCMYISGVPGTGKTATVHEVMRCLQQAAQANDVpPFQYIEVNGMKLT 573
Cdd:TIGR02928   8 LEPDYVPDRIVHRDEQIEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAEDRDV-RVVTVYVNCQILD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 574 EPHQVYVQILQKLTG-------QKATANHAAELLAKRFCTRGspqETTVLLVDELDLLWTHKQDIMYNL---FDWPTHKE 643
Cdd:TIGR02928  87 TLYQVLVELANQLRGsgeevptTGLSTSEVFRRLYKELNERG---DSLIIVLDEIDYLVGDDDDLLYQLsraRSNGDLDN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 644 ARLVVLTIANTMDLPERIMlNRVSSRLGLTRMSFQPYTYSQLQQILRSRLKqlKAF-----EDDAIQLVARKVAALSGDA 718
Cdd:TIGR02928 164 AKVGVIGISNDLKFRENLD-PRVKSSLCEEEIIFPPYDAEELRDILENRAE--KAFydgvlDDGVIPLCAALAAQEHGDA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 719 RRCLDICRRATEICEFsqqkpDSPGLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAIlAEFRRSGLEEATFQQIY 798
Cdd:TIGR02928 241 RKAIDLLRVAGEIAER-----EGAERVTEDHVEKAQEKIEKDRLLELIRGLPTHSKLVLLAI-ANLAANDEDPFRTGEVY 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1411078766 799 SQHVALCR---MEGLSYPTVSETMAVCSHLG 826
Cdd:TIGR02928 315 EVYKEVCEdigVDPLTQRRISDLLNELDMLG 345
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 770-853 1.43e-17

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: 78.05  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 770 SVLEQSFLRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLSYPTVSETMAVCSHLGSCRLLLVEPSRNDL---LLRVRL 846
Cdd:cd08768     1 PLHQKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISL 80


                  ....*..
gi 1411078766 847 NVSQDDV 853
Cdd:cd08768    81 NVDPDDV 87
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 777-856 1.90e-17

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: 77.63  E-value: 1.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 777 LRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLSYPTVSETMAVCSHLGSCRLLLVEPS----RNDLLLRVRLNVSQDD 852
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 1411078766 853 VLYA 856
Cdd:pfam09079  81 VLEA 84
Cdc6_C smart01074
CDC6, C terminal; The C terminal domain of CDC6 assumes a winged helix fold, with a five ...
 777-857 2.77e-16

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: 74.59  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  777 LRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLSYPTVSETMAVCSHLGSCRLLLVEPS---RNDLLLRVRLNVSQDDV 853
Cdd:smart01074   1 LLAIVLLLTRGGKEEVTTGEVYEVYKELCKELGVDPLTYTRIYDLLNELEMLGIIELRVSnrgRRGRTREISLNVDPDDV 80


                   ....
gi 1411078766  854 LYAL 857
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 ...
 701-733 1.61e-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: 55.59  E-value: 1.61e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1411078766 701 DDAIQLVARKVAALSGDARRCLDICRRATEICE 733
Cdd:pfam17872  47 DDAIEIASRKVASVSGDARRALKICKRAAEIAE 79
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 509-599 2.29e-03

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: 39.44  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 509 EFQDIYNFVESKLLDRTGGCMYISGVPGTGKTATVHEVmrclqqaAQANDVPPFQYIEVNGMKLTEPHQVYVQILQKLTG 588
Cdd:cd00009     2 GQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAI-------ANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVR 74

                          90
                  ....*....|.
gi 1411078766 589 QKATANHAAEL 599
Cdd:cd00009    75 LLFELAEKAKP 85
 
Name Accession Description Interval E-value
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 44-170 1.21e-63

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: 209.54  E-value: 1.21e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  44 EIHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPHKKRARVQWFVRFCEVPACKRHLLGRKPGAQEIFWYDYPACDNN 123
Cdd:cd04719     1 ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDND 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1411078766 124 INAETIIGLVRVIPLAPKDVVP-TNLKNEKTLFVKLSWNEKKFRPLSS 170
Cdd:cd04719    81 IDAETIIGKVRVEPVEPKTDLPeTKKKTGGPLFVKRYWDTKTFRSLDS 128
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 494-742 7.68e-46

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 178.65  E-value: 7.68e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  494 LHVSAVPESLPCREQEFQDIYNFVESKLlDRTGG--CMYISGVPGTGKTATVHEVMRCLQQAAQANDVPPFQYIEVNGMK 571
Cdd:PTZ00112   748 MQLDVVPKYLPCREKEIKEVHGFLESGI-KQSGSnqILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMN 826

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  572 LTEPHQVYvQILQKLTGQKATAN--HAAELLAKRFC-TRGSPQETTVLLVDELDLLWTHKQDIMYNLFDWPTHKEARLVV 648
Cdd:PTZ00112   827 VVHPNAAY-QVLYKQLFNKKPPNalNSFKILDRLFNqNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVL 905

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  649 LTIANTMDLPERiMLNRVSSRLGLTRMSFQPYTYSQLQQILRSRLKQLKAFED-DAIQLVARKVAALSGDARRCLDICRR 727
Cdd:PTZ00112   906 IAISNTMDLPER-LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRK 984

                          250       260
                   ....*....|....*....|....*.
gi 1411078766  728 ATE-----------ICEFSQQKPDSP 742
Cdd:PTZ00112   985 AFEnkrgqkivprdITEATNQLFDSP 1010
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
494-817 8.48e-36

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 139.98  E-value: 8.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 494 LHVSAVPESLPCREQEFQDIYNFVESKLLDRTGGCMYISGVPGTGKTATVHEVMRCLQQAAQANDVPpFQYIEVNGMKLT 573
Cdd:COG1474    19 LSPDYVPDRLPHREEEIEELASALRPALRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGVD-VRVVYVNCRQAS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 574 EPHQVYVQILQKLTGQK---ATANHAAEL---LAKRFCTRGSP-----------QETtvllvdeldllwtHKQDIMYNLF 636
Cdd:COG1474    98 TRYRVLSRILEELGSGEdipSTGLSTDELfdrLYEALDERDGVlvvvldeidylVDD-------------EGDDLLYQLL 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 637 DWPT-HKEARLVVLTIANTMDLPERimLN-RVSSRLGLTRMSFQPYTYSQLQQILRSRLKQlkAF-----EDDAIQLVAR 709
Cdd:COG1474   165 RANEeLEGARVGVIGISNDLEFLEN--LDpRVKSSLGEEEIVFPPYDADELRDILEDRAEL--AFydgvlSDEVIPLIAA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 710 KVAALSGDARRCLDICRRATEICEFSQQKpdspgLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAIlAEFRRSGL 789
Cdd:COG1474   241 LAAQEHGDARKAIDLLRVAGEIAEREGSD-----RVTEEHVREAREKIERDRLLEVLRGLPTHEKLVLLAI-AELLKDGE 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1411078766 790 EEATFQQIYSQHVALCRMEG---LSYPTVSE 817
Cdd:COG1474   315 DPVRTGEVYEAYEELCEELGvdpLSYRRVRD 345
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 45-169 2.26e-24

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: 98.92  E-value: 2.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  45 IHIQIGQFVLIEGDD-DENPYVAKLLELFEDDSDppHKKRARVQWFVRFCEVPacKRHLLGRKPGaqEIFWYDYPACdnn 123
Cdd:pfam01426   1 ETYSVGDFVLVEPDDaDEPYYVARIEELFEDTKN--GKKMVRVQWFYRPEETV--HRAGKAFNKD--ELFLSDEEDD--- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1411078766 124 INAETIIGLVRVIPLAP-KDVVPTNLKNEKTLFVKLSWNE--KKFRPLS 169
Cdd:pfam01426  72 VPLSAIIGKCSVLHKSDlESLDPYKIKEPDDFFCELLYDPktKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
46-169 3.85e-24

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 98.13  E-value: 3.85e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766   46 HIQIGQFVLIEGDD-DENPYVAKLLELFEDDSDPpHKKRARVQWFVRFCEVPACKRHLLGRkpgaQEIFWYDypaCDNNI 124
Cdd:smart00439   1 TISVGDFVLVEPDDaDEPYYIGRIEEIFETKKNS-ESKMVRVRWFYRPEETVLEKAALFDK----NEVFLSD---EYDTV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1411078766  125 NAETIIGLVRVIPLAPKDVVPTNLKN--EKTLFVKLSWNEKKFRPLS 169
Cdd:smart00439  73 PLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSFKK 119
cdc6 PRK00411
ORC1-type DNA replication protein;
499-818 1.01e-22

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 101.46  E-value: 1.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 499 VPESLPCREQEFQDI-YNFVESKLLDRTGGCMyISGVPGTGKTATVHEVMRCLQQAAQandvpPFQYIEVNGMKLTEPHQ 577
Cdd:PRK00411   28 VPENLPHREEQIEELaFALRPALRGSRPLNVL-IYGPPGTGKTTTVKKVFEELEEIAV-----KVVYVYINCQIDRTRYA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 578 VYVQILQKLTGQ-------------KATANHAAE----LL-----AKRFCTrgspqettvllvdeldllwTHKQDIMYNL 635
Cdd:PRK00411  102 IFSEIARQLFGHpppssglsfdelfDKIAEYLDErdrvLIvalddINYLFE-------------------KEGNDVLYSL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 636 FDWPT-HKEARLVVLTIANTMDLPEriMLN-RVSSRLGLTRMSFQPYTYSQLQQILRSRLKQlkAF-----EDDAIQLVA 708
Cdd:PRK00411  163 LRAHEeYPGARIGVIGISSDLTFLY--ILDpRVKSVFRPEEIYFPPYTADEIFDILKDRVEE--GFypgvvDDEVLDLIA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 709 RKVAALSGDARRCLDICRRATEICEFSQQKpdspgLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAIlAEFRRSG 788
Cdd:PRK00411  239 DLTAREHGDARVAIDLLRRAGLIAEREGSR-----KVTEEDVRKAYEKSEIVHLSEVLRTLPLHEKLLLRAI-VRLLKKG 312

                         330       340       350
                  ....*....|....*....|....*....|
gi 1411078766 789 LEEATFQQIYSQHVALCrmEGLSYPTVSET 818
Cdd:PRK00411  313 GDEVTTGEVYEEYKELC--EELGYEPRTHT 340
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 494-826 1.85e-22

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: 100.01  E-value: 1.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 494 LHVSAVPESLPCREQEFQDIYNFVESKLLDRTGGCMYISGVPGTGKTATVHEVMRCLQQAAQANDVpPFQYIEVNGMKLT 573
Cdd:TIGR02928   8 LEPDYVPDRIVHRDEQIEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAEDRDV-RVVTVYVNCQILD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 574 EPHQVYVQILQKLTG-------QKATANHAAELLAKRFCTRGspqETTVLLVDELDLLWTHKQDIMYNL---FDWPTHKE 643
Cdd:TIGR02928  87 TLYQVLVELANQLRGsgeevptTGLSTSEVFRRLYKELNERG---DSLIIVLDEIDYLVGDDDDLLYQLsraRSNGDLDN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 644 ARLVVLTIANTMDLPERIMlNRVSSRLGLTRMSFQPYTYSQLQQILRSRLKqlKAF-----EDDAIQLVARKVAALSGDA 718
Cdd:TIGR02928 164 AKVGVIGISNDLKFRENLD-PRVKSSLCEEEIIFPPYDAEELRDILENRAE--KAFydgvlDDGVIPLCAALAAQEHGDA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 719 RRCLDICRRATEICEFsqqkpDSPGLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAIlAEFRRSGLEEATFQQIY 798
Cdd:TIGR02928 241 RKAIDLLRVAGEIAER-----EGAERVTEDHVEKAQEKIEKDRLLELIRGLPTHSKLVLLAI-ANLAANDEDPFRTGEVY 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1411078766 799 SQHVALCR---MEGLSYPTVSETMAVCSHLG 826
Cdd:TIGR02928 315 EVYKEVCEdigVDPLTQRRISDLLNELDMLG 345
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 770-853 1.43e-17

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: 78.05  E-value: 1.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 770 SVLEQSFLRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLSYPTVSETMAVCSHLGSCRLLLVEPSRNDL---LLRVRL 846
Cdd:cd08768     1 PLHQKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISL 80


                  ....*..
gi 1411078766 847 NVSQDDV 853
Cdd:cd08768    81 NVDPDDV 87
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 777-856 1.90e-17

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: 77.63  E-value: 1.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 777 LRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLSYPTVSETMAVCSHLGSCRLLLVEPS----RNDLLLRVRLNVSQDD 852
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 1411078766 853 VLYA 856
Cdd:pfam09079  81 VLEA 84
Cdc6_C smart01074
CDC6, C terminal; The C terminal domain of CDC6 assumes a winged helix fold, with a five ...
 777-857 2.77e-16

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: 74.59  E-value: 2.77e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  777 LRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLSYPTVSETMAVCSHLGSCRLLLVEPS---RNDLLLRVRLNVSQDDV 853
Cdd:smart01074   1 LLAIVLLLTRGGKEEVTTGEVYEVYKELCKELGVDPLTYTRIYDLLNELEMLGIIELRVSnrgRRGRTREISLNVDPDDV 80


                   ....
gi 1411078766  854 LYAL 857
Cdd:smart01074  81 LEAL 84
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 44-169 4.00e-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: 58.17  E-value: 4.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766  44 EIHIQIGQFVLIEGDDD---ENPYVAKLLELFEDDSdppHKKRARVQWFVRFCEVPACKRHLLGRKpgaqEIFWydypAC 120
Cdd:cd04370     1 GITYEVGDSVYVEPDDSiksDPPYIARIEELWEDTN---GSKQVKVRWFYRPEETPKGLSPFALRR----ELFL----SD 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1411078766 121 DNNIN-AETIIGLVRVIPLAP--KDVVPTNLKNEKTLFVKLSWNE--KKFRPLS 169
Cdd:cd04370    70 HLDEIpVESIIGKCKVLFVSEfeGLKQRPNKIDTDDFFCRLAYDPttKEFKALE 123
AAA_lid_10 pfam17872
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 701-733 1.61e-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: 55.59  E-value: 1.61e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1411078766 701 DDAIQLVARKVAALSGDARRCLDICRRATEICE 733
Cdd:pfam17872  47 DDAIEIASRKVASVSGDARRALKICKRAAEIAE 79
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 529-674 2.06e-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: 53.37  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 529 MYISGVPGTGKTATVHEVmrclqqAAQANdvppFQYIEVNGMKLTEPH--QVYVQILQKLTGQKATAN--------HAae 598
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAV------AKELG----APFIEISGSELVSKYvgESEKRLRELFEAAKKLAPcvifideiDA-- 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1411078766 599 LLAKRFCTRGSPQETTvllvdeldllwthkQDIMYNLFDWPTHKEARLVVLTIANTMDLPERIMLNRVSSRLGLTR 674
Cdd:pfam00004  69 LAGSRGSGGDSESRRV--------------VNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 503-548 7.91e-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: 44.03  E-value: 7.91e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1411078766 503 LPCREQEFQDIYNFVEsKLLDRTGGCMYISGVPGTGKTATVHEVMR 548
Cdd:pfam13191   2 LVGREEELEQLLDALD-RVRSGRPPSVLLTGEAGTGKTTLLRELLR 46
AAA_22 pfam13401
AAA domain;
522-601 5.78e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 40.79  E-value: 5.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 522 LDRTGGCMYISGVPGTGKTATVHEVMRCLQQAaqandvpPFQYIEVNGMKLTEPHQVYVQILQKLTGQKATANHAAELLA 601
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPEV-------RDSVVFVDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLA 73
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 509-599 2.29e-03

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: 39.44  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411078766 509 EFQDIYNFVESKLLDRTGGCMYISGVPGTGKTATVHEVmrclqqaAQANDVPPFQYIEVNGMKLTEPHQVYVQILQKLTG 588
Cdd:cd00009     2 GQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAI-------ANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVR 74

                          90
                  ....*....|.
gi 1411078766 589 QKATANHAAEL 599
Cdd:cd00009    75 LLFELAEKAKP 85
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 45-94 2.59e-03

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: 38.58  E-value: 2.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1411078766  45 IHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPHkkrARVQWFVRFCE 94
Cdd:cd04716     2 ITYNLGDDAYVQGGEGEEPFICKITEFFEGTDGKTY---FTAQWFYRAED 48
 
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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