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Conserved domains on  [gi|665399931|ref|NP_001286261|]
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transitional endoplasmic reticulum 94, isoform E [Drosophila melanogaster]

Protein Classification

CDC48 family AAA ATPase( domain architecture ID 1001098)

CDC48 family AAA ATPase is involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus; similar to yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CDC48 super family cl36852
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
47-786 0e+00

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.


The actual alignment was detected with superfamily member TIGR01243:

Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 743.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931   47 RLIVEEAQNDD--NSVVSLSQAKMDELQLFRGDTVILKGKRRKeTVCIVLSddTCPDEK----IRMNRVVRNNLCVHLSD 120
Cdd:TIGR01243   3 ELRVAEAYPRDvgRGIVRIDRQTAARLGVEPGDFVEIEKGDRS-VVAIVWP--LRPDDEgrgiIRMDGYLRANAGVTIGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  121 VVSVQSCpDVKYGKRVRILPideSTEGVTGNLFEIYLKPYFLEayRPIHMGDNFIVRAAMRPIEFKVVLTDPEPYCIVAP 200
Cdd:TIGR01243  80 TVTVERA-EVKEAKKVVLAP---TQPIRFGRDFVDYVKEFLLG--KPISKGETVIVPVLEGALPFVVVSTQPAGFVYVTE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  201 ETVIFCDGDPIkREEEEESLNAVGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAV 280
Cdd:TIGR01243 154 ATEVEIREKPV-REEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  281 ANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKS 360
Cdd:TIGR01243 233 ANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  361 SHLIVMAATNRPNSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEA 440
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  441 ALQQIREKMDL--IDLEDDKIDAEVLASLAVTMENFRYAMTKSSPSALRETVVEVPNTTWTDIGGLESVKKELQELVQYP 518
Cdd:TIGR01243 393 AMAALRRFIREgkINFEAEEIPAEVLKELKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWP 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  519 VEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARSAAPCVLFF 598
Cdd:TIGR01243 473 LKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFF 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  599 DELDSIAKARGGNVGDAggAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDDKSREAI 678
Cdd:TIGR01243 553 DEIDAIAPARGARFDTS--VTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEI 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  679 LKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIRQAIEAEirrEKERAEnqnsAMDDEDDPVPEITSAHF 758
Cdd:TIGR01243 631 FKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSP---AKEKLE----VGEEEFLKDLKVEMRHF 703
                         730       740
                  ....*....|....*....|....*...
gi 665399931  759 EEAMKFARRSVSDNDIRKYEMFAQTLQQ 786
Cdd:TIGR01243 704 LEALKKVKPSVSKEDMLRYERLAKELKR 731
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
47-786 0e+00

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: 743.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931   47 RLIVEEAQNDD--NSVVSLSQAKMDELQLFRGDTVILKGKRRKeTVCIVLSddTCPDEK----IRMNRVVRNNLCVHLSD 120
Cdd:TIGR01243   3 ELRVAEAYPRDvgRGIVRIDRQTAARLGVEPGDFVEIEKGDRS-VVAIVWP--LRPDDEgrgiIRMDGYLRANAGVTIGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  121 VVSVQSCpDVKYGKRVRILPideSTEGVTGNLFEIYLKPYFLEayRPIHMGDNFIVRAAMRPIEFKVVLTDPEPYCIVAP 200
Cdd:TIGR01243  80 TVTVERA-EVKEAKKVVLAP---TQPIRFGRDFVDYVKEFLLG--KPISKGETVIVPVLEGALPFVVVSTQPAGFVYVTE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  201 ETVIFCDGDPIkREEEEESLNAVGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAV 280
Cdd:TIGR01243 154 ATEVEIREKPV-REEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  281 ANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKS 360
Cdd:TIGR01243 233 ANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  361 SHLIVMAATNRPNSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEA 440
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  441 ALQQIREKMDL--IDLEDDKIDAEVLASLAVTMENFRYAMTKSSPSALRETVVEVPNTTWTDIGGLESVKKELQELVQYP 518
Cdd:TIGR01243 393 AMAALRRFIREgkINFEAEEIPAEVLKELKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWP 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  519 VEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARSAAPCVLFF 598
Cdd:TIGR01243 473 LKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFF 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  599 DELDSIAKARGGNVGDAggAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDDKSREAI 678
Cdd:TIGR01243 553 DEIDAIAPARGARFDTS--VTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEI 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  679 LKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIRQAIEAEirrEKERAEnqnsAMDDEDDPVPEITSAHF 758
Cdd:TIGR01243 631 FKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSP---AKEKLE----VGEEEFLKDLKVEMRHF 703
                         730       740
                  ....*....|....*....|....*...
gi 665399931  759 EEAMKFARRSVSDNDIRKYEMFAQTLQQ 786
Cdd:TIGR01243 704 LEALKKVKPSVSKEDMLRYERLAKELKR 731
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
507-667 1.25e-121

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: 362.98  E-value: 1.25e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 507 VKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 586
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 587 KARSAAPCVLFFDELDSIAKARGGNVGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 666
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 665399931 667 I 667
Cdd:cd19528  161 I 161
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
430-738 2.31e-115

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 353.16  E-value: 2.31e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 430 GADLASLCSEAALQQIREKMdLIDLEDDKIDAEVLASLAVTMENFRYAMTKSSPSALRETVV-EVPNTTWTDIGGLESVK 508
Cdd:COG1222    9 ENIKALLALIDALQERLGVE-LALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPaESPDVTFDDIGGLDEQI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 509 KELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 588
Cdd:COG1222   88 EEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 589 RSAAPCVLFFDELDSIAKARGGNvGDaGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIP 668
Cdd:COG1222  168 REKAPSIIFIDEIDAIAARRTDD-GT-SGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 669 LPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIR------------QAIEaEIRREKERA 736
Cdd:COG1222  246 LPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRegrdtvtmedleKAIE-KVKKKTETA 324

                 ..
gi 665399931 737 EN 738
Cdd:COG1222  325 TN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
215-480 2.86e-89

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 287.50  E-value: 2.86e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 215 EEEESLNaVGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGP 294
Cdd:PRK03992 121 EVIESPN-VTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 295 EIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKR--DKTHGEVE-RRIVSQLLTLMDGMKKSSHLIVMAATNR 371
Cdd:PRK03992 200 ELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMDGFDPRGNVKIIAATNR 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 372 PNSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDl 451
Cdd:PRK03992 280 IDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRT- 358
                        250       260
                 ....*....|....*....|....*....
gi 665399931 452 idleddkidaevlaslAVTMENFRYAMTK 480
Cdd:PRK03992 359 ----------------EVTMEDFLKAIEK 371
cell_div_CdvC NF041006
cell division protein CdvC;
462-778 3.04e-59

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 206.12  E-value: 3.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 462 EVLASLAVTMEnfryAMTKSSPSALRETVV-EVPNTTWTDIGGLESVKKELQELVQYPVEHPDKFlkfgmqP---SRGVL 537
Cdd:NF041006  69 EVLEELVPAEP----AGPDVEKESDEELVVkEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF------PlgwPRGIL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 538 FYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARSAA-----PCVLFFDELDSIAKARGGNV 612
Cdd:NF041006 139 LYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEV 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 613 gdaGGAAdRVINQILTEMDGM---GAKKNVFIIGATNRPDIIDPAILRpgRLDQLIYIPLPDDKSREAILKANLRKSPLA 689
Cdd:NF041006 219 ---GGEV-RVRNQFLKEMDGLqdkSENYHVYVIGATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLE 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 690 KEVDLTYIAKVTQGFSGADLTEICQracklairqaiEAEIRREKERAENQnsamddEDDPVPeITSAHFEEAMKFARRSV 769
Cdd:NF041006 293 NDVDLDELAEMTEGYTASDIRDIVQ-----------AAHMRVVKEMFEKG------LGEPRP-ITMEDFKEVLKIRKPSV 354

                 ....*....
gi 665399931 770 SDNDIRKYE 778
Cdd:NF041006 355 NQEMLKAYE 363
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
263-392 1.52e-54

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: 184.33  E-value: 1.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  263 ILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEV 342
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665399931  343 ERRIVSQLLTLMDGMKKSSH-LIVMAATNRPNSIDPALRrfGRFDREIDIG 392
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
532-671 1.86e-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: 88.58  E-value: 1.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931   532 PSRGVLFYGPPGCGKTLLAKAIANECQANFISVK-----------------GPELLTMWFGESEANVRDIFDKARSAAPC 594
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665399931   595 VLFFDELDSIAkarggnvgDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPgRLDQLIYIPLPD 671
Cdd:smart00382  81 VLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
536-570 2.83e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 2.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 665399931 536 VLFYGPPGCGKTLLAKAIANE-CQAN----FISVkgPELL 570
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAaCRQGyrvrFTTA--ADLV 130
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
47-786 0e+00

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: 743.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931   47 RLIVEEAQNDD--NSVVSLSQAKMDELQLFRGDTVILKGKRRKeTVCIVLSddTCPDEK----IRMNRVVRNNLCVHLSD 120
Cdd:TIGR01243   3 ELRVAEAYPRDvgRGIVRIDRQTAARLGVEPGDFVEIEKGDRS-VVAIVWP--LRPDDEgrgiIRMDGYLRANAGVTIGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  121 VVSVQSCpDVKYGKRVRILPideSTEGVTGNLFEIYLKPYFLEayRPIHMGDNFIVRAAMRPIEFKVVLTDPEPYCIVAP 200
Cdd:TIGR01243  80 TVTVERA-EVKEAKKVVLAP---TQPIRFGRDFVDYVKEFLLG--KPISKGETVIVPVLEGALPFVVVSTQPAGFVYVTE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  201 ETVIFCDGDPIkREEEEESLNAVGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAV 280
Cdd:TIGR01243 154 ATEVEIREKPV-REEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAV 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  281 ANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKS 360
Cdd:TIGR01243 233 ANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGR 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  361 SHLIVMAATNRPNSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEA 440
Cdd:TIGR01243 313 GRVIVIGATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEA 392
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  441 ALQQIREKMDL--IDLEDDKIDAEVLASLAVTMENFRYAMTKSSPSALRETVVEVPNTTWTDIGGLESVKKELQELVQYP 518
Cdd:TIGR01243 393 AMAALRRFIREgkINFEAEEIPAEVLKELKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWP 472
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  519 VEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARSAAPCVLFF 598
Cdd:TIGR01243 473 LKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFF 552
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  599 DELDSIAKARGGNVGDAggAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDDKSREAI 678
Cdd:TIGR01243 553 DEIDAIAPARGARFDTS--VTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEI 630
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  679 LKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIRQAIEAEirrEKERAEnqnsAMDDEDDPVPEITSAHF 758
Cdd:TIGR01243 631 FKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSP---AKEKLE----VGEEEFLKDLKVEMRHF 703
                         730       740
                  ....*....|....*....|....*...
gi 665399931  759 EEAMKFARRSVSDNDIRKYEMFAQTLQQ 786
Cdd:TIGR01243 704 LEALKKVKPSVSKEDMLRYERLAKELKR 731
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
507-667 1.25e-121

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: 362.98  E-value: 1.25e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 507 VKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 586
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 587 KARSAAPCVLFFDELDSIAKARGGNVGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 666
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGGNIGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                 .
gi 665399931 667 I 667
Cdd:cd19528  161 I 161
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
227-392 1.38e-115

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: 347.50  E-value: 1.38e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 227 DIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 306
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 307 NLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFD 386
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                 ....*.
gi 665399931 387 REIDIG 392
Cdd:cd19519  161 REIDIG 166
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
430-738 2.31e-115

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 353.16  E-value: 2.31e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 430 GADLASLCSEAALQQIREKMdLIDLEDDKIDAEVLASLAVTMENFRYAMTKSSPSALRETVV-EVPNTTWTDIGGLESVK 508
Cdd:COG1222    9 ENIKALLALIDALQERLGVE-LALLLQPVKALELLEEAPALLLNDANLTQKRLGTPRGTAVPaESPDVTFDDIGGLDEQI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 509 KELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 588
Cdd:COG1222   88 EEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 589 RSAAPCVLFFDELDSIAKARGGNvGDaGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIP 668
Cdd:COG1222  168 REKAPSIIFIDEIDAIAARRTDD-GT-SGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVP 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 669 LPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIR------------QAIEaEIRREKERA 736
Cdd:COG1222  246 LPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRegrdtvtmedleKAIE-KVKKKTETA 324

                 ..
gi 665399931 737 EN 738
Cdd:COG1222  325 TN 326
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
207-456 1.83e-110

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 340.45  E-value: 1.83e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 207 DGDPIKREEEEESLNAVGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGA 286
Cdd:COG1222   59 RLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGA 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 287 FFFLINGPEIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKR--DKTHGEVeRRIVSQLLTLMDGMKKSSHLI 364
Cdd:COG1222  139 PFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRtdDGTSGEV-QRTVNQLLAELDGFESRGDVL 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 365 VMAATNRPNSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQ 444
Cdd:COG1222  218 IIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFA 297
                        250
                 ....*....|..
gi 665399931 445 IREKMDLIDLED 456
Cdd:COG1222  298 IREGRDTVTMED 309
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
227-391 7.63e-102

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: 311.92  E-value: 7.63e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 227 DIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 306
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 307 NLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFD 386
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                 ....*
gi 665399931 387 REIDI 391
Cdd:cd19503  161 REVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
507-667 3.03e-97

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: 299.58  E-value: 3.03e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 507 VKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 586
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 587 KARSAAPCVLFFDELDSIAKARGGNvgDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 666
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQS--DSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIY 158

                 .
gi 665399931 667 I 667
Cdd:cd19511  159 V 159
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
343-738 5.99e-94

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: 299.90  E-value: 5.99e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 343 ERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIA 422
Cdd:COG0464    1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 423 AESHGHVGADLASLCSEAALQQIREKMDLIDLEDDKIDAEVLASLAVTMENFRYAMTKSSPSALRETVVEVPNTTWTDIG 502
Cdd:COG0464   81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 503 GLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVR 582
Cdd:COG0464  161 GLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 583 DIFDKARSAAPCVLFFDELDSIAKARGgnvGDAGGAADRVINQILTEMDGMgaKKNVFIIGATNRPDIIDPAILRpgRLD 662
Cdd:COG0464  241 EVFDKARGLAPCVLFIDEADALAGKRG---EVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--RFD 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 663 QLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIRQA--------IEAEIRREKE 734
Cdd:COG0464  314 EIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGrepvttedLLEALEREDI 393

                 ....
gi 665399931 735 RAEN 738
Cdd:COG0464  394 FLKR 397
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
215-480 2.86e-89

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 287.50  E-value: 2.86e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 215 EEEESLNaVGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGP 294
Cdd:PRK03992 121 EVIESPN-VTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGS 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 295 EIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKR--DKTHGEVE-RRIVSQLLTLMDGMKKSSHLIVMAATNR 371
Cdd:PRK03992 200 ELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMDGFDPRGNVKIIAATNR 279
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 372 PNSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDl 451
Cdd:PRK03992 280 IDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRDDRT- 358
                        250       260
                 ....*....|....*....|....*....
gi 665399931 452 idleddkidaevlaslAVTMENFRYAMTK 480
Cdd:PRK03992 359 ----------------EVTMEDFLKAIEK 371
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
490-743 1.26e-87

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 282.88  E-value: 1.26e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 490 VVEVPNTTWTDIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPEL 569
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSEL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 570 LTMWFGESEANVRDIFDKARSAAPCVLFFDELDSIAKARggnvGDAGGAADRVIN----QILTEMDGMGAKKNVFIIGAT 645
Cdd:PRK03992 202 VQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR----TDSGTSGDREVQrtlmQLLAEMDGFDPRGNVKIIAAT 277
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 646 NRPDIIDPAILRPGRLDQLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIR--- 722
Cdd:PRK03992 278 NRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRddr 357
                        250       260       270
                 ....*....|....*....|....*....|
gi 665399931 723 ---------QAIEAEIRREKERAENQNSAM 743
Cdd:PRK03992 358 tevtmedflKAIEKVMGKEEKDSMEEPGVM 387
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
214-456 5.12e-85

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: 276.41  E-value: 5.12e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 214 EEEEESLNAVGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLING 293
Cdd:COG0464  145 EEELLELREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDL 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 294 PEIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGmkKSSHLIVMAATNRPN 373
Cdd:COG0464  225 SDLVSKYVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEE--LRSDVVVIAATNRPD 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 374 SIDPALRRfgRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDLID 453
Cdd:COG0464  303 LLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVT 380

                 ...
gi 665399931 454 LED 456
Cdd:COG0464  381 TED 383
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
492-776 4.32e-77

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: 258.37  E-value: 4.32e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  492 EVPNTTWTDIGGLESVKKELQELVQYpVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLT 571
Cdd:TIGR01241  48 EKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVE 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  572 MWFGESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDII 651
Cdd:TIGR01241 127 MFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVL 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  652 DPAILRPGRLDQLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIRQaieaeirr 731
Cdd:TIGR01241 207 DPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARK-------- 278
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 665399931  732 ekeraeNQnsamddeddpvPEITSAHFEEA-----MKFARRSVSDNDIRK 776
Cdd:TIGR01241 279 ------NK-----------TEITMNDIEEAidrviAGPEKKSRVISEKEK 311
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
494-761 1.12e-76

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 259.97  E-value: 1.12e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 494 PNTTWTDIGGLESVKKELQELVQYpVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMW 573
Cdd:COG0465  137 PKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 574 FGESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGdaGGAADR--VINQILTEMDGMGAKKNVFIIGATNRPDII 651
Cdd:COG0465  216 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLG--GGHDEReqTLNQLLVEMDGFEGNEGVIVIAATNRPDVL 293
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 652 DPAILRPGRLDQLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRAcklAIRQAieaeiRR 731
Cdd:COG0465  294 DPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEA---ALLAA-----RR 365
                        250       260       270
                 ....*....|....*....|....*....|
gi 665399931 732 EKEraenqnsamddeddpvpEITSAHFEEA 761
Cdd:COG0465  366 NKK-----------------AVTMEDFEEA 378
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
507-667 4.08e-75

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: 241.25  E-value: 4.08e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 507 VKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 586
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 587 KARSAAPCVLFFDELDSIAKARGGNvGDAgGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 666
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTT-GDS-GVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158

                 .
gi 665399931 667 I 667
Cdd:cd19529  159 I 159
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
504-667 8.63e-73

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: 235.07  E-value: 8.63e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 504 LESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRD 583
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 584 IFDKARSAAPCVLFFDELDSIAKARGGNvgdAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQ 663
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDG---GSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157

                 ....
gi 665399931 664 LIYI 667
Cdd:cd19530  158 TLYV 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
217-456 1.17e-72

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: 246.43  E-value: 1.17e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  217 EESLNAVGYDDIGGCRKQLAQIKEMVELpLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEI 296
Cdd:TIGR01241  46 NEEKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDF 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  297 MSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDK----THGEVERRIvSQLLTLMDGMKKSSHLIVMAATNRP 372
Cdd:TIGR01241 125 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAglggGNDEREQTL-NQLLVEMDGFGTNTGVIVIAATNRP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  373 NSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDLI 452
Cdd:TIGR01241 204 DVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEI 283

                  ....
gi 665399931  453 DLED 456
Cdd:TIGR01241 284 TMND 287
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
507-667 1.82e-72

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: 234.33  E-value: 1.82e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 507 VKKELQELVQYPVEHPDKFLKfGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 586
Cdd:cd19527    1 VKKEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 587 KARSAAPCVLFFDELDSIAKARgGNVGDAGGAADRVINQILTEMDGM-GAKKNVFIIGATNRPDIIDPAILRPGRLDQLI 665
Cdd:cd19527   80 KARDAKPCVIFFDELDSLAPSR-GNSGDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFDKLL 158

                 ..
gi 665399931 666 YI 667
Cdd:cd19527  159 YL 160
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
223-459 2.44e-72

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 248.03  E-value: 2.44e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 223 VGYDDIGGCRKQLAQIKEMVELpLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAG 302
Cdd:COG0465  139 VTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 303 ESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEV--ER-RIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPAL 379
Cdd:COG0465  218 VGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGhdEReQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPAL 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 380 RRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDLIDLED--- 456
Cdd:COG0465  298 LRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTMEDfee 377

                 ....*
gi 665399931 457 --DKI 459
Cdd:COG0465  378 aiDRV 382
ftsH CHL00176
cell division protein; Validated
497-735 1.50e-70

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 244.57  E-value: 1.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 497 TWTDIGGLESVKKELQELVQYpVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGE 576
Cdd:CHL00176 181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 577 SEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAIL 656
Cdd:CHL00176 260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALL 339
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 657 RPGRLDQLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIRQAIEA----EIRRE 732
Cdd:CHL00176 340 RPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATitmkEIDTA 419

                 ...
gi 665399931 733 KER 735
Cdd:CHL00176 420 IDR 422
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
500-667 5.26e-69

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: 225.25  E-value: 5.26e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 500 DIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEA 579
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 580 NVRDIFDKARSAAPCVLFFDELDSIAKARGgnvGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPG 659
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKRE---EDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPG 157

                 ....*...
gi 665399931 660 RLDQLIYI 667
Cdd:cd19503  158 RFDREVEI 165
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
227-389 1.53e-68

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: 223.82  E-value: 1.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 227 DIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 306
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 307 NLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMK----KSSHLIVMAATNRPNSIDPALRRF 382
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPALRRA 160

                 ....*..
gi 665399931 383 GRFDREI 389
Cdd:cd19518  161 GRFDREI 167
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
498-749 2.16e-68

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 226.69  E-value: 2.16e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 498 WTDIGGLESVKKELQELVQYpVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGES 577
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKE-LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 578 EANVRDIFDKARSaAPCVLFFDELDSIAKARGGN--VGDAGgaadRVINQILTEMDGMgaKKNVFIIGATNRPDIIDPAI 655
Cdd:COG1223   80 ARNLRKLFDFARR-APCVIFFDEFDAIAKDRGDQndVGEVK----RVVNALLQELDGL--PSGSVVIAATNHPELLDSAL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 656 LRpgRLDQLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIRQAIEAEIRREKER 735
Cdd:COG1223  153 WR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKEDLEE 230
                        250
                 ....*....|....
gi 665399931 736 AENQNSAMDDEDDP 749
Cdd:COG1223  231 ALKQRKERKKEPKK 244
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
225-486 7.86e-68

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 231.58  E-value: 7.86e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 225 YDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGES 304
Cdd:PTZ00361 182 YADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 305 ESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTH--GEVE-RRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRR 381
Cdd:PTZ00361 262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATsgGEKEiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 382 FGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDLIDLEDdkida 461
Cdd:PTZ00361 342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRERRMKVTQAD----- 416
                        250       260
                 ....*....|....*....|....*
gi 665399931 462 evlasLAVTMENFRYAMTKSSPSAL 486
Cdd:PTZ00361 417 -----FRKAKEKVLYRKKGNIPEGL 436
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
507-666 1.72e-67

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: 220.76  E-value: 1.72e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 507 VKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 586
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 587 KARSAAPCVLFFDELDSIAKARGgnvGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 666
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRG---HDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
223-446 6.50e-67

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 227.72  E-value: 6.50e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 223 VGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAG 302
Cdd:PTZ00454 142 VTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLG 221
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 303 ESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKR-DKTHG---EVErRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPA 378
Cdd:PTZ00454 222 EGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfDAQTGadrEVQ-RILLELLNQMDGFDQTTNVKVIMATNRADTLDPA 300
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399931 379 LRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIR 446
Cdd:PTZ00454 301 LLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVR 368
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
237-389 1.68e-66

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: 217.92  E-value: 1.68e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 237 QIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAE 316
Cdd:cd19511    4 ELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKAR 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665399931 317 KNSPAIIFIDEIDAIAPKRDKTHG-EVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREI 389
Cdd:cd19511   84 QAAPCIIFFDEIDSLAPRRGQSDSsGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
480-797 7.23e-66

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 231.85  E-value: 7.23e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 480 KSSPSALRETVVEvpnTTWTDIGGLESVKKELQELVQYpVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQA 559
Cdd:PRK10733 136 KSKARMLTEDQIK---TTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 560 NFISVKGPELLTMWFGESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDAGGAADRVINQILTEMDGMGAKKNV 639
Cdd:PRK10733 212 PFFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGI 291
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 640 FIIGATNRPDIIDPAILRPGRLDQLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKL 719
Cdd:PRK10733 292 IVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALF 371
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 720 AIR--QAIEAEIRREKER------AENQNSAMDDEDDPvpeiTSAHFEEAMKFARRSVSDND-IRKYEMfaqtLQQSRGF 790
Cdd:PRK10733 372 AARgnKRVVSMVEFEKAKdkimmgAERRSMVMTEAQKE----STAYHEAGHAIIGRLVPEHDpVHKVTI----IPRGRAL 443

                 ....*..
gi 665399931 791 GQNFRFP 797
Cdd:PRK10733 444 GVTFFLP 450
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
496-667 1.12e-65

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: 216.33  E-value: 1.12e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 496 TTWTDIGGLESVKKELQELVQYpVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFG 575
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 576 ESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAI 655
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|..
gi 665399931 656 LRPGRLDQLIYI 667
Cdd:cd19501  160 LRPGRFDRQVYV 171
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
492-723 1.57e-64

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 221.56  E-value: 1.57e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 492 EVPNTTWTDIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLT 571
Cdd:PTZ00454 138 EKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQ 217
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 572 MWFGESEANVRDIFDKARSAAPCVLFFDELDSIAKARggnvGDAGGAADRVINQILTE----MDGMGAKKNVFIIGATNR 647
Cdd:PTZ00454 218 KYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKR----FDAQTGADREVQRILLEllnqMDGFDQTTNVKVIMATNR 293
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665399931 648 PDIIDPAILRPGRLDQLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIRQ 723
Cdd:PTZ00454 294 ADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
225-391 3.81e-64

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: 212.20  E-value: 3.81e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 225 YDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGES 304
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 305 ESNLRKAFEEAEKNSPAIIFIDEIDAIAPKR--DKTHGEVE-RRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRR 381
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLR 161
                        170
                 ....*....|
gi 665399931 382 FGRFDREIDI 391
Cdd:cd19502  162 PGRFDRKIEF 171
ftsH CHL00176
cell division protein; Validated
222-461 2.44e-63

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 224.54  E-value: 2.44e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 222 AVGYDDIGGCRKQLAQIKEMVELpLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLA 301
Cdd:CHL00176 179 GITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 302 GESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDK----THGEVERrIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDP 377
Cdd:CHL00176 258 GVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAgiggGNDEREQ-TLNQLLTEMDGFKGNKGVIVIAATNRVDILDA 336
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 378 ALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREK-----MDLI 452
Cdd:CHL00176 337 ALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKkatitMKEI 416

                 ....*....
gi 665399931 453 DLEDDKIDA 461
Cdd:CHL00176 417 DTAIDRVIA 425
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
507-667 2.55e-63

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: 209.45  E-value: 2.55e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 507 VKKELQELVQYPVEHPdKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 586
Cdd:cd19481    1 LKASLREAVEAPRRGS-RLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 587 KARSAAPCVLFFDELDSIAKARGGNVGDagGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 666
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKRDSSGES--GELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIE 157

                 .
gi 665399931 667 I 667
Cdd:cd19481  158 F 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
237-391 2.68e-63

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: 209.66  E-value: 2.68e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 237 QIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAE 316
Cdd:cd19529    4 ELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKAR 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665399931 317 KNSPAIIFIDEIDAIAPKRDKTHGE-VERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREIDI 391
Cdd:cd19529   84 QVAPCVIFFDEIDSIAPRRGTTGDSgVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
497-665 4.37e-62

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: 206.80  E-value: 4.37e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 497 TWTDIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGE 576
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 577 SEANVRDIFDKARSAAPCVLFFDELDSIAKARggnvGDAGGAADRVIN----QILTEMDGMGAKKNVFIIGATNRPDIID 652
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKR----FDSGTGGDREVQrtmlELLNQLDGFDPRGNIKVIMATNRPDILD 156
                        170
                 ....*....|...
gi 665399931 653 PAILRPGRLDQLI 665
Cdd:cd19502  157 PALLRPGRFDRKI 169
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
475-746 2.15e-61

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: 216.11  E-value: 2.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  475 RYAMTKSSPSALRETVV-EVPNTTWTDIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAI 553
Cdd:TIGR03689 157 GYAFEAIPRTEVEDLVLeEVPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAV 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  554 ANE-CQ---------ANFISVKGPELLTMWFGESEANVRDIFDKARSAA----PCVLFFDELDSIAKARGGNVgdAGGAA 619
Cdd:TIGR03689 237 ANSlAArigaegggkSYFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGV--SSDVE 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  620 DRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIYIPLPDDKSREAILKANLRKS-PLAKE------- 691
Cdd:TIGR03689 315 TTVVPQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLTDDlPLPEDlaahdgd 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  692 -------------------------VDLTYIAKVTQGF------SGADLTEICQRACKLAIRQAIEAeiRREKERAENQN 740
Cdd:TIGR03689 395 reataaaliqrvvdalyarseanryVEVTYANGSTEVLyfadfvSGAMLANIVDRAKKRAIKDHITG--GQVGLRAEHLL 472

                  ....*.
gi 665399931  741 SAMDDE 746
Cdd:TIGR03689 473 AAVEDE 478
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
234-391 7.46e-60

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: 200.20  E-value: 7.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 234 QLAQIKEMVELPLRHPSLFKAiGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFE 313
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399931 314 EAEKNSPAIIFIDEIDAIAPKRDKT-HGEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREIDI 391
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
232-456 8.28e-60

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 203.19  E-value: 8.28e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 232 RKQLAQIKEMvelpLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKA 311
Cdd:COG1223   11 KKKLKLIIKE----LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 312 FEEAEKNsPAIIFIDEIDAIAPKRDKTH--GEVeRRIVSQLLTLMDGMKksSHLIVMAATNRPNSIDPALRRfgRFDREI 389
Cdd:COG1223   87 FDFARRA-PCVIFFDEFDAIAKDRGDQNdvGEV-KRVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR--RFDEVI 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665399931 390 DIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDLIDLED 456
Cdd:COG1223  161 EFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDREKVTKED 227
cell_div_CdvC NF041006
cell division protein CdvC;
462-778 3.04e-59

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 206.12  E-value: 3.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 462 EVLASLAVTMEnfryAMTKSSPSALRETVV-EVPNTTWTDIGGLESVKKELQELVQYPVEHPDKFlkfgmqP---SRGVL 537
Cdd:NF041006  69 EVLEELVPAEP----AGPDVEKESDEELVVkEKPKVTFSDIVGLEDVKEALKEAIVYPSKRPDLF------PlgwPRGIL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 538 FYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARSAA-----PCVLFFDELDSIAKARGGNV 612
Cdd:NF041006 139 LYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALLGVYSSEV 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 613 gdaGGAAdRVINQILTEMDGM---GAKKNVFIIGATNRPDIIDPAILRpgRLDQLIYIPLPDDKSREAILKANLRKSPLA 689
Cdd:NF041006 219 ---GGEV-RVRNQFLKEMDGLqdkSENYHVYVIGATNKPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTSKIKLE 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 690 KEVDLTYIAKVTQGFSGADLTEICQracklairqaiEAEIRREKERAENQnsamddEDDPVPeITSAHFEEAMKFARRSV 769
Cdd:NF041006 293 NDVDLDELAEMTEGYTASDIRDIVQ-----------AAHMRVVKEMFEKG------LGEPRP-ITMEDFKEVLKIRKPSV 354

                 ....*....
gi 665399931 770 SDNDIRKYE 778
Cdd:NF041006 355 NQEMLKAYE 363
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
500-668 1.10e-57

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: 194.58  E-value: 1.10e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 500 DIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEA 579
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 580 NVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDaggAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPG 659
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGE---VERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFG 157

                 ....*....
gi 665399931 660 RLDQLIYIP 668
Cdd:cd19519  158 RFDREIDIG 166
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
225-446 3.50e-57

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 207.58  E-value: 3.50e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 225 YDDIGGCRKQLAQIKEMVELpLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGES 304
Cdd:PRK10733 151 FADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 305 ESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDK----THGEVERRIvSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALR 380
Cdd:PRK10733 230 ASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAglggGHDEREQTL-NQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665399931 381 RFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIR 446
Cdd:PRK10733 309 RPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAAR 374
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
223-391 6.82e-57

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: 192.45  E-value: 6.82e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 223 VGYDDIGGCRKQLAQIKEMVELpLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAG 302
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 303 ESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDK----THGEVERRIvSQLLTLMDGMKKSSHLIVMAATNRPNSIDPA 378
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAglggGHDEREQTL-NQLLVEMDGFESNTGVIVIAATNRPDVLDPA 158
                        170
                 ....*....|...
gi 665399931 379 LRRFGRFDREIDI 391
Cdd:cd19501  159 LLRPGRFDRQVYV 171
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
227-388 1.57e-56

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: 191.57  E-value: 1.57e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 227 DIGGCRKQLAQIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGA-----FFFLINGPEIMSKLA 301
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 302 GESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRR 381
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                 ....*..
gi 665399931 382 FGRFDRE 388
Cdd:cd19517  161 PGRFDRE 167
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
500-665 9.32e-55

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: 186.46  E-value: 9.32e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 500 DIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEA 579
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 580 NVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDaggAADRVINQILTEMDGMGAKKN----VFIIGATNRPDIIDPAI 655
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQRE---MERRIVSQLLTCMDELNNEKTaggpVLVIGATNRPDSLDPAL 157
                        170
                 ....*....|
gi 665399931 656 LRPGRLDQLI 665
Cdd:cd19518  158 RRAGRFDREI 167
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
490-736 1.37e-54

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 194.99  E-value: 1.37e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 490 VVEVPNTTWTDIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPEL 569
Cdd:PTZ00361 174 VDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSEL 253
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 570 LTMWFGESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNvgDAGGAAD--RVINQILTEMDGMGAKKNVFIIGATNR 647
Cdd:PTZ00361 254 IQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDA--TSGGEKEiqRTMLELLNQLDGFDSRGDVKVIMATNR 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 648 PDIIDPAILRPGRLDQLIYIPLPDDKSREAILKANLRKSPLAKEVDLTYIAKVTQGFSGADLTEICQRACKLAIR----Q 723
Cdd:PTZ00361 332 IESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRerrmK 411
                        250
                 ....*....|...
gi 665399931 724 AIEAEIRREKERA 736
Cdd:PTZ00361 412 VTQADFRKAKEKV 424
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
263-392 1.52e-54

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: 184.33  E-value: 1.52e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  263 ILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEV 342
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 665399931  343 ERRIVSQLLTLMDGMKKSSH-LIVMAATNRPNSIDPALRrfGRFDREIDIG 392
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
536-669 1.93e-53

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: 181.25  E-value: 1.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  536 VLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNvgdA 615
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG---G 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 665399931  616 GGAADRVINQILTEMDGMGAKK-NVFIIGATNRPDIIDPAILrpGRLDQLIYIPL 669
Cdd:pfam00004  78 DSESRRVVNQLLTELDGFTSSNsKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
245-387 6.95e-52

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: 178.45  E-value: 6.95e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 245 PLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNSPAIIF 324
Cdd:cd19530   15 PIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIF 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665399931 325 IDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDR 387
Cdd:cd19530   95 FDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
228-391 8.72e-52

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: 177.93  E-value: 8.72e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 228 IGGCRKQLAQIKEMVELPLRHPSLFKAIgVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESN 307
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGL-RGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 308 LRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGM--KKSSHLIVMAATNRPNSIDPALRRfgRF 385
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVlnKPEDRVLVLGATNRPWELDEAFLR--RF 157

                 ....*.
gi 665399931 386 DREIDI 391
Cdd:cd19509  158 EKRIYI 163
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
501-667 1.69e-51

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: 177.16  E-value: 1.69e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 501 IGGLESVKKELQELVQYPVEHPDKFlKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEAN 580
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 581 VRDIFDKARSAAPCVLFFDELDSIAKARGGnvGDAGGAAdRVINQILTEMDGMGAKKN--VFIIGATNRPDIIDPAILRp 658
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGS--GEHEASR-RVKTEFLVQMDGVLNKPEdrVLVLGATNRPWELDEAFLR- 155

                 ....*....
gi 665399931 659 gRLDQLIYI 667
Cdd:cd19509  156 -RFEKRIYI 163
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
237-391 2.38e-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: 176.93  E-value: 2.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 237 QIKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAE 316
Cdd:cd19528    4 ELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKAR 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399931 317 KNSPAIIFIDEIDAIAPKRDKTHGE---VERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREIDI 391
Cdd:cd19528   84 AAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
238-389 3.07e-47

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: 165.29  E-value: 3.07e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 238 IKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAEK 317
Cdd:cd19526    5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 665399931 318 NSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREI 389
Cdd:cd19526   85 AKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
237-387 1.18e-45

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: 160.76  E-value: 1.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 237 QIKEMVELPLRHPSLFkAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESNLRKAFEEAE 316
Cdd:cd19527    4 EILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKAR 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665399931 317 KNSPAIIFIDEIDAIAPKRDKT--HGEVERRIVSQLLTLMDGMKKSSH-LIVMAATNRPNSIDPALRRFGRFDR 387
Cdd:cd19527   83 DAKPCVIFFDELDSLAPSRGNSgdSGGVMDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
500-666 3.07e-45

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: 159.98  E-value: 3.07e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 500 DIGGLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANEC-----QANFISVKGPELLTMWF 574
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECskggqKVSFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 575 GESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDAGGAadrVINQILTEMDGMGAKKNVFIIGATNRPDIIDPA 654
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHAS---IVSTLLALMDGLDNRGQVVVIGATNRPDALDPA 157
                        170
                 ....*....|..
gi 665399931 655 ILRPGRLDQLIY 666
Cdd:cd19517  158 LRRPGRFDREFY 169
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
494-667 1.07e-42

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: 152.71  E-value: 1.07e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 494 PNTTWTDIGGLESVKKELQELVQYPVEHPDKFlKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMW 573
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLF-TGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 574 FGESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDaggAADRVINQILTEMDGMGAKKN-VFIIGATNRPDIID 652
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESE---ASRRIKTELLVQMNGVGNDSQgVLVLGATNIPWQLD 157
                        170
                 ....*....|....*
gi 665399931 653 PAILRpgRLDQLIYI 667
Cdd:cd19521  158 SAIRR--RFEKRIYI 170
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
223-391 1.78e-42

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: 152.32  E-value: 1.78e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 223 VGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAiGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAG 302
Cdd:cd19521    4 VKWEDVAGLEGAKEALKEAVILPVKFPHLFTG-NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 303 ESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGM-KKSSHLIVMAATNRPNSIDPALRR 381
Cdd:cd19521   83 ESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSAIRR 162
                        170
                 ....*....|
gi 665399931 382 fgRFDREIDI 391
Cdd:cd19521  163 --RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
227-381 2.22e-42

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: 151.81  E-value: 2.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 227 DIGGCRKQLAQIKEMVELPLRHPSLFKAIGV-KPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESE 305
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399931 306 SNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSSH--LIVMAATNRPNSIDPALRR 381
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEAILR 158
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
500-657 2.98e-42

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: 151.42  E-value: 2.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 500 DIGGLESVKKELQELVQYPVEHPDKFLKFGM-QPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESE 578
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 579 ANVRDIFDKARSAAPCVLFFDELDSIAKARggNVGDAGGAAdRVINQILTEMDGMGAKKN--VFIIGATNRPDIIDPAIL 656
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQR--SSTDHEATA-MMKAEFMSLWDGLSTDGNcrVIVMGATNRPQDLDEAIL 157

                 .
gi 665399931 657 R 657
Cdd:cd19520  158 R 158
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
221-391 7.35e-42

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: 151.29  E-value: 7.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 221 NAVGYDDIGGCRKQLAQIKEMVELPLRHPSLFKAIGvKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKL 300
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLR-GPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 301 AGESESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSS--HLIVMAATNRPNSIDPA 378
Cdd:cd19525   96 VGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSedRILVVGATNRPQEIDEA 175
                        170
                 ....*....|...
gi 665399931 379 LRRfgRFDREIDI 391
Cdd:cd19525  176 ARR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
500-667 4.18e-40

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: 145.51  E-value: 4.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 500 DIGGLESVKKELQELVQYPVEHPDkFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEA 579
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPE-FFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 580 NVRDIFDKARSAAPCVLFFDELDSIAKARGGnvGDAGGAADRVINQILTEMDGMG-------AKKNVFIIGATNRPDIID 652
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGT--SEEHEASRRVKSELLVQMDGVGgasenddPSKMVMVLAATNFPWDID 157
                        170
                 ....*....|....*
gi 665399931 653 PAILRpgRLDQLIYI 667
Cdd:cd19522  158 EALRR--RLEKRIYI 170
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
227-391 1.16e-38

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: 141.28  E-value: 1.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 227 DIGGCRKQLAQIKEMVELPLRHPSLFKAIGvKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 306
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 307 NLRKAFEEAEKNSPAIIFIDEIDAIAPKR-DKTHGEVERRIVSQLLTLMDGM-------KKSSHLIVMAATNRPNSIDPA 378
Cdd:cd19522   80 LVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDEA 159
                        170
                 ....*....|...
gi 665399931 379 LRRfgRFDREIDI 391
Cdd:cd19522  160 LRR--RLEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
494-667 2.40e-37

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: 138.20  E-value: 2.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 494 PNTTWTDIGGLESVKKELQELVQYPVEHPDKFLkfGMQ-PSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTM 572
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIFT--GLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 573 WFGESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDaggAADRVINQILTEMDGM--GAKKNVFIIGATNRPDI 650
Cdd:cd19525   95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHE---SSRRIKTEFLVQLDGAttSSEDRILVVGATNRPQE 171
                        170
                 ....*....|....*..
gi 665399931 651 IDPAILRpgRLDQLIYI 667
Cdd:cd19525  172 IDEAARR--RLVKRLYI 186
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
501-662 3.16e-37

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: 137.62  E-value: 3.16e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 501 IGGLEsvkKELQELVQYP----VEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFIS-VKGPELLTMWFG 575
Cdd:cd19504    2 IGGLD---KEFSDIFRRAfasrVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKiVNGPEILNKYVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 576 ESEANVRDIF--------DKARSAAPCVLFFDELDSIAKARGgNVGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNR 647
Cdd:cd19504   79 ESEANIRKLFadaeeeqrRLGANSGLHIIIFDEIDAICKQRG-SMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNR 157
                        170
                 ....*....|....*
gi 665399931 648 PDIIDPAILRPGRLD 662
Cdd:cd19504  158 KDLIDEALLRPGRLE 172
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
500-667 3.69e-35

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: 131.13  E-value: 3.69e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 500 DIGGLESVKKELQELVQYPVEHPDKFLkfGMQ-PSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESE 578
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 579 ANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDaggAADRVINQILTEMDGM--GAKKNVFIIGATNRPDIIDPAIL 656
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHE---ASRRLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVL 155
                        170
                 ....*....|.
gi 665399931 657 RpgRLDQLIYI 667
Cdd:cd19524  156 R--RFTKRVYV 164
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
227-382 1.85e-34

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: 129.20  E-value: 1.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 227 DIGGCRKQLAQIKEMVELPLRHPSLFKAIGvKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 306
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLR-APARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399931 307 NLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSS--HLIVMAATNRPNSIDPA-LRRF 382
Cdd:cd19524   80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGddRVLVMGATNRPQELDDAvLRRF 158
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
249-391 4.05e-34

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 128.76  E-value: 4.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 249 PSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFF-FLINGPEIMSKLAGESESNLRKAFEEAEKNSPA------ 321
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREpKIVNGPEILNKYVGESEANIRKLFADAEEEQRRlgansg 103
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665399931 322 --IIFIDEIDAIAPKRDKTHGE--VERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREIDI 391
Cdd:cd19504  104 lhIIIFDEIDAICKQRGSMAGStgVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
227-382 1.12e-30

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: 118.45  E-value: 1.12e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 227 DIGGCRKQLAQIKEMVELPLRHPSLFKAIgVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 306
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399931 307 NLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVErRIVSQLLTLMDGMKKSS--HLIVMAATNRPNSIDPALRRF 382
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVLGSGedGVLVVCTTSKPEEIDESLRRY 156
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
502-669 6.54e-30

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: 115.71  E-value: 6.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 502 GGLESVKKELQELVQYPvehpdkflkfgmqPSRGVLFYGPPGCGKTLLAKAIANEC---QANFISVKGPELLTMWFGESE 578
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 579 AN---VRDIFDKARSAAPCVLFFDELDSIAKarggnvgdagGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAI 655
Cdd:cd00009   68 FGhflVRLLFELAEKAKPGVLFIDEIDSLSR----------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDR 137
                        170
                 ....*....|....
gi 665399931 656 LRPGRLDQLIYIPL 669
Cdd:cd00009  138 ALYDRLDIRIVIPL 151
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
229-392 8.10e-30

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: 115.32  E-value: 8.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 229 GGCRKQLAQIKEMVELPlrhpslfkaigvkPPRGILMYGPPGTGKTLIARAVANET---GAFFFLINGPEIMSKLAGESE 305
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 306 ---SNLRKAFEEAEKNSPAIIFIDEIDAIAPkrdkthgEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRF 382
Cdd:cd00009   68 fghFLVRLLFELAEKAKPGVLFIDEIDSLSR-------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALY 140
                        170
                 ....*....|
gi 665399931 383 GRFDREIDIG 392
Cdd:cd00009  141 DRLDIRIVIP 150
ycf46 CHL00195
Ycf46; Provisional
494-725 1.15e-27

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 117.81  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 494 PNTTWTDIGGLESVKKELQelvQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMW 573
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLK---KRSTSFSKQASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGI 299
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 574 FGESEANVRDIFDKARSAAPCVLFFDELDSiAKARGGNVGDaGGAADRVINQILTEMDGmgAKKNVFIIGATNRPDIIDP 653
Cdd:CHL00195 300 VGESESRMRQMIRIAEALSPCILWIDEIDK-AFSNSESKGD-SGTTNRVLATFITWLSE--KKSPVFVVATANNIDLLPL 375
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665399931 654 AILRPGRLDQLIYIPLPDDKSREAILKANLRKS-PLA-KEVDLTYIAKVTQGFSGADlteicqracklaIRQAI 725
Cdd:CHL00195 376 EILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFrPKSwKKYDIKKLSKLSNKFSGAE------------IEQSI 437
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
227-387 7.18e-27

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: 107.45  E-value: 7.18e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 227 DIGGcrkqLAQIKEMveLPLRHPSLFK---AIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGE 303
Cdd:cd19507    1 DVGG----LDNLKDW--LKKRKAAFSKqasAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 304 SESNLRKAFEEAEKNSPAIIFIDEID-AIAPKRDKTHGEVERRIVSQLLTLMDgmKKSSHLIVMAATNRPNSIDPALRRF 382
Cdd:cd19507   75 SESRLRQMIQTAEAIAPCVLWIDEIEkGFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRK 152

                 ....*
gi 665399931 383 GRFDR 387
Cdd:cd19507  153 GRFDE 157
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
500-667 6.51e-26

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: 104.76  E-value: 6.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 500 DIGGLESVKKELQElvQYPVEHPDKFlKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEA 579
Cdd:cd19507    1 DVGGLDNLKDWLKK--RKAAFSKQAS-AYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 580 NVRDIFDKARSAAPCVLFFDELDSiAKARGGNVGDaGGAADRVINQILTEMDgmGAKKNVFIIGATNRPDIIDPAILRPG 659
Cdd:cd19507   78 RLRQMIQTAEAIAPCVLWIDEIEK-GFSNADSKGD-SGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKG 153

                 ....*...
gi 665399931 660 RLDQLIYI 667
Cdd:cd19507  154 RFDEIFFV 161
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
500-657 4.23e-24

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: 99.57  E-value: 4.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 500 DIGGLESVKKELQELVQYPVEHPDKFLKFgMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEA 579
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 580 NVRDIFDKARSAAPCVLFFDELDSIAKARggnvGDAGGAADRVINQILTEMDGM--GAKKNVFIIGATNRPDIIDPAILR 657
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQ----DDEASPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
CDC48_N pfam02359
Cell division protein 48 (CDC48), N-terminal domain; This domain has a double psi-beta barrel ...
47-129 2.81e-22

Cell division protein 48 (CDC48), N-terminal domain; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the N-terminus. The VAT-N domain found in AAA ATPases pfam00004 is a substrate 185-residue recognition domain.


Pssm-ID: 426738  Cd Length: 85  Bit Score: 91.49  E-value: 2.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931   47 RLIVEEAQNDD--NSVVSLSQAKMDELQLFRGDTVILKGKRRkeTVCIVLSDDTCPD--EKIRMNRVVRNNLCVHLSDVV 122
Cdd:pfam02359   1 RLRVAEAPDRDvgRGIARLNPEDMEELGLFPGDVVEIKGKRK--TVAIVWSAYPEDEgpGIIRMDGVTRKNAGVSIGDTV 78

                  ....*..
gi 665399931  123 SVQSCPD 129
Cdd:pfam02359  79 TVRPAEV 85
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
532-671 1.86e-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: 88.58  E-value: 1.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931   532 PSRGVLFYGPPGCGKTLLAKAIANECQANFISVK-----------------GPELLTMWFGESEANVRDIFDKARSAAPC 594
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 665399931   595 VLFFDELDSIAkarggnvgDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPgRLDQLIYIPLPD 671
Cdd:smart00382  81 VLILDEITSLL--------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
259-395 4.24e-20

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 87.43  E-value: 4.24e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931   259 PPRGILMYGPPGTGKTLIARAVANE---TGAFFFLINGPEIMS--------------KLAGESESNLRKAFEEAEKNSPA 321
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665399931   322 IIFIDEIDAIAPKRdkthgEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFgRFDREIDIGIPD 395
Cdd:smart00382  81 VLILDEITSLLDAE-----QEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
CDC48_N smart01073
Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel ...
48-127 9.26e-19

Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the N-terminus. The VAT-N domain found in AAA ATPases is a substrate 185-residue recognition domain.


Pssm-ID: 215012 [Multi-domain]  Cd Length: 82  Bit Score: 81.50  E-value: 9.26e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931    48 LIVEEAQNDD---NSVVSLSQAKMDELQLFRGDTVILKGKRRkeTVCIVLSDDTC-PDEKIRMNRVVRNNLCVHLSDVVS 123
Cdd:smart01073   1 LRVAEAPSDEdvgRGIARLSPEDMDELGLFPGDYVLITGKRR--TVAIVWPAYPEdPGGIIRIDGVQRKNAGVSIGDTVT 78

                   ....
gi 665399931   124 VQSC 127
Cdd:smart01073  79 VRKA 82
ycf46 CHL00195
Ycf46; Provisional
226-449 2.08e-18

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 89.31  E-value: 2.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 226 DDIGGcrkqLAQIKEMveLPLRHPSLFKA---IGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAG 302
Cdd:CHL00195 228 SDIGG----LDNLKDW--LKKRSTSFSKQasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVG 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 303 ESESNLRKAFEEAEKNSPAIIFIDEID-AIAPKRDKTHGEVERRIVSQLLTLMDgmKKSSHLIVMAATNRPNSIDPALRR 381
Cdd:CHL00195 302 ESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVATANNIDLLPLEILR 379
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 382 FGRFDREIDIGIPDATGRLEVLRIHTKNM--KLHDDVDLEQIAAESHGHVGADLAslcseaalQQIREKM 449
Cdd:CHL00195 380 KGRFDEIFFLDLPSLEEREKIFKIHLQKFrpKSWKKYDIKKLSKLSNKFSGAEIE--------QSIIEAM 441
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
238-389 3.74e-15

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: 73.54  E-value: 3.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 238 IKEMVELPLRHPSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEImsklaGESESNLRKAFEEAEK 317
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEV-----VLTDDRLNHLLNTAPK 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399931 318 NSpaIIFIDEIDA------IAPKRDKTHGEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREI 389
Cdd:cd19510   76 QS--IILLEDIDAafesreHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
534-667 5.89e-14

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: 71.32  E-value: 5.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 534 RGVLFYGPPGCGKTLLAKAIANEC---------QANFISVKGPELLTMWFGESEANVRDIFDK------ARSAAPCVLfF 598
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAQKLsirlssryrYGQLIEINSHSLFSKWFSESGKLVTKMFQKiqelidDKDALVFVL-I 131
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 599 DELDSIAKARGG-NVGDAGGAADRVINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILrpGRLDQLIYI 667
Cdd:cd19508  132 DEVESLAAARSAsSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAFV--DRADIKQYI 199
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
261-386 2.32e-13

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: 68.32  E-value: 2.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 261 RGILMYGPPGTGKTLIARAVANETGAFFFLINGPEImSKLAGESESNLRKAFEEAEK-NSPAIIFIDEIDAIAPKRDKTH 339
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAIHKVFDWANTsRRGLLLFVDEADAFLRKRSTEK 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 665399931 340 -GEVERRIVSQLLTLMDgmKKSSHLIVMAATNRPNSIDPALRrfGRFD 386
Cdd:cd19512  102 iSEDLRAALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAIN--DRID 145
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
534-667 2.46e-13

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: 68.15  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 534 RGVLFYGPPGCGKTLLAKAIANECQANFIsvkgpeLLTMwfgeSEANVRDiFDKAR--SAAP--CVLFFDELDSIAKARG 609
Cdd:cd19510   24 RGYLLYGPPGTGKSSFIAALAGELDYDIC------DLNL----SEVVLTD-DRLNHllNTAPkqSIILLEDIDAAFESRE 92
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665399931 610 GNV--GDAGGAADRV-INQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 667
Cdd:cd19510   93 HNKknPSAYGGLSRVtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
251-328 3.90e-12

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 68.96  E-value: 3.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 251 LFKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGpeIMSKLAgesesNLRKAFEEAEKNSPA----IIFID 326
Cdd:PRK13342  27 LRRMIEAGRLSSMILWGPPGTGKTTLARIIAGATDAPFEALSA--VTSGVK-----DLREVIEEARQRRSAgrrtILFID 99

                 ..
gi 665399931 327 EI 328
Cdd:PRK13342 100 EI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
245-328 8.04e-12

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 68.16  E-value: 8.04e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 245 PLRhpslfKAIGVKPPRGILMYGPPGTGKTLIARAVANETGAFFFLINGpeIMSKLAgesesNLRKAFEEAEKNS----P 320
Cdd:COG2256   39 PLR-----RAIEAGRLSSMILWGPPGTGKTTLARLIANATDAEFVALSA--VTSGVK-----DIREVIEEARERRaygrR 106

                 ....*...
gi 665399931 321 AIIFIDEI 328
Cdd:COG2256  107 TILFVDEI 114
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
261-379 1.35e-11

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 64.39  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 261 RGILMYGPPGTGKTLIARAVA-------NETGAFFFL--INGPEIMSKLAGESESNLRKAF---EEAEKNSPAIIF--ID 326
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCKALAqklsirlSSRYRYGQLieINSHSLFSKWFSESGKLVTKMFqkiQELIDDKDALVFvlID 132
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665399931 327 EIDAIAPKRDKTHGEVER----RIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPAL 379
Cdd:cd19508  133 EVESLAAARSASSSGTEPsdaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
415-456 1.42e-10

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 56.78  E-value: 1.42e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 665399931  415 DVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDLIDLED 456
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQED 42
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
526-667 6.46e-10

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: 58.54  E-value: 6.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 526 LKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWF-----------GESEANVRDI---FDKARSA 591
Cdd:cd19505    5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPdfgnddwidgmLILKESLHRLnlqFELAKAM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 592 APCVLFFD---ELDSiakarggNVGDAGGAADR-----VINQILTEMDGMGAKKNVFIIGATNRPDIIDPAILRPGRLDQ 663
Cdd:cd19505   85 SPCIIWIPnihELNV-------NRSTQNLEEDPklllgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT 157

                 ....
gi 665399931 664 LIYI 667
Cdd:cd19505  158 CINI 161
CDC48_2 smart01072
Cell division protein 48 (CDC48) domain 2; This domain has a double psi-beta barrel fold and ...
153-213 8.74e-10

Cell division protein 48 (CDC48) domain 2; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the C-terminus. The VAT-N domain found in AAA ATPases is a substrate 185-residue recognition domain.


Pssm-ID: 215011  Cd Length: 64  Bit Score: 55.30  E-value: 8.74e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665399931   153 FEIYLKPYFLEayRPIHMGDNFIVRAAMRPIEFKVVLTDPEPYCIVAPETVIFCDGDPIKR 213
Cdd:smart01072   6 FAEYVKRKLLG--RPVTKGDTIVVPFLGKALPFVVVSTEPSGPVIVTDDTEIEILEKPVEE 64
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
256-391 9.12e-10

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: 58.16  E-value: 9.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 256 GVKPPRGILMYGPPGTGKTLIARAVANET--------------GAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNSPA 321
Cdd:cd19505    8 GLSPSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLILKESLHRLNLQFELAKAMSPC 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665399931 322 IIFIDEIDAIAPKRDKTHGEVERRIVSQLLT--LMDGMKKSS--HLIVMAATNRPNSIDPALRRFGRFDREIDI 391
Cdd:cd19505   88 IIWIPNIHELNVNRSTQNLEEDPKLLLGLLLnyLSRDFEKSStrNILVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
260-385 1.49e-09

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU 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: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 58.16  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 260 PRGILMYGPPGTGKTLIARAVANETGAFFFLINGPEI--MSKLAGESESNLRKAFEeaeknspAIIFIDEIDAIAPKRDK 337
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFteVGYVGRDVESIIRDLVE-------GIVFIDEIDKIAKRGGS 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665399931 338 THGEVERRIVSQ-LLTLMDG--------MKKSSHLIVMAA----TNRPNSIDPALRrfGRF 385
Cdd:cd19498  119 SGPDVSREGVQRdLLPIVEGstvstkygPVKTDHILFIAAgafhVAKPSDLIPELQ--GRF 177
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
176-424 2.18e-09

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: 61.01  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  176 VRAAMRPIEFKVVLTDPEPycIVA------PETVIFCDG--DPIKRE-------EEEESLNA-VGYDDIggcRKQLAQIK 239
Cdd:TIGR03922 218 VEEALDDPSYRLVTTTAET--IEArtdpwdPSSAPSRAEfvDPAAAErkakllaEAEAELAEqIGLERV---KRQVAALK 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  240 EMVELPLRHpslfKAIGVKPP---RGILMYGPPGTGKTLIARAVANETgAFFFLINGPEIM----SKLAGESESnlrkaf 312
Cdd:TIGR03922 293 SSTAMALAR----AERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIY-CGLGVLRKPLVRevsrADLIGQYIG------ 361
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  313 eEAEKNSPAII--------FIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKksSHLIVMAATNRpNSID------PA 378
Cdd:TIGR03922 362 -ESEAKTNEIIdsalggvlFLDEAYTLVETGYGQKDPFGLEAIDTLLARMENDR--DRLVVIGAGYR-KDLDkflevnEG 437
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 665399931  379 LRRfgRFDREIDIgipDATGRLEVLRIHTKNMKLHDDVdLEQIAAE 424
Cdd:TIGR03922 438 LRS--RFTRVIEF---PSYSPDELVEIARRMATERDSV-LDDAAAD 477
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
536-600 2.68e-09

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 60.07  E-value: 2.68e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665399931 536 VLFYGPPGCGKTLLAKAIANECQANFIS-------VKgpelltmwfgeseaNVRDIFDKARSAA----PCVLFFDE 600
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVAlsavtsgVK--------------DIREVIEEARERRaygrRTILFVDE 113
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
532-665 6.47e-09

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: 55.61  E-value: 6.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 532 PSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWfGESEANVRDIFDKA-RSAAPCVLFFDELDSIAKARGG 610
Cdd:cd19512   21 LYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRST 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665399931 611 N-VGDAGGAAdrvINQILTEmdgMGAKKNVF-IIGATNRPDIIDPAIlrPGRLDQLI 665
Cdd:cd19512  100 EkISEDLRAA---LNAFLYR---TGEQSNKFmLVLASNQPEQFDWAI--NDRIDEMV 148
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
503-650 8.10e-09

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: 59.09  E-value: 8.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  503 GLESVKKELqELVQYPVEHPDKFLKFGM---QPSRGVLFYGPPGCGKTLLAKAIANE-C------QANFISVKGPELLTM 572
Cdd:TIGR03922 280 GLERVKRQV-AALKSSTAMALARAERGLpvaQTSNHMLFAGPPGTGKTTIARVVAKIyCglgvlrKPLVREVSRADLIGQ 358
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 665399931  573 WFGESEANVRDIFDKARSAapcVLFFDELDSIAKARGGNVGDAGGAAdrvINQILTEMDgmGAKKNVFIIGATNRPDI 650
Cdd:TIGR03922 359 YIGESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGLEA---IDTLLARME--NDRDRLVVIGAGYRKDL 428
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
691-727 2.29e-08

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: 50.61  E-value: 2.29e-08
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 665399931  691 EVDLTYIAKVTQGFSGADLTEICQRACKLAIRQAIEA 727
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEA 37
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
536-600 2.89e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 57.02  E-value: 2.89e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665399931 536 VLFYGPPGCGKTLLAKAIANECQANFI-------SVKgpelltmwfgeseaNVRDIFDKARSAA----PCVLFFDE 600
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEalsavtsGVK--------------DLREVIEEARQRRsagrRTILFIDE 100
44 PHA02544
clamp loader, small subunit; Provisional
238-402 6.83e-08

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 55.00  E-value: 6.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 238 IKEMVeLPLRHPSLFKAIgVKP---PRGILMYGPPGTGKTLIARAVANETGAFFFLINGpeimSKLAGESESNLRKAFEE 314
Cdd:PHA02544  20 IDECI-LPAADKETFKSI-VKKgriPNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNG----SDCRIDFVRNRLTRFAS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 315 A--EKNSPAIIFIDEIDaiapkRDKTHgEVERrivsQLLTLMDgmKKSSHLIVMAATNRPNSIDPALRrfGRFdREIDIG 392
Cdd:PHA02544  94 TvsLTGGGKVIIIDEFD-----RLGLA-DAQR----HLRSFME--AYSKNCSFIITANNKNGIIEPLR--SRC-RVIDFG 158
                        170
                 ....*....|
gi 665399931 393 IPDATGRLEV 402
Cdd:PHA02544 159 VPTKEEQIEM 168
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
262-385 7.64e-08

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 51.91  E-value: 7.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  262 GILMYGPPGTGKTLIARAVANET-GAFFFLINGP------------EIMSKLAGESESNLRKAFEEAEknspaIIFIDEI 328
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsNRPVFYVQLTrdtteedlfgrrNIDPGGASWVDGPLVRAAREGE-----IAVLDEI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 665399931  329 DAIAPK-RDKTHGEVERRIvsqlLTLMDG----MKKSSHLIVMAATNRP----NSIDPALRRfgRF 385
Cdd:pfam07728  76 NRANPDvLNSLLSLLDERR----LLLPDGgelvKAAPDGFRLIATMNPLdrglNELSPALRS--RF 135
PRK13341 PRK13341
AAA family ATPase;
264-328 3.36e-07

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 53.91  E-value: 3.36e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 264 LMYGPPGTGKTLIARAVANETGAFFFLINgpeimSKLAGESEsnLRKAFEEAEK-----NSPAIIFIDEI 328
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLN-----AVLAGVKD--LRAEVDRAKErlerhGKRTILFIDEV 118
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
536-569 5.80e-07

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 49.81  E-value: 5.80e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 665399931  536 VLFYGPPGCGKTLLAKAIANECQANFISVKGPEL 569
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
PRK04195 PRK04195
replication factor C large subunit; Provisional
258-458 8.53e-07

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 52.23  E-value: 8.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 258 KPPRGILMYGPPGTGKTLIARAVANETGafFFLI--NGP-----EIMSKLAGESeSNLRKAFEEAEKnspaIIFIDEIDA 330
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALANDYG--WEVIelNASdqrtaDVIERVAGEA-ATSGSLFGARRK----LILLDEVDG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 331 IAPKRDkthgeveRRIVSQLLTLmdgMKKSSHLIVMAATN---------RPNSIDPALRRFGRfdREIdigipdatgrLE 401
Cdd:PRK04195 110 IHGNED-------RGGARAILEL---IKKAKQPIILTANDpydpslrelRNACLMIEFKRLST--RSI----------VP 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665399931 402 VLR-IHTKNMKLHDDVDLEQIAAESHGhvgaDLaslcsEAA---LQQIREKMDLIDLEDDK 458
Cdd:PRK04195 168 VLKrICRKEGIECDDEALKEIAERSGG----DL-----RSAindLQAIAEGYGKLTLEDVK 219
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
261-376 9.98e-07

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. 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: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 49.45  E-value: 9.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 261 RGILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGES--ESNLRKAFEEAEKNSPAIIFIDEIDAIAPKR-DK 337
Cdd:cd19506   27 KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKvPK 106
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 665399931 338 THGEVE-RRIVSQLLTLMDGMKKSSHLIVMAATNRPNSID 376
Cdd:cd19506  107 TEKQLDpKRLKKDLPKILKSLKPEDRVLIVGTTSRPFEAD 146
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
536-569 1.41e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 51.28  E-value: 1.41e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 665399931 536 VLFYGPPGCGKTLLAKAIANECQANFISVKGPEL 569
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
263-333 1.58e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 50.90  E-value: 1.58e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665399931 263 ILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSK--LAGeSESNLrkafeeaEKNSpaIIFIDEIDAIAP 333
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKPgdLAA-ILTNL-------EEGD--VLFIDEIHRLSP 116
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
263-333 2.83e-06

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 49.99  E-value: 2.83e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 665399931  263 ILMYGPPGTGKTLIARAVANETGAFFFLINGPEImsklagESESNLRKAFEEAEKNSpaIIFIDEIDAIAP 333
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL------EKPGDLAAILTNLEEGD--VLFIDEIHRLSP 95
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
261-311 4.39e-06

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 49.97  E-value: 4.39e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 665399931 261 RGILMYGPPGTGKTLIARAVANETGAF--FFLINGPEIMSKLAGESE---SNLRKA 311
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEflmQALRKA 120
CDC48_2 pfam02933
Cell division protein 48 (CDC48), domain 2; This domain has a double psi-beta barrel fold and ...
153-212 5.68e-06

Cell division protein 48 (CDC48), domain 2; This domain has a double psi-beta barrel fold and includes VCP-like ATPase and N-ethylmaleimide sensitive fusion protein N-terminal domains. Both the VAT and NSF N-terminal functional domains consist of two structural domains of which this is at the C-terminus. The VAT-N domain found in AAA ATPases pfam00004 is a substrate 185-residue recognition domain.


Pssm-ID: 427063  Cd Length: 64  Bit Score: 44.54  E-value: 5.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  153 FEIYLKPYFLEayRPIHMGDNFIVRAAMRPIEFKVVLTDPEPYCIVAPETVIFCDGDPIK 212
Cdd:pfam02933   6 ELAYVKRNLEG--RPVSKGDTIVVEFLGGAIPLVVVSTEPSGPVVVTETTEIEIGEKPVQ 63
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
263-423 6.00e-06

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 49.01  E-value: 6.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 263 ILMYGPPGTGKTLIARAVANETGAFFFLING-PEIM-SKLAGesESNLRKAFEEAE-------KNspaIIFIDEIDAiAP 333
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpSDILG--TYIYDQQTGEFEfrpgplfAN---VLLADEINR-AP 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 334 krDKTHgeverrivSQLLTLM-------DG--MKKSSHLIVMAATNRPNSI------DPALRRFGRFdreIDIGIPDATG 398
Cdd:COG0714  108 --PKTQ--------SALLEAMeerqvtiPGgtYKLPEPFLVIATQNPIEQEgtyplpEAQLDRFLLK---LYIGYPDAEE 174
                        170       180
                 ....*....|....*....|....*..
gi 665399931 399 RLEVLRIHTKNM--KLHDDVDLEQIAA 423
Cdd:COG0714  175 EREILRRHTGRHlaEVEPVLSPEELLA 201
PRK04195 PRK04195
replication factor C large subunit; Provisional
500-556 1.91e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 47.99  E-value: 1.91e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 665399931 500 DIGGLESVKKELQELVqypvehpDKFLKfgMQPSRGVLFYGPPGCGKTLLAKAIANE 556
Cdd:PRK04195  15 DVVGNEKAKEQLREWI-------ESWLK--GKPKKALLLYGPPGVGKTSLAHALAND 62
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
536-567 2.13e-05

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 47.38  E-value: 2.13e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 665399931 536 VLFYGPPGCGKTLLAKAIANECQANFISVKGP 567
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
263-333 2.18e-05

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 45.57  E-value: 2.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665399931  263 ILMYGPPGTGKTLIARAVANETGAFFFLINGPEIMSK--LAGesesnLRKAFEEAEknspaIIFIDEIDAIAP 333
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERPgdLAA-----ILTNLEPGD-----VLFIDEIHRLNR 98
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
236-389 2.74e-05

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 47.15  E-value: 2.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 236 AQIKEMVELpLRhPSLFkaiGVKPPRgILMYGPPGTGKTLIARAVANE-------------------------TGAFFFL 290
Cdd:COG1474   33 EEIEELASA-LR-PALR---GERPSN-VLIYGPTGTGKTAVAKYVLEEleeeaeergvdvrvvyvncrqastrYRVLSRI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 291 IN--GPEIMSKLAGESESNLRKAFEEA--EKNSPAIIFIDEIDAIapkrDKTHGEverRIVSQLLTLMDGMkKSSHLIVM 366
Cdd:COG1474  107 LEelGSGEDIPSTGLSTDELFDRLYEAldERDGVLVVVLDEIDYL----VDDEGD---DLLYQLLRANEEL-EGARVGVI 178
                        170       180
                 ....*....|....*....|....*..
gi 665399931 367 AATNRPN---SIDPALR-RFGrfDREI 389
Cdd:COG1474  179 GISNDLEfleNLDPRVKsSLG--EEEI 203
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
261-311 3.15e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 46.92  E-value: 3.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 665399931  261 RGILMYGPPGTGKTLIARAVANETGAF--FFLINGPEIMSKLAGESES---NLRKA 311
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGEDtpFTSISGSEVYSLEMKKTEAltqAFRKA 106
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
263-333 5.44e-05

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 44.49  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  263 ILMYGPPGTGKTLIARAVANETGAF---FFLINGPEIM-----SKLAGESESNLRKA-----FEEAEKNSPAIIFIDEID 329
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGDeraLIRIDMSEYMeehsvSRLIGAPPGYVGYEeggqlTEAVRRKPYSIVLIDEIE 85

                  ....
gi 665399931  330 AIAP 333
Cdd:pfam07724  86 KAHP 89
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
534-571 6.52e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 45.16  E-value: 6.52e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 665399931 534 RGVLFYGPPGCGKTLLAKAIANE-CQAN----FISVkgPELLT 571
Cdd:COG1484  100 ENLILLGPPGTGKTHLAIALGHEaCRAGyrvrFTTA--PDLVN 140
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
231-366 7.84e-05

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 44.03  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  231 CR-KQLAQIKEMVElPLRHPSlfkaigvkpPRGILMYGPPGTGKTLIARAV---ANETGAFFFLINGPEIMSKLA---GE 303
Cdd:pfam13191   4 GReEELEQLLDALD-RVRSGR---------PPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPlleAL 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 665399931  304 SESNLRKAFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSSHLIVM 366
Cdd:pfam13191  74 TREGLLRQLLDELESSLLEAWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL 136
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
497-569 9.28e-05

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 45.37  E-value: 9.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399931  497 TWTDIGGLESVKKELQ------ELVQYPVEHpdkflkfgmqpsrgVLFYGPPGCGKTLLAKAIANECQANFISVKGPEL 569
Cdd:TIGR00635   2 LLAEFIGQEKVKEQLQlfieaaKMRQEALDH--------------LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
PRK08116 PRK08116
hypothetical protein; Validated
533-565 1.27e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 44.63  E-value: 1.27e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 665399931 533 SRGVLFYGPPGCGKTLLAKAIANECQANFISVK 565
Cdd:PRK08116 114 NVGLLLWGSVGTGKTYLAACIANELIEKGVPVI 146
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
751-782 2.01e-04

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 40.17  E-value: 2.01e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 665399931  751 PEITSAHFEEAMKFARRSVSDNDIRKYEMFAQ 782
Cdd:pfam09336  27 PPVTMKDFLKALKSSRPTVSKEDLEKYEEFTK 58
PRK13341 PRK13341
AAA family ATPase;
537-564 2.15e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 45.05  E-value: 2.15e-04
                         10        20
                 ....*....|....*....|....*...
gi 665399931 537 LFYGPPGCGKTLLAKAIANECQANFISV 564
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSL 83
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
263-376 3.63e-04

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: 40.95  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 263 ILMYGPPGTGKTLIARAVANETGAF---FFLINGPEIMsklagesesnLRKAFEEAEKNSPAIIFIDEIDAIAPKRDkth 339
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEQALLSdepVIFISFLDTI----------LEAIEDLIEEKKLDIIIIDSLSSLARASQ--- 67
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 665399931 340 GEVERRIVSQLLTLMDGMKKsSHLIVMAATNRPNSID 376
Cdd:cd01120   68 GDRSSELLEDLAKLLRAARN-TGITVIATIHSDKFDI 103
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
366-657 3.87e-04

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 44.03  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 366 MAATNRPNSIDPALRRFGRFDREIDIGIPDATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQI 445
Cdd:COG5635    3 LLLALILALLALVLLLDLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 446 REK----------MDLIDLEDDKIDAEVLASLAVTMENFRYAMTKSSPSALRETVVEVPNTTWTDIGGLESVKKELQELV 515
Cdd:COG5635   83 VLLllesllllllLLLLLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDDLYVPLN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 516 QYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQANFISVKGP-----------------ELLTMWFGESE 578
Cdd:COG5635  163 LLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALELAERYLDAEDPipilielrdlaeeasleDLLAEALEKRG 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399931 579 ANVRDIFDKARSAAPCVLFFDELDSIAkarggnvgdAGGAADRVINQILTEMDgmGAKKNVFIIgaTNRPDIIDPAILR 657
Cdd:COG5635  243 GEPEDALERLLRNGRLLLLLDGLDEVP---------DEADRDEVLNQLRRFLE--RYPKARVII--TSRPEGYDSSELE 308
TIGR02928 TIGR02928
orc1/cdc6 family replication initiation protein; Members of this protein family are found ...
237-336 4.83e-04

orc1/cdc6 family replication initiation protein; Members of this protein family are found exclusively in the archaea. This set of DNA binding proteins shows homology to the origin recognition complex subunit 1/cell division control protein 6 family in eukaryotes. Several members may be found in genome and interact with each other. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 274354 [Multi-domain]  Cd Length: 365  Bit Score: 43.39  E-value: 4.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  237 QIKEMVElplrhpSLFKAIGVKPPRGILMYGPPGTGKTLIARAVANE-------TGAFFFLI-------NGP-EIMSKLA 301
Cdd:TIGR02928  23 QIEELAK------ALRPILRGSRPSNVFIYGKTGTGKTAVTKYVMKEleeaaedRDVRVVTVyvncqilDTLyQVLVELA 96
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 665399931  302 ---GESESN-----------LRKAFEEAEKNSPAIIFI-DEIDAIAPKRD 336
Cdd:TIGR02928  97 nqlRGSGEEvpttglstsevFRRLYKELNERGDSLIIVlDEIDYLVGDDD 146
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
263-332 5.13e-04

lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an evolutionarily conserved ATP-dependent serine protease, present in bacteria and eukaryotic mitochondria and peroxisomes, which mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Lon protease is both an ATP-dependent peptidase and a protein-activated ATPase. This RecA-like Lon 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: 410908 [Multi-domain]  Cd Length: 182  Bit Score: 41.78  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 263 ILMYGPPGTGKTLIARAVANETGAFFFLINgpeimskLAG-ESESNLR---------------KAFEEAEKNSPaIIFID 326
Cdd:cd19500   40 LCLVGPPGVGKTSLGKSIARALGRKFVRIS-------LGGvRDEAEIRghrrtyvgampgriiQALKKAGTNNP-VFLLD 111

                 ....*.
gi 665399931 327 EIDAIA 332
Cdd:cd19500  112 EIDKIG 117
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
263-328 5.68e-04

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 42.76  E-value: 5.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399931 263 ILMYGPPGTGKTLIARAVANETGAFFFLINGPEImSK---LAGeSESNLrkafeeaEKNSpaIIFIDEI 328
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGPAI-EKpgdLAA-ILTNL-------EEGD--VLFIDEI 114
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
311-560 8.30e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 42.83  E-value: 8.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 311 AFEEAEKNSPAIIFIDEIDAIAPKRDKTHGEVERRIVSQLLTLMDGMKKSSHLIVMAATNRPNSIDPALRRFGRFDREID 390
Cdd:COG1401    3 RPVLEFKFLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 391 IGIPdATGRLEVLRIHTKNMKLHDDVDLEQIAAESHGHVGADLASLCSEAALQQIREKMDLIDLEDDKIDAEVLASLAVT 470
Cdd:COG1401   83 LEKV-ELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 471 MENFRYAMTKSSPSALRETVVEVPNTTWTDiggLESVKKELQELVQYPVEHPDKFLKFGMQPSRGVLFYGPPGCGKTLLA 550
Cdd:COG1401  162 LEELLAAPEDLSADALAAELSAAEELYSED---LESEDDYLKDLLREKFEETLEAFLAALKTKKNVILAGPPGTGKTYLA 238
                        250
                 ....*....|
gi 665399931 551 KAIANECQAN 560
Cdd:COG1401  239 RRLAEALGGE 248
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
535-657 9.10e-04

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 40.35  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  535 GVLFYGPPGCGKTLLAKAIANE-CQANFISVKGPELLTmwfgesEANVRDIFDKARSAA-------------PCVLFFDE 600
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTT------EEDLFGRRNIDPGGAswvdgplvraareGEIAVLDE 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 665399931  601 LDSIAKArggnvgdaggAADRVI----NQILTEMDG---MGAKKNVF-IIGATNRPDI----IDPAILR 657
Cdd:pfam07728  75 INRANPD----------VLNSLLslldERRLLLPDGgelVKAAPDGFrLIATMNPLDRglneLSPALRS 133
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
536-556 1.35e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 38.74  E-value: 1.35e-03
                          10        20
                  ....*....|....*....|.
gi 665399931  536 VLFYGPPGCGKTLLAKAIANE 556
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
536-606 1.48e-03

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 40.26  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  536 VLFYGPPGCGKTLLAKAIANE---CQANFISVKGPELL-----TMWFGESEANVR-----DIFDKARSAAPCVLFFDELD 602
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMeehsvSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85

                  ....
gi 665399931  603 SIAK 606
Cdd:pfam07724  86 KAHP 89
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
524-579 1.51e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 41.88  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665399931 524 KFLKFGMQPSRGVLFYGPPGCGKTLLAKAIANECQAN--FISVKGPELLTMWFGESEA 579
Cdd:COG1224   55 KMIKEGKMAGKGILIVGPPGTGKTALAVAIARELGEDtpFVAISGSEIYSAELKKTEF 112
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
258-386 2.07e-03

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: 39.85  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 258 KPPRGILMYGPPGTGKTLIARAVA---NETGAFFFLINGPEIMSKlagESESNLRKA-------------FEEAEKNSPA 321
Cdd:cd19499   39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEK---HSVSRLIGAppgyvgyteggqlTEAVRRKPYS 115
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 665399931 322 IIFIDEIdaiapkrDKTHGEVeRRIVSQLL---TLMDG------MKKSshLIVMAAtnrpNSIDPALrrFGRFD 386
Cdd:cd19499  116 VVLLDEI-------EKAHPDV-QNLLLQVLddgRLTDShgrtvdFKNT--IIIMTS----NHFRPEF--LNRID 173
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
536-570 2.83e-03

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


Pssm-ID: 439516  Cd Length: 232  Bit Score: 40.15  E-value: 2.83e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 665399931 536 VLFYGPPGCGKTLLAKAIANE-CQAN----FISVkgPELL 570
Cdd:NF038214  93 VLLLGPPGTGKTHLAIALGYAaCRQGyrvrFTTA--ADLV 130
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
536-615 3.33e-03

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU 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: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 39.29  E-value: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 536 VLFYGPPGCGKTLLAKAIANECQANFISVKGPElltmwFGESEANVRDIFDKARSAAPCVLFFDELDSIAKARGGNVGDA 615
Cdd:cd19498   49 ILMIGPTGVGKTEIARRLAKLAGAPFIKVEATK-----FTEVGYVGRDVESIIRDLVEGIVFIDEIDKIAKRGGSSGPDV 123
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
504-559 3.53e-03

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 40.34  E-value: 3.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 665399931 504 LESVKKELQELVQYPVEHPdkflkfgmqpsrGVLFYGPPGCGKTLLAKAIANE--CQA 559
Cdd:COG0470    1 QEEAWEQLLAAAESGRLPH------------ALLLHGPPGIGKTTLALALARDllCEN 46
AAA_22 pfam13401
AAA domain;
257-334 3.63e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.48  E-value: 3.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931  257 VKPPRGILM-YGPPGTGKTLIARAVAN---ETGAFFFLINGP------EIMSKLAGE---------SESNLRKAFEEA-- 315
Cdd:pfam13401   1 IRFGAGILVlTGESGTGKTTLLRRLLEqlpEVRDSVVFVDLPsgtspkDLLRALLRAlglplsgrlSKEELLAALQQLll 80
                          90
                  ....*....|....*....
gi 665399931  316 EKNSPAIIFIDEIDAIAPK 334
Cdd:pfam13401  81 ALAVAVVLIIDEAQHLSLE 99
PRK08116 PRK08116
hypothetical protein; Validated
261-283 4.17e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.00  E-value: 4.17e-03
                         10        20
                 ....*....|....*....|...
gi 665399931 261 RGILMYGPPGTGKTLIARAVANE 283
Cdd:PRK08116 115 VGLLLWGSVGTGKTYLAACIANE 137
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
536-553 4.82e-03

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 39.06  E-value: 4.82e-03
                          10
                  ....*....|....*...
gi 665399931  536 VLFYGPPGCGKTLLAKAI 553
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKRL 42
Parvo_NS1 pfam01057
Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses ...
536-555 4.95e-03

Parvovirus non-structural protein NS1; This family also contains the NS2 protein. Parvoviruses encode two non-structural proteins, NS1 and NS2. The mRNA for NS2 contains the coding sequence for the first 87 amino acids of NS1, then by an alternative splicing mechanism mRNA from a different reading frame, encoding the last 78 amino acids, makes up the full length of the NS2 mRNA. NS1, is the major non-structural protein. It is essential for DNA replication. It is an 83-kDa nuclear phosphoprotein. It has DNA helicase and ATPase activity.


Pssm-ID: 426020  Cd Length: 271  Bit Score: 39.60  E-value: 4.95e-03
                          10        20
                  ....*....|....*....|
gi 665399931  536 VLFYGPPGCGKTLLAKAIAN 555
Cdd:pfam01057 116 VWFYGPASTGKTNLAQAIAH 135
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
263-286 6.63e-03

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 38.36  E-value: 6.63e-03
                         10        20
                 ....*....|....*....|....
gi 665399931 263 ILMYGPPGTGKTLIARAVANETGA 286
Cdd:COG0645    2 ILVCGLPGSGKSTLARALAERLGA 25
hslU PRK05201
ATP-dependent protease ATPase subunit HslU;
309-344 6.91e-03

ATP-dependent protease ATPase subunit HslU;


Pssm-ID: 235364 [Multi-domain]  Cd Length: 443  Bit Score: 39.68  E-value: 6.91e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 665399931 309 RKAFEEAEKNspAIIFIDEIDAIAPKRDKTHGEVER 344
Cdd:PRK05201 241 QEAIERVEQN--GIVFIDEIDKIAARGGSSGPDVSR 274
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
263-279 7.62e-03

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.67  E-value: 7.62e-03
                          10
                  ....*....|....*..
gi 665399931  263 ILMYGPPGTGKTLIARA 279
Cdd:pfam01078  25 LLMIGPPGSGKTMLAKR 41
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
263-278 7.64e-03

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 39.64  E-value: 7.64e-03
                         10
                 ....*....|....*.
gi 665399931 263 ILMYGPPGTGKTLIAR 278
Cdd:COG0606  214 LLMIGPPGSGKTMLAR 229
COG2842 COG2842
Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons]; ...
536-769 8.15e-03

Bacteriophage DNA transposition protein, AAA+ family ATPase [Mobilome: prophages, transposons];


Pssm-ID: 442090 [Multi-domain]  Cd Length: 254  Bit Score: 38.78  E-value: 8.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 536 VLFYGPPGCGKTLLAKAIANEcQANFIsvkgpeLLTMWfgeSEANVRDIFDKarsaapcvlffdeldsIAKARGgnVGDA 615
Cdd:COG2842   53 GVVYGESGVGKTTAAREYANR-NPNVI------YVTAS---PSWTSKELLEE----------------LAEELG--IPAP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 616 GGAADRVINQILTEMDGmgakknvfiigaTNRPDIIDPA-ILRPGRLDQL--IYiplpdDKSREAI-------LKANLRK 685
Cdd:COG2842  105 PGTIADLRDRILERLAG------------TGRLLIIDEAdHLKPKALEELrdIH-----DETGVGVvligmerLPAKLKR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 665399931 686 --------------SPLAKEvDLTYIAKVTQGFSGADLTEICQRACKLAIRQaIEAEIRREKERAENQNsamddeddpVP 751
Cdd:COG2842  168 yeqlysrigfwvefKPLSLE-DVRALAEAWGELTDPDLLELLHRITRGNLRR-LDRTLRLAARAAKRNG---------LT 236
                        250
                 ....*....|....*...
gi 665399931 752 EITSAHFEEAMKFARRSV 769
Cdd:COG2842  237 KITLDHVRAAALMLGEGP 254
 
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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