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Conserved domains on  [gi|299890795|ref|NP_001177748|]
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origin recognition complex subunit 1 isoform 2 [Homo sapiens]

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 ...
 44-170 1.31e-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: 1.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  44 EIHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPPKKRARVQWFVRFCEVPACKRHLLGRKPGAQEIFWYDYPACDSN 123
Cdd:cd04719    1 ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDND 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 299890795 124 INAETIIGLVRVIPLAPKDVVP-TNLKNEKTLFVKLSWNEKKFRPLSS 170
Cdd:cd04719   81 IDAETIIGKVRVEPVEPKTDLPeTKKKTGGPLFVKRYWDTKTFRSLDS 128
PTZ00112 super family cl36513
origin recognition complex 1 protein; Provisional
 490-738 2.57e-47

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: 182.88  E-value: 2.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  490 LHVSAVPESLPCREQEFQDIYNFVESKLlDHTGG--CMYISGVPGTGKTATVHEVIRCLQQAAQANDVPPFQYIEVNGMK 567
Cdd:PTZ00112  748 MQLDVVPKYLPCREKEIKEVHGFLESGI-KQSGSnqILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMN 826

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  568 LTEPHQVYvQILQKLTGQKATAN--HAAELLAKQFC-TRGSPQETTVLLVDELDLLWTHKQDIMYNLFDWPTHKEARLVV 644
Cdd:PTZ00112  827 VVHPNAAY-QVLYKQLFNKKPPNalNSFKILDRLFNqNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVL 905

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  645 LAIANTMDLPERiMMNRVSSRLGLTRMCFQPYTYSQLQQILRSRLKHLKAFED-DAIQLVARKVAALSGDARRCLDICRR 723
Cdd:PTZ00112  906 IAISNTMDLPER-LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRK 984

                         250       260
                  ....*....|....*....|....*.
gi 299890795  724 ATE-----------ICEFSQQKPDSP 738
Cdd:PTZ00112  985 AFEnkrgqkivprdITEATNQLFDSP 1010
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 773-852 3.48e-18

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: 79.94  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  773 LRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPS----RNDLLLRVRLNVSQDD 848
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 299890795  849 VLYA 852
Cdd:pfam09079  81 VLEA 84
rne super family cl35953
ribonuclease E; Reviewed
 362-482 3.48e-04

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 44.26  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  362 DAKEAKAQNEATSTPHRIRrkssvltmNRIRQQLRflgnsKSDQEEKEILPAAEISDSSSDEEEASTPPLPRRAPRTVSR 441
Cdd:PRK10811  661 VTEKARTQDEQQQAPRRER--------QRRRNDEK-----RQAQQEAKALNVEEQSVQETEQEERVQQVQPRRKQRQLNQ 727

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 299890795  442 NLR-----SSLKSSLHTLTKLKPRTPRCAAPQIRSRSLAAQEPASV 482
Cdd:PRK10811  728 KVRieqsvAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVA 773
 
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 1.31e-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: 1.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  44 EIHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPPKKRARVQWFVRFCEVPACKRHLLGRKPGAQEIFWYDYPACDSN 123
Cdd:cd04719    1 ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDND 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 299890795 124 INAETIIGLVRVIPLAPKDVVP-TNLKNEKTLFVKLSWNEKKFRPLSS 170
Cdd:cd04719   81 IDAETIIGKVRVEPVEPKTDLPeTKKKTGGPLFVKRYWDTKTFRSLDS 128
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 490-738 2.57e-47

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 182.88  E-value: 2.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  490 LHVSAVPESLPCREQEFQDIYNFVESKLlDHTGG--CMYISGVPGTGKTATVHEVIRCLQQAAQANDVPPFQYIEVNGMK 567
Cdd:PTZ00112  748 MQLDVVPKYLPCREKEIKEVHGFLESGI-KQSGSnqILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMN 826

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  568 LTEPHQVYvQILQKLTGQKATAN--HAAELLAKQFC-TRGSPQETTVLLVDELDLLWTHKQDIMYNLFDWPTHKEARLVV 644
Cdd:PTZ00112  827 VVHPNAAY-QVLYKQLFNKKPPNalNSFKILDRLFNqNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVL 905

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  645 LAIANTMDLPERiMMNRVSSRLGLTRMCFQPYTYSQLQQILRSRLKHLKAFED-DAIQLVARKVAALSGDARRCLDICRR 723
Cdd:PTZ00112  906 IAISNTMDLPER-LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRK 984

                         250       260
                  ....*....|....*....|....*.
gi 299890795  724 ATE-----------ICEFSQQKPDSP 738
Cdd:PTZ00112  985 AFEnkrgqkivprdITEATNQLFDSP 1010
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
490-806 1.04e-33

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 133.82  E-value: 1.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 490 LHVSAVPESLPCREQEFQDIYNFVESKLLDHTGGCMYISGVPGTGKTATVHEVIRCLQQAAQANDVpPFQYIEVNGMKLT 569
Cdd:COG1474   19 LSPDYVPDRLPHREEEIEELASALRPALRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGV-DVRVVYVNCRQAS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 570 EPHQVYVQILQKLTGQK---ATANHAAEL---LAKQFCTRGSP-----------QEttvllvdeldllwTHKQDIMYNLF 632
Cdd:COG1474   98 TRYRVLSRILEELGSGEdipSTGLSTDELfdrLYEALDERDGVlvvvldeidylVD-------------DEGDDLLYQLL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 633 DWPT-HKEARLVVLAIANTMDLPERiMMNRVSSRLGLTRMCFQPYTYSQLQQILRSRLKHlkAF-----EDDAIQLVARK 706
Cdd:COG1474  165 RANEeLEGARVGVIGISNDLEFLEN-LDPRVKSSLGEEEIVFPPYDADELRDILEDRAEL--AFydgvlSDEVIPLIAAL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 707 VAALSGDARRCLDICRRATEICEFSQQKpdspgLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAIlAEFRRSGLE 786
Cdd:COG1474  242 AAQEHGDARKAIDLLRVAGEIAEREGSD-----RVTEEHVREAREKIERDRLLEVLRGLPTHEKLVLLAI-AELLKDGED 315

                        330       340
                 ....*....|....*....|
gi 299890795 787 EATFQQIYSQHVALCRMEGL 806
Cdd:COG1474  316 PVRTGEVYEAYEELCEELGV 335
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 45-169 2.25e-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: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795   45 IHIQIGQFVLIEGDD-DENPYVAKLLELFEDDSDppPKKRARVQWFVRFCEVPacKRHLLGRKPGaqEIFWYDYPACdsn 123
Cdd:pfam01426   1 ETYSVGDFVLVEPDDaDEPYYVARIEELFEDTKN--GKKMVRVQWFYRPEETV--HRAGKAFNKD--ELFLSDEEDD--- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 299890795  124 INAETIIGLVRVIPLAP-KDVVPTNLKNEKTLFVKLSWNE--KKFRPLS 169
Cdd:pfam01426  72 VPLSAIIGKCSVLHKSDlESLDPYKIKEPDDFFCELLYDPktKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
46-169 1.22e-23

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 96.59  E-value: 1.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795    46 HIQIGQFVLIEGDD-DENPYVAKLLELFEDDSDPPPKKrARVQWFVRFCEVPACKRHLLGRkpgaQEIFWYDypaCDSNI 124
Cdd:smart00439   1 TISVGDFVLVEPDDaDEPYYIGRIEEIFETKKNSESKM-VRVRWFYRPEETVLEKAALFDK----NEVFLSD---EYDTV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 299890795   125 NAETIIGLVRVIPLAPKDVVPTNLKN--EKTLFVKLSWNEKKFRPLS 169
Cdd:smart00439  73 PLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSFKK 119
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 490-752 2.72e-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: 2.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  490 LHVSAVPESLPCREQEFQDIYNFVESKLLDHTGGCMYISGVPGTGKTATVHEVIRCLQQAAQANDVpPFQYIEVNGMKLT 569
Cdd:TIGR02928   8 LEPDYVPDRIVHRDEQIEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAEDRDV-RVVTVYVNCQILD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  570 EPHQVYVQILQKLTGQkatanhaaellAKQFCTRGSPQETTVLLVDELDLL---------------WTHKQDIMYNL--- 631
Cdd:TIGR02928  87 TLYQVLVELANQLRGS-----------GEEVPTTGLSTSEVFRRLYKELNErgdsliivldeidylVGDDDDLLYQLsra 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  632 FDWPTHKEARLVVLAIANTMDLPERIMMnRVSSRLGLTRMCFQPYTYSQLQQILRSRLKhlKAF-----EDDAIQLVARK 706
Cdd:TIGR02928 156 RSNGDLDNAKVGVIGISNDLKFRENLDP-RVKSSLCEEEIIFPPYDAEELRDILENRAE--KAFydgvlDDGVIPLCAAL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 299890795  707 VAALSGDARRCLDICRRATEICEFsqqkpDSPGLVTIAHSMEAVDE 752
Cdd:TIGR02928 233 AAQEHGDARKAIDLLRVAGEIAER-----EGAERVTEDHVEKAQEK 273
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 773-852 3.48e-18

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: 79.94  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  773 LRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPS----RNDLLLRVRLNVSQDD 848
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 299890795  849 VLYA 852
Cdd:pfam09079  81 VLEA 84
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 766-849 4.09e-18

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: 79.59  E-value: 4.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 766 SVLEQSFLRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPSRNDL---LLRVRL 842
Cdd:cd08768    1 PLHQKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISL 80


                 ....*..
gi 299890795 843 NVSQDDV 849
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 ...
 773-853 1.74e-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: 74.98  E-value: 1.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795   773 LRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPS---RNDLLLRVRLNVSQDDV 849
Cdd:smart01074   1 LLAIVLLLTRGGKEEVTTGEVYEVYKELCKELGVDPLTYTRIYDLLNELEMLGIIELRVSnrgRRGRTREISLNVDPDDV 80


                   ....
gi 299890795   850 LYAL 853
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 ...
 697-729 1.82e-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: 1.82e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 299890795  697 DDAIQLVARKVAALSGDARRCLDICRRATEICE 729
Cdd:pfam17872  47 DDAIEIASRKVASVSGDARRALKICKRAAEIAE 79
rne PRK10811
ribonuclease E; Reviewed
 362-482 3.48e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 44.26  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  362 DAKEAKAQNEATSTPHRIRrkssvltmNRIRQQLRflgnsKSDQEEKEILPAAEISDSSSDEEEASTPPLPRRAPRTVSR 441
Cdd:PRK10811  661 VTEKARTQDEQQQAPRRER--------QRRRNDEK-----RQAQQEAKALNVEEQSVQETEQEERVQQVQPRRKQRQLNQ 727

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 299890795  442 NLR-----SSLKSSLHTLTKLKPRTPRCAAPQIRSRSLAAQEPASV 482
Cdd:PRK10811  728 KVRieqsvAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVA 773
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 505-595 2.94e-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: 39.05  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 505 EFQDIYNFVESKLLDHTGGCMYISGVPGTGKTATVHEVirclqqaAQANDVPPFQYIEVNGMKLTEPHQVYVQILQKLTG 584
Cdd:cd00009    2 GQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAI-------ANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVR 74

                         90
                 ....*....|.
gi 299890795 585 QKATANHAAEL 595
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 1.31e-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: 1.31e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  44 EIHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDPPPKKRARVQWFVRFCEVPACKRHLLGRKPGAQEIFWYDYPACDSN 123
Cdd:cd04719    1 ALTIEVGDFVLIEGEDADGPDVARILHLYEDGNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDND 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 299890795 124 INAETIIGLVRVIPLAPKDVVP-TNLKNEKTLFVKLSWNEKKFRPLSS 170
Cdd:cd04719   81 IDAETIIGKVRVEPVEPKTDLPeTKKKTGGPLFVKRYWDTKTFRSLDS 128
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 490-738 2.57e-47

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 182.88  E-value: 2.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  490 LHVSAVPESLPCREQEFQDIYNFVESKLlDHTGG--CMYISGVPGTGKTATVHEVIRCLQQAAQANDVPPFQYIEVNGMK 567
Cdd:PTZ00112  748 MQLDVVPKYLPCREKEIKEVHGFLESGI-KQSGSnqILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMN 826

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  568 LTEPHQVYvQILQKLTGQKATAN--HAAELLAKQFC-TRGSPQETTVLLVDELDLLWTHKQDIMYNLFDWPTHKEARLVV 644
Cdd:PTZ00112  827 VVHPNAAY-QVLYKQLFNKKPPNalNSFKILDRLFNqNKKDNRNVSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVL 905

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  645 LAIANTMDLPERiMMNRVSSRLGLTRMCFQPYTYSQLQQILRSRLKHLKAFED-DAIQLVARKVAALSGDARRCLDICRR 723
Cdd:PTZ00112  906 IAISNTMDLPER-LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRK 984

                         250       260
                  ....*....|....*....|....*.
gi 299890795  724 ATE-----------ICEFSQQKPDSP 738
Cdd:PTZ00112  985 AFEnkrgqkivprdITEATNQLFDSP 1010
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
490-806 1.04e-33

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 133.82  E-value: 1.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 490 LHVSAVPESLPCREQEFQDIYNFVESKLLDHTGGCMYISGVPGTGKTATVHEVIRCLQQAAQANDVpPFQYIEVNGMKLT 569
Cdd:COG1474   19 LSPDYVPDRLPHREEEIEELASALRPALRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGV-DVRVVYVNCRQAS 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 570 EPHQVYVQILQKLTGQK---ATANHAAEL---LAKQFCTRGSP-----------QEttvllvdeldllwTHKQDIMYNLF 632
Cdd:COG1474   98 TRYRVLSRILEELGSGEdipSTGLSTDELfdrLYEALDERDGVlvvvldeidylVD-------------DEGDDLLYQLL 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 633 DWPT-HKEARLVVLAIANTMDLPERiMMNRVSSRLGLTRMCFQPYTYSQLQQILRSRLKHlkAF-----EDDAIQLVARK 706
Cdd:COG1474  165 RANEeLEGARVGVIGISNDLEFLEN-LDPRVKSSLGEEEIVFPPYDADELRDILEDRAEL--AFydgvlSDEVIPLIAAL 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 707 VAALSGDARRCLDICRRATEICEFSQQKpdspgLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAIlAEFRRSGLE 786
Cdd:COG1474  242 AAQEHGDARKAIDLLRVAGEIAEREGSD-----RVTEEHVREAREKIERDRLLEVLRGLPTHEKLVLLAI-AELLKDGED 315

                        330       340
                 ....*....|....*....|
gi 299890795 787 EATFQQIYSQHVALCRMEGL 806
Cdd:COG1474  316 PVRTGEVYEAYEELCEELGV 335
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 45-169 2.25e-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: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795   45 IHIQIGQFVLIEGDD-DENPYVAKLLELFEDDSDppPKKRARVQWFVRFCEVPacKRHLLGRKPGaqEIFWYDYPACdsn 123
Cdd:pfam01426   1 ETYSVGDFVLVEPDDaDEPYYVARIEELFEDTKN--GKKMVRVQWFYRPEETV--HRAGKAFNKD--ELFLSDEEDD--- 71

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 299890795  124 INAETIIGLVRVIPLAP-KDVVPTNLKNEKTLFVKLSWNE--KKFRPLS 169
Cdd:pfam01426  72 VPLSAIIGKCSVLHKSDlESLDPYKIKEPDDFFCELLYDPktKSFKKLP 120
BAH smart00439
Bromo adjacent homology domain;
46-169 1.22e-23

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 96.59  E-value: 1.22e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795    46 HIQIGQFVLIEGDD-DENPYVAKLLELFEDDSDPPPKKrARVQWFVRFCEVPACKRHLLGRkpgaQEIFWYDypaCDSNI 124
Cdd:smart00439   1 TISVGDFVLVEPDDaDEPYYIGRIEEIFETKKNSESKM-VRVRWFYRPEETVLEKAALFDK----NEVFLSD---EYDTV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 299890795   125 NAETIIGLVRVIPLAPKDVVPTNLKN--EKTLFVKLSWNEKKFRPLS 169
Cdd:smart00439  73 PLSDIIGKCNVLYKSDYPGLRPEGSIgePDVFFCESAYDPEKGSFKK 119
cdc6 PRK00411
ORC1-type DNA replication protein;
495-806 3.57e-22

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 99.54  E-value: 3.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 495 VPESLPCREQEFQDI-YNFVeSKLLDHTGGCMYISGVPGTGKTATVHEVIRCLQQAAQandvpPFQYIEVNGMKLTEPHQ 573
Cdd:PRK00411  28 VPENLPHREEQIEELaFALR-PALRGSRPLNVLIYGPPGTGKTTTVKKVFEELEEIAV-----KVVYVYINCQIDRTRYA 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 574 VYVQILQKLTGQ-------------KATANHAAE-----LLA-----KQFCTRGSpqettvllvdeldllwthkqDIMYN 630
Cdd:PRK00411 102 IFSEIARQLFGHpppssglsfdelfDKIAEYLDErdrvlIVAlddinYLFEKEGN--------------------DVLYS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 631 LFDWPT-HKEARLVVLAIANTMDLPERIMMnRVSSRLGLTRMCFQPYTYSQLQQILRSRLKHlkAF-----EDDAIQLVA 704
Cdd:PRK00411 162 LLRAHEeYPGARIGVIGISSDLTFLYILDP-RVKSVFRPEEIYFPPYTADEIFDILKDRVEE--GFypgvvDDEVLDLIA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 705 RKVAALSGDARRCLDICRRATEICEFSQQKpdspgLVTIAHSMEAVDEMFSSSYITAIKNSSVLEQSFLRAIlAEFRRSG 784
Cdd:PRK00411 239 DLTAREHGDARVAIDLLRRAGLIAEREGSR-----KVTEEDVRKAYEKSEIVHLSEVLRTLPLHEKLLLRAI-VRLLKKG 312

                        330       340
                 ....*....|....*....|..
gi 299890795 785 LEEATFQQIYSQHVALCRMEGL 806
Cdd:PRK00411 313 GDEVTTGEVYEEYKELCEELGY 334
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 490-752 2.72e-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: 2.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  490 LHVSAVPESLPCREQEFQDIYNFVESKLLDHTGGCMYISGVPGTGKTATVHEVIRCLQQAAQANDVpPFQYIEVNGMKLT 569
Cdd:TIGR02928   8 LEPDYVPDRIVHRDEQIEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAEDRDV-RVVTVYVNCQILD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  570 EPHQVYVQILQKLTGQkatanhaaellAKQFCTRGSPQETTVLLVDELDLL---------------WTHKQDIMYNL--- 631
Cdd:TIGR02928  87 TLYQVLVELANQLRGS-----------GEEVPTTGLSTSEVFRRLYKELNErgdsliivldeidylVGDDDDLLYQLsra 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  632 FDWPTHKEARLVVLAIANTMDLPERIMMnRVSSRLGLTRMCFQPYTYSQLQQILRSRLKhlKAF-----EDDAIQLVARK 706
Cdd:TIGR02928 156 RSNGDLDNAKVGVIGISNDLKFRENLDP-RVKSSLCEEEIIFPPYDAEELRDILENRAE--KAFydgvlDDGVIPLCAAL 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 299890795  707 VAALSGDARRCLDICRRATEICEFsqqkpDSPGLVTIAHSMEAVDE 752
Cdd:TIGR02928 233 AAQEHGDARKAIDLLRVAGEIAER-----EGAERVTEDHVEKAQEK 273
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 773-852 3.48e-18

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: 79.94  E-value: 3.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  773 LRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPS----RNDLLLRVRLNVSQDD 848
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 299890795  849 VLYA 852
Cdd:pfam09079  81 VLEA 84
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 766-849 4.09e-18

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: 79.59  E-value: 4.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 766 SVLEQSFLRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPSRNDL---LLRVRL 842
Cdd:cd08768    1 PLHQKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISL 80


                 ....*..
gi 299890795 843 NVSQDDV 849
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 ...
 773-853 1.74e-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: 74.98  E-value: 1.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795   773 LRAILAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSHLGSCRLLLVEPS---RNDLLLRVRLNVSQDDV 849
Cdd:smart01074   1 LLAIVLLLTRGGKEEVTTGEVYEVYKELCKELGVDPLTYTRIYDLLNELEMLGIIELRVSnrgRRGRTREISLNVDPDDV 80


                   ....
gi 299890795   850 LYAL 853
Cdd:smart01074  81 LEAL 84
BAH cd04370
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 44-169 4.34e-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: 4.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  44 EIHIQIGQFVLIEGDDD---ENPYVAKLLELFEDDSDPppkKRARVQWFVRFCEVPACKRHLLGRKpgaqEIFWydypAC 120
Cdd:cd04370    1 GITYEVGDSVYVEPDDSiksDPPYIARIEELWEDTNGS---KQVKVRWFYRPEETPKGLSPFALRR----ELFL----SD 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 299890795 121 DSNIN-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 ...
 697-729 1.82e-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: 1.82e-09
                          10        20        30
                  ....*....|....*....|....*....|...
gi 299890795  697 DDAIQLVARKVAALSGDARRCLDICRRATEICE 729
Cdd:pfam17872  47 DDAIEIASRKVASVSGDARRALKICKRAAEIAE 79
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 525-670 1.11e-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: 54.14  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  525 MYISGVPGTGKTATVHEVirclqqAAQANdvppFQYIEVNGMKLTEPH--QVYVQILQKLTGQKATANHA-----AELLA 597
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAV------AKELG----APFIEISGSELVSKYvgESEKRLRELFEAAKKLAPCVifideIDALA 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 299890795  598 KqfcTRGSPQETTVLLVdeldllwthkQDIMYNLFDWPTHKEARLVVLAIANTMDLPERIMMNRVSSRLGLTR 670
Cdd:pfam00004  71 G---SRGSGGDSESRRV----------VNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 499-544 1.10e-04

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: 43.65  E-value: 1.10e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 299890795  499 LPCREQEFQDIYNFVEsKLLDHTGGCMYISGVPGTGKTATVHEVIR 544
Cdd:pfam13191   2 LVGREEELEQLLDALD-RVRSGRPPSVLLTGEAGTGKTTLLRELLR 46
rne PRK10811
ribonuclease E; Reviewed
 362-482 3.48e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 44.26  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  362 DAKEAKAQNEATSTPHRIRrkssvltmNRIRQQLRflgnsKSDQEEKEILPAAEISDSSSDEEEASTPPLPRRAPRTVSR 441
Cdd:PRK10811  661 VTEKARTQDEQQQAPRRER--------QRRRNDEK-----RQAQQEAKALNVEEQSVQETEQEERVQQVQPRRKQRQLNQ 727

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 299890795  442 NLR-----SSLKSSLHTLTKLKPRTPRCAAPQIRSRSLAAQEPASV 482
Cdd:PRK10811  728 KVRieqsvAEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPLPVVA 773
AAA_22 pfam13401
AAA domain;
518-597 4.15e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.17  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795  518 LDHTGGCMYISGVPGTGKTATVHEVIRCLQQAaqandvpPFQYIEVNGMKLTEPHQVYVQILQKLTGQKATANHAAELLA 597
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKTTLLRRLLEQLPEV-------RDSVVFVDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLA 73
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 505-595 2.94e-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: 39.05  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 299890795 505 EFQDIYNFVESKLLDHTGGCMYISGVPGTGKTATVHEVirclqqaAQANDVPPFQYIEVNGMKLTEPHQVYVQILQKLTG 584
Cdd:cd00009    2 GQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAI-------ANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVR 74

                         90
                 ....*....|.
gi 299890795 585 QKATANHAAEL 595
Cdd:cd00009   75 LLFELAEKAKP 85
BAH_plantDCM_I cd04716
BAH, or Bromo Adjacent Homology domain, first copy present in DNA (Cytosine-5) ...
 45-94 4.34e-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: 38.19  E-value: 4.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 299890795  45 IHIQIGQFVLIEGDDDENPYVAKLLELFEDDSDpppKKRARVQWFVRFCE 94
Cdd:cd04716    2 ITYNLGDDAYVQGGEGEEPFICKITEFFEGTDG---KTYFTAQWFYRAED 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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