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Conserved domains on  [gi|729737493|ref|XP_010564867|]
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PREDICTED: putative fidgetin-like protein 2 [Haliaeetus leucocephalus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 358-521 2.67e-66

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


The actual alignment was detected with superfamily member cd19523:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 163  Bit Score: 213.98  E-value: 2.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRPGAYTGASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKI 437
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 438 LQTVFFVASCRQPAVVLITEAESLLVARAGEDgSQAGNLKSQLLSYLDNVATSSEQNVVVIGTTSRPGSMDEASHRRFAK 517
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDDEA-SPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                 ....
gi 729737493 518 RFYI 521
Cdd:cd19523  160 RLLV 163
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 102-343 2.26e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  102 PVAHGSDGAYPLTPIHDGLPGAkgvVPPAVPPSGGAIGLGGSPVVSANLADPMYPGNSCGGAAAGSGGLGSSQEYPSGYG 181
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAP---APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  182 GTYLPsgyctqpaaalpPPHPPALHGSGLLQPPHPSPALVPGYGSSGAMYNYAAGSYPPQPGYGTihPPHPSASYLPSGI 261
Cdd:PHA03247 2825 AGPLP------------PPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA--PARPPVRRLARPA 2890

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  262 AAPTSGGQPMKSMVSPPYGAGDAPLRPAEPFEKFSPPLangEQAAEPGPPFPlrLPPKAPVFGSPPV-EEQPKNVDPLVL 340
Cdd:PHA03247 2891 VSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ---PQPPPPPPPRP--QPPLAPTTDPAGAgEPSGAVPQPWLG 2965


                  ...
gi 729737493  341 ELV 343
Cdd:PHA03247 2966 ALV 2968
Vps4_C super family cl07827
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 585-618 1.15e-03

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.


The actual alignment was detected with superfamily member pfam09336:

Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 37.48  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 729737493  585 PTSYQDFEKAFCKVRPAASQKELDLFLEWDKMYG 618
Cdd:pfam09336  28 PVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 358-521 2.67e-66

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: 213.98  E-value: 2.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRPGAYTGASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKI 437
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 438 LQTVFFVASCRQPAVVLITEAESLLVARAGEDgSQAGNLKSQLLSYLDNVATSSEQNVVVIGTTSRPGSMDEASHRRFAK 517
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDDEA-SPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                 ....
gi 729737493 518 RFYI 521
Cdd:cd19523  160 RLLV 163
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 284-594 1.70e-42

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: 157.77  E-value: 1.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 284 APLRPAEPFEKFSPPLANGEQAAEPGPPFPLRLPPKAPVFGSPPVEEqpknVDPLVLELVNTKIVERGppvqWTDIAGQV 363
Cdd:COG0464   92 LLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTY----EDIGGLEEELLELREAI----LDDLGGLE 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 364 SVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVF 442
Cdd:COG0464  164 EVKEELRELVALPLKRPELREEYGlPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVF 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 443 FVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVatssEQNVVVIGTTSRPGSMDEASHRRFAKRFYIS 522
Cdd:COG0464  244 DKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL----RSDVVVIAATNRPDLLDPALLRRFDEIIFFP 319

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 729737493 523 PPDSIARRQILHHALAQQNsCLSEREMASLVQHTESFSGSELVQLCQHAGATTLHALPGQIqptSYQDFEKA 594
Cdd:COG0464  320 LPDAEERLEIFRIHLRKRP-LDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPV---TTEDLLEA 387
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 330-618 4.95e-37

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: 147.36  E-value: 4.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  330 EQPKNVDPLVLELVNTKIvergPPVQWTDIAGQVSVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSR 408
Cdd:TIGR01243 430 EALKMVEPSAIREVLVEV----PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGiRPPKGVLLFGPPGTGKTLLAK 505

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  409 CISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITEAESLLVAR-AGEDGSQAGNLKSQLLSYLDNV 487
Cdd:TIGR01243 506 AVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARgARFDTSVTDRIVNQLLTEMDGI 585

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  488 ATSSeqNVVVIGTTSRPGSMDEASHR--RFAKRFYISPPDSIARRQILhhALAQQNSCLSER-EMASLVQHTESFSGSEL 564
Cdd:TIGR01243 586 QELS--NVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIF--KIHTRSMPLAEDvDLEELAEMTEGYTGADI 661

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737493  565 VQLCQHAGATTLHALPGQIQP---------------TSYQDFEKAFCKVRPAASQKELDLFLEWDKMYG 618
Cdd:TIGR01243 662 EAVCREAAMAALRESIGSPAKeklevgeeeflkdlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 393-522 1.51e-28

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: 110.38  E-value: 1.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  393 ILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQ 472
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 729737493  473 AGNLKSQLLSYLDNVaTSSEQNVVVIGTTSRPGSMDEASHRRFAKRFYIS 522
Cdd:pfam00004  81 SRRVVNQLLTELDGF-TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFP 129
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 334-598 3.59e-20

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 93.68  E-value: 3.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 334 NVDPLVlelvNTKIVERGPPVQWTDIAGQVSVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSRCIST 412
Cdd:PTZ00361 164 EVDPLV----SVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGiKPPKGVILYGPPGTGKTLLAKAVAN 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 413 QLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITEAESLLVAR-----AGEDGSQAGNLksQLLSYLDNV 487
Cdd:PTZ00361 240 ETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydatsGGEKEIQRTML--ELLNQLDGF 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 488 atSSEQNVVVIGTTSRPGSMDEASHR--RFAKRFYISPPDSIARRQILHHALAQQNscLSER-EMASLVQHTESFSGSEL 564
Cdd:PTZ00361 318 --DSRGDVKVIMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMT--LAEDvDLEEFIMAKDELSGADI 393

                        250       260       270
                 ....*....|....*....|....*....|....
gi 729737493 565 VQLCQHAGattLHALPGQIQPTSYQDFEKAFCKV 598
Cdd:PTZ00361 394 KAICTEAG---LLALRERRMKVTQADFRKAKEKV 424
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 389-525 2.26e-06

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: 47.75  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493   389 PPRTILLFGPHGTGKTLLSRCISTQLGSTLLK---LSGKTLLSTWKAEAEKILQTVFFVASCR--------------QPA 451
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviyIDGEDILEEVLDQLLLIIVGGKKASGSGelrlrlalalarklKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 729737493   452 VVLITEAESLLvaragedGSQAGNLKSQLLSYLDNVATSSEQNVVVIGTTSRPG-SMDEASHRRFAKRFYISPPD 525
Cdd:smart00382  81 VLILDEITSLL-------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKdLGPALLRRRFDRRIVLLLIL 148
PHA03247 PHA03247
large tegument protein UL36; Provisional
 102-343 2.26e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  102 PVAHGSDGAYPLTPIHDGLPGAkgvVPPAVPPSGGAIGLGGSPVVSANLADPMYPGNSCGGAAAGSGGLGSSQEYPSGYG 181
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAP---APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  182 GTYLPsgyctqpaaalpPPHPPALHGSGLLQPPHPSPALVPGYGSSGAMYNYAAGSYPPQPGYGTihPPHPSASYLPSGI 261
Cdd:PHA03247 2825 AGPLP------------PPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA--PARPPVRRLARPA 2890

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  262 AAPTSGGQPMKSMVSPPYGAGDAPLRPAEPFEKFSPPLangEQAAEPGPPFPlrLPPKAPVFGSPPV-EEQPKNVDPLVL 340
Cdd:PHA03247 2891 VSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ---PQPPPPPPPRP--QPPLAPTTDPAGAgEPSGAVPQPWLG 2965


                  ...
gi 729737493  341 ELV 343
Cdd:PHA03247 2966 ALV 2968
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 585-618 1.15e-03

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: 37.48  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 729737493  585 PTSYQDFEKAFCKVRPAASQKELDLFLEWDKMYG 618
Cdd:pfam09336  28 PVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
 
Name Accession Description Interval E-value
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 358-521 2.67e-66

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: 213.98  E-value: 2.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRPGAYTGASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKI 437
Cdd:cd19523    1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 438 LQTVFFVASCRQPAVVLITEAESLLVARAGEDgSQAGNLKSQLLSYLDNVATSSEQNVVVIGTTSRPGSMDEASHRRFAK 517
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDDEA-SPVGRLQVELLAQLDGVLGSGEDGVLVVCTTSKPEEIDESLRRYFSK 159


                 ....
gi 729737493 518 RFYI 521
Cdd:cd19523  160 RLLV 163
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 336-521 9.55e-61

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: 200.21  E-value: 9.55e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 336 DPLVLELVNTKIVERGPPVQWTDIAGQVSVKATIEEELVWPILRPGAYTGASRPPRTILLFGPHGTGKTLLSRCISTQLG 415
Cdd:cd19525    1 EPKMIELIMSEIMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 416 STLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVATSSEQNV 495
Cdd:cd19525   81 ATFFSISASSLTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSSEDRI 160

                        170       180
                 ....*....|....*....|....*.
gi 729737493 496 VVIGTTSRPGSMDEASHRRFAKRFYI 521
Cdd:cd19525  161 LVVGATNRPQEIDEAARRRLVKRLYI 186
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 359-521 3.22e-53

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: 179.47  E-value: 3.22e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 359 IAGQVSVKATIEEELVWPILRPGAYTGASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKIL 438
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKIV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 439 QTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVATSSEQNVVVIGTTSRPGSMDEASHRRFAKR 518
Cdd:cd19509   81 RALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKPEDRVLVLGATNRPWELDEAFLRRFEKR 160


                 ...
gi 729737493 519 FYI 521
Cdd:cd19509  161 IYI 163
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 284-594 1.70e-42

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: 157.77  E-value: 1.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 284 APLRPAEPFEKFSPPLANGEQAAEPGPPFPLRLPPKAPVFGSPPVEEqpknVDPLVLELVNTKIVERGppvqWTDIAGQV 363
Cdd:COG0464   92 LLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTY----EDIGGLEEELLELREAI----LDDLGGLE 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 364 SVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVF 442
Cdd:COG0464  164 EVKEELRELVALPLKRPELREEYGlPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVF 243

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 443 FVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVatssEQNVVVIGTTSRPGSMDEASHRRFAKRFYIS 522
Cdd:COG0464  244 DKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL----RSDVVVIAATNRPDLLDPALLRRFDEIIFFP 319

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 729737493 523 PPDSIARRQILHHALAQQNsCLSEREMASLVQHTESFSGSELVQLCQHAGATTLHALPGQIqptSYQDFEKA 594
Cdd:COG0464  320 LPDAEERLEIFRIHLRKRP-LDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPV---TTEDLLEA 387
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 352-605 1.96e-42

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 155.55  E-value: 1.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 352 PPVQWTDIAGQVSVKATIEEELVWPILRPGAYT--GAsRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLST 429
Cdd:COG1222   73 PDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyGI-EPPKGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 430 WKAEAEKILQTVFFVASCRQPAVVLITEAESLLVARagEDGSQAGNLK---SQLLSYLDNVatSSEQNVVVIGTTSRPGS 506
Cdd:COG1222  152 YIGEGARNVREVFELAREKAPSIIFIDEIDAIAARR--TDDGTSGEVQrtvNQLLAELDGF--ESRGDVLIIAATNRPDL 227

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 507 MDEASHR--RFAKRFYISPPDSIARRQILHHALAQQNsCLSEREMASLVQHTESFSGSELVQLCQHAGATTLHALPGQIQ 584
Cdd:COG1222  228 LDPALLRpgRFDRVIEVPLPDEEAREEILKIHLRDMP-LADDVDLDKLAKLTEGFSGADLKAIVTEAGMFAIREGRDTVT 306

                        250       260
                 ....*....|....*....|.
gi 729737493 585 PtsyQDFEKAFCKVRPAASQK 605
Cdd:COG1222  307 M---EDLEKAIEKVKKKTETA 324
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 358-521 1.05e-40

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: 145.76  E-value: 1.05e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRPGAYTGASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKI 437
Cdd:cd19524    1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 438 LQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVATSSEQNVVVIGTTSRPGSMDEASHRRFAK 517
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDDRVLVMGATNRPQELDDAVLRRFTK 160


                 ....
gi 729737493 518 RFYI 521
Cdd:cd19524  161 RVYV 164
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 330-618 4.95e-37

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: 147.36  E-value: 4.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  330 EQPKNVDPLVLELVNTKIvergPPVQWTDIAGQVSVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSR 408
Cdd:TIGR01243 430 EALKMVEPSAIREVLVEV----PNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGiRPPKGVLLFGPPGTGKTLLAK 505

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  409 CISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITEAESLLVAR-AGEDGSQAGNLKSQLLSYLDNV 487
Cdd:TIGR01243 506 AVATESGANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARgARFDTSVTDRIVNQLLTEMDGI 585

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  488 ATSSeqNVVVIGTTSRPGSMDEASHR--RFAKRFYISPPDSIARRQILhhALAQQNSCLSER-EMASLVQHTESFSGSEL 564
Cdd:TIGR01243 586 QELS--NVVVIAATNRPDILDPALLRpgRFDRLILVPPPDEEARKEIF--KIHTRSMPLAEDvDLEELAEMTEGYTGADI 661

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737493  565 VQLCQHAGATTLHALPGQIQP---------------TSYQDFEKAFCKVRPAASQKELDLFLEWDKMYG 618
Cdd:TIGR01243 662 EAVCREAAMAALRESIGSPAKeklevgeeeflkdlkVEMRHFLEALKKVKPSVSKEDMLRYERLAKELK 730
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 352-521 1.02e-35

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 131.91  E-value: 1.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 352 PPVQWTDIAGQVSVKATIEEELVWPILRPGAYTGASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWK 431
Cdd:cd19521    2 PNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSKWM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 432 AEAEKILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVATSSeQNVVVIGTTSRPGSMDEAS 511
Cdd:cd19521   82 GESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDS-QGVLVLGATNIPWQLDSAI 160

                        170
                 ....*....|
gi 729737493 512 HRRFAKRFYI 521
Cdd:cd19521  161 RRRFEKRIYI 170
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 358-521 7.24e-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: 127.02  E-value: 7.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRPGAYTGASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKI 437
Cdd:cd19522    1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 438 LQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAG-NLKSQLLSYLDNVATSSEQN-----VVVIGTTSRPGSMDEAS 511
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGTSEEHEASrRVKSELLVQMDGVGGASENDdpskmVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|
gi 729737493 512 HRRFAKRFYI 521
Cdd:cd19522  161 RRRLEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 358-521 3.27e-33

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: 124.84  E-value: 3.27e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRPGAYTGAS--RPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAE 435
Cdd:cd19520    1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 436 KILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVATSSEQNVVVIGTTSRPGSMDEASHRRF 515
Cdd:cd19520   81 KLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDGNCRVIVMGATNRPQDLDEAILRRM 160


                 ....*.
gi 729737493 516 AKRFYI 521
Cdd:cd19520  161 PKRFHI 166
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 318-602 1.90e-29

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: 123.86  E-value: 1.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  318 PKAPV----FGSPPVEEQPknvdplVLELVNTKIvergPPVQWTDIAGQVSVKATIEEELVWPILRPGAYTGAS-RPPRT 392
Cdd:TIGR01243 145 PAGFVyvteATEVEIREKP------VREEIERKV----PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGiEPPKG 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  393 ILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQ 472
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEV 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  473 AGNLKSQLLSYLDNVATSSEqnVVVIGTTSRPGSMDEASHR--RFAKRFYISPPDSIARRQILHhaLAQQNSCLSE-REM 549
Cdd:TIGR01243 295 EKRVVAQLLTLMDGLKGRGR--VIVIGATNRPDALDPALRRpgRFDREIVIRVPDKRARKEILK--VHTRNMPLAEdVDL 370

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737493  550 ASLVQHTESFSGSELVQLCQHAGATTLHAL--PGQIQP--------------TSYQDFEKAFCKVRPAA 602
Cdd:TIGR01243 371 DKLAEVTHGFVGADLAALAKEAAMAALRRFirEGKINFeaeeipaevlkelkVTMKDFMEALKMVEPSA 439
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 365-521 3.05e-29

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: 113.53  E-value: 3.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 365 VKATIEEELVWPILRPGAYT-GASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFF 443
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKrLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 444 VASCRQPAVVLITEAESLLVARAGEDGSQAGN-LKSQLLSYLDNVatSSEQNVVVIGTTSRPGSMDEASHR--RFAKRFY 520
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDSSGVTDrVVSQLLTELDGI--ESLKGVVVIAATNRPDMIDPALLRpgRLDKLIY 158


                 .
gi 729737493 521 I 521
Cdd:cd19511  159 V 159
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 393-522 1.51e-28

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: 110.38  E-value: 1.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  393 ILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQ 472
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 729737493  473 AGNLKSQLLSYLDNVaTSSEQNVVVIGTTSRPGSMDEASHRRFAKRFYIS 522
Cdd:pfam00004  81 SRRVVNQLLTELDGF-TSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFP 129
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 358-521 4.48e-28

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: 110.46  E-value: 4.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRPGAYT--GAsRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAE 435
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRalGL-KPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 436 KILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVatSSEQNVVVIGTTSRPGSMDEASHR-- 513
Cdd:cd19503   80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGM--SSRGKVVVIAATNRPDAIDPALRRpg 157


                 ....*...
gi 729737493 514 RFAKRFYI 521
Cdd:cd19503  158 RFDREVEI 165
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 364-521 1.35e-27

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: 108.91  E-value: 1.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 364 SVKATIEEELVWPILRpgayTGASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFF 443
Cdd:cd19481    4 SLREAVEAPRRGSRLR----RYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 444 VASCRQPAVVLITEAESLLVARAGEDGSQAGN-LKSQLLSYLDNVATSSeqNVVVIGTTSRPGSMDEA--SHRRFAKRFY 520
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKRDSSGESGELRrVLNQLLTELDGVNSRS--KVLVIAATNRPDLLDPAllRPGRFDEVIE 157


                 .
gi 729737493 521 I 521
Cdd:cd19481  158 F 158
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 365-521 4.46e-27

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: 107.58  E-value: 4.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 365 VKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFF 443
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGiRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 444 VASCRQPAVVLITEAESLLVARAGEDGSQAGN-LKSQLLSYLDNVATSSEqnVVVIGTTSRPGSMDEASHR--RFAKRFY 520
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTGDSGVTErVVNQLLTELDGLEEMNG--VVVIAATNRPDIIDPALLRagRFDRLIY 158


                 .
gi 729737493 521 I 521
Cdd:cd19529  159 I 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 365-521 3.27e-23

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: 96.43  E-value: 3.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 365 VKATIEEELVWPILRPGAYTG-ASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFF 443
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKfGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 444 VASCRQPAVVLITEAESLLVARAGEDGSQAG---NLKSQLLSYLDNVatSSEQNVVVIGTTSRPGSMDEASHR--RFAKR 518
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGGNIGDAGGaadRVINQILTEMDGM--NTKKNVFIIGATNRPDIIDPAILRpgRLDQL 158


                 ...
gi 729737493 519 FYI 521
Cdd:cd19528  159 IYI 161
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
389-571 6.97e-23

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 98.03  E-value: 6.97e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 389 PPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVAScRQPAVVLITEAESLLVARAGE 468
Cdd:COG1223   34 PPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFAR-RAPCVIFFDEFDAIAKDRGDQ 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 469 DGSqaGNLK---SQLLSYLDNVAtsseQNVVVIGTTSRPGSMDEASHRRFAKRFYISPPDSIARRQILhHALAQQNSCLS 545
Cdd:COG1223  113 NDV--GEVKrvvNALLQELDGLP----SGSVVIAATNHPELLDSALWRRFDEVIEFPLPDKEERKEIL-ELNLKKFPLPF 185

                        170       180
                 ....*....|....*....|....*.
gi 729737493 546 EREMASLVQHTESFSGSELVQLCQHA 571
Cdd:COG1223  186 ELDLKKLAKKLEGLSGADIEKVLKTA 211
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 358-519 2.59e-22

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: 94.04  E-value: 2.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEK 436
Cdd:cd19519    1 DIGGCRKQLAQIREMVELPLRHPELFKAIGiKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESES 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 437 ILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVATSSeqNVVVIGTTSRPGSMDEAShRRFA 516
Cdd:cd19519   81 NLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRA--HVIVMAATNRPNSIDPAL-RRFG 157


                 ...
gi 729737493 517 kRF 519
Cdd:cd19519  158 -RF 159
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 358-519 5.53e-22

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: 93.24  E-value: 5.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRP--GAYTGAsRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAE 435
Cdd:cd19518    1 DIGGMDSTLKELCELLIHPILPPeyFQHLGV-EPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 436 KILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVA--TSSEQNVVVIGTTSRPGSMDEASHR 513
Cdd:cd19518   80 EKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNneKTAGGPVLVIGATNRPDSLDPALRR 159


                 ....*.
gi 729737493 514 rfAKRF 519
Cdd:cd19518  160 --AGRF 163
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 365-521 1.32e-21

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: 91.81  E-value: 1.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 365 VKATIEEELVWPILRPGAYTGASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFV 444
Cdd:cd19527    1 VKKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 445 ASCRQPAVVLITEAESLLVAR--AGEDGSQAGNLKSQLLSYLDNVATSSeQNVVVIGTTSRPGSMDEASHR--RFAKRFY 520
Cdd:cd19527   81 ARDAKPCVIFFDELDSLAPSRgnSGDSGGVMDRVVSQLLAELDGMSSSG-QDVFVIGATNRPDLLDPALLRpgRFDKLLY 159


                 .
gi 729737493 521 I 521
Cdd:cd19527  160 L 160
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 334-598 3.59e-20

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 93.68  E-value: 3.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 334 NVDPLVlelvNTKIVERGPPVQWTDIAGQVSVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSRCIST 412
Cdd:PTZ00361 164 EVDPLV----SVMKVDKAPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDIGiKPPKGVILYGPPGTGKTLLAKAVAN 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 413 QLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITEAESLLVAR-----AGEDGSQAGNLksQLLSYLDNV 487
Cdd:PTZ00361 240 ETSATFLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRydatsGGEKEIQRTML--ELLNQLDGF 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 488 atSSEQNVVVIGTTSRPGSMDEASHR--RFAKRFYISPPDSIARRQILHHALAQQNscLSER-EMASLVQHTESFSGSEL 564
Cdd:PTZ00361 318 --DSRGDVKVIMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSKMT--LAEDvDLEEFIMAKDELSGADI 393

                        250       260       270
                 ....*....|....*....|....*....|....
gi 729737493 565 VQLCQHAGattLHALPGQIQPTSYQDFEKAFCKV 598
Cdd:PTZ00361 394 KAICTEAG---LLALRERRMKVTQADFRKAKEKV 424
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 328-618 4.71e-20

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 92.59  E-value: 4.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 328 VEEQPKNVDPLVLELvntKIVERgPPVQWTDIAGqvsVKATIEE-----ELvwPILRPGAYT--GASrPPRTILLFGPHG 400
Cdd:PRK03992 106 VEVLPSEKDPRVQAM---EVIES-PNVTYEDIGG---LEEQIREvreavEL--PLKKPELFEevGIE-PPKGVLLYGPPG 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 401 TGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITEAESlLVARAGEDGSqagnlkS-- 478
Cdd:PRK03992 176 TGKTLLAKAVAHETNATFIRVVGSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDA-IAAKRTDSGT------Sgd 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 479 --------QLLSYLDNVatSSEQNVVVIGTTSRPGSMDEASHR--RFAKRFYISPPDSIARRQILH-HAlaqqnsclseR 547
Cdd:PRK03992 249 revqrtlmQLLAEMDGF--DPRGNVKIIAATNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKiHT----------R 316

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737493 548 EM--------ASLVQHTESFSGSELVQLCQHAGATTLHALPGQIqptSYQDFEKAFCKVRpaaSQKELDLFLEWDKMYG 618
Cdd:PRK03992 317 KMnladdvdlEELAELTEGASGADLKAICTEAGMFAIRDDRTEV---TMEDFLKAIEKVM---GKEEKDSMEEPGVMFA 389
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 369-521 1.26e-19

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: 86.00  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 369 IEEELVWPILRPGAYTGASRP-----PRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFF 443
Cdd:cd19530    4 VREELTMSILRPIKRPDIYKAlgidlPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQVFQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 444 VASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVatSSEQNVVVIGTTSRPGSMDEASHR--RFAKRFYI 521
Cdd:cd19530   84 RARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGL--EERSNVFVIAATNRPDIIDPAMLRpgRLDKTLYV 161
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 358-520 1.50e-19

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: 86.41  E-value: 1.50e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLS-----GKTLLSTWK 431
Cdd:cd19517    1 DIGGLSHYINQLKEMVFFPLLYPEVFAKFKiTPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrkGADCLSKWV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 432 AEAEKILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVATSSEqnVVVIGTTSRPGSMDEAS 511
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQ--VVVIGATNRPDALDPAL 158

                        170
                 ....*....|.
gi 729737493 512 HR--RFAKRFY 520
Cdd:cd19517  159 RRpgRFDREFY 169
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 352-598 8.43e-19

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 89.05  E-value: 8.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 352 PPVQWTDIAGQVSVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTW 430
Cdd:PTZ00454 140 PDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGiDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEFVQKY 219

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 431 KAEAEKILQTVFFVASCRQPAVVLITEAESLLV----ARAGEDgSQAGNLKSQLLSYLDNVATSSeqNVVVIGTTSRPGS 506
Cdd:PTZ00454 220 LGEGPRMVRDVFRLARENAPSIIFIDEVDSIATkrfdAQTGAD-REVQRILLELLNQMDGFDQTT--NVKVIMATNRADT 296

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 507 MDEASHR--RFAKRFYISPPDSIARRQILHHALAQQNscLSER-EMASLVQHTESFSGSELVQLCQHAGattLHALPGQI 583
Cdd:PTZ00454 297 LDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSKMN--LSEEvDLEDFVSRPEKISAADIAAICQEAG---MQAVRKNR 371

                        250
                 ....*....|....*
gi 729737493 584 QPTSYQDFEKAFCKV 598
Cdd:PTZ00454 372 YVILPKDFEKGYKTV 386
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 354-521 6.76e-17

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: 78.43  E-value: 6.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 354 VQWTDIAGQVSVKATIEEeLVWPILRPGAYT--GAsRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWK 431
Cdd:cd19501    1 VTFKDVAGCEEAKEELKE-VVEFLKNPEKFTklGA-KIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 432 AEAEKILQTVFFVASCRQPAVVLITEAESllVARAGEDGSQAGNLK-----SQLLSYLDNVATSSeqNVVVIGTTSRPGS 506
Cdd:cd19501   79 GVGASRVRDLFEQAKKNAPCIVFIDEIDA--VGRKRGAGLGGGHDEreqtlNQLLVEMDGFESNT--GVIVIAATNRPDV 154

                        170
                 ....*....|....*..
gi 729737493 507 MDEASHR--RFAKRFYI 521
Cdd:cd19501  155 LDPALLRpgRFDRQVYV 171
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 356-510 6.96e-16

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: 75.84  E-value: 6.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 356 WTDIAGQVSVKATIEEELVWPILRPGAYTGAS-RPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEA 434
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGiEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737493 435 EKILQTVFFVASCRQPAVVLITEAESLLVARAGEDGSQAGNLKS---QLLSYLDNVATSSeqNVVVIGTTSRPGSMDEA 510
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDREVQRtmlELLNQLDGFDPRG--NIKVIMATNRPDILDPA 158
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 365-520 2.00e-15

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: 74.00  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 365 VKATIEEELVWPILRPGAYTGASRPPRT-ILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFF 443
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSgILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737493 444 VASCRQPAVVLITEAESLLVARAGEDGSQAGNLKSQLLSYLDNVatSSEQNVVVIGTTSRPGSMDEASHR--RFAKRFY 520
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGV--EGLDGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
356-607 3.33e-15

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 78.92  E-value: 3.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 356 WTDIAGQVSVKATIEEeLVWPILRPGAYTG-ASRPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEA 434
Cdd:PRK10733 151 FADVAGCDEAKEEVAE-LVEYLREPSRFQKlGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVG 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 435 EKILQTVFFVASCRQPAVVLITEAESLLVAR-AGEDGSQAGNLKS--QLLSYLDNVatSSEQNVVVIGTTSRPGSMDEAS 511
Cdd:PRK10733 230 ASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRgAGLGGGHDEREQTlnQMLVEMDGF--EGNEGIIVIAATNRPDVLDPAL 307

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 512 HR--RFAKRFYISPPDSIARRQILHHALaQQNSCLSEREMASLVQHTESFSGSELVQLCQHAGattLHALPGQIQPTSYQ 589
Cdd:PRK10733 308 LRpgRFDRQVVVGLPDVRGREQILKVHM-RRVPLAPDIDAAIIARGTPGFSGADLANLVNEAA---LFAARGNKRVVSMV 383

                        250
                 ....*....|....*...
gi 729737493 590 DFEKAFCKVRPAASQKEL 607
Cdd:PRK10733 384 EFEKAKDKIMMGAERRSM 401
ftsH CHL00176
cell division protein; Validated
 358-567 3.95e-14

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 75.47  E-value: 3.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 358 DIAGQVSVKATIEEeLVWPILRPGAYT--GASrPPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAE 435
Cdd:CHL00176 184 DIAGIEEAKEEFEE-VVSFLKKPERFTavGAK-IPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGA 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 436 KILQTVFFVASCRQPAVVLITEAESllVARAGEDGSQAGNLKS-----QLLSYLDNVatSSEQNVVVIGTTSRPGSMDEA 510
Cdd:CHL00176 262 ARVRDLFKKAKENSPCIVFIDEIDA--VGRQRGAGIGGGNDEReqtlnQLLTEMDGF--KGNKGVIVIAATNRVDILDAA 337

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 729737493 511 SHR--RFAKRFYISPPDSIARRQILH-HAlaqQNSCLSE---REMasLVQHTESFSGSELVQL 567
Cdd:CHL00176 338 LLRpgRFDRQITVSLPDREGRLDILKvHA---RNKKLSPdvsLEL--IARRTPGFSGADLANL 395
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 387-523 3.67e-12

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: 64.47  E-value: 3.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 387 SRPPRTILLFGPHGTGKTLLSRCISTQL---GSTLLKLSGKTLLSTWKAEAEK---ILQTVFFVASCRQPAVVLITEAES 460
Cdd:cd00009   16 LPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEIDS 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 729737493 461 LlvaragedgsqAGNLKSQLLSYLD--NVATSSEQNVVVIGTTSRP--GSMDEASHRRFAKRFYISP 523
Cdd:cd00009   96 L-----------SRGAQNALLRVLEtlNDLRIDRENVRVIGATNRPllGDLDRALYDRLDIRIVIPL 151
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 365-519 4.77e-12

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: 64.47  E-value: 4.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 365 VKATIEEELVWPIlrpGAYTGASRPP--RTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTW--KAEAEKILQT 440
Cdd:cd19506    2 VRQLLTLYGILPL---GSQAVHEKAPlvKSLLLAGPSGVGKKMLVHAICTETGANLFNLSPSNIAGKYpgKNGLQMMLHL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 441 VFFVASCRQPAVVLITEAESLLVARA--GEDGSQAGNLKSQLLSYLDNVAtsSEQNVVVIGTTSRPGSMDEASHRRFAKR 518
Cdd:cd19506   79 VLKVARQLQPSVIWIGDAEKTFYKKVpkTEKQLDPKRLKKDLPKILKSLK--PEDRVLIVGTTSRPFEADLKSFCKVYNK 156


                 .
gi 729737493 519 F 519
Cdd:cd19506  157 I 157
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 391-513 5.56e-12

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: 64.43  E-value: 5.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 391 RTILLFGPHGTGKTLLSRCISTQLGSTLLKL-SGKTLLSTWKAEAEKILQTVFFVASCRQPA--------VVLITEAESL 461
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIvNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAI 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 729737493 462 LVAR-AGEDGSQAG-NLKSQLLSYLDNVatSSEQNVVVIGTTSRPGSMDEASHR 513
Cdd:cd19504  116 CKQRgSMAGSTGVHdTVVNQLLSKIDGV--EQLNNILVIGMTNRKDLIDEALLR 167
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 391-521 7.89e-10

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: 59.00  E-value: 7.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 391 RTILLFGPHGTGKTLLS---------RCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFF----VASCRQPAV-VLIT 456
Cdd:cd19508   53 RLVLLHGPPGTGKTSLCkalaqklsiRLSSRYRYGQLIEINSHSLFSKWFSESGKLVTKMFQkiqeLIDDKDALVfVLID 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 729737493 457 EAESLLVAR----AGEDGSQAGNLKSQLLSYLDNVATSseQNVVVIGTTSRPGSMDEASHRRFAKRFYI 521
Cdd:cd19508  133 EVESLAAARsassSGTEPSDAIRVVNAVLTQIDRIKRY--HNNVILLTSNLLEKIDVAFVDRADIKQYI 199
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 375-521 1.92e-08

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: 53.91  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 375 WPILRPGAYTGASR-----PPRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQ 449
Cdd:cd19507   11 WLKKRKAAFSKQASayglpTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESESRLRQMIQTAEAIA 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 729737493 450 PAVVLITEAESLL-VARAGEDGSQAGNLKSQLLSYLdnvatsSEQN--VVVIGTTSRPGSMDEASHR--RFAKRFYI 521
Cdd:cd19507   91 PCVLWIDEIEKGFsNADSKGDSGTSSRVLGTFLTWL------QEKKkpVFVVATANNVQSLPPELLRkgRFDEIFFV 161
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 389-525 2.26e-06

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: 47.75  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493   389 PPRTILLFGPHGTGKTLLSRCISTQLGSTLLK---LSGKTLLSTWKAEAEKILQTVFFVASCR--------------QPA 451
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGviyIDGEDILEEVLDQLLLIIVGGKKASGSGelrlrlalalarklKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 729737493   452 VVLITEAESLLvaragedGSQAGNLKSQLLSYLDNVATSSEQNVVVIGTTSRPG-SMDEASHRRFAKRFYISPPD 525
Cdd:smart00382  81 VLILDEITSLL-------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKdLGPALLRRRFDRRIVLLLIL 148
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 371-515 2.78e-06

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 47.52  E-value: 2.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 371 EELVWPILRPGAYTGASRPP-RTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQ 449
Cdd:cd19512    2 EARVRDIAIATRNTKKNKGLyRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSRR 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 729737493 450 PAVVLITEAESLLVARAGEDGSQAgnLKSQLLSYLDNVATSSEQNVVVIGtTSRPGSMDEASHRRF 515
Cdd:cd19512   82 GLLLFVDEADAFLRKRSTEKISED--LRAALNAFLYRTGEQSNKFMLVLA-SNQPEQFDWAINDRI 144
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
347-536 9.05e-06

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 48.49  E-value: 9.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 347 IVERGPPVQWTDIAGQVSVKATIEEelvwpI---LR-PGAYT--GAsRPPRTILLFGPHGTGKTLLSR-----------C 409
Cdd:COG0465  132 YDEDKPKVTFDDVAGVDEAKEELQE-----IvdfLKdPEKFTrlGA-KIPKGVLLVGPPGTGKTLLAKavageagvpffS 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 410 IStqlGSTllklsgktllstwkaeaekilqtvF---FV---AScR------Q-----PAVVLITE--AesllVAR---AG 467
Cdd:COG0465  206 IS---GSD------------------------FvemFVgvgAS-RvrdlfeQakknaPCIIFIDEidA----VGRqrgAG 253

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 729737493 468 EDGS-----QAGNlksQLLSYLDNVATSSeqNVVVIGTTSRPGSMDEASHR--RFAKRFYISPPDSIARRQILH-HA 536
Cdd:COG0465  254 LGGGhdereQTLN---QLLVEMDGFEGNE--GVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKvHA 325
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 391-508 3.17e-05

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: 44.26  E-value: 3.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 391 RTILLFGPHGTGKTLLSRCISTQLGST--LLKLSGKTLLSTWKaeaEKILQTVffvascRQPAVVLITEAESLLVAR--A 466
Cdd:cd19510   24 RGYLLYGPPGTGKSSFIAALAGELDYDicDLNLSEVVLTDDRL---NHLLNTA------PKQSIILLEDIDAAFESRehN 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 729737493 467 GEDGSQAGNLK----SQLLSYLDNVATSSEQnvVVIGTTS----------RPGSMD 508
Cdd:cd19510   95 KKNPSAYGGLSrvtfSGLLNALDGVASSEER--IVFMTTNhierldpaliRPGRVD 148
PHA03247 PHA03247
large tegument protein UL36; Provisional
 102-343 2.26e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.54  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  102 PVAHGSDGAYPLTPIHDGLPGAkgvVPPAVPPSGGAIGLGGSPVVSANLADPMYPGNSCGGAAAGSGGLGSSQEYPSGYG 181
Cdd:PHA03247 2748 PATPGGPARPARPPTTAGPPAP---APPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASP 2824

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  182 GTYLPsgyctqpaaalpPPHPPALHGSGLLQPPHPSPALVPGYGSSGAMYNYAAGSYPPQPGYGTihPPHPSASYLPSGI 261
Cdd:PHA03247 2825 AGPLP------------PPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAAKPAA--PARPPVRRLARPA 2890

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  262 AAPTSGGQPMKSMVSPPYGAGDAPLRPAEPFEKFSPPLangEQAAEPGPPFPlrLPPKAPVFGSPPV-EEQPKNVDPLVL 340
Cdd:PHA03247 2891 VSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQ---PQPPPPPPPRP--QPPLAPTTDPAGAgEPSGAVPQPWLG 2965


                  ...
gi 729737493  341 ELV 343
Cdd:PHA03247 2966 ALV 2968
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 585-618 1.15e-03

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: 37.48  E-value: 1.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 729737493  585 PTSYQDFEKAFCKVRPAASQKELDLFLEWDKMYG 618
Cdd:pfam09336  28 PVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
ycf46 CHL00195
Ycf46; Provisional
 390-566 1.18e-03

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 41.93  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 390 PRTILLFGPHGTGKTLLSRCISTQLGSTLLKLSGKTLLSTWKAEAEKILQTVFFVASCRQPAVVLITE---AESLLVARA 466
Cdd:CHL00195 259 PRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEidkAFSNSESKG 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 467 geDGSQAGNLKSQLLSYLdnvatsSEQN--VVVIGTTSRPGSMDEASHR--RFAKRFYISPPDSIARRQI--LHHALAQQ 540
Cdd:CHL00195 339 --DSGTTNRVLATFITWL------SEKKspVFVVATANNIDLLPLEILRkgRFDEIFFLDLPSLEEREKIfkIHLQKFRP 410

                        170       180
                 ....*....|....*....|....*.
gi 729737493 541 NScLSEREMASLVQHTESFSGSELVQ 566
Cdd:CHL00195 411 KS-WKKYDIKKLSKLSNKFSGAEIEQ 435
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 390-498 1.34e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 39.79  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  390 PRTILLFGPHGTGKTLLSRCISTQL-GSTLLKLSGKTLLSTWKAE-AEKILQTVFFVASCRQPAVVLITEAESLLVARAG 467
Cdd:pfam13191  24 PPSVLLTGEAGTGKTTLLRELLRALeRDGGYFLRGKCDENLPYSPlLEALTREGLLRQLLDELESSLLEAWRAALLEALA 103

                          90       100       110
                  ....*....|....*....|....*....|....
gi 729737493  468 EDGSQAGNLKSQLLSYLDNV---ATSSEQNVVVI 498
Cdd:pfam13191 104 PVPELPGDLAERLLDLLLRLldlLARGERPLVLV 137
PHA03247 PHA03247
large tegument protein UL36; Provisional
 74-382 1.34e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 42.23  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493   74 PYERPALSGYGDGAFGPVNGQKGDGEPWPVAHGSDGAYPLTPIHDGLPGAKGVVPPAVPPSGGAIGLGGSPvvsANLADP 153
Cdd:PHA03247 2663 RPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASP---ALPAAP 2739

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  154 MYPGNSCGGAAAGSGGLGSSQEYPSGYGGTYLPSGYCT--QPAAALPPPHPPALHGSGLLQPPHPSPALVPGYGSSGAMY 231
Cdd:PHA03247 2740 APPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAgpPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALP 2819

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493  232 NYAAgsypPQPGYGTIHPPHPSASYLPSGIAAPTsggQPMKSMVSPpygAGDAPLRP------AEPFEKFSPPLANGEQA 305
Cdd:PHA03247 2820 PAAS----PAGPLPPPTSAQPTAPPPPPGPPPPS---LPLGGSVAP---GGDVRRRPpsrspaAKPAAPARPPVRRLARP 2889

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 729737493  306 AEPGPPFPLRLPPKAPVFGSPPVEEQPKNVDPLVLELVNTKIVERGPPVQWTDIAGQVSVKATIEEELVWPILRPGA 382
Cdd:PHA03247 2890 AVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGA 2966
PHA03378 PHA03378
EBNA-3B; Provisional
 212-333 6.78e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 39.67  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 729737493 212 QPPHPSPALVPGYGSSGAMYNY------AAGSYPPQPGYGTIHPPHPSASYLPSGIAAPTSGGQPMKSM--VSPPYGAGD 283
Cdd:PHA03378 653 QPPQVEITPYKPTWTQIGHIPYqpsptgANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATgrARPPAAAPG 732

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 729737493 284 APLRPAEPFEKFSPPlANGEQAAEPGPPFPLRLPPKAPVFGSPPVEEQPK 333
Cdd:PHA03378 733 RARPPAAAPGRARPP-AAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQ 781
 
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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