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Conserved domains on  [gi|18390588|ref|NP_563753|]
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cell division cycle protein 48-related / CDC48-like protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
382-551 5.48e-111

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd19517:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 170  Bit Score: 344.11  E-value: 5.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSFYMRKGADVLSKWV 461
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  462 GEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRR 541
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160
                        170
                 ....*....|
gi 18390588  542 PGRFDREFNF 551
Cdd:cd19517  161 PGRFDREFYF 170
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
258-617 1.40e-69

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: 239.04  E-value: 1.40e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  258 RRVLHQGMGTRVGRDGRRGGSRPHKRHRFTRTDDSDDSLLVDELDQGPAIPWARGGNRSGAPWLFGGLDTYGSSSLGLNV 337
Cdd:COG0464   35 AALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  338 GASGWGHQSDGLAALTSGVQTAGPSSKGGADIQPLQINEDInFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRG 417
Cdd:COG0464  115 ERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAI-LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRG 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  418 VLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSS 497
Cdd:COG0464  194 LLLYGPPGTGKTLLARALAGEL-----GLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGE 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  498 KQEQIHNSIVSTLLALMDGLdsRGQVVLIGATNRVDAIDGALRRpgRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRE 577
Cdd:COG0464  269 VGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVD 344
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 18390588  578 LkEELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTSD 617
Cdd:COG0464  345 L-EELAEATEGLSGADIRNVVRRAALQALRLGREPVTTED 383
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
895-1005 6.72e-55

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: 186.02  E-value: 6.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  895 LRRLRMCLRDVCNRILYDKRFSAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNG 974
Cdd:cd05528    1 LRELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNP 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 18390588  975 DDY-AGARIVSRAYELRDVVHGMLSQMDPALL 1005
Cdd:cd05528   81 DRDpADKLIRSRACELRDEVHAMIEAELDPLF 112
 
Name Accession Description Interval E-value
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
382-551 5.48e-111

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: 344.11  E-value: 5.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSFYMRKGADVLSKWV 461
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  462 GEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRR 541
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160
                        170
                 ....*....|
gi 18390588  542 PGRFDREFNF 551
Cdd:cd19517  161 PGRFDREFYF 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
356-623 9.01e-89

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 289.98  E-value: 9.01e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  356 VQTAGPSSKGGADIQPLQINE--DINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIAR 433
Cdd:COG1222   51 NDANLTQKRLGTPRGTAVPAEspDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  434 ALACAAskagqKVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRS-SKQEQIHNSIVSTLLA 512
Cdd:COG1222  131 AVAGEL-----GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTdDGTSGEVQRTVNQLLA 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  513 LMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGA 592
Cdd:COG1222  206 ELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDL-DKLAKLTEGFSGA 284
                        250       260       270
                 ....*....|....*....|....*....|.
gi 18390588  593 DLKALCTEAAIRAFREKYPQVYTSDDKYAID 623
Cdd:COG1222  285 DLKAIVTEAGMFAIREGRDTVTMEDLEKAIE 315
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
377-652 9.17e-72

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: 255.22  E-value: 9.17e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    377 DINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASkagqkVSFYMRKGADV 456
Cdd:TIGR01243  174 KVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAG-----AYFISINGPEI 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    457 LSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAID 536
Cdd:TIGR01243  249 MSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALD 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    537 GALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTS 616
Cdd:TIGR01243  329 PALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDL-DKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKIN 407
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 18390588    617 DDKYAIDVGLVN---VEKSHFVEAMSAITPAAHRGSVVQ 652
Cdd:TIGR01243  408 FEAEEIPAEVLKelkVTMKDFMEALKMVEPSAIREVLVE 446
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
258-617 1.40e-69

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: 239.04  E-value: 1.40e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  258 RRVLHQGMGTRVGRDGRRGGSRPHKRHRFTRTDDSDDSLLVDELDQGPAIPWARGGNRSGAPWLFGGLDTYGSSSLGLNV 337
Cdd:COG0464   35 AALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  338 GASGWGHQSDGLAALTSGVQTAGPSSKGGADIQPLQINEDInFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRG 417
Cdd:COG0464  115 ERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAI-LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRG 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  418 VLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSS 497
Cdd:COG0464  194 LLLYGPPGTGKTLLARALAGEL-----GLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGE 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  498 KQEQIHNSIVSTLLALMDGLdsRGQVVLIGATNRVDAIDGALRRpgRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRE 577
Cdd:COG0464  269 VGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVD 344
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 18390588  578 LkEELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTSD 617
Cdd:COG0464  345 L-EELAEATEGLSGADIRNVVRRAALQALRLGREPVTTED 383
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
377-623 2.55e-66

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 229.33  E-value: 2.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   377 DINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADV 456
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHET-----NATFIRVVGSEL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   457 LSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSskqeqihNSIVS----------TLLALMDGLDSRGQVVLI 526
Cdd:PRK03992  202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT-------DSGTSgdrevqrtlmQLLAEMDGFDPRGNVKII 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   527 GATNRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGADLKALCTEAAIRAF 606
Cdd:PRK03992  275 AATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDL-EELAELTEGASGADLKAICTEAGMFAI 353
                         250
                  ....*....|....*..
gi 18390588   607 REKYPQVYTSDDKYAID 623
Cdd:PRK03992  354 RDDRTEVTMEDFLKAIE 370
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
895-1005 6.72e-55

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: 186.02  E-value: 6.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  895 LRRLRMCLRDVCNRILYDKRFSAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNG 974
Cdd:cd05528    1 LRELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNP 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 18390588  975 DDY-AGARIVSRAYELRDVVHGMLSQMDPALL 1005
Cdd:cd05528   81 DRDpADKLIRSRACELRDEVHAMIEAELDPLF 112
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
418-553 1.50e-43

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: 154.29  E-value: 1.50e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    418 VLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSS 497
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKEL-----GAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18390588    498 KQEQIHNSIVSTLLALMDGLDSR-GQVVLIGATNRVDAIDGALRrpGRFDREFNFSL 553
Cdd:pfam00004   76 GGDSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
414-554 5.52e-20

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: 87.81  E-value: 5.52e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588     414 PPRGVLLCGPPGTGKTLIARALACAASKAGQKV------------SFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPS 481
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390588     482 IIFFDEIDGLAPVRSSKQEQihnsiVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPgRFDREFNFSLP 554
Cdd:smart00382   81 VLILDEITSLLDAEQEALLL-----LLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
BROMO smart00297
bromo domain;
895-993 2.63e-14

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 70.00  E-value: 2.63e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588     895 LRRLRMCLRDvcnrilyDKRFSAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNG 974
Cdd:smart00297   12 LKAVLDKLDS-------HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNG 84
                            90
                    ....*....|....*....
gi 18390588     975 DDyagARIVSRAYELRDVV 993
Cdd:smart00297   85 PD---SEVYKDAKKLEKFF 100
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
917-976 5.92e-10

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: 56.94  E-value: 5.92e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    917 AFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD 976
Cdd:pfam00439   16 PFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPG 75
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
822-977 1.81e-09

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 60.97  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  822 FDNRSVYTVDKPSSEDRSLFFDRLIEAALSVISGLNG-----KPDGPQPLPELPKVPKEPTGPKPAEVKAKVE-AEQHAL 895
Cdd:COG5076   75 NVNDDLENVGGITYSPFEKNRPESLRFDEIVFLAIESvtpesGLGSLLMAHLKTSVKKRKTPKIEDELLYADNkAIAKFK 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  896 RRLrmclrdvcNRILYDKRFSAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGD 975
Cdd:COG5076  155 KQL--------FLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGP 226

                 ..
gi 18390588  976 DY 977
Cdd:COG5076  227 DS 228
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
580-617 5.93e-09

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 52.93  E-value: 5.93e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 18390588    580 EELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTSD 617
Cdd:pfam17862    5 EELAERTEGFSGADLEALCREAALAALRRGLEAVTQED 42
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
376-494 8.50e-06

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: 48.24  E-value: 8.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   376 EDINFDDIGGLSEY-INDLKEMVFfpllypeffasysITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSFYmrKGA 454
Cdd:NF038214   63 EDFDFTAAPGLDKAqIRELATLDF-------------IERAENVLLLGPPGTGKTHLAIALGYAACRQGYRVRFT--TAA 127
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 18390588   455 DVLSKWvGEAERQLKLLFEEAQRNQPSIIFFDEIdGLAPV 494
Cdd:NF038214  128 DLVEQL-AQARADGRLGRLLRRLARYDLLIIDEL-GYLPF 165
 
Name Accession Description Interval E-value
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
382-551 5.48e-111

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: 344.11  E-value: 5.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSFYMRKGADVLSKWV 461
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  462 GEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRR 541
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160
                        170
                 ....*....|
gi 18390588  542 PGRFDREFNF 551
Cdd:cd19517  161 PGRFDREFYF 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
356-623 9.01e-89

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 289.98  E-value: 9.01e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  356 VQTAGPSSKGGADIQPLQINE--DINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIAR 433
Cdd:COG1222   51 NDANLTQKRLGTPRGTAVPAEspDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  434 ALACAAskagqKVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRS-SKQEQIHNSIVSTLLA 512
Cdd:COG1222  131 AVAGEL-----GAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTdDGTSGEVQRTVNQLLA 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  513 LMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGA 592
Cdd:COG1222  206 ELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDL-DKLAKLTEGFSGA 284
                        250       260       270
                 ....*....|....*....|....*....|.
gi 18390588  593 DLKALCTEAAIRAFREKYPQVYTSDDKYAID 623
Cdd:COG1222  285 DLKAIVTEAGMFAIREGRDTVTMEDLEKAIE 315
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
382-551 3.61e-78

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: 254.14  E-value: 3.61e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSKWV 461
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEA-----GANFLSISGPSIVSKYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  462 GEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRR 541
Cdd:cd19503   76 GESEKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRR 155
                        170
                 ....*....|
gi 18390588  542 PGRFDREFNF 551
Cdd:cd19503  156 PGRFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
377-652 9.17e-72

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: 255.22  E-value: 9.17e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    377 DINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASkagqkVSFYMRKGADV 456
Cdd:TIGR01243  174 KVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAG-----AYFISINGPEI 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    457 LSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAID 536
Cdd:TIGR01243  249 MSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALD 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    537 GALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTS 616
Cdd:TIGR01243  329 PALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDL-DKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKIN 407
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 18390588    617 DDKYAIDVGLVN---VEKSHFVEAMSAITPAAHRGSVVQ 652
Cdd:TIGR01243  408 FEAEEIPAEVLKelkVTMKDFMEALKMVEPSAIREVLVE 446
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
258-617 1.40e-69

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: 239.04  E-value: 1.40e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  258 RRVLHQGMGTRVGRDGRRGGSRPHKRHRFTRTDDSDDSLLVDELDQGPAIPWARGGNRSGAPWLFGGLDTYGSSSLGLNV 337
Cdd:COG0464   35 AALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAALLSALELLLLGELLLLLLLLLLLLLLLLDL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  338 GASGWGHQSDGLAALTSGVQTAGPSSKGGADIQPLQINEDInFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRG 417
Cdd:COG0464  115 ERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAI-LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRG 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  418 VLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSS 497
Cdd:COG0464  194 LLLYGPPGTGKTLLARALAGEL-----GLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGE 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  498 KQEQIHNSIVSTLLALMDGLdsRGQVVLIGATNRVDAIDGALRRpgRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRE 577
Cdd:COG0464  269 VGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVD 344
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 18390588  578 LkEELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTSD 617
Cdd:COG0464  345 L-EELAEATEGLSGADIRNVVRRAALQALRLGREPVTTED 383
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
377-623 2.55e-66

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 229.33  E-value: 2.55e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   377 DINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADV 456
Cdd:PRK03992  127 NVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHET-----NATFIRVVGSEL 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   457 LSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSskqeqihNSIVS----------TLLALMDGLDSRGQVVLI 526
Cdd:PRK03992  202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRT-------DSGTSgdrevqrtlmQLLAEMDGFDPRGNVKII 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   527 GATNRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGADLKALCTEAAIRAF 606
Cdd:PRK03992  275 AATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDL-EELAELTEGASGADLKAICTEAGMFAI 353
                         250
                  ....*....|....*..
gi 18390588   607 REKYPQVYTSDDKYAID 623
Cdd:PRK03992  354 RDDRTEVTMEDFLKAIE 370
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
368-644 2.10e-65

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: 236.34  E-value: 2.10e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    368 DIQPLQINE------DINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASk 441
Cdd:TIGR01243  434 MVEPSAIREvlvevpNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESG- 512
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    442 agqkVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVR-SSKQEQIHNSIVSTLLALMDGLDSR 520
Cdd:TIGR01243  513 ----ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARgARFDTSVTDRIVNQLLTEMDGIQEL 588
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    521 GQVVLIGATNRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGADLKALCTE 600
Cdd:TIGR01243  589 SNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDL-EELAEMTEGYTGADIEAVCRE 667
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 18390588    601 AAIRAFREkypqVYTSDDKYAIDVGL------VNVEKSHFVEAMSAITPA 644
Cdd:TIGR01243  668 AAMAALRE----SIGSPAKEKLEVGEeeflkdLKVEMRHFLEALKKVKPS 713
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
377-623 2.96e-62

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: 216.97  E-value: 2.96e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    377 DINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADV 456
Cdd:TIGR01242  118 NVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHET-----NATFIRVVGSEL 192
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    457 LSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVR----SSKQEQIHNSIVStLLALMDGLDSRGQVVLIGATNRV 532
Cdd:TIGR01242  193 VRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRtdsgTSGDREVQRTLMQ-LLAELDGFDPRGNVKVIAATNRP 271
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    533 DAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGADLKALCTEAAIRAFREKYPQ 612
Cdd:TIGR01242  272 DILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDL-EAIAKMTEGASGADLKAICTEAGMFAIREERDY 350
                          250
                   ....*....|.
gi 18390588    613 VYTSDDKYAID 623
Cdd:TIGR01242  351 VTMDDFIKAVE 361
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
382-548 3.15e-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: 209.21  E-value: 3.15e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASkagqkVSFYMRKGADVLSKWV 461
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETG-----AFFFLINGPEIMSKLA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  462 GEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRR 541
Cdd:cd19519   76 GESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRR 155

                 ....*..
gi 18390588  542 PGRFDRE 548
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 ...
393-547 2.64e-55

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: 189.03  E-value: 2.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  393 LKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSKWVGEAERQLKLLF 472
Cdd:cd19511    5 LKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEA-----GLNFISVKGPELFSKYVGESERAVREIF 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390588  473 EEAQRNQPSIIFFDEIDGLAPVRS-SKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFDR 547
Cdd:cd19511   80 QKARQAAPCIIFFDEIDSLAPRRGqSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDK 155
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
895-1005 6.72e-55

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: 186.02  E-value: 6.72e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  895 LRRLRMCLRDVCNRILYDKRFSAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNG 974
Cdd:cd05528    1 LRELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNP 80
                         90       100       110
                 ....*....|....*....|....*....|..
gi 18390588  975 DDY-AGARIVSRAYELRDVVHGMLSQMDPALL 1005
Cdd:cd05528   81 DRDpADKLIRSRACELRDEVHAMIEAELDPLF 112
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
378-631 2.16e-54

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: 198.28  E-value: 2.16e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    378 INFDDIGGLSEYINDLKEMVFFpLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVL 457
Cdd:TIGR01241   52 VTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEA-----GVPFFSISGSDFV 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    458 SKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVR-------SSKQEQIHNSivstLLALMDGLDSRGQVVLIGATN 530
Cdd:TIGR01241  126 EMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglgggNDEREQTLNQ----LLVEMDGFGTNTGVIVIAATN 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    531 RVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELKeELAATCVGYCGADLKALCTEAAIRAFREKY 610
Cdd:TIGR01241  202 RPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLK-AVARRTPGFSGADLANLLNEAALLAARKNK 280
                          250       260
                   ....*....|....*....|.
gi 18390588    611 PQVYTSDDKYAIDVGLVNVEK 631
Cdd:TIGR01241  281 TEITMNDIEEAIDRVIAGPEK 301
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
380-617 2.23e-52

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 190.75  E-value: 2.23e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   380 FDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASkagqkVSFYMRKGADVLSK 459
Cdd:PTZ00361  182 YADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETS-----ATFLRVVGSELIQK 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   460 WVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLAL---MDGLDSRGQVVLIGATNRVDAID 536
Cdd:PTZ00361  257 YLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTMLELlnqLDGFDSRGDVKVIMATNRIESLD 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   537 GALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTS 616
Cdd:PTZ00361  337 PALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDL-EEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQA 415

                  .
gi 18390588   617 D 617
Cdd:PTZ00361  416 D 416
ftsH CHL00176
cell division protein; Validated
364-623 2.79e-51

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 192.57  E-value: 2.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   364 KGGADIQpLQINEDINFDDIGGLSEYINDLKEMVFFpLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASkag 443
Cdd:CHL00176  167 KSKARFQ-MEADTGITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAE--- 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   444 qkVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSS-------KQEQIHNSivstLLALMDG 516
Cdd:CHL00176  242 --VPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgigggndEREQTLNQ----LLTEMDG 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   517 LDSRGQVVLIGATNRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWK-HPPTreLKEELAATCVGYCGADLK 595
Cdd:CHL00176  316 FKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKlSPDV--SLELIARRTPGFSGADLA 393
                         250       260
                  ....*....|....*....|....*...
gi 18390588   596 ALCTEAAIRAFREKYPQVYTSDDKYAID 623
Cdd:CHL00176  394 NLLNEAAILTARRKKATITMKEIDTAID 421
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
380-551 1.12e-49

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: 173.68  E-value: 1.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  380 FDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSfymrkGADVLSK 459
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVV-----GSELVQK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  460 WVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLAL---MDGLDSRGQVVLIGATNRVDAID 536
Cdd:cd19502   77 YIGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELlnqLDGFDPRGNIKVIMATNRPDILD 156
                        170
                 ....*....|....*
gi 18390588  537 GALRRPGRFDREFNF 551
Cdd:cd19502  157 PALLRPGRFDRKIEF 171
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
382-548 1.54e-49

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: 172.97  E-value: 1.54e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALacaaskAGQ-KVSFYMRKGADVLSKW 460
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAI------AGElKVPFLKISATEIVSGV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  461 VGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGL----DSRGQVVLIGATNRVDAID 536
Cdd:cd19518   75 SGESEEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLD 154
                        170
                 ....*....|..
gi 18390588  537 GALRRPGRFDRE 548
Cdd:cd19518  155 PALRRAGRFDRE 166
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
391-547 1.82e-49

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: 172.68  E-value: 1.82e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  391 NDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSKWVGEAERQLKL 470
Cdd:cd19529    3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATES-----NANFISVKGPELLSKWVGESEKAIRE 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390588  471 LFEEAQRNQPSIIFFDEIDGLAPVR-SSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFDR 547
Cdd:cd19529   78 IFRKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDR 155
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
380-623 6.01e-49

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 174.30  E-value: 6.01e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  380 FDDIGGLSEYINDLKEMVFFpLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSK 459
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKE-LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGEL-----KLPLLTVRLDSLIGS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  460 WVGEAERQLKLLFEEAqRNQPSIIFFDEIDGLAPVRSSKQE--QIHNsIVSTLLALMDGLDSrgQVVLIGATNRVDAIDG 537
Cdd:COG1223   75 YLGETARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQNDvgEVKR-VVNALLQELDGLPS--GSVVIAATNHPELLDS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  538 ALRRpgRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELKeELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTSD 617
Cdd:COG1223  151 ALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLK-KLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKED 227

                 ....*.
gi 18390588  618 DKYAID 623
Cdd:COG1223  228 LEEALK 233
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
378-623 4.45e-47

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 178.69  E-value: 4.45e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  378 INFDDIGGLSEYINDLKEMVFFpLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVL 457
Cdd:COG0465  139 VTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEA-----GVPFFSISGSDFV 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  458 SKWVG-EAERqLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQ-------EQIHNSivstLLALMDGLDSRGQVVLIGAT 529
Cdd:COG0465  213 EMFVGvGASR-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLggghderEQTLNQ----LLVEMDGFEGNEGVIVIAAT 287
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  530 NRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGADLKALCTEAAIRAFREK 609
Cdd:COG0465  288 NRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDL-EVIARRTPGFSGADLANLVNEAALLAARRN 366
                        250
                 ....*....|....
gi 18390588  610 YPQVYTSDDKYAID 623
Cdd:COG0465  367 KKAVTMEDFEEAID 380
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
378-548 2.10e-46

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: 164.33  E-value: 2.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  378 INFDDIGGLSEYINDLKEMVFFpLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVL 457
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEA-----GVPFFSISGSDFV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  458 SKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSK-------QEQIHNSivstLLALMDGLDSRGQVVLIGATN 530
Cdd:cd19501   75 EMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGlggghdeREQTLNQ----LLVEMDGFESNTGVIVIAATN 150
                        170
                 ....*....|....*...
gi 18390588  531 RVDAIDGALRRPGRFDRE 548
Cdd:cd19501  151 RPDVLDPALLRPGRFDRQ 168
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
392-551 3.90e-46

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: 162.84  E-value: 3.90e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  392 DLKEMVFFPLLYPEFFAsYSITPPRGVLLCGPPGTGKTLIARALAcaaSKAGqkVSFYMRKGADVLSKWVGEAERQLKLL 471
Cdd:cd19481    4 SLREAVEAPRRGSRLRR-YGLGLPKGILLYGPPGTGKTLLAKALA---GELG--LPLIVVKLSSLLSKYVGESEKNLRKI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  472 FEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIH-NSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFDREFN 550
Cdd:cd19481   78 FERARRLAPCILFIDEIDAIGRKRDSSGESGElRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                 .
gi 18390588  551 F 551
Cdd:cd19481  158 F 158
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
418-553 1.50e-43

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: 154.29  E-value: 1.50e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    418 VLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSS 497
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKEL-----GAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGS 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 18390588    498 KQEQIHNSIVSTLLALMDGLDSR-GQVVLIGATNRVDAIDGALRrpGRFDREFNFSL 553
Cdd:pfam00004   76 GGDSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
386-547 2.49e-43

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: 154.95  E-value: 2.49e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  386 LSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARAlacAASKAGqkVSFYMRKGADVLSKWVGEAE 465
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKA---VANESG--ANFISVKGPELLNKYVGESE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  466 RQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPGRF 545
Cdd:cd19530   76 RAVRQVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRL 155

                 ..
gi 18390588  546 DR 547
Cdd:cd19530  156 DK 157
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
367-607 4.97e-43

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 162.24  E-value: 4.97e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   367 ADIQPLQINE--DINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALAcaaskAGQ 444
Cdd:PTZ00454  129 SSIQLLQMSEkpDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVA-----HHT 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   445 KVSFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLAL---MDGLDSRG 521
Cdd:PTZ00454  204 TATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADREVQRILLELlnqMDGFDQTT 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   522 QVVLIGATNRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRELkEELAATCVGYCGADLKALCTEA 601
Cdd:PTZ00454  284 NVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDL-EDFVSRPEKISAADIAAICQEA 362

                  ....*.
gi 18390588   602 AIRAFR 607
Cdd:PTZ00454  363 GMQAVR 368
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
383-549 1.87e-42

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: 152.51  E-value: 1.87e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  383 IGGLSEYINDLKEMVFFPLLYPEFFaSYSITPPRGVLLCGPPGTGKTLIARALACAASkagqkVSFYMRKGADVLSKWVG 462
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESG-----STFFSISASSLVSKWVG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  463 EAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGL--DSRGQVVLIGATNRVDAIDGALR 540
Cdd:cd19509   75 ESEKIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFL 154

                 ....*....
gi 18390588  541 RpgRFDREF 549
Cdd:cd19509  155 R--RFEKRI 161
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
392-547 8.98e-42

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: 150.74  E-value: 8.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  392 DLKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALA--CAAskagqkvSFYMRKGADVLSKWVGEAERQLK 469
Cdd:cd19528    4 ELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIAneCQA-------NFISVKGPELLTMWFGESEANVR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  470 LLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNS---IVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFD 546
Cdd:cd19528   77 DIFDKARAAAPCVLFFDELDSIAKARGGNIGDAGGAadrVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLD 156

                 .
gi 18390588  547 R 547
Cdd:cd19528  157 Q 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
382-545 1.77e-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: 141.41  E-value: 1.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFASYSIT-PPRGVLLCGPPGTGKTLIARALACAASkagqkVSFYMRKGADVLSKW 460
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLLqPPKGVLLYGPPGCGKTMLAKATAKEAG-----ARFINLQVSSLTDKW 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  461 VGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRG--QVVLIGATNRVDAIDGA 538
Cdd:cd19520   76 YGESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGncRVIVMGATNRPQDLDEA 155

                 ....*....
gi 18390588  539 LRR--PGRF 545
Cdd:cd19520  156 ILRrmPKRF 164
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
393-547 9.99e-37

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: 136.02  E-value: 9.99e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  393 LKEMVFFPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASkagqkVSFYMRKGADVLSKWVGEAERQLKLLF 472
Cdd:cd19526    5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECG-----LNFISVKGPELLNKYIGASEQNVRDLF 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390588  473 EEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFDR 547
Cdd:cd19526   80 SRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDK 154
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
379-607 1.36e-36

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 147.87  E-value: 1.36e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   379 NFDDIGGLSEYINDLKEMVFFpLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLS 458
Cdd:PRK10733  150 TFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEA-----KVPFFTISGSDFVE 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   459 KWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTL---LALMDGLDSRGQVVLIGATNRVDAI 535
Cdd:PRK10733  224 MFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLnqmLVEMDGFEGNEGIIVIAATNRPDVL 303
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390588   536 DGALRRPGRFDREFNFSLPGCEARAEILDIHTRKWKHPPTRElKEELAATCVGYCGADLKALCTEAAIRAFR 607
Cdd:PRK10733  304 DPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDID-AAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
392-547 4.71e-36

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: 134.18  E-value: 4.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  392 DLKEMVFFPLLYPEFFASySITPPRGVLLCGPPGTGKTLIARALACAASkagqkVSFYMRKGADVLSKWVGEAERQLKLL 471
Cdd:cd19527    4 EILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECS-----LNFLSVKGPELINMYIGESEANVREV 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390588  472 FEEAQRNQPSIIFFDEIDGLAPVRSSKQEQ--IHNSIVSTLLALMDGLDSRGQ-VVLIGATNRVDAIDGALRRPGRFDR 547
Cdd:cd19527   78 FQKARDAKPCVIFFDELDSLAPSRGNSGDSggVMDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
377-547 2.75e-35

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: 132.29  E-value: 2.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  377 DINFDDIGGLSEYINDLKEMVFFPLLYPEFFaSYSITPPRGVLLCGPPGTGKTLIARALACAASKagqkvSFYMRKGADV 456
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLF-TGNRKPWSGILLYGPPGTGKSYLAKAVATEANS-----TFFSVSSSDL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  457 LSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGL--DSRGQVVLiGATNRVDA 534
Cdd:cd19521   77 VSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgnDSQGVLVL-GATNIPWQ 155
                        170
                 ....*....|...
gi 18390588  535 IDGALRRpgRFDR 547
Cdd:cd19521  156 LDSAIRR--RFEK 166
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
372-541 3.21e-35

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: 132.80  E-value: 3.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  372 LQINEDINFDDIGGLSEYINDLKEMVFFPLLYPEFFASYSiTPPRGVLLCGPPGTGKTLIARalaCAASKAGqkVSFYMR 451
Cdd:cd19525   13 MDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGK---CIASQSG--ATFFSI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  452 KGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLD--SRGQVVLIGAT 529
Cdd:cd19525   87 SASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATtsSEDRILVVGAT 166
                        170
                 ....*....|..
gi 18390588  530 NRVDAIDGALRR 541
Cdd:cd19525  167 NRPQEIDEAARR 178
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
383-546 3.23e-33

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: 126.84  E-value: 3.23e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  383 IGGLSEYINDLKEMVF----FPllyPEFFASYSITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSfymrKGADVLS 458
Cdd:cd19504    2 IGGLDKEFSDIFRRAFasrvFP---PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIV----NGPEILN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  459 KWVGEAERQLKLLFEEAQRNQPS--------IIFFDEIDGLAPVRSSKQEQ--IHNSIVSTLLALMDGLDSRGQVVLIGA 528
Cdd:cd19504   75 KYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQRGSMAGStgVHDTVVNQLLSKIDGVEQLNNILVIGM 154
                        170
                 ....*....|....*...
gi 18390588  529 TNRVDAIDGALRRPGRFD 546
Cdd:cd19504  155 TNRKDLIDEALLRPGRLE 172
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
382-541 1.25e-31

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: 122.02  E-value: 1.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFASYSiTPPRGVLLCGPPGTGKTLIARALACAAskagqKVSFYMRKGADVLSKWV 461
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATEC-----GTTFFNVSSSTLTSKYR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  462 GEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQE-QIHNSIVSTLLALMDGL-------DSRGQVVLIGATNRVD 533
Cdd:cd19522   75 GESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEhEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPW 154

                 ....*...
gi 18390588  534 AIDGALRR 541
Cdd:cd19522  155 DIDEALRR 162
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
382-541 2.27e-30

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: 118.03  E-value: 2.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFASYSiTPPRGVLLCGPPGTGKTLIARALAcaaskAGQKVSFYMRKGADVLSKWV 461
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVA-----AESNATFFNISAASLTSKYV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  462 GEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIHNSIVSTLLALMDGLDSRG--QVVLIGATNRVDAID-GA 538
Cdd:cd19524   75 GEGEKLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGddRVLVMGATNRPQELDdAV 154

                 ...
gi 18390588  539 LRR 541
Cdd:cd19524  155 LRR 157
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
382-549 1.30e-28

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: 113.06  E-value: 1.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLSEYINDLKEMVFFPLLYPEFFaSYSITPPRGVLLCGPPGTGKTLIARalaCAASKAGqkVSFYMRKGADVLSKWV 461
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAF-SGLLRLPRSILLFGPRGTGKTLLGR---CLASQLG--ATFLRLRGSTLVAKWA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  462 GEAERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEQIhNSIVSTLLALMDGLDSRG--QVVLIGATNRVDAIDGAL 539
Cdd:cd19523   75 GEGEKILQASFLAARCRQPSVLFISDLDALLSSQDDEASPV-GRLQVELLAQLDGVLGSGedGVLVVCTTSKPEEIDESL 153
                        170
                 ....*....|
gi 18390588  540 RRpgRFDREF 549
Cdd:cd19523  154 RR--YFSKRL 161
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
414-553 4.76e-27

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: 108.00  E-value: 4.76e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  414 PPRGVLLCGPPGTGKTLIARALACAASKAGqkVSFYMRKGADVLSKWVGEAERQ---LKLLFEEAQRNQPSIIFFDEIDG 490
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIANELFRPG--APFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPGVLFIDEIDS 95
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390588  491 LAPvrsskqeQIHNSIVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFDREFNFSL 553
Cdd:cd00009   96 LSR-------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
414-554 5.52e-20

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: 87.81  E-value: 5.52e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588     414 PPRGVLLCGPPGTGKTLIARALACAASKAGQKV------------SFYMRKGADVLSKWVGEAERQLKLLFEEAQRNQPS 481
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD 80
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390588     482 IIFFDEIDGLAPVRSSKQEQihnsiVSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPgRFDREFNFSLP 554
Cdd:smart00382   81 VLILDEITSLLDAEQEALLL-----LLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLI 147
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
902-993 1.55e-19

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: 84.73  E-value: 1.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  902 LRDVCNRIL------YDKRFSAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGD 975
Cdd:cd04369    1 LKKKLRSLLdalkklKRDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYNGP 80
                         90
                 ....*....|....*...
gi 18390588  976 DyagARIVSRAYELRDVV 993
Cdd:cd04369   81 G---SPIYKDAKKLEKLF 95
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
382-549 7.07e-15

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: 73.56  E-value: 7.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  382 DIGGLseyiNDLKEMVFF--PLLYPEFFAsYSITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSFymrkgADVLSK 459
Cdd:cd19507    1 DVGGL----DNLKDWLKKrkAAFSKQASA-YGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDM-----GRLFGG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  460 WVGEAERQLKLLFEEAQRNQPSIIFFDEID-GLAPVRSSKQEQIHNSIVSTLLALMdglDSRGQVVLIGAT-NRVDAIDG 537
Cdd:cd19507   71 LVGESESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWL---QEKKKPVFVVATaNNVQSLPP 147
                        170
                 ....*....|..
gi 18390588  538 ALRRPGRFDREF 549
Cdd:cd19507  148 ELLRKGRFDEIF 159
ycf46 CHL00195
Ycf46; Provisional
369-618 9.78e-15

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 78.52  E-value: 9.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   369 IQPLQINE----DINFDDIGGLSEYINDLKEMvffPLLYPEFFASYSITPPRGVLLCGPPGTGKTLIARALAcaaskagq 444
Cdd:CHL00195  212 ISQTEILEfysvNEKISDIGGLDNLKDWLKKR---STSFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIA-------- 280
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   445 kvsfymrkgadvlSKW----------------VGEAERQLKLLFEEAQRNQPSIIFFDEID-GLAPVRSSKQEQIHNSIV 507
Cdd:CHL00195  281 -------------NDWqlpllrldvgklfggiVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVL 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   508 STLLALMDglDSRGQVVLIGATNRVDAIDGALRRPGRFDREFNFSLPGCEARAEILDIHTRK-----WKHPPTrelkEEL 582
Cdd:CHL00195  348 ATFITWLS--EKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKfrpksWKKYDI----KKL 421
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 18390588   583 AATCVGYCGADLKALCTEAAIRAFREKypQVYTSDD 618
Cdd:CHL00195  422 SKLSNKFSGAEIEQSIIEAMYIAFYEK--REFTTDD 455
BROMO smart00297
bromo domain;
895-993 2.63e-14

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 70.00  E-value: 2.63e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588     895 LRRLRMCLRDvcnrilyDKRFSAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNG 974
Cdd:smart00297   12 LKAVLDKLDS-------HPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNARTYNG 84
                            90
                    ....*....|....*....
gi 18390588     975 DDyagARIVSRAYELRDVV 993
Cdd:smart00297   85 PD---SEVYKDAKKLEKFF 100
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
921-976 6.69e-13

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: 65.65  E-value: 6.69e-13
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18390588  921 PVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD 976
Cdd:cd05509   25 PVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGPD 80
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
917-989 4.32e-12

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: 63.82  E-value: 4.32e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390588  917 AFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDDY----AGARIVSRAYEL 989
Cdd:cd05511   20 PFHTPVNKKKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYNGPDSvytkKAKEMLELAEEL 96
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
412-539 8.00e-12

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: 65.55  E-value: 8.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  412 ITPPRGVLLCGPPGTGKTLIARALacaASKAGQKVSFYMRKG-------ADVLSKWVGEAERQLKLLFEEAQR--NQPSI 482
Cdd:cd19508   49 ITWNRLVLLHGPPGTGKTSLCKAL---AQKLSIRLSSRYRYGqlieinsHSLFSKWFSESGKLVTKMFQKIQEliDDKDA 125
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18390588  483 IFF---DEIDGLAPVRSSKQEQIHNS----IVSTLLALMDGLDSRGQVVLIGATNRVDAIDGAL 539
Cdd:cd19508  126 LVFvliDEVESLAAARSASSSGTEPSdairVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
918-973 9.59e-12

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: 62.43  E-value: 9.59e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18390588  918 FHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYN 973
Cdd:cd05513   22 FAFPVTDFIAPGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYN 77
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
917-976 5.92e-10

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: 56.94  E-value: 5.92e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    917 AFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD 976
Cdd:pfam00439   16 PFLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNGPG 75
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
908-976 1.50e-09

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: 56.60  E-value: 1.50e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  908 RILYDKRF-SAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD 976
Cdd:cd05507   13 RTLASHRYaSVFLKPVTEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNSSD 82
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
917-975 1.60e-09

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: 56.68  E-value: 1.60e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18390588  917 AFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGD 975
Cdd:cd05510   28 PFLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYNSD 86
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
822-977 1.81e-09

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 60.97  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  822 FDNRSVYTVDKPSSEDRSLFFDRLIEAALSVISGLNG-----KPDGPQPLPELPKVPKEPTGPKPAEVKAKVE-AEQHAL 895
Cdd:COG5076   75 NVNDDLENVGGITYSPFEKNRPESLRFDEIVFLAIESvtpesGLGSLLMAHLKTSVKKRKTPKIEDELLYADNkAIAKFK 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  896 RRLrmclrdvcNRILYDKRFSAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGD 975
Cdd:COG5076  155 KQL--------FLRDGRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYNGP 226

                 ..
gi 18390588  976 DY 977
Cdd:COG5076  227 DS 228
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
918-976 3.54e-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: 55.07  E-value: 3.54e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18390588  918 FHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD 976
Cdd:cd05503   21 FLEPVNTKLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDD 79
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
416-547 4.24e-09

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: 56.59  E-value: 4.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  416 RGVLLCGPPGTGKTLIARALACaaskagqkvsfYMRKGADVLS-KWVGEAERQLKLLFEEAQrnQPSIIFFDEID----- 489
Cdd:cd19510   24 RGYLLYGPPGTGKSSFIAALAG-----------ELDYDICDLNlSEVVLTDDRLNHLLNTAP--KQSIILLEDIDaafes 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18390588  490 GLAPVRSSKQEQIHNSI-VSTLLALMDGLDSRGQVVLIGATNRVDAIDGALRRPGRFDR 547
Cdd:cd19510   91 REHNKKNPSAYGGLSRVtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
906-975 5.37e-09

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: 54.60  E-value: 5.37e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390588  906 CNRILYD---KRFSAFHFPV---TDEDA---PNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGD 975
Cdd:cd05499    5 CEEVLKElmkPKHSAYNWPFldpVDPVAlniPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPE 83
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
906-982 5.42e-09

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: 54.99  E-value: 5.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  906 CNRI---LYDKRFSA-FHFPVTdEDAPNYRSIIQIPMDTATL---LQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDDYA 978
Cdd:cd05502    9 CERLlleLYCHELSLpFHEPVS-PSVPNYYKIIKTPMDLSLIrkkLQPKSPQHYSSPEEFVADVRLMFKNCYKFNEEDSE 87

                 ....
gi 18390588  979 GARI 982
Cdd:cd05502   88 VAQA 91
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
580-617 5.93e-09

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 52.93  E-value: 5.93e-09
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 18390588    580 EELAATCVGYCGADLKALCTEAAIRAFREKYPQVYTSD 617
Cdd:pfam17862    5 EELAERTEGFSGADLEALCREAALAALRRGLEAVTQED 42
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
918-976 8.02e-09

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: 54.33  E-value: 8.02e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18390588  918 FHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD 976
Cdd:cd05512   22 FSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYNAKD 80
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
918-973 8.88e-09

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: 54.77  E-value: 8.88e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 18390588  918 FHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYN 973
Cdd:cd05496   26 FRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYT 81
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
416-568 4.87e-08

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: 57.16  E-value: 4.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    416 RGVLLCGPPGTGKTLIARALACAASKAG--QKVSFYMRKGADVLSKWVGEAERQLKLLFEEAqrnQPSIIFFDEIDGLAP 493
Cdd:TIGR03922  313 NHMLFAGPPGTGKTTIARVVAKIYCGLGvlRKPLVREVSRADLIGQYIGESEAKTNEIIDSA---LGGVLFLDEAYTLVE 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    494 VRSSKQEQIHNSIVSTLLALMDglDSRGQVVLIGA--TNRVDA---IDGALRRpgRFDREFNFSlpgCEARAEILDIHTR 568
Cdd:TIGR03922  390 TGYGQKDPFGLEAIDTLLARME--NDRDRLVVIGAgyRKDLDKfleVNEGLRS--RFTRVIEFP---SYSPDELVEIARR 462
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
918-986 1.21e-07

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: 51.24  E-value: 1.21e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390588  918 FHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDDYAGARIVSRA 986
Cdd:cd05504   33 FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHTSVYKAGTRL 101
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
914-973 1.69e-07

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: 50.23  E-value: 1.69e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18390588  914 RFS-AFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYN 973
Cdd:cd05505   16 RFSwPFREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYY 76
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
417-545 3.71e-07

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 50.37  E-value: 3.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    417 GVLLCGPPGTGKTLIARALACAASkagQKVSFYM--RKG---ADVLSKW---VGEAERQLKLLFEEAQRnqPSIIFFDEI 488
Cdd:pfam07728    1 GVLLVGPPGTGKTELAERLAAALS---NRPVFYVqlTRDtteEDLFGRRnidPGGASWVDGPLVRAARE--GEIAVLDEI 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390588    489 DglapvrsskqeQIHNSIVSTLLALMD----GLDSRGQVV--------LIGATNRVDA----IDGALRRpgRF 545
Cdd:pfam07728   76 N-----------RANPDVLNSLLSLLDerrlLLPDGGELVkaapdgfrLIATMNPLDRglneLSPALRS--RF 135
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
416-551 4.70e-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: 50.60  E-value: 4.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  416 RGVLLCGPPGTGKTLIARALacaASKAGqkVSFYMRKGADVlSKWVGEAERQLKLLFEEAQRNQPSIIFF-DEIDGLAPV 494
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKL---ALHSG--MDYAIMTGGDV-APMGREGVTAIHKVFDWANTSRRGLLLFvDEADAFLRK 96
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18390588  495 RSSkqEQIHNSIVSTLLALM--DGLDSRgQVVLIGATNRVDAIDGALRrpGRFDREFNF 551
Cdd:cd19512   97 RST--EKISEDLRAALNAFLyrTGEQSN-KFMLVLASNQPEQFDWAIN--DRIDEMVEF 150
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
916-976 6.67e-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: 48.53  E-value: 6.67e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18390588  916 SAFHFPVTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD 976
Cdd:cd05508   21 EPFLKPVDLEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIYNGGD 81
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
418-549 8.79e-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: 50.27  E-value: 8.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    418 VLLCGPPGTGKTLIARALACAASKAGQKV-----SFYMRKgaDVLSKWVGEAER-----QLKLLFEEAQRNQPSIIFFDE 487
Cdd:pfam07724    6 FLFLGPTGVGKTELAKALAELLFGDERALiridmSEYMEE--HSVSRLIGAPPGyvgyeEGGQLTEAVRRKPYSIVLIDE 83
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390588    488 IdglapvrsskqEQIHNSIVSTLLALMDG---LDSRGQVV------LIGATNR-VDAIDGALRRPGRFDREF 549
Cdd:pfam07724   84 I-----------EKAHPGVQNDLLQILEGgtlTDKQGRTVdfkntlFIMTGNFgSEKISDASRLGDSPDYEL 144
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
376-449 1.89e-06

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 50.55  E-value: 1.89e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390588  376 EDINFDDIGGLSE-YINDLKEMVFfpllypeffasysITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSFY 449
Cdd:COG1484   72 EDFDFDAQPGLDRrQILELATLDF-------------IERGENLILLGPPGTGKTHLAIALGHEACRAGYRVRFT 133
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
890-976 2.64e-06

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: 47.31  E-value: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  890 AEQH--ALRRLRMCLRdvcnriLYDKRFsaFHFPVTDE--DAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLI 965
Cdd:cd05500    3 KHQHkfLLSSIRSLKR------LKDARP--FLVPVDPVklNIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLM 74
                         90
                 ....*....|.
gi 18390588  966 VRNAKAYNGDD 976
Cdd:cd05500   75 VDNCLTFNGPE 85
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
906-992 4.13e-06

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: 46.50  E-value: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  906 CNRIL---YDKRFSAFHFPVTDE-DA-----PNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYN--G 974
Cdd:cd05498    5 CSGILkelFSKKHKAYAWPFYKPvDPealglHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNppD 84
                         90
                 ....*....|....*...
gi 18390588  975 DDyagarIVSRAYELRDV 992
Cdd:cd05498   85 HP-----VHAMARKLQDV 97
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
918-1000 5.17e-06

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: 46.26  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  918 FHFPVtdeDA-----PNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYN--GDDyagarIVSRAYELR 990
Cdd:cd05497   26 FQQPV---DAvklnlPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNkpGDD-----VVLMAQTLE 97
                         90
                 ....*....|
gi 18390588  991 DVVHGMLSQM 1000
Cdd:cd05497   98 KLFLQKLAQM 107
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
376-494 8.50e-06

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: 48.24  E-value: 8.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   376 EDINFDDIGGLSEY-INDLKEMVFfpllypeffasysITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSFYmrKGA 454
Cdd:NF038214   63 EDFDFTAAPGLDKAqIRELATLDF-------------IERAENVLLLGPPGTGKTHLAIALGYAACRQGYRVRFT--TAA 127
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 18390588   455 DVLSKWvGEAERQLKLLFEEAQRNQPSIIFFDEIdGLAPV 494
Cdd:NF038214  128 DLVEQL-AQARADGRLGRLLRRLARYDLLIIDEL-GYLPF 165
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
907-990 8.98e-06

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: 45.40  E-value: 8.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  907 NRILYDKRFSAFHFPVtDEDA---PNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYN--GDD-YAGA 980
Cdd:cd05506   10 RKLMKHKWGWVFNAPV-DVVAlglPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNppGNDvHTMA 88
                         90
                 ....*....|
gi 18390588  981 RIVSRAYELR 990
Cdd:cd05506   89 KELLKIFETR 98
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
414-551 1.15e-05

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: 46.99  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  414 PPRGVLLCGPPGTGKTLIARALAC---------AASKA-GQKVSFYMRKGADVLSKWvGEAERQLKLLFEEAQRNQPSII 483
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAAnsyvpliriSLNKLlYNKPDFGNDDWIDGMLIL-KESLHRLNLQFELAKAMSPCII 89
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18390588  484 FFDEIDGLApVRSSKQEQIHNSivSTLLALMDGLDSRG-------QVVLIGATNRVDAIDGALRRPGRFDREFNF 551
Cdd:cd19505   90 WIPNIHELN-VNRSTQNLEEDP--KLLLGLLLNYLSRDfeksstrNILVIASTHIPQKVDPALIAPNRLDTCINI 161
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
418-529 1.38e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 48.93  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   418 VLLCGPPGTGKTLIARALACAASKAGQKVSfymrkgAdVLSKwVGEaerqLKLLFEEAQRN----QPSIIFFDEIDglap 493
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALS------A-VTSG-VKD----LREVIEEARQRrsagRRTILFIDEIH---- 102
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 18390588   494 vRSSKQEQihnsivSTLLALMDgldsRGQVVLIGAT 529
Cdd:PRK13342  103 -RFNKAQQ------DALLPHVE----DGTITLIGAT 127
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
415-535 2.84e-05

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: 46.02  E-value: 2.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  415 PRGVLL-CGPPGTGKTLIARALACAASKAGQKV-----SFYMRKGAdvLSKWVGEA-----ERQLKLLFEEAQRNQPSII 483
Cdd:cd19499   40 PIGSFLfLGPTGVGKTELAKALAELLFGDEDNLiridmSEYMEKHS--VSRLIGAPpgyvgYTEGGQLTEAVRRKPYSVV 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18390588  484 FFDEIDGLAPVrsskqeqIHNSIvstLLALMDG--LDSRGQVVLIGAT--------------NRVDAI 535
Cdd:cd19499  118 LLDEIEKAHPD-------VQNLL---LQVLDDGrlTDSHGRTVDFKNTiiimtsnhfrpeflNRIDEI 175
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
411-493 3.32e-05

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 45.31  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  411 SITPPRG--VLLCGPPGTGKTLIARALACAASKAGQKVSFymrKGADVLSKWVGEAERQLKLLFE----EAQR------- 477
Cdd:cd00267   19 SLTLKAGeiVALVGPNGSGKSTLLRAIAGLLKPTSGEILI---DGKDIAKLPLEELRRRIGYVPQlsggQRQRvalaral 95
                         90
                 ....*....|....*...
gi 18390588  478 -NQPSIIFFDEID-GLAP 493
Cdd:cd00267   96 lLNPDLLLLDEPTsGLDP 113
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
418-529 3.46e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 47.74  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  418 VLLCGPPGTGKTLIARALACAASKAGQKVSfymrkgAdVLSKwVGEaerqLKLLFEEAQRN----QPSIIFFDEIDglap 493
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALS------A-VTSG-VKD----IREVIEEARERraygRRTILFVDEIH---- 115
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 18390588  494 vRSSKQEQihnsivSTLLALMDgldsRGQVVLIGAT 529
Cdd:COG2256  116 -RFNKAQQ------DALLPHVE----DGTITLIGAT 140
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
923-973 4.04e-05

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: 43.96  E-value: 4.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18390588  923 TDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYN 973
Cdd:cd05516   33 SRKELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFN 83
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
925-973 1.07e-04

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: 42.68  E-value: 1.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 18390588  925 EDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYN 973
Cdd:cd05515   34 SEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYN 82
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
418-493 1.19e-04

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 45.13  E-value: 1.19e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18390588    418 VLLCGPPGTGKTLIARALACAASKAGQKVSFYmrkGADVLSKWVGEAERQLKLLFEEAQRNQPSIIFFDEIdGLAP 493
Cdd:pfam01695   95 VVLLGPPGVGKTHLAIALGVEACRAGYSVRFT---SAADLVNQLKRAHGDGKLTRKLQQLLKPDVLILDEW-GYLP 166
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
416-578 1.24e-04

TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and archaeal RuvB-like 1 (Pontin or TIP49a) and RuvB-like 2 (Reptin or TIP49b) proteins. The N-terminal domain contains the pfam00004 domain. In zebrafish, the liebeskummer (lik) mutation, causes development of hyperplastic embryonic hearts. lik encodes Reptin, a component of a DNA-stimulated ATPase complex. Beta-catenin and Pontin, a DNA-stimulated ATPase that is often part of complexes with Reptin, are in the same genetic pathways. The Reptin/Pontin ratio serves to regulate heart growth during development, at least in part via the beta-catenin pathway. TBP-interacting protein 49 (TIP49) was originally identified as a TBP-binding protein, and two related proteins are encoded by individual genes, tip49a and b. Although the function of this gene family has not been elucidated, they are supposed to play a critical role in nuclear events because they interact with various kinds of nuclear factors and have DNA helicase activities.TIP49a has been suggested to act as an autoantigen in some patients with autoimmune diseases.


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.76  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    416 RGVLLCGPPGTGKTliarALACAASKA-GQKVSFYMRKGADVLSKWVGEAE--------------RQLKLLFE------- 473
Cdd:pfam06068   51 RAVLIAGPPGTGKT----ALAIAISKElGEDTPFTSISGSEVYSLEMKKTEaltqafrkaigvriKEEKEVYEgevvele 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    474 --EAQR--NQPSIIFFDEIdGLAPVRSSKQEQIHNSIVSTLLAlmdgldsrgQVVLIGATNRVDAIDGALRRPGRfdref 549
Cdd:pfam06068  127 ieEAENplSGGKTIKGGKI-TLKTTKMEKTLKLGPKIYEQLQK---------EKVSAGDVIYIDKNTGRVKKLGR----- 191
                          170       180
                   ....*....|....*....|....*....
gi 18390588    550 nfslpgCEARAEILDIHTRKWKHPPTREL 578
Cdd:pfam06068  192 ------SFARATDFDLEATEFVPCPKGEV 214
PRK04195 PRK04195
replication factor C large subunit; Provisional
414-491 1.77e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 45.68  E-value: 1.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   414 PPRGVLLCGPPGTGKTLIARALA---------CAASKagqkvsfymRKGADVLSKWVGEAERQlKLLFEEAQRnqpsIIF 484
Cdd:PRK04195   38 PKKALLLYGPPGVGKTSLAHALAndygwevieLNASD---------QRTADVIERVAGEAATS-GSLFGARRK----LIL 103

                  ....*..
gi 18390588   485 FDEIDGL 491
Cdd:PRK04195  104 LDEVDGI 110
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
918-987 1.92e-04

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: 42.05  E-value: 1.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18390588  918 FHFPVtDEDA---PNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNgddyagaRIVSRAY 987
Cdd:cd05495   25 FRQPV-DPKLlgiPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYN-------RKTSRVY 89
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
418-492 2.73e-04

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 44.76  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   418 VLLCGPPGTGKTLIARALAcaaskagqK---VSFYMrkgADVLS----KWVGE-AERQL-KLLF------EEAQRnqpSI 482
Cdd:PRK05342  111 ILLIGPTGSGKTLLAQTLA--------RildVPFAI---ADATTlteaGYVGEdVENILlKLLQaadydvEKAQR---GI 176
                          90
                  ....*....|
gi 18390588   483 IFFDEIDGLA 492
Cdd:PRK05342  177 VYIDEIDKIA 186
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
900-973 3.42e-04

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: 41.27  E-value: 3.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18390588  900 MCLRDVCNRI---LYDKRFSAFHFPvtdedapNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYN 973
Cdd:cd05517   13 MTATDPSGRLiseLFQKLPSKVLYP-------DYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFN 82
PRK06526 PRK06526
transposase; Provisional
339-488 4.12e-04

transposase; Provisional


Pssm-ID: 180607  Cd Length: 254  Bit Score: 43.70  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   339 ASGWGHQSDGLAALTSgvQTAGPSSKGG------ADIQPLQINEDINFDDIGGLS-EYINDLKEMVFfpllypeffasys 411
Cdd:PRK06526   30 AESWSHEEFLAACLQR--EVAARESHGGegriraARFPARKSLEEFDFDHQRSLKrDTIAHLGTLDF------------- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   412 ITPPRGVLLCGPPGTGKTLIARALACAASKAGQKVSFymrkgaDVLSKWV---GEAERQLKLLFEEAQRNQPSIIFFDEI 488
Cdd:PRK06526   95 VTGKENVVFLGPPGTGKTHLAIGLGIRACQAGHRVLF------ATAAQWVarlAAAHHAGRLQAELVKLGRYPLLIVDEV 168
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
897-992 9.63e-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: 40.07  E-value: 9.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  897 RLRMCLRDVCNRILYDKRFS----AFHF---PvTDEDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNA 969
Cdd:cd05525    2 RLAQVLKEICDAIITYKDSNgqslAIPFinlP-SKKKNPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNA 80
                         90       100
                 ....*....|....*....|...
gi 18390588  970 KAYNGDDYAGARIVSRayeLRDV 992
Cdd:cd05525   81 EKYYGRKSPIGRDVCR---LRKA 100
clpC CHL00095
Clp protease ATP binding subunit
419-524 1.09e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 43.12  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588   419 LLCGPPGTGKTLIARALA-----CAASKAGQKVSFYMRKgaDVLSK-------WVGEAER-QLKllfeEAQRNQP-SIIF 484
Cdd:CHL00095  543 LFSGPTGVGKTELTKALAsyffgSEDAMIRLDMSEYMEK--HTVSKligsppgYVGYNEGgQLT----EAVRKKPyTVVL 616
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 18390588   485 FDEIdglapvrsskqEQIHNSIVSTLLALM-DG--LDSRGQVV 524
Cdd:CHL00095  617 FDEI-----------EKAHPDIFNLLLQILdDGrlTDSKGRTI 648
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
925-976 1.12e-03

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: 39.53  E-value: 1.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 18390588  925 EDAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD 976
Cdd:cd05522   35 AREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYNEND 86
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
926-991 1.15e-03

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: 39.74  E-value: 1.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18390588  926 DAPNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD---YAGARIVSRAyeLRD 991
Cdd:cd05518   35 DYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYNEEGsqvYEDANILEKV--LKE 101
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
415-526 1.26e-03

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 41.82  E-value: 1.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  415 PRG--VLLCGPPGTGKTLIARALACAASKAGQK---VSF--------------------YMRKGA----DVLSK-WVGEA 464
Cdd:COG0467   18 PRGssTLLSGPPGTGKTTLALQFLAEGLRRGEKglyVSFeespeqllrraeslgldleeYIESGLlriiDLSPEeLGLDL 97
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18390588  465 ERQLKLLFEEAQRNQPSIIFFDEIDGLAPVRSSKQEqihnsIVSTLLALMDGLDSRGQVVLI 526
Cdd:COG0467   98 EELLARLREAVEEFGAKRVVIDSLSGLLLALPDPER-----LREFLHRLLRYLKKRGVTTLL 154
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
418-492 1.31e-03

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain 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: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 41.82  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  418 VLLCGPPGTGKTLIARALAcaaskAGQKVSFYMrkgADVLS----KWVGE-AERQLKLLFEEA----QRNQPSIIFFDEI 488
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLA-----KILDVPFAI---ADATTlteaGYVGEdVENILLKLLQAAdydvERAQRGIVYIDEI 124

                 ....
gi 18390588  489 DGLA 492
Cdd:cd19497  125 DKIA 128
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
418-521 1.42e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.


Pssm-ID: 459992  Cd Length: 102  Bit Score: 39.12  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588    418 VLLCGPPGTGKTLIARALACAASKA--GQKVSFYMR-KGADVLSKWVGeaerqlkllfeeaqrnQPSIIFFDeidgLAPV 494
Cdd:pfam00910    1 IWLYGPPGCGKSTLAKYLARALLKKlgLPKDSVYSRnPDDDFWDGYTG----------------QPVVIIDD----FGQN 60
                           90       100
                   ....*....|....*....|....*....
gi 18390588    495 RSSKQEQIHNSIVST--LLALMDGLDSRG 521
Cdd:pfam00910   61 PDGPDEAELIRLVSStpYPPPMAALEEKG 89
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
928-976 2.50e-03

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: 38.85  E-value: 2.50e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 18390588  928 PNYRSIIQIPMDTATLLQRVDTGQYLTCTPFLQDVDLIVRNAKAYNGDD 976
Cdd:cd05524   39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAYYKPD 87
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
419-438 3.82e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 40.95  E-value: 3.82e-03
                         10        20
                 ....*....|....*....|
gi 18390588  419 LLCGPPGTGKTLIARALACA 438
Cdd:COG2812   36 LFTGPRGVGKTTLARILAKA 55
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
416-436 4.64e-03

DNA helicase TIP49, TBP-interacting protein [Transcription];


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.11  E-value: 4.64e-03
                         10        20
                 ....*....|....*....|.
gi 18390588  416 RGVLLCGPPGTGKTLIARALA 436
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIA 85
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
418-436 5.75e-03

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 40.15  E-value: 5.75e-03
                         10
                 ....*....|....*....
gi 18390588  418 VLLCGPPGTGKTLIARALA 436
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALA 52
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
343-438 9.55e-03

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.14  E-value: 9.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18390588  343 GHQSDGLAALTSGVQTAGPSSKGGADIQPLQINEDINFDDIGGLSEYINDLKEMVFfPLLYPEFFASysITPPRGVLLCG 422
Cdd:COG1401  152 TEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLREKF-EETLEAFLAA--LKTKKNVILAG 228
                         90
                 ....*....|....*.
gi 18390588  423 PPGTGKTLIARALACA 438
Cdd:COG1401  229 PPGTGKTYLARRLAEA 244
 
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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