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Conserved domains on  [gi|542097447|ref|WP_021013987|]
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MULTISPECIES: CDC48 family AAA ATPase [Pectobacteriaceae]

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 ...
4-712 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: 770.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447    4 ELKLKVAEALPKDAGRGYARLDPADMARLNLAVGDIVQLTSKKGTGIAKLMPTYPDMRNKGIVQLDGLTRRNTSLSLDEK 83
Cdd:TIGR01243   1 SVELRVAEAYPRDVGRGIVRIDRQTAARLGVEPGDFVEIEKGDRSVVAIVWPLRPDDEGRGIIRMDGYLRANAGVTIGDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447   84 VQIEPASCKHATQIVLIPTT-ITPNQRDLDYIGSLLDGLPVQKGDLLRAHLFGSrSADFKVESTIPDGAVLIDPTTTLVI 162
Cdd:TIGR01243  81 VTVERAEVKEAKKVVLAPTQpIRFGRDFVDYVKEFLLGKPISKGETVIVPVLEG-ALPFVVVSTQPAGFVYVTEATEVEI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  163 GKSNAVGNSSHSTQRLSYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQ 242
Cdd:TIGR01243 160 REKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  243 FFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIA 322
Cdd:TIGR01243 240 FISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  323 ATNLPNAIDPALRRPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRR 402
Cdd:TIGR01243 320 ATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  403 LLPE--IDFSSAELPYDRLAELTVMMDDFRAALCEVSPSAIRELFVDIPDVRWEDVGGLDDVRRRLIESVEWPIKYPELY 480
Cdd:TIGR01243 400 FIREgkINFEAEEIPAEVLKELKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIF 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  481 EQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFLKARQAAPCIIFLDEVDSVI 560
Cdd:TIGR01243 480 EKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIA 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  561 PARNEgAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEIIELGLPDEDARRQILAVHLRNK 640
Cdd:TIGR01243 560 PARGA-RFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSM 638
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542097447  641 PLGDNIHADDLAERCDGASGAELAAVCNRAALAALRRAIQQSEEAVLSpstVGETPVALTVRIEQHDFAEVI 712
Cdd:TIGR01243 639 PLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLE---VGEEEFLKDLKVEMRHFLEAL 707
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
4-712 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: 770.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447    4 ELKLKVAEALPKDAGRGYARLDPADMARLNLAVGDIVQLTSKKGTGIAKLMPTYPDMRNKGIVQLDGLTRRNTSLSLDEK 83
Cdd:TIGR01243   1 SVELRVAEAYPRDVGRGIVRIDRQTAARLGVEPGDFVEIEKGDRSVVAIVWPLRPDDEGRGIIRMDGYLRANAGVTIGDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447   84 VQIEPASCKHATQIVLIPTT-ITPNQRDLDYIGSLLDGLPVQKGDLLRAHLFGSrSADFKVESTIPDGAVLIDPTTTLVI 162
Cdd:TIGR01243  81 VTVERAEVKEAKKVVLAPTQpIRFGRDFVDYVKEFLLGKPISKGETVIVPVLEG-ALPFVVVSTQPAGFVYVTEATEVEI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  163 GKSNAVGNSSHSTQRLSYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQ 242
Cdd:TIGR01243 160 REKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  243 FFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIA 322
Cdd:TIGR01243 240 FISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  323 ATNLPNAIDPALRRPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRR 402
Cdd:TIGR01243 320 ATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  403 LLPE--IDFSSAELPYDRLAELTVMMDDFRAALCEVSPSAIRELFVDIPDVRWEDVGGLDDVRRRLIESVEWPIKYPELY 480
Cdd:TIGR01243 400 FIREgkINFEAEEIPAEVLKELKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIF 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  481 EQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFLKARQAAPCIIFLDEVDSVI 560
Cdd:TIGR01243 480 EKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIA 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  561 PARNEgAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEIIELGLPDEDARRQILAVHLRNK 640
Cdd:TIGR01243 560 PARGA-RFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSM 638
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542097447  641 PLGDNIHADDLAERCDGASGAELAAVCNRAALAALRRAIQQSEEAVLSpstVGETPVALTVRIEQHDFAEVI 712
Cdd:TIGR01243 639 PLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLE---VGEEEFLKDLKVEMRHFLEAL 707
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
178-439 3.68e-113

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 344.68  E-value: 3.68e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 178 LSYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYG 257
Cdd:COG1222   75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 258 ESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVV-GDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRR 336
Cdd:COG1222  155 EGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGtSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLR 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 337 PGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRLLPEIDfssaelpy 416
Cdd:COG1222  235 PGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT-------- 306
                        250       260
                 ....*....|....*....|...
gi 542097447 417 drlaeltvmMDDFRAALCEVSPS 439
Cdd:COG1222  307 ---------MEDLEKAIEKVKKK 320
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
179-433 4.45e-97

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 305.22  E-value: 4.45e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 179 SYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGE 258
Cdd:PRK03992 129 TYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGE 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 259 SEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHR--DKVVGDVE-KRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALR 335
Cdd:PRK03992 209 GARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAIL 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 336 RPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRllpeidfssaelp 415
Cdd:PRK03992 289 RPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD------------- 355
                        250
                 ....*....|....*...
gi 542097447 416 yDRLAeltVMMDDFRAAL 433
Cdd:PRK03992 356 -DRTE---VTMEDFLKAI 369
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
182-347 7.05e-91

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: 280.86  E-value: 7.05e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 182 DVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEA 261
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 262 HLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFD 341
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                 ....*.
gi 542097447 342 REISIP 347
Cdd:cd19519  161 REIDIG 166
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
218-347 6.22e-50

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: 170.85  E-value: 6.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  218 VLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDV 297
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 542097447  298 EKRIVAQLLALMDGLKNR-GKVIVIAATNLPNAIDPALRrpGRFDREISIP 347
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
cell_div_CdvC NF041006
cell division protein CdvC;
177-444 1.26e-47

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 172.61  E-value: 1.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 177 RLSYEDVGGLKNQVRRIREMIELPLRYPEVFErLGidAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFY 256
Cdd:NF041006  99 KVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP-LG--WPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 257 GESEAHLRKIFEEAGRKG-----PSIIFLDEIDSI-APHRDKVVGDVekRIVAQLLALMDGLKNRG---KVIVIAATNLP 327
Cdd:NF041006 176 GEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALlGVYSSEVGGEV--RVRNQFLKEMDGLQDKSenyHVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 328 NAID-PALRrpgRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRLLPE 406
Cdd:NF041006 254 WRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEK 330
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 542097447 407 idfssaelpydRLAE-LTVMMDDFRAALCEVSPSAIREL 444
Cdd:NF041006 331 -----------GLGEpRPITMEDFKEVLKIRKPSVNQEM 358
CDC48_N smart01073
Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel ...
7-89 1.28e-20

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: 86.51  E-value: 1.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447     7 LKVAEAL-PKDAGRGYARLDPADMARLNLAVGDIVQLTSKKGTgIAKLMPTYPDMRNkGIVQLDGLTRRNTSLSLDEKVQ 85
Cdd:smart01073   1 LRVAEAPsDEDVGRGIARLSPEDMDELGLFPGDYVLITGKRRT-VAIVWPAYPEDPG-GIIRIDGVQRKNAGVSIGDTVT 78

                   ....
gi 542097447    86 IEPA 89
Cdd:smart01073  79 VRKA 82
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
4-712 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: 770.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447    4 ELKLKVAEALPKDAGRGYARLDPADMARLNLAVGDIVQLTSKKGTGIAKLMPTYPDMRNKGIVQLDGLTRRNTSLSLDEK 83
Cdd:TIGR01243   1 SVELRVAEAYPRDVGRGIVRIDRQTAARLGVEPGDFVEIEKGDRSVVAIVWPLRPDDEGRGIIRMDGYLRANAGVTIGDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447   84 VQIEPASCKHATQIVLIPTT-ITPNQRDLDYIGSLLDGLPVQKGDLLRAHLFGSrSADFKVESTIPDGAVLIDPTTTLVI 162
Cdd:TIGR01243  81 VTVERAEVKEAKKVVLAPTQpIRFGRDFVDYVKEFLLGKPISKGETVIVPVLEG-ALPFVVVSTQPAGFVYVTEATEVEI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  163 GKSNAVGNSSHSTQRLSYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQ 242
Cdd:TIGR01243 160 REKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAY 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  243 FFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIA 322
Cdd:TIGR01243 240 FISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIG 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  323 ATNLPNAIDPALRRPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRR 402
Cdd:TIGR01243 320 ATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  403 LLPE--IDFSSAELPYDRLAELTVMMDDFRAALCEVSPSAIRELFVDIPDVRWEDVGGLDDVRRRLIESVEWPIKYPELY 480
Cdd:TIGR01243 400 FIREgkINFEAEEIPAEVLKELKVTMKDFMEALKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIF 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  481 EQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFLKARQAAPCIIFLDEVDSVI 560
Cdd:TIGR01243 480 EKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIA 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  561 PARNEgAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEIIELGLPDEDARRQILAVHLRNK 640
Cdd:TIGR01243 560 PARGA-RFDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSM 638
                         650       660       670       680       690       700       710
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542097447  641 PLGDNIHADDLAERCDGASGAELAAVCNRAALAALRRAIQQSEEAVLSpstVGETPVALTVRIEQHDFAEVI 712
Cdd:TIGR01243 639 PLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLE---VGEEEFLKDLKVEMRHFLEAL 707
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
178-439 3.68e-113

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 344.68  E-value: 3.68e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 178 LSYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYG 257
Cdd:COG1222   75 VTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIG 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 258 ESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVV-GDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRR 336
Cdd:COG1222  155 EGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGtSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLR 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 337 PGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRLLPEIDfssaelpy 416
Cdd:COG1222  235 PGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT-------- 306
                        250       260
                 ....*....|....*....|...
gi 542097447 417 drlaeltvmMDDFRAALCEVSPS 439
Cdd:COG1222  307 ---------MEDLEKAIEKVKKK 320
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
447-668 1.34e-100

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 311.94  E-value: 1.34e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 447 DIPDVRWEDVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMS 526
Cdd:COG1222   71 ESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVS 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 527 RYVGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPARNeGAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLID 606
Cdd:COG1222  151 KYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRT-DDGTSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLD 229
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542097447 607 PAMLRPGRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVCN 668
Cdd:COG1222  230 PALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVT 291
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
179-433 4.45e-97

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 305.22  E-value: 4.45e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 179 SYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGE 258
Cdd:PRK03992 129 TYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKFIGE 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 259 SEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHR--DKVVGDVE-KRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALR 335
Cdd:PRK03992 209 GARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGTSGDREvQRTLMQLLAEMDGFDPRGNVKIIAATNRIDILDPAIL 288
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 336 RPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRllpeidfssaelp 415
Cdd:PRK03992 289 RPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD------------- 355
                        250
                 ....*....|....*...
gi 542097447 416 yDRLAeltVMMDDFRAAL 433
Cdd:PRK03992 356 -DRTE---VTMEDFLKAI 369
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
182-347 7.05e-91

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: 280.86  E-value: 7.05e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 182 DVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEA 261
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 262 HLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFD 341
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                 ....*.
gi 542097447 342 REISIP 347
Cdd:cd19519  161 REIDIG 166
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
182-346 1.33e-87

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: 272.24  E-value: 1.33e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 182 DVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEA 261
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 262 HLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFD 341
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160

                 ....*
gi 542097447 342 REISI 346
Cdd:cd19503  161 REVEI 165
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
178-436 2.06e-86

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 276.68  E-value: 2.06e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  178 LSYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYG 257
Cdd:TIGR01242 119 VSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKYIG 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  258 ESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVV--GDVE-KRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPAL 334
Cdd:TIGR01242 199 EGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGtsGDREvQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDPAL 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  335 RRPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRLLPEidfssael 414
Cdd:TIGR01242 279 LRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIREERDY-------- 350
                         250       260
                  ....*....|....*....|..
gi 542097447  415 pydrlaeltVMMDDFRAALCEV 436
Cdd:TIGR01242 351 ---------VTMDDFIKAVEKV 363
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
319-668 2.95e-84

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: 272.17  E-value: 2.95e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 319 IVIAATNLPNAIDPALRRPGRFDREISIPIPDREGRREII-EIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAM 397
Cdd:COG0464   18 LDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLlLLLSGALAALLLLALLLLALLALLAALLSALELLLLGEL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 398 SALRRLLPEIDFSSAELPYDRLAELTVMMDDFRAALCEVSPSAIRELFVDIPDVR---WEDVGGLDDVRRRLIESVEWPI 474
Cdd:COG0464   98 LLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELReaiLDDLGGLEEVKEELRELVALPL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 475 KYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFLKARQAAPCIIFLD 554
Cdd:COG0464  178 KRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFID 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 555 EVDSVIPARNEGaiDSHVAERVLSQFLSEMDGLEElkGVFVMGATNRADLIDPAMLRpgRFDEIIELGLPDEDARRQILA 634
Cdd:COG0464  258 EADALAGKRGEV--GDGVGRRVVNTLLTEMEELRS--DVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFR 331
                        330       340       350
                 ....*....|....*....|....*....|....
gi 542097447 635 VHLRNKPLGDNIHADDLAERCDGASGAELAAVCN 668
Cdd:COG0464  332 IHLRKRPLDEDVDLEELAEATEGLSGADIRNVVR 365
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
180-443 1.94e-82

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: 276.79  E-value: 1.94e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  180 YEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGES 259
Cdd:TIGR01243 452 WSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGES 531
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  260 EAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGD-VEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPG 338
Cdd:TIGR01243 532 EKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTsVTDRIVNQLLTEMDGIQELSNVVVIAATNRPDILDPALLRPG 611
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  339 RFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRLLPEIDFSSAEL-PYD 417
Cdd:TIGR01243 612 RFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGSPAKEKLEVgEEE 691
                         250       260
                  ....*....|....*....|....*.
gi 542097447  418 RLAELTVMMDDFRAALCEVSPSAIRE 443
Cdd:TIGR01243 692 FLKDLKVEMRHFLEALKKVKPSVSKE 717
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
449-667 1.52e-80

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 261.69  E-value: 1.52e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 449 PDVRWEDVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRY 528
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 529 VGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPARNEGAI--DSHVaERVLSQFLSEMDGLEELKGVFVMGATNRADLID 606
Cdd:PRK03992 206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTsgDREV-QRTLMQLLAEMDGFDPRGNVKIIAATNRIDILD 284
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542097447 607 PAMLRPGRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVC 667
Cdd:PRK03992 285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAIC 345
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
462-619 2.54e-80

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: 252.97  E-value: 2.54e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 462 VRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFL 541
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447 542 KARQAAPCIIFLDEVDSVIPARNeGAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEII 619
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRG-QSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLI 157
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
180-433 2.65e-80

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: 261.77  E-value: 2.65e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 180 YEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGES 259
Cdd:COG0464  156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 260 EAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLknRGKVIVIAATNLPNAIDPALRRpgR 339
Cdd:COG0464  236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDLLDPALLR--R 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 340 FDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRLLPEIDfssaelpydrl 419
Cdd:COG0464  312 FDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVT----------- 380
                        250
                 ....*....|....
gi 542097447 420 aeltvmMDDFRAAL 433
Cdd:COG0464  381 ------TEDLLEAL 388
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
462-619 8.03e-78

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: 246.25  E-value: 8.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 462 VRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFL 541
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447 542 KARQAAPCIIFLDEVDSVIPARNEGAiDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEII 619
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTG-DSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
162-408 2.50e-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: 243.35  E-value: 2.50e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  162 IGKSNAVGNSSHSTqRLSYEDVGGLKNQVRRIREMIELpLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDA 241
Cdd:TIGR01241  37 FGKSKAKLLNEEKP-KVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  242 QFFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVG---DVEKRIVAQLLALMDGLKNRGKV 318
Cdd:TIGR01241 115 PFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGggnDEREQTLNQLLVEMDGFGTNTGV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  319 IVIAATNLPNAIDPALRRPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMS 398
Cdd:TIGR01241 195 IVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALL 274
                         250
                  ....*....|
gi 542097447  399 ALRRLLPEID 408
Cdd:TIGR01241 275 AARKNKTEIT 284
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
449-668 7.75e-71

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: 239.49  E-value: 7.75e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  449 PDVRWEDVGGLDDVRRRLIESVEWpIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRY 528
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  529 VGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPARNEGAIDSH-VAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDP 607
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNdEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542097447  608 AMLRPGRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVCN 668
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLN 269
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
449-667 2.51e-70

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


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 233.92  E-value: 2.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  449 PDVRWEDVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRY 528
Cdd:TIGR01242 117 PNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKY 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  529 VGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPAR-NEGAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDP 607
Cdd:TIGR01242 197 IGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRtDSGTSGDREVQRTLMQLLAELDGFDPRGNVKVIAATNRPDILDP 276
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  608 AMLRPGRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVC 667
Cdd:TIGR01242 277 ALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAIC 336
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
455-621 5.53e-68

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: 220.63  E-value: 5.53e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 455 DVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEK 534
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 535 GVRELFLKARQAAPCIIFLDEVDSVIPARNEGaiDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGR 614
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREED--QREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGR 158

                 ....*..
gi 542097447 615 FDEIIEL 621
Cdd:cd19503  159 FDREVEI 165
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
459-619 1.02e-66

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: 216.97  E-value: 1.02e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 459 LDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRE 538
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 539 LFLKARQAAPCIIFLDEVDSVIPARNEGaiDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEI 618
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDG--GSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKT 158

                 .
gi 542097447 619 I 619
Cdd:cd19530  159 L 159
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
162-402 1.23e-66

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 230.31  E-value: 1.23e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 162 IGKSNA---VGNSShstqRLSYEDVGGLKNQVRRIREMIELpLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQE 238
Cdd:COG0465  124 FGKSKAklyDEDKP----KVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGE 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 239 TDAQFFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVG---DVEKRIVAQLLALMDGLKNR 315
Cdd:COG0465  199 AGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGgghDEREQTLNQLLVEMDGFEGN 278
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 316 GKVIVIAATNLPNAIDPALRRPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREA 395
Cdd:COG0465  279 EGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVNEA 358

                 ....*..
gi 542097447 396 AMSALRR 402
Cdd:COG0465  359 ALLAARR 365
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
462-619 2.24e-66

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: 216.22  E-value: 2.24e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 462 VRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFL 541
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542097447 542 KARQAAPCIIFLDEVDSVIPARNEGAIDSH-VAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEII 619
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGGNIGDAGgAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
179-346 4.28e-66

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: 215.66  E-value: 4.28e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 179 SYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGE 258
Cdd:cd19502    1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 259 SEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHR--DKVVGDVE-KRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALR 335
Cdd:cd19502   81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdSGTGGDREvQRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|.
gi 542097447 336 RPGRFDREISI 346
Cdd:cd19502  161 RPGRFDRKIEF 171
ftsH CHL00176
cell division protein; Validated
450-668 9.29e-65

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 226.47  E-value: 9.29e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 450 DVRWEDVGGLDDVRRRLIESVEWpIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYV 529
Cdd:CHL00176 179 GITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFV 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 530 GDSEKGVRELFLKARQAAPCIIFLDEVDSVipARNEGA---IDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLID 606
Cdd:CHL00176 258 GVGAARVRDLFKKAKENSPCIVFIDEIDAV--GRQRGAgigGGNDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILD 335
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542097447 607 PAMLRPGRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVCN 668
Cdd:CHL00176 336 AALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLN 397
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
191-346 1.17e-63

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: 208.68  E-value: 1.17e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 191 RRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEA 270
Cdd:cd19511    3 RELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542097447 271 GRKGPSIIFLDEIDSIAPHR-DKVVGDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFDREISI 346
Cdd:cd19511   83 RQAAPCIIFFDEIDSLAPRRgQSDSSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
179-402 2.96e-63

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 216.17  E-value: 2.96e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 179 SYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGE 258
Cdd:PTZ00454 143 TYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKYLGE 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 259 SEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHR-DKVVG-DVE-KRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALR 335
Cdd:PTZ00454 223 GPRMVRDVFRLARENAPSIIFIDEVDSIATKRfDAQTGaDREvQRILLELLNQMDGFDQTTNVKVIMATNRADTLDPALL 302
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542097447 336 RPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRR 402
Cdd:PTZ00454 303 RPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
462-620 3.54e-63

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: 207.67  E-value: 3.54e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 462 VRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFL 541
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542097447 542 KARQAAPCIIFLDEVDSVIPARneGAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEIIE 620
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKR--GHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
449-668 1.02e-62

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 219.91  E-value: 1.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 449 PDVRWEDVGGLDDVRRRLIESVEWpIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRY 528
Cdd:COG0465  137 PKVTFDDVAGVDEAKEELQEIVDF-LKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 529 VGdseKG---VRELFLKARQAAPCIIFLDEVDSVIPARNEGAIDSHvAER--VLSQFLSEMDGLEELKGVFVMGATNRAD 603
Cdd:COG0465  216 VG---VGasrVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGH-DEReqTLNQLLVEMDGFEGNEGVIVIAATNRPD 291
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542097447 604 LIDPAMLRPGRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVCN 668
Cdd:COG0465  292 VLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLVN 356
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
182-346 4.02e-62

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: 204.95  E-value: 4.02e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 182 DVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEA 261
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 262 HLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNR----GKVIVIAATNLPNAIDPALRRP 337
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEktagGPVLVIGATNRPDSLDPALRRA 160

                 ....*....
gi 542097447 338 GRFDREISI 346
Cdd:cd19518  161 GRFDREICL 169
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
179-401 2.13e-61

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 212.32  E-value: 2.13e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 179 SYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGE 258
Cdd:PTZ00361 181 SYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGD 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 259 SEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEK---RIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALR 335
Cdd:PTZ00361 261 GPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKeiqRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALI 340
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542097447 336 RPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALR 401
Cdd:PTZ00361 341 RPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALR 406
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
455-622 3.37e-61

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: 202.67  E-value: 3.37e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 455 DVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEK 534
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 535 GVRELFLKARQAAPCIIFLDEVDSVIPARNEgaIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGR 614
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREK--THGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGR 158

                 ....*...
gi 542097447 615 FDEIIELG 622
Cdd:cd19519  159 FDREIDIG 166
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
453-620 9.16e-60

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: 198.72  E-value: 9.16e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 453 WEDVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDS 532
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 533 EKGVRELFLKARQAAPCIIFLDEVDSVIPARNEGAI--DSHVaERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAML 610
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTggDREV-QRTMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160
                        170
                 ....*....|
gi 542097447 611 RPGRFDEIIE 620
Cdd:cd19502  161 RPGRFDRKIE 170
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
430-665 1.21e-59

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: 209.57  E-value: 1.21e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  430 RAALCEVSPSAIRELFV-DIPDVRWEDVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAV 508
Cdd:TIGR03689 157 GYAFEAIPRTEVEDLVLeEVPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAV 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  509 AN-------ESGVN---VISVKGPALMSRYVGDSEKGVRELFLKARQAA----PCIIFLDEVDSVIPARNEGaIDSHVAE 574
Cdd:TIGR03689 237 ANslaarigAEGGGksyFLNIKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSG-VSSDVET 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  575 RVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEIIELGLPDEDARRQILAVHLR-NKPLgdnihADDLAE 653
Cdd:TIGR03689 316 TVVPQLLAEIDGVESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKYLTdDLPL-----PEDLAA 390
                         250
                  ....*....|..
gi 542097447  654 RcDGASGAELAA 665
Cdd:TIGR03689 391 H-DGDREATAAA 401
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
191-346 3.64e-59

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: 196.95  E-value: 3.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 191 RRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEA 270
Cdd:cd19529    3 QELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542097447 271 GRKGPSIIFLDEIDSIAPHRDKVVGD-VEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFDREISI 346
Cdd:cd19529   83 RQVAPCVIFFDEIDSIAPRRGTTGDSgVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
439-667 1.67e-58

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 203.46  E-value: 1.67e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 439 SAIRELFV-DIPDVRWEDVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVI 517
Cdd:PTZ00454 129 SSIQLLQMsEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFI 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 518 SVKGPALMSRYVGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPAR---NEGAiDSHVaERVLSQFLSEMDGLEELKGVF 594
Cdd:PTZ00454 209 RVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaQTGA-DREV-QRILLELLNQMDGFDQTTNVK 286
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542097447 595 VMGATNRADLIDPAMLRPGRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVC 667
Cdd:PTZ00454 287 VIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAIC 359
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
451-619 2.06e-58

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: 195.14  E-value: 2.06e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 451 VRWEDVGGLDDVRRRLIESVEWpIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVG 530
Cdd:cd19501    1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 531 DSEKGVRELFLKARQAAPCIIFLDEVDSVIPARNEGAIDSH-VAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAM 609
Cdd:cd19501   80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHdEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                        170
                 ....*....|
gi 542097447 610 LRPGRFDEII 619
Cdd:cd19501  160 LRPGRFDRQV 169
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
177-413 2.54e-58

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 209.12  E-value: 2.54e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 177 RLSYEDVGGLKNQVRRIREMIELpLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFY 256
Cdd:PRK10733 148 KTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFV 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 257 GESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVG---DVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPA 333
Cdd:PRK10733 227 GVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGgghDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPA 306
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 334 LRRPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALR---RLLPEIDFS 410
Cdd:PRK10733 307 LLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARgnkRVVSMVEFE 386

                 ...
gi 542097447 411 SAE 413
Cdd:PRK10733 387 KAK 389
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
182-343 3.72e-58

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: 194.65  E-value: 3.72e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 182 DVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQE--TDAQ---FFTISGPEIVHKFY 256
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAEcsKGGQkvsFFMRKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 257 GESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRR 336
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                 ....*..
gi 542097447 337 PGRFDRE 343
Cdd:cd19517  161 PGRFDRE 167
ftsH CHL00176
cell division protein; Validated
178-427 6.70e-58

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 207.60  E-value: 6.70e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 178 LSYEDVGGLKNQVRRIREMIELpLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYG 257
Cdd:CHL00176 180 ITFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVG 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 258 ESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVG---DVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPAL 334
Cdd:CHL00176 259 VGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIGggnDEREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAAL 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 335 RRPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRLLPEIDFSSAEL 414
Cdd:CHL00176 339 LRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARRKKATITMKEIDT 418
                        250
                 ....*....|....*.
gi 542097447 415 PYDRLA---ELTVMMD 427
Cdd:CHL00176 419 AIDRVIaglEGTPLED 434
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
181-395 5.70e-57

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 193.95  E-value: 5.70e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 181 EDVGGLKNQVRRIREMIElPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESE 260
Cdd:COG1223    2 DDVVGQEEAKKKLKLIIK-ELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 261 AHLRKIFEEAgRKGPSIIFLDEIDSIAPHRD--KVVGDVeKRIVAQLLALMDGLKNrgKVIVIAATNLPNAIDPALRRpg 338
Cdd:COG1223   81 RNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGdqNDVGEV-KRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR-- 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 542097447 339 RFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREA 395
Cdd:COG1223  155 RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
189-346 1.10e-56

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: 190.19  E-value: 1.10e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 189 QVRRIREMIELPLRYPEVfERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFE 268
Cdd:cd19481    1 LKASLREAVEAPRRGSRL-RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542097447 269 EAGRKGPSIIFLDEIDSIAPHRDKVVGD-VEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFDREISI 346
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKRDSSGESgELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
462-621 1.36e-55

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: 187.34  E-value: 1.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 462 VRRRLIESVEWPIKYPELYeQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFL 541
Cdd:cd19527    1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 542 KARQAAPCIIFLDEVDSVIPARNEGAIDSHVAERVLSQFLSEMDGLEE-LKGVFVMGATNRADLIDPAMLRPGRFDEIIE 620
Cdd:cd19527   80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGVMDRVVSQLLAELDGMSSsGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                 .
gi 542097447 621 L 621
Cdd:cd19527  160 L 160
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
459-621 1.25e-54

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: 184.41  E-value: 1.25e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 459 LDDVRRRLIESVEWPIKypelyEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRE 538
Cdd:cd19481    2 KASLREAVEAPRRGSRL-----RRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 539 LFLKARQAAPCIIFLDEVDSvIPARNEGAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEI 618
Cdd:cd19481   77 IFERARRLAPCILFIDEIDA-IGRKRDSSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155

                 ...
gi 542097447 619 IEL 621
Cdd:cd19481  156 IEF 158
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
439-668 1.34e-54

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 198.72  E-value: 1.34e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 439 SAIRELFVDIPDVRWEDVGGLDDVRRRLIESVEWpIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVIS 518
Cdd:PRK10733 137 SKARMLTEDQIKTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFT 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 519 VKGPALMSRYVGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPARNEGAIDSH-VAERVLSQFLSEMDGLEELKGVFVMG 597
Cdd:PRK10733 216 ISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGGGHdEREQTLNQMLVEMDGFEGNEGIIVIA 295
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542097447 598 ATNRADLIDPAMLRPGRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVCN 668
Cdd:PRK10733 296 ATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVN 366
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
179-391 5.09e-54

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: 194.16  E-value: 5.09e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  179 SYEDVGGLKNQVRRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIA---------RIIAQETDAQFF-TISG 248
Cdd:TIGR03689 180 TYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAkavanslaaRIGAEGGGKSYFlNIKG 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  249 PEIVHKFYGESEAHLRKIFEEAGRKG----PSIIFLDEIDSIAPHRDK-VVGDVEKRIVAQLLALMDGLKNRGKVIVIAA 323
Cdd:TIGR03689 260 PELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSgVSSDVETTVVPQLLAEIDGVESLDNVIVIGA 339
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447  324 TNLPNAIDPALRRPGRFDREISIPIPDREGRREIIEIHstgmpLNADVDLNVLADITHGFVGADLEAL 391
Cdd:TIGR03689 340 SNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKY-----LTDDLPLPEDLAAHDGDREATAAAL 402
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
453-667 6.17e-53

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 183.16  E-value: 6.17e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 453 WEDVGGLDDVRRRLIESVEWpIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDS 532
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKE-LRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGET 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 533 EKGVRELFLKARQaAPCIIFLDEVDSVIPARNegaiDSH-VAE--RVLSQFLSEMDGLEElkGVFVMGATNRADLIDPAM 609
Cdd:COG1223   80 ARNLRKLFDFARR-APCVIFFDEFDAIAKDRG----DQNdVGEvkRVVNALLQELDGLPS--GSVVIAATNHPELLDSAL 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447 610 LRpgRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVC 667
Cdd:COG1223  153 WR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVL 208
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
449-667 7.03e-53

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 189.21  E-value: 7.03e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 449 PDVRWEDVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRY 528
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 529 VGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPARnegaIDSHVA-----ERVLSQFLSEMDGLEELKGVFVMGATNRAD 603
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKR----YDATSGgekeiQRTMLELLNQLDGFDSRGDVKVIMATNRIE 333
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542097447 604 LIDPAMLRPGRFDEIIELGLPDEDARRQILAVHLRNKPLGDNIHADDLAERCDGASGAELAAVC 667
Cdd:PTZ00361 334 SLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAIC 397
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
179-346 7.60e-53

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: 180.12  E-value: 7.60e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 179 SYEDVGGLKNQVRRIREMIELpLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGE 258
Cdd:cd19501    2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 259 SEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVG---DVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALR 335
Cdd:cd19501   81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGgghDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALL 160
                        170
                 ....*....|.
gi 542097447 336 RPGRFDREISI 346
Cdd:cd19501  161 RPGRFDRQVYV 171
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
191-346 9.13e-52

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: 9.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 191 RRIREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEA 270
Cdd:cd19528    3 RELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFDKA 82
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542097447 271 GRKGPSIIFLDEIDSIAPHRDKVVGD---VEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFDREISI 346
Cdd:cd19528   83 RAAAPCVLFFDELDSIAKARGGNIGDaggAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
200-342 4.10e-50

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: 172.29  E-value: 4.10e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 200 PLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIF 279
Cdd:cd19530   15 PIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQRARASAPCVIF 94
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542097447 280 LDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFDR 342
Cdd:cd19530   95 FDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDK 157
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
455-621 4.48e-50

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 172.59  E-value: 4.48e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 455 DVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEK 534
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 535 GVRELFLKARQAAPCIIFLDEVDSVIPARnEGAiDSHVAERVLSQFLSEMDGLEEL----KGVFVMGATNRADLIDPAML 610
Cdd:cd19518   81 KIRELFDQAISNAPCIVFIDEIDAITPKR-ESA-QREMERRIVSQLLTCMDELNNEktagGPVLVIGATNRPDSLDPALR 158
                        170
                 ....*....|.
gi 542097447 611 RPGRFDEIIEL 621
Cdd:cd19518  159 RAGRFDREICL 169
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
218-347 6.22e-50

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: 170.85  E-value: 6.22e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  218 VLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDV 297
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 542097447  298 EKRIVAQLLALMDGLKNR-GKVIVIAATNLPNAIDPALRrpGRFDREISIP 347
Cdd:pfam00004  81 SRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
456-615 1.41e-48

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: 168.30  E-value: 1.41e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 456 VGGLDDVRRRLIESVEWPIKYPELYeQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKG 535
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 536 VRELFLKARQAAPCIIFLDEVDSVIPARNEGaiDSHVAERVLSQFLSEMDGLE--ELKGVFVMGATNRADLIDPAMLRpg 613
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSG--EHEASRRVKTEFLVQMDGVLnkPEDRVLVLGATNRPWELDEAFLR-- 155

                 ..
gi 542097447 614 RF 615
Cdd:cd19509  156 RF 157
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
491-623 2.09e-48

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 166.61  E-value: 2.09e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  491 LLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPARNEGaiDS 570
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG--GD 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 542097447  571 HVAERVLSQFLSEMDGLEELKG-VFVMGATNRADLIDPAMLrpGRFDEIIELGL 623
Cdd:pfam00004  79 SESRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
177-444 1.26e-47

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 172.61  E-value: 1.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 177 RLSYEDVGGLKNQVRRIREMIELPLRYPEVFErLGidAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFY 256
Cdd:NF041006  99 KVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP-LG--WPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 257 GESEAHLRKIFEEAGRKG-----PSIIFLDEIDSI-APHRDKVVGDVekRIVAQLLALMDGLKNRG---KVIVIAATNLP 327
Cdd:NF041006 176 GEAEKNVAKIFKKAREKSkeegkPAIIFIDEIDALlGVYSSEVGGEV--RVRNQFLKEMDGLQDKSenyHVYVIGATNKP 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 328 NAID-PALRrpgRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMSALRRLLPE 406
Cdd:NF041006 254 WRLDePFLR---RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFEK 330
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 542097447 407 idfssaelpydRLAE-LTVMMDDFRAALCEVSPSAIREL 444
Cdd:NF041006 331 -----------GLGEpRPITMEDFKEVLKIRKPSVNQEM 358
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
193-344 2.24e-46

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: 161.83  E-value: 2.24e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 193 IREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEAGR 272
Cdd:cd19526    5 LEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQS 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542097447 273 KGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFDREI 344
Cdd:cd19526   85 AKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLV 156
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
183-346 4.15e-44

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: 155.97  E-value: 4.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 183 VGGLKNQVRRIREMIELPLRYPEVFeRLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAH 262
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 263 LRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNR--GKVIVIAATNLPNAIDPALRRpgRF 340
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR--RF 157

                 ....*.
gi 542097447 341 DREISI 346
Cdd:cd19509  158 EKRIYI 163
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
449-619 4.20e-43

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: 153.48  E-value: 4.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 449 PDVRWEDVGGLDDVRRRLIESVEWPIKYPELYeQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRY 528
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLF-TGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 529 VGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPARNEGaiDSHVAERVLSQFLSEMDGL-EELKGVFVMGATNRADLIDP 607
Cdd:cd19521   81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEG--ESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDS 158
                        170
                 ....*....|..
gi 542097447 608 AMLRpgRFDEII 619
Cdd:cd19521  159 AIRR--RFEKRI 168
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
193-342 7.27e-43

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: 152.28  E-value: 7.27e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 193 IREMIELPLRYPEVFErLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEAGR 272
Cdd:cd19527    5 ILDTIQLPLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQKARD 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542097447 273 KGPSIIFLDEIDSIAPHRDKV--VGDVEKRIVAQLLALMDGLKNRGK-VIVIAATNLPNAIDPALRRPGRFDR 342
Cdd:cd19527   84 AKPCVIFFDELDSLAPSRGNSgdSGGVMDRVVSQLLAELDGMSSSGQdVFVIGATNRPDLLDPALLRPGRFDK 156
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
455-615 2.62e-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: 151.04  E-value: 2.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 455 DVGGLDDVRRRLIESVEWPIKYPELYEQAGV-KPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSE 533
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 534 KGVRELFLKARQAAPCIIFLDEVDSVIPARNEGaiDSHVAERVLSQFLSEMDGL--EELKGVFVMGATNRADLIDPAMLR 611
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST--DHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAILR 158

                 ....*.
gi 542097447 612 --PGRF 615
Cdd:cd19520  159 rmPKRF 164
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
455-616 1.92e-41

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: 148.81  E-value: 1.92e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 455 DVGGLDDVRRRLIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANE--SGVNVISV---KGPALMSRYV 529
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAEcsKGGQKVSFfmrKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 530 GDSEKGVRELFLKARQAAPCIIFLDEVDSVIPARNEGAIDSHVAerVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAM 609
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHAS--IVSTLLALMDGLDNRGQVVVIGATNRPDALDPAL 158

                 ....*..
gi 542097447 610 LRPGRFD 616
Cdd:cd19517  159 RRPGRFD 165
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
182-340 6.36e-39

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 141.41  E-value: 6.36e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 182 DVGGLKNQVRRIREMIELPLRYPEVFERLGI-DAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESE 260
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 261 AHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRG--KVIVIAATNLPNAIDPALRR-- 336
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGncRVIVMGATNRPQDLDEAILRrm 160

                 ....
gi 542097447 337 PGRF 340
Cdd:cd19520  161 PKRF 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
456-621 2.18e-38

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: 140.32  E-value: 2.18e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 456 VGGLD----DVRRRLIESVEWPikyPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAV-----ANESGVnvisVKGPALMS 526
Cdd:cd19504    2 IGGLDkefsDIFRRAFASRVFP---PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 527 RYVGDSEKGVRELFLKARQ--------AAPCIIFLDEVDSVIPARNEGAIDSHVAERVLSQFLSEMDGLEELKGVFVMGA 598
Cdd:cd19504   75 KYVGESEANIRKLFADAEEeqrrlganSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGM 154
                        170       180
                 ....*....|....*....|...
gi 542097447 599 TNRADLIDPAMLRPGRFDEIIEL 621
Cdd:cd19504  155 TNRKDLIDEALLRPGRLEVQMEI 177
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
449-611 2.51e-38

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 140.51  E-value: 2.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 449 PDVRWEDVGGLDDVRRRLIESVEWPIKYPELYeqAGVK-PPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSR 527
Cdd:cd19525   17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 528 YVGDSEKGVRELFLKARQAAPCIIFLDEVDSVIPARNEGAIDShvAERVLSQFLSEMDGLEEL--KGVFVMGATNRADLI 605
Cdd:cd19525   95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHES--SRRIKTEFLVQLDGATTSseDRILVVGATNRPQEI 172

                 ....*.
gi 542097447 606 DPAMLR 611
Cdd:cd19525  173 DEAARR 178
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
180-346 2.54e-37

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 137.30  E-value: 2.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 180 YEDVGGLKNQVRRIREMIELPLRYPEVFErlGIDAP-KGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGE 258
Cdd:cd19521    6 WEDVAGLEGAKEALKEAVILPVKFPHLFT--GNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWMGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 259 SEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGL-KNRGKVIVIAATNLPNAIDPALRRp 337
Cdd:cd19521   84 SEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSAIRR- 162

                 ....*....
gi 542097447 338 gRFDREISI 346
Cdd:cd19521  163 -RFEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
455-611 6.50e-37

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: 135.75  E-value: 6.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 455 DVGGLDDVRRRLIESVEWPIKYPELYeqAGVK-PPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSE 533
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 534 KGVRELFLKARQAAPCIIFLDEVDSVIPARNEGaiDSHVAERVLSQFLSEMDGLEELKG--VFVMGATNRADLIDPAMLR 611
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEG--EHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR 156
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
182-346 5.34e-36

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: 133.57  E-value: 5.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 182 DVGGLKNQVRRIREMIELPLRYPEVFErlGIDAP-KGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESE 260
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 261 AHLRKIFEEAGRKGPSIIFLDEIDSIAPHR-DKVVGDVEKRIVAQLLALMDGLKN-------RGKVIVIAATNLPNAIDP 332
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVGGasenddpSKMVMVLAATNFPWDIDE 158
                        170
                 ....*....|....
gi 542097447 333 ALRRpgRFDREISI 346
Cdd:cd19522  159 ALRR--RLEKRIYI 170
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
183-346 4.99e-35

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 131.07  E-value: 4.99e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 183 VGGLKNQVRRI-REMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTI-SGPEIVHKFYGESE 260
Cdd:cd19504    2 IGGLDKEFSDIfRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 261 AHLRKIF----EEAGRKGPS----IIFLDEIDSIAPHRDKVVGD--VEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAI 330
Cdd:cd19504   82 ANIRKLFadaeEEQRRLGANsglhIIIFDEIDAICKQRGSMAGStgVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLI 161
                        170
                 ....*....|....*.
gi 542097447 331 DPALRRPGRFDREISI 346
Cdd:cd19504  162 DEALLRPGRLEVQMEI 177
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
178-346 8.72e-35

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 130.49  E-value: 8.72e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 178 LSYEDVGGLKNQVRRIREMIELPLRYPEVFErlGIDAP-KGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFY 256
Cdd:cd19525   19 INWADIAGLEFAKKTIKEIVVWPMLRPDIFT--GLRGPpKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 257 GESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRG--KVIVIAATNLPNAIDPAL 334
Cdd:cd19525   97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSedRILVVGATNRPQEIDEAA 176
                        170
                 ....*....|..
gi 542097447 335 RRpgRFDREISI 346
Cdd:cd19525  177 RR--RLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
455-611 3.45e-34

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 128.56  E-value: 3.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 455 DVGGLDDVRRRLIESVEWPIKYPELYEqaGVKPP-KGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSE 533
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 534 KGVRELFLKARQAAPCIIFLDEVDSVIPARneGAIDSHVA-ERVLSQFLSEMDGL-------EELKGVFVMGATNRADLI 605
Cdd:cd19522   79 KLVRLLFEMARFYAPTTIFIDEIDSICSRR--GTSEEHEAsRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDI 156

                 ....*.
gi 542097447 606 DPAMLR 611
Cdd:cd19522  157 DEALRR 162
ycf46 CHL00195
Ycf46; Provisional
449-663 4.38e-32

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 130.52  E-value: 4.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 449 PDVRWEDVGGLDDVRRrliesveWPIKYPELY-EQA---GVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPAL 524
Cdd:CHL00195 223 VNEKISDIGGLDNLKD-------WLKKRSTSFsKQAsnyGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 525 MSRYVGDSEKGVRELFLKARQAAPCIIFLDEVDSVIpARNEGAIDSHVAERVLSQFLSEMDglEELKGVFVMGATNRADL 604
Cdd:CHL00195 296 FGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAF-SNSESKGDSGTTNRVLATFITWLS--EKKSPVFVVATANNIDL 372
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542097447 605 IDPAMLRPGRFDEIIELGLPDEDARRQILAVHLRN-KPLG-DNIHADDLAERCDGASGAEL 663
Cdd:CHL00195 373 LPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKfRPKSwKKYDIKKLSKLSNKFSGAEI 433
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
455-618 5.14e-32

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: 121.71  E-value: 5.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 455 DVGGLDDVRRRL-IESVEWPIKYpelyEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSE 533
Cdd:cd19507    1 DVGGLDNLKDWLkKRKAAFSKQA----SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 534 KGVRELFLKARQAAPCIIFLDEVDSVIpARNEGAIDSHVAERVLSQFLSEMDglEELKGVFVMGATNRADLIDPAMLRPG 613
Cdd:cd19507   77 SRLRQMIQTAEAIAPCVLWIDEIEKGF-SNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKG 153

                 ....*
gi 542097447 614 RFDEI 618
Cdd:cd19507  154 RFDEI 158
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
182-346 1.15e-29

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: 115.33  E-value: 1.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 182 DVGGLKNQVRRIREMIELPLRYPEVFErlGIDAP-KGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESE 260
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFT--GLRAPaRGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 261 AHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRG--KVIVIAATNLPNAIDPALRRpg 338
Cdd:cd19524   79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGddRVLVMGATNRPQELDDAVLR-- 156

                 ....*...
gi 542097447 339 RFDREISI 346
Cdd:cd19524  157 RFTKRVYV 164
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
457-623 3.39e-27

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 107.62  E-value: 3.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 457 GGLDDVRRRLIESVEWPikypelyeqagvkPPKGLLLAGPPGVGKTLIAKAVANES---GVNVISVKGPALMSRYVGDSE 533
Cdd:cd00009    1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 534 KG---VRELFLKARQAAPCIIFLDEVDSviparnegaIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAML 610
Cdd:cd00009   68 FGhflVRLLFELAEKAKPGVLFIDEIDS---------LSRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRA 138
                        170
                 ....*....|...
gi 542097447 611 RPGRFDEIIELGL 623
Cdd:cd00009  139 LYDRLDIRIVIPL 151
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
205-347 6.65e-25

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: 101.07  E-value: 6.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 205 EVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQET---DAQFFTISGPEIVHKFYGESEAH---LRKIFEEAGRKGPSII 278
Cdd:cd00009    9 ALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGhflVRLLFELAEKAKPGVL 88
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542097447 279 FLDEIDSIAPhrdkvvgDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFDREISIP 347
Cdd:cd00009   89 FIDEIDSLSR-------GAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
CDC48_N pfam02359
Cell division protein 48 (CDC48), N-terminal domain; This domain has a double psi-beta barrel ...
6-90 8.45e-23

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: 92.64  E-value: 8.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447    6 KLKVAEALPKDAGRGYARLDPADMARLNLAVGDIVQLTSKKGTgIAKLMPTYPDMRNKGIVQLDGLTRRNTSLSLDEKVQ 85
Cdd:pfam02359   1 RLRVAEAPDRDVGRGIARLNPEDMEELGLFPGDVVEIKGKRKT-VAIVWSAYPEDEGPGIIRMDGVTRKNAGVSIGDTVT 79

                  ....*
gi 542097447   86 IEPAS 90
Cdd:pfam02359  80 VRPAE 84
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
455-611 2.37e-22

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: 94.18  E-value: 2.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 455 DVGGLDDVRRRLIESVEWPIKYPELYEqAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDSEK 534
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFS-GLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 542097447 535 GVRELFLKARQAAPCIIFLDEVDSVIPARNEGAidsHVAERVLSQFLSEMDGL--EELKGVFVMGATNRADLIDPAMLR 611
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEA---SPVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
CDC48_N smart01073
Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel ...
7-89 1.28e-20

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: 86.51  E-value: 1.28e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447     7 LKVAEAL-PKDAGRGYARLDPADMARLNLAVGDIVQLTSKKGTgIAKLMPTYPDMRNkGIVQLDGLTRRNTSLSLDEKVQ 85
Cdd:smart01073   1 LRVAEAPsDEDVGRGIARLSPEDMDELGLFPGDYVLITGKRRT-VAIVWPAYPEDPG-GIIRIDGVQRKNAGVSIGDTVT 78

                   ....
gi 542097447    86 IEPA 89
Cdd:smart01073  79 VRKA 82
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
182-336 3.36e-20

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: 88.02  E-value: 3.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 182 DVGGLKNQVRRIREMIELPLRYPEVFERLgIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEA 261
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542097447 262 HLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVGDVeKRIVAQLLALMDGLKNRGK--VIVIAATNLPNAIDPALRR 336
Cdd:cd19523   80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEASPV-GRLQVELLAQLDGVLGSGEdgVLVVCTTSKPEEIDESLRR 155
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
208-342 2.37e-17

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: 79.72  E-value: 2.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 208 ERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIFLDEIDS-I 286
Cdd:cd19507   24 SAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKgF 103
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 542097447 287 APHRDKVVGDVEKRIVAQLLALMDGLKNrgKVIVIAATNLPNAIDPALRRPGRFDR 342
Cdd:cd19507  104 SNADSKGDSGTSSRVLGTFLTWLQEKKK--PVFVVATANNVQSLPPELLRKGRFDE 157
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
487-625 6.10e-17

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: 78.18  E-value: 6.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447   487 PPKGLLLAGPPGVGKTLIAKAVANESGVN---VISVKGPALMSR--------------YVGDSEKGVRELFLKARQAAPC 549
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILEEvldqllliivggkkASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542097447   550 IIFLDEVDSVIPARNEGAIDSHVAERVLSQFLSEmdgleelKGVFVMGATNRADLIDPAMLRPgRFDEIIELGLPD 625
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSE-------KNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
215-350 2.54e-15

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: 73.56  E-value: 2.54e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447   215 PKGVLLSGPPGCGKTLIARIIAQE---TDAQFFTISGPEI--------------VHKFYGESEAHLRKIFEEAGRKGPSI 277
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARElgpPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542097447   278 IFLDEIDSIAPHRDKVVgdvekRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPgRFDREISIPIPD 350
Cdd:smart00382  82 LILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
ycf46 CHL00195
Ycf46; Provisional
179-389 1.89e-14

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 76.60  E-value: 1.89e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 179 SYEDVGGLKN----QVRRIREMIELPLRYpevferlGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHK 254
Cdd:CHL00195 226 KISDIGGLDNlkdwLKKRSTSFSKQASNY-------GLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGG 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 255 FYGESEAHLRKIFEEAGRKGPSIIFLDEIDSiAPHRDKVVGD--VEKRIVAQLLALMDGLKNrgKVIVIAATNLPNAIDP 332
Cdd:CHL00195 299 IVGESESRMRQMIRIAEALSPCILWIDEIDK-AFSNSESKGDsgTTNRVLATFITWLSEKKS--PVFVVATANNIDLLPL 375
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 542097447 333 ALRRPGRFDREISIPIPDREGRREIIEIH-STGMPLN-ADVDLNVLADITHGFVGADLE 389
Cdd:CHL00195 376 EILRKGRFDEIFFLDLPSLEEREKIFKIHlQKFRPKSwKKYDIKKLSKLSNKFSGAEIE 434
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
218-404 4.58e-14

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 74.74  E-value: 4.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 218 VLLSGPPGCGKTLIARIIAQETDAQFFTISGPEivhkfygESEAHLRKIFEEA----GRKGPSIIFLDEIdsiapHR-DK 292
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEArqrrSAGRRTILFIDEI-----HRfNK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 293 vvgdvekrivAQ---LLALMDglknRGKVIVIAAT--NlPN-AIDPALRrpgrfdreiSipipdregRREIIEIHstgmP 366
Cdd:PRK13342 107 ----------AQqdaLLPHVE----DGTITLIGATteN-PSfEVNPALL---------S--------RAQVFELK----P 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 542097447 367 LNADvDL-----NVLADITHGFVGADLEALCREAAMSA--LRRLL 404
Cdd:PRK13342 151 LSEE-DIeqllkRALEDKERGLVELDDEALDALARLANgdARRAL 194
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
370-410 2.49e-13

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: 64.48  E-value: 2.49e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 542097447  370 DVDLNVLADITHGFVGADLEALCREAAMSALRRLLPEIDFS 410
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQE 41
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
466-621 6.45e-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: 66.99  E-value: 6.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 466 LIESVEWPIKYPELYEQAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNV--ISVKGpalmsryVGDSEKGVRELFLKA 543
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDIcdLNLSE-------VVLTDDRLNHLLNTA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 544 RQAApcIIFLDEVDSVIPARN---EGAIDSHVAERV-LSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEII 619
Cdd:cd19510   74 PKQS--IILLEDIDAAFESREhnkKNPSAYGGLSRVtFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151

                 ..
gi 542097447 620 EL 621
Cdd:cd19510  152 YM 153
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
193-344 9.29e-12

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 63.52  E-value: 9.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 193 IREMIELPLRYPEVFERLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVhkfygESEAHLRKIFEEAGR 272
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVV-----LTDDRLNHLLNTAPK 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447 273 KgpSIIFLDEIDS------IAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPALRRPGRFDREI 344
Cdd:cd19510   76 Q--SIILLEDIDAafesreHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
218-324 1.02e-11

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 67.77  E-value: 1.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 218 VLLSGPPGCGKTLIARIIAQETDAQFFTISGpeiVhkFYGESEahLRKIFEEA----GRKGPSIIFLDEIdsiapHR--- 290
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA---V--TSGVKD--IREVIEEArerrAYGRRTILFVDEI-----HRfnk 119
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 542097447 291 ---DKVVGDVEKrivaqllalmdglknrGKVIVIAAT 324
Cdd:COG2256  120 aqqDALLPHVED----------------GTITLIGAT 140
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
209-346 8.12e-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: 8.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 209 RLGIDAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTIS--------------GPEIVHKFYGESEAHLRKIFEEAGRKG 274
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynkpdfgndDWIDGMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542097447 275 PSIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLA--LMDGLKNRGK--VIVIAATNLPNAIDPALRRPGRFDREISI 346
Cdd:cd19505   86 PCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLnyLSRDFEKSSTrnILVIASTHIPQKVDPALIAPNRLDTCINI 161
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
218-334 1.28e-09

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: 58.61  E-value: 1.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 218 VLLSGPPGCGKTLIARIIAQETD---------AQFFTISGPEIVHKFYGESEAHLRKIF---EEAGRKGPSIIFL--DEI 283
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSirlssryryGQLIEINSHSLFSKWFSESGKLVTKMFqkiQELIDDKDALVFVliDEV 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 542097447 284 DSIAPHRDKVVGDVEK----RIVAQLLALMDGLKNRGKVIVIAATNLPNAIDPAL 334
Cdd:cd19508  135 ESLAAARSASSSGTEPsdaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
PRK04195 PRK04195
replication factor C large subunit; Provisional
454-557 3.36e-09

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 59.93  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 454 EDVGGLDDVRRRLIESVE-WpikypelyeQAGvKPPKGLLLAGPPGVGKTLIAKAVANESGVNVIS-----VKGPALMSR 527
Cdd:PRK04195  14 SDVVGNEKAKEQLREWIEsW---------LKG-KPKKALLLYGPPGVGKTSLAHALANDYGWEVIElnasdQRTADVIER 83
                         90       100       110
                 ....*....|....*....|....*....|
gi 542097447 528 YVGDSEKGvRELFLKARQaapcIIFLDEVD 557
Cdd:PRK04195  84 VAGEAATS-GSLFGARRK----LILLDEVD 108
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
217-340 2.55e-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: 53.07  E-value: 2.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  217 GVLLSGPPGCGKTLIARIIAQETD-AQFFTISGpeivHKFYGESE------------AHLRKIFEEAGRKGpSIIFLDEI 283
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSnRPVFYVQL----TRDTTEEDlfgrrnidpggaSWVDGPLVRAAREG-EIAVLDEI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 542097447  284 DSIAPH-RDKVVGDVEKRIvaqlLALMDG----LKNRGKVIVIAATNLP----NAIDPALRRpgRF 340
Cdd:pfam07728  76 NRANPDvLNSLLSLLDERR----LLLPDGgelvKAAPDGFRLIATMNPLdrglNELSPALRS--RF 135
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
187-360 3.00e-08

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 56.78  E-value: 3.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  187 KNQVRRIREMIELPLRYPEvferLGIDAP---KGVLLSGPPGCGKTLIARIIAQETdAQFFTISGPEIVH--------KF 255
Cdd:TIGR03922 285 KRQVAALKSSTAMALARAE----RGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIY-CGLGVLRKPLVREvsradligQY 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  256 YGESEAHLRKIFEEA-GRkgpsIIFLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDglKNRGKVIVIAAtNLPNAID--- 331
Cdd:TIGR03922 360 IGESEAKTNEIIDSAlGG----VLFLDEAYTLVETGYGQKDPFGLEAIDTLLARME--NDRDRLVVIGA-GYRKDLDkfl 432
                         170       180       190
                  ....*....|....*....|....*....|....
gi 542097447  332 ---PALRRpgRFDREISIP--IPDregrrEIIEI 360
Cdd:TIGR03922 433 evnEGLRS--RFTRVIEFPsySPD-----ELVEI 459
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
491-608 4.11e-08

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: 53.99  E-value: 4.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 491 LLLAGPPGVGKTLIAKAVANESGVN---------VISVKGPALMSRYVGDSEKGVRELFLKARQAAP---CIIFL--DEV 556
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKLSIRlssryrygqLIEINSHSLFSKWFSESGKLVTKMFQKIQELIDdkdALVFVliDEV 134
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 542097447 557 DSVIPARN--EGAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPA 608
Cdd:cd19508  135 ESLAAARSasSSGTEPSDAIRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
486-619 6.11e-08

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: 52.95  E-value: 6.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 486 KPPKGLLLAGPPGVGKTLIAKAVA---NESGVNVISVKGPALMSR------------YVGDSEKGVreLFLKARQAAPCI 550
Cdd:cd19499   39 RPIGSFLFLGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYVGYTEGGQ--LTEAVRRKPYSV 116
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447 551 IFLDEVDSViparnegaiDSHVAeRVLSQFLSemDG-LEELKG--------VFVMgATNRadlIDPAMLrpGRFDEII 619
Cdd:cd19499  117 VLLDEIEKA---------HPDVQ-NLLLQVLD--DGrLTDSHGrtvdfkntIIIM-TSNH---FRPEFL--NRIDEIV 176
CDC48_2 pfam02933
Cell division protein 48 (CDC48), domain 2; This domain has a double psi-beta barrel fold and ...
107-167 8.29e-08

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: 49.54  E-value: 8.29e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542097447  107 NQRDLDYIGSLLDGLPVQKGDLLRAHLFGsRSADFKVESTIPDGAVLIDPTTTLVIGKSNA 167
Cdd:pfam02933   3 DGDELAYVKRNLEGRPVSKGDTIVVEFLG-GAIPLVVVSTEPSGPVVVTETTEIEIGEKPV 62
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
213-290 1.11e-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: 51.73  E-value: 1.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447  213 DAPKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKfyGESEAHLRKIfeEAGrkgpSIIFLDEIdsiapHR 290
Cdd:pfam05496  31 EALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAIERP--GDLAAILTNL--EPG----DVLFIDEI-----HR 95
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
199-327 2.47e-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: 50.99  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 199 LPLRYPEVFERlgidAP--KGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFYGES--EAHLRKIFEEAGRKG 274
Cdd:cd19506   12 LPLGSQAVHEK----APlvKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQ 87
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 542097447 275 PSIIFLDEIDSI----APHRDKVVGdvEKRIVAQLLALMDGLKNRGKVIVIAATNLP 327
Cdd:cd19506   88 PSVIWIGDAEKTfykkVPKTEKQLD--PKRLKKDLPKILKSLKPEDRVLIVGTTSRP 142
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
461-601 3.02e-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: 50.60  E-value: 3.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 461 DVRRRLIESVEWPIKYPELYEQAGVKppKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMSRYVGDS--EKGVRE 538
Cdd:cd19506    1 DVRQLLTLYGILPLGSQAVHEKAPLV--KSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHL 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542097447 539 LFLKARQAAPCIIFLDEVDSV----IPaRNEGAIDSHVAERVLSQFLSEMDGLEElkgVFVMGATNR 601
Cdd:cd19506   79 VLKVARQLQPSVIWIGDAEKTfykkVP-KTEKQLDPKRLKKDLPKILKSLKPEDR---VLIVGTTSR 141
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
488-557 4.15e-07

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 50.27  E-value: 4.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  488 PKG-LLLAGPPGVGKTLIAKAVANESGV---NVISVKGPALM-----SR-------YVGDSEKGVreLFLKARQAAPCII 551
Cdd:pfam07724   2 PIGsFLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMeehsvSRligappgYVGYEEGGQ--LTEAVRRKPYSIV 79

                  ....*.
gi 542097447  552 FLDEVD 557
Cdd:pfam07724  80 LIDEIE 85
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
458-652 6.09e-07

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: 52.54  E-value: 6.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  458 GLDDVRRRlIESVEWPIKYPELYEQAGVKPP---KGLLLAGPPGVGKTLIAKAVANES---GV----NVISVKGPALMSR 527
Cdd:TIGR03922 280 GLERVKRQ-VAALKSSTAMALARAERGLPVAqtsNHMLFAGPPGTGKTTIARVVAKIYcglGVlrkpLVREVSRADLIGQ 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  528 YVGDSEKGVRELFLKARQAapcIIFLDEVDSVIpARNEGAIDSHVAErVLSQFLSEMDGLEELKGVFVMGATNRAD-LID 606
Cdd:TIGR03922 359 YIGESEAKTNEIIDSALGG---VLFLDEAYTLV-ETGYGQKDPFGLE-AIDTLLARMENDRDRLVVIGAGYRKDLDkFLE 433
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542097447  607 PAMLRPGRF-----------DEIIELG---------LPDEDARRQIL--AVHLRNKPL----GDNIHADDLA 652
Cdd:TIGR03922 434 VNEGLRSRFtrviefpsyspDELVEIArrmaterdsVLDDAAADALLeaATTLAQDTTpdanGDLRRGLDIA 505
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
489-620 1.07e-06

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: 48.68  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 489 KGLLLAGPPGVGKTLIAKAVANESGVNVISVKGP--ALMSRyvgDSEKGVRELFLKARQAAP-CIIFLDEVDSVIPARNE 565
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGdvAPMGR---EGVTAIHKVFDWANTSRRgLLLFVDEADAFLRKRST 99
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 542097447 566 GAIdSHVAERVLSQFLSEMdGLEELKGVFVMgATNRADLIDPAMlrPGRFDEIIE 620
Cdd:cd19512  100 EKI-SEDLRAALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVE 149
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
216-341 1.30e-06

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: 48.68  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 216 KGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEiVHKFYGESEAHLRKIFEEAG--RKGpSIIFLDEIDSIAPHRDKV 293
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAIHKVFDWANtsRRG-LLLFVDEADAFLRKRSTE 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 542097447 294 VGDVEKRIVAQLLALMDGLKNRgKVIVIAATNLPNAIDPALRrpGRFD 341
Cdd:cd19512  101 KISEDLRAALNAFLYRTGEQSN-KFMLVLASNQPEQFDWAIN--DRID 145
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
218-288 2.09e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 50.51  E-value: 2.09e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542097447 218 VLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKfyGESEAHLRKIfeEAGrkgpSIIFLDEIDSIAP 288
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPALEKP--GDLAAILTNL--EEG----DVLFIDEIHRLSP 116
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
215-311 2.32e-06

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: 48.53  E-value: 2.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 215 PKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKFY--GESEAHLRKIFEeagrkgpSIIFLDEIDSIAPHRDK 292
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEVGYvgRDVESIIRDLVE-------GIVFIDEIDKIAKRGGS 118
                         90       100
                 ....*....|....*....|
gi 542097447 293 VVGDVEKRIVAQ-LLALMDG 311
Cdd:cd19498  119 SGPDVSREGVQRdLLPIVEG 138
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
209-288 3.40e-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: 49.61  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  209 RLGIDAPKG-------VLLSGPPGCGKTLIARIIAQETDAQFFTISGPEIVHKfyGESEAHLRKIfeEAGrkgpSIIFLD 281
Cdd:TIGR00635  17 QLFIEAAKMrqealdhLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALEKP--GDLAAILTNL--EEG----DVLFID 88

                  ....*..
gi 542097447  282 EIDSIAP 288
Cdd:TIGR00635  89 EIHRLSP 95
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
218-366 3.76e-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: 49.40  E-value: 3.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 218 VLLSGPPGCGKTLIARIIAQETDAQF----FT-------ISGPEIVHKFYGESEAHLRKIFEeagrkgpSIIFLDEIDSI 286
Cdd:COG0714   34 LLLEGVPGVGKTTLAKALARALGLPFiriqFTpdllpsdILGTYIYDQQTGEFEFRPGPLFA-------NVLLADEINRA 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 287 APhrdkvvgDVEkrivAQLLALM-------DG----LKNRgkVIVIAATN---------LPnaidPALRRpgRFDREISI 346
Cdd:COG0714  107 PP-------KTQ----SALLEAMeerqvtiPGgtykLPEP--FLVIATQNpieqegtypLP----EAQLD--RFLLKLYI 167
                        170       180
                 ....*....|....*....|
gi 542097447 347 PIPDREGRREIIEIHSTGMP 366
Cdd:COG0714  168 GYPDAEEEREILRRHTGRHL 187
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
491-524 6.77e-06

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: 46.72  E-value: 6.77e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 542097447  491 LLLAGPPGVGKTLIAKAVANESGVNVISVKGPAL 524
Cdd:pfam05496  36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
218-251 7.88e-06

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 48.54  E-value: 7.88e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 542097447 218 VLLSGPPGCGKTLIARIIAQETDAQFFTISGPEI 251
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGPAI 90
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
482-619 8.23e-06

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 46.60  E-value: 8.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 482 QAGVKPPKGLLLAGPPGVGKTLIAKAVANESGVNVISV--------------KGPALMSRYVGDSEKGVRELFLKARQAA 547
Cdd:cd19505    6 RLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRIslnkllynkpdfgnDDWIDGMLILKESLHRLNLQFELAKAMS 85
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 542097447 548 PCIIFLD---EVDsVIPARNEGAIDSHVAERVLSQFLSEMDGLEELKGVFVMGATNRADLIDPAMLRPGRFDEII 619
Cdd:cd19505   86 PCIIWIPnihELN-VNRSTQNLEEDPKLLLGLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCI 159
ycf2 CHL00206
Ycf2; Provisional
209-395 8.34e-06

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 49.52  E-value: 8.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  209 RLGIDAPKGVLLSGPPGCGKTLIARIIA-------------------------------------------QETDAQFFT 245
Cdd:CHL00206 1624 RLALSPSRGILVIGSIGTGRSYLVKYLAtnsyvpfitvflnkfldnkpkgfliddididdsddiddsddidRDLDTELLT 1703
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  246 ISGPEIVHKFYGESEAHLRKIFEEAGRKGPSIIFLDEIDSIAPHRDKVVgdvekrivaQLLALMDGLKNR------GKVI 319
Cdd:CHL00206 1704 MMNALTMDMMPKIDRFYITLQFELAKAMSPCIIWIPNIHDLNVNESNYL---------SLGLLVNSLSRDcercstRNIL 1774
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  320 VIAATNLPNAIDPALRRPGRFDREISIP---IPDREgRREIIEIHSTGMPLNADV-DLNVLADITHGFVGADLEALCREA 395
Cdd:CHL00206 1775 VIASTHIPQKVDPALIAPNKLNTCIKIRrllIPQQR-KHFFTLSYTRGFHLEKKMfHTNGFGSITMGSNARDLVALTNEA 1853
PRK13341 PRK13341
AAA family ATPase;
219-334 8.96e-06

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 49.28  E-value: 8.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 219 LLSGPPGCGKTLIARIIAQETDAQFFTISGpeIVHkfyGESEahLRKIFEEA----GRKGP-SIIFLDEIdsiapHR-DK 292
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA--VLA---GVKD--LRAEVDRAkerlERHGKrTILFIDEV-----HRfNK 123
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 542097447 293 vvgdvekrivAQLLALMDGLKNrGKVIVIAAT--NLPNAIDPAL 334
Cdd:PRK13341 124 ----------AQQDALLPWVEN-GTITLIGATteNPYFEVNKAL 156
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
491-524 1.37e-05

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 47.82  E-value: 1.37e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 542097447 491 LLLAGPPGVGKTLIAKAVANESGVNVISVKGPAL 524
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
491-556 2.52e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 47.39  E-value: 2.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 491 LLLAGPPGVGKTLIAKAVANESGVNVISVKGpalmsryVGDSEKGVRELFLKARQAA----PCIIFLDEV 556
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSA-------VTSGVKDLREVIEEARQRRsagrRTILFIDEI 101
CDC48_2 smart01072
Cell division protein 48 (CDC48) domain 2; This domain has a double psi-beta barrel fold and ...
107-169 3.00e-05

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: 42.20  E-value: 3.00e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542097447   107 NQRDLDYIGSLLDGLPVQKGDLLRAHLFGsRSADFKVESTIPDGAVLIDPTTTLVIGKSNAVG 169
Cdd:smart01072   3 DGDFAEYVKRKLLGRPVTKGDTIVVPFLG-KALPFVVVSTEPSGPVIVTDDTEIEILEKPVEE 64
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
491-556 3.37e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 46.97  E-value: 3.37e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 491 LLLAGPPGVGKTLIAKAVANESGVNVISVKGpalmsryVGDSEKGVRELFLKARQAA----PCIIFLDEV 556
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVALSA-------VTSGVKDIREVIEEARERRaygrRTILFVDEI 114
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
215-326 3.68e-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: 44.88  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  215 PKGV-LLSGPPGCGKTLIARIIAQE--TDAQFFTISG------PEIVHKFYGESEAHLRkiFEEAG-------RKGPSII 278
Cdd:pfam07724   2 PIGSfLFLGPTGVGKTELAKALAELlfGDERALIRIDmseymeEHSVSRLIGAPPGYVG--YEEGGqlteavrRKPYSIV 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  279 FLDEIDSIAPhrdkvvgDVEkRIvaqLLALMDG------------LKNrgkVIVIAATNL 326
Cdd:pfam07724  80 LIDEIEKAHP-------GVQ-ND---LLQILEGgtltdkqgrtvdFKN---TLFIMTGNF 125
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
205-321 4.60e-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: 44.42  E-value: 4.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  205 EVFERLGIDAPKGVLLSGPPGCGKT-LIARIIAQETDAQFFTISGPEIVHKFYGE-----SEAHLRKIFEEAGRKGPSII 278
Cdd:pfam13191  14 DALDRVRSGRPPSVLLTGEAGTGKTtLLRELLRALERDGGYFLRGKCDENLPYSPllealTREGLLRQLLDELESSLLEA 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 542097447  279 FLDEIDSIAPHRDKVVGDVEKRIVAQLLALMDGLKNRGKVIVI 321
Cdd:pfam13191  94 WRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL 136
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
491-524 4.90e-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: 45.75  E-value: 4.90e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 542097447  491 LLLAGPPGVGKTLIAKAVANESGVNVISVKGPAL 524
Cdd:TIGR00635  33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
218-321 6.05e-05

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: 42.88  E-value: 6.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 218 VLLSGPPGCGKTLIARIIAQ---ETDAQFFTISGPEIVhkfygeseahLRKIFEEAGRKGPSIIFLDEIDSIAPHRDkvv 294
Cdd:cd01120    1 ILITGPPGSGKTTLLLQFAEqalLSDEPVIFISFLDTI----------LEAIEDLIEEKKLDIIIIDSLSSLARASQ--- 67
                         90       100
                 ....*....|....*....|....*..
gi 542097447 295 GDVEKRIVAQLLALMDGLKNRGKVIVI 321
Cdd:cd01120   68 GDRSSELLEDLAKLLRAARNTGITVIA 94
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
488-566 8.88e-05

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: 43.91  E-value: 8.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 488 PKGLLLAGPPGVGKTLIAKAVANESGVNVISVKGPALMS-RYVG-DSEKGVRELflkarqaAPCIIFLDEVDSvIPARNE 565
Cdd:cd19498   46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATKFTEvGYVGrDVESIIRDL-------VEGIVFIDEIDK-IAKRGG 117

                 .
gi 542097447 566 G 566
Cdd:cd19498  118 S 118
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
491-524 9.04e-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: 45.07  E-value: 9.04e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 542097447 491 LLLAGPPGVGKTLIAKAVANESGVNVISVKGPAL 524
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGPAI 90
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
319-637 1.41e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 45.15  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 319 IVIAATNLPNAIDPALRRPGRFDREISIPIPDREGRREIIEIHSTGMPLNADVDLNVLADITHGFVGADLEALCREAAMS 398
Cdd:COG1401   54 LLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALE 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 399 ALRRLLPEID-FSSAELPYDRLAELTVMMDDFRAALCEVSPSAIRELFVDIPDVRWEDVGGLDDVRRRLIEsvewpIKYP 477
Cdd:COG1401  134 RARLLLELADlEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSEDLESEDDYLKDLLR-----EKFE 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 478 ELYEQ--AGVKPPKGLLLAGPPGVGKTLIAKAVA------NESGVNVISVkGPA------LMSRYVGDSEKGVR---ELF 540
Cdd:COG1401  209 ETLEAflAALKTKKNVILAGPPGTGKTYLARRLAealggeDNGRIEFVQF-HPSwsyedfLLGYRPSLDEGKYEptpGIF 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 541 LKARQAA------PCIIFLDEVdsviparNEGaidsHVaERVLSQFLSEMD---GLEELKG----------------VFV 595
Cdd:COG1401  288 LRFCLKAeknpdkPYVLIIDEI-------NRA----NV-EKYFGELLSLLEsdkRGEELSIelpysgegeefsippnLYI 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 542097447 596 MGATNRAD----LIDPAMLRpgRFdeIIELGLPDEDARRQILAVHL 637
Cdd:COG1401  356 IGTMNTDDrslaLSDKALRR--RF--TFEFLDPDLDKLSNEEVVDL 397
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
490-615 2.13e-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: 41.89  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  490 GLLLAGPPGVGKTLIAKAVANE-SGVNVISVKGPALMS------RYVGDSEKGVR---ELFLKARQAapCIIFLDEVDSv 559
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYVQLTRDTTeedlfgRRNIDPGGASWvdgPLVRAAREG--EIAVLDEINR- 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447  560 iparnegaIDSHVAERVLSQF----LSEMDGLEELK----GVFVMGATNRADL----IDPAMLRpgRF 615
Cdd:pfam07728  78 --------ANPDVLNSLLSLLderrLLLPDGGELVKaapdGFRLIATMNPLDRglneLSPALRS--RF 135
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
214-251 2.33e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 44.19  E-value: 2.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 542097447 214 APKGVLLSGPPGCGKTLIARIIAQE--TDAQFFTISGPEI 251
Cdd:COG1224   63 AGKGILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEI 102
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
214-251 4.91e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 43.07  E-value: 4.91e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 542097447  214 APKGVLLSGPPGCGKTLIARIIAQE--TDAQFFTISGPEI 251
Cdd:pfam06068  49 AGRAVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEV 88
AAA_14 pfam13173
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
218-283 6.24e-04

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


Pssm-ID: 463799 [Multi-domain]  Cd Length: 128  Bit Score: 40.26  E-value: 6.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447  218 VLLSGPPGCGKTLIARIIAQE--TDAQFFTISGPEIvhKFYGESEAHLRKIFEEAGRKGPSIIFLDEI 283
Cdd:pfam13173   5 LVITGPRQVGKTTLLLQLIKEllPPENILYINLDDP--RLLKLADFELLELFLELLYPGKTYLFLDEI 70
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
218-311 6.72e-04

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 42.20  E-value: 6.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 218 VLLSGPPGCGKTLIARIIAQE-------TDAQFFTISGpeivhkFYGES-EAHLRKIFEEAG------RKGpsIIFLDEI 283
Cdd:cd19497   53 ILLIGPTGSGKTLLAQTLAKIldvpfaiADATTLTEAG------YVGEDvENILLKLLQAADydveraQRG--IVYIDEI 124
                         90       100       110
                 ....*....|....*....|....*....|.
gi 542097447 284 DSIAPHRDKVVG--DVEKRIVAQ-LLALMDG 311
Cdd:cd19497  125 DKIARKSENPSItrDVSGEGVQQaLLKILEG 155
Lon COG0466
ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, ...
458-509 6.90e-04

ATP-dependent Lon protease, bacterial type [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440234 [Multi-domain]  Cd Length: 785  Bit Score: 43.08  E-value: 6.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 542097447 458 GLDDVRRRLIE--SVewpikypelyeQAGVKPPKG--LLLAGPPGVGKTLIAKAVA 509
Cdd:COG0466  329 GLEKVKERILEylAV-----------RKLKKKLKGpiLCLVGPPGVGKTSLGKSIA 373
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
458-510 7.61e-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: 41.00  E-value: 7.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542097447 458 GLDDVRRRLIE---------SVEWPIkypelyeqagvkppkgLLLAGPPGVGKTLIAKAVAN 510
Cdd:cd19500   14 GLEDVKERILEylavrklkgSMKGPI----------------LCLVGPPGVGKTSLGKSIAR 59
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
219-349 1.36e-03

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: 40.23  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 219 LLSGPPGCGKTLIARIIAQETDAQFFTISgpeiVHKFYGESE--AHLR--------KIFE---EAGRKGPsIIFLDEIds 285
Cdd:cd19500   41 CLVGPPGVGKTSLGKSIARALGRKFVRIS----LGGVRDEAEirGHRRtyvgampgRIIQalkKAGTNNP-VFLLDEI-- 113
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 542097447 286 iaphrDKVVGDVEKRIVAQLLALMDGLKNR-------------GKVIVIAATNLPNAIDPALRrpgrfDR-EIsIPIP 349
Cdd:cd19500  114 -----DKIGSSFRGDPASALLEVLDPEQNStfsdhyldvpfdlSKVLFIATANSLDTIPGPLL-----DRmEI-IELS 180
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
218-287 1.50e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 41.68  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 218 VLLSGPPGCGKTLIARIIAQE-------TDAQFFTISGpeivhkFYGES-EAHLRKIFEEAG------RKGpsIIFLDEI 283
Cdd:PRK05342 111 ILLIGPTGSGKTLLAQTLARIldvpfaiADATTLTEAG------YVGEDvENILLKLLQAADydvekaQRG--IVYIDEI 182

                 ....
gi 542097447 284 DSIA 287
Cdd:PRK05342 183 DKIA 186
PRK08116 PRK08116
hypothetical protein; Validated
475-554 1.77e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.77  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 475 KYPELYEQAGvKPPKGLLLAGPPGVGKTLIAKAVAN---ESGVNVISVKGPALMSR---YVGDSEKGVRELFLKARQAAP 548
Cdd:PRK08116 102 KYVKKFEEMK-KENVGLLLWGSVGTGKTYLAACIANeliEKGVPVIFVNFPQLLNRiksTYKSSGKEDENEIIRSLVNAD 180

                 ....*.
gi 542097447 549 CIIfLD 554
Cdd:PRK08116 181 LLI-LD 185
FlhF COG1419
Flagellar biosynthesis GTPase FlhF [Cell motility];
386-506 2.05e-03

Flagellar biosynthesis GTPase FlhF [Cell motility];


Pssm-ID: 441029 [Multi-domain]  Cd Length: 361  Bit Score: 41.00  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 386 ADLEALCREaaMSALRRLLPEIDFSSAELPYDRLAELTVMMDDFRAAlcEVSPSAIRELFVDIPDvRWEDVGGLDDVRRR 465
Cdd:COG1419   74 EELEELRRE--LAELKELLEEQLSGLAGESARLPPELAELLERLLEA--GVSPELARELLEKLPE-DLSAEEAWRALLEA 148
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 542097447 466 LIESVewPIKYPELYEQAGVkppkgLLLAGPPGVGKT-LIAK 506
Cdd:COG1419  149 LARRL--PVAEDPLLDEGGV-----IALVGPTGVGKTtTIAK 183
Pgk2 COG2074
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ...
486-519 2.09e-03

2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];


Pssm-ID: 441677  Cd Length: 207  Bit Score: 39.93  E-value: 2.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 542097447 486 KPPKGLLLAGPPGVGKTLIAKAVANESGVN-VISV 519
Cdd:COG2074    4 KRPRIILIGGASGVGKSTIAAELARRLGIPrVIST 38
44 PHA02544
clamp loader, small subunit; Provisional
215-379 3.12e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 40.36  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 215 PKGVLLSGPPGCGKTLIARIIAQETDAQFFTISGpeivhkfygeSEAHLRKIFEEAGR--------KGPSIIFLDEIDsi 286
Cdd:PHA02544  43 PNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNG----------SDCRIDFVRNRLTRfastvsltGGGKVIIIDEFD-- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 287 aphrDKVVGDVEKrivaQLLALMDGL-KNrgkVIVIAATNLPNAIDPALRrpGRFdREISIPIPDREGR----------- 354
Cdd:PHA02544 111 ----RLGLADAQR----HLRSFMEAYsKN---CSFIITANNKNGIIEPLR--SRC-RVIDFGVPTKEEQiemmkqmivrc 176
                        170       180
                 ....*....|....*....|....*
gi 542097447 355 REIIEIHstgmplNADVDLNVLADI 379
Cdd:PHA02544 177 KGILEAE------GVEVDMKVLAAL 195
PRK07773 PRK07773
replicative DNA helicase; Validated
386-510 3.88e-03

replicative DNA helicase; Validated


Pssm-ID: 236093 [Multi-domain]  Cd Length: 886  Bit Score: 40.50  E-value: 3.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 386 ADLEALCREAAMSALRRLLPEIDFSSAELPYDRLAELTVMMDDFRAALCEVSPSAIRELFVDIPDVRWEDVGGLDDVRRR 465
Cdd:PRK07773 114 ANADYYARIVAEKALLRRLIEAGTRIVQYGYAEGADVAEVVDRAQAEIYDVTDRRLSEDFVALEDLLQPTFDEIDAIASS 193
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 542097447 466 LIESVEWPIKYPELYE-QAGVKPPKGLLLAGPPGVGKTLIAKAVAN 510
Cdd:PRK07773 194 GGLARGVPTGFTELDAmTNGLHPGQLIIVAARPSMGKTTFGLDFAR 239
FlhF TIGR03499
flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]
310-506 3.94e-03

flagellar biosynthetic protein FlhF; [Cellular processes, Chemotaxis and motility]


Pssm-ID: 274609 [Multi-domain]  Cd Length: 282  Bit Score: 40.01  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  310 DGLKNRGKVIVIAAtnlpnaIDPALRRPGRFDREISIPIPDREGRReiieIHSTGMPLNADVDLNVLADITHGFVGADLE 389
Cdd:TIGR03499  36 KGLFGKKFVEVTAA------IDEEEAAAASAEEEASKALEQADPKP----LSATAEPLELPAPQEEPAAPAAQAAEPLLP 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447  390 ALCREAAMSALRRLLPEIdFSSAelpydRLAELTVMMDDFRAALCE--VSPSAIRELFVDIPDVrwedvGGLDDVRRRLI 467
Cdd:TIGR03499 106 EEELRKELEALRELLERL-LAGL-----AWLQRPPERAKLYERLLEagVSEELARELLEKLPED-----ADAEDAWRWLR 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 542097447  468 ESVEWPIKYPeLYEQAGVKPPKGLLLAGPPGVGKTL-IAK 506
Cdd:TIGR03499 175 EALEGMLPVK-PEEDPILEQGGVIALVGPTGVGKTTtLAK 213
DnaX COG2812
DNA polymerase III, gamma/tau subunits [Replication, recombination and repair];
219-237 4.17e-03

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


Pssm-ID: 442061 [Multi-domain]  Cd Length: 340  Bit Score: 40.17  E-value: 4.17e-03
                         10
                 ....*....|....*....
gi 542097447 219 LLSGPPGCGKTLIARIIAQ 237
Cdd:COG2812   36 LFTGPRGVGKTTLARILAK 54
PRK05748 PRK05748
replicative DNA helicase; Provisional
393-516 4.20e-03

replicative DNA helicase; Provisional


Pssm-ID: 180232 [Multi-domain]  Cd Length: 448  Bit Score: 40.32  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 393 REAAMsaLRRLLpEIDFSSAELPYDRLAELTVMMDDFRAALCEVSPSAIRELFVDIPDVRWEDVGGLDDVRRRLIESVEW 472
Cdd:PRK05748 110 AEKAM--LRRLI-RTATEIANDAYEPEDDADEILDEAEKKIFEVSERRNKSGFKNIKDVLVKAYDRIEMLHNQTGDITGI 186
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 542097447 473 PIKYPELYEQ-AGVKPPKGLLLAGPPGVGKTL----IAKAVANESGVNV 516
Cdd:PRK05748 187 PTGFTDLDKMtSGLQPNDLIIVAARPSVGKTAfalnIAQNVATKTDKNV 235
MopB_CT cd02775
Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a ...
17-68 4.45e-03

Molybdopterin-Binding, C-terminal (MopB_CT) domain of the MopB superfamily of proteins, a large, diverse, heterogeneous superfamily of enzymes that, in general, bind molybdopterin as a cofactor. The MopB domain is found in a wide variety of molybdenum- and tungsten-containing enzymes, including formate dehydrogenase-H (Fdh-H) and -N (Fdh-N), several forms of nitrate reductase (Nap, Nas, NarG), dimethylsulfoxide reductase (DMSOR), thiosulfate reductase, formylmethanofuran dehydrogenase, and arsenite oxidase. Molybdenum is present in most of these enzymes in the form of molybdopterin, a modified pterin ring with a dithiolene side chain, which is responsible for ligating the Mo. In many bacterial and archaeal species, molybdopterin is in the form of a dinucleotide, with two molybdopterin dinucleotide units per molybdenum. These proteins can function as monomers, heterodimers, or heterotrimers, depending on the protein and organism. Also included in the MopB superfamily is the eukaryotic/eubacterial protein domain family of the 75-kDa subunit/Nad11/NuoG (second domain) of respiratory complex 1/NADH-quinone oxidoreductase which is postulated to have lost an ancestral formate dehydrogenase activity and only vestigial sequence evidence remains of a molybdopterin binding site. This hierarchy is of the conserved MopB_CT domain present in many, but not all, MopB homologs.


Pssm-ID: 239176 [Multi-domain]  Cd Length: 101  Bit Score: 37.30  E-value: 4.45e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 542097447  17 AGRGYARLDPADMARLNLAVGDIVQLTSKKGTGIAKLMPTyPDMRnKGIVQL 68
Cdd:cd02775   20 APEPVVEINPEDAAALGIKDGDLVRVESRRGSVVLRAKVT-DGVP-PGVVFL 69
clpC CHL00095
Clp protease ATP binding subunit
220-360 4.51e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 40.42  E-value: 4.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 220 LSGPPGCGKTLIA-----RIIAQET-----DAQFFT------ISGPeivhKFYGESEAHLRKIFEEAGRKGPSIIFLDEI 283
Cdd:CHL00095 205 LIGEPGVGKTAIAeglaqRIVNRDVpdileDKLVITldigllLAGT----KYRGEFEERLKRIFDEIQENNNIILVIDEV 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 284 DSI--APHRDkvvGDVE-KRIVAQLLAlmdglknRGKVIVIAATNLPN-----AIDPALRRpgRFdREISIPIPDREgrr 355
Cdd:CHL00095 281 HTLigAGAAE---GAIDaANILKPALA-------RGELQCIGATTLDEyrkhiEKDPALER--RF-QPVYVGEPSVE--- 344

                 ....*
gi 542097447 356 EIIEI 360
Cdd:CHL00095 345 ETIEI 349
44 PHA02544
clamp loader, small subunit; Provisional
488-521 5.37e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 39.59  E-value: 5.37e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 542097447 488 PKGLLLAGPPGVGKTLIAKAVANESGVNVISVKG 521
Cdd:PHA02544  43 PNMLLHSPSPGTGKTTVAKALCNEVGAEVLFVNG 76
PRK11361 PRK11361
acetoacetate metabolism transcriptional regulator AtoC;
491-655 6.67e-03

acetoacetate metabolism transcriptional regulator AtoC;


Pssm-ID: 183099 [Multi-domain]  Cd Length: 457  Bit Score: 39.45  E-value: 6.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 491 LLLAGPPGVGKTLIAKAVANES--------GVNVISVKGPALMSRYVGdSEKGV--------RELFLKARQAApciIFLD 554
Cdd:PRK11361 169 VLISGESGTGKELIARAIHYNSrrakgpfiKVNCAALPESLLESELFG-HEKGAftgaqtlrQGLFERANEGT---LLLD 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 555 EVDSVIPARNEGAIdshvaeRVLSQFLSE-MDGLEELK-GVFVMGATNRaDLidPAMLRPGRFDE-------IIELGLPD 625
Cdd:PRK11361 245 EIGEMPLVLQAKLL------RILQEREFErIGGHQTIKvDIRIIAATNR-DL--QAMVKEGTFREdlfyrlnVIHLILPP 315
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 542097447 626 EDARRQ---ILAVHLRNKPLGDN----IHADDLAERC 655
Cdd:PRK11361 316 LRDRREdisLLANHFLQKFSSENqrdiIDIDPMAMSL 352
MopB_CT_NDH-1_NuoG2-N7 cd02788
MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a ...
2-48 6.89e-03

MopB_CT_NDH-1_NuoG2-N7: C-terminal region of the NuoG-like subunit (of the variant with a [4Fe-4S] cluster, N7) of the NADH-quinone oxidoreductase/NADH dehydrogenase-1 (NDH-1) found in various bacteria. The NDH-1 is the first energy-transducting complex in the respiratory chain and functions as a redox pump that uses the redox energy to translocate H+ ions across the membrane, resulting in a significant contribution to energy production. In Escherichia coli NDH-1, the largest subunit is encoded by the nuoG gene, and is part of the 14 distinct subunits constituting the functional enzyme. The NuoG subunit is made of two domains: the first contains three binding sites for FeS clusters (the fer2 domain), the second domain, is of unknown function or, as postulated, has lost an ancestral formate dehydrogenase activity that became redundant during the evolution of the complex I enzyme. Unique to this group, compared to the other prokaryotic and eukaryotic groups in this domain protein family (NADH-Q-OR-NuoG2), is an N-terminal [4Fe-4S] cluster (N7/N1c) present in the second domain and a C-terminal region (this CD) homologous to the formate dehydrogenase C-terminal molybdopterin_binding (MopB) region.


Pssm-ID: 239189 [Multi-domain]  Cd Length: 96  Bit Score: 36.52  E-value: 6.89e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 542097447   2 SEELKLKvAEALPKDAGRGYARLDPADMARLNLAVGDIVQLTSKKGT 48
Cdd:cd02788   12 SEELSQR-SPVIAERAPAPYARLSPADAARLGLADGDLVEFSLGDGT 57
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
491-576 7.52e-03

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 37.87  E-value: 7.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 491 LLLAGPPGVGKTLIAKAVANESGVNVISVkgpalmSRYVGdsEKGVRELFLKARQAApcIIFLDEVDSVIPARNEGA--I 568
Cdd:COG1936    3 IAITGTPGTGKTTVAKLLAERLGLEVIHL------NDLVK--EEGLYTEVDEERDSL--VVDEDALAEELEELKEGDviI 72

                 ....*...
gi 542097447 569 DSHVAERV 576
Cdd:COG1936   73 EGHLAHLV 80
rfc PRK00440
replication factor C small subunit; Reviewed
452-558 7.63e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 39.09  E-value: 7.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542097447 452 RWEDVGGLDDVRRRLIESVEwpikypelyeqAGVKPpkGLLLAGPPGVGKTLIAKAVA------------------NESG 513
Cdd:PRK00440  15 TLDEIVGQEEIVERLKSYVK-----------EKNMP--HLLFAGPPGTGKTTAALALArelygedwrenflelnasDERG 81
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 542097447 514 VNVI--SVKGPAlMSRYVGDsekgvrelflkarqaAPC-IIFLDEVDS 558
Cdd:PRK00440  82 IDVIrnKIKEFA-RTAPVGG---------------APFkIIFLDEADN 113
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
212-283 8.74e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 39.16  E-value: 8.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542097447 212 IDAPKGVLLSGPPGCGKT-LIARIIAQETDAQFFTISGPEIVHKFYGESEAHLRKIFEEAGRKGPsiIFLDEI 283
Cdd:COG1373   17 LDNRKAVVITGPRQVGKTtLLKQLAKELENILYINLDDPRLRALAEEDPDDLLEALKELYPGKTY--LFLDEI 87
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
489-513 9.31e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 39.18  E-value: 9.31e-03
                         10        20
                 ....*....|....*....|....*
gi 542097447 489 KGLLLAGPPGVGKTLIAKAVANESG 513
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELG 89
 
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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