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Conserved domains on  [gi|6322994|ref|NP_013066|]
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putative AAA family ATPase RIX7 [Saccharomyces cerevisiae S288C]

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 ...
192-824 5.02e-180

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: 535.64  E-value: 5.02e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    192 KIKEDRSPPNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISIS 271
Cdd:TIGR01243 165 REEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISIN 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    272 APSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRDGgAQREMERRIVAQLLTSMDELtmeKTNGKpVIIIG 351
Cdd:TIGR01243 245 GPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREE-VTGEVEKRVVAQLLTLMDGL---KGRGR-VIVIG 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    352 ATNRPDSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKR 431
Cdd:TIGR01243 320 ATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    432 IFQtyanikstpttatdSSEDNMEIDEtangdesslkntanmidpLPLSVVQQfirnypeplsgeqlslLSIKYEDFLKA 511
Cdd:TIGR01243 400 FIR--------------EGKINFEAEE------------------IPAEVLKE----------------LKVTMKDFMEA 431
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    512 LPTIQPTAKREGFATVPDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANES 591
Cdd:TIGR01243 432 LKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATES 511
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    592 RANFISIKGPELLNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSES-SSRVVNTLLTELDGLNDRRGI 670
Cdd:TIGR01243 512 GANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQELSNV 591
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    671 FVIGATNRPDMIDPAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKShgTPLSSDVDFEEIIRneKCNNFSGADLAALVRE 750
Cdd:TIGR01243 592 VVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRS--MPLAEDVDLEELAE--MTEGYTGADIEAVCRE 667
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322994    751 SSVLALKRkffqseEIQSVLDNDLDKEFEDLSvgvsgEEIIVTMSDFRSALRKIKPSVSDKDRLKYDRLNKKMG 824
Cdd:TIGR01243 668 AAMAALRE------SIGSPAKEKLEVGEEEFL-----KDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
192-824 5.02e-180

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: 535.64  E-value: 5.02e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    192 KIKEDRSPPNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISIS 271
Cdd:TIGR01243 165 REEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISIN 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    272 APSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRDGgAQREMERRIVAQLLTSMDELtmeKTNGKpVIIIG 351
Cdd:TIGR01243 245 GPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREE-VTGEVEKRVVAQLLTLMDGL---KGRGR-VIVIG 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    352 ATNRPDSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKR 431
Cdd:TIGR01243 320 ATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    432 IFQtyanikstpttatdSSEDNMEIDEtangdesslkntanmidpLPLSVVQQfirnypeplsgeqlslLSIKYEDFLKA 511
Cdd:TIGR01243 400 FIR--------------EGKINFEAEE------------------IPAEVLKE----------------LKVTMKDFMEA 431
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    512 LPTIQPTAKREGFATVPDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANES 591
Cdd:TIGR01243 432 LKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATES 511
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    592 RANFISIKGPELLNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSES-SSRVVNTLLTELDGLNDRRGI 670
Cdd:TIGR01243 512 GANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQELSNV 591
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    671 FVIGATNRPDMIDPAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKShgTPLSSDVDFEEIIRneKCNNFSGADLAALVRE 750
Cdd:TIGR01243 592 VVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRS--MPLAEDVDLEELAE--MTEGYTGADIEAVCRE 667
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322994    751 SSVLALKRkffqseEIQSVLDNDLDKEFEDLSvgvsgEEIIVTMSDFRSALRKIKPSVSDKDRLKYDRLNKKMG 824
Cdd:TIGR01243 668 AAMAALRE------SIGSPAKEKLEVGEEEFL-----KDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
206-375 1.17e-107

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: 327.44  E-value: 1.17e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  206 SLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEK 285
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  286 KIRDLFDEARSLAPCLVFFDEIDAITPKRDgGAQREMERRIVAQLLTSMDELTMEKTNGKPVIIIGATNRPDSLDAALRR 365
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRE-SAQREMERRIVSQLLTCMDELNNEKTAGGPVLVIGATNRPDSLDPALRR 159
                       170
                ....*....|
gi 6322994  366 AGRFDREICL 375
Cdd:cd19518 160 AGRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
524-813 5.91e-99

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 310.78  E-value: 5.91e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  524 FATVPDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPEL 603
Cdd:COG1222  69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  604 LNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSL-SESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMI 682
Cdd:COG1222 149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGtSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLL 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  683 DPAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKShgTPLSSDVDFEEIIRneKCNNFSGADLAALVRESSVLALKRkffq 762
Cdd:COG1222 229 DPALLRPGRFDRVIEVPLPDEEAREEILKIHLRD--MPLADDVDLDKLAK--LTEGFSGADLKAIVTEAGMFAIRE---- 300
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6322994  763 seeiqsvldndldkefedlsvgvsgEEIIVTMSDFRSALRKIKPSVSDKDR 813
Cdd:COG1222 301 -------------------------GRDTVTMEDLEKAIEKVKKKTETATN 326
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
528-805 7.30e-74

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 246.67  E-value: 7.30e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   528 PDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKY 607
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   608 VGESERSIRQVFTRARASVPCVIFFDELDALVPRRdTSLSESSSRVVN----TLLTELDGLNDRRGIFVIGATNRPDMID 683
Cdd:PRK03992 206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR-TDSGTSGDREVQrtlmQLLAEMDGFDPRGNVKIIAATNRIDILD 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   684 PAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKshGTPLSSDVDFEEIIrnEKCNNFSGADLAALVRESSVLALKRKFFQs 763
Cdd:PRK03992 285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTR--KMNLADDVDLEELA--ELTEGASGADLKAICTEAGMFAIRDDRTE- 359
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 6322994   764 eeiqsvldndldkefedlsvgvsgeeiiVTMSDFRSALRKIK 805
Cdd:PRK03992 360 ----------------------------VTMEDFLKAIEKVM 373
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
570-700 4.25e-54

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 183.18  E-value: 4.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    570 VLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSES 649
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6322994    650 SSRVVNTLLTELDGL-NDRRGIFVIGATNRPDMIDPAMLrpGRLDKSLFIEL 700
Cdd:pfam00004  81 SRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
cell_div_CdvC NF041006
cell division protein CdvC;
528-815 2.01e-45

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 167.60  E-value: 2.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   528 PDVTWANVGALQRVRLELNMAIVQPIKRPELYEkvgISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKY 607
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   608 VGESERSIRQVFTRAR-----ASVPCVIFFDELDALVprrDTSLSE--SSSRVVNTLLTELDGLNDRRG---IFVIGATN 677
Cdd:NF041006 175 LGEAEKNVAKIFKKARekskeEGKPAIIFIDEIDALL---GVYSSEvgGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATN 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   678 RPDMIDPAMLRpgRLDKSLFIELPNTEEKLDIIKTLTKshGTPLSSDVDFEEIirNEKCNNFSGADLAALVRESSVLALK 757
Cdd:NF041006 252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS--KIKLENDVDLDEL--AEMTEGYTASDIRDIVQAAHMRVVK 325
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322994   758 RKFFQSEeiqsvldndldkefedlsvgvsGEEIIVTMSDFRSALRKIKPSVsDKDRLK 815
Cdd:NF041006 326 EMFEKGL----------------------GEPRPITMEDFKEVLKIRKPSV-NQEMLK 360
cell_div_CdvC NF041006
cell division protein CdvC;
139-434 3.04e-42

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 158.36  E-value: 3.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   139 ERDTNEMNKRITsTWSKSGSVSESITETDDPKTEEVkkskkrskegtckVKRQKikedrspPNSSLKSLGGMDDVVAQLM 218
Cdd:NF041006  58 EQMINEYKKRIE-VLEELVPAEPAGPDVEKESDEEL-------------VVKEK-------PKVTFSDIVGLEDVKEALK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   219 ELIGLPILHPEIFlstgveP---PRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFDEAR 295
Cdd:NF041006 117 EAIVYPSKRPDLF------PlgwPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAR 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   296 SLA-----PCLVFFDEIDAIT---PKRDGGaqremERRIVAQLLTSMDELtMEKTNGKPVIIIGATNRPDSLDAALRRag 367
Cdd:NF041006 191 EKSkeegkPAIIFIDEIDALLgvySSEVGG-----EVRVRNQFLKEMDGL-QDKSENYHVYVIGATNKPWRLDEPFLR-- 262
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322994   368 RFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKRIFQ 434
Cdd:NF041006 263 RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFE 329
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
567-702 1.11e-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: 80.50  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994     567 PGGVLLWGPPGCGKTLLAKAVANESRAN---FISIKGPELL--------------NKYVGESERSIRQVFTRARASVPCV 629
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILeevldqllliivggKKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322994     630 IFFDELDALVPRRDTSLsesssRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPgRLDKSLFIELPN 702
Cdd:smart00382  82 LILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
192-824 5.02e-180

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: 535.64  E-value: 5.02e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    192 KIKEDRSPPNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISIS 271
Cdd:TIGR01243 165 REEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISIN 244
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    272 APSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRDGgAQREMERRIVAQLLTSMDELtmeKTNGKpVIIIG 351
Cdd:TIGR01243 245 GPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREE-VTGEVEKRVVAQLLTLMDGL---KGRGR-VIVIG 319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    352 ATNRPDSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKR 431
Cdd:TIGR01243 320 ATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    432 IFQtyanikstpttatdSSEDNMEIDEtangdesslkntanmidpLPLSVVQQfirnypeplsgeqlslLSIKYEDFLKA 511
Cdd:TIGR01243 400 FIR--------------EGKINFEAEE------------------IPAEVLKE----------------LKVTMKDFMEA 431
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    512 LPTIQPTAKREGFATVPDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANES 591
Cdd:TIGR01243 432 LKMVEPSAIREVLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATES 511
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    592 RANFISIKGPELLNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSES-SSRVVNTLLTELDGLNDRRGI 670
Cdd:TIGR01243 512 GANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSvTDRIVNQLLTEMDGIQELSNV 591
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    671 FVIGATNRPDMIDPAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKShgTPLSSDVDFEEIIRneKCNNFSGADLAALVRE 750
Cdd:TIGR01243 592 VVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRS--MPLAEDVDLEELAE--MTEGYTGADIEAVCRE 667
                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322994    751 SSVLALKRkffqseEIQSVLDNDLDKEFEDLSvgvsgEEIIVTMSDFRSALRKIKPSVSDKDRLKYDRLNKKMG 824
Cdd:TIGR01243 668 AAMAALRE------SIGSPAKEKLEVGEEEFL-----KDLKVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
206-375 1.17e-107

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: 327.44  E-value: 1.17e-107
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  206 SLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEK 285
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  286 KIRDLFDEARSLAPCLVFFDEIDAITPKRDgGAQREMERRIVAQLLTSMDELTMEKTNGKPVIIIGATNRPDSLDAALRR 365
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRE-SAQREMERRIVSQLLTCMDELNNEKTAGGPVLVIGATNRPDSLDPALRR 159
                       170
                ....*....|
gi 6322994  366 AGRFDREICL 375
Cdd:cd19518 160 AGRFDREICL 169
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
524-813 5.91e-99

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 310.78  E-value: 5.91e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  524 FATVPDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPEL 603
Cdd:COG1222  69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  604 LNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSL-SESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMI 682
Cdd:COG1222 149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGtSGEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLL 228
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  683 DPAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKShgTPLSSDVDFEEIIRneKCNNFSGADLAALVRESSVLALKRkffq 762
Cdd:COG1222 229 DPALLRPGRFDRVIEVPLPDEEAREEILKIHLRD--MPLADDVDLDKLAK--LTEGFSGADLKAIVTEAGMFAIRE---- 300
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6322994  763 seeiqsvldndldkefedlsvgvsgEEIIVTMSDFRSALRKIKPSVSDKDR 813
Cdd:COG1222 301 -------------------------GRDTVTMEDLEKAIEKVKKKTETATN 326
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
538-698 1.15e-95

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: 295.94  E-value: 1.15e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  538 LQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQ 617
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  618 VFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLF 697
Cdd:cd19530  81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160

                .
gi 6322994  698 I 698
Cdd:cd19530 161 V 161
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
196-431 7.51e-93

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 294.61  E-value: 7.51e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  196 DRSPPNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSV 275
Cdd:COG1222  69 PAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSEL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  276 VSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRDGGAQREMERRIVAQLLTSMDELtmekTNGKPVIIIGATNR 355
Cdd:COG1222 149 VSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTSGEVQRTVNQLLAELDGF----ESRGDVLIIAATNR 224
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322994  356 PDSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKR 431
Cdd:COG1222 225 PDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIRE 300
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
541-698 2.27e-83

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: 263.38  E-value: 2.27e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  541 VRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFT 620
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322994  621 RARASVPCVIFFDELDALVPRRDTSLSESSS-RVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLFI 698
Cdd:cd19511  81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTdRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
206-375 7.03e-82

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: 259.53  E-value: 7.03e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  206 SLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEK 285
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  286 KIRDLFDEARSLAPCLVFFDEIDAITPKRDGGaQREMERRIVAQLLTSMDELtmekTNGKPVIIIGATNRPDSLDAALRR 365
Cdd:cd19503  81 NLREIFEEARSHAPSIIFIDEIDALAPKREED-QREVERRVVAQLLTLMDGM----SSRGKVVVIAATNRPDAIDPALRR 155
                       170
                ....*....|
gi 6322994  366 AGRFDREICL 375
Cdd:cd19503 156 PGRFDREVEI 165
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
527-756 1.35e-77

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: 256.76  E-value: 1.35e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  527 VPDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNK 606
Cdd:COG0464 151 LREAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSK 230
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  607 YVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLNDRrgIFVIGATNRPDMIDPAM 686
Cdd:COG0464 231 YVGETEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEELRSD--VVVIAATNRPDLLDPAL 308
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  687 LRpgRLDKSLFIELPNTEEKLDIIKTLTKshGTPLSSDVDFEEIIrnEKCNNFSGADLAALVRESSVLAL 756
Cdd:COG0464 309 LR--RFDEIIFFPLPDAEERLEIFRIHLR--KRPLDEDVDLEELA--EATEGLSGADIRNVVRRAALQAL 372
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
528-805 7.30e-74

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 246.67  E-value: 7.30e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   528 PDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKY 607
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   608 VGESERSIRQVFTRARASVPCVIFFDELDALVPRRdTSLSESSSRVVN----TLLTELDGLNDRRGIFVIGATNRPDMID 683
Cdd:PRK03992 206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKR-TDSGTSGDREVQrtlmQLLAEMDGFDPRGNVKIIAATNRIDILD 284
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   684 PAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKshGTPLSSDVDFEEIIrnEKCNNFSGADLAALVRESSVLALKRKFFQs 763
Cdd:PRK03992 285 PAILRPGRFDRIIEVPLPDEEGRLEILKIHTR--KMNLADDVDLEELA--ELTEGASGADLKAICTEAGMFAIRDDRTE- 359
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 6322994   764 eeiqsvldndldkefedlsvgvsgeeiiVTMSDFRSALRKIK 805
Cdd:PRK03992 360 ----------------------------VTMEDFLKAIEKVM 373
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
204-424 2.24e-72

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: 242.89  E-value: 2.24e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  204 LKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGES 283
Cdd:COG0464 156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGET 235
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  284 EKKIRDLFDEARSLAPCLVFFDEIDAITPKRDGGAQReMERRIVAQLLTSMDELTmektngKPVIIIGATNRPDSLDAAL 363
Cdd:COG0464 236 EKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDG-VGRRVVNTLLTEMEELR------SDVVVIAATNRPDLLDPAL 308
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322994  364 RRagRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAA 424
Cdd:COG0464 309 LR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRA 367
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
541-698 1.17e-71

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: 232.00  E-value: 1.17e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  541 VRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFT 620
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322994  621 RARASVPCVIFFDELDALVPRRDTSL-SESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLFI 698
Cdd:cd19529  81 KARQVAPCVIFFDEIDSIAPRRGTTGdSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
541-698 5.21e-70

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: 227.78  E-value: 5.21e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  541 VRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFT 620
Cdd:cd19528   1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  621 RARASVPCVIFFDELDALVPRRDTSLSES---SSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLF 697
Cdd:cd19528  81 KARAAAPCVLFFDELDSIAKARGGNIGDAggaADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160

                .
gi 6322994  698 I 698
Cdd:cd19528 161 I 161
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
535-698 1.98e-66

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: 218.31  E-value: 1.98e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  535 VGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERS 614
Cdd:cd19503   2 IGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEKN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  615 IRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDK 694
Cdd:cd19503  82 LREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFDR 161

                ....
gi 6322994  695 SLFI 698
Cdd:cd19503 162 EVEI 165
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
200-431 8.35e-66

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 224.71  E-value: 8.35e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   200 PNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGM 279
Cdd:PRK03992 126 PNVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVQKF 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   280 SGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKR--DG-GAQREMERRIVaQLLTSMDELtmeKTNGKpVIIIGATNRP 356
Cdd:PRK03992 206 IGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRtdSGtSGDREVQRTLM-QLLAEMDGF---DPRGN-VKIIAATNRI 280
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994   357 DSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKR 431
Cdd:PRK03992 281 DILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
549-697 4.68e-64

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: 211.52  E-value: 4.68e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  549 IVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFTRARASVPC 628
Cdd:cd19526   9 IEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFSRAQSAKPC 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322994  629 VIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLF 697
Cdd:cd19526  89 ILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
527-724 5.03e-63

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: 220.74  E-value: 5.03e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    527 VPDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANE----------SRANFI 596
Cdd:TIGR03689 176 VPDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSlaarigaeggGKSYFL 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    597 SIKGPELLNKYVGESERSIRQVFTRAR--AS--VPCVIFFDELDALVPRRDTSLS-ESSSRVVNTLLTELDGLNDRRGIF 671
Cdd:TIGR03689 256 NIKGPELLNKYVGETERQIRLIFQRARekASegRPVIVFFDEMDSLFRTRGSGVSsDVETTVVPQLLAEIDGVESLDNVI 335
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6322994    672 VIGATNRPDMIDPAMLRPGRLDKSLFIELPNTEEKLDII-KTLTKShgTPLSSD 724
Cdd:TIGR03689 336 VIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFaKYLTDD--LPLPED 387
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
207-373 1.81e-62

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 207.67  E-value: 1.81e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  207 LGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKK 286
Cdd:cd19519   2 IGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  287 IRDLFDEARSLAPCLVFFDEIDAITPKRDgGAQREMERRIVAQLLTSMDELtmeKTNGKpVIIIGATNRPDSLDAALRRA 366
Cdd:cd19519  82 LRKAFEEAEKNAPAIIFIDEIDAIAPKRE-KTHGEVERRIVSQLLTLMDGL---KQRAH-VIVMAATNRPNSIDPALRRF 156

                ....*..
gi 6322994  367 GRFDREI 373
Cdd:cd19519 157 GRFDREI 163
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
216-373 3.61e-60

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: 200.97  E-value: 3.61e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  216 QLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFDEAR 295
Cdd:cd19511   4 ELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQKAR 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322994  296 SLAPCLVFFDEIDAITPKRDGGAQREMERRIVAQLLTSMDelTMEKTNGkpVIIIGATNRPDSLDAALRRAGRFDREI 373
Cdd:cd19511  84 QAAPCIIFFDEIDSLAPRRGQSDSSGVTDRVVSQLLTELD--GIESLKG--VVVIAATNRPDMIDPALLRPGRLDKLI 157
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
200-431 4.06e-60

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: 208.50  E-value: 4.06e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    200 PNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGM 279
Cdd:TIGR01242 117 PNVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVRKY 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    280 SGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKR---DGGAQREMERRIVaQLLTSMDELTMEKTngkpVIIIGATNRP 356
Cdd:TIGR01242 197 IGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRtdsGTSGDREVQRTLM-QLLAELDGFDPRGN----VKVIAATNRP 271
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994    357 DSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKR 431
Cdd:TIGR01242 272 DILDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAIRE 346
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
169-440 4.28e-59

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: 214.77  E-value: 4.28e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    169 PKT--EEVKKSKKRSKEGTCKVKRQKIKEDR-SPPNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLH 245
Cdd:TIGR01243 414 PAEvlKELKVTMKDFMEALKMVEPSAIREVLvEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLF 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    246 GPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRDGGAQREMERR 325
Cdd:TIGR01243 494 GPPGTGKTLLAKAVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTDR 573
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    326 IVAQLLTSMDelTMEKTNGkpVIIIGATNRPDSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKL 405
Cdd:TIGR01243 574 IVNQLLTEMD--GIQELSN--VVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEEL 649
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 6322994    406 AKLTPGFVGADLKALVTAAGTCAIKRIFQTYANIK 440
Cdd:TIGR01243 650 AEMTEGYTGADIEAVCREAAMAALRESIGSPAKEK 684
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
531-694 6.76e-58

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: 195.25  E-value: 6.76e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  531 TWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGE 610
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  611 SERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNT---LLTELDGLNDRRGIFVIGATNRPDMIDPAML 687
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRTmleLLNQLDGFDPRGNIKVIMATNRPDILDPALL 160

                ....*..
gi 6322994  688 RPGRLDK 694
Cdd:cd19502 161 RPGRFDR 167
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
528-758 9.07e-57

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 200.37  E-value: 9.07e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   528 PDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKY 607
Cdd:PTZ00454 140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   608 VGESERSIRQVFTRARASVPCVIFFDELDALVPRR---DTSLSESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDP 684
Cdd:PTZ00454 220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaQTGADREVQRILLELLNQMDGFDQTTNVKVIMATNRADTLDP 299
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994   685 AMLRPGRLDKSLFIELPNTEEKLDIIKTLTKSHGtpLSSDVDFEEII-RNEKcnnFSGADLAALVRESSVLALKR 758
Cdd:PTZ00454 300 ALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMN--LSEEVDLEDFVsRPEK---ISAADIAAICQEAGMQAVRK 369
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
541-698 1.40e-56

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: 191.19  E-value: 1.40e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  541 VRLELNMAIVQPIKRPELYEKvGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFT 620
Cdd:cd19527   1 VKKEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  621 RARASVPCVIFFDELDALVPRRDTSLSESS--SRVVNTLLTELDGLND-RRGIFVIGATNRPDMIDPAMLRPGRLDKSLF 697
Cdd:cd19527  80 KARDAKPCVIFFDELDSLAPSRGNSGDSGGvmDRVVSQLLAELDGMSSsGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159

                .
gi 6322994  698 I 698
Cdd:cd19527 160 L 160
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
534-698 4.31e-56

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: 190.34  E-value: 4.31e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  534 NVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESER 613
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  614 SIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLD 693
Cdd:cd19519  81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160

                ....*
gi 6322994  694 KSLFI 698
Cdd:cd19519 161 REIDI 165
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
213-373 5.43e-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: 189.42  E-value: 5.43e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  213 VVAQLMELIGLPILHPEIFLStGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFD 292
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRY-GLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  293 EARSLAPCLVFFDEIDAITPKRDGGAQREMERRIVAQLLTSMDELTMEktngKPVIIIGATNRPDSLDAALRRAGRFDRE 372
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKRDSSGESGELRRVLNQLLTELDGVNSR----SKVLVIAATNRPDLLDPALLRPGRFDEV 155

                .
gi 6322994  373 I 373
Cdd:cd19481 156 I 156
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
187-424 2.50e-55

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 199.05  E-value: 2.50e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    187 KVKRQKIKEDRspPNSSLKSLGGMDDVVAQLMELIGLpILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVP 266
Cdd:TIGR01241  39 KSKAKLLNEEK--PKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVP 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    267 FISISAPSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRD---GGAQREMERRIvAQLLTSMDelTMEKTN 343
Cdd:TIGR01241 116 FFSISGSDFVEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGNDEREQTL-NQLLVEMD--GFGTNT 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    344 GkpVIIIGATNRPDSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTA 423
Cdd:TIGR01241 193 G--VIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNE 270

                  .
gi 6322994    424 A 424
Cdd:TIGR01241 271 A 271
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
209-421 7.39e-55

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 199.49  E-value: 7.39e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  209 GMDDVVAQLMELIGLpiLH-PEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVS---GMsGESe 284
Cdd:COG0465 146 GVDEAKEELQEIVDF--LKdPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEmfvGV-GAS- 221
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  285 kKIRDLFDEARSLAPCLVFFDEIDAITPKRD---GGAQREMERrIVAQLLTSMDeltmektnG----KPVIIIGATNRPD 357
Cdd:COG0465 222 -RVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglGGGHDEREQ-TLNQLLVEMD--------GfegnEGVIVIAATNRPD 291
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322994  358 SLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALV 421
Cdd:COG0465 292 VLDPALLRPGRFDRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLV 355
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
549-698 8.28e-55

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: 186.33  E-value: 8.28e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  549 IVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFTRARASVPC 628
Cdd:cd19481   8 AVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFERARRLAPC 87
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322994  629 VIFFDELDALVPRRDTSL-SESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLFI 698
Cdd:cd19481  88 ILFIDEIDAIGRKRDSSGeSGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
528-758 2.34e-54

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 196.35  E-value: 2.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    528 PDVTWANVGALQRVRLELnMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKY 607
Cdd:TIGR01241  50 PKVTFKDVAGIDEAKEEL-MEIVDFLKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    608 VGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSS---RVVNTLLTELDGLNDRRGIFVIGATNRPDMIDP 684
Cdd:TIGR01241 129 VGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGNDereQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDP 208
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322994    685 AMLRPGRLDKSLFIELPNTEEKLDIIKtlTKSHGTPLSSDVDFEEIIRneKCNNFSGADLAALVRESSVLALKR 758
Cdd:TIGR01241 209 ALLRPGRFDRQVVVDLPDIKGREEILK--VHAKNKKLAPDVDLKAVAR--RTPGFSGADLANLLNEAALLAARK 278
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
570-700 4.25e-54

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 183.18  E-value: 4.25e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    570 VLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSES 649
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6322994    650 SSRVVNTLLTELDGL-NDRRGIFVIGATNRPDMIDPAMLrpGRLDKSLFIEL 700
Cdd:pfam00004  81 SRRVVNQLLTELDGFtSSNSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
216-373 1.01e-53

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: 183.47  E-value: 1.01e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  216 QLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFDEAR 295
Cdd:cd19529   4 ELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFRKAR 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322994  296 SLAPCLVFFDEIDAITPKRDGGAQREMERRIVAQLLTSMDelTMEKTNGkpVIIIGATNRPDSLDAALRRAGRFDREI 373
Cdd:cd19529  84 QVAPCVIFFDEIDSIAPRRGTTGDSGVTERVVNQLLTELD--GLEEMNG--VVVIAATNRPDIIDPALLRAGRFDRLI 157
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
530-698 1.69e-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: 183.20  E-value: 1.69e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  530 VTWANVGALQRVRLELnMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVG 609
Cdd:cd19501   1 VTFKDVAGCEEAKEEL-KEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  610 ESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSS---RVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAM 686
Cdd:cd19501  80 VGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPAL 159
                       170
                ....*....|..
gi 6322994  687 LRPGRLDKSLFI 698
Cdd:cd19501 160 LRPGRFDRQVYV 171
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
213-373 1.67e-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: 180.01  E-value: 1.67e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  213 VVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFD 292
Cdd:cd19528   1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  293 EARSLAPCLVFFDEIDAITPKRDG--GAQREMERRIVAQLLTSMDELTMEKTngkpVIIIGATNRPDSLDAALRRAGRFD 370
Cdd:cd19528  81 KARAAAPCVLFFDELDSIAKARGGniGDAGGAADRVINQILTEMDGMNTKKN----VFIIGATNRPDIIDPAILRPGRLD 156

                ...
gi 6322994  371 REI 373
Cdd:cd19528 157 QLI 159
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
210-424 3.60e-52

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 182.39  E-value: 3.60e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  210 MDDVVAQ----------LMELIGLPILHpeiflSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGM 279
Cdd:COG1223   1 LDDVVGQeeakkklkliIKELRRRENLR-----KFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  280 SGESEKKIRDLFDEARSlAPCLVFFDEIDAItpkrdgGAQREME------RRIVAQLLTSMDELTMEktngkpVIIIGAT 353
Cdd:COG1223  76 LGETARNLRKLFDFARR-APCVIFFDEFDAI------AKDRGDQndvgevKRVVNALLQELDGLPSG------SVVIAAT 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322994  354 NRPDSLDAALRRagRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAA 424
Cdd:COG1223 143 NHPELLDSALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTA 211
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
554-776 4.75e-52

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 182.01  E-value: 4.75e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  554 KRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFTRARaSVPCVIFFD 633
Cdd:COG1223  22 RRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFAR-RAPCVIFFD 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  634 ELDALVPRR-DTSLSESSSRVVNTLLTELDGLNDrrGIFVIGATNRPDMIDPAMLRpgRLDKSLFIELPNTEEKLDIIKT 712
Cdd:COG1223 101 EFDAIAKDRgDQNDVGEVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERKEILEL 176
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322994  713 LTKshGTPLSSDVDFEEIIrnEKCNNFSGADLAALVREssvlALKRKFFQSEEiqSVLDNDLDK 776
Cdd:COG1223 177 NLK--KFPLPFELDLKKLA--KKLEGLSGADIEKVLKT----ALKKAILEDRE--KVTKEDLEE 230
ftsH CHL00176
cell division protein; Validated
203-424 1.60e-51

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 191.42  E-value: 1.60e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   203 SLKSLGGMDDVVAQLMELIGLpILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGE 282
Cdd:CHL00176 181 TFRDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   283 SEKKIRDLFDEARSLAPCLVFFDEIDAITPKRD---GGAQREMErRIVAQLLTSMDelTMEKTNGkpVIIIGATNRPDSL 359
Cdd:CHL00176 260 GAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGagiGGGNDERE-QTLNQLLTEMD--GFKGNKG--VIVIAATNRVDIL 334
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994   360 DAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAA 424
Cdd:CHL00176 335 DAALLRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEA 399
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
534-694 3.07e-51

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 176.83  E-value: 3.07e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  534 NVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESER 613
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  614 SIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLN----DRRGIFVIGATNRPDMIDPAMLRP 689
Cdd:cd19518  81 KIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNnektAGGPVLVIGATNRPDSLDPALRRA 160

                ....*
gi 6322994  690 GRLDK 694
Cdd:cd19518 161 GRFDR 165
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
242-373 1.82e-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: 173.16  E-value: 1.82e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    242 VLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRDGGaQRE 321
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSG-GDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6322994    322 MERRIVAQLLTSMDELTmekTNGKPVIIIGATNRPDSLDAALRraGRFDREI 373
Cdd:pfam00004  80 ESRRVVNQLLTELDGFT---SSNSKVIVIAATNRPDKLDPALL--GRFDRII 126
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
528-759 2.11e-50

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 183.43  E-value: 2.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   528 PDVTWANVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKY 607
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   608 VGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNT---LLTELDGLNDRRGIFVIGATNRPDMIDP 684
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRTmleLLNQLDGFDSRGDVKVIMATNRIESLDP 337
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994   685 AMLRPGRLDKSLFIELPNTEEKLDIIKTLTKShgTPLSSDVDFEEIIRNEkcNNFSGADLAALVRESSVLALKRK 759
Cdd:PTZ00361 338 ALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSK--MTLAEDVDLEEFIMAK--DELSGADIKAICTEAGLLALRER 408
ftsH CHL00176
cell division protein; Validated
524-793 4.62e-50

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 187.18  E-value: 4.62e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   524 FATVPD--VTWANVGALQRVRLELNmAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGP 601
Cdd:CHL00176 172 FQMEADtgITFRDIAGIEEAKEEFE-EVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGS 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   602 ELLNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSL---SESSSRVVNTLLTELDGLNDRRGIFVIGATNR 678
Cdd:CHL00176 251 EFVEMFVGVGAARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGIgggNDEREQTLNQLLTEMDGFKGNKGVIVIAATNR 330
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   679 PDMIDPAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKShgTPLSSDVDFEEIIRneKCNNFSGADLAALVRESSVLALKR 758
Cdd:CHL00176 331 VDILDAALLRPGRFDRQITVSLPDREGRLDILKVHARN--KKLSPDVSLELIAR--RTPGFSGADLANLLNEAAILTARR 406
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 6322994   759 KffqseeIQSVLDNDLDKEFEDLSVGVSGEEIIVT 793
Cdd:CHL00176 407 K------KATITMKEIDTAIDRVIAGLEGTPLEDS 435
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
535-698 5.41e-49

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: 170.23  E-value: 5.41e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  535 VGALQRVRLELNMAIVQPIKRPELYeKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERS 614
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  615 IRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLNDR--RGIFVIGATNRPDMIDPAMLRpgRL 692
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpeDRVLVLGATNRPWELDEAFLR--RF 157

                ....*.
gi 6322994  693 DKSLFI 698
Cdd:cd19509 158 EKRIYI 163
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
203-373 6.03e-49

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: 170.49  E-value: 6.03e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  203 SLKSLGGMDDVVAQLMELIGLpILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGE 282
Cdd:cd19501   2 TFKDVAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  283 SEKKIRDLFDEARSLAPCLVFFDEIDAITPKRD---GGAQREMERRIvAQLLTSMDELTmekTNgKPVIIIGATNRPDSL 359
Cdd:cd19501  81 GASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGaglGGGHDEREQTL-NQLLVEMDGFE---SN-TGVIVIAATNRPDVL 155
                       170
                ....*....|....
gi 6322994  360 DAALRRAGRFDREI 373
Cdd:cd19501 156 DPALLRPGRFDRQV 169
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
203-373 7.25e-49

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 170.21  E-value: 7.25e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  203 SLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGE 282
Cdd:cd19502   1 TYEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  283 SEKKIRDLFDEARSLAPCLVFFDEIDAITPKR---DGGAQREMERRIVaQLLTSMDELTMEKTngkpVIIIGATNRPDSL 359
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRfdsGTGGDREVQRTML-ELLNQLDGFDPRGN----IKVIMATNRPDIL 155
                       170
                ....*....|....
gi 6322994  360 DAALRRAGRFDREI 373
Cdd:cd19502 156 DPALLRPGRFDRKI 169
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
531-832 1.42e-47

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 179.85  E-value: 1.42e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   531 TWANVGALQRVRLELNmAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGE 610
Cdd:PRK10733 150 TFADVAGCDEAKEEVA-ELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGV 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   611 SERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLS---ESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAML 687
Cdd:PRK10733 229 GASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGAGLGgghDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALL 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   688 RPGRLDKSLFIELPNTEEKLDIIKTLTKShgTPLSSDVDFEEIIRNEKcnNFSGADLAALVRESSVLALKrkffqseeiq 767
Cdd:PRK10733 309 RPGRFDRQVVVGLPDVRGREQILKVHMRR--VPLAPDIDAAIIARGTP--GFSGADLANLVNEAALFAAR---------- 374
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994   768 svldndldkefedlsvgvsGEEIIVTMSDFRSAlrkikpsvsdKDRLKYDRLNKKMGLTEEMKDA 832
Cdd:PRK10733 375 -------------------GNKRVVSMVEFEKA----------KDKIMMGAERRSMVMTEAQKES 410
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
206-372 1.72e-47

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: 166.53  E-value: 1.72e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  206 SLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALA-----GELQVPFISISAPSVVSGMS 280
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAaecskGGQKVSFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  281 GESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRDgGAQREMERRIVAQLLTSMDELtmekTNGKPVIIIGATNRPDSLD 360
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRS-SKQEQIHASIVSTLLALMDGL----DNRGQVVVIGATNRPDALD 155
                       170
                ....*....|..
gi 6322994  361 AALRRAGRFDRE 372
Cdd:cd19517 156 PALRRPGRFDRE 167
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
210-371 1.26e-46

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 163.81  E-value: 1.26e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  210 MDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRD 289
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  290 LFDEARSLAPCLVFFDEIDAITPKRDGGAQREMErRIVAQLLTSMDELTmEKTNgkpVIIIGATNRPDSLDAALRRAGRF 369
Cdd:cd19530  81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASE-RVVNQLLTEMDGLE-ERSN---VFVIAATNRPDIIDPAMLRPGRL 155

                ..
gi 6322994  370 DR 371
Cdd:cd19530 156 DK 157
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
207-373 7.14e-46

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: 161.75  E-value: 7.14e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  207 LGGMDDVVAQLMELIGLPILHPEIFlSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKK 286
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  287 IRDLFDEARSLAPCLVFFDEIDAITPKRDGGaQREMERRIVAQLLTSMDelTMEKTNGKPVIIIGATNRPDSLDAALRRa 366
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSG-EHEASRRVKTEFLVQMD--GVLNKPEDRVLVLGATNRPWELDEAFLR- 155

                ....*..
gi 6322994  367 gRFDREI 373
Cdd:cd19509 156 -RFEKRI 161
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
534-697 1.84e-45

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 160.75  E-value: 1.84e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  534 NVGALQRVRLELNMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANE-SRAN----FISIKGPELLNKYV 608
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAEcSKGGqkvsFFMRKGADCLSKWV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  609 GESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLR 688
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRR 160

                ....*....
gi 6322994  689 PGRLDKSLF 697
Cdd:cd19517 161 PGRFDREFY 169
cell_div_CdvC NF041006
cell division protein CdvC;
528-815 2.01e-45

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 167.60  E-value: 2.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   528 PDVTWANVGALQRVRLELNMAIVQPIKRPELYEkvgISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKY 607
Cdd:NF041006  98 PKVTFSDIVGLEDVKEALKEAIVYPSKRPDLFP---LGWPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKW 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   608 VGESERSIRQVFTRAR-----ASVPCVIFFDELDALVprrDTSLSE--SSSRVVNTLLTELDGLNDRRG---IFVIGATN 677
Cdd:NF041006 175 LGEAEKNVAKIFKKARekskeEGKPAIIFIDEIDALL---GVYSSEvgGEVRVRNQFLKEMDGLQDKSEnyhVYVIGATN 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   678 RPDMIDPAMLRpgRLDKSLFIELPNTEEKLDIIKTLTKshGTPLSSDVDFEEIirNEKCNNFSGADLAALVRESSVLALK 757
Cdd:NF041006 252 KPWRLDEPFLR--RFQKRIYIPLPDREQRLELLKYYTS--KIKLENDVDLDEL--AEMTEGYTASDIRDIVQAAHMRVVK 325
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6322994   758 RKFFQSEeiqsvldndldkefedlsvgvsGEEIIVTMSDFRSALRKIKPSVsDKDRLK 815
Cdd:NF041006 326 EMFEKGL----------------------GEPRPITMEDFKEVLKIRKPSV-NQEMLK 360
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
528-758 7.26e-45

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 170.99  E-value: 7.26e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  528 PDVTWANVGALQRVRLELnMAIVQPIKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKY 607
Cdd:COG0465 137 PKVTFDDVAGVDEAKEEL-QEIVDFLKDPEKFTRLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMF 215
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  608 VG--ESeRsIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSS---RVVNTLLTELDGLNDRRGIFVIGATNRPDMI 682
Cdd:COG0465 216 VGvgAS-R-VRDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDereQTLNQLLVEMDGFEGNEGVIVIAATNRPDVL 293
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322994  683 DPAMLRPGRLDKSLFIELPNTEEKLDIIKTLTKshGTPLSSDVDFEEIIRneKCNNFSGADLAALVRESSVLALKR 758
Cdd:COG0465 294 DPALLRPGRFDRQVVVDLPDVKGREAILKVHAR--KKPLAPDVDLEVIAR--RTPGFSGADLANLVNEAALLAARR 365
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
187-430 8.63e-45

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 171.76  E-value: 8.63e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   187 KVKRQKIKEDRSppNSSLKSLGGMDDVVAQLMELIGLpILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVP 266
Cdd:PRK10733 136 KSKARMLTEDQI--KTTFADVAGCDEAKEEVAELVEY-LREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVP 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   267 FISISAPSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRD---GGAQREMERRIvAQLLTSMDelTMEKTN 343
Cdd:PRK10733 213 FFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGaglGGGHDEREQTL-NQMLVEMD--GFEGNE 289
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   344 GkpVIIIGATNRPDSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTA 423
Cdd:PRK10733 290 G--IIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNE 367

                 ....*..
gi 6322994   424 AGTCAIK 430
Cdd:PRK10733 368 AALFAAR 374
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
213-373 2.53e-44

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: 157.21  E-value: 2.53e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  213 VVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFD 292
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  293 EARSLAPCLVFFDEIDAITPKRdGGAQREMERRIVAQLLTSMDelTMEKTNGkpVIIIGATNRPDSLDAALRRAGRFDRE 372
Cdd:cd19526  81 RAQSAKPCILFFDEFDSIAPKR-GHDSTGVTDRVVNQLLTQLD--GVEGLDG--VYVLAATSRPDLIDPALLRPGRLDKL 155

                .
gi 6322994  373 I 373
Cdd:cd19526 156 V 156
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
213-371 1.29e-42

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 152.28  E-value: 1.29e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  213 VVAQLMELIGLPILHPEIFlSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFD 292
Cdd:cd19527   1 VKKEILDTIQLPLEHPELF-SSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  293 EARSLAPCLVFFDEIDAITPKR-DGGAQREMERRIVAQLLTSMDELTmekTNGKPVIIIGATNRPDSLDAALRRAGRFDR 371
Cdd:cd19527  80 KARDAKPCVIFFDELDSLAPSRgNSGDSGGVMDRVVSQLLAELDGMS---SSGQDVFVIGATNRPDLLDPALLRPGRFDK 156
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
200-431 3.03e-42

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 159.16  E-value: 3.03e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   200 PNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGM 279
Cdd:PTZ00454 140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   280 SGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKR---DGGAQREMErRIVAQLLTSMDELTmEKTNGKpviIIGATNRP 356
Cdd:PTZ00454 220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRfdaQTGADREVQ-RILLELLNQMDGFD-QTTNVK---VIMATNRA 294
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994   357 DSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKR 431
Cdd:PTZ00454 295 DTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
cell_div_CdvC NF041006
cell division protein CdvC;
139-434 3.04e-42

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 158.36  E-value: 3.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   139 ERDTNEMNKRITsTWSKSGSVSESITETDDPKTEEVkkskkrskegtckVKRQKikedrspPNSSLKSLGGMDDVVAQLM 218
Cdd:NF041006  58 EQMINEYKKRIE-VLEELVPAEPAGPDVEKESDEEL-------------VVKEK-------PKVTFSDIVGLEDVKEALK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   219 ELIGLPILHPEIFlstgveP---PRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFDEAR 295
Cdd:NF041006 117 EAIVYPSKRPDLF------PlgwPRGILLYGPPGCGKTMLAAAVANEIDSEFIHVDAASIMSKWLGEAEKNVAKIFKKAR 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   296 SLA-----PCLVFFDEIDAIT---PKRDGGaqremERRIVAQLLTSMDELtMEKTNGKPVIIIGATNRPDSLDAALRRag 367
Cdd:NF041006 191 EKSkeegkPAIIFIDEIDALLgvySSEVGG-----EVRVRNQFLKEMDGL-QDKSENYHVYVIGATNKPWRLDEPFLR-- 262
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322994   368 RFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIKRIFQ 434
Cdd:NF041006 263 RFQKRIYIPLPDREQRLELLKYYTSKIKLENDVDLDELAEMTEGYTASDIRDIVQAAHMRVVKEMFE 329
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
528-698 6.27e-41

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: 148.60  E-value: 6.27e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  528 PDVTWANVGALQRVRLELNMAIVQPIKRPELYekVGISAP-GGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNK 606
Cdd:cd19525  17 PPINWADIAGLEFAKKTIKEIVVWPMLRPDIF--TGLRGPpKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSK 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  607 YVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLN---DRRgIFVIGATNRPDMID 683
Cdd:cd19525  95 WVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATtssEDR-ILVVGATNRPQEID 173
                       170
                ....*....|....*
gi 6322994  684 PAMLRpgRLDKSLFI 698
Cdd:cd19525 174 EAARR--RLVKRLYI 186
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
200-421 2.23e-40

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: 156.41  E-value: 2.23e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    200 PNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGEL----------QVPFIS 269
Cdd:TIGR03689 177 PDVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLaarigaegggKSYFLN 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    270 ISAPSVVSGMSGESEKKIRDLFDEARSLA----PCLVFFDEIDAITPKRDGGAQREMERRIVAQLLTSMDELTmEKTNgk 345
Cdd:TIGR03689 257 IKGPELLNKYVGETERQIRLIFQRAREKAsegrPVIVFFDEMDSLFRTRGSGVSSDVETTVVPQLLAEIDGVE-SLDN-- 333
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322994    346 pVIIIGATNRPDSLDAALRRAGRFDREICLNVPNEVSRLHILKK-MSDNLKIDGaiDFAKLAkltpGFVGADLKALV 421
Cdd:TIGR03689 334 -VIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFAKyLTDDLPLPE--DLAAHD----GDREATAAALI 403
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
534-698 9.16e-40

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: 144.49  E-value: 9.16e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  534 NVGALQRVRLELNMAIVQPIKRPELYEKVGI-SAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESE 612
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  613 RSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGL--NDRRGIFVIGATNRPDMIDPAMLRpg 690
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAILR-- 158

                ....*...
gi 6322994  691 RLDKSLFI 698
Cdd:cd19520 159 RMPKRFHI 166
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
528-698 1.75e-39

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: 143.85  E-value: 1.75e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  528 PDVTWANVGALQRVRLELNMAIVQPIKRPELYekVGISAP-GGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNK 606
Cdd:cd19521   2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLF--TGNRKPwSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  607 YVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGL-NDRRGIFVIGATNRPDMIDPA 685
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDSA 159
                       170
                ....*....|...
gi 6322994  686 MLRpgRLDKSLFI 698
Cdd:cd19521 160 IRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
206-365 6.44e-38

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 139.10  E-value: 6.44e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  206 SLGGMDDVVAQLMELIGLPILHPEIFLSTGV-EPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESE 284
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  285 KKIRDLFDEARSLAPCLVFFDEIDAITPKRDGGaQREMERRIVAQLLTSMDELTmekTNGKP-VIIIGATNRPDSLDAAL 363
Cdd:cd19520  81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST-DHEATAMMKAEFMSLWDGLS---TDGNCrVIVMGATNRPQDLDEAI 156

                ..
gi 6322994  364 RR 365
Cdd:cd19520 157 LR 158
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
200-430 1.67e-37

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 146.07  E-value: 1.67e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   200 PNSSLKSLGGMDDVVAQLMELIGLPILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGM 279
Cdd:PTZ00361 178 PLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKY 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   280 SGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKR---DGGAQREMERRIVaQLLTSMDELTMEKTngkpVIIIGATNRP 356
Cdd:PTZ00361 258 LGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydaTSGGEKEIQRTML-ELLNQLDGFDSRGD----VKVIMATNRI 332
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322994   357 DSLDAALRRAGRFDREICLNVPNEVSRLHILKKMSDNLKIDGAIDFAKLAKLTPGFVGADLKALVTAAGTCAIK 430
Cdd:PTZ00361 333 ESLDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALR 406
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
556-693 2.73e-36

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


Pssm-ID: 410912 [Multi-domain]  Cd Length: 177  Bit Score: 134.92  E-value: 2.73e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  556 PELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISI-KGPELLNKYVGESERSIRQVFTRARA--------SV 626
Cdd:cd19504  24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEeqrrlganSG 103
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322994  627 PCVIFFDELDALVPRRDTSLSESS--SRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLD 693
Cdd:cd19504 104 LHIIIFDEIDAICKQRGSMAGSTGvhDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
534-698 5.34e-35

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 130.74  E-value: 5.34e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  534 NVGALQRVRLELNMAIVQPIKRPELYekVGISAPG-GVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESE 612
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELF--TGLRAPArGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  613 RSIRQVFTRARASVPCVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDGL--NDRRGIFVIGATNRPDMIDPAMLRpg 690
Cdd:cd19524  79 KLVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVLR-- 156

                ....*...
gi 6322994  691 RLDKSLFI 698
Cdd:cd19524 157 RFTKRVYV 164
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
207-373 6.10e-35

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 130.87  E-value: 6.10e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  207 LGGMDDVVAQLMELIGLPILHPEIFlsTGVEPP-RGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEK 285
Cdd:cd19522   2 IADLEEAKKLLEEAVVLPMWMPEFF--KGIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  286 KIRDLFDEARSLAPCLVFFDEIDAITPKRDGGAQREMERRIVAQLLTSMDELTMEKTNGKP---VIIIGATNRPDSLDAA 362
Cdd:cd19522  80 LVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASRRVKSELLVQMDGVGGASENDDPskmVMVLAATNFPWDIDEA 159
                       170
                ....*....|.
gi 6322994  363 LRRagRFDREI 373
Cdd:cd19522 160 LRR--RLEKRI 168
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
534-698 6.11e-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: 128.18  E-value: 6.11e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  534 NVGALQRVRLELNMAIVQPIKRPELYEkvGISAP-GGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESE 612
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  613 RSIRQVFTRARASVPCVIFFDELDALVPRRDTSLS-ESSSRVVNTLLTELDGL-------NDRRGIFVIGATNRPDMIDP 684
Cdd:cd19522  79 KLVRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEhEASRRVKSELLVQMDGVggasendDPSKMVMVLAATNFPWDIDE 158
                       170
                ....*....|....
gi 6322994  685 AMLRpgRLDKSLFI 698
Cdd:cd19522 159 ALRR--RLEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
207-365 5.92e-33

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 124.96  E-value: 5.92e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  207 LGGMDDVVAQLMELIGLPILHPEIFlsTGVE-PPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEK 285
Cdd:cd19524   2 IAGQDLAKQALQEMVILPSLRPELF--TGLRaPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  286 KIRDLFDEARSLAPCLVFFDEIDAITPKRDGGaQREMERRIVAQLLTSMDELTmekTNGKP-VIIIGATNRPDSLD-AAL 363
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEG-EHEASRRLKTEFLIEFDGVQ---SNGDDrVLVMGATNRPQELDdAVL 155

                ..
gi 6322994  364 RR 365
Cdd:cd19524 156 RR 157
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
207-373 1.01e-32

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: 125.10  E-value: 1.01e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  207 LGGMDDVVAQLMELIGLPILHPEIFlsTGVE-PPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEK 285
Cdd:cd19525  24 IAGLEFAKKTIKEIVVWPMLRPDIF--TGLRgPPKGILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWVGEGEK 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  286 KIRDLFDEARSLAPCLVFFDEIDAITPKRdGGAQREMERRIVAQLLTSMDELTmeKTNGKPVIIIGATNRPDSLDAALRR 365
Cdd:cd19525 102 MVRALFSVARCKQPAVIFIDEIDSLLSQR-GEGEHESSRRIKTEFLVQLDGAT--TSSEDRILVVGATNRPQEIDEAARR 178

                ....*...
gi 6322994  366 agRFDREI 373
Cdd:cd19525 179 --RLVKRL 184
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
200-373 3.39e-32

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: 123.05  E-value: 3.39e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  200 PNSSLKSLGGMDDVVAQLMELIGLPILHPEIFlSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGM 279
Cdd:cd19521   2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLF-TGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  280 SGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKRDGGaQREMERRIVAQLLTSMDELtmeKTNGKPVIIIGATNRPDSL 359
Cdd:cd19521  81 MGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEG-ESEASRRIKTELLVQMNGV---GNDSQGVLVLGATNIPWQL 156
                       170
                ....*....|....
gi 6322994  360 DAALRRagRFDREI 373
Cdd:cd19521 157 DSAIRR--RFEKRI 168
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
557-700 3.46e-27

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 108.00  E-value: 3.46e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  557 ELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANES---RANFISIKGPELLNKYVGESER---SIRQVFTRARASVPCVI 630
Cdd:cd00009   9 ALREALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVL 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  631 FFDELDALVPRrdtslseSSSRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLFIEL 700
Cdd:cd00009  89 FIDEIDSLSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
235-371 5.25e-27

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 107.84  E-value: 5.25e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  235 GVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEIDAITPKR 314
Cdd:cd19507  27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNA 106
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322994  315 DGGAQREMERRIVAQLLTSMDELTmektngKPVIIIGATNRPDSLDAALRRAGRFDR 371
Cdd:cd19507 107 DSKGDSGTSSRVLGTFLTWLQEKK------KPVFVVATANNVQSLPPELLRKGRFDE 157
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
563-698 6.49e-26

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 104.76  E-value: 6.49e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  563 GISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRR 642
Cdd:cd19507  27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIAPCVLWIDEIEKGFSNA 106
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6322994  643 DTSL-SESSSRVVNTLLTELDglNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLFI 698
Cdd:cd19507 107 DSKGdSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRFDEIFFV 161
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
208-376 2.65e-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: 102.61  E-value: 2.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  208 GGMDDVVAQLMELIGLPilhpeiflstgvePPRGVLLHGPPGCGKTSIANALAGEL---QVPFISISAPSVVSGMSGESE 284
Cdd:cd00009   1 VGQEEAIEALREALELP-------------PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAEL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  285 KK---IRDLFDEARSLAPCLVFFDEIDAITpkrdggaqremeRRIVAQLLTSMDELTMEKTNGKPVIIIGATNRPDSLDA 361
Cdd:cd00009  68 FGhflVRLLFELAEKAKPGVLFIDEIDSLS------------RGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDL 135
                       170
                ....*....|....*
gi 6322994  362 ALRRAGRFDREICLN 376
Cdd:cd00009 136 DRALYDRLDIRIVIP 150
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
534-698 1.61e-23

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: 98.03  E-value: 1.61e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  534 NVGALQRVRLELNMAIVQPIKRPELYEKVgISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGESER 613
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGL-LRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  614 SIRQVFTRARASVPCVIFFDELDALVPRRDTSLSeSSSRVVNTLLTELDGL--NDRRGIFVIGATNRPDMIDPAMLRpgR 691
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEAS-PVGRLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR--Y 156

                ....*..
gi 6322994  692 LDKSLFI 698
Cdd:cd19523 157 FSKRLLV 163
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
225-373 2.10e-23

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: 97.95  E-value: 2.10e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  225 ILHPEIFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQV--PFIsISAPSVVSGMSGESEKKIRDLFDEA----RSLA 298
Cdd:cd19504  21 VFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNArePKI-VNGPEILNKYVGESEANIRKLFADAeeeqRRLG 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  299 PC----LVFFDEIDAITPKR-DGGAQREMERRIVAQLLTSMDelTMEKTNGkpVIIIGATNRPDSLDAALRRAGRFDREI 373
Cdd:cd19504 100 ANsglhIIIFDEIDAICKQRgSMAGSTGVHDTVVNQLLSKID--GVEQLNN--ILVIGMTNRKDLIDEALLRPGRLEVQM 175
ycf46 CHL00195
Ycf46; Provisional
528-760 4.80e-23

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 103.56  E-value: 4.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   528 PDVTWANVGALQRVRLELNmaivqpiKRPELYEK----VGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPEL 603
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLK-------KRSTSFSKqasnYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   604 LNKYVGESERSIRQVFTRARASVPCVIFFDELDALVPRRDTSL-SESSSRVVNTLLTELDglNDRRGIFVIGATNRPDMI 682
Cdd:CHL00195 296 FGGIVGESESRMRQMIRIAEALSPCILWIDEIDKAFSNSESKGdSGTTNRVLATFITWLS--EKKSPVFVVATANNIDLL 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   683 DPAMLRPGRLDKSLFIELPNTEEKLDIIKT-LTKSHgtPLS-SDVDFEEIirNEKCNNFSGADLAALVRESSVLAL--KR 758
Cdd:CHL00195 374 PLEILRKGRFDEIFFLDLPSLEEREKIFKIhLQKFR--PKSwKKYDIKKL--SKLSNKFSGAEIEQSIIEAMYIAFyeKR 449

                 ..
gi 6322994   759 KF 760
Cdd:CHL00195 450 EF 451
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
207-365 5.85e-21

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: 90.33  E-value: 5.85e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  207 LGGMDDVVAQLMELIGLPILHPEIFlSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKK 286
Cdd:cd19523   2 IAGLGALKAAIKEEVLWPLLRPDAF-SGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322994  287 IRDLFDEARSLAPCLVFFDEIDAITPKRDGGAQreMERRIVAQLLTSMDELTMEKTNGkpVIIIGATNRPDSLDAALRR 365
Cdd:cd19523  81 LQASFLAARCRQPSVLFISDLDALLSSQDDEAS--PVGRLQVELLAQLDGVLGSGEDG--VLVVCTTSKPEEIDESLRR 155
ycf46 CHL00195
Ycf46; Provisional
189-435 2.24e-19

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 92.39  E-value: 2.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   189 KRQKIKEDR----SPPNSSLKSLGGMDDVVAQLMeliglpiLHPEIF----LSTGVEPPRGVLLHGPPGCGKTSIANALA 260
Cdd:CHL00195 208 KKQIISQTEilefYSVNEKISDIGGLDNLKDWLK-------KRSTSFskqaSNYGLPTPRGLLLVGIQGTGKSLTAKAIA 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   261 GELQVPFISISAPSVVSGMSGESEKKIRDLFDEARSLAPCLVFFDEID-AIT---PKRDGGAQremeRRIVAQLLTSMDE 336
Cdd:CHL00195 281 NDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSnseSKGDSGTT----NRVLATFITWLSE 356
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   337 LTmektngKPVIIIGATNRPDSLDAALRRAGRFDREICLNVPNEVSR-----LHILKKMSDNLKidgAIDFAKLAKLTPG 411
Cdd:CHL00195 357 KK------SPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEERekifkIHLQKFRPKSWK---KYDIKKLSKLSNK 427
                        250       260
                 ....*....|....*....|....*.
gi 6322994   412 FVGADLKALVTAAGTCAI--KRIFQT 435
Cdd:CHL00195 428 FSGAEIEQSIIEAMYIAFyeKREFTT 453
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
567-702 1.11e-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: 80.50  E-value: 1.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994     567 PGGVLLWGPPGCGKTLLAKAVANESRAN---FISIKGPELL--------------NKYVGESERSIRQVFTRARASVPCV 629
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEDILeevldqllliivggKKASGSGELRLRLALALARKLKPDV 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322994     630 IFFDELDALVPRRDTSLsesssRVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPgRLDKSLFIELPN 702
Cdd:smart00382  82 LILDEITSLLDAEQEAL-----LLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
238-373 1.57e-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: 80.11  E-value: 1.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994     238 PPRGVLLHGPPGCGKTSIANALAGELQVP---FISISAP--------------SVVSGMSGESEKKIRDLFDEARSLAPC 300
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPgggVIYIDGEdileevldqllliiVGGKKASGSGELRLRLALALARKLKPD 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6322994     301 LVFFDEIDAITPKRDGGAQREMERrivaqlltsmDELTMEKTNGKPVIIIGATNRPDSLDAALRRAgRFDREI 373
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEE----------LRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRI 142
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
553-693 3.91e-15

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 73.54  E-value: 3.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  553 IKRPELYEKVGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKgpelLNKYVGESERSIRQVFTRARASvpcVIFF 632
Cdd:cd19510   9 IKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLN----LSEVVLTDDRLNHLLNTAPKQS---IILL 81
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6322994  633 DELD-ALVPRRDTSLSESSSRVVNT-----LLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLD 693
Cdd:cd19510  82 EDIDaAFESREHNKKNPSAYGGLSRvtfsgLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVD 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
240-373 1.57e-13

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 68.92  E-value: 1.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  240 RGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVSgmsgeSEKKIRDLFDEARSLApcLVFFDEIDA-----ITPKR 314
Cdd:cd19510  24 RGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVL-----TDDRLNHLLNTAPKQS--IILLEDIDAafesrEHNKK 96
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6322994  315 DGGAQREMERRIVAQLLTSMDELtmekTNGKPVIIIGATNRPDSLDAALRRAGRFDREI 373
Cdd:cd19510  97 NPSAYGGLSRVTFSGLLNALDGV----ASSEERIVFMTTNHIERLDPALIRPGRVDMKI 151
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
242-307 4.14e-13

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 72.40  E-value: 4.14e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  242 VLLHGPPGCGKTSIANALAGELQVPFISISApsVVSGMsgeseKKIRDLFDEARSLA----PCLVFFDEI 307
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSA--VTSGV-----KDIREVIEEARERRaygrRTILFVDEI 114
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
240-363 4.92e-13

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: 68.63  E-value: 4.92e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  240 RGVLLHGPPGCGKTSIANALAGELQV---------PFISISAPSVVSGMSGESEKKIRDLFDEARSLAP---CLVF--FD 305
Cdd:cd19508  53 RLVLLHGPPGTGKTSLCKALAQKLSIrlssryrygQLIEINSHSLFSKWFSESGKLVTKMFQKIQELIDdkdALVFvlID 132
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322994  306 EIDAITPKRDGGAQREMER---RIVAQLLTSMDELtmekTNGKPVIIIGATNRPDSLDAAL 363
Cdd:cd19508 133 EVESLAAARSASSSGTEPSdaiRVVNAVLTQIDRI----KRYHNNVILLTSNLLEKIDVAF 189
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
242-307 1.35e-12

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 70.50  E-value: 1.35e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   242 VLLHGPPGCGKTSIANALAGELQVPFISISApsVVSGMsgeseKKIRDLFDEARSLA----PCLVFFDEI 307
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSA--VTSGV-----KDLREVIEEARQRRsagrRTILFIDEI 101
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
570-685 1.23e-11

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 64.78  E-value: 1.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  570 VLLWGPPGCGKTLLAKAVANE---------SRANFISIKGPELLNKYVGESERSIRQVFTRARASVP---CVIF--FDEL 635
Cdd:cd19508  55 VLLHGPPGTGKTSLCKALAQKlsirlssryRYGQLIEINSHSLFSKWFSESGKLVTKMFQKIQELIDdkdALVFvlIDEV 134
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 6322994  636 DALVPRRDTSLSESSS----RVVNTLLTELDGLNDRRGIFVIGATNRPDMIDPA 685
Cdd:cd19508 135 ESLAAARSASSSGTEPsdaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVA 188
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
563-698 1.38e-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: 60.47  E-value: 1.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  563 GISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYV-----------GESERSIRQ---VFTRARASVPC 628
Cdd:cd19505   8 GLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNKPdfgnddwidgmLILKESLHRlnlQFELAKAMSPC 87
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6322994  629 VIFFDELDALVPRRDTSLSESSSR----VVNTLLTELDGLNDRRGIFVIGATNRPDMIDPAMLRPGRLDKSLFI 698
Cdd:cd19505  88 IIWIPNIHELNVNRSTQNLEEDPKlllgLLLNYLSRDFEKSSTRNILVIASTHIPQKVDPALIAPNRLDTCINI 161
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
537-681 3.14e-10

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: 63.71  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    537 ALQRVRLELNMAIVQPIKRpelyekvgisapggVLLWGPPGCGKTLLAKAVANE-------SRANFISIKGPELLNKYVG 609
Cdd:TIGR03922 296 AMALARAERGLPVAQTSNH--------------MLFAGPPGTGKTTIARVVAKIycglgvlRKPLVREVSRADLIGQYIG 361
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322994    610 ESERSIRQVFTRARASvpcVIFFDELDALVPRRDTSLSESSSRVVNTLLTELDglNDRRGIFVIGATNRPDM 681
Cdd:TIGR03922 362 ESEAKTNEIIDSALGG---VLFLDEAYTLVETGYGQKDPFGLEAIDTLLARME--NDRDRLVVIGAGYRKDL 428
PRK04195 PRK04195
replication factor C large subunit; Provisional
237-322 3.68e-10

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 63.02  E-value: 3.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   237 EPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAP-----SVVSGMSGESEKKiRDLFDEARSlapcLVFFDEIDAIT 311
Cdd:PRK04195  37 KPKKALLLYGPPGVGKTSLAHALANDYGWEVIELNASdqrtaDVIERVAGEAATS-GSLFGARRK----LILLDEVDGIH 111
                         90
                 ....*....|.
gi 6322994   312 PKRDGGAQREM 322
Cdd:PRK04195 112 GNEDRGGARAI 122
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
237-369 1.25e-08

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: 54.81  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    237 EPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVvsgmsgesEKKiRDLFDEARSLAPCLVFF-DEIDAITPkrd 315
Cdd:pfam05496  31 EALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI--------ERP-GDLAAILTNLEPGDVLFiDEIHRLNR--- 98
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322994    316 ggAQREMerrivaqLLTSMDELTMEKTNGK------------PVIIIGATNRPDSLDAALRraGRF 369
Cdd:pfam05496  99 --AVEEI-------LYPAMEDFRLDIVIGKgpsarsirldlpPFTLVGATTRAGLLTSPLR--DRF 153
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
400-435 1.62e-08

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 51.00  E-value: 1.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6322994    400 IDFAKLAKLTPGFVGADLKALVTAAGTCAIKRIFQT 435
Cdd:pfam17862   2 VDLEELAERTEGFSGADLEALCREAALAALRRGLEA 37
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
240-370 1.62e-08

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: 54.45  E-value: 1.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  240 RGVLLHGPPGCGKTSIANALAGELQVPFiSISAPSVVSGMSGESEKKIRDLFDEA-RSLAPCLVFFDEIDAITPKRDGGA 318
Cdd:cd19512  23 RNILFYGPPGTGKTLFAKKLALHSGMDY-AIMTGGDVAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLRKRSTEK 101
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 6322994  319 QREMERRIVAQLLTSMDEltmektNGKPVIIIGATNRPDSLDAALRraGRFD 370
Cdd:cd19512 102 ISEDLRAALNAFLYRTGE------QSNKFMLVLASNQPEQFDWAIN--DRID 145
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
570-640 1.85e-08

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 57.76  E-value: 1.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  570 VLLWGPPGCGKTLLAKAVANESRANFISIK----GpellnkyVGEsersIRQVFTRARA----SVPCVIFFDEL------ 635
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATDAEFVALSavtsG-------VKD----IREVIEEARErrayGRRTILFVDEIhrfnka 120

                ....*..
gi 6322994  636 --DALVP 640
Cdd:COG2256 121 qqDALLP 127
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
570-640 1.90e-08

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 57.40  E-value: 1.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   570 VLLWGPPGCGKTLLAKAVANESRANFISIKGpellnkyVGESERSIRQVFTRARASV----PCVIFFDEL--------DA 637
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATDAPFEALSA-------VTSGVKDLREVIEEARQRRsagrRTILFIDEIhrfnkaqqDA 111

                 ...
gi 6322994   638 LVP 640
Cdd:PRK13342 112 LLP 114
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
237-410 1.96e-08

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: 56.54  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    237 EPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAPSVVsgmsgesekKIRDLFDEARSLAPCLVFF-DEIDAITPkrd 315
Cdd:TIGR00635  28 EALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPALE---------KPGDLAAILTNLEEGDVLFiDEIHRLSP--- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    316 ggAQREMerrivaqLLTSMDELTMEKTNGK------------PVIIIGATNRPDSLDAALRraGRFDreICLNV----PN 379
Cdd:TIGR00635  96 --AVEEL-------LYPAMEDFRLDIVIGKgpsarsvrldlpPFTLVGATTRAGMLTSPLR--DRFG--IILRLefytVE 162
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6322994    380 EVSRlhILKKMSDNLKI----DGAIDFAKLAKLTP 410
Cdd:TIGR00635 163 ELAE--IVSRSAGLLNVeiepEAALEIARRSRGTP 195
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
232-377 4.47e-08

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 53.15  E-value: 4.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  232 LSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISIS--------------APSVVSGMSGESEKKIRDLFDEARSL 297
Cdd:cd19505   5 LRLGLSPSKGILLIGSIETGRSYLIKSLAANSYVPLIRISlnkllynkpdfgndDWIDGMLILKESLHRLNLQFELAKAM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  298 APCLVFFDEIDAITPKRDGGAQREMERRIVAQLLTSMDElTMEKTNGKPVIIIGATNRPDSLDAALRRAGRFDReiCLNV 377
Cdd:cd19505  85 SPCIIWIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSR-DFEKSSTRNILVIASTHIPQKVDPALIAPNRLDT--CINI 161
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
570-686 7.53e-08

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 52.53  E-value: 7.53e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  570 VLLWGPPGCGKTLLAKAVANESRANFISIKGPEL--LNKyvgESERSIRQVFTRARASVPCVIFF-DELDALVPRRDTS- 645
Cdd:cd19512  25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAIHKVFDWANTSRRGLLLFvDEADAFLRKRSTEk 101
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6322994  646 LSESSSRVVNTLLTELdGLNDRRGIFVIgATNRPDMIDPAM 686
Cdd:cd19512 102 ISEDLRAALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI 140
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
557-673 1.20e-07

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: 52.12  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    557 ELYEKVGISAPGGVLLWGPPGCGKTLLAKAV---ANESRANFISIKGPELLNKYVG----ESERSIRQVFTRARASVPcV 629
Cdd:pfam13191  14 DALDRVRSGRPPSVLLTGEAGTGKTTLLRELlraLERDGGYFLRGKCDENLPYSPLlealTREGLLRQLLDELESSLL-E 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 6322994    630 IFFDELDALVPRRDTSLSESSSRVVNTLLTELDGLNDRRGIFVI 673
Cdd:pfam13191  93 AWRAALLEALAPVPELPGDLAERLLDLLLRLLDLLARGERPLVL 136
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
724-776 1.91e-07

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: 47.92  E-value: 1.91e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6322994    724 DVDFEEIIrnEKCNNFSGADLAALVRESSVLALKRkffqseEIQSVLDNDLDK 776
Cdd:pfam17862   1 DVDLEELA--ERTEGFSGADLEALCREAALAALRR------GLEAVTQEDLEE 45
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
239-369 1.50e-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: 49.30  E-value: 1.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  239 PRGVLLHGPPGCGKTSIANALAGELQVPFISISAP--SVVSGMSGESEKKIRDLFDEarslapcLVFFDEIDAITpKRDG 316
Cdd:cd19498  46 PKNILMIGPTGVGKTEIARRLAKLAGAPFIKVEATkfTEVGYVGRDVESIIRDLVEG-------IVFIDEIDKIA-KRGG 117
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6322994  317 GAQREMERRIVAQLLTSMDELTMEKTNGKPV-------IIIGATN--RPDSLDAALRraGRF 369
Cdd:cd19498 118 SSGPDVSREGVQRDLLPIVEGSTVSTKYGPVktdhilfIAAGAFHvaKPSDLIPELQ--GRF 177
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
562-753 1.91e-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: 50.55  E-value: 1.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  562 VGISAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKG-PELL-NKYVGES-------ERSIRQ--VFTRarasvpcVI 630
Cdd:COG0714  26 IALLAGGHLLLEGVPGVGKTTLAKALARALGLPFIRIQFtPDLLpSDILGTYiydqqtgEFEFRPgpLFAN-------VL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  631 FFDELDalvpRrdtslseSSSRVVNTLLTELDglnDRR------------GIFVIGATNRPDMID-----PAMLRpgRLD 693
Cdd:COG0714  99 LADEIN----R-------APPKTQSALLEAME---ERQvtipggtyklpePFLVIATQNPIEQEGtyplpEAQLD--RFL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  694 KSLFIELPNTEEKLDIIKTLTKSHGTPLSSDVDFEEIIRnekcnnfsgadLAALVRESSV 753
Cdd:COG0714 163 LKLYIGYPDAEEEREILRRHTGRHLAEVEPVLSPEELLA-----------LQELVRQVHV 211
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
237-273 4.13e-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: 49.69  E-value: 4.13e-06
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 6322994  237 EPPRGVLLHGPPGCGKTSIANALAGELQVPFISISAP 273
Cdd:COG2255  52 EALDHVLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
242-273 8.90e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 48.59  E-value: 8.90e-06
                         10        20        30
                 ....*....|....*....|....*....|..
gi 6322994   242 VLLHGPPGCGKTSIANALAGELQVPFISISAP 273
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGP 85
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
240-284 1.23e-05

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 48.46  E-value: 1.23e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6322994    240 RGVLLHGPPGCGKTSIANALAGEL--QVPFISISAPSVVSGMSGESE 284
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELgeDTPFTSISGSEVYSLEMKKTE 97
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
240-373 1.29e-05

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: 48.69  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    240 RGVLLHGPPGCGKTSIANALA------GELQVPFI-SISAPSVVSGMSGESEKKIRDLFDEARSLApclVFFDEIDAITP 312
Cdd:TIGR03922 313 NHMLFAGPPGTGKTTIARVVAkiycglGVLRKPLVrEVSRADLIGQYIGESEAKTNEIIDSALGGV---LFLDEAYTLVE 389
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322994    313 KRDgGAQREMERRIVAQLLTSM----DELTmektngkpVIIIGATNRPDS-LDAALRRAGRFDREI 373
Cdd:TIGR03922 390 TGY-GQKDPFGLEAIDTLLARMendrDRLV--------VIGAGYRKDLDKfLEVNEGLRSRFTRVI 446
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
241-369 1.34e-05

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: 45.36  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    241 GVLLHGPPGCGKTSIANALAGEL--QVPFI-----SISAPSVVSGMS---GESEKKIRDLFDEARSlaPCLVFFDEIDAI 310
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALsnRPVFYvqltrDTTEEDLFGRRNidpGGASWVDGPLVRAARE--GEIAVLDEINRA 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6322994    311 TPKrdggaqremerrIVAQLLTSMDELTMEKTNGKPVI--------IIGATNRPD----SLDAALRRagRF 369
Cdd:pfam07728  79 NPD------------VLNSLLSLLDERRLLLPDGGELVkaapdgfrLIATMNPLDrglnELSPALRS--RF 135
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
789-824 1.93e-05

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


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 42.87  E-value: 1.93e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 6322994    789 EIIVTMSDFRSALRKIKPSVSDKDRLKYDRLNKKMG 824
Cdd:pfam09336  26 EPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
240-284 2.44e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 47.66  E-value: 2.44e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 6322994  240 RGVLLHGPPGCGKTSIANALAGEL--QVPFISISAPSVVSGMSGESE 284
Cdd:COG1224  65 KGILIVGPPGTGKTALAVAIARELgeDTPFVAISGSEIYSAELKKTE 111
PRK13341 PRK13341
AAA family ATPase;
555-640 3.67e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 47.36  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   555 RPE-LYEKVG---ISAPGGVL-------------LWGPPGCGKTLLAKAVANESRANFISikgpelLNKYV-GESErsIR 616
Cdd:PRK13341  23 RPRtLEEFVGqdhILGEGRLLrraikadrvgsliLYGPPGVGKTTLARIIANHTRAHFSS------LNAVLaGVKD--LR 94
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 6322994   617 QVFTRARASVP-----CVIFFDEL--------DALVP 640
Cdd:PRK13341  95 AEVDRAKERLErhgkrTILFIDEVhrfnkaqqDALLP 131
RecA-like_Lon cd19500
lon protease homolog 2 peroxisomal; Lon protease (also known as Lon peptidase) is an ...
209-311 3.98e-05

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: 45.24  E-value: 3.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  209 GMDDVVAQLMELIGLPILHPEIflstgveppRG--VLLHGPPGCGKTSIANALAGELQVPFISISapsvVSGMSGESE-- 284
Cdd:cd19500  14 GLEDVKERILEYLAVRKLKGSM---------KGpiLCLVGPPGVGKTSLGKSIARALGRKFVRIS----LGGVRDEAEir 80
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 6322994  285 -----------KKIRDLFDEARSLAPcLVFFDEIDAIT 311
Cdd:cd19500  81 ghrrtyvgampGRIIQALKKAGTNNP-VFLLDEIDKIG 117
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
570-679 5.15e-05

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: 44.44  E-value: 5.15e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  570 VLLWGPPGCGKTLLAKAVANESRANFISIKGPELLNKYVGES--ERSIRQVFTRARASVPCVIFFDELDAL----VPRRD 643
Cdd:cd19506  29 LLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTfykkVPKTE 108
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 6322994  644 TSLseSSSRVVNTLLTELDGLNDRRGIFVIGATNRP 679
Cdd:cd19506 109 KQL--DPKRLKKDLPKILKSLKPEDRVLIVGTTSRP 142
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
569-688 5.41e-05

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: 43.82  E-value: 5.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    569 GVLLWGPPGCGKTLLAKAVANE-SRANFISIkgpeLLNKYVGESE----RSIR--------QVFTRArASVPCVIFFDEL 635
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAAlSNRPVFYV----QLTRDTTEEDlfgrRNIDpggaswvdGPLVRA-AREGEIAVLDEI 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322994    636 DalvprrdtslsESSSRVVNTLLTELD----GLNDRR--------GIFVIGATNRPDM----IDPAMLR 688
Cdd:pfam07728  76 N-----------RANPDVLNSLLSLLDerrlLLPDGGelvkaapdGFRLIATMNPLDRglneLSPALRS 133
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
539-603 6.62e-05

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 44.03  E-value: 6.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994    539 QRVRLELNMAIVQPIKRPElyekvgisAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPEL 603
Cdd:pfam05496  13 EKVKENLKIFIEAAKQRGE--------ALDHVLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
PRK13341 PRK13341
AAA family ATPase;
243-296 7.28e-05

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.59  E-value: 7.28e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6322994   243 LLHGPPGCGKTSIANALAGELQVPFISISApsVVSGMsgeseKKIRDLFDEARS 296
Cdd:PRK13341  56 ILYGPPGVGKTTLARIIANHTRAHFSSLNA--VLAGV-----KDLRAEVDRAKE 102
PRK04195 PRK04195
replication factor C large subunit; Provisional
570-645 2.05e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 44.91  E-value: 2.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994   570 VLLWGPPGCGKTLLAKAVANE------------SRaNFISIKgpellnKYVGESERSiRQVFTRARAsvpcVIFFDELDA 637
Cdd:PRK04195  42 LLLYGPPGVGKTSLAHALANDygwevielnasdQR-TADVIE------RVAGEAATS-GSLFGARRK----LILLDEVDG 109

                 ....*...
gi 6322994   638 LVPRRDTS 645
Cdd:PRK04195 110 IHGNEDRG 117
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
239-350 2.34e-04

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: 42.49  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    239 PRGVLLHGPPGCGKTSIANALAGEL---QVPFISISAPSVVS-GMSGESEKK---IRDLFDEARSLAPcLVFFDEIDAIT 311
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELLRALerdGGYFLRGKCDENLPySPLLEALTReglLRQLLDELESSLL-EAWRAALLEAL 102
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6322994    312 pkRDGGAQREMERRIVAQLLTSMdeLTMEKTNGKPVIII 350
Cdd:pfam13191 103 --APVPELPGDLAERLLDLLLRL--LDLLARGERPLVLV 137
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
242-365 2.65e-04

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


Pssm-ID: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 41.33  E-value: 2.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  242 VLLHGPPGCGKTSIANALAGELQ---VPFISISAPSVVSgmsgeseKKIRDLFDEARslaPCLVFFDEIDAITPKRDGGA 318
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALlsdEPVIFISFLDTIL-------EAIEDLIEEKK---LDIIIIDSLSSLARASQGDR 70
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 6322994  319 QREMeRRIVAQLLTSMdeltmeKTNGKPVIiigATNRPDSLDAALRR 365
Cdd:cd01120  71 SSEL-LEDLAKLLRAA------RNTGITVI---ATIHSDKFDIDRGG 107
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
570-603 2.76e-04

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 43.97  E-value: 2.76e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 6322994   570 VLLWGPPGCGKTLLAKAVANESRANFISIKGPEL 603
Cdd:PRK00080  54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
570-636 4.61e-04

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: 41.80  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    570 VLLWGPPGCGKTLLAKAVANE---SRANFISIKGPELLNK------------YVGESERSirQVFTRARASVPCVIFFDE 634
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELlfgDERALIRIDMSEYMEEhsvsrligappgYVGYEEGG--QLTEAVRRKPYSIVLIDE 83

                  ..
gi 6322994    635 LD 636
Cdd:pfam07724  84 IE 85
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
242-383 4.84e-04

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 41.44  E-value: 4.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  242 VLLHGPPGCGKTSIANALAGELQVPFISIsapsvvsgmsgesekkirdlfDEARS-LAPclvffDEIDAITPKRDGGAQ- 319
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLGAVRLRS---------------------DVVRKrLFG-----AGLAPLERSPEATARt 55
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322994  320 -REMeRRIVAQLLTSmdeltmektnGKPVIIIGATNRPDSLDAALRRAGRFD---REICLNVPNEVSR 383
Cdd:COG0645  56 yARL-LALARELLAA----------GRSVILDATFLRRAQREAFRALAEEAGapfVLIWLDAPEEVLR 112
AroK COG0703
Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the ...
246-331 5.27e-04

Shikimate kinase [Amino acid transport and metabolism]; Shikimate kinase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440467 [Multi-domain]  Cd Length: 165  Bit Score: 41.65  E-value: 5.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  246 GPPGCGKTSIANALAGELQVPFIS----ISApsvVSGMSgesekkIRDLFDEarslapclvffdeidaitpkrDGGAQ-R 320
Cdd:COG0703   5 GMMGAGKSTVGRLLAKRLGLPFVDtdaeIEE---RAGMS------IPEIFAE---------------------EGEAGfR 54
                        90
                ....*....|.
gi 6322994  321 EMERRIVAQLL 331
Cdd:COG0703  55 ELEREVLAELL 65
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
237-364 6.49e-04

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 42.91  E-value: 6.49e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  237 EPPRGVLLHGPPGCGKTSIANALAGELQ---------VPFISI------SAPSVVSG------------MSGESEKKIRD 289
Cdd:COG1474  49 ERPSNVLIYGPTGTGKTAVAKYVLEELEeeaeergvdVRVVYVncrqasTRYRVLSRileelgsgedipSTGLSTDELFD 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  290 LFDEA--RSLAPCLVFFDEIDAITPKRDGgaqremerRIVAQLLTSMDELTmektnGKPVIIIGATNRP---DSLDAALR 364
Cdd:COG1474 129 RLYEAldERDGVLVVVLDEIDYLVDDEGD--------DLLYQLLRANEELE-----GARVGVIGISNDLeflENLDPRVK 195
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
239-364 7.50e-04

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 42.27  E-value: 7.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  239 PRGVLLHGPPGCGKTSIANALAGEL-------QVPFISISAPSVVSG-------MSGESEKK------IRDLFDEARSLA 298
Cdd:COG0470  18 PHALLLHGPPGIGKTTLALALARDLlcenpegGKACGQCHSRLMAAGnhpdlleLNPEEKSDqigidqIRELGEFLSLTP 97
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  299 PC----LVFFDEIDAITpkrdGGAQRemerrivAqLLTsmdelTMEKTNGKPVIIIgATNRPDSLDAALR 364
Cdd:COG0470  98 LEggrkVVIIDEADAMN----EAAAN-------A-LLK-----TLEEPPKNTPFIL-IANDPSRLLPTIR 149
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
242-268 7.58e-04

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 40.70  E-value: 7.58e-04
                        10        20
                ....*....|....*....|....*..
gi 6322994  242 VLLHGPPGCGKTSIANALAGELQVPFI 268
Cdd:cd02021   2 IVVMGVSGSGKSTVGKALAERLGAPFI 28
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
242-354 9.25e-04

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 40.64  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    242 VLLHGPPGCGKTSIANALAGELQV---PFISISA-----PSVVSGMSGESEKKIR-----DLFDEARSLAPCLVFFDEID 308
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELLFGderALIRIDMseymeEHSVSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6322994    309 AITPkrdgGAQREmerrivaqLLTSMDELTMEKTNGKPV-----IIIGATN 354
Cdd:pfam07724  86 KAHP----GVQND--------LLQILEGGTLTDKQGRTVdfkntLFIMTGN 124
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
539-603 1.05e-03

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: 41.90  E-value: 1.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994    539 QRVRLELNMAIVQPIKRPElyekvgisAPGGVLLWGPPGCGKTLLAKAVANESRANFISIKGPEL 603
Cdd:TIGR00635  10 EKVKEQLQLFIEAAKMRQE--------ALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL 66
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
570-601 1.08e-03

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 41.99  E-value: 1.08e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 6322994  570 VLLWGPPGCGKTLLAKAVANESRANFISIKGP 601
Cdd:COG2255  57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
242-270 1.27e-03

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 41.69  E-value: 1.27e-03
                        10        20
                ....*....|....*....|....*....
gi 6322994  242 VLLHGPPGCGKTSIANALAGELQVPFISI 270
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALGLPFIRI 62
PRK08116 PRK08116
hypothetical protein; Validated
569-606 1.33e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 41.54  E-value: 1.33e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 6322994   569 GVLLWGPPGCGKTLLAKAVANESRANFISIKG---PELLNK 606
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANELIEKGVPVIFvnfPQLLNR 156
RecA-like_ClpB_Hsp104-like cd19499
Chaperone protein ClpB/Hsp104 subfamily; Bacterial Caseinolytic peptidase B (ClpB) and ...
548-636 1.58e-03

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


Pssm-ID: 410907 [Multi-domain]  Cd Length: 178  Bit Score: 40.24  E-value: 1.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  548 AIVQPIKRPelyeKVGISAPGGVLLW----GPPGCGKTLLAKAVA---NESRANFISIKGPELLNK------------YV 608
Cdd:cd19499  22 AVSDAIRRA----RAGLSDPNRPIGSflflGPTGVGKTELAKALAellFGDEDNLIRIDMSEYMEKhsvsrligappgYV 97
                        90       100
                ....*....|....*....|....*...
gi 6322994  609 GESERSirQVFTRARASVPCVIFFDELD 636
Cdd:cd19499  98 GYTEGG--QLTEAVRRKPYSVVLLDEIE 123
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
242-282 1.98e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 38.35  E-value: 1.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6322994    242 VLLHGPPGCGKTSIANALAGELQvPFISISAPSVVSGMSGE 282
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARALL-KKLGLPKDSVYSRNPDD 40
GntK COG3265
Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the ...
239-268 2.22e-03

Gluconate kinase [Carbohydrate transport and metabolism]; Gluconate kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 442496 [Multi-domain]  Cd Length: 164  Bit Score: 39.73  E-value: 2.22e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 6322994  239 PRGVLLHGPPGCGKTSIANALAGELQVPFI 268
Cdd:COG3265   1 PMVIVVMGVSGSGKSTVGQALAERLGWPFI 30
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
224-371 2.40e-03

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 39.54  E-value: 2.40e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  224 PILHPeifLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISI----------------SAPSVVSGMSGeSEKKi 287
Cdd:cd00267  13 TALDN---VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEIlidgkdiaklpleelrRRIGYVPQLSG-GQRQ- 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  288 rdLFDEARSLA--PCLVFFDEIDAitpkrdggAQREMERRIVAQLLTSMDEltmektNGKPVIIIgaTNRPDSLDAALRR 365
Cdd:cd00267  88 --RVALARALLlnPDLLLLDEPTS--------GLDPASRERLLELLRELAE------EGRTVIIV--THDPELAELAADR 149

                ....*.
gi 6322994  366 AGRFDR 371
Cdd:cd00267 150 VIVLKD 155
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
225-316 2.58e-03

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 40.28  E-value: 2.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  225 ILHPEIFLSTGVEPPRG-VLLHGPPGCGKTSIANALAGELQVPFISISAPSVV-SGMSGES-EKKIRDL-----FDEARS 296
Cdd:cd19497  35 IRNNLKQKDDDVELEKSnILLIGPTGSGKTLLAQTLAKILDVPFAIADATTLTeAGYVGEDvENILLKLlqaadYDVERA 114
                        90       100
                ....*....|....*....|
gi 6322994  297 lAPCLVFFDEIDAITPKRDG 316
Cdd:cd19497 115 -QRGIVYIDEIDKIARKSEN 133
Rad51B cd19493
RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair ...
239-396 3.25e-03

RAD51B recombinase; RAD51B recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. RAD51B, together with the other RAD51 paralogs, RAD51C, RAD51D, XRCC3, and XRCC2, helps recruit RAD51 to the break site.


Pssm-ID: 410901 [Multi-domain]  Cd Length: 222  Bit Score: 40.00  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  239 PRGVL--LHGPPGCGKTSIANALAGELQVPFISISAPSVVSGMSGESEKKIRDLFDEARSLAPclvffdeIDAITPKRDG 316
Cdd:cd19493   9 PLGAIteITGASGSGKTQFALTLASSAAMPARKGGLDGGVLYIDTESKFSAERLAEIAEARFP-------EAFSGFMEEN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  317 GAQREMERRI-------VAQLLTSMDEL--TMEKTNGKPVIIigatnrpDSLDAALRRAGRFDREICLNVPNEVSRL-HI 386
Cdd:cd19493  82 ERAEEMLKRVavvrvttLAQLLERLPNLeeHILSSGVRLVVI-------DSIAALVRREFGGSDGEVTERHNALAREaSS 154
                       170
                ....*....|
gi 6322994  387 LKKMSDNLKI 396
Cdd:cd19493 155 LKRLAEEFRI 164
PRK12402 PRK12402
replication factor C small subunit 2; Reviewed
209-263 3.31e-03

replication factor C small subunit 2; Reviewed


Pssm-ID: 237090 [Multi-domain]  Cd Length: 337  Bit Score: 40.74  E-value: 3.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6322994   209 GMDDVVAQLMELIGLPIL-HpeiflstgvepprgVLLHGPPGCGKTSIANALAGEL 263
Cdd:PRK12402  19 GQDEVVERLSRAVDSPNLpH--------------LLVQGPPGSGKTAAVRALAREL 60
AAA_33 pfam13671
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ...
242-292 3.51e-03

AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.


Pssm-ID: 463952 [Multi-domain]  Cd Length: 143  Bit Score: 38.83  E-value: 3.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6322994    242 VLLHGPPGCGKTSIANALAGELqvPFISISAPSVVSGMSGESEKKIRDLFD 292
Cdd:pfam13671   2 ILLVGLPGSGKSTLARRLLEEL--GAVRLSSDDERKRLFGEGRPSISYYTD 50
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
564-586 3.87e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 39.44  E-value: 3.87e-03
                          10        20
                  ....*....|....*....|....*
gi 6322994    564 ISAPGG--VLLWGPPGCGKTLLAKA 586
Cdd:pfam01078  17 IAAAGGhnLLMIGPPGSGKTMLAKR 41
COG3896 COG3896
Chloramphenicol 3-O-phosphotransferase [Defense mechanisms];
238-373 3.99e-03

Chloramphenicol 3-O-phosphotransferase [Defense mechanisms];


Pssm-ID: 443103  Cd Length: 182  Bit Score: 39.13  E-value: 3.99e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  238 PPRGVLLHGPPGCGKTSIANALAGELQVPFISIS--------APSVVSGMSGESEK----KIRDLFDEA--RSLAP---- 299
Cdd:COG3896   4 KGRIIILNGASSSGKSSIARALQELLPEPWLHLSidtfvdmlPPRLLRGIDGPGGAidvgPILRRLIRGmhRAIAAfara 83
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6322994  300 -CLVFFDEIdaitpKRDGGAQREMERRIVaqlltsmdeltmektnGKPVIIIGATNRPDSLDAalRRAGRFDREI 373
Cdd:COG3896  84 gNNVIVDDV-----LLEGAWLQDLLRALS----------------GLPVLFVGVRCPLEELER--RERARGDRPI 135
ycf2 CHL00206
Ycf2; Provisional
230-339 5.08e-03

Ycf2; Provisional


Pssm-ID: 214396 [Multi-domain]  Cd Length: 2281  Bit Score: 40.66  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994    230 IFLSTGVEPPRGVLLHGPPGCGKTSIANALAGELQVPFISISapsvvsgmsgesekkIRDLFDEarslAPCLVFFDEIDa 309
Cdd:CHL00206 1621 FSLRLALSPSRGILVIGSIGTGRSYLVKYLATNSYVPFITVF---------------LNKFLDN----KPKGFLIDDID- 1680
                          90       100       110
                  ....*....|....*....|....*....|
gi 6322994    310 ITPKRDGGAQREMERRIVAQLLTSMDELTM 339
Cdd:CHL00206 1681 IDDSDDIDDSDDIDRDLDTELLTMMNALTM 1710
CmkB COG1102
Cytidylate kinase [Nucleotide transport and metabolism];
246-351 5.34e-03

Cytidylate kinase [Nucleotide transport and metabolism];


Pssm-ID: 440719 [Multi-domain]  Cd Length: 188  Bit Score: 39.04  E-value: 5.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322994  246 GPPGCGKTSIANALAGELQVPFISisapsvvsgmsgesekkiRDLFDE-ARSLAPCLVFFDEIDAITPKRDGGAQREmER 324
Cdd:COG1102   7 REPGSGGTTIAKRLAEKLGLPLYD------------------GEILREaAKERGLSEEEFEKLDEKAPSLLYRDTAE-ED 67
                        90       100
                ....*....|....*....|....*..
gi 6322994  325 RIVAQLltsmDELTMEKTNGKPVIIIG 351
Cdd:COG1102  68 EIDRAL----DKVIRELARKGNCVIVG 90
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
570-590 9.87e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 36.43  E-value: 9.87e-03
                          10        20
                  ....*....|....*....|.
gi 6322994    570 VLLWGPPGCGKTLLAKAVANE 590
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
 
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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