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Conserved domains on  [gi|91199557|ref|NP_081711|]
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ATPase family AAA domain-containing protein 2 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 406-575 3.42e-113

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


:

Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 352.20  E-value: 3.42e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  406 SVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSRGDKRVAFFMRKGADCLSKWV 485
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  486 GESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRR 565
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                        170
                 ....*....|
gi 91199557  566 PGRFDREFLF 575
Cdd:cd19517  161 PGRFDREFYF 170
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 960-1070 6.39e-56

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: 189.11  E-value: 6.39e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  960 RELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPD 1039
Cdd:cd05528    2 RELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNPD 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 91199557 1040 RDPGDRLIRHRACALRDTAYAIIKEELDEDF 1070
Cdd:cd05528   82 RDPADKLIRSRACELRDEVHAMIEAELDPLF 112
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 603-637 1.56e-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: 54.47  E-value: 1.56e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 91199557    603 LEELAEHCVGYCGADIKSICAEAALCALRRRYPQI 637
Cdd:pfam17862    4 LEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
ycf46 super family cl31783
Ycf46; Provisional
 766-907 1.02e-04

Ycf46; Provisional


The actual alignment was detected with superfamily member CHL00195:

Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 46.55  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   766 PR-LLIVGEPGFGQSshLAPAVIHALEKFTVYTLDIPVLFGISTTSPEEACSQMIREAKRTAPSIvyvphihLWW-EI-- 841
Cdd:CHL00195  259 PRgLLLVGIQGTGKS--LTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCI-------LWIdEIdk 329

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91199557   842 ----------VGPTLK--ATFTTLLQTIPSfaPVLLLATSEKPYSaLPEEVqeLFTHDYGEIFNVQLPDKEERTKFFE 907
Cdd:CHL00195  330 afsnseskgdSGTTNRvlATFITWLSEKKS--PVFVVATANNIDL-LPLEI--LRKGRFDEIFFLDLPSLEEREKIFK 402
 
Name Accession Description Interval E-value
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 406-575 3.42e-113

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 352.20  E-value: 3.42e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  406 SVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSRGDKRVAFFMRKGADCLSKWV 485
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  486 GESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRR 565
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                        170
                 ....*....|
gi 91199557  566 PGRFDREFLF 575
Cdd:cd19517  161 PGRFDREFYF 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 401-672 1.13e-94

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 307.70  E-value: 1.13e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  401 SVRFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADC 480
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELG-----APFIRVRGSEL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  481 LSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQD-QIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSI 559
Cdd:COG1222  149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTsGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLL 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  560 DPALRRPGRFDREFLFSLPDKNARKEILKIHTRDwNPKPVDMFLEELAEHCVGYCGADIKSICAEAALCALRRRYPqiyt 639
Cdd:COG1222  229 DPALLRPGRFDRVIEVPLPDEEAREEILKIHLRD-MPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRD---- 303

                        250       260       270
                 ....*....|....*....|....*....|...
gi 91199557  640 tseklqldlssiTISAKDFEAALQKIRPASQRA 672
Cdd:COG1222  304 ------------TVTMEDLEKAIEKVKKKTETA 324
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 361-668 9.38e-78

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: 273.32  E-value: 9.38e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    361 RAINRCLP---LNFRKDEIRGIYKDRMKIGA-----SLADVDPMQLDT------SVRFDSVGGLSSHIAALKEMVVFPLL 426
Cdd:TIGR01243  395 AALRRFIRegkINFEAEEIPAEVLKELKVTMkdfmeALKMVEPSAIREvlvevpNVRWSDIGGLEEVKQELREAVEWPLK 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    427 YPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPAI 506
Cdd:TIGR01243  475 HPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESG-----ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAI 549

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    507 IFFDEIDGLAPVRSSRQDQ-IHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKE 585
Cdd:TIGR01243  550 IFFDEIDAIAPARGARFDTsVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKE 629

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    586 ILKIHTRDWnPKPVDMFLEELAEHCVGYCGADIKSICAEAALCALRRRYPQIytTSEKLQLDLSSIT----ISAKDFEAA 661
Cdd:TIGR01243  630 IFKIHTRSM-PLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSP--AKEKLEVGEEEFLkdlkVEMRHFLEA 706


                   ....*..
gi 91199557    662 LQKIRPA 668
Cdd:TIGR01243  707 LKKVKPS 713
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 396-666 9.34e-72

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 245.51  E-value: 9.34e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   396 MQLDTS--VRFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrvAFF 473
Cdd:PRK03992  120 MEVIESpnVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETN------ATF 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   474 MR-KGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLApvrSSRQDQIHS---SIVST---LLALMDGLDSRGE 546
Cdd:PRK03992  194 IRvVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIA---AKRTDSGTSgdrEVQRTlmqLLAEMDGFDPRGN 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   547 IVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDWNPKP-VDmfLEELAEHCVGYCGADIKSICAEA 625
Cdd:PRK03992  271 VKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADdVD--LEELAELTEGASGADLKAICTEA 348

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 91199557   626 ALCALRRRYPQiyttseklqldlssitISAKDFEAALQKIR 666
Cdd:PRK03992  349 GMFAIRDDRTE----------------VTMEDFLKAIEKVM 373
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 960-1070 6.39e-56

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: 189.11  E-value: 6.39e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  960 RELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPD 1039
Cdd:cd05528    2 RELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNPD 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 91199557 1040 RDPGDRLIRHRACALRDTAYAIIKEELDEDF 1070
Cdd:cd05528   82 RDPADKLIRSRACELRDEVHAMIEAELDPLF 112
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 443-577 8.92e-48

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 166.61  E-value: 8.92e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    443 LFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSR 522
Cdd:pfam00004    2 LLYGPPGTGKTTLAKAVAKELG-----APFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557    523 QDQIHSSIVSTLLALMDGLDSR-GEIVVIGATNRLDSIDPALRrpGRFDREFLFSL 577
Cdd:pfam00004   77 GDSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 438-579 5.03e-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: 88.20  E-value: 5.03e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557     438 PPRGCLFYGPPGTGKTLVARALANECSRGDKRVAFF------------MRKGADCLSKWVGESERQLRLLFDQAYQMRPA 505
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIdgedileevldqLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91199557     506 IIFFDEIDGLAPVRSSRQDQihssiVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPgRFDREFLFSLPD 579
Cdd:smart00382   81 VLILDEITSLLDAEQEALLL-----LLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
BROMO smart00297
bromo domain;
955-1065 2.90e-17

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 78.47  E-value: 2.90e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557     955 EEDTFRELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNAL 1034
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNAR 80

                            90       100       110
                    ....*....|....*....|....*....|.
gi 91199557    1035 EYNPDrdpgDRLIRHRACALRDTAYAIIKEE 1065
Cdd:smart00297   81 TYNGP----DSEVYKDAKKLEKFFEKKLREL 107
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 982-1038 6.66e-15

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


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 71.19  E-value: 6.66e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 91199557    982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNP 1038
Cdd:pfam00439   17 FLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 603-637 1.56e-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: 54.47  E-value: 1.56e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 91199557    603 LEELAEHCVGYCGADIKSICAEAALCALRRRYPQI 637
Cdd:pfam17862    4 LEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 975-1085 2.98e-08

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 57.51  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  975 IDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNpdrDPGDRLIRHRacal 1054
Cdd:COG5076  162 GRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYN---GPDSSVYVDA---- 234

                         90       100       110
                 ....*....|....*....|....*....|.
gi 91199557 1055 rdtayAIIKEELDEDFEQLCEEIQESRKKRG 1085
Cdd:COG5076  235 -----KELEKYFLKLIEEIPEEMLELSIKPG 260
ycf46 CHL00195
Ycf46; Provisional
 766-907 1.02e-04

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 46.55  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   766 PR-LLIVGEPGFGQSshLAPAVIHALEKFTVYTLDIPVLFGISTTSPEEACSQMIREAKRTAPSIvyvphihLWW-EI-- 841
Cdd:CHL00195  259 PRgLLLVGIQGTGKS--LTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCI-------LWIdEIdk 329

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91199557   842 ----------VGPTLK--ATFTTLLQTIPSfaPVLLLATSEKPYSaLPEEVqeLFTHDYGEIFNVQLPDKEERTKFFE 907
Cdd:CHL00195  330 afsnseskgdSGTTNRvlATFITWLSEKKS--PVFVVATANNIDL-LPLEI--LRKGRFDEIFFLDLPSLEEREKIFK 402
 
Name Accession Description Interval E-value
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 406-575 3.42e-113

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 352.20  E-value: 3.42e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  406 SVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSRGDKRVAFFMRKGADCLSKWV 485
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSFFMRKGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  486 GESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRR 565
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                        170
                 ....*....|
gi 91199557  566 PGRFDREFLF 575
Cdd:cd19517  161 PGRFDREFYF 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 401-672 1.13e-94

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 307.70  E-value: 1.13e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  401 SVRFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADC 480
Cdd:COG1222   74 DVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELG-----APFIRVRGSEL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  481 LSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQD-QIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSI 559
Cdd:COG1222  149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTsGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLL 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  560 DPALRRPGRFDREFLFSLPDKNARKEILKIHTRDwNPKPVDMFLEELAEHCVGYCGADIKSICAEAALCALRRRYPqiyt 639
Cdd:COG1222  229 DPALLRPGRFDRVIEVPLPDEEAREEILKIHLRD-MPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRD---- 303

                        250       260       270
                 ....*....|....*....|....*....|...
gi 91199557  640 tseklqldlssiTISAKDFEAALQKIRPASQRA 672
Cdd:COG1222  304 ------------TVTMEDLEKAIEKVKKKTETA 324
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 406-575 3.98e-80

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: 260.30  E-value: 3.98e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  406 SVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWV 485
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAG-----ANFLSISGPSIVSKYL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  486 GESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRR 565
Cdd:cd19503   76 GESEKNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRR 155

                        170
                 ....*....|
gi 91199557  566 PGRFDREFLF 575
Cdd:cd19503  156 PGRFDREVEI 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 361-668 9.38e-78

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: 273.32  E-value: 9.38e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    361 RAINRCLP---LNFRKDEIRGIYKDRMKIGA-----SLADVDPMQLDT------SVRFDSVGGLSSHIAALKEMVVFPLL 426
Cdd:TIGR01243  395 AALRRFIRegkINFEAEEIPAEVLKELKVTMkdfmeALKMVEPSAIREvlvevpNVRWSDIGGLEEVKQELREAVEWPLK 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    427 YPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPAI 506
Cdd:TIGR01243  475 HPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESG-----ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAI 549

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    507 IFFDEIDGLAPVRSSRQDQ-IHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKE 585
Cdd:TIGR01243  550 IFFDEIDAIAPARGARFDTsVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKE 629

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    586 ILKIHTRDWnPKPVDMFLEELAEHCVGYCGADIKSICAEAALCALRRRYPQIytTSEKLQLDLSSIT----ISAKDFEAA 661
Cdd:TIGR01243  630 IFKIHTRSM-PLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSP--AKEKLEVGEEEFLkdlkVEMRHFLEA 706


                   ....*..
gi 91199557    662 LQKIRPA 668
Cdd:TIGR01243  707 LKKVKPS 713
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 402-673 9.75e-78

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: 273.32  E-value: 9.75e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    402 VRFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCL 481
Cdd:TIGR01243  175 VTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAG-----AYFISINGPEIM 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    482 SKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDP 561
Cdd:TIGR01243  250 SKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDP 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    562 ALRRPGRFDREFLFSLPDKNARKEILKIHTRDwNPKPVDMFLEELAEHCVGYCGADIKSICAEAALCALRRRYPQIYTTS 641
Cdd:TIGR01243  330 ALRRPGRFDREIVIRVPDKRARKEILKVHTRN-MPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRFIREGKINF 408

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 91199557    642 EKLQLD---LSSITISAKDFEAALQKIRPASQRAV 673
Cdd:TIGR01243  409 EAEEIPaevLKELKVTMKDFMEALKMVEPSAIREV 443
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 393-671 2.19e-76

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: 259.07  E-value: 2.19e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  393 VDPMQLDTSVRFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECsrgdkRVAF 472
Cdd:COG0464  145 EEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGEL-----GLPL 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  473 FMRKGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLdsRGEIVVIGA 552
Cdd:COG0464  220 IEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAA 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  553 TNRLDSIDPALRRpgRFDREFLFSLPDKNARKEILKIHTRDwNPKPVDMFLEELAEHCVGYCGADIKSICAEAALCALRr 632
Cdd:COG0464  298 TNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRK-RPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALR- 373

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 91199557  633 rypqiyttseklqldLSSITISAKDFEAALQKIRPASQR 671
Cdd:COG0464  374 ---------------LGREPVTTEDLLEALEREDIFLKR 397
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 396-666 9.34e-72

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 245.51  E-value: 9.34e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   396 MQLDTS--VRFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrvAFF 473
Cdd:PRK03992  120 MEVIESpnVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETN------ATF 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   474 MR-KGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLApvrSSRQDQIHS---SIVST---LLALMDGLDSRGE 546
Cdd:PRK03992  194 IRvVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIA---AKRTDSGTSgdrEVQRTlmqLLAEMDGFDPRGN 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   547 IVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDWNPKP-VDmfLEELAEHCVGYCGADIKSICAEA 625
Cdd:PRK03992  271 VKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADdVD--LEELAELTEGASGADLKAICTEA 348

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 91199557   626 ALCALRRRYPQiyttseklqldlssitISAKDFEAALQKIR 666
Cdd:PRK03992  349 GMFAIRDDRTE----------------VTMEDFLKAIEKVM 373
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
 402-633 4.44e-64

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 222.37  E-value: 4.44e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    402 VRFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrvAFFMR-KGADC 480
Cdd:TIGR01242  119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETN------ATFIRvVGSEL 192

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    481 LSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVR---SSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLD 557
Cdd:TIGR01242  193 VRKYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPD 272

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557    558 SIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDWNPKPvDMFLEELAEHCVGYCGADIKSICAEAALCALRRR 633
Cdd:TIGR01242  273 ILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAE-DVDLEAIAKMTEGASGADLKAICTEAGMFAIREE 347
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 407-572 1.07e-62

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 210.76  E-value: 1.07e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  407 VGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVG 486
Cdd:cd19519    2 IGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETG-----AFFFLINGPEIMSKLAG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  487 ESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRP 566
Cdd:cd19519   77 ESESNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRF 156


                 ....*.
gi 91199557  567 GRFDRE 572
Cdd:cd19519  157 GRFDRE 162
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 416-571 1.24e-61

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 207.52  E-value: 1.24e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  416 ALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECsrgdkRVAFFMRKGADCLSKWVGESERQLRLL 495
Cdd:cd19511    4 ELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEA-----GLNFISVKGPELFSKYVGESERAVREI 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91199557  496 FDQAYQMRPAIIFFDEIDGLAPVRSSRQD-QIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 571
Cdd:cd19511   79 FQKARQAAPCIIFFDEIDSLAPRRGQSDSsGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDK 155
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 369-637 5.15e-57

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 204.62  E-value: 5.15e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   369 LNFRKDEIRGIYKDRMKIGASLADVDPMQLDTsvrFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPP 448
Cdd:PTZ00361  150 LHNKTHSVVGILLDEVDPLVSVMKVDKAPLES---YADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPP 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   449 GTGKTLVARALANECSrgdkrvAFFMR-KGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIH 527
Cdd:PTZ00361  227 GTGKTLLAKAVANETS------ATFLRvVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGE 300

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   528 SSIVSTLLAL---MDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDWNPKPvDMFLE 604
Cdd:PTZ00361  301 KEIQRTMLELlnqLDGFDSRGDVKVIMATNRIESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAE-DVDLE 379

                         250       260       270
                  ....*....|....*....|....*....|...
gi 91199557   605 ELAEHCVGYCGADIKSICAEAALCALRRRYPQI 637
Cdd:PTZ00361  380 EFIMAKDELSGADIKAICTEAGLLALRERRMKV 412
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 417-571 5.54e-57

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: 194.25  E-value: 5.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  417 LKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANEcsrgdKRVAFFMRKGADCLSKWVGESERQLRLLF 496
Cdd:cd19529    5 LKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATE-----SNANFISVKGPELLSKWVGESEKAIREIF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557  497 DQAYQMRPAIIFFDEIDGLAPVRSSRQDQ-IHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 571
Cdd:cd19529   80 RKARQVAPCVIFFDEIDSIAPRRGTTGDSgVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDR 155
Bromo_AAA cd05528
Bromodomain; sub-family co-occurring with AAA domains. Bromodomains are 110 amino acid long ...
 960-1070 6.39e-56

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: 189.11  E-value: 6.39e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  960 RELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPD 1039
Cdd:cd05528    2 RELRLFLRDVLKRLASDKRFNAFTKPVDEEEVPDYYEIIKQPMDLQTILQKLDTHQYLTAKDFLKDIDLIVTNALEYNPD 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 91199557 1040 RDPGDRLIRHRACALRDTAYAIIKEELDEDF 1070
Cdd:cd05528   82 RDPADKLIRSRACELRDEVHAMIEAELDPLF 112
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 384-665 1.91e-55

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: 201.75  E-value: 1.91e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    384 MKIGASLADVDpMQLDTSVRFDSVGGLSSHIAALKEMVVFpLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANEC 463
Cdd:TIGR01241   35 FSFGKSKAKLL-NEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    464 SrgdkrVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGlapVRSSRQDQI---HSSIVSTL---LAL 537
Cdd:TIGR01241  113 G-----VPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDA---VGRQRGAGLgggNDEREQTLnqlLVE 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    538 MDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDWNPKPvDMFLEELAEHCVGYCGAD 617
Cdd:TIGR01241  185 MDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAP-DVDLKAVARRTPGFSGAD 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 91199557    618 IKSICAEAALCALRRRYPqiyttseklqldlssiTISAKDFEAALQKI 665
Cdd:TIGR01241  264 LANLLNEAALLAARKNKT----------------EITMNDIEEAIDRV 295
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 402-642 2.21e-52

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 193.00  E-value: 2.21e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    402 VRFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANE-CSR----GDKRVAFFMRK 476
Cdd:TIGR03689  179 VTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlAARigaeGGGKSYFLNIK 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    477 GADCLSKWVGESERQLRLLFDQAYQM----RPAIIFFDEIDGLAPVRSS-RQDQIHSSIVSTLLALMDGLDSRGEIVVIG 551
Cdd:TIGR03689  259 GPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRGSgVSSDVETTVVPQLLAEIDGVESLDNVIVIG 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    552 ATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDWNPKPvdmflEELAEHcvgycgadikSICAEAALCALR 631
Cdd:TIGR03689  339 ASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLTDDLPLP-----EDLAAH----------DGDREATAAALI 403

                          250
                   ....*....|..
gi 91199557    632 RR-YPQIYTTSE 642
Cdd:TIGR03689  404 QRvVDALYARSE 415
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 404-571 3.08e-52

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: 181.00  E-value: 3.08e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  404 FDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrvAFFMR-KGADCLS 482
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTD------ATFIRvVGSELVQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  483 KWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLAL---MDGLDSRGEIVVIGATNRLDSI 559
Cdd:cd19502   76 KYIGEGARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTMLELlnqLDGFDPRGNIKVIMATNRPDIL 155

                        170
                 ....*....|..
gi 91199557  560 DPALRRPGRFDR 571
Cdd:cd19502  156 DPALLRPGRFDR 167
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
399-665 1.86e-51

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 192.17  E-value: 1.86e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  399 DTSVRFDSVGGLSSHIAALKEMVVFpLLYPEVFEKF--KIqpPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFF--- 473
Cdd:COG0465  136 KPKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLgaKI--PKGVLLVGPPGTGKTLLAKAVAGEAG-----VPFFsis 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  474 ------MRKGadclskwVGESeRqLRLLFDQAYQMRPAIIFFDEIDGLAPVRSS--------RqDQihssivsTL---LA 536
Cdd:COG0465  208 gsdfveMFVG-------VGAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglggghdeR-EQ-------TLnqlLV 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  537 LMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDwnpKP----VDmfLEELAEHCVG 612
Cdd:COG0465  271 EMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARK---KPlapdVD--LEVIARRTPG 345

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 91199557  613 YCGADIKSICAEAALCALRRRypqiyttseklqldlsSITISAKDFEAALQKI 665
Cdd:COG0465  346 FSGADLANLVNEAALLAARRN----------------KKAVTMEDFEEAIDRV 382
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 417-571 4.06e-51

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 177.32  E-value: 4.06e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  417 LKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVGESERQLRLLF 496
Cdd:cd19528    5 LQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQ-----ANFISVKGPELLTMWFGESEANVRDIF 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91199557  497 DQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSS---IVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 571
Cdd:cd19528   80 DKARAAAPCVLFFDELDSIAKARGGNIGDAGGAadrVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQ 157
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 406-572 4.61e-51

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: 177.60  E-value: 4.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  406 SVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECsrgdkRVAFFMRKGADCLSKWV 485
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGEL-----KVPFLKISATEIVSGVS 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  486 GESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGL----DSRGEIVVIGATNRLDSIDP 561
Cdd:cd19518   76 GESEEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDP 155

                        170
                 ....*....|.
gi 91199557  562 ALRRPGRFDRE 572
Cdd:cd19518  156 ALRRAGRFDRE 166
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
404-666 3.65e-50

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 178.15  E-value: 3.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  404 FDSVGGLSSHIAALKEMVVFpLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECsrgdkRVAFFMRKGADCLSK 483
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKE-LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGEL-----KLPLLTVRLDSLIGS 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  484 WVGESERQLRLLFDQAYQmRPAIIFFDEIDGLAPVRSSRQD--QIHsSIVSTLLALMDGLDSrgEIVVIGATNRLDSIDP 561
Cdd:COG1223   75 YLGETARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQNDvgEVK-RVVNALLQELDGLPS--GSVVIAATNHPELLDS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  562 ALRRpgRFDREFLFSLPDKNARKEILKIHTRDWnPKPVDMFLEELAEHCVGYCGADIKSICAEaalcALRRrypQIYTTS 641
Cdd:COG1223  151 ALWR--RFDEVIEFPLPDKEERKEILELNLKKF-PLPFELDLKKLAKKLEGLSGADIEKVLKT----ALKK---AILEDR 220

                        250       260
                 ....*....|....*....|....*
gi 91199557  642 EKlqldlssitISAKDFEAALQKIR 666
Cdd:COG1223  221 EK---------VTKEDLEEALKQRK 236
ftsH CHL00176
cell division protein; Validated
 378-637 6.75e-50

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 188.72  E-value: 6.75e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   378 GIYKDRMKIGASLADVDpMQLDTSVRFDSVGGLSSHIAALKEMVVFpLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVAR 457
Cdd:CHL00176  157 GPGQNLMNFGKSKARFQ-MEADTGITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAK 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   458 ALANECSrgdkrVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSR----QDQiHSSIVST 533
Cdd:CHL00176  235 AIAGEAE-----VPFFSISGSEFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGigggNDE-REQTLNQ 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   534 LLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDwnpKPV--DMFLEELAEHCV 611
Cdd:CHL00176  309 LLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARN---KKLspDVSLELIARRTP 385

                         250       260
                  ....*....|....*....|....*.
gi 91199557   612 GYCGADIKSICAEAALCALRRRYPQI 637
Cdd:CHL00176  386 GFSGADLANLLNEAAILTARRKKATI 411
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 414-575 6.43e-49

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


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 170.93  E-value: 6.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  414 IAALKEMVVFPLLYPEVfEKFKIQPPRGCLFYGPPGTGKTLVARALANECsrgdkRVAFFMRKGADCLSKWVGESERQLR 493
Cdd:cd19481    2 KASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGEL-----GLPLIVVKLSSLLSKYVGESEKNLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  494 LLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSS-IVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDRE 572
Cdd:cd19481   76 KIFERARRLAPCILFIDEIDAIGRKRDSSGESGELRrVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155


                 ...
gi 91199557  573 FLF 575
Cdd:cd19481  156 IEF 158
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 379-665 2.47e-48

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 178.03  E-value: 2.47e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   379 IYKDRMKIGASLA---------DVDPMQLDTSVR-----------FDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKIQP 438
Cdd:PTZ00454   99 LNRELLKPNASVAlhrhshavvDILPPEADSSIQllqmsekpdvtYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDP 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   439 PRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPV 518
Cdd:PTZ00454  179 PRGVLLYGPPGTGKTMLAKAVAHHTT-----ATFIRVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATK 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   519 RSSRQ---DQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDWN 595
Cdd:PTZ00454  254 RFDAQtgaDREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMN 333

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91199557   596 PKPvDMFLEELAEHCVGYCGADIKSICAEAALCALRR-RYpqiyttseklqldlssiTISAKDFEAALQKI 665
Cdd:PTZ00454  334 LSE-EVDLEDFVSRPEKISAADIAAICQEAGMQAVRKnRY-----------------VILPKDFEKGYKTV 386
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 443-577 8.92e-48

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 166.61  E-value: 8.92e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    443 LFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSR 522
Cdd:pfam00004    2 LLYGPPGTGKTTLAKAVAKELG-----APFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557    523 QDQIHSSIVSTLLALMDGLDSR-GEIVVIGATNRLDSIDPALRrpGRFDREFLFSL 577
Cdd:pfam00004   77 GDSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 417-571 3.88e-46

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 163.43  E-value: 3.88e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  417 LKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECsrgdkRVAFFMRKGADCLSKWVGESERQLRLLF 496
Cdd:cd19530    8 LTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANES-----GANFISVKGPELLNKYVGESERAVRQVF 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91199557  497 DQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 571
Cdd:cd19530   83 QRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 402-572 1.66e-45

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: 161.63  E-value: 1.66e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  402 VRFDSVGGLSSHIAALKEMVVFpLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECsrgdkRVAFFMRKGADCL 481
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEA-----GVPFFSISGSDFV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  482 SKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTL---LALMDGLDSRGEIVVIGATNRLDS 558
Cdd:cd19501   75 EMFVGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLnqlLVEMDGFESNTGVIVIAATNRPDV 154

                        170
                 ....*....|....
gi 91199557  559 IDPALRRPGRFDRE 572
Cdd:cd19501  155 LDPALLRPGRFDRQ 168
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 407-574 5.80e-45

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 159.83  E-value: 5.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  407 VGGLSSHIAALKEMVVFPLLYPEVFeKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVG 486
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESG-----STFFSISASSLVSKWVG 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  487 ESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGL--DSRGEIVVIGATNRLDSIDPALR 564
Cdd:cd19509   75 ESEKIVRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFL 154

                        170
                 ....*....|
gi 91199557  565 RpgRFDREFL 574
Cdd:cd19509  155 R--RFEKRIY 162
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 419-571 1.35e-42

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: 153.05  E-value: 1.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  419 EMVVFPLLYPEVFEKfKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVGESERQLRLLFDQ 498
Cdd:cd19527    7 DTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECS-----LNFLSVKGPELINMYIGESEANVREVFQK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557  499 AYQMRPAIIFFDEIDGLAPVRSSRQDQ--IHSSIVSTLLALMDGLDSRGE-IVVIGATNRLDSIDPALRRPGRFDR 571
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRGNSGDSggVMDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDK 156
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
381-671 5.45e-42

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 164.82  E-value: 5.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   381 KDRMKIGASLAD-VDPMQLDTSvrFDSVGGLSSHIAALKEMVVFpLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARAL 459
Cdd:PRK10733  129 KGAMSFGKSKARmLTEDQIKTT--FADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAI 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   460 AnecsrGDKRVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTL---LA 536
Cdd:PRK10733  206 A-----GEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLnqmLV 280

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   537 LMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRDWnPKPVDMFLEELAEHCVGYCGA 616
Cdd:PRK10733  281 EMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRV-PLAPDIDAAIIARGTPGFSGA 359

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 91199557   617 DIKSICAEAALCALR--RRypqiyttseklqldlssiTISAKDFEAALQKIRPASQR 671
Cdd:PRK10733  360 DLANLVNEAALFAARgnKR------------------VVSMVEFEKAKDKIMMGAER 398
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 415-571 2.27e-40

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


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 146.42  E-value: 2.27e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  415 AALKEMVVFPLLYPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVGESERQLRL 494
Cdd:cd19526    3 KALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECG-----LNFISVKGPELLNKYIGASEQNVRD 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91199557  495 LFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 571
Cdd:cd19526   78 LFSRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDK 154
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 406-569 3.51e-38

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 140.64  E-value: 3.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  406 SVGGLSSHIAALKEMVVFPLLYPEVFEKFKI-QPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKW 484
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAG-----ARFINLQVSSLTDKW 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  485 VGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRG--EIVVIGATNRLDSIDPA 562
Cdd:cd19520   76 YGESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGncRVIVMGATNRPQDLDEA 155


                 ....*....
gi 91199557  563 LRR--PGRF 569
Cdd:cd19520  156 ILRrmPKRF 164
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 389-565 1.13e-36

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: 137.04  E-value: 1.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  389 SLADVDPMQLDTSVRFDSVGGLSSHIAALKEMVVFPLLYPEVFEKFKiQPPRGCLFYGPPGTGKTLVARALANECsrgdk 468
Cdd:cd19525    6 ELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQS----- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  469 RVAFFMRKGADCLSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGE-- 546
Cdd:cd19525   80 GATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEdr 159

                        170
                 ....*....|....*....
gi 91199557  547 IVVIGATNRLDSIDPALRR 565
Cdd:cd19525  160 ILVVGATNRPQEIDEAARR 178
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 407-570 8.77e-36

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: 134.15  E-value: 8.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  407 VGGLSSHIAALKEMV----VFPllyPEVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSRGDKRVAffmrKGADCLS 482
Cdd:cd19504    2 IGGLDKEFSDIFRRAfasrVFP---PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIV----NGPEILN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  483 KWVGESERQLRLLFDQAYQMRPA--------IIFFDEIDGLAPVRSSRQDQ--IHSSIVSTLLALMDGLDSRGEIVVIGA 552
Cdd:cd19504   75 KYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAICKQRGSMAGStgVHDTVVNQLLSKIDGVEQLNNILVIGM 154

                        170
                 ....*....|....*...
gi 91199557  553 TNRLDSIDPALRRPGRFD 570
Cdd:cd19504  155 TNRKDLIDEALLRPGRLE 172
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 401-571 1.46e-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: 133.45  E-value: 1.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  401 SVRFDSVGGLSSHIAALKEMVVFPLLYPEVFeKFKIQPPRGCLFYGPPGTGKTLVARALANECSRgdkrvAFFMRKGADC 480
Cdd:cd19521    3 NVKWEDVAGLEGAKEALKEAVILPVKFPHLF-TGNRKPWSGILLYGPPGTGKSYLAKAVATEANS-----TFFSVSSSDL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  481 LSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGL--DSRGeIVVIGATNRLDS 558
Cdd:cd19521   77 VSKWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgnDSQG-VLVLGATNIPWQ 155

                        170
                 ....*....|...
gi 91199557  559 IDPALRRpgRFDR 571
Cdd:cd19521  156 LDSAIRR--RFEK 166
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 407-565 1.38e-32

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: 124.58  E-value: 1.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  407 VGGLSSHIAALKEMVVFPLLYPEVFEKFKiQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVG 486
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESN-----ATFFNISAASLTSKYVG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  487 ESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIVSTLLALMDGLDSRGE--IVVIGATNRLDSIDPA-L 563
Cdd:cd19524   76 EGEKLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAvL 155


                 ..
gi 91199557  564 RR 565
Cdd:cd19524  156 RR 157
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 407-565 1.54e-32

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: 124.71  E-value: 1.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  407 VGGLSSHIAALKEMVVFPLLYPEVFEKFKiQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVG 486
Cdd:cd19522    2 IADLEEAKKLLEEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATECG-----TTFFNVSSSTLTSKYRG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  487 ESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIHSSIV-STLLALMDGL-------DSRGEIVVIGATNRLDS 558
Cdd:cd19522   76 ESEKLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVkSELLVQMDGVggasendDPSKMVMVLAATNFPWD 155


                 ....*..
gi 91199557  559 IDPALRR 565
Cdd:cd19522  156 IDEALRR 162
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 429-577 4.91e-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: 4.91e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  429 EVFEKFKIQPPRGCLFYGPPGTGKTLVARALANECSRgdKRVAFFMRKGADCLSKWVGESERQ---LRLLFDQAYQMRPA 505
Cdd:cd00009    9 ALREALELPPPKNLLLYGPPGTGKTTLARAIANELFR--PGAPFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPG 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91199557  506 IIFFDEIDGLAPvrssrqdQIHSSIVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSL 577
Cdd:cd00009   87 VLFIDEIDSLSR-------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 407-574 6.18e-27

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: 108.43  E-value: 6.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  407 VGGLSSHIAALKEMVVFPLLYPEVFEKFkIQPPRGCLFYGPPGTGKTLVARALANECSrgdkrVAFFMRKGADCLSKWVG 486
Cdd:cd19523    2 IAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLG-----ATFLRLRGSTLVAKWAG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  487 ESERQLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSRQDQIhSSIVSTLLALMDGLDSRGE--IVVIGATNRLDSIDPALR 564
Cdd:cd19523   76 EGEKILQASFLAARCRQPSVLFISDLDALLSSQDDEASPV-GRLQVELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLR 154

                        170
                 ....*....|
gi 91199557  565 RpgRFDREFL 574
Cdd:cd19523  155 R--YFSKRLL 162
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 438-579 5.03e-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: 88.20  E-value: 5.03e-20
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557     438 PPRGCLFYGPPGTGKTLVARALANECSRGDKRVAFF------------MRKGADCLSKWVGESERQLRLLFDQAYQMRPA 505
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIdgedileevldqLLLIIVGGKKASGSGELRLRLALALARKLKPD 80

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91199557     506 IIFFDEIDGLAPVRSSRQDQihssiVSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPgRFDREFLFSLPD 579
Cdd:smart00382   81 VLILDEITSLLDAEQEALLL-----LLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
Bromodomain cd04369
Bromodomain. Bromodomains are found in many chromatin-associated proteins and in nuclear ...
 960-1062 6.33e-20

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: 85.89  E-value: 6.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  960 RELRIFLRNVthRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPD 1039
Cdd:cd04369    3 KKLRSLLDAL--KKLKRDLSEPFLEPVDPKEAPDYYEVIKNPMDLSTIKKKLKNGEYKSLEEFEADVRLIFSNAKTYNGP 80

                         90       100
                 ....*....|....*....|...
gi 91199557 1040 RDPgdrlIRHRACALRDTAYAII 1062
Cdd:cd04369   81 GSP----IYKDAKKLEKLFEKLL 99
Bromo_gcn5_like cd05509
Bromodomain; Gcn5_like subfamily. Gcn5p is a histone acetyltransferase (HAT) which mediates ...
 982-1077 1.72e-18

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


Pssm-ID: 99941 [Multi-domain]  Cd Length: 101  Bit Score: 81.83  E-value: 1.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPDrdpgdrlirhracalrDTAYAI 1061
Cdd:cd05509   22 FLEPVDKEEAPDYYDVIKKPMDLSTMEEKLENGYYVTLEEFVADLKLIFDNCRLYNGP----------------DTEYYK 85

                         90
                 ....*....|....*.
gi 91199557 1062 IKEELDEDFEQLCEEI 1077
Cdd:cd05509   86 CANKLEKFFWKKLKEL 101
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 432-573 8.17e-18

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: 82.03  E-value: 8.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  432 EKFKIQPPRGCLFYGPPGTGKTLVARALANECSRGDKRV---AFFmrkgadclSKWVGESERQLRLLFDQAYQMRPAIIF 508
Cdd:cd19507   24 SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLdmgRLF--------GGLVGESESRLRQMIQTAEAIAPCVLW 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557  509 FDEIDGLAPVRSSRQDQ-IHSSIVSTLLALMDglDSRGEIVVIGATNRLDSIDPALRRPGRFDREF 573
Cdd:cd19507   96 IDEIEKGFSNADSKGDSgTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEIF 159
Bromo_brd1_like cd05512
Bromodomain; brd1_like subfamily. BRD1 is a mammalian gene which encodes for a nuclear protein ...
 962-1062 1.67e-17

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: 78.98  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  962 LRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNpDRD 1041
Cdd:cd05512    2 LEVLLRKTLDQLQEKDTAEIFSEPVDLSEVPDYLDHIKQPMDFSTMRKKLESQRYRTLEDFEADFNLIINNCLAYN-AKD 80

                         90       100
                 ....*....|....*....|..
gi 91199557 1042 PgdrlIRHRACA-LRDTAYAII 1062
Cdd:cd05512   81 T----IFYRAAVrLRDQGGAIL 98
ycf46 CHL00195
Ycf46; Provisional
 439-625 2.41e-17

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 87.00  E-value: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   439 PRGCLFYGPPGTGKTLVARALANECS----RGDKRVAFfmrkgadclSKWVGESERQLRLLFDQAYQMRPAIIFFDEIDG 514
Cdd:CHL00195  259 PRGLLLVGIQGTGKSLTAKAIANDWQlpllRLDVGKLF---------GGIVGESESRMRQMIRIAEALSPCILWIDEIDK 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   515 LAPVRSSRQDQIHSSIV-STLLALMDglDSRGEIVVIGATNRLDSIDPALRRPGRFDREFLFSLPDKNARKEILKIHTRD 593
Cdd:CHL00195  330 AFSNSESKGDSGTTNRVlATFITWLS--EKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQK 407

                         170       180       190
                  ....*....|....*....|....*....|...
gi 91199557   594 WNPKPVDMF-LEELAEHCVGYCGADIKSICAEA 625
Cdd:CHL00195  408 FRPKSWKKYdIKKLSKLSNKFSGAEIEQSIIEA 440
BROMO smart00297
bromo domain;
955-1065 2.90e-17

bromo domain;


Pssm-ID: 197636 [Multi-domain]  Cd Length: 107  Bit Score: 78.47  E-value: 2.90e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557     955 EEDTFRELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNAL 1034
Cdd:smart00297    1 DPKLQKKLQELLKAVLDKLDSHPLSWPFLKPVSRKEAPDYYDIIKKPMDLKTIKKKLENGKYSSVEEFVADFNLMFSNAR 80

                            90       100       110
                    ....*....|....*....|....*....|.
gi 91199557    1035 EYNPDrdpgDRLIRHRACALRDTAYAIIKEE 1065
Cdd:smart00297   81 TYNGP----DSEVYKDAKKLEKFFEKKLREL 107
Bromo_TFIID cd05511
Bromodomain, TFIID-like subfamily. Human TAFII250 (or TAF250) is the largest subunit of TFIID, ...
 982-1037 1.98e-15

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: 73.45  E-value: 1.98e-15
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557  982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05511   21 FHTPVNKKKVPDYYKIIKRPMDLQTIRKKISKHKYQSREEFLEDIELIVDNSVLYN 76
Bromodomain pfam00439
Bromodomain; Bromodomains are 110 amino acid long domains, that are found in many chromatin ...
 982-1038 6.66e-15

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


Pssm-ID: 425683 [Multi-domain]  Cd Length: 84  Bit Score: 71.19  E-value: 6.66e-15
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 91199557    982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNP 1038
Cdd:pfam00439   17 FLEPVDPDEYPDYYSVIKKPMDLSTIKKKLENGEYKSLAEFLADVKLIFSNARTYNG 73
Bromo_Brdt_II_like cd05498
Bromodomain, Brdt_like subfamily, repeat II. Human Brdt is a testis-specific member of the BET ...
 981-1042 5.64e-14

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: 69.23  E-value: 5.64e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91199557  981 VFTKPVDP--DEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPDRDP 1042
Cdd:cd05498   23 PFYKPVDPeaLGLHDYHDIIKHPMDLSTIKKKLDNREYADAQEFAADVRLMFSNCYKYNPPDHP 86
Bromo_plant1 cd05506
Bromodomain, uncharacterized subfamily specific to plants. Might function as a global ...
 972-1038 9.02e-13

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: 65.43  E-value: 9.02e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91199557  972 RLAIDKRFRVFTKPVDPD--EVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNP 1038
Cdd:cd05506   11 KLMKHKWGWVFNAPVDVValGLPDYFDIIKKPMDLGTVKKKLEKGEYSSPEEFAADVRLTFANAMRYNP 79
Bromo_SPT7_like cd05510
Bromodomain; SPT7_like subfamily. SPT7 is a yeast protein that functions as a component of the ...
 982-1063 9.15e-13

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: 65.93  E-value: 9.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNpdRDPGDRLIRHrACALRDTAYAI 1061
Cdd:cd05510   29 FLTKVSKREAPDYYDIIKKPMDLGTMLKKLKNLQYKSKAEFVDDLNLIWKNCLLYN--SDPSHPLRRH-ANFMKKKAEHL 105


                 ..
gi 91199557 1062 IK 1063
Cdd:cd05510  106 LK 107
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 440-571 1.38e-12

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: 66.61  E-value: 1.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  440 RGCLFYGPPGTGKTLVARALANEcsrgdkrvaffMRKGADCLS-KWVGESERQLRLLFDQAYQmrPAIIFFDEID----- 513
Cdd:cd19510   24 RGYLLYGPPGTGKSSFIAALAGE-----------LDYDICDLNlSEVVLTDDRLNHLLNTAPK--QSIILLEDIDaafes 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 91199557  514 GLAPVRSSRQDQIHSSI-VSTLLALMDGLDSRGEIVVIGATNRLDSIDPALRRPGRFDR 571
Cdd:cd19510   91 REHNKKNPSAYGGLSRVtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149
Bromo_BDF1_2_I cd05500
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat I. BDF1 and BDF2 are yeast ...
 980-1037 3.82e-12

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: 63.87  E-value: 3.82e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  980 RVFTKPVDPDE--VPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05500   23 RPFLVPVDPVKlnIPHYPTIIKKPMDLGTIERKLKSNVYTSVEEFTADFNLMVDNCLTFN 82
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 443-563 5.37e-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: 66.32  E-value: 5.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  443 LFYGPPGTGKTLVARALANECSrgdKRVAFFMRKG-------ADCLSKWVGESERQLRLLFDQAYQM---RPAIIF--FD 510
Cdd:cd19508   56 LLHGPPGTGKTSLCKALAQKLS---IRLSSRYRYGqlieinsHSLFSKWFSESGKLVTKMFQKIQELiddKDALVFvlID 132

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 91199557  511 EIDGLAPVRSSRQDQIHSS----IVSTLLALMDGLDSRGEIVVIGATNRLDSIDPAL 563
Cdd:cd19508  133 EVESLAAARSASSSGTEPSdairVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
Bromo_BDF1_2_II cd05499
Bromodomain. BDF1/BDF2 like subfamily, restricted to fungi, repeat II. BDF1 and BDF2 are yeast ...
 981-1042 1.65e-11

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: 61.92  E-value: 1.65e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91199557  981 VFTKPVDPD--EVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPDRDP 1042
Cdd:cd05499   23 PFLDPVDPValNIPNYFSIIKKPMDLGTISKKLQNGQYQSAKEFERDVRLIFKNCYTFNPEGTD 86
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 443-609 2.02e-11

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 68.33  E-value: 2.02e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    443 LFYGPPGTGKTLVARALANE-CSRGD-KRVAFFMRKGADCLSKWVGESERQLRLLFDQAYQmrpAIIFFDEIDGLAPVRS 520
Cdd:TIGR03922  316 LFAGPPGTGKTTIARVVAKIyCGLGVlRKPLVREVSRADLIGQYIGESEAKTNEIIDSALG---GVLFLDEAYTLVETGY 392

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    521 SRQDQIHSSIVSTLLALMDglDSRGEIVVIGA--TNRLD---SIDPALRRpgRFDR--EFLFSLPDknarkEILKIHTRD 593
Cdd:TIGR03922  393 GQKDPFGLEAIDTLLARME--NDRDRLVVIGAgyRKDLDkflEVNEGLRS--RFTRviEFPSYSPD-----ELVEIARRM 463

                          170
                   ....*....|....*.
gi 91199557    594 WNPKPvDMFLEELAEH 609
Cdd:TIGR03922  464 ATERD-SVLDDAAADA 478
Bromo_Acf1_like cd05504
Bromodomain; Acf1_like or BAZ1A_like subfamily. Bromo adjacent to zinc finger 1A (BAZ1A) was ...
 982-1041 4.39e-11

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: 61.26  E-value: 4.39e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPDRD 1041
Cdd:cd05504   33 FLRPVSKIEVPDYYDIIKKPMDLGTIKEKLNMGEYKLAEEFLSDIQLVFSNCFLYNPEHT 92
Bromo_brd7_like cd05513
Bromodomain, brd7_like subgroup. The BRD7 gene encodes a nuclear protein that has been shown ...
 982-1037 1.53e-10

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: 59.35  E-value: 1.53e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557  982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05513   22 FAFPVTDFIAPGYSSIIKHPMDFSTMKEKIKNNDYQSIEEFKDDFKLMCENAMKYN 77
Bromo_WDR9_II cd05496
Bromodomain; WDR9 repeat II_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 982-1040 4.26e-10

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


Pssm-ID: 99928  Cd Length: 119  Bit Score: 58.62  E-value: 4.26e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 91199557  982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPDR 1040
Cdd:cd05496   26 FRQPVDLLKYPDYRDIIDTPMDLGTVKETLFGGNYDDPMEFAKDVRLIFSNSKSYTPNK 84
Bromo_BAZ2A_B_like cd05503
Bromodomain, BAZ2A/BAZ2B_like subfamily. Bromo adjacent to zinc finger 2A (BAZ2A) and 2B ...
 982-1042 1.06e-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: 56.61  E-value: 1.06e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91199557  982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPDRDP 1042
Cdd:cd05503   21 FLEPVNTKLVPGYRKIIKKPMDFSTIREKLESGQYKTLEEFAEDVRLVFDNCETFNEDDSE 81
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 603-637 1.56e-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: 54.47  E-value: 1.56e-09
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 91199557    603 LEELAEHCVGYCGADIKSICAEAALCALRRRYPQI 637
Cdd:pfam17862    4 LEELAERTEGFSGADLEALCREAALAALRRGLEAV 38
Bromo_WSTF_like cd05505
Bromodomain; Williams syndrome transcription factor-like subfamily (WSTF-like). The ...
 982-1037 1.56e-09

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: 56.39  E-value: 1.56e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557  982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05505   21 FREPVTADEAEDYKKVITNPMDLQTMQTKCSCGSYSSVQEFLDDMKLVFSNAEKYY 76
Bromo_cbp_like cd05495
Bromodomain, cbp_like subfamily. Cbp (CREB binding protein or CREBBP) is an acetyltransferase ...
 961-1038 3.19e-09

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: 55.91  E-value: 3.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  961 ELRIFLRNVTHRLAIDKRFRV-FTKPVDPD--EVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05495    3 ELRQALMPTLEKLYKQDPESLpFRQPVDPKllGIPDYFDIVKNPMDLSTIRRKLDTGQYQDPWQYVDDVWLMFDNAWLYN 82


                 .
gi 91199557 1038 P 1038
Cdd:cd05495   83 R 83
Bromo_Brdt_I_like cd05497
Bromodomain, Brdt_like subfamily, repeat I. Human Brdt is a testis-specific member of the BET ...
 982-1047 6.17e-09

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


Pssm-ID: 99929  Cd Length: 107  Bit Score: 54.74  E-value: 6.17e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91199557  982 FTKPVDPD--EVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPdrdPGDRLI 1047
Cdd:cd05497   26 FQQPVDAVklNLPDYHKIIKTPMDLGTIKKRLENNYYWSASECIQDFNTMFTNCYIYNK---PGDDVV 90
Bromo_polybromo_V cd05515
Bromodomain, polybromo repeat V. Polybromo is a nuclear protein of unknown function, which ...
 971-1039 6.55e-09

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: 54.62  E-value: 6.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  971 HRLAIdkrfrVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN-PD 1039
Cdd:cd05515   21 RRLSL-----IFMRLPSKSEYPDYYDVIKKPIDMEKIRSKIEGNQYQSLDDMVSDFVLMFDNACKYNePD 85
COG5076 COG5076
Transcription factor involved in chromatin remodeling, contains bromodomain [Chromatin ...
 975-1085 2.98e-08

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


Pssm-ID: 227408 [Multi-domain]  Cd Length: 371  Bit Score: 57.51  E-value: 2.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  975 IDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNpdrDPGDRLIRHRacal 1054
Cdd:COG5076  162 GRFLSSIFLGLPSKREYPDYYEIIKSPMDLLTIQKKLKNGRYKSFEEFVSDLNLMFDNCKLYN---GPDSSVYVDA---- 234

                         90       100       110
                 ....*....|....*....|....*....|.
gi 91199557 1055 rdtayAIIKEELDEDFEQLCEEIQESRKKRG 1085
Cdd:COG5076  235 -----KELEKYFLKLIEEIPEEMLELSIKPG 260
Bromo_SNF2L2 cd05516
Bromodomain, SNF2L2-like subfamily, specific to animals. SNF2L2 (SNF2-alpha) or SWI ...
 990-1037 3.12e-08

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: 52.82  E-value: 3.12e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 91199557  990 EVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05516   36 ELPEYYELIRKPVDFKKIKERIRNHKYRSLEDLEKDVMLLCQNAQTFN 83
Bromodomain_1 cd05494
Bromodomain; uncharacterized subfamily. Bromodomains are found in many chromatin-associated ...
 953-1083 6.08e-08

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


Pssm-ID: 99926 [Multi-domain]  Cd Length: 114  Bit Score: 52.45  E-value: 6.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  953 EQEEDTFRELRIFLRNvthrlaidKRFRVFTKPVDPDE--VPDYVTVIKQPMDLSsviSKIDLHkyltVKDYLKDIDLIC 1030
Cdd:cd05494    3 EALERVLRELKRHRRN--------EDAWPFLEPVNPPRrgAPDYRDVIKRPMSFG---TKVNNI----VETGARDLEDLQ 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 91199557 1031 SNAleynpdRDPGDRLIRHRACALRDTAYAIIKEELDEDFEQLCEEIQESRKK 1083
Cdd:cd05494   68 IVQ------EDPADKQIDDEGRRSPSNIYAVEALEQLIVFQCKQVKGLKQKRH 114
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 438-571 8.91e-08

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 53.15  E-value: 8.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  438 PPRGCLFYGPPGTGKTLVARALA------------NECSrgDKRVAFFMRKGADCLSKWvGESERQLRLLFDQAYQMRPA 505
Cdd:cd19505   11 PSKGILLIGSIETGRSYLIKSLAansyvplirislNKLL--YNKPDFGNDDWIDGMLIL-KESLHRLNLQFELAKAMSPC 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91199557  506 IIFFDEIDGLApVRSSRQDQIHSSivSTLLALMDGLDSRG-------EIVVIGATNRLDSIDPALRRPGRFDR 571
Cdd:cd19505   88 IIWIPNIHELN-VNRSTQNLEEDP--KLLLGLLLNYLSRDfeksstrNILVIASTHIPQKVDPALIAPNRLDT 157
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 440-570 1.06e-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: 52.53  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  440 RGCLFYGPPGTGKTLVARALANEC-------SRGDkrVAFFMRKGADCLSK---WVGESERQLrllfdqayqmrpaIIFF 509
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSgmdyaimTGGD--VAPMGREGVTAIHKvfdWANTSRRGL-------------LLFV 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91199557  510 DEIDGLAPVRSSrqDQIHSSIVSTLLALM--DGLDSRgEIVVIGATNRLDSIDPALRrpGRFD 570
Cdd:cd19512   88 DEADAFLRKRST--EKISEDLRAALNAFLyrTGEQSN-KFMLVLASNQPEQFDWAIN--DRID 145
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 442-564 7.50e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.16  E-value: 7.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   442 CLFYGPPGTGKTLVARALANECSRgdkrvAFFMrkgadcLSKwVGESERQLRLLFDQAYQMRPA----IIFFDEIDGLAp 517
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDA-----PFEA------LSA-VTSGVKDLREVIEEARQRRSAgrrtILFIDEIHRFN- 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 91199557   518 vrSSRQDqihssivsTLLALMDgldsRGEIVVIGAT--NRLDSIDPALR 564
Cdd:PRK13342  106 --KAQQD--------ALLPHVE----DGTITLIGATteNPSFEVNPALL 140
Bromo_brd8_like cd05507
Bromodomain, brd8_like subgroup. In mammals, brd8 (bromodomain containing 8) interacts with ...
 981-1041 9.19e-07

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


Pssm-ID: 99939  Cd Length: 104  Bit Score: 48.51  E-value: 9.19e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91199557  981 VFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN-PDRD 1041
Cdd:cd05507   23 VFLKPVTEDIAPGYHSVVYRPMDLSTIKKNIENGTIRSTAEFQRDVLLMFQNAIMYNsSDHD 84
Bromo_Rsc1_2_II cd05522
Bromodomain, repeat II in Rsc1/2_like subfamily, specific to fungi. Rsc1 and Rsc2 are ...
 978-1037 1.04e-06

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: 48.39  E-value: 1.04e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  978 RFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05522   24 LTLHFEKLPDKAREPEYYQEISNPISLDDIKKKVKRRKYKSFDQFLNDLNLMFENAKLYN 83
Bromo_tif1_like cd05502
Bromodomain; tif1_like subfamily. Tif1 (transcription intermediary factor 1) is a member of ...
 943-1039 1.33e-06

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


Pssm-ID: 99934 [Multi-domain]  Cd Length: 109  Bit Score: 48.44  E-value: 1.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  943 LTAEEVKRLEeqeedtfrelRIFLRNVTHRLAIDkrfrvFTKPVDPdEVPDYVTVIKQPMDLSSVISKIDLH---KYLTV 1019
Cdd:cd05502    1 LSPIDQRKCE----------RLLLELYCHELSLP-----FHEPVSP-SVPNYYKIIKTPMDLSLIRKKLQPKspqHYSSP 64

                         90       100
                 ....*....|....*....|
gi 91199557 1020 KDYLKDIDLICSNALEYNPD 1039
Cdd:cd05502   65 EEFVADVRLMFKNCYKFNEE 84
Bromo_polybromo_II cd05517
Bromodomain, polybromo repeat II. Polybromo is a nuclear protein of unknown function, which ...
 980-1037 1.40e-06

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: 48.20  E-value: 1.40e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 91199557  980 RVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05517   25 ELFQKLPSKVLYPDYYAVIKEPIDLKTIAQRIQSGYYKSIEDMEKDLDLMVKNAKTFN 82
Bromo_polybromo_IV cd05518
Bromodomain, polybromo repeat IV. Polybromo is a nuclear protein of unknown function, which ...
 990-1037 8.68e-06

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


Pssm-ID: 99949 [Multi-domain]  Cd Length: 103  Bit Score: 45.90  E-value: 8.68e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 91199557  990 EVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05518   35 DYPDYYKIILEPIDLKTIEHNIRNDKYATEEELMDDFKLMFRNARHYN 82
Bromo_polybromo_III cd05520
Bromodomain, polybromo repeat III. Polybromo is a nuclear protein of unknown function, which ...
 992-1038 1.03e-05

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


Pssm-ID: 99951  Cd Length: 103  Bit Score: 45.79  E-value: 1.03e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 91199557  992 PDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNP 1038
Cdd:cd05520   37 PDYYQEIKNPISLQQIRTKLKNGEYETLEELEADLNLMFENAKRYNV 83
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 443-553 1.81e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 48.90  E-value: 1.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  443 LFYGPPGTGKTLVARALANECSRgdkrvAFFMrkgadcLSKwVGESERQLRLLFDQAYQMR----PAIIFFDEIDglapv 518
Cdd:COG2256   53 ILWGPPGTGKTTLARLIANATDA-----EFVA------LSA-VTSGVKDIREVIEEARERRaygrRTILFVDEIH----- 115

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 91199557  519 R--SSRQDqihssivsTLLALMDgldsRGEIVVIGAT 553
Cdd:COG2256  116 RfnKAQQD--------ALLPHVE----DGTITLIGAT 140
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
437-588 3.49e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 47.92  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  437 QPPRGCLFYGPPGTGKTLVARA----LANECSRGDKRVAF-------------FMRKGADCLSKWVGESERQLRL--LFD 497
Cdd:COG1474   49 ERPSNVLIYGPTGTGKTAVAKYvleeLEEEAEERGVDVRVvyvncrqastryrVLSRILEELGSGEDIPSTGLSTdeLFD 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  498 QAYQM-----RPAIIFFDEIDGLapvrssrQDQIHSSIVSTLLALMDGLDSRGeIVVIGATNRL---DSIDPALRRpgRF 569
Cdd:COG1474  129 RLYEAlderdGVLVVVLDEIDYL-------VDDEGDDLLYQLLRANEELEGAR-VGVIGISNDLeflENLDPRVKS--SL 198

                        170       180
                 ....*....|....*....|
gi 91199557  570 -DREFLFSLPDKNARKEILK 588
Cdd:COG1474  199 gEEEIVFPPYDADELRDILE 218
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
436-473 5.98e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 46.31  E-value: 5.98e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 91199557  436 IQPPRGCLFYGPPGTGKTLVARALANECSRGDKRVAFF 473
Cdd:COG1484   96 IERGENLILLGPPGTGKTHLAIALGHEACRAGYRVRFT 133
PRK04195 PRK04195
replication factor C large subunit; Provisional
 435-515 7.52e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 46.84  E-value: 7.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   435 KIQPPRGCLFYGPPGTGKTLVARALANE---------CSrgDKRvaffmrkGADCLSKWVGESERQlRLLFDQAYQmrpa 505
Cdd:PRK04195   35 KGKPKKALLLYGPPGVGKTSLAHALANDygwevielnAS--DQR-------TADVIERVAGEAATS-GSLFGARRK---- 100

                          90
                  ....*....|
gi 91199557   506 IIFFDEIDGL 515
Cdd:PRK04195  101 LILLDEVDGI 110
Bromo_RACK7 cd05508
Bromodomain, RACK7_like subfamily. RACK7 (also called human protein kinase C-binding protein) ...
 982-1037 9.31e-05

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: 42.76  E-value: 9.31e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 91199557  982 FTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05508   23 FLKPVDLEQFPDYAQYVFKPMDLSTLEKNVRKKAYGSTDAFLADAKWILHNAIIYN 78
ycf46 CHL00195
Ycf46; Provisional
 766-907 1.02e-04

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 46.55  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   766 PR-LLIVGEPGFGQSshLAPAVIHALEKFTVYTLDIPVLFGISTTSPEEACSQMIREAKRTAPSIvyvphihLWW-EI-- 841
Cdd:CHL00195  259 PRgLLLVGIQGTGKS--LTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCI-------LWIdEIdk 329

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91199557   842 ----------VGPTLK--ATFTTLLQTIPSfaPVLLLATSEKPYSaLPEEVqeLFTHDYGEIFNVQLPDKEERTKFFE 907
Cdd:CHL00195  330 afsnseskgdSGTTNRvlATFITWLSEKKS--PVFVVATANNIDL-LPLEI--LRKGRFDEIFFLDLPSLEEREKIFK 402
Bromo_polybromo_I cd05524
Bromodomain, polybromo repeat I. Polybromo is a nuclear protein of unknown function, which ...
 992-1036 1.69e-04

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: 42.32  E-value: 1.69e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 91199557  992 PDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEY 1036
Cdd:cd05524   39 PEYYEVVSNPIDLLKIQQKLKTEEYDDVDDLTADFELLINNAKAY 83
Bromo_WDR9_I_like cd05529
Bromodomain; WDR9 repeat I_like subfamily. WDR9 is a human gene located in the Down Syndrome ...
 952-1038 2.85e-04

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


Pssm-ID: 99958  Cd Length: 128  Bit Score: 42.32  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  952 EEQEEDTFRELRIFLRNVthRLAIDKRFRVftkPVD-PDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLIC 1030
Cdd:cd05529   23 DEERERLISGLDKLLLSL--QLEIAEYFEY---PVDlRAWYPDYWNRVPVPMDLETIRSRLENRYYRSLEALRHDVRLIL 97


                 ....*...
gi 91199557 1031 SNALEYNP 1038
Cdd:cd05529   98 SNAETFNE 105
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
439-577 3.78e-04

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


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 43.37  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  439 PRGC--LFYGPPGTGKTLVARALANE-CSRGDKrVAFFMrkgadclskwVGESERQLR-----LLFD-QAYQMRPAIIFF 509
Cdd:COG0467   18 PRGSstLLSGPPGTGKTTLALQFLAEgLRRGEK-GLYVS----------FEESPEQLLrraesLGLDlEEYIESGLLRII 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91199557  510 DeidglapVRSSRQDQIHSSIVSTLLALMDGLDSRgeIVVIgatnrlDSIDP---ALRRPGRFdREFLFSL 577
Cdd:COG0467   87 D-------LSPEELGLDLEELLARLREAVEEFGAK--RVVI------DSLSGlllALPDPERL-REFLHRL 141
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
 443-559 5.21e-04

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 42.55  E-value: 5.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  443 LFYGPPGTGKTLVARALANE-CSRGDKRVAF----FMRKGADCLSK-----WVGESERQlrLLFDQAYQMRPAIIFFDEI 512
Cdd:cd19499   45 LFLGPTGVGKTELAKALAELlFGDEDNLIRIdmseYMEKHSVSRLIgappgYVGYTEGG--QLTEAVRRKPYSVVLLDEI 122

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91199557  513 dglapvrssrqDQIHSSIVSTLLALMD-G--LDSRGEIVVIGAT--------------NRLDSI 559
Cdd:cd19499  123 -----------EKAHPDVQNLLLQVLDdGrlTDSHGRTVDFKNTiiimtsnhfrpeflNRIDEI 175
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 439-550 1.47e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 40.95  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    439 PRGCLFYGPPGTGKTLVARALANECSRgdKRVAFFMRKGADCLSK---WVGESERQLRLLFDQAYQMRPAIIFFDEIDGL 515
Cdd:pfam13191   24 PPSVLLTGEAGTGKTTLLRELLRALER--DGGYFLRGKCDENLPYsplLEALTREGLLRQLLDELESSLLEAWRAALLEA 101

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 91199557    516 APVRSSRQDQIHSSIVSTLLALMDGLDSRGEIVVI 550
Cdd:pfam13191  102 LAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL 136
PRK13341 PRK13341
AAA family ATPase;
443-621 2.09e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 42.35  E-value: 2.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   443 LFYGPPGTGKTLVARALANECSrgdkrvAFFMRKGAdCLSkwvGESErqLRLLFDQAYQMRP-----AIIFFDEIDGLap 517
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTR------AHFSSLNA-VLA---GVKD--LRAEVDRAKERLErhgkrTILFIDEVHRF-- 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557   518 vRSSRQDqihssivstllALMDGLDsRGEIVVIGAT--NRLDSIDPALRRPGRFDRefLFSLPDKNARK---EILKIHTR 592
Cdd:PRK13341  122 -NKAQQD-----------ALLPWVE-NGTITLIGATteNPYFEVNKALVSRSRLFR--LKSLSDEDLHQllkRALQDKER 186

                         170       180
                  ....*....|....*....|....*....
gi 91199557   593 DWNPKPVDmFLEELAEHCVGYCGADIKSI 621
Cdd:PRK13341  187 GYGDRKVD-LEPEAEKHLVDVANGDARSL 214
PRK08116 PRK08116
hypothetical protein; Validated
 427-462 2.71e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.16  E-value: 2.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 91199557   427 YPEVFEKFKIQPpRGCLFYGPPGTGKTLVARALANE 462
Cdd:PRK08116  103 YVKKFEEMKKEN-VGLLLWGSVGTGKTYLAACIANE 137
Bromo_SNF2 cd05519
Bromodomain, SNF2-like subfamily, specific to fungi. SNF2 is a yeast protein involved in ...
 977-1037 3.46e-03

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


Pssm-ID: 99950  Cd Length: 103  Bit Score: 38.47  E-value: 3.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91199557  977 KRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYN 1037
Cdd:cd05519   22 KLSELFLEKPSKKLYPDYYVIIKRPIALDQIKRRIEGRAYKSLEEFLEDFHLMFANARTYN 82
AAA_22 pfam13401
AAA domain;
436-559 5.27e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.48  E-value: 5.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    436 IQPPRGCLF-YGPPGTGKTLVARALANECSRGDKRVAFFMRKGADCLS---KWV-------GESERQLRLLFDQAYQ--- 501
Cdd:pfam13401    1 IRFGAGILVlTGESGTGKTTLLRRLLEQLPEVRDSVVFVDLPSGTSPKdllRALlralglpLSGRLSKEELLAALQQlll 80

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557    502 --MRPAIIFFDEIDGLapvrssrqdqiHSSIVSTLLALMDGLDSRGEIVVIGaTNRLDSI 559
Cdd:pfam13401   81 alAVAVVLIIDEAQHL-----------SLEALEELRDLLNLSSKLLQLILVG-TPELREL 128
Bromo_ASH1 cd05525
Bromodomain; ASH1_like sub-family. ASH1 (absent, small, or homeotic 1) is a member of the ...
 991-1063 5.80e-03

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: 37.75  E-value: 5.80e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91199557  991 VPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLKDIDLICSNALEYNPDRDPGDRlirhRACALRDtAYAIIK 1063
Cdd:cd05525   38 NPDYYERITDPVDLSTIEKQILTGYYKTPEAFDSDMLKVFRNAEKYYGRKSPIGR----DVCRLRK-AYYQAK 105
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 443-560 5.91e-03

RecA-like_NTPases; RecA-like NTPases. This superfamily 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: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 38.25  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  443 LFYGPPGTGKTLVARALANECSRGDKRVAFFMrkGADCLskwvgeserqLRLLFDQAYQMRPAIIFFDEIDGLAPVRSSR 522
Cdd:cd01120    2 LITGPPGSGKTTLLLQFAEQALLSDEPVIFIS--FLDTI----------LEAIEDLIEEKKLDIIIIDSLSSLARASQGD 69

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 91199557  523 QDQIHSSIVSTLLALMdgldSRGEIVVIgATNRLDSID 560
Cdd:cd01120   70 RSSELLEDLAKLLRAA----RNTGITVI-ATIHSDKFD 102
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
442-462 6.38e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.50  E-value: 6.38e-03
                          10        20
                  ....*....|....*....|.
gi 91199557   442 CLFYGPPGTGKTLVARALANE 462
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANE 74
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 443-516 7.96e-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: 39.51  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91199557  443 LFYGPPGTGKTLVARALANECSrgdkrVAFFMrkgADCLS----KWVGESERQ--LRLLFDQAYQMRPA---IIFFDEID 513
Cdd:cd19497   54 LLIGPTGSGKTLLAQTLAKILD-----VPFAI---ADATTlteaGYVGEDVENilLKLLQAADYDVERAqrgIVYIDEID 125


                 ...
gi 91199557  514 GLA 516
Cdd:cd19497  126 KIA 128
 
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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