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Conserved domains on  [gi|164658097|ref|XP_001730174|]
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hypothetical protein MGL_2556 [Malassezia globosa CBS 7966]

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 ...
257-433 2.14e-116

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 cd19504:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 177  Bit Score: 348.71  E-value: 2.14e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 257 GIGGLDTEFSAIFRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVNGPEILSKYVGAS 336
Cdd:cd19504    1 GIGGLDKEFSDIFRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGPEILNKYVGES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 337 EENIRKLFAEAEAEFRSKGDESGLHIIIFDELDAICRQRGTTGGGTGVGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDM 416
Cdd:cd19504   81 EANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160
                        170
                 ....*....|....*..
gi 164658097 417 IDEALLRPGRLEVHMEI 433
Cdd:cd19504  161 IDEALLRPGRLEVQMEI 177
CDC48 super family cl36852
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
249-689 2.26e-60

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


The actual alignment was detected with superfamily member TIGR01243:

Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 217.47  E-value: 2.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  249 PNFKFEDmgIGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREpKVVNGPEI 328
Cdd:TIGR01243 173 PKVTYED--IGGLKEAKEKI-REMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYF-ISINGPEI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  329 LSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGGGTGVgdSVVNQLLSKMDGVDQLNNILII 408
Cdd:TIGR01243 249 MSKYYGESEERLREIFKEAE--------ENAPSIIFIDEIDAIAPKREEVTGEVEK--RVVAQLLTLMDGLKGRGRVIVI 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  409 GMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMrtngVMDGDVNLQELAALTKNFSGAEIAGLVKSATS 488
Cdd:TIGR01243 319 GATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNM----PLAEDVDLDKLAEVTHGFVGADLAALAKEAAM 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  489 FAFNRHVKVGTMAGISDDV-----EGMRVNREDFLCALDEVKPA------FGVAE---------EELQQVVRNGIMHFAP 548
Cdd:TIGR01243 395 AALRRFIREGKINFEAEEIpaevlKELKVTMKDFMEALKMVEPSairevlVEVPNvrwsdigglEEVKQELREAVEWPLK 474
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  549 HIDTILRDGqlrveqVRTSErtslvTALLHGPPGSGKTALAATIAMASDFPFIKLVAPE---NMVGMNEQGkiayLNKVF 625
Cdd:TIGR01243 475 HPEIFEKMG------IRPPK-----GVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEilsKWVGESEKA----IREIF 539
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  626 NDSYKSPLSIVVVDNLEKIiewVPI-GPRFSNPVL-----QTLAVLLGKQPPKDrrLFVLATTSNKAMLN 689
Cdd:TIGR01243 540 RKARQAAPAIIFFDEIDAI---APArGARFDTSVTdrivnQLLTEMDGIQELSN--VVVIAATNRPDILD 604
CDC48_2 super family cl08380
Cell division protein 48 (CDC48), domain 2; This domain has a double psi-beta barrel fold and ...
161-202 2.28e-04

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


The actual alignment was detected with superfamily member pfam02933:

Pssm-ID: 447617  Cd Length: 64  Bit Score: 39.91  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 164658097  161 PFSADEMQgIFTRVFDSHVLSNGQVLVFEFHGQNLKATVRGV 202
Cdd:pfam02933   1 RFDGDELA-YVKRNLEGRPVSKGDTIVVEFLGGAIPLVVVST 41
CDC48_N super family cl21693
Cell division protein 48 (CDC48), N-terminal domain; This domain has a double psi-beta barrel ...
55-132 7.76e-04

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


The actual alignment was detected with superfamily member pfam02359:

Pssm-ID: 451359  Cd Length: 85  Bit Score: 39.10  E-value: 7.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097   55 MFRIVKSPPTLNTTNCVILNPS---EWGNTR--YVLVSGRFAFTAI--PDNTHTIAPGTIGTALLQRQWARLSaEGHDVA 127
Cdd:pfam02359   1 RLRVAEAPDRDVGRGIARLNPEdmeELGLFPgdVVEIKGKRKTVAIvwSAYPEDEGPGIIRMDGVTRKNAGVS-IGDTVT 79

                  ....*
gi 164658097  128 VEAFE 132
Cdd:pfam02359  80 VRPAE 84
 
Name Accession Description Interval E-value
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
257-433 2.14e-116

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: 348.71  E-value: 2.14e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 257 GIGGLDTEFSAIFRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVNGPEILSKYVGAS 336
Cdd:cd19504    1 GIGGLDKEFSDIFRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGPEILNKYVGES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 337 EENIRKLFAEAEAEFRSKGDESGLHIIIFDELDAICRQRGTTGGGTGVGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDM 416
Cdd:cd19504   81 EANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160
                        170
                 ....*....|....*..
gi 164658097 417 IDEALLRPGRLEVHMEI 433
Cdd:cd19504  161 IDEALLRPGRLEVQMEI 177
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
226-526 7.35e-75

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 246.07  E-value: 7.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 226 VAQGSALEIKASGKRARPNAILQPNFKFEDmgIGGLDTEFSAIfRRAFasrIFP---PDLVEKLGIQHVKGLLLYGPPGT 302
Cdd:COG1222   50 LNDANLTQKRLGTPRGTAVPAESPDVTFDD--IGGLDEQIEEI-REAV---ELPlknPELFRKYGIEPPKGVLLYGPPGT 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 303 GKTLMARQIGKMLNA---RepkvVNGPEILSKYVGASEENIRKLFAEAEAEFRSkgdesglhIIIFDELDAICRQRGTTG 379
Cdd:COG1222  124 GKTLLAKAVAGELGApfiR----VRGSELVSKYIGEGARNVREVFELAREKAPS--------IIFIDEIDAIAARRTDDG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 380 GGTGVgDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMRTngvmD 459
Cdd:COG1222  192 TSGEV-QRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPL----A 266
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164658097 460 GDVNLQELAALTKNFSGAEIAGLVKSATSFAfnrhvkvgtmagISDDVEgmRVNREDFLCALDEVKP 526
Cdd:COG1222  267 DDVDLDKLAKLTEGFSGADLKAIVTEAGMFA------------IREGRD--TVTMEDLEKAIEKVKK 319
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
249-689 2.26e-60

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: 217.47  E-value: 2.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  249 PNFKFEDmgIGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREpKVVNGPEI 328
Cdd:TIGR01243 173 PKVTYED--IGGLKEAKEKI-REMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYF-ISINGPEI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  329 LSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGGGTGVgdSVVNQLLSKMDGVDQLNNILII 408
Cdd:TIGR01243 249 MSKYYGESEERLREIFKEAE--------ENAPSIIFIDEIDAIAPKREEVTGEVEK--RVVAQLLTLMDGLKGRGRVIVI 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  409 GMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMrtngVMDGDVNLQELAALTKNFSGAEIAGLVKSATS 488
Cdd:TIGR01243 319 GATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNM----PLAEDVDLDKLAEVTHGFVGADLAALAKEAAM 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  489 FAFNRHVKVGTMAGISDDV-----EGMRVNREDFLCALDEVKPA------FGVAE---------EELQQVVRNGIMHFAP 548
Cdd:TIGR01243 395 AALRRFIREGKINFEAEEIpaevlKELKVTMKDFMEALKMVEPSairevlVEVPNvrwsdigglEEVKQELREAVEWPLK 474
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  549 HIDTILRDGqlrveqVRTSErtslvTALLHGPPGSGKTALAATIAMASDFPFIKLVAPE---NMVGMNEQGkiayLNKVF 625
Cdd:TIGR01243 475 HPEIFEKMG------IRPPK-----GVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEilsKWVGESEKA----IREIF 539
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  626 NDSYKSPLSIVVVDNLEKIiewVPI-GPRFSNPVL-----QTLAVLLGKQPPKDrrLFVLATTSNKAMLN 689
Cdd:TIGR01243 540 RKARQAAPAIIFFDEIDAI---APArGARFDTSVTdrivnQLLTEMDGIQELSN--VVVIAATNRPDILD 604
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
249-545 1.16e-54

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 193.12  E-value: 1.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 249 PNFKFEDmgIGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVnGPEI 328
Cdd:PRK03992 126 PNVTYED--IGGLEEQIREV-REAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVV-GSEL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 329 LSKYVGASEENIRKLFAEAeaefRSKGDEsglhiIIF-DELDAICRQRGTTGGGTgvgDSVVN----QLLSKMDGVDQLN 403
Cdd:PRK03992 202 VQKFIGEGARLVRELFELA----REKAPS-----IIFiDEIDAIAAKRTDSGTSG---DREVQrtlmQLLAEMDGFDPRG 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 404 NILIIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMRtngvMDGDVNLQELAALTKNFSGAEIAGLV 483
Cdd:PRK03992 270 NVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMN----LADDVDLEELAELTEGASGADLKAIC 345
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164658097 484 KSATSFAfnrhvkvgtmagISDDVEgmRVNREDFLCALDEVKpafgvAEEELQQVVRNGIMH 545
Cdd:PRK03992 346 TEAGMFA------------IRDDRT--EVTMEDFLKAIEKVM-----GKEEKDSMEEPGVMF 388
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
239-527 4.37e-54

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: 199.36  E-value: 4.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  239 KRARPNAILQ-----PNFKFEDmgIGGLDtEFSAIFRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGK 313
Cdd:TIGR01243 433 KMVEPSAIREvlvevPNVRWSD--IGGLE-EVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVAT 509
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  314 MLNAREpKVVNGPEILSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGGGTGVgDSVVNQLL 393
Cdd:TIGR01243 510 ESGANF-IAVRGPEILSKWVGESEKAIREIFRKAR--------QAAPAIIFFDEIDAIAPARGARFDTSVT-DRIVNQLL 579
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  394 SKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMRtngvMDGDVNLQELAALTKN 473
Cdd:TIGR01243 580 TEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMP----LAEDVDLEELAEMTEG 655
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097  474 FSGAEIAGLVKSATSFAFNRHVKVGTM----AGISDDVEGMRVNREDFLCALDEVKPA 527
Cdd:TIGR01243 656 YTGADIEAVCREAAMAALRESIGSPAKekleVGEEEFLKDLKVEMRHFLEALKKVKPS 713
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
294-435 1.51e-37

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: 136.57  E-value: 1.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  294 LLLYGPPGTGKTLMARQIGKMLNArEPKVVNGPEILSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICR 373
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGA-PFIEISGSELVSKYVGESEKRLRELFEAAK--------KLAPCVIFIDEIDALAG 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164658097  374 QRgtTGGGTGVGDSVVNQLLSKMDGVDQL-NNILIIGMTNRLDMIDEALLrpGRLEVHMEINL 435
Cdd:pfam00004  72 SR--GSGGDSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
292-437 4.50e-12

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: 64.32  E-value: 4.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097   292 KGLLLYGPPGTGKTLMARQIGKMLNAREPKVV----------------NGPEILSKYVGASEENIRKLFAEAEAEFRSkg 355
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097   356 desglhIIIFDELDAICRQRGTTGGGTGVGDSVVNQLLSKmdgvdqlNNILIIGMTNRLDMIDEALLRPgRLEVHMEINL 435
Cdd:smart00382  81 ------VLILDEITSLLDAEQEALLLLLEELRLLLLLKSE-------KNLTVILTTNDEKDLGPALLRR-RFDRRIVLLL 146

                   ..
gi 164658097   436 PD 437
Cdd:smart00382 147 IL 148
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
565-704 2.95e-10

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: 59.08  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 565 RTSERTSLVTALLHGPPGSGKTALAATIAMAS---DFPFIKLVAPENMVGMNEQGKIAY--LNKVFNDSYKSPLSIVVVD 639
Cdd:cd00009   12 EALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHflVRLLFELAEKAKPGVLFID 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164658097 640 NLEKiiewvpIGPRFSNPVLQTLAVLLGKQPPKDRRLFVLATTSNKAMLNDMDMANAFLADIRVP 704
Cdd:cd00009   92 EIDS------LSRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
576-693 8.27e-10

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: 57.22  E-value: 8.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPEnMVGMNEQGKIAYLNKVFNDSYKSPLSIVVVDNLEKIiewvpIGPRFS 655
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-LVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL-----AGSRGS 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 164658097  656 NP------VLQTLAVLLGKQPPKDRRLFVLATTsnkamlNDMDM 693
Cdd:pfam00004  76 GGdsesrrVVNQLLTELDGFTSSNSKVIVIAAT------NRPDK 113
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
576-707 1.32e-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: 48.52  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097   576 LLHGPPGSGKTALAATIA--MASDFPFIKLVAPENM--------------VGMNEQGKIAYLNKVFNDSYKSPLSIVVVD 639
Cdd:smart00382   6 LIVGPPGSGKTTLARALAreLGPPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPDVLILD 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097   640 NLEKIiewvpIGPRFSNPVLQTLAVLLGKQPPKDRRLFVLATTSNKAMLNDMDMANAFLADIRVPDIT 707
Cdd:smart00382  86 EITSL-----LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
576-607 7.34e-05

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 45.77  E-value: 7.34e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPE 607
Cdd:COG1222  116 LLYGPPGTGKTLLAKAVAGELGAPFIRVRGSE 147
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
576-607 1.25e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 45.21  E-value: 1.25e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPE 607
Cdd:PRK03992 169 LLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
CDC48_2 pfam02933
Cell division protein 48 (CDC48), domain 2; This domain has a double psi-beta barrel fold and ...
161-202 2.28e-04

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


Pssm-ID: 427063  Cd Length: 64  Bit Score: 39.91  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 164658097  161 PFSADEMQgIFTRVFDSHVLSNGQVLVFEFHGQNLKATVRGV 202
Cdd:pfam02933   1 RFDGDELA-YVKRNLEGRPVSKGDTIVVEFLGGAIPLVVVST 41
CDC48_N pfam02359
Cell division protein 48 (CDC48), N-terminal domain; This domain has a double psi-beta barrel ...
55-132 7.76e-04

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


Pssm-ID: 426738  Cd Length: 85  Bit Score: 39.10  E-value: 7.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097   55 MFRIVKSPPTLNTTNCVILNPS---EWGNTR--YVLVSGRFAFTAI--PDNTHTIAPGTIGTALLQRQWARLSaEGHDVA 127
Cdd:pfam02359   1 RLRVAEAPDRDVGRGIARLNPEdmeELGLFPgdVVEIKGKRKTVAIvwSAYPEDEGPGIIRMDGVTRKNAGVS-IGDTVT 79

                  ....*
gi 164658097  128 VEAFE 132
Cdd:pfam02359  80 VRPAE 84
CDC48_N smart01073
Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel ...
56-120 1.54e-03

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


Pssm-ID: 215012 [Multi-domain]  Cd Length: 82  Bit Score: 37.97  E-value: 1.54e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164658097    56 FRIVKSP-PTLNTTNCVILNPS-----EWGNTRYVLVSG-RFAFTAIPDNTHTIAPGTIGTALLQRQWARLS 120
Cdd:smart01073   1 LRVAEAPsDEDVGRGIARLSPEdmdelGLFPGDYVLITGkRRTVAIVWPAYPEDPGGIIRIDGVQRKNAGVS 72
 
Name Accession Description Interval E-value
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
257-433 2.14e-116

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: 348.71  E-value: 2.14e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 257 GIGGLDTEFSAIFRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVNGPEILSKYVGAS 336
Cdd:cd19504    1 GIGGLDKEFSDIFRRAFASRVFPPEIVEQLGCKHVKGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGPEILNKYVGES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 337 EENIRKLFAEAEAEFRSKGDESGLHIIIFDELDAICRQRGTTGGGTGVGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDM 416
Cdd:cd19504   81 EANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDL 160
                        170
                 ....*....|....*..
gi 164658097 417 IDEALLRPGRLEVHMEI 433
Cdd:cd19504  161 IDEALLRPGRLEVQMEI 177
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
226-526 7.35e-75

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 246.07  E-value: 7.35e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 226 VAQGSALEIKASGKRARPNAILQPNFKFEDmgIGGLDTEFSAIfRRAFasrIFP---PDLVEKLGIQHVKGLLLYGPPGT 302
Cdd:COG1222   50 LNDANLTQKRLGTPRGTAVPAESPDVTFDD--IGGLDEQIEEI-REAV---ELPlknPELFRKYGIEPPKGVLLYGPPGT 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 303 GKTLMARQIGKMLNA---RepkvVNGPEILSKYVGASEENIRKLFAEAEAEFRSkgdesglhIIIFDELDAICRQRGTTG 379
Cdd:COG1222  124 GKTLLAKAVAGELGApfiR----VRGSELVSKYIGEGARNVREVFELAREKAPS--------IIFIDEIDAIAARRTDDG 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 380 GGTGVgDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMRTngvmD 459
Cdd:COG1222  192 TSGEV-QRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPL----A 266
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 164658097 460 GDVNLQELAALTKNFSGAEIAGLVKSATSFAfnrhvkvgtmagISDDVEgmRVNREDFLCALDEVKP 526
Cdd:COG1222  267 DDVDLDKLAKLTEGFSGADLKAIVTEAGMFA------------IREGRD--TVTMEDLEKAIEKVKK 319
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
249-689 2.26e-60

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: 217.47  E-value: 2.26e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  249 PNFKFEDmgIGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREpKVVNGPEI 328
Cdd:TIGR01243 173 PKVTYED--IGGLKEAKEKI-REMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYF-ISINGPEI 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  329 LSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGGGTGVgdSVVNQLLSKMDGVDQLNNILII 408
Cdd:TIGR01243 249 MSKYYGESEERLREIFKEAE--------ENAPSIIFIDEIDAIAPKREEVTGEVEK--RVVAQLLTLMDGLKGRGRVIVI 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  409 GMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMrtngVMDGDVNLQELAALTKNFSGAEIAGLVKSATS 488
Cdd:TIGR01243 319 GATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNM----PLAEDVDLDKLAEVTHGFVGADLAALAKEAAM 394
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  489 FAFNRHVKVGTMAGISDDV-----EGMRVNREDFLCALDEVKPA------FGVAE---------EELQQVVRNGIMHFAP 548
Cdd:TIGR01243 395 AALRRFIREGKINFEAEEIpaevlKELKVTMKDFMEALKMVEPSairevlVEVPNvrwsdigglEEVKQELREAVEWPLK 474
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  549 HIDTILRDGqlrveqVRTSErtslvTALLHGPPGSGKTALAATIAMASDFPFIKLVAPE---NMVGMNEQGkiayLNKVF 625
Cdd:TIGR01243 475 HPEIFEKMG------IRPPK-----GVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEilsKWVGESEKA----IREIF 539
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  626 NDSYKSPLSIVVVDNLEKIiewVPI-GPRFSNPVL-----QTLAVLLGKQPPKDrrLFVLATTSNKAMLN 689
Cdd:TIGR01243 540 RKARQAAPAIIFFDEIDAI---APArGARFDTSVTdrivnQLLTEMDGIQELSN--VVVIAATNRPDILD 604
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
249-545 1.16e-54

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 193.12  E-value: 1.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 249 PNFKFEDmgIGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVnGPEI 328
Cdd:PRK03992 126 PNVTYED--IGGLEEQIREV-REAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVV-GSEL 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 329 LSKYVGASEENIRKLFAEAeaefRSKGDEsglhiIIF-DELDAICRQRGTTGGGTgvgDSVVN----QLLSKMDGVDQLN 403
Cdd:PRK03992 202 VQKFIGEGARLVRELFELA----REKAPS-----IIFiDEIDAIAAKRTDSGTSG---DREVQrtlmQLLAEMDGFDPRG 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 404 NILIIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMRtngvMDGDVNLQELAALTKNFSGAEIAGLV 483
Cdd:PRK03992 270 NVKIIAATNRIDILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMN----LADDVDLEELAELTEGASGADLKAIC 345
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164658097 484 KSATSFAfnrhvkvgtmagISDDVEgmRVNREDFLCALDEVKpafgvAEEELQQVVRNGIMH 545
Cdd:PRK03992 346 TEAGMFA------------IRDDRT--EVTMEDFLKAIEKVM-----GKEEKDSMEEPGVMF 388
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
239-527 4.37e-54

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: 199.36  E-value: 4.37e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  239 KRARPNAILQ-----PNFKFEDmgIGGLDtEFSAIFRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGK 313
Cdd:TIGR01243 433 KMVEPSAIREvlvevPNVRWSD--IGGLE-EVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVAT 509
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  314 MLNAREpKVVNGPEILSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGGGTGVgDSVVNQLL 393
Cdd:TIGR01243 510 ESGANF-IAVRGPEILSKWVGESEKAIREIFRKAR--------QAAPAIIFFDEIDAIAPARGARFDTSVT-DRIVNQLL 579
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  394 SKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMRtngvMDGDVNLQELAALTKN 473
Cdd:TIGR01243 580 TEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMP----LAEDVDLEELAEMTEG 655
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097  474 FSGAEIAGLVKSATSFAFNRHVKVGTM----AGISDDVEGMRVNREDFLCALDEVKPA 527
Cdd:TIGR01243 656 YTGADIEAVCREAAMAALRESIGSPAKekleVGEEEFLKDLKVEMRHFLEALKKVKPS 713
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
258-525 7.80e-51

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: 182.80  E-value: 7.80e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLDTEFSAIFRRAFASRIFPpDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNArePKV-VNGPEILSKYVGAS 336
Cdd:COG0464  159 LGGLEEVKEELRELVALPLKRP-ELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGL--PLIeVDLSDLVSKYVGET 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 337 EENIRKLFAEAEAEFRSkgdesglhIIIFDELDAICRQRgtTGGGTGVGDSVVNQLLSKMDGVDqlNNILIIGMTNRLDM 416
Cdd:COG0464  236 EKNLREVFDKARGLAPC--------VLFIDEADALAGKR--GEVGDGVGRRVVNTLLTEMEELR--SDVVVIAATNRPDL 303
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 417 IDEALLRpgRLEVHMEINLPDENGRLQIINIQTAKMRtngvMDGDVNLQELAALTKNFSGAEIAGLVKSATSFAFnrhvk 496
Cdd:COG0464  304 LDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRP----LDEDVDLEELAEATEGLSGADIRNVVRRAALQAL----- 372
                        250       260
                 ....*....|....*....|....*....
gi 164658097 497 vgtmagisdDVEGMRVNREDFLCALDEVK 525
Cdd:COG0464  373 ---------RLGREPVTTEDLLEALERED 392
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
268-433 1.07e-43

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: 155.13  E-value: 1.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 268 IFRRAFASRIFPPdlVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNArEPKVVNGPEILSKYVGASEENIRKLFAEA 347
Cdd:cd19481    5 LREAVEAPRRGSR--LRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGL-PLIVVKLSSLLSKYVGESEKNLRKIFERA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 348 EaefrskgdESGLHIIIFDELDAICRQRGTTGGGTGVGDsVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRL 427
Cdd:cd19481   82 R--------RLAPCILFIDEIDAIGRKRDSSGESGELRR-VLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRF 152

                 ....*.
gi 164658097 428 EVHMEI 433
Cdd:cd19481  153 DEVIEF 158
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
257-433 1.10e-43

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: 155.14  E-value: 1.10e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 257 GIGGLDTEFsAIFRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREpKVVNGPEILSKYVGAS 336
Cdd:cd19503    1 DIGGLDEQI-ASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANF-LSISGPSIVSKYLGES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 337 EENIRKLFAEAEAEFRSkgdesglhIIIFDELDAICRQRGTTGGGTGVgdSVVNQLLSKMDGVDQLNNILIIGMTNRLDM 416
Cdd:cd19503   79 EKNLREIFEEARSHAPS--------IIFIDEIDALAPKREEDQREVER--RVVAQLLTLMDGMSSRGKVVVIAATNRPDA 148
                        170
                 ....*....|....*..
gi 164658097 417 IDEALLRPGRLEVHMEI 433
Cdd:cd19503  149 IDPALRRPGRFDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
280-428 2.38e-42

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: 151.28  E-value: 2.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 280 PDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYVGASEENIRKLFAEAEAEFRSkg 355
Cdd:cd19511   16 PDAFKRLGIRPPKGVLLYGPPGCGKTLLAKAL-----ASEAGLnfisVKGPELFSKYVGESERAVREIFQKARQAAPC-- 88
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164658097 356 desglhIIIFDELDAICRQRGTTGGGTGVgDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLE 428
Cdd:cd19511   89 ------IIFFDEIDSLAPRRGQSDSSGVT-DRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLD 154
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
249-444 6.44e-42

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


Pssm-ID: 200312 [Multi-domain]  Cd Length: 512  Bit Score: 160.26  E-value: 6.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  249 PNFKFEDmgIGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKV------ 322
Cdd:TIGR03689 177 PDVTYAD--IGGLGSQIEQI-RDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARIGAEgggksy 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  323 ---VNGPEILSKYVGASEENIRKLFAEAeaefRSKGDESGLHIIIFDELDAICRQRGTTGGGTGVGdSVVNQLLSKMDGV 399
Cdd:TIGR03689 254 flnIKGPELLNKYVGETERQIRLIFQRA----REKASEGRPVIVFFDEMDSLFRTRGSGVSSDVET-TVVPQLLAEIDGV 328
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 164658097  400 DQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQI 444
Cdd:TIGR03689 329 ESLDNVIVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADI 373
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
280-433 1.35e-40

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: 146.49  E-value: 1.35e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 280 PDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVvNGPEILSKYVGASEENIRKLFAEAEaefrskgdESG 359
Cdd:cd19529   16 PEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISV-KGPELLSKWVGESEKAIREIFRKAR--------QVA 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164658097 360 LHIIIFDELDAICRQRGTTGGGTGVgDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEI 433
Cdd:cd19529   87 PCVIFFDEIDSIAPRRGTTGDSGVT-ERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIYI 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
279-428 3.61e-39

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: 142.26  E-value: 3.61e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 279 PPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYVGASEENIRKLFAEAEAefrsk 354
Cdd:cd19528   15 HPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAI-----ANECQAnfisVKGPELLTMWFGESEANVRDIFDKARA----- 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164658097 355 gdeSGLHIIIFDELDAICRQRGTTGGGTG-VGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLE 428
Cdd:cd19528   85 ---AAPCVLFFDELDSIAKARGGNIGDAGgAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLD 156
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
227-508 1.18e-38

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 150.51  E-value: 1.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  227 AQGSALEIKASGK-RARPNAILQPNFKFEDMGigGLD------TEFSAIFRRafasrifpPDLVEKLGIQHVKGLLLYGP 299
Cdd:TIGR01241  27 MQGGGGRAFSFGKsKAKLLNEEKPKVTFKDVA--GIDeakeelMEIVDFLKN--------PSKFTKLGAKIPKGVLLVGP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  300 PGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYVGASEENIRKLFAEAEAEFRSkgdesglhIIIFDELDAICRQR 375
Cdd:TIGR01241  97 PGTGKTLLAKAV-----AGEAGVpffsISGSDFVEMFVGVGASRVRDLFEQAKKNAPC--------IIFIDEIDAVGRQR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  376 GTTGGGTG-VGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMRt 454
Cdd:TIGR01241 164 GAGLGGGNdEREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPALLRPGRFDRQVVVDLPDIKGREEILKVHAKNKK- 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 164658097  455 ngvMDGDVNLQELAALTKNFSGAEIAGLVKSATSFAFNRHVKVGTMAGISDDVE 508
Cdd:TIGR01241 243 ---LAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKNKTEITMNDIEEAID 293
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
258-433 1.34e-37

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: 137.95  E-value: 1.34e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREpKVVNGPEILSKYVGASE 337
Cdd:cd19519    2 IGGCRKQLAQI-REMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFF-FLINGPEIMSKLAGESE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 338 ENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGGGTGVgdSVVNQLLSKMDGVDQLNNILIIGMTNRLDMI 417
Cdd:cd19519   80 SNLRKAFEEAE--------KNAPAIIFIDEIDAIAPKREKTHGEVER--RIVSQLLTLMDGLKQRAHVIVMAATNRPNSI 149
                        170
                 ....*....|....*.
gi 164658097 418 DEALLRPGRLEVHMEI 433
Cdd:cd19519  150 DPALRRFGRFDREIDI 165
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
281-525 1.39e-37

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 140.79  E-value: 1.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 281 DLVEKLGIQHVKGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYVGASEENIRKLFAEAEaefRSKGd 356
Cdd:COG1223   25 ENLRKFGLWPPRKILFYGPPGTGKTMLAEAL-----AGELKLplltVRLDSLIGSYLGETARNLRKLFDFAR---RAPC- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 357 esglhIIIFDELDAICRQRgttgggtgvGDS--------VVNQLLSKMDGVDqlNNILIIGMTNRLDMIDEALLRpgRLE 428
Cdd:COG1223   96 -----VIFFDEFDAIAKDR---------GDQndvgevkrVVNALLQELDGLP--SGSVVIAATNHPELLDSALWR--RFD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 429 VHMEINLPDENGRLQIINIQTAKMRtngvMDGDVNLQELAALTKNFSGAEIAGLVKSATSFAfnrhvkvgtmagISDDVE 508
Cdd:COG1223  158 EVIEFPLPDKEERKEILELNLKKFP----LPFELDLKKLAKKLEGLSGADIEKVLKTALKKA------------ILEDRE 221
                        250
                 ....*....|....*..
gi 164658097 509 gmRVNREDFLCALDEVK 525
Cdd:COG1223  222 --KVTKEDLEEALKQRK 236
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
294-435 1.51e-37

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: 136.57  E-value: 1.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  294 LLLYGPPGTGKTLMARQIGKMLNArEPKVVNGPEILSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICR 373
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGA-PFIEISGSELVSKYVGESEKRLRELFEAAK--------KLAPCVIFIDEIDALAG 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164658097  374 QRgtTGGGTGVGDSVVNQLLSKMDGVDQL-NNILIIGMTNRLDMIDEALLrpGRLEVHMEINL 435
Cdd:pfam00004  72 SR--GSGGDSESRRVVNQLLTELDGFTSSnSKVIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
258-433 7.88e-37

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: 135.93  E-value: 7.88e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVnGPEILSKYVGASE 337
Cdd:cd19502    5 IGGLDEQIREI-REVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVV-GSELVQKYIGEGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 338 ENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGGGTgvgDSVVN----QLLSKMDGVDQLNNILIIGMTNR 413
Cdd:cd19502   83 RLVRELFEMAR--------EKAPSIIFIDEIDAIGAKRFDSGTGG---DREVQrtmlELLNQLDGFDPRGNIKVIMATNR 151
                        170       180
                 ....*....|....*....|
gi 164658097 414 LDMIDEALLRPGRLEVHMEI 433
Cdd:cd19502  152 PDILDPALLRPGRFDRKIEF 171
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
280-432 1.44e-35

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: 132.17  E-value: 1.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 280 PDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVvNGPEILSKYVGASEENIRKLFAEAEAefrskgdeSG 359
Cdd:cd19526   16 PKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISV-KGPELLNKYIGASEQNVRDLFSRAQS--------AK 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164658097 360 LHIIIFDELDAICRQRGTTGGGTGvgDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHME 432
Cdd:cd19526   87 PCILFFDEFDSIAPKRGHDSTGVT--DRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVY 157
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
248-495 6.97e-35

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 137.59  E-value: 6.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 248 QPNFKFEDmgIGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVnGPE 327
Cdd:PTZ00454 139 KPDVTYSD--IGGLDIQKQEI-REAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVV-GSE 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 328 ILSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGG-GTGVGDSVVNQLLSKMDGVDQLNNIL 406
Cdd:PTZ00454 215 FVQKYLGEGPRMVRDVFRLAR--------ENAPSIIFIDEVDSIATKRFDAQTgADREVQRILLELLNQMDGFDQTTNVK 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 407 IIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMRtngvMDGDVNLQELAALTKNFSGAEIAGLVKSA 486
Cdd:PTZ00454 287 VIMATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMN----LSEEVDLEDFVSRPEKISAADIAAICQEA 362
                        250
                 ....*....|.
gi 164658097 487 TSFAF--NRHV 495
Cdd:PTZ00454 363 GMQAVrkNRYV 373
ftsH CHL00176
cell division protein; Validated
253-508 1.05e-34

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 140.96  E-value: 1.05e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 253 FEDmgIGGLD---TEFSAIfrrafASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNG 325
Cdd:CHL00176 182 FRD--IAGIEeakEEFEEV-----VSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAI-----AGEAEVpffsISG 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 326 PEILSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQR-GTTGGGTGVGDSVVNQLLSKMDGVDQLNN 404
Cdd:CHL00176 250 SEFVEMFVGVGAARVRDLFKKAK--------ENSPCIVFIDEIDAVGRQRgAGIGGGNDEREQTLNQLLTEMDGFKGNKG 321
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 405 ILIIGMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQtAKmrtNGVMDGDVNLQELAALTKNFSGAEIAGLVK 484
Cdd:CHL00176 322 VIVIAATNRVDILDAALLRPGRFDRQITVSLPDREGRLDILKVH-AR---NKKLSPDVSLELIARRTPGFSGADLANLLN 397
                        250       260
                 ....*....|....*....|....
gi 164658097 485 SATSFAFNRHVKVGTMAGISDDVE 508
Cdd:CHL00176 398 EAAILTARRKKATITMKEIDTAID 421
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
269-428 1.64e-33

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: 126.45  E-value: 1.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 269 FRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYVGASEENIRKLF 344
Cdd:cd19530    8 LTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAV-----ANESGAnfisVKGPELLNKYVGESERAVRQVF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 345 AEAEAefrskgdeSGLHIIIFDELDAICRQRGTTGGGTGvgDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRP 424
Cdd:cd19530   83 QRARA--------SAPCVIFFDEVDALVPKRGDGGSWAS--ERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRP 152

                 ....
gi 164658097 425 GRLE 428
Cdd:cd19530  153 GRLD 156
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
292-501 4.77e-33

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 135.16  E-value: 4.77e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 292 KGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYVG--ASEenIRKLFAEAEAEFRSkgdesglhiIIF 365
Cdd:COG0465  176 KGVLLVGPPGTGKTLLAKAV-----AGEAGVpffsISGSDFVEMFVGvgASR--VRDLFEQAKKNAPC---------IIF 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 366 -DELDAICRQRgttgggtgvgDSVV-----------NQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEI 433
Cdd:COG0465  240 iDEIDAVGRQR----------GAGLggghdereqtlNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRFDRQVVV 309
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097 434 NLPDENGRLQIINIQTAKMRtngvMDGDVNLQELAALTKNFSGAEIAGLVKSATSFAFNRHVKVGTMA 501
Cdd:COG0465  310 DLPDVKGREAILKVHARKKP----LAPDVDLEVIARRTPGFSGADLANLVNEAALLAARRNKKAVTME 373
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
258-524 1.01e-32

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 131.82  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVnGPEILSKYVGASE 337
Cdd:PTZ00361 185 IGGLEQQIQEI-KEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVV-GSELIQKYLGDGP 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 338 ENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGGG-TGVGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDM 416
Cdd:PTZ00361 263 KLVRELFRVAE--------ENAPSIVFIDEIDAIGTKRYDATSGgEKEIQRTMLELLNQLDGFDSRGDVKVIMATNRIES 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 417 IDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMrtngVMDGDVNLQELAALTKNFSGAEIAGLVKSATSFAFNRhvk 496
Cdd:PTZ00361 335 LDPALIRPGRIDRKIEFPNPDEKTKRRIFEIHTSKM----TLAEDVDLEEFIMAKDELSGADIKAICTEAGLLALRE--- 407
                        250       260
                 ....*....|....*....|....*...
gi 164658097 497 vgtmagisddvEGMRVNREDFLCALDEV 524
Cdd:PTZ00361 408 -----------RRMKVTQADFRKAKEKV 424
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
280-500 3.24e-32

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 133.24  E-value: 3.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 280 PDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYVGASEENIRKLFAEAEaefrskg 355
Cdd:PRK10733 174 PSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAI-----AGEAKVpfftISGSDFVEMFVGVGASRVRDMFEQAK------- 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 356 dESGLHIIIFDELDAICRQRGTTGGG-TGVGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEIN 434
Cdd:PRK10733 242 -KAAPCIIFIDEIDAVGRQRGAGLGGgHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVG 320
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164658097 435 LPDENGRLQIINIQTAKMRtngvMDGDVNLQELAALTKNFSGAEIAGLVKSATSFAFNRHVKVGTM 500
Cdd:PRK10733 321 LPDVRGREQILKVHMRRVP----LAPDIDAAIIARGTPGFSGADLANLVNEAALFAARGNKRVVSM 382
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
280-433 3.82e-30

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: 116.95  E-value: 3.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 280 PDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYVGASEENIRKLFAEAEAEFRSkg 355
Cdd:cd19501   26 PEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAV-----AGEAGVpffsISGSDFVEMFVGVGASRVRDLFEQAKKNAPC-- 98
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164658097 356 desglhIIIFDELDAICRQRGTTGGGT-GVGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEI 433
Cdd:cd19501   99 ------IVFIDEIDAVGRKRGAGLGGGhDEREQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLRPGRFDRQVYV 171
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
280-428 9.44e-30

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: 115.69  E-value: 9.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 280 PDLVEKlGIQHVKGLLLYGPPGTGKTLMARQIGK--MLNAREpkvVNGPEILSKYVGASEENIRKLFAEAEAefrskgde 357
Cdd:cd19527   16 PELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATecSLNFLS---VKGPELINMYIGESEANVREVFQKARD-------- 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164658097 358 SGLHIIIFDELDAICRQRGTTGGGTGVGDSVVNQLLSKMDGV-DQLNNILIIGMTNRLDMIDEALLRPGRLE 428
Cdd:cd19527   84 AKPCVIFFDELDSLAPSRGNSGDSGGVMDRVVSQLLAELDGMsSSGQDVFVIGATNRPDLLDPALLRPGRFD 155
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
258-428 1.43e-29

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: 115.30  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLDTEFSAIFRRAFASRIFPpDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVV----NGPEILSKYV 333
Cdd:cd19517    2 IGGLSHYINQLKEMVFFPLLYP-EVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKGGQKVSffmrKGADCLSKWV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 334 GASEENIRKLFAEAEAEFRSkgdesglhIIIFDELDAICRQRGTTGGGTGVgdSVVNQLLSKMDGVDQLNNILIIGMTNR 413
Cdd:cd19517   81 GEAERQLRLLFEEAYRMQPS--------IIFFDEIDGLAPVRSSKQEQIHA--SIVSTLLALMDGLDNRGQVVVIGATNR 150
                        170
                 ....*....|....*
gi 164658097 414 LDMIDEALLRPGRLE 428
Cdd:cd19517  151 PDALDPALRRPGRFD 165
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
258-428 2.08e-25

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: 103.25  E-value: 2.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLDTEFSAIfRRAFASRIFPPDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYV 333
Cdd:cd19518    2 IGGMDSTLKEL-CELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAI-----AGELKVpflkISATEIVSGVS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 334 GASEENIRKLFAEAEAEFRSkgdesglhIIIFDELDAICRQRGTTGGGTGVgdSVVNQLLSKMDGvdqLNN-------IL 406
Cdd:cd19518   76 GESEEKIRELFDQAISNAPC--------IVFIDEIDAITPKRESAQREMER--RIVSQLLTCMDE---LNNektaggpVL 142
                        170       180
                 ....*....|....*....|..
gi 164658097 407 IIGMTNRLDMIDEALLRPGRLE 428
Cdd:cd19518  143 VIGATNRPDSLDPALRRAGRFD 164
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
258-428 1.51e-23

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: 97.81  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLDTEFSAIfRRAFASRIFPPDLVeKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKvVNGPEILSKYVGASE 337
Cdd:cd19509    1 IAGLDDAKEAL-KEAVILPSLRPDLF-PGLRGPPRGILLYGPPGTGKTLLARAVASESGSTFFS-ISASSLVSKWVGESE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 338 ENIRKLFAEAEAEFRSkgdesglhIIIFDELDAICRQRGTTGGGTGVgdSVVNQLLSKMDGV--DQLNNILIIGMTNRLD 415
Cdd:cd19509   78 KIVRALFALARELQPS--------IIFIDEIDSLLSERGSGEHEASR--RVKTEFLVQMDGVlnKPEDRVLVLGATNRPW 147
                        170
                 ....*....|...
gi 164658097 416 MIDEALLRpgRLE 428
Cdd:cd19509  148 ELDEAFLR--RFE 158
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
282-435 2.25e-21

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: 91.05  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 282 LVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKV--VNGPEILSKYVGASEENIRKLFAEAEAEFRSKGDesg 359
Cdd:cd00009   10 LREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGAPFlyLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPG--- 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 164658097 360 lhIIIFDELDAICRQrgttgggtgVGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEINL 435
Cdd:cd00009   87 --VLFIDEIDSLSRG---------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
258-429 1.97e-15

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: 74.77  E-value: 1.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLDTEFSAIFRRAfasrIFP---PDLVEKLGI-QHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVNGpEILSKYV 333
Cdd:cd19520    2 IGGLDEVITELKELV----ILPlqrPELFDNSRLlQPPKGVLLYGPPGCGKTMLAKATAKEAGARFINLQVS-SLTDKWY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 334 GASEENIRKLFAEAeaefrSKGDESglhIIIFDELDAICRQRGTTGGGTGVGdsVVNQLLSKMDGV--DQLNNILIIGMT 411
Cdd:cd19520   77 GESQKLVAAVFSLA-----SKLQPS---IIFIDEIDSFLRQRSSTDHEATAM--MKAEFMSLWDGLstDGNCRVIVMGAT 146
                        170       180
                 ....*....|....*....|
gi 164658097 412 NRLDMIDEALLR--PGRLEV 429
Cdd:cd19520  147 NRPQDLDEAILRrmPKRFHI 166
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
258-433 1.42e-14

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: 72.32  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLdTEFSAIFRRAFASRIFPPDLVEklGIQHV-KGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKY 332
Cdd:cd19522    2 IADL-EEAKKLLEEAVVLPMWMPEFFK--GIRRPwKGVLMVGPPGTGKTLLAKAV-----ATECGTtffnVSSSTLTSKY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 333 VGASEENIRKLFAEAEAEFRSKgdesglhiIIFDELDAICRQRGTTGGGTGVGdSVVNQLLSKMDGV-------DQLNNI 405
Cdd:cd19522   74 RGESEKLVRLLFEMARFYAPTT--------IFIDEIDSICSRRGTSEEHEASR-RVKSELLVQMDGVggasendDPSKMV 144
                        170       180
                 ....*....|....*....|....*...
gi 164658097 406 LIIGMTNRLDMIDEALLRpgRLEVHMEI 433
Cdd:cd19522  145 MVLAATNFPWDIDEALRR--RLEKRIYI 170
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
292-423 2.31e-14

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: 71.94  E-value: 2.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 292 KGLLLYGPPGTGKTLMARQIGKMLNAREPKvVNGPEILSKYVGASEENIRKLFAEAEAEFRSkgdesglhIIIFDELDAI 371
Cdd:cd19525   56 KGILLFGPPGTGKTLIGKCIASQSGATFFS-ISASSLTSKWVGEGEKMVRALFSVARCKQPA--------VIFIDEIDSL 126
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 164658097 372 CRQRGTTGGGTGVgdSVVNQLLSKMDGVDQLNN--ILIIGMTNRLDMIDEALLR 423
Cdd:cd19525  127 LSQRGEGEHESSR--RIKTEFLVQLDGATTSSEdrILVVGATNRPQEIDEAARR 178
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
248-423 1.41e-13

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: 69.51  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 248 QPNFKFEDmgIGGLDTEFSAIFRRAFASRIFPPDLVEKLgiQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKvVNGPE 327
Cdd:cd19521    1 KPNVKWED--VAGLEGAKEALKEAVILPVKFPHLFTGNR--KPWSGILLYGPPGTGKSYLAKAVATEANSTFFS-VSSSD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 328 ILSKYVGASEENIRKLFAEAEaefrskgdESGLHIIIFDELDAICRQRGTTGGGTGVgdSVVNQLLSKMDGVDQLNN-IL 406
Cdd:cd19521   76 LVSKWMGESEKLVKQLFAMAR--------ENKPSIIFIDEVDSLCGTRGEGESEASR--RIKTELLVQMNGVGNDSQgVL 145
                        170
                 ....*....|....*..
gi 164658097 407 IIGMTNRLDMIDEALLR 423
Cdd:cd19521  146 VLGATNIPWQLDSAIRR 162
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
292-423 3.07e-12

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: 65.26  E-value: 3.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 292 KGLLLYGPPGTGKTLMARQIgkmlnAREPKV----VNGPEILSKYVGASEENIRKLFAEAEAEFRSkgdesglhIIIFDE 367
Cdd:cd19524   34 RGLLLFGPPGNGKTMLAKAV-----AAESNAtffnISAASLTSKYVGEGEKLVRALFAVARELQPS--------IIFIDE 100
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097 368 LDAICRQRGTTGGGTGVgdSVVNQLLSKMDGV--DQLNNILIIGMTNRLDMIDEALLR 423
Cdd:cd19524  101 VDSLLSERSEGEHEASR--RLKTEFLIEFDGVqsNGDDRVLVMGATNRPQELDDAVLR 156
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
292-437 4.50e-12

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: 64.32  E-value: 4.50e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097   292 KGLLLYGPPGTGKTLMARQIGKMLNAREPKVV----------------NGPEILSKYVGASEENIRKLFAEAEAEFRSkg 355
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqllLIIVGGKKASGSGELRLRLALALARKLKPD-- 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097   356 desglhIIIFDELDAICRQRGTTGGGTGVGDSVVNQLLSKmdgvdqlNNILIIGMTNRLDMIDEALLRPgRLEVHMEINL 435
Cdd:smart00382  81 ------VLILDEITSLLDAEQEALLLLLEELRLLLLLKSE-------KNLTVILTTNDEKDLGPALLRR-RFDRRIVLLL 146

                   ..
gi 164658097   436 PD 437
Cdd:smart00382 147 IL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
280-433 7.67e-12

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


Pssm-ID: 410918 [Multi-domain]  Cd Length: 153  Bit Score: 63.91  E-value: 7.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 280 PDLVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNaREPKVVNgpeiLSKyVGASEENIRKLfaeaeaeFRSKGDESg 359
Cdd:cd19510   12 EDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELD-YDICDLN----LSE-VVLTDDRLNHL-------LNTAPKQS- 77
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097 360 lhIIIFDELDA--ICRQRGTTGGGTGVGDSVVN--QLLSKMDGVDQLNNILIIGMTNRLDMIDEALLRPGRLEVHMEI 433
Cdd:cd19510   78 --IILLEDIDAafESREHNKKNPSAYGGLSRVTfsGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
294-421 3.56e-11

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 63.23  E-value: 3.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 294 LLLYGPPGTGKT----LMARQIGKMLNAREPKV----VNGPEILSKYVGASEENIRKLFAEAEaEFRSkgDESGLHIIIF 365
Cdd:cd19508   55 VLLHGPPGTGKTslckALAQKLSIRLSSRYRYGqlieINSHSLFSKWFSESGKLVTKMFQKIQ-ELID--DKDALVFVLI 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097 366 DELDAICRQRGTTGGGTGVGDS--VVNQLLSKMDGVDQLNNILIIGMTNRLDMIDEAL 421
Cdd:cd19508  132 DEVESLAAARSASSSGTEPSDAirVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
565-704 2.95e-10

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: 59.08  E-value: 2.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 565 RTSERTSLVTALLHGPPGSGKTALAATIAMAS---DFPFIKLVAPENMVGMNEQGKIAY--LNKVFNDSYKSPLSIVVVD 639
Cdd:cd00009   12 EALELPPPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLEGLVVAELFGHflVRLLFELAEKAKPGVLFID 91
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 164658097 640 NLEKiiewvpIGPRFSNPVLQTLAVLLGKQPPKDRRLFVLATTSNKAMLNDMDMANAFLADIRVP 704
Cdd:cd00009   92 EIDS------LSRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIP 150
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
576-693 8.27e-10

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: 57.22  E-value: 8.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPEnMVGMNEQGKIAYLNKVFNDSYKSPLSIVVVDNLEKIiewvpIGPRFS 655
Cdd:pfam00004   2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSE-LVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDAL-----AGSRGS 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 164658097  656 NP------VLQTLAVLLGKQPPKDRRLFVLATTsnkamlNDMDM 693
Cdd:pfam00004  76 GGdsesrrVVNQLLTELDGFTSSNSKVIVIAAT------NRPDK 113
ycf46 CHL00195
Ycf46; Provisional
249-492 4.48e-09

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 59.65  E-value: 4.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 249 PNFKFEDmgIGGLDTEFSAIFRRafaSRIFPPDlVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVNGpEI 328
Cdd:CHL00195 223 VNEKISD--IGGLDNLKDWLKKR---STSFSKQ-ASNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVG-KL 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 329 LSKYVGASEENIRKLFAEAEAefrskgdeSGLHIIIFDELDAiCRQRGTTGGGTGVGDSVVNQLLSKMDgvDQLNNILII 408
Cdd:CHL00195 296 FGGIVGESESRMRQMIRIAEA--------LSPCILWIDEIDK-AFSNSESKGDSGTTNRVLATFITWLS--EKKSPVFVV 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 409 GMTNRLDMIDEALLRPGRLEVHMEINLPDENGRLQIINIQTAKMRTNGVMDGDvnLQELAALTKNFSGAEIAGLVKSATS 488
Cdd:CHL00195 365 ATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIHLQKFRPKSWKKYD--IKKLSKLSNKFSGAEIEQSIIEAMY 442

                 ....
gi 164658097 489 FAFN 492
Cdd:CHL00195 443 IAFY 446
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
461-505 1.26e-08

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 51.39  E-value: 1.26e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 164658097  461 DVNLQELAALTKNFSGAEIAGLVKSATSFAFNRHVKVGTMAGISD 505
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLEE 45
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
258-349 1.29e-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: 54.68  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 258 IGGLDTEFSAIFRR--AFASRifppdlVEKLGIQHVKGLLLYGPPGTGKTLMARQIGKMLNAREPKVVNGpEILSKYVGA 335
Cdd:cd19507    2 VGGLDNLKDWLKKRkaAFSKQ------ASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMG-RLFGGLVGE 74
                         90
                 ....*....|....
gi 164658097 336 SEENIRKLFAEAEA 349
Cdd:cd19507   75 SESRLRQMIQTAEA 88
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
576-688 6.49e-08

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: 52.67  E-value: 6.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPENM-VGMNEQGKIayLNKVFNDSYKSPLSIVVVDNLEKiiewvpIGPRF 654
Cdd:cd19481   30 LLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLsKYVGESEKN--LRKIFERARRLAPCILFIDEIDA------IGRKR 101
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 164658097 655 SNP-----VLQTLAVLL----GKQPpkDRRLFVLATTSNKAML 688
Cdd:cd19481  102 DSSgesgeLRRVLNQLLteldGVNS--RSKVLVIAATNRPDLL 142
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
576-644 7.83e-08

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: 52.79  E-value: 7.83e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPENMVGMNEQGKiAYLNKVFNDSYKSPLSIVVVDNLEKI 644
Cdd:cd19518   38 LLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESE-EKIRELFDQAISNAPCIVFIDEIDAI 105
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
292-423 1.21e-06

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: 49.11  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 292 KGLLLYGPPGTGKTLMARQIGKMLNAREPKvVNGPEILSKYVGASEENIRKLFAEAEAEFRSkgdesglhIIIFDELDAI 371
Cdd:cd19523   34 RSILLFGPRGTGKTLLGRCLASQLGATFLR-LRGSTLVAKWAGEGEKILQASFLAARCRQPS--------VLFISDLDAL 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 164658097 372 CRQRGTTGGGTGVGDSvvnQLLSKMDGV--DQLNNILIIGMTNRLDMIDEALLR 423
Cdd:cd19523  105 LSSQDDEASPVGRLQV---ELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
576-707 1.32e-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: 48.52  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097   576 LLHGPPGSGKTALAATIA--MASDFPFIKLVAPENM--------------VGMNEQGKIAYLNKVFNDSYKSPLSIVVVD 639
Cdd:smart00382   6 LIVGPPGSGKTTLARALAreLGPPGGGVIYIDGEDIleevldqllliivgGKKASGSGELRLRLALALARKLKPDVLILD 85
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097   640 NLEKIiewvpIGPRFSNPVLQTLAVLLGKQPPKDRRLFVLATTSNKAMLNDMDMANAFLADIRVPDIT 707
Cdd:smart00382  86 EITSL-----LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
576-644 2.49e-06

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: 48.06  E-value: 2.49e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPE---NMVGMNEQGkiayLNKVFNDSYKSPLSIVVVDNLEKI 644
Cdd:cd19503   38 LLHGPPGTGKTLLARAVANEAGANFLSISGPSivsKYLGESEKN----LREIFEEARSHAPSIIFIDEIDAL 105
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
576-644 4.42e-06

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: 47.43  E-value: 4.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPENM---VGMNEQGkiayLNKVFNDSYKSPLSIVVVDNLEKI 644
Cdd:cd19519   38 LLYGPPGTGKTLIARAVANETGAFFFLINGPEIMsklAGESESN----LRKAFEEAEKNAPAIIFIDEIDAI 105
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
293-423 2.24e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 44.59  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  293 GLLLYGPPGTGKTLMARQIGKMLNAREPKVVNGPEilskyvGASEENIR-------KLFAEAEAEFRSKGDESglHIIIF 365
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVQLTR------DTTEEDLFgrrnidpGGASWVDGPLVRAAREG--EIAVL 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 164658097  366 DELDAIcrqrgttgggtgvGDSVVNQLLSKMD----------GVDQ--LNNILIIGMTNRLDM----IDEALLR 423
Cdd:pfam07728  73 DEINRA-------------NPDVLNSLLSLLDerrlllpdggELVKaaPDGFRLIATMNPLDRglneLSPALRS 133
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
267-367 4.80e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 46.62  E-value: 4.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 267 AIFRRAFASRIFPPdlveklgiqhvkgLLLYGPPGTGKTLMARQIGKMLNAREpkvvngpEILSKyVGASEENIRKLFAE 346
Cdd:PRK13342  25 KPLRRMIEAGRLSS-------------MILWGPPGTGKTTLARIIAGATDAPF-------EALSA-VTSGVKDLREVIEE 83
                         90       100
                 ....*....|....*....|..
gi 164658097 347 AEAEFRskgdeSGLHIIIF-DE 367
Cdd:PRK13342  84 ARQRRS-----AGRRTILFiDE 100
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
576-616 6.78e-05

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: 43.96  E-value: 6.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPE---NMVGMNEQG 616
Cdd:cd19526   31 LLYGPPGCGKTLLASAIASECGLNFISVKGPEllnKYIGASEQN 74
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
576-607 7.34e-05

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 45.77  E-value: 7.34e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPE 607
Cdd:COG1222  116 LLYGPPGTGKTLLAKAVAGELGAPFIRVRGSE 147
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
295-373 1.20e-04

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


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 44.51  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 295 LLYGPPGTGKTLMARQIGKMLNArePKVVNGPEILSK--YVGASEENI-RKLFaeAEAEFRSKGDESGlhIIIFDELDAI 371
Cdd:cd19497   54 LLIGPTGSGKTLLAQTLAKILDV--PFAIADATTLTEagYVGEDVENIlLKLL--QAADYDVERAQRG--IVYIDEIDKI 127

                 ..
gi 164658097 372 CR 373
Cdd:cd19497  128 AR 129
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
576-607 1.25e-04

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 45.21  E-value: 1.25e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPE 607
Cdd:PRK03992 169 LLYGPPGTGKTLLAKAVAHETNATFIRVVGSE 200
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
576-607 1.61e-04

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: 43.09  E-value: 1.61e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPE 607
Cdd:cd19502   41 LLYGPPGTGKTLLAKAVANHTDATFIRVVGSE 72
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
294-419 1.78e-04

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


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 44.45  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 294 LLLYGPPGTGKTLMARQIGKMLNAREPKvvNGPEILSKYVGASEEN-----IRKLFAE--AEAEFRSKG----------- 355
Cdd:COG1474   54 VLIYGPTGTGKTAVAKYVLEELEEEAEE--RGVDVRVVYVNCRQAStryrvLSRILEElgSGEDIPSTGlstdelfdrly 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097 356 ----DESGLHIIIFDELDAIcrqrgttggGTGVGDSVVNQLLSKMDGVDQlNNILIIGMTNRLDMIDE 419
Cdd:COG1474  132 ealdERDGVLVVVLDEIDYL---------VDDEGDDLLYQLLRANEELEG-ARVGVIGISNDLEFLEN 189
CDC48_2 pfam02933
Cell division protein 48 (CDC48), domain 2; This domain has a double psi-beta barrel fold and ...
161-202 2.28e-04

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


Pssm-ID: 427063  Cd Length: 64  Bit Score: 39.91  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 164658097  161 PFSADEMQgIFTRVFDSHVLSNGQVLVFEFHGQNLKATVRGV 202
Cdd:pfam02933   1 RFDGDELA-YVKRNLEGRPVSKGDTIVVEFLGGAIPLVVVST 41
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
292-342 2.33e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 44.22  E-value: 2.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 164658097  292 KGLLLYGPPGTGKTLMARQIGKMLNAREPKV-VNGPEILSKYVGASE---ENIRK 342
Cdd:pfam06068  51 RAVLIAGPPGTGKTALAIAISKELGEDTPFTsISGSEVYSLEMKKTEaltQAFRK 105
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
576-644 2.47e-04

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: 42.27  E-value: 2.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPENM---VGMNEQGkiayLNKVFNDSYKSPLSIVVVDNLEKI 644
Cdd:cd19511   31 LLYGPPGCGKTLLAKALASEAGLNFISVKGPELFskyVGESERA----VREIFQKARQAAPCIIFFDEIDSL 98
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
576-689 3.45e-04

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: 41.71  E-value: 3.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPENM---VGMNEQGkiayLNKVFNDSYKSPLSIVVVDNLEKIiewVPIGP 652
Cdd:cd19529   31 LLYGPPGTGKTLLAKAVATESNANFISVKGPELLskwVGESEKA----IREIFRKARQVAPCVIFFDEIDSI---APRRG 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 164658097 653 RFSNP------VLQTLAVLLGKQPPKDrrLFVLATTSNKAMLN 689
Cdd:cd19529  104 TTGDSgvtervVNQLLTELDGLEEMNG--VVVIAATNRPDIID 144
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
289-397 3.88e-04

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 43.68  E-value: 3.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  289 QHVKGLLLYGPPGTGKTLMARQIGKMLNA----REPKV--VNGPEILSKYVGASEENIRKLFaeaeaefrskgdESGLHI 362
Cdd:TIGR03922 310 QTSNHMLFAGPPGTGKTTIARVVAKIYCGlgvlRKPLVreVSRADLIGQYIGESEAKTNEII------------DSALGG 377
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 164658097  363 IIF-DELDAICRQRGTTGGGTGVGdsVVNQLLSKMD 397
Cdd:TIGR03922 378 VLFlDEAYTLVETGYGQKDPFGLE--AIDTLLARME 411
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
292-342 3.95e-04

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 43.81  E-value: 3.95e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 164658097 292 KGLLLYGPPGTGKTLMARQIGKMLNAREPKV-VNGPEILSKYVGASE---ENIRK 342
Cdd:COG1224   65 KGILIVGPPGTGKTALAVAIARELGEDTPFVaISGSEIYSAELKKTEflmQALRK 119
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
575-689 3.97e-04

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: 43.36  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 575 ALLHGPPGSGKTALAATIAMASDFPFIKLVAPENM---VGMNEQGkiayLNKVFNDSYKSPLSIVVVDNLEKII-EWVPI 650
Cdd:COG0464  194 LLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVskyVGETEKN----LREVFDKARGLAPCVLFIDEADALAgKRGEV 269
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 164658097 651 GPRFSNPVLQTLAVLLGKqppKDRRLFVLATTSNKAMLN 689
Cdd:COG0464  270 GDGVGRRVVNTLLTEMEE---LRSDVVVIAATNRPDLLD 305
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
292-421 5.00e-04

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: 41.36  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 292 KGLLLYGPPGTGKTLMARQIGkMLNAREPKVVNGPEILSkyVGASE-ENIRKLFAEAEAEFRskgdesGLhIIIFDELDA 370
Cdd:cd19512   23 RNILFYGPPGTGKTLFAKKLA-LHSGMDYAIMTGGDVAP--MGREGvTAIHKVFDWANTSRR------GL-LLFVDEADA 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 164658097 371 ICRQRGTTGGGTGVGdSVVNQLLSKMDgvDQLNNILIIGMTNRLDMIDEAL 421
Cdd:cd19512   93 FLRKRSTEKISEDLR-AALNAFLYRTG--EQSNKFMLVLASNQPEQFDWAI 140
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
576-683 5.27e-04

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: 41.18  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPENMVG-MNEQGKIayLNKVFNDSYKSPLSIVVVDNLEKII-----EWVP 649
Cdd:cd19509   36 LLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKwVGESEKI--VRALFALARELQPSIIFIDEIDSLLsergsGEHE 113
                         90       100       110
                 ....*....|....*....|....*....|....
gi 164658097 650 IGPRFSNPVLQTLAVLLGKQppkDRRLFVLATTS 683
Cdd:cd19509  114 ASRRVKTEFLVQMDGVLNKP---EDRVLVLGATN 144
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
576-605 6.14e-04

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 43.12  E-value: 6.14e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVA 605
Cdd:COG2256   53 ILWGPPGTGKTTLARLIANATDAEFVALSA 82
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
267-367 6.46e-04

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 43.12  E-value: 6.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 267 AIFRRAFASRIFPPdlveklgiqhvkgLLLYGPPGTGKTLMARQIGKMLNAREpkvvngpEILSKyVGASEENIRKLFAE 346
Cdd:COG2256   38 KPLRRAIEAGRLSS-------------MILWGPPGTGKTTLARLIANATDAEF-------VALSA-VTSGVKDIREVIEE 96
                         90       100
                 ....*....|....*....|..
gi 164658097 347 AEAEFRskgdeSGLHIIIF-DE 367
Cdd:COG2256   97 ARERRA-----YGRRTILFvDE 113
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
576-605 7.26e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 42.76  E-value: 7.26e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVA 605
Cdd:PRK13342  40 ILWGPPGTGKTTLARIIAGATDAPFEALSA 69
CDC48_N pfam02359
Cell division protein 48 (CDC48), N-terminal domain; This domain has a double psi-beta barrel ...
55-132 7.76e-04

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


Pssm-ID: 426738  Cd Length: 85  Bit Score: 39.10  E-value: 7.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097   55 MFRIVKSPPTLNTTNCVILNPS---EWGNTR--YVLVSGRFAFTAI--PDNTHTIAPGTIGTALLQRQWARLSaEGHDVA 127
Cdd:pfam02359   1 RLRVAEAPDRDVGRGIARLNPEdmeELGLFPgdVVEIKGKRKTVAIvwSAYPEDEGPGIIRMDGVTRKNAGVS-IGDTVT 79

                  ....*
gi 164658097  128 VEAFE 132
Cdd:pfam02359  80 VRPAE 84
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
576-611 1.25e-03

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 41.41  E-value: 1.25e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIkLVAPENMVG 611
Cdd:COG1223   39 LFYGPPGTGKTMLAEALAGELKLPLL-TVRLDSLIG 73
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
576-644 1.32e-03

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: 40.19  E-value: 1.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLVAPE--NM-VGMNEqgkiAYLNKVFNDSYKSPLSIVVVDNLEKI 644
Cdd:cd19527   30 LLYGPPGTGKTLLAKAIATECSLNFLSVKGPEliNMyIGESE----ANVREVFQKARDAKPCVIFFDELDSL 97
CDC48_N smart01073
Cell division protein 48 (CDC48) N-terminal domain; This domain has a double psi-beta barrel ...
56-120 1.54e-03

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


Pssm-ID: 215012 [Multi-domain]  Cd Length: 82  Bit Score: 37.97  E-value: 1.54e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 164658097    56 FRIVKSP-PTLNTTNCVILNPS-----EWGNTRYVLVSG-RFAFTAIPDNTHTIAPGTIGTALLQRQWARLS 120
Cdd:smart01073   1 LRVAEAPsDEDVGRGIARLSPEdmdelGLFPGDYVLITGkRRTVAIVWPAYPEDPGGIIRIDGVQRKNAGVS 72
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
576-642 1.86e-03

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: 39.72  E-value: 1.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 164658097 576 LLHGPPGSGKTALAATIAMASDFPFIKLvAPENMVG--MNEQGKIAylNKVFNDSYKSPLSIVVVDNLE 642
Cdd:cd19520   39 LLYGPPGCGKTMLAKATAKEAGARFINL-QVSSLTDkwYGESQKLV--AAVFSLASKLQPSIIFIDEID 104
PRK08116 PRK08116
hypothetical protein; Validated
293-331 2.60e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 40.39  E-value: 2.60e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 164658097 293 GLLLYGPPGTGKTLMARQIGKMLNAREPKV--VNGPEILSK 331
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANELIEKGVPVifVNFPQLLNR 156
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
576-607 3.08e-03

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 40.72  E-value: 3.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 164658097 576 LLHGPPGSGKTALAATIA--MASDFPFIKLVAPE 607
Cdd:COG1224   68 LIVGPPGTGKTALAVAIAreLGEDTPFVAISGSE 101
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
576-607 3.41e-03

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 40.37  E-value: 3.41e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 164658097  576 LLHGPPGSGKTALAATIA--MASDFPFIKLVAPE 607
Cdd:pfam06068  54 LIAGPPGTGKTALAIAISkeLGEDTPFTSISGSE 87
COG3903 COG3903
Predicted ATPase [General function prediction only];
545-599 3.49e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 40.77  E-value: 3.49e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 164658097 545 HFAPHIDTILRDGQLRVEQVRTSERTSLVTalLHGPPGSGKTALAATIA--MASDFP 599
Cdd:COG3903  151 PPAPLAALARRAAALAAAARALLSAARLVT--LTGPGGVGKTRLALEVAhrLADRFP 205
PRK13341 PRK13341
AAA family ATPase;
274-318 3.63e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 40.81  E-value: 3.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 164658097 274 ASRIFPPDLVEKLGIQHVKG----------------LLLYGPPGTGKTLMARQIGKMLNAR 318
Cdd:PRK13341  19 ADRLRPRTLEEFVGQDHILGegrllrraikadrvgsLILYGPPGVGKTTLARIIANHTRAH 79
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
290-328 4.89e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 39.73  E-value: 4.89e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 164658097 290 HVkglLLYGPPGTGKTLMARQIGKMLNARePKVVNGPEI 328
Cdd:PRK00080  53 HV---LLYGPPGLGKTTLANIIANEMGVN-IRITSGPAL 87
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
292-321 5.00e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.14  E-value: 5.00e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 164658097 292 KGLLLYGPPGTGKTLMARQIGKMLNAREPK 321
Cdd:COG1401  222 KNVILAGPPGTGKTYLARRLAEALGGEDNG 251
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
575-644 5.26e-03

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: 38.37  E-value: 5.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 164658097 575 ALLHGPPGSGKTALAATIAMASDFPFIKLVAPE--NM-VGMNEqgkiAYLNKVFNDSYKSPLSIVVVDNLEKI 644
Cdd:cd19501   40 VLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDfvEMfVGVGA----SRVRDLFEQAKKNAPCIVFIDEIDAV 108
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
295-373 5.33e-03

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 40.03  E-value: 5.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 295 LLYGPPGTGKTLMARQIGKMLN-------------ArepkvvnGpeilskYVGASEENI-RKLFAEAE-----AEfrsKG 355
Cdd:COG1219  113 LLIGPTGSGKTLLAQTLARILDvpfaiadattlteA-------G------YVGEDVENIlLKLLQAADydvekAE---RG 176
                         90
                 ....*....|....*....
gi 164658097 356 desglhiIIF-DELDAICR 373
Cdd:COG1219  177 -------IIYiDEIDKIAR 188
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
295-445 6.04e-03

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 38.33  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  295 LLYGPPGTGKTLMARQIGKMLNAREPKVVNG-------PEILSKYVGASEENIRklfAEAEAEFRSKGDESGLHIIIFDE 367
Cdd:pfam07724   7 LFLGPTGVGKTELAKALAELLFGDERALIRIdmseymeEHSVSRLIGAPPGYVG---YEEGGQLTEAVRRKPYSIVLIDE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  368 LDAICRqrgttgggtgvgdSVVNQLLSKMDG----------VDqLNNILIIGMTNR--LDMIDEALLRPGRLEVHMEINL 435
Cdd:pfam07724  84 IEKAHP-------------GVQNDLLQILEGgtltdkqgrtVD-FKNTLFIMTGNFgsEKISDASRLGDSPDYELLKEEV 149
                         170
                  ....*....|....*....
gi 164658097  436 PDEN---------GRLQII 445
Cdd:pfam07724 150 MDLLkkgfipeflGRLPII 168
AAA_22 pfam13401
AAA domain;
294-417 6.34e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 37.71  E-value: 6.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097  294 LLLYGPPGTGKTLMARQIGKMLNAREPKVV-------NGPEILSKYV-------GASEENIRKLFAEAEAEFRSKGDEsg 359
Cdd:pfam13401   8 LVLTGESGTGKTTLLRRLLEQLPEVRDSVVfvdlpsgTSPKDLLRALlralglpLSGRLSKEELLAALQQLLLALAVA-- 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 164658097  360 lHIIIFDELDAIcrqrgttgggtgvGDSVVNQLLSKMDGVDQLNNILIIGMTNRLDMI 417
Cdd:pfam13401  86 -VVLIIDEAQHL-------------SLEALEELRDLLNLSSKLLQLILVGTPELRELL 129
PRK13341 PRK13341
AAA family ATPase;
551-593 9.22e-03

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 39.65  E-value: 9.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 164658097 551 DTILRDGQLRVEQVRTSERTSLvtaLLHGPPGSGKTALAATIA 593
Cdd:PRK13341  34 DHILGEGRLLRRAIKADRVGSL---ILYGPPGVGKTTLARIIA 73
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
289-371 9.64e-03

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


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 38.80  E-value: 9.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 164658097 289 QHVKGLLLYGPPGTGKTLMARQIGKMLNAREPK----------------------VVNgPEILSKYVGAseENIRklfaE 346
Cdd:COG0470   16 RLPHALLLHGPPGIGKTTLALALARDLLCENPEggkacgqchsrlmaagnhpdllELN-PEEKSDQIGI--DQIR----E 88
                         90       100
                 ....*....|....*....|....*
gi 164658097 347 AEAEFRSKGDESGLHIIIFDELDAI 371
Cdd:COG0470   89 LGEFLSLTPLEGGRKVVIIDEADAM 113
 
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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