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Conserved domains on  [gi|23274262|gb|AAH38007|]
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Orc1l protein, partial [Mus musculus]

Protein Classification

P-loop containing Nucleoside Triphosphate Hydrolases and Cdc6_C domain-containing protein( domain architecture ID 13064601)

protein containing domains BAH, 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
PTZ00112 super family cl36513
origin recognition complex 1 protein; Provisional
 419-765 2.50e-50

origin recognition complex 1 protein; Provisional


The actual alignment was detected with superfamily member PTZ00112:

Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 192.13  E-value: 2.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   419 PTRNSLGQSRTRQTPSKSPQKNPKPRTPHRA-TPQIRDRNLAVQEPASALEEARLR------------LHVSAVPDSLPC 485
Cdd:PTZ00112  680 HSKTKNDHNKSKTSKNKEPSSTSFLQDVKKKsDPHNVDFKSFIKQDQENYYVNLLRnitdptdkairmMQLDVVPKYLPC 759

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   486 REQEFQDIYSFVESKL-LDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAETDDVPPFQYVEVNGMKLTEPHQVYVQILK 564
Cdd:PTZ00112  760 REKEIKEVHGFLESGIkQSGSNQILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMNVVHPNAAYQVLYK 839

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   565 KLTGQKA-TANHAAELLAKQFcgQGSQKET---TVLLVDELDLLWTHKQDVMYNLFDWPTHKGAHLIVLTIANTMDLPER 640
Cdd:PTZ00112  840 QLFNKKPpNALNSFKILDRLF--NQNKKDNrnvSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVLIAISNTMDLPER 917

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   641 iMMNRVSSRLGLTRMSFQPYSHSQLKQILVSRLRNLRAFED-DAIQLVARKVAALSGDARRCLDICRRATEicelsHLRG 719
Cdd:PTZ00112  918 -LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRKAFE-----NKRG 991

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 23274262   720 DSlslVTVAHLMEAIDEMFSSSYITAIKNSSVVEQSFLRAIIAEFR 765
Cdd:PTZ00112  992 QK---IVPRDITEATNQLFDSPLTNAINYLPWPFKMFLTCLIVELR 1034
BAH super family cl02608
BAH, or Bromo Adjacent Homology domain (also called ELM1 and BAM for Bromo Adjacent Motif). ...
 74-169 3.86e-29

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.


The actual alignment was detected with superfamily member cd04719:

Pssm-ID: 470629  Cd Length: 128  Bit Score: 112.86  E-value: 3.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262  74 GAEVPPKKCARVQWFVRFLEIPVSKRHLLGRSPPAQEIFWYDCSDWDNKINVETIIGPVQVVALAPEEVIPVDQ-KSEET 152
Cdd:cd04719  32 GNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDNDIDAETIIGKVRVEPVEPKTDLPETKkKTGGP 111

                        90
                ....*....|....*..
gi 23274262 153 LFVKLSWNKKDFAPLPP 169
Cdd:cd04719 112 LFVKRYWDTKTFRSLDS 128
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 753-833 3.80e-19

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


:

Pssm-ID: 176573 [Multi-domain]  Cd Length: 87  Bit Score: 82.67  E-value: 3.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 753 EQSFLRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRLLLVEPSRNDL---LLRVRLNVS 829
Cdd:cd08768   4 QKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISLNVD 83


                ....
gi 23274262 830 QNDV 833
Cdd:cd08768  84 PDDV 87
 
Name Accession Description Interval E-value
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 419-765 2.50e-50

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 192.13  E-value: 2.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   419 PTRNSLGQSRTRQTPSKSPQKNPKPRTPHRA-TPQIRDRNLAVQEPASALEEARLR------------LHVSAVPDSLPC 485
Cdd:PTZ00112  680 HSKTKNDHNKSKTSKNKEPSSTSFLQDVKKKsDPHNVDFKSFIKQDQENYYVNLLRnitdptdkairmMQLDVVPKYLPC 759

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   486 REQEFQDIYSFVESKL-LDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAETDDVPPFQYVEVNGMKLTEPHQVYVQILK 564
Cdd:PTZ00112  760 REKEIKEVHGFLESGIkQSGSNQILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMNVVHPNAAYQVLYK 839

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   565 KLTGQKA-TANHAAELLAKQFcgQGSQKET---TVLLVDELDLLWTHKQDVMYNLFDWPTHKGAHLIVLTIANTMDLPER 640
Cdd:PTZ00112  840 QLFNKKPpNALNSFKILDRLF--NQNKKDNrnvSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVLIAISNTMDLPER 917

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   641 iMMNRVSSRLGLTRMSFQPYSHSQLKQILVSRLRNLRAFED-DAIQLVARKVAALSGDARRCLDICRRATEicelsHLRG 719
Cdd:PTZ00112  918 -LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRKAFE-----NKRG 991

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 23274262   720 DSlslVTVAHLMEAIDEMFSSSYITAIKNSSVVEQSFLRAIIAEFR 765
Cdd:PTZ00112  992 QK---IVPRDITEATNQLFDSPLTNAINYLPWPFKMFLTCLIVELR 1034
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
474-790 2.97e-33

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 132.66  E-value: 2.97e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 474 LHVSAVPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAETDDVpPFQYVEVNGMKLT 553
Cdd:COG1474  19 LSPDYVPDRLPHREEEIEELASALRPALRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGV-DVRVVYVNCRQAS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 554 EPHQVYVQILKKLTGQK---ATANHAAELLaKQFCGQGSQKETT-----------VLlvdeldllwTHKQDVMYNLFDWP 619
Cdd:COG1474  98 TRYRVLSRILEELGSGEdipSTGLSTDELF-DRLYEALDERDGVlvvvldeidylVD---------DEGDDLLYQLLRAN 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 620 T-HKGAHLIVLTIANTMDLPERiMMNRVSSRLGLTRMSFQPYSHSQLKQILVSRLRnlRAF-----EDDAIQLVARKVAA 693
Cdd:COG1474 168 EeLEGARVGVIGISNDLEFLEN-LDPRVKSSLGEEEIVFPPYDADELRDILEDRAE--LAFydgvlSDEVIPLIAALAAQ 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 694 LSGDARRCLDICRRATEICElshLRGDslSLVTVAHLMEAIDEMFSSSYITAIKNSSVVEQSFLRAiIAEFRRSGLEEAT 773
Cdd:COG1474 245 EHGDARKAIDLLRVAGEIAE---REGS--DRVTEEHVREAREKIERDRLLEVLRGLPTHEKLVLLA-IAELLKDGEDPVR 318

                       330
                ....*....|....*..
gi 23274262 774 FQQIYSQHVALCRMEGL 790
Cdd:COG1474 319 TGEVYEAYEELCEELGV 335
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 74-169 3.86e-29

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: 112.86  E-value: 3.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262  74 GAEVPPKKCARVQWFVRFLEIPVSKRHLLGRSPPAQEIFWYDCSDWDNKINVETIIGPVQVVALAPEEVIPVDQ-KSEET 152
Cdd:cd04719  32 GNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDNDIDAETIIGKVRVEPVEPKTDLPETKkKTGGP 111

                        90
                ....*....|....*..
gi 23274262 153 LFVKLSWNKKDFAPLPP 169
Cdd:cd04719 112 LFVKRYWDTKTFRSLDS 128
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 474-806 1.34e-19

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: 91.54  E-value: 1.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   474 LHVSAVPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAETDDVpPFQYVEVNGMKLT 553
Cdd:TIGR02928   8 LEPDYVPDRIVHRDEQIEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAEDRDV-RVVTVYVNCQILD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   554 EPHQVYVQILKKLTG-------QKATANHAAELLAKQFcgqGSQKETTVLLVDELDLLWTHKQDVMYNL---FDWPTHKG 623
Cdd:TIGR02928  87 TLYQVLVELANQLRGsgeevptTGLSTSEVFRRLYKEL---NERGDSLIIVLDEIDYLVGDDDDLLYQLsraRSNGDLDN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   624 AHLIVLTIANTMDLPERIMMnRVSSRLGLTRMSFQPYSHSQLKQILVSRLRnlRAF-----EDDAIQLVARKVAALSGDA 698
Cdd:TIGR02928 164 AKVGVIGISNDLKFRENLDP-RVKSSLCEEEIIFPPYDAEELRDILENRAE--KAFydgvlDDGVIPLCAALAAQEHGDA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   699 RRCLDICRRATEICElshLRGDslSLVTVAHLMEAIDEMFSSSYITAIKNSSVVEQSFLRAIIAEFRRSGlEEATFQQIY 778
Cdd:TIGR02928 241 RKAIDLLRVAGEIAE---REGA--ERVTEDHVEKAQEKIEKDRLLELIRGLPTHSKLVLLAIANLAANDE-DPFRTGEVY 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 23274262   779 SQHVALCR---MEGLPYPTMSETMAVCSRLG 806
Cdd:TIGR02928 315 EVYKEVCEdigVDPLTQRRISDLLNELDMLG 345
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 753-833 3.80e-19

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


Pssm-ID: 176573 [Multi-domain]  Cd Length: 87  Bit Score: 82.67  E-value: 3.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 753 EQSFLRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRLLLVEPSRNDL---LLRVRLNVS 829
Cdd:cd08768   4 QKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISLNVD 83


                ....
gi 23274262 830 QNDV 833
Cdd:cd08768  84 PDDV 87
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 757-836 4.17e-19

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


Pssm-ID: 462672  Cd Length: 84  Bit Score: 82.25  E-value: 4.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   757 LRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRLLLVEPS----RNDLLLRVRLNVSQND 832
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 23274262   833 VLFA 836
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 ...
 757-837 1.04e-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: 75.75  E-value: 1.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262    757 LRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRLLLVEPS---RNDLLLRVRLNVSQNDV 833
Cdd:smart01074   1 LLAIVLLLTRGGKEEVTTGEVYEVYKELCKELGVDPLTYTRIYDLLNELEMLGIIELRVSnrgRRGRTREISLNVDPDDV 80


                   ....
gi 23274262    834 LFAL 837
Cdd:smart01074  81 LEAL 84
BAH smart00439
Bromo adjacent homology domain;
63-169 1.25e-12

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 65.39  E-value: 1.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262     63 CRIE----NSSNKctgaevpPKKCARVQWFVRFLEIPVSKRHLLGRsppaQEIFWYDCSDwdnKINVETIIGPVQVVALA 138
Cdd:smart00439  22 GRIEeifeTKKNS-------ESKMVRVRWFYRPEETVLEKAALFDK----NEVFLSDEYD---TVPLSDIIGKCNVLYKS 87

                           90       100       110
                   ....*....|....*....|....*....|...
gi 23274262    139 PEEVIPVDQKS--EETLFVKLSWNKKDFAPLPP 169
Cdd:smart00439  88 DYPGLRPEGSIgePDVFFCESAYDPEKGSFKKL 120
AAA_lid_10 pfam17872
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 653-713 6.41e-10

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: 56.75  E-value: 6.41e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23274262   653 TRMSFQPYSHSQLKQILVSRLRNLR-AFEDDAIQLVARKVAALSGDARRCLDICRRATEICE 713
Cdd:pfam17872  18 TGMAILNDSCEEQEQKLPAGVKKVRlTMSDDAIEIASRKVASVSGDARRALKICKRAAEIAE 79
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 79-168 6.06e-08

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: 51.92  E-value: 6.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262    79 PKKCARVQWFVRFLEIPvsKRHLLGRSPpaQEIFWydcSDWDNKINVETIIGPVQVVALAPEEVIPVDQKSEE-TLFVKL 157
Cdd:pfam01426  35 GKKMVRVQWFYRPEETV--HRAGKAFNK--DELFL---SDEEDDVPLSAIIGKCSVLHKSDLESLDPYKIKEPdDFFCEL 107

                          90
                  ....*....|...
gi 23274262   158 SWNKKD--FAPLP 168
Cdd:pfam01426 108 LYDPKTksFKKLP 120
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 489-579 6.19e-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: 38.28  E-value: 6.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 489 EFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQqaaetddVPPFQYVEVNGMKLTEPHQVYVQILKKLTG 568
Cdd:cd00009   2 GQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF-------RPGAPFLYLNASDLLEGLVVAELFGHFLVR 74

                        90
                ....*....|.
gi 23274262 569 QKATANHAAEL 579
Cdd:cd00009  75 LLFELAEKAKP 85
 
Name Accession Description Interval E-value
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 419-765 2.50e-50

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 192.13  E-value: 2.50e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   419 PTRNSLGQSRTRQTPSKSPQKNPKPRTPHRA-TPQIRDRNLAVQEPASALEEARLR------------LHVSAVPDSLPC 485
Cdd:PTZ00112  680 HSKTKNDHNKSKTSKNKEPSSTSFLQDVKKKsDPHNVDFKSFIKQDQENYYVNLLRnitdptdkairmMQLDVVPKYLPC 759

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   486 REQEFQDIYSFVESKL-LDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAETDDVPPFQYVEVNGMKLTEPHQVYVQILK 564
Cdd:PTZ00112  760 REKEIKEVHGFLESGIkQSGSNQILYISGMPGTGKTATVYSVIQLLQHKTKQKLLPSFNVFEINGMNVVHPNAAYQVLYK 839

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   565 KLTGQKA-TANHAAELLAKQFcgQGSQKET---TVLLVDELDLLWTHKQDVMYNLFDWPTHKGAHLIVLTIANTMDLPER 640
Cdd:PTZ00112  840 QLFNKKPpNALNSFKILDRLF--NQNKKDNrnvSILIIDEIDYLITKTQKVLFTLFDWPTKINSKLVLIAISNTMDLPER 917

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   641 iMMNRVSSRLGLTRMSFQPYSHSQLKQILVSRLRNLRAFED-DAIQLVARKVAALSGDARRCLDICRRATEicelsHLRG 719
Cdd:PTZ00112  918 -LIPRCRSRLAFGRLVFSPYKGDEIEKIIKERLENCKEIIDhTAIQLCARKVANVSGDIRKALQICRKAFE-----NKRG 991

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 23274262   720 DSlslVTVAHLMEAIDEMFSSSYITAIKNSSVVEQSFLRAIIAEFR 765
Cdd:PTZ00112  992 QK---IVPRDITEATNQLFDSPLTNAINYLPWPFKMFLTCLIVELR 1034
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
474-790 2.97e-33

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 132.66  E-value: 2.97e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 474 LHVSAVPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAETDDVpPFQYVEVNGMKLT 553
Cdd:COG1474  19 LSPDYVPDRLPHREEEIEELASALRPALRGERPSNVLIYGPTGTGKTAVAKYVLEELEEEAEERGV-DVRVVYVNCRQAS 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 554 EPHQVYVQILKKLTGQK---ATANHAAELLaKQFCGQGSQKETT-----------VLlvdeldllwTHKQDVMYNLFDWP 619
Cdd:COG1474  98 TRYRVLSRILEELGSGEdipSTGLSTDELF-DRLYEALDERDGVlvvvldeidylVD---------DEGDDLLYQLLRAN 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 620 T-HKGAHLIVLTIANTMDLPERiMMNRVSSRLGLTRMSFQPYSHSQLKQILVSRLRnlRAF-----EDDAIQLVARKVAA 693
Cdd:COG1474 168 EeLEGARVGVIGISNDLEFLEN-LDPRVKSSLGEEEIVFPPYDADELRDILEDRAE--LAFydgvlSDEVIPLIAALAAQ 244

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 694 LSGDARRCLDICRRATEICElshLRGDslSLVTVAHLMEAIDEMFSSSYITAIKNSSVVEQSFLRAiIAEFRRSGLEEAT 773
Cdd:COG1474 245 EHGDARKAIDLLRVAGEIAE---REGS--DRVTEEHVREAREKIERDRLLEVLRGLPTHEKLVLLA-IAELLKDGEDPVR 318

                       330
                ....*....|....*..
gi 23274262 774 FQQIYSQHVALCRMEGL 790
Cdd:COG1474 319 TGEVYEAYEELCEELGV 335
BAH_Orc1p_animal cd04719
BAH, or Bromo Adjacent Homology domain, as present in animal homologs of Saccharomyces ...
 74-169 3.86e-29

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: 112.86  E-value: 3.86e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262  74 GAEVPPKKCARVQWFVRFLEIPVSKRHLLGRSPPAQEIFWYDCSDWDNKINVETIIGPVQVVALAPEEVIPVDQ-KSEET 152
Cdd:cd04719  32 GNEDDDPKRAIVQWFSRPSEVPKNKRKLLGREPHSQEVFFYSRSSCDNDIDAETIIGKVRVEPVEPKTDLPETKkKTGGP 111

                        90
                ....*....|....*..
gi 23274262 153 LFVKLSWNKKDFAPLPP 169
Cdd:cd04719 112 LFVKRYWDTKTFRSLDS 128
cdc6 PRK00411
ORC1-type DNA replication protein;
479-790 4.57e-22

ORC1-type DNA replication protein;


Pssm-ID: 234751 [Multi-domain]  Cd Length: 394  Bit Score: 99.54  E-value: 4.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262  479 VPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAEtddvpPFQYVEVNGMKLTEPHQV 558
Cdd:PRK00411  28 VPENLPHREEQIEELAFALRPALRGSRPLNVLIYGPPGTGKTTTVKKVFEELEEIAV-----KVVYVYINCQIDRTRYAI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262  559 YVQILKKLTGQ-------------KATANHAAE-----LLA-----KQFCGQGSqkettvllvdeldllwthkqDVMYNL 615
Cdd:PRK00411 103 FSEIARQLFGHpppssglsfdelfDKIAEYLDErdrvlIVAlddinYLFEKEGN--------------------DVLYSL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262  616 FDWPT-HKGAHLIVLTIANTMDLPERIMMnRVSSRLGLTRMSFQPYSHSQLKQILVSRLRnlRAF-----EDDAIQLVAR 689
Cdd:PRK00411 163 LRAHEeYPGARIGVIGISSDLTFLYILDP-RVKSVFRPEEIYFPPYTADEIFDILKDRVE--EGFypgvvDDEVLDLIAD 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262  690 KVAALSGDARRCLDICRRATEICElshLRGDslSLVTVAHLMEAIDEMFSSSYITAIKNSSVVEQSFLRAIIaEFRRSGL 769
Cdd:PRK00411 240 LTAREHGDARVAIDLLRRAGLIAE---REGS--RKVTEEDVRKAYEKSEIVHLSEVLRTLPLHEKLLLRAIV-RLLKKGG 313

                        330       340
                 ....*....|....*....|.
gi 23274262  770 EEATFQQIYSQHVALCRMEGL 790
Cdd:PRK00411 314 DEVTTGEVYEEYKELCEELGY 334
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
 474-806 1.34e-19

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: 91.54  E-value: 1.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   474 LHVSAVPDSLPCREQEFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQQAAETDDVpPFQYVEVNGMKLT 553
Cdd:TIGR02928   8 LEPDYVPDRIVHRDEQIEELAKALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKELEEAAEDRDV-RVVTVYVNCQILD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   554 EPHQVYVQILKKLTG-------QKATANHAAELLAKQFcgqGSQKETTVLLVDELDLLWTHKQDVMYNL---FDWPTHKG 623
Cdd:TIGR02928  87 TLYQVLVELANQLRGsgeevptTGLSTSEVFRRLYKEL---NERGDSLIIVLDEIDYLVGDDDDLLYQLsraRSNGDLDN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   624 AHLIVLTIANTMDLPERIMMnRVSSRLGLTRMSFQPYSHSQLKQILVSRLRnlRAF-----EDDAIQLVARKVAALSGDA 698
Cdd:TIGR02928 164 AKVGVIGISNDLKFRENLDP-RVKSSLCEEEIIFPPYDAEELRDILENRAE--KAFydgvlDDGVIPLCAALAAQEHGDA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   699 RRCLDICRRATEICElshLRGDslSLVTVAHLMEAIDEMFSSSYITAIKNSSVVEQSFLRAIIAEFRRSGlEEATFQQIY 778
Cdd:TIGR02928 241 RKAIDLLRVAGEIAE---REGA--ERVTEDHVEKAQEKIEKDRLLELIRGLPTHSKLVLLAIANLAANDE-DPFRTGEVY 314

                         330       340       350
                  ....*....|....*....|....*....|.
gi 23274262   779 SQHVALCR---MEGLPYPTMSETMAVCSRLG 806
Cdd:TIGR02928 315 EVYKEVCEdigVDPLTQRRISDLLNELDMLG 345
Cdc6_C cd08768
Winged-helix domain of essential DNA replication protein Cell division control protein (Cdc6), ...
 753-833 3.80e-19

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


Pssm-ID: 176573 [Multi-domain]  Cd Length: 87  Bit Score: 82.67  E-value: 3.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 753 EQSFLRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRLLLVEPSRNDL---LLRVRLNVS 829
Cdd:cd08768   4 QKLVLLALLLLFKRGGEEEATTGEVYEVYEELCEEIGVDPLTQRRISDLLSELEMLGLLETEVSSKGRrgrTRKISLNVD 83


                ....
gi 23274262 830 QNDV 833
Cdd:cd08768  84 PDDV 87
Cdc6_C pfam09079
CDC6, C terminal winged helix domain; The C terminal domain of CDC6 assumes a winged helix ...
 757-836 4.17e-19

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


Pssm-ID: 462672  Cd Length: 84  Bit Score: 82.25  E-value: 4.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   757 LRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRLLLVEPS----RNDLLLRVRLNVSQND 832
Cdd:pfam09079   1 LCALLLLLRRSGKEEVTTGEVYEVYKKLCEKLGVDPLTQRRVSDLLSELEMLGILEAEVSsrgrRGGRTRKIRLNVDPDD 80


                  ....
gi 23274262   833 VLFA 836
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 ...
 757-837 1.04e-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: 75.75  E-value: 1.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262    757 LRAIIAEFRRSGLEEATFQQIYSQHVALCRMEGLPYPTMSETMAVCSRLGSCRLLLVEPS---RNDLLLRVRLNVSQNDV 833
Cdd:smart01074   1 LLAIVLLLTRGGKEEVTTGEVYEVYKELCKELGVDPLTYTRIYDLLNELEMLGIIELRVSnrgRRGRTREISLNVDPDDV 80


                   ....
gi 23274262    834 LFAL 837
Cdd:smart01074  81 LEAL 84
BAH smart00439
Bromo adjacent homology domain;
63-169 1.25e-12

Bromo adjacent homology domain;


Pssm-ID: 214664 [Multi-domain]  Cd Length: 121  Bit Score: 65.39  E-value: 1.25e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262     63 CRIE----NSSNKctgaevpPKKCARVQWFVRFLEIPVSKRHLLGRsppaQEIFWYDCSDwdnKINVETIIGPVQVVALA 138
Cdd:smart00439  22 GRIEeifeTKKNS-------ESKMVRVRWFYRPEETVLEKAALFDK----NEVFLSDEYD---TVPLSDIIGKCNVLYKS 87

                           90       100       110
                   ....*....|....*....|....*....|...
gi 23274262    139 PEEVIPVDQKS--EETLFVKLSWNKKDFAPLPP 169
Cdd:smart00439  88 DYPGLRPEGSIgePDVFFCESAYDPEKGSFKKL 120
AAA_lid_10 pfam17872
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 653-713 6.41e-10

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: 56.75  E-value: 6.41e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23274262   653 TRMSFQPYSHSQLKQILVSRLRNLR-AFEDDAIQLVARKVAALSGDARRCLDICRRATEICE 713
Cdd:pfam17872  18 TGMAILNDSCEEQEQKLPAGVKKVRlTMSDDAIEIASRKVASVSGDARRALKICKRAAEIAE 79
BAH pfam01426
BAH domain; This domain has been called BAH (Bromo adjacent homology) domain and has also been ...
 79-168 6.06e-08

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: 51.92  E-value: 6.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262    79 PKKCARVQWFVRFLEIPvsKRHLLGRSPpaQEIFWydcSDWDNKINVETIIGPVQVVALAPEEVIPVDQKSEE-TLFVKL 157
Cdd:pfam01426  35 GKKMVRVQWFYRPEETV--HRAGKAFNK--DELFL---SDEEDDVPLSAIIGKCSVLHKSDLESLDPYKIKEPdDFFCEL 107

                          90
                  ....*....|...
gi 23274262   158 SWNKKD--FAPLP 168
Cdd:pfam01426 108 LYDPKTksFKKLP 120
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 509-654 1.14e-07

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: 51.44  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   509 MYISGVPGTGKTATVHEVirclqqAAETDdvppFQYVEVNGMKLTEPH--QVYVQILKKLTGQKATAN--------HAae 578
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAV------AKELG----APFIEISGSELVSKYvgESEKRLRELFEAAKKLAPcvifideiDA-- 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23274262   579 LLAKQFCGQGSQKETTvllvdeldllwthkQDVMYNLFDWPTHKGAHLIVLTIANTMDLPERIMMNRVSSRLGLTR 654
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 ...
 483-539 1.20e-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: 46.34  E-value: 1.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 23274262   483 LPCREQEFQDIYSFVEsKLLDGTGGCMYISGVPGTGKTAtvheVIRCLQQAAETDDV 539
Cdd:pfam13191   2 LVGREEELEQLLDALD-RVRSGRPPSVLLTGEAGTGKTT----LLRELLRALERDGG 53
AAA_22 pfam13401
AAA domain;
502-581 3.14e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.56  E-value: 3.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262   502 LDGTGGCMYISGVPGTGKTatvheviRCLQQAAETDDVPPFQYVEVNGMKLTEPHQVYVQILKKLTGQKATANHAAELLA 581
Cdd:pfam13401   1 IRFGAGILVLTGESGTGKT-------TLLRRLLEQLPEVRDSVVFVDLPSGTSPKDLLRALLRALGLPLSGRLSKEELLA 73
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 489-579 6.19e-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: 38.28  E-value: 6.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262 489 EFQDIYSFVESKLLDGTGGCMYISGVPGTGKTATVHEVIRCLQqaaetddVPPFQYVEVNGMKLTEPHQVYVQILKKLTG 568
Cdd:cd00009   2 GQEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELF-------RPGAPFLYLNASDLLEGLVVAELFGHFLVR 74

                        90
                ....*....|.
gi 23274262 569 QKATANHAAEL 579
Cdd:cd00009  75 LLFELAEKAKP 85
COG3899 COG3899
Predicted ATPase [General function prediction only];
448-528 9.37e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443106 [Multi-domain]  Cd Length: 1244  Bit Score: 39.84  E-value: 9.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23274262  448 RATPQIRDRNLAVQEPASALEEARLRLHVSAVPDSLPCREQEFQDIYSFVESkLLDGTGGCMYISGVPGTGKTATVHEVI 527
Cdd:COG3899  254 RLLGLAGAAALLLLGLLAAAAAGRRLLARRLIPQPLVGREAELAALLAALER-ARAGRGELVLVSGEAGIGKSRLVRELA 332


                 .
gi 23274262  528 R 528
Cdd:COG3899  333 R 333
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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