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Conserved domains on  [gi|2004839052|ref|XP_039873026|]
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ATPase family AAA domain-containing protein 2B isoform X2 [Simochromis diagramma]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
349-518 1.31e-113

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


:

Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 354.12  E-value: 1.31e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSHGDRKVSFFMRKGADCLSKWV 428
Cdd:cd19517      1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMRKGADCLSKWV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  429 GESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRR 508
Cdd:cd19517     81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160
                          170
                   ....*....|
gi 2004839052  509 PGRFDREFLF 518
Cdd:cd19517    161 PGRFDREFYF 170
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
914-1025 8.01e-63

Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver


:

Pssm-ID: 99957  Cd Length: 112  Bit Score: 209.14  E-value: 8.01e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  914 LRELRLFLRDVTKRLATDKRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:cd05528      1 LRELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNP 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2004839052  994 DKDPGDKVIRHRACSLKDTAHAIFAAELDPEF 1025
Cdd:cd05528     81 DRDPADKLIRSRACELRDEVHAMIEAELDPLF 112
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
546-580 4.99e-11

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


:

Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 58.70  E-value: 4.99e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2004839052  546 LDELAEKCVGYCGADIKALCTEAALMALRRRYPQI 580
Cdd:pfam17862    4 LEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
AAA super family cl47477
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
724-842 3.43e-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.


The actual alignment was detected with superfamily member pfam00004:

Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 53.37  E-value: 3.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  724 LLLAGAPGSGQSShLAPALLHHLdKLPVHRLDLPTLYSVSAKTPEESCAQVFREARRSVPSVVYMPHI-------SEWWD 796
Cdd:pfam00004    1 LLLYGPPGTGKTT-LAKAVAKEL-GAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIdalagsrGSGGD 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2004839052  797 TVSDTVKSTFLTLLQDV-PSFSPVLVLATAeTHYSKLSDEVRSIFQR 842
Cdd:pfam00004   79 SESRRVVNQLLTELDGFtSSNSKVIVIAAT-NRPDKLDPALLGRFDR 124
LGT super family cl00478
Prolipoprotein diacylglyceryl transferase;
1134-1224 1.43e-03

Prolipoprotein diacylglyceryl transferase;


The actual alignment was detected with superfamily member PRK13108:

Pssm-ID: 469786 [Multi-domain]  Cd Length: 460  Bit Score: 43.04  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052 1134 DEESSCDITGPQPN---GHHPHAPSTEEESSNEPPVAAPDKPPDASEAREAPMPKVEEPAAKEAEP-EITGKHTEPHCLG 1209
Cdd:PRK13108   364 EETSEADIEREQPGdlaGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPdELAVAGPGDDPAE 443
                           90
                   ....*....|....*
gi 2004839052 1210 GSSQPNTDGDSEASR 1224
Cdd:PRK13108   444 PDGIRRQDDFSSRRR 458
 
Name Accession Description Interval E-value
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
349-518 1.31e-113

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 354.12  E-value: 1.31e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSHGDRKVSFFMRKGADCLSKWV 428
Cdd:cd19517      1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMRKGADCLSKWV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  429 GESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRR 508
Cdd:cd19517     81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160
                          170
                   ....*....|
gi 2004839052  509 PGRFDREFLF 518
Cdd:cd19517    161 PGRFDREFYF 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
292-615 1.09e-92

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 302.70  E-value: 1.09e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  292 RFERRKSKSMTRARNRCLPMNLTAEDLASGVLRDRVKVGASLADVDPMNLD--PSVRFDNVGGLSNHIQSLKEMVVFPLL 369
Cdd:COG1222     20 ALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAesPDVTFDDIGGLDEQIEEIREAVELPLK 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  370 YPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPSI 449
Cdd:COG1222    100 NPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGEL-----GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSI 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  450 IFFDEIDGLAPVRSSKQD-QIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKKARKH 528
Cdd:COG1222    175 IFIDEIDAIAARRTDDGTsGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREE 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  529 ILEIHTRDwNPKLSEPFLDELAEKCVGYCGADIKALCTEAALMALRRRYPQIygssvklkldvasivlGPGDFSKAMRTI 608
Cdd:COG1222    255 ILKIHLRD-MPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTV----------------TMEDLEKAIEKV 317

                   ....*..
gi 2004839052  609 VPASQRA 615
Cdd:COG1222    318 KKKTETA 324
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
343-614 1.71e-74

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 264.08  E-value: 1.71e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  343 PSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGAD 422
Cdd:TIGR01243  173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAG-----AYFISINGPE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  423 CLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSI 502
Cdd:TIGR01243  248 IMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDAL 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  503 DPALRRPGRFDREFLFSLPDKKARKHILEIHTRDwNPKLSEPFLDELAEKCVGYCGADIKALCTEAALMALRRRYPQiyg 582
Cdd:TIGR01243  328 DPALRRPGRFDREIVIRVPDKRARKEILKVHTRN-MPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIRE--- 403
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2004839052  583 ssVKLKLDVASI---VLGP-----GDFSKAMRTIVPASQR 614
Cdd:TIGR01243  404 --GKINFEAEEIpaeVLKElkvtmKDFMEALKMVEPSAIR 441
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
318-580 8.83e-71

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 242.82  E-value: 8.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  318 LASGVLRDRVKVGASLA---------DV-----DP----MNLD--PSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFEKF 377
Cdd:PRK03992    81 VSPFIDREKLKPGARVAlnqqslaivEVlpsekDPrvqaMEVIesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  378 KIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDG 457
Cdd:PRK03992   161 GIEPPKGVLLYGPPGTGKTLLAKAVAHET-----NATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  458 LAPVR----SSKQDQIHSSIVStLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKKARKHILEIH 533
Cdd:PRK03992   236 IAAKRtdsgTSGDREVQRTLMQ-LLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIH 314
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2004839052  534 TRDWNpkLSEPF-LDELAEKCVGYCGADIKALCTEAALMALRRRYPQI 580
Cdd:PRK03992   315 TRKMN--LADDVdLEELAELTEGASGADLKAICTEAGMFAIRDDRTEV 360
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
914-1025 8.01e-63

Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver


Pssm-ID: 99957  Cd Length: 112  Bit Score: 209.14  E-value: 8.01e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  914 LRELRLFLRDVTKRLATDKRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:cd05528      1 LRELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNP 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2004839052  994 DKDPGDKVIRHRACSLKDTAHAIFAAELDPEF 1025
Cdd:cd05528     81 DRDPADKLIRSRACELRDEVHAMIEAELDPLF 112
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
386-520 2.16e-48

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: 168.54  E-value: 2.16e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  386 LFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSK 465
Cdd:pfam00004    2 LLYGPPGTGKTTLAKAVAKEL-----GAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2004839052  466 QDQIHSSIVSTLLALMDGLDSR-GEIVVIGATNRLDSIDPALRrpGRFDREFLFSL 520
Cdd:pfam00004   77 GDSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
381-522 1.76e-19

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 86.66  E-value: 1.76e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052   381 PPRGCLFYGPPGTGKTLVARALANE------------CSHGDRKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPS 448
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARElgppgggviyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004839052   449 IIFFDEIDGLAPVRSSKQDQihssiVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPgRFDREFLFSLPD 522
Cdd:smart00382   81 VLILDEITSLLDAEQEALLL-----LLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
BROMO smart00297
bromo domain;
914-1012 1.44e-18

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 82.33  E-value: 1.44e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052   914 LRELRLFLRDVTKRLATDKRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:smart00297    5 QKKLQELLKAVLDKLDSHPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNG 84
                            90
                    ....*....|....*....
gi 2004839052   994 DkdpgDKVIRHRACSLKDT 1012
Cdd:smart00297   85 P----DSEVYKDAKKLEKF 99
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
936-993 4.07e-15

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 71.96  E-value: 4.07e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2004839052  936 IFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:pfam00439   16 PFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
546-580 4.99e-11

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 58.70  E-value: 4.99e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2004839052  546 LDELAEKCVGYCGADIKALCTEAALMALRRRYPQI 580
Cdd:pfam17862    4 LEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
724-842 3.43e-08

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 53.37  E-value: 3.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  724 LLLAGAPGSGQSShLAPALLHHLdKLPVHRLDLPTLYSVSAKTPEESCAQVFREARRSVPSVVYMPHI-------SEWWD 796
Cdd:pfam00004    1 LLLYGPPGTGKTT-LAKAVAKEL-GAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIdalagsrGSGGD 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2004839052  797 TVSDTVKSTFLTLLQDV-PSFSPVLVLATAeTHYSKLSDEVRSIFQR 842
Cdd:pfam00004   79 SESRRVVNQLLTELDGFtSSNSKVIVIAAT-NRPDKLDPALLGRFDR 124
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
709-825 1.09e-07

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 52.76  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  709 FSSSALQQPTAYRPRLLLAGAPGSGQSShLAPALLHHLdKLPVHRLDLPTLYSVSAKTPEESCAQVFREARRSVPSVVYM 788
Cdd:cd19507     19 FSKQASAYGLPTPKGLLLVGIQGTGKSL-TAKAIAGVW-QLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWI 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2004839052  789 PHISEWWDT--------VSDTVKSTFLTLLQDvpSFSPVLVLATA 825
Cdd:cd19507     97 DEIEKGFSNadskgdsgTSSRVLGTFLTWLQE--KKKPVFVVATA 139
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
899-1056 1.33e-07

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 55.58  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  899 SAEEQRRLAEQEENTLRELR-LFLRDVTKRlatdkrFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDF 977
Cdd:COG5076    136 PKIEDELLYADNKAIAKFKKqLFLRDGRFL------SSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEF 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  978 LVDIDLICSNALEYNpdkDPGDKVIRHRacslkDTAHAIFAAELDPEFDRMCEE-IKEARRKRDLLTPAQLSAVPGAGAT 1056
Cdd:COG5076    210 VSDLNLMFDNCKLYN---GPDSSVYVDA-----KELEKYFLKLIEEIPEEMLELsIKPGREEREERESVLITNSQAHVGA 281
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
723-866 5.88e-07

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 53.76  E-value: 5.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  723 RLLLAGAPGSGQSsHLAPALLHHLDkLPVHRLDLPTLYS----VSAKtpeeSCAQVFREARRSVPSVVYM-------PHI 791
Cdd:COG0464    193 GLLLYGPPGTGKT-LLARALAGELG-LPLIEVDLSDLVSkyvgETEK----NLREVFDKARGLAPCVLFIdeadalaGKR 266
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004839052  792 SEWWDTVSDTVKSTFLTLLQDVPsfSPVLVLATAeTHYSKLSDEVRSIFQrtygEVVALSPPGEEEIRHFFSDLL 866
Cdd:COG0464    267 GEVGDGVGRRVVNTLLTEMEELR--SDVVVIAAT-NRPDLLDPALLRRFD----EIIFFPLPDAEERLEIFRIHL 334
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
385-461 8.12e-04

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 42.46  E-value: 8.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  385 CLFYGPPGTGKTLVARALANE-CSHGdRKVSFFmrKGADCLSKWvGESERQLRL--LFDQayLMRPSIIFFDEIdGLAPV 461
Cdd:NF038214    93 VLLLGPPGTGKTHLAIALGYAaCRQG-YRVRFT--TAADLVEQL-AQARADGRLgrLLRR--LARYDLLIIDEL-GYLPF 165
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
1134-1224 1.43e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.04  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052 1134 DEESSCDITGPQPN---GHHPHAPSTEEESSNEPPVAAPDKPPDASEAREAPMPKVEEPAAKEAEP-EITGKHTEPHCLG 1209
Cdd:PRK13108   364 EETSEADIEREQPGdlaGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPdELAVAGPGDDPAE 443
                           90
                   ....*....|....*
gi 2004839052 1210 GSSQPNTDGDSEASR 1224
Cdd:PRK13108   444 PDGIRRQDDFSSRRR 458
 
Name Accession Description Interval E-value
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
349-518 1.31e-113

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 354.12  E-value: 1.31e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSHGDRKVSFFMRKGADCLSKWV 428
Cdd:cd19517      1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMRKGADCLSKWV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  429 GESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRR 508
Cdd:cd19517     81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160
                          170
                   ....*....|
gi 2004839052  509 PGRFDREFLF 518
Cdd:cd19517    161 PGRFDREFYF 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
292-615 1.09e-92

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 302.70  E-value: 1.09e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  292 RFERRKSKSMTRARNRCLPMNLTAEDLASGVLRDRVKVGASLADVDPMNLD--PSVRFDNVGGLSNHIQSLKEMVVFPLL 369
Cdd:COG1222     20 ALQERLGVELALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPAesPDVTFDDIGGLDEQIEEIREAVELPLK 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  370 YPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPSI 449
Cdd:COG1222    100 NPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGEL-----GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSI 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  450 IFFDEIDGLAPVRSSKQD-QIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKKARKH 528
Cdd:COG1222    175 IFIDEIDAIAARRTDDGTsGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREE 254
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  529 ILEIHTRDwNPKLSEPFLDELAEKCVGYCGADIKALCTEAALMALRRRYPQIygssvklkldvasivlGPGDFSKAMRTI 608
Cdd:COG1222    255 ILKIHLRD-MPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTV----------------TMEDLEKAIEKV 317

                   ....*..
gi 2004839052  609 VPASQRA 615
Cdd:COG1222    318 KKKTETA 324
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
350-518 8.64e-79

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 256.83  E-value: 8.64e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  350 VGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVG 429
Cdd:cd19503      2 IGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEA-----GANFLSISGPSIVSKYLG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  430 ESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRP 509
Cdd:cd19503     77 ESEKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156

                   ....*....
gi 2004839052  510 GRFDREFLF 518
Cdd:cd19503    157 GRFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
343-614 1.71e-74

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 264.08  E-value: 1.71e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  343 PSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGAD 422
Cdd:TIGR01243  173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAG-----AYFISINGPE 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  423 CLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSI 502
Cdd:TIGR01243  248 IMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDAL 327
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  503 DPALRRPGRFDREFLFSLPDKKARKHILEIHTRDwNPKLSEPFLDELAEKCVGYCGADIKALCTEAALMALRRRYPQiyg 582
Cdd:TIGR01243  328 DPALRRPGRFDREIVIRVPDKRARKEILKVHTRN-MPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIRE--- 403
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2004839052  583 ssVKLKLDVASI---VLGP-----GDFSKAMRTIVPASQR 614
Cdd:TIGR01243  404 --GKINFEAEEIpaeVLKElkvtmKDFMEALKMVEPSAIR 441
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
303-611 1.32e-73

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 261.38  E-value: 1.32e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  303 RARNRCLP---MNLTAEDLASGVLrDRVKVGA-----SLADVDPMNLD------PSVRFDNVGGLSNHIQSLKEMVVFPL 368
Cdd:TIGR01243  395 AALRRFIRegkINFEAEEIPAEVL-KELKVTMkdfmeALKMVEPSAIRevlvevPNVRWSDIGGLEEVKQELREAVEWPL 473
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  369 LYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPS 448
Cdd:TIGR01243  474 KHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESG-----ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPA 548
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  449 IIFFDEIDGLAPVRSSKQDQ-IHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKKARK 527
Cdd:TIGR01243  549 IIFFDEIDAIAPARGARFDTsVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARK 628
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  528 HILEIHTRDWNpkLSEPF-LDELAEKCVGYCGADIKALCTEAALMALRRrypqIYGSSVKLKLDVAS------IVLGPGD 600
Cdd:TIGR01243  629 EIFKIHTRSMP--LAEDVdLEELAEMTEGYTGADIEAVCREAAMAALRE----SIGSPAKEKLEVGEeeflkdLKVEMRH 702
                          330
                   ....*....|.
gi 2004839052  601 FSKAMRTIVPA 611
Cdd:TIGR01243  703 FLEALKKVKPS 713
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
346-580 1.32e-73

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 251.37  E-value: 1.32e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  346 RFDNVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLS 425
Cdd:COG0464    155 ILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGEL-----GLPLIEVDLSDLVS 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  426 KWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLdsRGEIVVIGATNRLDSIDPA 505
Cdd:COG0464    230 KYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPA 307
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004839052  506 LRRpgRFDREFLFSLPDKKARKHILEIHTRDWnpKLSEPF-LDELAEKCVGYCGADIKALCTEAALMALRRRYPQI 580
Cdd:COG0464    308 LLR--RFDEIIFFPLPDAEERLEIFRIHLRKR--PLDEDVdLEELAEATEGLSGADIRNVVRRAALQALRLGREPV 379
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
318-580 8.83e-71

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 242.82  E-value: 8.83e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  318 LASGVLRDRVKVGASLA---------DV-----DP----MNLD--PSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFEKF 377
Cdd:PRK03992    81 VSPFIDREKLKPGARVAlnqqslaivEVlpsekDPrvqaMEVIesPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEV 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  378 KIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDG 457
Cdd:PRK03992   161 GIEPPKGVLLYGPPGTGKTLLAKAVAHET-----NATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA 235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  458 LAPVR----SSKQDQIHSSIVStLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKKARKHILEIH 533
Cdd:PRK03992   236 IAAKRtdsgTSGDREVQRTLMQ-LLAEMDGFDPRGNVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIH 314
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 2004839052  534 TRDWNpkLSEPF-LDELAEKCVGYCGADIKALCTEAALMALRRRYPQI 580
Cdd:PRK03992   315 TRKMN--LADDVdLEELAELTEGASGADLKAICTEAGMFAIRDDRTEV 360
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
317-576 3.55e-64

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 222.75  E-value: 3.55e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  317 DLASGVLRDRVKVGASLA---------DVDPMNLD-----------PSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFEK 376
Cdd:TIGR01242   71 NVSAFIDRKSLKPGARVAlnqqtltivDVLPTSKDplvkgmeveerPNVSYEDIGGLEEQIREIREAVELPLKHPELFEE 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  377 FKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEID 456
Cdd:TIGR01242  151 VGIEPPKGVLLYGPPGTGKTLLAKAVAHET-----NATFIRVVGSELVRKYIGEGARLVREIFELAKEKAPSIIFIDEID 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  457 GLAPVR---SSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKKARKHILEIH 533
Cdd:TIGR01242  226 AIAAKRtdsGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPALLRPGRFDRIIEVPLPDFEGRLEILKIH 305
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 2004839052  534 TRdwNPKLSEPF-LDELAEKCVGYCGADIKALCTEAALMALRRR 576
Cdd:TIGR01242  306 TR--KMKLAEDVdLEAIAKMTEGASGADLKAICTEAGMFAIREE 347
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
914-1025 8.01e-63

Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine. The structure(2DKW) in this alignment is an uncharacterized protein predicted from analysis of cDNA clones from human fetal liver


Pssm-ID: 99957  Cd Length: 112  Bit Score: 209.14  E-value: 8.01e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  914 LRELRLFLRDVTKRLATDKRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:cd05528      1 LRELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNP 80
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2004839052  994 DKDPGDKVIRHRACSLKDTAHAIFAAELDPEF 1025
Cdd:cd05528     81 DRDPADKLIRSRACELRDEVHAMIEAELDPLF 112
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
349-515 1.59e-62

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 210.37  E-value: 1.59e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGADCLSKWV 428
Cdd:cd19519      1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETG-----AFFFLINGPEIMSKLA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  429 GESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRR 508
Cdd:cd19519     76 GESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRR 155

                   ....*..
gi 2004839052  509 PGRFDRE 515
Cdd:cd19519    156 FGRFDRE 162
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
358-514 1.37e-61

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 207.52  E-value: 1.37e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  358 QSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRL 437
Cdd:cd19511      3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEA-----GLNFISVKGPELFSKYVGESERAVRE 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004839052  438 LFDQAYLMRPSIIFFDEIDGLAPVRS-SKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 514
Cdd:cd19511     78 IFQKARQAAPCIIFFDEIDSLAPRRGqSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDK 155
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
329-580 1.02e-60

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 215.41  E-value: 1.02e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  329 VGASLADVDP----MNLD--PSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARAL 402
Cdd:PTZ00361   158 VGILLDEVDPlvsvMKVDkaPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAV 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  403 ANECShgdrkVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLAL-- 480
Cdd:PTZ00361   238 ANETS-----ATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELln 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  481 -MDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKKARKHILEIHTRDWNpkLSEPF-LDELAEKCVGYCG 558
Cdd:PTZ00361   313 qLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMT--LAEDVdLEEFIMAKDELSG 390
                          250       260
                   ....*....|....*....|..
gi 2004839052  559 ADIKALCTEAALMALRRRYPQI 580
Cdd:PTZ00361   391 ADIKAICTEAGLLALRERRMKV 412
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
342-617 1.01e-57

ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct cell division in bacteria. It has ATP-dependent zinc metalloprotease activity. It was formerly designated cell division protein FtsH. [Cellular processes, Cell division, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 208.29  E-value: 1.01e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  342 DPSVRFDNVGGLSNHIQSLKEMVVFpLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALAnecshGDRKVSFFMRKGA 421
Cdd:TIGR01241   49 KPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVA-----GEAGVPFFSISGS 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  422 DCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTL---LALMDGLDSRGEIVVIGATNR 498
Cdd:TIGR01241  123 DFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLnqlLVEMDGFGTNTGVIVIAATNR 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  499 LDSIDPALRRPGRFDREFLFSLPDKKARKHILEIHTRdwNPKLSEPF-LDELAEKCVGYCGADIKALCTEAALMALRRRY 577
Cdd:TIGR01241  203 PDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAK--NKKLAPDVdLKAVARRTPGFSGADLANLLNEAALLAARKNK 280
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 2004839052  578 PQIYGSSVKLKLDvaSIVLGPgdfSKAMRTIVPASQRALA 617
Cdd:TIGR01241  281 TEITMNDIEEAID--RVIAGP---EKKSRVISEKEKKLVA 315
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
358-514 8.09e-55

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 188.09  E-value: 8.09e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  358 QSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRL 437
Cdd:cd19529      3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATES-----NANFISVKGPELLSKWVGESEKAIRE 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004839052  438 LFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQ-IHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 514
Cdd:cd19529     78 IFRKARQVAPCVIFFDEIDSIAPRRGTTGDSgVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDR 155
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
347-514 7.55e-53

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 182.92  E-value: 7.55e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  347 FDNVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGADCLSK 426
Cdd:cd19502      2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTD-----ATFIRVVGSELVQK 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  427 WVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLAL---MDGLDSRGEIVVIGATNRLDSID 503
Cdd:cd19502     77 YIGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELlnqLDGFDPRGNIKVIMATNRPDILD 156
                          170
                   ....*....|.
gi 2004839052  504 PALRRPGRFDR 514
Cdd:cd19502    157 PALLRPGRFDR 167
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
358-514 2.77e-51

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 178.09  E-value: 2.77e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  358 QSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRL 437
Cdd:cd19528      3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANEC-----QANFISVKGPELLTMWFGESEANVRD 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  438 LFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSS---IVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 514
Cdd:cd19528     78 IFDKARAAAPCVLFFDELDSIAKARGGNIGDAGGAadrVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQ 157
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
343-614 6.84e-51

26S protease regulatory subunit 6B-like protein; Provisional


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 185.35  E-value: 6.84e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  343 PSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGAD 422
Cdd:PTZ00454   140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHT-----TATFIRVVGSE 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  423 CLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQ---DQIHSSIVSTLLALMDGLDSRGEIVVIGATNRL 499
Cdd:PTZ00454   215 FVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQtgaDREVQRILLELLNQMDGFDQTTNVKVIMATNRA 294
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  500 DSIDPALRRPGRFDREFLFSLPDKKARKHILEIHTRDWNpkLSEPF-LDELAEKCVGYCGADIKALCTEAALMALRR-RY 577
Cdd:PTZ00454   295 DTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMN--LSEEVdLEDFVSRPEKISAADIAAICQEAGMQAVRKnRY 372
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 2004839052  578 pqiygssvklkldvasiVLGPGDFSKAMRTIVPASQR 614
Cdd:PTZ00454   373 -----------------VILPKDFEKGYKTVVRKTDR 392
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
343-564 2.90e-50

proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some proteins are modified by ligation between an epsilon-amino group of a lysine side chain and the C-terminal carboxylate of the ubiquitin-like protein Pup. This modification leads to protein degradation by the archaeal-like proteasome found in the Actinobacteria. Members of this protein family belong to the AAA family of ATPases and tend to be clustered with the genes for Pup, the Pup ligase PafA, and structural components of the proteasome. This protein forms hexameric rings with ATPase activity. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 186.84  E-value: 2.90e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  343 PSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANE-----CSHGDRKVSFFM 417
Cdd:TIGR03689  177 PDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlaariGAEGGGKSYFLN 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  418 RKGADCLSKWVGESERQLRLLFDQAYLM----RPSIIFFDEIDGLAPVRSS-KQDQIHSSIVSTLLALMDGLDSRGEIVV 492
Cdd:TIGR03689  257 IKGPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRGSgVSSDVETTVVPQLLAEIDGVESLDNVIV 336
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004839052  493 IGATNRLDSIDPALRRPGRFDREFLFSLPDKKARKHILEIHTRDwnpklSEPFLDELAEKcVGYCGADIKAL 564
Cdd:TIGR03689  337 IGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLTD-----DLPLPEDLAAH-DGDREATAAAL 402
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
347-574 3.99e-50

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 178.15  E-value: 3.99e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  347 FDNVGGLSNHIQSLKEMVVFpLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSK 426
Cdd:COG1223      1 LDDVVGQEEAKKKLKLIIKE-LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGEL-----KLPLLTVRLDSLIGS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  427 WVGESERQLRLLFDQAYLmRPSIIFFDEIDGLAPVRSSKQD--QIHsSIVSTLLALMDGLDSrgEIVVIGATNRLDSIDP 504
Cdd:COG1223     75 YLGETARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDvgEVK-RVVNALLQELDGLPS--GSVVIAATNHPELLDS 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  505 ALRRpgRFDREFLFSLPDKKARKHILEIHTRDWNPKLSEPfLDELAEKCVGYCGADIKALCTEAALMALR 574
Cdd:COG1223    151 ALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELD-LKKLAKKLEGLSGADIEKVLKTALKKAIL 217
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
349-515 5.02e-50

first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 174.90  E-value: 5.02e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNHIQSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWV 428
Cdd:cd19518      1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGEL-----KVPFLKISATEIVSGVS 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  429 GESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGL----DSRGEIVVIGATNRLDSIDP 504
Cdd:cd19518     76 GESEEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDP 155
                          170
                   ....*....|.
gi 2004839052  505 ALRRPGRFDRE 515
Cdd:cd19518    156 ALRRAGRFDRE 166
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
342-576 1.12e-49

ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 186.78  E-value: 1.12e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  342 DPSVRFDNVGGLSNHIQSLKEMVVFpLLYPEIFEKF--KIqpPRGCLFYGPPGTGKTLVARALANECshgdrKVSFF--- 416
Cdd:COG0465    136 KPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLgaKI--PKGVLLVGPPGTGKTLLAKAVAGEA-----GVPFFsis 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  417 ------MRKGadclskwVGESeRqLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQ-------DQihssivsTL---LAL 480
Cdd:COG0465    208 gsdfveMFVG-------VGAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLggghderEQ-------TLnqlLVE 271
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  481 MDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKKARKHILEIHTRdwNPKLSEPF-LDELAEKCVGYCGA 559
Cdd:COG0465    272 MDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHAR--KKPLAPDVdLEVIARRTPGFSGA 349
                          250
                   ....*....|....*..
gi 2004839052  560 DIKALCTEAALMALRRR 576
Cdd:COG0465    350 DLANLVNEAALLAARRN 366
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
357-518 4.75e-49

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 171.31  E-value: 4.75e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  357 IQSLKEMVVFPLLYPEiFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLR 436
Cdd:cd19481      2 KASLREAVEAPRRGSR-LRRYGLGLPKGILLYGPPGTGKTLLAKALAGEL-----GLPLIVVKLSSLLSKYVGESEKNLR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  437 LLFDQAYLMRPSIIFFDEIDGLAPVRSS-KQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDRE 515
Cdd:cd19481     76 KIFERARRLAPCILFIDEIDAIGRKRDSsGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155

                   ...
gi 2004839052  516 FLF 518
Cdd:cd19481    156 IEF 158
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
386-520 2.16e-48

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: 168.54  E-value: 2.16e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  386 LFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSK 465
Cdd:pfam00004    2 LLYGPPGTGKTTLAKAVAKEL-----GAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG 76
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2004839052  466 QDQIHSSIVSTLLALMDGLDSR-GEIVVIGATNRLDSIDPALRrpGRFDREFLFSL 520
Cdd:pfam00004   77 GDSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
ftsH CHL00176
cell division protein; Validated
339-629 4.28e-48

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 183.33  E-value: 4.28e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  339 MNLDPSVRFDNVGGLSNHIQSLKEMVVFpLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMR 418
Cdd:CHL00176   174 MEADTGITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAE-----VPFFSI 247
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  419 KGADCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSK----QDQiHSSIVSTLLALMDGLDSRGEIVVIG 494
Cdd:CHL00176   248 SGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGigggNDE-REQTLNQLLTEMDGFKGNKGVIVIA 326
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  495 ATNRLDSIDPALRRPGRFDREFLFSLPDKKARKHILEIHTRdwNPKLSEPF-LDELAEKCVGYCGADIKALCTEAALMAL 573
Cdd:CHL00176   327 ATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHAR--NKKLSPDVsLELIARRTPGFSGADLANLLNEAAILTA 404
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2004839052  574 RRRYPQIYGSSVKLKLD--VASIVLGPGDFSKAMRTIvpasqrALAPPGRALSPTLRP 629
Cdd:CHL00176   405 RRKKATITMKEIDTAIDrvIAGLEGTPLEDSKNKRLI------AYHEVGHAIVGTLLP 456
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
345-515 8.90e-47

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 165.48  E-value: 8.90e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  345 VRFDNVGGLSNHIQSLKEMVVFpLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCL 424
Cdd:cd19501      1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEA-----GVPFFSISGSDFV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  425 SKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTL---LALMDGLDSRGEIVVIGATNRLDS 501
Cdd:cd19501     75 EMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLnqlLVEMDGFESNTGVIVIAATNRPDV 154
                          170
                   ....*....|....
gi 2004839052  502 IDPALRRPGRFDRE 515
Cdd:cd19501    155 LDPALLRPGRFDRQ 168
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
360-514 4.14e-46

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 163.04  E-value: 4.14e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  360 LKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWVGESERQLRLLF 439
Cdd:cd19530      8 LTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANES-----GANFISVKGPELLNKYVGESERAVRQVF 82
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004839052  440 DQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 514
Cdd:cd19530     83 QRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
350-517 2.47e-45

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 160.98  E-value: 2.47e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  350 VGGLSNHIQSLKEMVVFPLLYPEIFeKFKIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGADCLSKWVG 429
Cdd:cd19509      1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESG-----STFFSISASSLVSKWVG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  430 ESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGL--DSRGEIVVIGATNRLDSIDPALR 507
Cdd:cd19509     75 ESEKIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFL 154
                          170
                   ....*....|
gi 2004839052  508 RpgRFDREFL 517
Cdd:cd19509    155 R--RFEKRIY 162
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
359-514 1.17e-41

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 150.36  E-value: 1.17e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  359 SLKEMVVFPLLYPEIFEKfKIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGADCLSKWVGESERQLRLL 438
Cdd:cd19527      4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECS-----LNFLSVKGPELINMYIGESEANVREV 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004839052  439 FDQAYLMRPSIIFFDEIDGLAPVRSSKQDQ--IHSSIVSTLLALMDGLDSRGE-IVVIGATNRLDSIDPALRRPGRFDR 514
Cdd:cd19527     78 FQKARDAKPCVIFFDELDSLAPSRGNSGDSggVMDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
358-514 1.22e-40

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 147.58  E-value: 1.22e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  358 QSLKEMVVFPLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGADCLSKWVGESERQLRL 437
Cdd:cd19526      3 KALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECG-----LNFISVKGPELLNKYIGASEQNVRD 77
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2004839052  438 LFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 514
Cdd:cd19526     78 LFSRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDK 154
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
347-574 3.70e-40

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 159.43  E-value: 3.70e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  347 FDNVGGLSNHIQSLKEMVVFpLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALAnecshGDRKVSFFMRKGADCLSK 426
Cdd:PRK10733   151 FADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIA-----GEAKVPFFTISGSDFVEM 224
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  427 WVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTL---LALMDGLDSRGEIVVIGATNRLDSID 503
Cdd:PRK10733   225 FVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLnqmLVEMDGFEGNEGIIVIAATNRPDVLD 304
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2004839052  504 PALRRPGRFDREFLFSLPDKKARKHILEIHTRDWnPKLSEPFLDELAEKCVGYCGADIKALCTEAALMALR 574
Cdd:PRK10733   305 PALLRPGRFDRQVVVGLPDVRGREQILKVHMRRV-PLAPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
332-508 1.97e-38

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 142.05  E-value: 1.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  332 SLADVDPMNLDPSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFEKFKiQPPRGCLFYGPPGTGKTLVARALANECshgdr 411
Cdd:cd19525      6 ELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQS----- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  412 KVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGE-- 489
Cdd:cd19525     80 GATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEdr 159
                          170
                   ....*....|....*....
gi 2004839052  490 IVVIGATNRLDSIDPALRR 508
Cdd:cd19525    160 ILVVGATNRPQEIDEAARR 178
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
349-512 4.55e-38

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 140.25  E-value: 4.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNHIQSLKEMVVFPLLYPEIFEKFKI-QPPRGCLFYGPPGTGKTLVARALANECshGDRKVSFFMrkgADCLSKW 427
Cdd:cd19520      1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEA--GARFINLQV---SSLTDKW 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  428 VGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRG--EIVVIGATNRLDSIDPA 505
Cdd:cd19520     76 YGESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGncRVIVMGATNRPQDLDEA 155

                   ....*....
gi 2004839052  506 LRR--PGRF 512
Cdd:cd19520    156 ILRrmPKRF 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
343-514 3.99e-37

ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein sorting-associated protein 4 (Vps4) is believed to be involved in intracellular protein transport out of a prevacuolar endosomal compartment. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 137.69  E-value: 3.99e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  343 PSVRFDNVGGLSNHIQSLKEMVVFPLLYPEIFeKFKIQPPRGCLFYGPPGTGKTLVARALANECSHgdrkvSFFMRKGAD 422
Cdd:cd19521      2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLF-TGNRKPWSGILLYGPPGTGKSYLAKAVATEANS-----TFFSVSSSD 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  423 CLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGL--DSRGeIVVIGATNRLD 500
Cdd:cd19521     76 LVSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgnDSQG-VLVLGATNIPW 154
                          170
                   ....*....|....
gi 2004839052  501 SIDPALRRpgRFDR 514
Cdd:cd19521    155 QLDSAIRR--RFEK 166
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
365-513 1.09e-34

first of two ATPase domains of NSF and SEC18, and similar ATPase domains; N-ethylmaleimide-sensitive factor (NSF) and Saccharomyces cerevisiae Vesicular-fusion protein Sec18, key factors for eukaryotic trafficking, are ATPases and SNARE disassembly chaperones. NSF/Sec18 activate or prime SNAREs, the terminal catalysts of membrane fusion. Sec18/NSF associates with SNARE complexes through binding Sec17/alpha-SNAP. Sec18 has an N-terminal cap domain and two nucleotide-binding domains (D1 and D2) which form the two rings of the hexameric complex. The hydrolysis of ATP by D1 generates most of the energy necessary to disassemble inactive SNARE bundles, while the D2 ring binds ATP to stabilize the homohexamer. This subfamily includes the first (D1) ATPase domain of NSF/Sec18, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 131.07  E-value: 1.09e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  365 VFPllyPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSHGDRKVSffmrKGADCLSKWVGESERQLRLLF----- 439
Cdd:cd19504     21 VFP---PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIV----NGPEILNKYVGESEANIRKLFadaee 93
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004839052  440 DQAYLMRPS---IIFFDEIDGLAPVRSSKQDQ--IHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFD 513
Cdd:cd19504     94 EQRRLGANSglhIIIFDEIDAICKQRGSMAGStgVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
349-508 2.15e-34

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 130.10  E-value: 2.15e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNHIQSLKEMVVFPLLYPEIFEKFKiQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWV 428
Cdd:cd19522      1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATEC-----GTTFFNVSSSTLTSKYR 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  429 GESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIV-STLLALMDGL-------DSRGEIVVIGATNRLD 500
Cdd:cd19522     75 GESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVkSELLVQMDGVggasendDPSKMVMVLAATNFPW 154

                   ....*...
gi 2004839052  501 SIDPALRR 508
Cdd:cd19522    155 DIDEALRR 162
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
349-508 2.48e-33

ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in microtubule dynamics; it specifically recognizes and cuts microtubules that are polyglutamylated. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 126.89  E-value: 2.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNHIQSLKEMVVFPLLYPEIFEKFKiQPPRGCLFYGPPGTGKTLVARALANECshgdrKVSFFMRKGADCLSKWV 428
Cdd:cd19524      1 DIAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAES-----NATFFNISAASLTSKYV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  429 GESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIVSTLLALMDGLDSRGE--IVVIGATNRLDSIDPA- 505
Cdd:cd19524     75 GEGEKLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAv 154

                   ...
gi 2004839052  506 LRR 508
Cdd:cd19524    155 LRR 157
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
378-520 5.04e-28

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: 111.08  E-value: 5.04e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  378 KIQPPRGCLFYGPPGTGKTLVARALANECSHgdRKVSFFMRKGADCLSKWVGESERQ---LRLLFDQAYLMRPSIIFFDE 454
Cdd:cd00009     15 ELPPPKNLLLYGPPGTGKTTLARAIANELFR--PGAPFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPGVLFIDE 92
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004839052  455 IDGLAPvrsskqdQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSL 520
Cdd:cd00009     93 IDSLSR-------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
349-517 1.20e-25

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 104.58  E-value: 1.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNHIQSLKEMVVFPLLYPEIFEKFkIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGADCLSKWV 428
Cdd:cd19523      1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLG-----ATFLRLRGSTLVAKWA 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  429 GESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIhSSIVSTLLALMDGLDSRGE--IVVIGATNRLDSIDPAL 506
Cdd:cd19523     75 GEGEKILQASFLAARCRQPSVLFISDLDALLSSQDDEASPV-GRLQVELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESL 153
                          170
                   ....*....|.
gi 2004839052  507 RRpgRFDREFL 517
Cdd:cd19523    154 RR--YFSKRLL 162
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
914-1017 7.40e-22

Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine.


Pssm-ID: 99922 [Multi-domain]  Cd Length: 99  Bit Score: 91.66  E-value: 7.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  914 LRELRLFLRDVTKRLATDkRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:cd04369      1 LKKKLRSLLDALKKLKRD-LSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYNG 79
                           90       100
                   ....*....|....*....|....
gi 2004839052  994 DkdpgDKVIRHRACSLKDTAHAIF 1017
Cdd:cd04369     80 P----GSPIYKDAKKLEKLFEKLL 99
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
917-1017 7.21e-21

Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein assumed to be a transcriptional regulator. BRD1 has been implicated with brain development and susceptibility to schizophrenia and bipolar affective disorder. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99944  Cd Length: 98  Bit Score: 88.61  E-value: 7.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  917 LRLFLRDVTKRLATDKRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNpDKD 996
Cdd:cd05512      2 LEVLLRKTLDQLQEKDTAEIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYN-AKD 80
                           90       100
                   ....*....|....*....|..
gi 2004839052  997 pgdkVIRHRAC-SLKDTAHAIF 1017
Cdd:cd05512     81 ----TIFYRAAvRLRDQGGAIL 98
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
381-522 1.76e-19

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 86.66  E-value: 1.76e-19
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052   381 PPRGCLFYGPPGTGKTLVARALANE------------CSHGDRKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLMRPS 448
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARElgppgggviyidGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004839052   449 IIFFDEIDGLAPVRSSKQDQihssiVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPgRFDREFLFSLPD 522
Cdd:smart00382   81 VLILDEITSLLDAEQEALLL-----LLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
937-997 1.02e-18

Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates acetylation of histones at lysine residues; such acetylation is generally correlated with the activation of transcription. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 82.60  E-value: 1.02e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2004839052  937 FSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNPDKDP 997
Cdd:cd05509     22 FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGPDTE 82
BROMO smart00297
bromo domain;
914-1012 1.44e-18

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 82.33  E-value: 1.44e-18
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052   914 LRELRLFLRDVTKRLATDKRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:smart00297    5 QKKLQELLKAVLDKLDSHPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNG 84
                            90
                    ....*....|....*....
gi 2004839052   994 DkdpgDKVIRHRACSLKDT 1012
Cdd:smart00297   85 P----DSEVYKDAKKLEKF 99
ycf46 CHL00195
Ycf46; Provisional
343-568 2.30e-18

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 90.08  E-value: 2.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  343 PSVRFDNVGGLSNHIQSLKEMvvfpllyPEIFEK----FKIQPPRGCLFYGPPGTGKTLVARALANECSHGDRKVSFfmr 418
Cdd:CHL00195   223 VNEKISDIGGLDNLKDWLKKR-------STSFSKqasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDV--- 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  419 kgADCLSKWVGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQIHSSIV-STLLALMDglDSRGEIVVIGATN 497
Cdd:CHL00195   293 --GKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGDSGTTNRVlATFITWLS--EKKSPVFVVATAN 368
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004839052  498 RLDSIDPALRRPGRFDREFLFSLPDKKARKHILEIHTRDWNPKLSEPF-LDELAEKCVGYCGADIKALCTEA 568
Cdd:CHL00195   369 NIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYdIKKLSKLSNKFSGAEIEQSIIEA 440
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
920-997 1.01e-17

Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99930  Cd Length: 102  Bit Score: 80.01  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  920 FLRDVTKRLATDKRFNI---FSKPVDIE--EVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNPD 994
Cdd:cd05498      4 FCSGILKELFSKKHKAYawpFYKPVDPEalGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPP 83

                   ...
gi 2004839052  995 KDP 997
Cdd:cd05498     84 DHP 86
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
349-516 5.01e-16

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 77.02  E-value: 5.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  349 NVGGLSNhiqsLKEMVVF-PLLYPEIFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSHGDRKVSFfmrkgADCLSKW 427
Cdd:cd19507      1 DVGGLDN----LKDWLKKrKAAFSKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDM-----GRLFGGL 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  428 VGESERQLRLLFDQAYLMRPSIIFFDEIDGLAPVRSSKQDQ-IHSSIVSTLLALMDglDSRGEIVVIGATNRLDSIDPAL 506
Cdd:cd19507     72 VGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNADSKGDSgTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPEL 149
                          170
                   ....*....|
gi 2004839052  507 RRPGRFDREF 516
Cdd:cd19507    150 LRKGRFDEIF 159
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
901-1013 1.32e-15

Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, and SLIK. SAGA is involved in the RNA polymerase II-dependent transcriptional regulation of about 10% of all yeast genes. The SPT7 bromodomain has been shown to weakly interact with acetylated histone H3, but not H4. The human representative of this subfamily is cat eye syndrome critical region protein 2 (CECR2). Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99942 [Multi-domain]  Cd Length: 112  Bit Score: 74.01  E-value: 1.32e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  901 EEQRRLAEQEENTLRELRLFLRDVTKrlatdkrfniFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVD 980
Cdd:cd05510      3 IGQEEFYESLDKVLNELKTYTEHSTP----------FLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDD 72
                           90       100       110
                   ....*....|....*....|....*....|...
gi 2004839052  981 IDLICSNALEYNPDKdpgDKVIRHRACSLKDTA 1013
Cdd:cd05510     73 LNLIWKNCLLYNSDP---SHPLRRHANFMKKKA 102
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
936-993 4.07e-15

Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 71.96  E-value: 4.07e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2004839052  936 IFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:pfam00439   16 PFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
926-1028 3.80e-14

Bromodomain, uncharacterized subfamily specific to plants. Might function as a global transcription factor. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99938  Cd Length: 99  Bit Score: 69.67  E-value: 3.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  926 KRLATDKRFNIFSKPVDIE--EVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNPdkdPGDKVir 1003
Cdd:cd05506     10 RKLMKHKWGWVFNAPVDVValGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNP---PGNDV-- 84
                           90       100
                   ....*....|....*....|....*
gi 2004839052 1004 hracslkdtaHAIfAAELDPEFDRM 1028
Cdd:cd05506     85 ----------HTM-AKELLKIFETR 98
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
383-514 8.76e-14

Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of mitochondrial respiratory chain complex III and plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 70.46  E-value: 8.76e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  383 RGCLFYGPPGTGKTLVARALANECSHGDRKVSffmrkgadcLSKwVGESERQLRLLFDQAylMRPSIIFFDEID-----G 457
Cdd:cd19510     24 RGYLLYGPPGTGKSSFIAALAGELDYDICDLN---------LSE-VVLTDDRLNHLLNTA--PKQSIILLEDIDaafesR 91
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2004839052  458 LAPVRSSKQDQIHSSI-VSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 514
Cdd:cd19510     92 EHNKKNPSAYGGLSRVtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
937-992 1.10e-13

Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, a large multi-domain complex, which initiates the assembly of the transcription machinery. TAFII250 contains two bromodomains that specifically bind to acetylated histone H4. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99943 [Multi-domain]  Cd Length: 112  Bit Score: 68.83  E-value: 1.10e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2004839052  937 FSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN 992
Cdd:cd05511     21 FHTPVNKKKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYN 76
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
916-997 5.26e-12

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99931  Cd Length: 102  Bit Score: 63.46  E-value: 5.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  916 ELRlFLRDVTKRLATDKRFNI---FSKPVDieEVSD----YLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNA 988
Cdd:cd05499      1 ELK-FCEEVLKELMKPKHSAYnwpFLDPVD--PVALnipnYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNC 77

                   ....*....
gi 2004839052  989 LEYNPDKDP 997
Cdd:cd05499     78 YTFNPEGTD 86
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
386-534 1.59e-11

type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the actinobacterial flavor of type VII secretion systems. Species such as Mycobacterium tuberculosis have several instances of this system per genome, designated EccA1, EccA2, etc. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 68.72  E-value: 1.59e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  386 LFYGPPGTGKTLVARALANE-CSHGD-RKVSFFMRKGADCLSKWVGESERQLRLLFDQAYlmrPSIIFFDEIDGLAPVRS 463
Cdd:TIGR03922  316 LFAGPPGTGKTTIARVVAKIyCGLGVlRKPLVREVSRADLIGQYIGESEAKTNEIIDSAL---GGVLFLDEAYTLVETGY 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  464 SKQDQIHSSIVSTLLALMDglDSRGEIVVIGATNRLD-----SIDPALRRpgRFDREFLF-------------------- 518
Cdd:TIGR03922  393 GQKDPFGLEAIDTLLARME--NDRDRLVVIGAGYRKDldkflEVNEGLRS--RFTRVIEFpsyspdelveiarrmaterd 468
                          170
                   ....*....|....*.
gi 2004839052  519 SLPDKKARKHILEIHT 534
Cdd:TIGR03922  469 SVLDDAAADALLEAAT 484
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
386-506 2.94e-11

ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as Thyroid hormone receptor interactor 13 (TRIP13) and 16E1BP) is a key regulator of specific chromosomal events, like the control of G2/prophase processes such as DNA break formation and recombination, checkpoint signaling, and chromosome synapsis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 64.39  E-value: 2.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  386 LFYGPPGTGKTLVARALANE----CSHGDRKVSFFMRKGADCLSKWVGESERQLRLLFDQAYLM---RPSIIF--FDEID 456
Cdd:cd19508     56 LLHGPPGTGKTSLCKALAQKlsirLSSRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELiddKDALVFvlIDEVE 135
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2004839052  457 GLAPVRSSKQDQIHSS----IVSTLLALMDGLDSRGEIVVIGATNRLDSIDPAL 506
Cdd:cd19508    136 SLAAARSASSSGTEPSdairVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
937-992 3.38e-11

Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown to inhibit cell growth and the progression of the cell cycle by regulating cell-cycle genes at the transcriptional level. BRD7 has been identified as a gene involved in nasopharyngeal carcinoma. The protein interacts with acetylated histone H3 via its bromodomain. Bromodomains are 110 amino acid long domains that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99945  Cd Length: 98  Bit Score: 61.27  E-value: 3.38e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2004839052  937 FSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN 992
Cdd:cd05513     22 FAFPVTDFIAPGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYN 77
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
546-580 4.99e-11

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 58.70  E-value: 4.99e-11
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2004839052  546 LDELAEKCVGYCGADIKALCTEAALMALRRRYPQI 580
Cdd:pfam17862    4 LEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
937-995 1.18e-10

Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99928  Cd Length: 119  Bit Score: 60.16  E-value: 1.18e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2004839052  937 FSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNPDK 995
Cdd:cd05496     26 FRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTPNK 84
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
916-1023 1.19e-10

Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase acting on histone, which gives a specific tag for transcriptional activation and also acetylates non-histone proteins. CREBBP binds specifically to phosphorylated CREB protein and augments the activity of phosphorylated CREB to activate transcription of cAMP-responsive genes. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99927  Cd Length: 108  Bit Score: 59.76  E-value: 1.19e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  916 ELRLFLRDVTKRLATDKRFNI-FSKPVD--IEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN 992
Cdd:cd05495      3 ELRQALMPTLEKLYKQDPESLpFRQPVDpkLLGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYN 82
                           90       100       110
                   ....*....|....*....|....*....|..
gi 2004839052  993 PDKdpgDKVirHRACS-LKDtahaIFAAELDP 1023
Cdd:cd05495     83 RKT---SRV--YKYCTkLAE----VFEQEIDP 105
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
937-996 1.43e-10

Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was identified as a novel human bromodomain gene by cDNA library screening. The Drosophila homologue, Acf1, is part of the CHRAC (chromatin accessibility complex) and regulates ISWI-induced nucleosome remodeling. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99936  Cd Length: 115  Bit Score: 59.72  E-value: 1.43e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  937 FSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNPDKD 996
Cdd:cd05504     33 FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHT 92
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
937-992 2.89e-10

Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The Williams-Beuren syndrome deletion transcript 9 is a putative transcriptional regulator. WSTF was found to play a role in vitamin D-mediated transcription as part of two chromatin remodeling complexes, WINAC and WICH. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99937  Cd Length: 97  Bit Score: 58.32  E-value: 2.89e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2004839052  937 FSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN 992
Cdd:cd05505     21 FREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYY 76
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
925-992 4.80e-10

Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast transcription factors involved in the expression of a wide range of genes, including snRNAs; they are required for sporulation and DNA repair and protect histone H4 from deacetylation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99932  Cd Length: 103  Bit Score: 58.09  E-value: 4.80e-10
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  925 TKRLaTDKRFniFSKPVDIEE--VSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN 992
Cdd:cd05500     16 LKRL-KDARP--FLVPVDPVKlnIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFN 82
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
937-997 1.00e-09

Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B (BAZ2B) were identified as a novel human bromodomain gene by cDNA library screening. BAZ2A is also known as Tip5 (Transcription termination factor I-interacting protein 5) and hWALp3. The proteins may play roles in transcriptional regulation. Human Tip5 is part of a complex termed NoRC (nucleolar remodeling complex), which induces nucleosome sliding and may play a role in the regulation of the rDNA locus. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99935  Cd Length: 97  Bit Score: 57.00  E-value: 1.00e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2004839052  937 FSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNPDKDP 997
Cdd:cd05503     21 FLEPVNTKLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSE 81
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
916-1002 8.39e-09

Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET subfamily of bromodomain proteins; the first bromodomain in Brdt has been shown to be essential for male germ cell differentiation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99929  Cd Length: 107  Bit Score: 54.74  E-value: 8.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  916 ELRLFLRDVTKRLATDKRFNIFSKPVDIE--EVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:cd05497      5 QLQYLLKVVLKALWKHKFAWPFQQPVDAVklNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNK 84

                   ....*....
gi 2004839052  994 dkdPGDKVI 1002
Cdd:cd05497     85 ---PGDDVV 90
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
914-994 1.26e-08

Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99946  Cd Length: 105  Bit Score: 53.85  E-value: 1.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  914 LRELRLFLRDVT----KRLATdkrfnIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNAL 989
Cdd:cd05515      5 LWELYNAVKNYTdgrgRRLSL-----IFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNAC 79

                   ....*.
gi 2004839052  990 EYN-PD 994
Cdd:cd05515     80 KYNePD 85
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
381-514 2.31e-08

ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; however, its function remains unclear. The gene encoding YCF2 is the largest known plastid gene in angiosperms and has been used to predict phylogenetic relationships. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 54.69  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  381 PPRGCLFYGPPGTGKTLVARALANEcSHG-----------DRKVSFFMRKGADCLSKWvGESERQLRLLFDQAYLMRPSI 449
Cdd:cd19505     11 PSKGILLIGSIETGRSYLIKSLAAN-SYVplirislnkllYNKPDFGNDDWIDGMLIL-KESLHRLNLQFELAKAMSPCI 88
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004839052  450 IFFDEIDGLApVRSSKQDQIHSSivSTLLALMDGLDSRG-------EIVVIGATNRLDSIDPALRRPGRFDR 514
Cdd:cd19505     89 IWIPNIHELN-VNRSTQNLEEDP--KLLLGLLLNYLSRDfeksstrNILVIASTHIPQKVDPALIAPNRLDT 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
724-842 3.43e-08

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 53.37  E-value: 3.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  724 LLLAGAPGSGQSShLAPALLHHLdKLPVHRLDLPTLYSVSAKTPEESCAQVFREARRSVPSVVYMPHI-------SEWWD 796
Cdd:pfam00004    1 LLLYGPPGTGKTT-LAKAVAKEL-GAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIdalagsrGSGGD 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 2004839052  797 TVSDTVKSTFLTLLQDV-PSFSPVLVLATAeTHYSKLSDEVRSIFQR 842
Cdd:pfam00004   79 SESRRVVNQLLTELDGFtSSNSKVIVIAAT-NRPDKLDPALLGRFDR 124
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
709-825 1.09e-07

ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of photosynthesis in cyanobacteria, especially in CO2 uptake and utilization. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 52.76  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  709 FSSSALQQPTAYRPRLLLAGAPGSGQSShLAPALLHHLdKLPVHRLDLPTLYSVSAKTPEESCAQVFREARRSVPSVVYM 788
Cdd:cd19507     19 FSKQASAYGLPTPKGLLLVGIQGTGKSL-TAKAIAGVW-QLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWI 96
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2004839052  789 PHISEWWDT--------VSDTVKSTFLTLLQDvpSFSPVLVLATA 825
Cdd:cd19507     97 DEIEKGFSNadskgdsgTSSRVLGTFLTWLQE--KKKPVFVVATA 139
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
697-824 1.09e-07

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 52.67  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  697 LTSSAMHRPFLHFSSSALQQ-PTAYRPRLLLAGAPGSGQSsHLAPALLHHLDkLPVHRLDLPTLYSVSAKTPEESCAQVF 775
Cdd:cd19481      1 LKASLREAVEAPRRGSRLRRyGLGLPKGILLYGPPGTGKT-LLAKALAGELG-LPLIVVKLSSLLSKYVGESEKNLRKIF 78
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2004839052  776 REARRSVPSVVYMPHI--------SEWWDTVSDTVKSTFLTLLQDVPSFSPVLVLAT 824
Cdd:cd19481     79 ERARRLAPCILFIDEIdaigrkrdSSGESGELRRVLNQLLTELDGVNSRSKVLVIAA 135
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
924-996 1.23e-07

Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with the thyroid hormone receptor in a ligand-dependent fashion and enhances thyroid hormone-dependent activation from thyroid response elements. Brd8 is thought to be a nuclear receptor coactivator. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99939  Cd Length: 104  Bit Score: 51.21  E-value: 1.23e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2004839052  924 VTKRLATDKRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN-PDKD 996
Cdd:cd05507     11 VYRTLASHRYASVFLKPVTEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNsSDHD 84
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
899-1056 1.33e-07

Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin structure and dynamics / Transcription];


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 55.58  E-value: 1.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  899 SAEEQRRLAEQEENTLRELR-LFLRDVTKRlatdkrFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDF 977
Cdd:COG5076    136 PKIEDELLYADNKAIAKFKKqLFLRDGRFL------SSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEF 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  978 LVDIDLICSNALEYNpdkDPGDKVIRHRacslkDTAHAIFAAELDPEFDRMCEE-IKEARRKRDLLTPAQLSAVPGAGAT 1056
Cdd:COG5076    210 VSDLNLMFDNCKLYN---GPDSSVYVDA-----KELEKYFLKLIEEIPEEMLELsIKPGREEREERESVLITNSQAHVGA 281
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
386-528 1.59e-07

AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected by the pfam00004 model.


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 52.58  E-value: 1.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  386 LFYGPPGTGKTLVARALANECSHGDRKV-----SFFMRKGAdcLSKWVGESERQLR-----LLFDQAYLMRPSIIFFDEI 455
Cdd:pfam07724    7 LFLGPTGVGKTELAKALAELLFGDERALiridmSEYMEEHS--VSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEI 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  456 dglapvrsskqDQIHSSIVSTLLALMDG---LDSRGE------IVVIGATNrLDSIDP--ALRRPGRFDREFLFSLPDKK 524
Cdd:pfam07724   85 -----------EKAHPGVQNDLLQILEGgtlTDKQGRtvdfknTLFIMTGN-FGSEKIsdASRLGDSPDYELLKEEVMDL 152

                   ....
gi 2004839052  525 ARKH 528
Cdd:pfam07724  153 LKKG 156
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
945-992 2.07e-07

Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 is a global transcriptional activator, which cooperates with nuclear hormone receptors to boost transcriptional activation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99947  Cd Length: 107  Bit Score: 50.50  E-value: 2.07e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 2004839052  945 EVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN 992
Cdd:cd05516     36 ELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFN 83
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
383-513 4.20e-07

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 50.99  E-value: 4.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  383 RGCLFYGPPGTGKTLVARALANEC-------SHGDrkVSFFMRKGADCLSK---WVGESERQLrllfdqaylmrpsIIFF 452
Cdd:cd19512     23 RNILFYGPPGTGKTLFAKKLALHSgmdyaimTGGD--VAPMGREGVTAIHKvfdWANTSRRGL-------------LLFV 87
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2004839052  453 DEIDGLAPVRSSkqDQIHSSIVSTLLALM--DGLDSRgEIVVIGATNRLDSIDPALRrpGRFD 513
Cdd:cd19512     88 DEADAFLRKRST--EKISEDLRAALNAFLyrTGEQSN-KFMLVLASNQPEQFDWAIN--DRID 145
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
937-992 5.15e-07

Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) was identified as a potential tumor suppressor genes, it shares domain architecture with BS69/ZMYND11; both have been implicated in the regulation of cellular proliferation. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99940  Cd Length: 99  Bit Score: 49.30  E-value: 5.15e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2004839052  937 FSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN 992
Cdd:cd05508     23 FLKPVDLEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIYN 78
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
723-866 5.88e-07

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 53.76  E-value: 5.88e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  723 RLLLAGAPGSGQSsHLAPALLHHLDkLPVHRLDLPTLYS----VSAKtpeeSCAQVFREARRSVPSVVYM-------PHI 791
Cdd:COG0464    193 GLLLYGPPGTGKT-LLARALAGELG-LPLIEVDLSDLVSkyvgETEK----NLREVFDKARGLAPCVLFIdeadalaGKR 266
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004839052  792 SEWWDTVSDTVKSTFLTLLQDVPsfSPVLVLATAeTHYSKLSDEVRSIFQrtygEVVALSPPGEEEIRHFFSDLL 866
Cdd:COG0464    267 GEVGDGVGRRVVNTLLTEMEELR--SDVVVIAAT-NRPDLLDPALLRRFD----EIIFFPLPDAEERLEIFRIHL 334
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
912-1016 6.76e-07

Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are components of the RSC complex (remodeling the structure of chromatin), are essential for transcriptional control, and have a specific domain architecture including two bromodomains. The RSC complex has also been linked to homologous recombination and nonhomologous end-joining repair of DNA double strand breaks. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99953 [Multi-domain]  Cd Length: 104  Bit Score: 49.16  E-value: 6.76e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  912 NTLRELRLFlRDVTKRLatdkRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEY 991
Cdd:cd05522      8 NILKGLRKE-RDENGRL----LTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLY 82
                           90       100
                   ....*....|....*....|....*
gi 2004839052  992 NpdkDPGDKVIRhRACSLKDTAHAI 1016
Cdd:cd05522     83 N---ENDSQEYK-DAVLLEKEARLL 103
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
385-507 1.16e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 52.78  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  385 CLFYGPPGTGKTLVARALANECshgDRKvsfFMRKGAdclskwVGESERQLRLLFDQAYLMRPS----IIFFDEIDGLAp 460
Cdd:PRK13342    39 MILWGPPGTGKTTLARIIAGAT---DAP---FEALSA------VTSGVKDLREVIEEARQRRSAgrrtILFIDEIHRFN- 105
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 2004839052  461 vrSSKQDqihssivsTLLALMDgldsRGEIVVIGAT--NRLDSIDPALR 507
Cdd:PRK13342   106 --KAQQD--------ALLPHVE----DGTITLIGATteNPSFEVNPALL 140
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
948-1035 1.21e-06

Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99954 [Multi-domain]  Cd Length: 113  Bit Score: 48.48  E-value: 1.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  948 DYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNPDKDPgdkviRHR-ACSLKDTahaifaaeldpeFD 1026
Cdd:cd05524     40 EYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPDSP-----EHKdACKLWEL------------FL 102

                   ....*....
gi 2004839052 1027 RMCEEIKEA 1035
Cdd:cd05524    103 SARNEVLSG 111
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
937-995 2.56e-06

Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of the tripartite motif (TRIM) protein family, which is characterized by a particular domain architecture. It functions by recruiting coactivators and/or corepressors to modulate transcription. Vertebrate Tif1-gamma, also labeled E3 ubiquitin-protein ligase TRIM33, plays a role in the control of hematopoiesis. Its homologue in Xenopus laevis, Ectodermin, has been shown to function in germ-layer specification and control of cell growth during embryogenesis. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 47.67  E-value: 2.56e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004839052  937 FSKPVDiEEVSDYLEVIRQPMDLSTVMTKID---THQYLTAKDFLVDIDLICSNALEYNPDK 995
Cdd:cd05502     25 FHEPVS-PSVPNYYKIIKTPMDLSLIRKKLQpksPQHYSSPEEFVADVRLMFKNCYKFNEED 85
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
915-992 1.10e-05

Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 45.51  E-value: 1.10e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2004839052  915 RELRLFLRDVTKRLATDKRF-NIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN 992
Cdd:cd05518      4 RMLALFLYVLEYREGSGRRLcDLFMEKPSKKDYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYN 82
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
936-993 1.74e-05

Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome critical region-2 of chromosome 21. It encodes for a nuclear protein containing WD40 repeats and two bromodomains, which may function as a transcriptional regulator involved in chromatin remodeling and play a role in embryonic development. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99958  Cd Length: 128  Bit Score: 45.79  E-value: 1.74e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2004839052  936 IFSKPVDI-EEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:cd05529     47 YFEYPVDLrAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLILSNAETFNE 105
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
386-496 5.54e-05

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 47.36  E-value: 5.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  386 LFYGPPGTGKTLVARALANECshgdrKVSFFMrkgadcLSKwVGESERQLRLLFDQAYLMR----PSIIFFDEIDglapv 461
Cdd:COG2256     53 ILWGPPGTGKTTLARLIANAT-----DAEFVA------LSA-VTSGVKDIREVIEEARERRaygrRTILFVDEIH----- 115
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2004839052  462 RSSK--QDqihssivsTLLALMDgldsRGEIVVIGAT 496
Cdd:COG2256    116 RFNKaqQD--------ALLPHVE----DGTITLIGAT 140
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
714-823 7.52e-05

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 44.59  E-value: 7.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  714 LQQPTAYR------PR-LLLAGAPGSGQSsHLAPALLHHLDkLPVHRLDLPTLYSVSAKTPEESCAQVFREARRSVPSVV 786
Cdd:cd19503     20 LKYPELFRalglkpPRgVLLHGPPGTGKT-LLARAVANEAG-ANFLSISGPSIVSKYLGESEKNLREIFEEARSHAPSII 97
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 2004839052  787 YMPHI-------SEWWDTVSDTVKSTFLTLLQDVPSFSPVLVLA 823
Cdd:cd19503     98 FIDEIdalapkrEEDQREVERRVVAQLLTLMDGMSSRGKVVVIA 141
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
948-1001 8.14e-05

Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99948  Cd Length: 103  Bit Score: 43.20  E-value: 8.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2004839052  948 DYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNpdkDPGDKV 1001
Cdd:cd05517     38 DYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFN---EPGSQV 88
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
948-993 1.58e-04

Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which contains 6 bromodomains. The human ortholog BAF180 is part of a SWI/SNF chromatin-remodeling complex, and it may carry out the functions of Yeast Rsc-1 and Rsc-2. It was shown that polybromo bromodomains bind to histone H3 at specific acetyl-lysine positions. Bromodomains are found in many chromatin-associated proteins and in nuclear histone acetyltransferases. They interact specifically with acetylated lysine, but not all the bromodomains in polybromo may bind to acetyl-lysine.


Pssm-ID: 99951  Cd Length: 103  Bit Score: 42.33  E-value: 1.58e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2004839052  948 DYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNP 993
Cdd:cd05520     38 DYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNV 83
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
946-1011 1.70e-04

Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the trithorax-group in Drosophila melanogaster, an epigenetic transcriptional regulator of HOX genes. Drosophila ASH1 has been shown to methylate specific lysines in histones H3 and H4. Mammalian ASH1 has been shown to methylate histone H3. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99955 [Multi-domain]  Cd Length: 106  Bit Score: 42.38  E-value: 1.70e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2004839052  946 VSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNPDKDPgdkvIRHRACSLKD 1011
Cdd:cd05525     38 NPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSP----IGRDVCRLRK 99
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
379-461 2.06e-04

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 44.39  E-value: 2.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  379 IQPPRGCLFYGPPGTGKTLVARALANE-CSHGdRKVSFFmrkgadCLSKWVGE-----SERQLRLLFDQayLMRPSIIFF 452
Cdd:COG1484     96 IERGENLILLGPPGTGKTHLAIALGHEaCRAG-YRVRFT------TAPDLVNElkearADGRLERLLKR--LAKVDLLIL 166

                   ....*....
gi 2004839052  453 DEIdGLAPV 461
Cdd:COG1484    167 DEL-GYLPL 174
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
386-502 4.97e-04

Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and eukaryotic Heat shock protein 104 (Hsp104) are ATP-dependent molecular chaperones and essential proteins of the heat-shock response. ClpB/Hsp104 ATPases, in concert with the DnaK/Hsp70 chaperone system, disaggregate and reactivate aggregated proteins. This RecA-like_ClpB_Hsp104_like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 42.55  E-value: 4.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  386 LFYGPPGTGKTLVARALAnECSHGDRK------VSFFMRKGADCLSK-----WVGESERQlrLLFDQAYLMRPSIIFFDE 454
Cdd:cd19499     45 LFLGPTGVGKTELAKALA-ELLFGDEDnliridMSEYMEKHSVSRLIgappgYVGYTEGG--QLTEAVRRKPYSVVLLDE 121
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2004839052  455 IdglapvrsskqDQIHSSIVSTLLALMD-G--LDSRGEIVVIGAT--------------NRLDSI 502
Cdd:cd19499    122 I-----------EKAHPDVQNLLLQVLDdGrlTDSHGRTVDFKNTiiimtsnhfrpeflNRIDEI 175
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
385-461 8.12e-04

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 42.46  E-value: 8.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  385 CLFYGPPGTGKTLVARALANE-CSHGdRKVSFFmrKGADCLSKWvGESERQLRL--LFDQayLMRPSIIFFDEIdGLAPV 461
Cdd:NF038214    93 VLLLGPPGTGKTHLAIALGYAaCRQG-YRVRFT--TAADLVEQL-AQARADGRLgrLLRR--LARYDLLIIDEL-GYLPF 165
Bromo_SP100C_like cd05501
Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major ...
934-1003 1.02e-03

Bromodomain, SP100C_like subfamily. The SP100C protein is a splice variant of SP100, a major component of PML-SP100 nuclear bodies (NBs), which are poorly understood. It is covalently modified by SUMO-1 and may play a role in processes at the chromatin level. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99933  Cd Length: 102  Bit Score: 40.10  E-value: 1.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  934 FNIfSKPVDIEevsDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYNPDKDPGDKVIR 1003
Cdd:cd05501     22 FFI-SKPYYIR---DYCQGIKEPMWLNKVKERLNERVYHTVEGFVRDMRLIFHNHKLFYKDDDFGQVGIT 87
PRK08116 PRK08116
hypothetical protein; Validated
370-405 1.38e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 42.32  E-value: 1.38e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2004839052  370 YPEIFEKFKIQPpRGCLFYGPPGTGKTLVARALANE 405
Cdd:PRK08116   103 YVKKFEEMKKEN-VGLLLWGSVGTGKTYLAACIANE 137
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
1134-1224 1.43e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.04  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052 1134 DEESSCDITGPQPN---GHHPHAPSTEEESSNEPPVAAPDKPPDASEAREAPMPKVEEPAAKEAEP-EITGKHTEPHCLG 1209
Cdd:PRK13108   364 EETSEADIEREQPGdlaGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIPDPAKPdELAVAGPGDDPAE 443
                           90
                   ....*....|....*
gi 2004839052 1210 GSSQPNTDGDSEASR 1224
Cdd:PRK13108   444 PDGIRRQDDFSSRRR 458
PRK04195 PRK04195
replication factor C large subunit; Provisional
378-405 1.62e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 42.60  E-value: 1.62e-03
                           10        20
                   ....*....|....*....|....*...
gi 2004839052  378 KIQPPRGCLFYGPPGTGKTLVARALANE 405
Cdd:PRK04195    35 KGKPKKALLLYGPPGVGKTSLAHALAND 62
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
380-507 1.82e-03

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 42.53  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  380 QPPRGCLFYGPPGTGKTLVARA----LANECSHGDRKVSF-------------FMRKGADCLSKWVGESERQLRllFDQA 442
Cdd:COG1474     49 ERPSNVLIYGPTGTGKTAVAKYvleeLEEEAEERGVDVRVvyvncrqastryrVLSRILEELGSGEDIPSTGLS--TDEL 126
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2004839052  443 YLM---------RPSIIFFDEIDGLapvrsskQDQIHSSIVSTLLALMDGLDSRGeIVVIGATNRL---DSIDPALR 507
Cdd:COG1474    127 FDRlyealderdGVLVVVLDEIDYL-------VDDEGDDLLYQLLRANEELEGAR-VGVIGISNDLeflENLDPRVK 195
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
382-530 2.79e-03

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: 40.18  E-value: 2.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  382 PRGCLFYGPPGTGKTLVARALANecSHGDRKVSFFMRKGADCLSK---WVGESERQLRLLFDQAYLMRPSIIFFDEIDGL 458
Cdd:pfam13191   24 PPSVLLTGEAGTGKTTLLRELLR--ALERDGGYFLRGKCDENLPYsplLEALTREGLLRQLLDELESSLLEAWRAALLEA 101
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2004839052  459 APVRSSKQDQIHSSIVSTLLALMDGLDSRGEIVVIgATNRLDSIDPAlrrpgrfDREFLFSLPDKKARKHIL 530
Cdd:pfam13191  102 LAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL-VLDDLQWADEA-------SLQLLAALLRLLESLPLL 165
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
382-520 4.72e-03

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 40.28  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2004839052  382 PRGC--LFYGPPGTGKTLVARALANE-CSHGDrKVSFFMrkgadclskwVGESERQLR-----LLFD-QAYLMRPSIIFF 452
Cdd:COG0467     18 PRGSstLLSGPPGTGKTTLALQFLAEgLRRGE-KGLYVS----------FEESPEQLLrraesLGLDlEEYIESGLLRII 86
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2004839052  453 DeidglapVRSSKQDQIHSSIVSTLLALMDGLDSRgeIVVIgatnrlDSIDP---ALRRPGRFdREFLFSL 520
Cdd:COG0467     87 D-------LSPEELGLDLEELLARLREAVEEFGAK--RVVI------DSLSGlllALPDPERL-REFLHRL 141
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
932-992 5.08e-03

Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in transcriptional activation, it is the catalytic component of the SWI/SNF ATP-dependent chromatin remodeling complex. The protein is essential for the regulation of gene expression (both positive and negative) of a large number of genes. The SWI/SNF complex changes chromatin structure by altering DNA-histone contacts within the nucleosome, which results in a re-positioning of the nucleosome and facilitates or represses the binding of gene-specific transcription factors. Bromodomains are 110 amino acid long domains, that are found in many chromatin associated proteins. Bromodomains can interact specifically with acetylated lysine.


Pssm-ID: 99950  Cd Length: 103  Bit Score: 38.09  E-value: 5.08e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2004839052  932 KRFNIFSKPVDIEEVSDYLEVIRQPMDLSTVMTKIDTHQYLTAKDFLVDIDLICSNALEYN 992
Cdd:cd05519     22 KLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANARTYN 82
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
385-405 6.46e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.50  E-value: 6.46e-03
                           10        20
                   ....*....|....*....|.
gi 2004839052  385 CLFYGPPGTGKTLVARALANE 405
Cdd:PRK00080    54 VLLYGPPGLGKTTLANIIANE 74
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
386-410 7.47e-03

DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 40.17  E-value: 7.47e-03
                           10        20
                   ....*....|....*....|....*...
gi 2004839052  386 LFYGPPGTGKTLVARALA---NeCSHGD 410
Cdd:COG2812     36 LFTGPRGVGKTTLARILAkalN-CENGP 62
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
380-414 9.39e-03

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: 39.92  E-value: 9.39e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2004839052  380 QPPRGCLFYGPPGTGKTLVARALANE----CSHGDRKVS 414
Cdd:TIGR02928   38 SRPSNVFIYGKTGTGKTAVTKYVMKEleeaAEDRDVRVV 76
44 PHA02544
clamp loader, small subunit; Provisional
358-423 9.48e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 39.97  E-value: 9.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2004839052  358 QSLKEmVVFPLLYPEIFEKF--KIQPPRGCLFYGPPGTGKTLVARALANECShgdrkVSFFMRKGADC 423
Cdd:PHA02544    18 STIDE-CILPAADKETFKSIvkKGRIPNMLLHSPSPGTGKTTVAKALCNEVG-----AEVLFVNGSDC 79
 
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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