NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1736318468|ref|NP_001361015|]
View 

mitochondrial chaperone BCS1 isoform c [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 34-186 7.69e-94

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: 272.30  E-value: 7.69e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  34 IVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVL 113
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLLNTAPKQSIIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736318468 114 LEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 186
Cdd:cd19510    81 LEDIDAAFESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
BCS1_N super family cl07381
BCS1 N terminal; This domain is found at the N terminal of the mitochondrial ATPase BSC1. It ...
 1-24 1.35e-05

BCS1 N terminal; This domain is found at the N terminal of the mitochondrial ATPase BSC1. It encodes the import and intramitochondrial sorting for the protein.


The actual alignment was detected with superfamily member smart01024:

Pssm-ID: 471658  Cd Length: 170  Bit Score: 44.14  E-value: 1.35e-05
                           10        20
                   ....*....|....*....|....
gi 1736318468    1 MYTAVGSEWRPFgYPRRRRPLNSV 24
Cdd:smart01024 148 IYTADGPEWRRF-APRRKRPLSSV 170
 
Name Accession Description Interval E-value
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 34-186 7.69e-94

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: 272.30  E-value: 7.69e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  34 IVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVL 113
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLLNTAPKQSIIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736318468 114 LEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 186
Cdd:cd19510    81 LEDIDAAFESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 59-188 3.71e-20

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: 83.03  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  59 YLLYGPPGCGKSSFITALAGEL-----EHSICLLSLTDSSLSDDRLNHLLSVAPQQ--SLVLLEDVDAAFLSRDlavenp 131
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELgapfiEISGSELVSKYVGESEKRLRELFEAAKKLapCVIFIDEIDALAGSRG------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1736318468 132 VKYQGLGRLTFSGLLNALDGVASTEAR-IVFMTTNHVDRLDPALIrpGRVDLKEYVGY 188
Cdd:pfam00004  75 SGGDSESRRVVNQLLTELDGFTSSNSKvIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 29-187 2.73e-17

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 79.67  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  29 GLaDRIVRDVQEFID----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSIcllsltdsslSDDRLNHLLS 104
Cdd:COG1222    82 GL-DEQIEEIREAVElplkNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPF----------IRVRGSELVS 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 105 -------------------VAPqqSLVLLEDVDAAFLSRDLAVENpvkyqGLGRLTFSGLLNALDGVASTEARIVFMTTN 165
Cdd:COG1222   151 kyigegarnvrevfelareKAP--SIIFIDEIDAIAARRTDDGTS-----GEVQRTVNQLLAELDGFESRGDVLIIAATN 223

                         170       180
                  ....*....|....*....|..
gi 1736318468 166 HVDRLDPALIRPGRVDLKEYVG 187
Cdd:COG1222   224 RPDLLDPALLRPGRFDRVIEVP 245
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 18-183 1.24e-13

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 69.80  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  18 RRPLNSVVLQQGLADRI--VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSL 94
Cdd:PTZ00361  176 KAPLESYADIGGLEQQIqeIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQ 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  95 SDD-----RLNHLLSVAPQQ--SLVLLEDVDAAFLSR---DLAVENPVKYqglgrlTFSGLLNALDGVASTEARIVFMTT 164
Cdd:PTZ00361  256 KYLgdgpkLVRELFRVAEENapSIVFIDEIDAIGTKRydaTSGGEKEIQR------TMLELLNQLDGFDSRGDVKVIMAT 329

                         170
                  ....*....|....*....
gi 1736318468 165 NHVDRLDPALIRPGRVDLK 183
Cdd:PTZ00361  330 NRIESLDPALIRPGRIDRK 348
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 29-183 6.21e-12

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: 64.73  E-value: 6.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  29 GLADRI--VRDVQE--FIdNPKWYTDRGIPYRRGYLLYGPPGCGKssfiTALAGELEHSICLLSLTDSSLSDDRLN---- 100
Cdd:TIGR03689 186 GLGSQIeqIRDAVElpFL-HPELYREYGLKPPKGVLLYGPPGCGK----TLIAKAVANSLAARIGAEGGGKSYFLNikgp 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 101 HLLS-----------VAPQQS----------LVLLEDVDAAFLSRDLAV----ENPVKYQglgrltfsgLLNALDGVAST 155
Cdd:TIGR03689 261 ELLNkyvgeterqirLIFQRArekasegrpvIVFFDEMDSLFRTRGSGVssdvETTVVPQ---------LLAEIDGVESL 331

                         170       180
                  ....*....|....*....|....*...
gi 1736318468 156 EARIVFMTTNHVDRLDPALIRPGRVDLK 183
Cdd:TIGR03689 332 DNVIVIGASNREDMIDPAILRPGRLDVK 359
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 56-187 1.10e-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: 46.98  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468   56 RRGYLLYGPPGCGKSSFITALAGEL------------EHSICLLSLTDSSLSDDRLNHLLSVA------------PQQSL 111
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppgggviyidgEDILEEVLDQLLLIIVGGKKASGSGElrlrlalalarkLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736318468  112 VLLEDVDAAflsrdlavenpVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPgRVDLKEYVG 187
Cdd:smart00382  82 LILDEITSL-----------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLL 145
BCS1_N smart01024
This domain is found at the N terminal of the mitochondrial ATPase BCS1. It encodes the import ...
 1-24 1.35e-05

This domain is found at the N terminal of the mitochondrial ATPase BCS1. It encodes the import and intramitochondrial sorting for the protein;


Pssm-ID: 214980  Cd Length: 170  Bit Score: 44.14  E-value: 1.35e-05
                           10        20
                   ....*....|....*....|....
gi 1736318468    1 MYTAVGSEWRPFgYPRRRRPLNSV 24
Cdd:smart01024 148 IYTADGPEWRRF-APRRKRPLSSV 170
cell_div_CdvC NF041006
cell division protein CdvC;
57-81 2.10e-04

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 42.03  E-value: 2.10e-04
                          10        20
                  ....*....|....*....|....*
gi 1736318468  57 RGYLLYGPPGCGKSSFITALAGELE 81
Cdd:NF041006  135 RGILLYGPPGCGKTMLAAAVANEID 159
 
Name Accession Description Interval E-value
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 34-186 7.69e-94

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: 272.30  E-value: 7.69e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  34 IVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVL 113
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLLNTAPKQSIIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736318468 114 LEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 186
Cdd:cd19510    81 LEDIDAAFESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 34-183 1.27e-34

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: 121.62  E-value: 1.27e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  34 IVRDVQEFIDNPKWYTD---RGIPYRRGYLLYGPPGCGKSSFITALAGELEH-----SICLLSLTDSSLSDDRLNHLLSV 105
Cdd:cd19481     1 LKASLREAVEAPRRGSRlrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLplivvKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 106 APQQ--SLVLLEDVDAAFLSRDLAVENPVkyqglGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLK 183
Cdd:cd19481    81 ARRLapCILFIDEIDAIGRKRDSSGESGE-----LRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 59-188 3.71e-20

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: 83.03  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  59 YLLYGPPGCGKSSFITALAGEL-----EHSICLLSLTDSSLSDDRLNHLLSVAPQQ--SLVLLEDVDAAFLSRDlavenp 131
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELgapfiEISGSELVSKYVGESEKRLRELFEAAKKLapCVIFIDEIDALAGSRG------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1736318468 132 VKYQGLGRLTFSGLLNALDGVASTEAR-IVFMTTNHVDRLDPALIrpGRVDLKEYVGY 188
Cdd:pfam00004  75 SGGDSESRRVVNQLLTELDGFTSSNSKvIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 29-187 2.73e-17

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 79.67  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  29 GLaDRIVRDVQEFID----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSIcllsltdsslSDDRLNHLLS 104
Cdd:COG1222    82 GL-DEQIEEIREAVElplkNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPF----------IRVRGSELVS 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 105 -------------------VAPqqSLVLLEDVDAAFLSRDLAVENpvkyqGLGRLTFSGLLNALDGVASTEARIVFMTTN 165
Cdd:COG1222   151 kyigegarnvrevfelareKAP--SIIFIDEIDAIAARRTDDGTS-----GEVQRTVNQLLAELDGFESRGDVLIIAATN 223

                         170       180
                  ....*....|....*....|..
gi 1736318468 166 HVDRLDPALIRPGRVDLKEYVG 187
Cdd:COG1222   224 RPDLLDPALLRPGRFDRVIEVP 245
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 17-229 2.23e-15

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: 74.56  E-value: 2.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  17 RRRPLNSVVLQQGLADRIVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELE--------------- 81
Cdd:COG0464   152 REAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGlplievdlsdlvsky 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  82 --HSicllsltdsslsDDRLNHLLSVAPQQS--LVLLEDVDAAFLSRDLAVEnpvkyqGLGRLTFSGLLNALDGVasTEA 157
Cdd:COG0464   232 vgET------------EKNLREVFDKARGLApcVLFIDEADALAGKRGEVGD------GVGRRVVNTLLTEMEEL--RSD 291

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1736318468 158 RIVFMTTNHVDRLDPALIRpgRVDLKEYVGYCSHWQLTQMFQRFYPGQAPSLAENFAEhVLRATNQISPAQV 229
Cdd:COG0464   292 VVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEE-LAEATEGLSGADI 360
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 35-186 3.26e-15

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: 71.11  E-value: 3.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  35 VRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGE-----LEHSICLLSLTDSSLSDDRLNHLLSVAPQQ 109
Cdd:cd19501    16 LKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEagvpfFSISGSDFVEMFVGVGASRVRDLFEQAKKN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 110 S--LVLLEDVDAAFLSRDLAV--ENPVKYQglgrlTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEY 185
Cdd:cd19501    96 ApcIVFIDEIDAVGRKRGAGLggGHDEREQ-----TLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLRPGRFDRQVY 170


                  .
gi 1736318468 186 V 186
Cdd:cd19501   171 V 171
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 29-181 7.02e-15

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: 70.01  E-value: 7.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  29 GLADRIVRdVQEFID----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELE--------HSIcllSLTDSSLSD 96
Cdd:cd19503     4 GLDEQIAS-LKELIElplkYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGanflsisgPSI---VSKYLGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  97 DRLNHLLSVAP--QQSLVLLEDVDAAFLSRDLAVEnpvkyqGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPAL 174
Cdd:cd19503    80 KNLREIFEEARshAPSIIFIDEIDALAPKREEDQR------EVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPAL 153


                  ....*..
gi 1736318468 175 IRPGRVD 181
Cdd:cd19503   154 RRPGRFD 160
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 29-181 9.98e-15

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: 69.74  E-value: 9.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  29 GLADRIVRDVQEF----IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGEL-----EHSICLLSLTDSSLSDDRL 99
Cdd:cd19518     3 GGMDSTLKELCELlihpILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELkvpflKISATEIVSGVSGESEEKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 100 NHLLSVAPQQS--LVLLEDVDAAFLSRDLAVENpvkyqgLGRLTFSGLLNALDGV----ASTEARIVFMTTNHVDRLDPA 173
Cdd:cd19518    83 RELFDQAISNApcIVFIDEIDAITPKRESAQRE------MERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPA 156


                  ....*...
gi 1736318468 174 LIRPGRVD 181
Cdd:cd19518   157 LRRAGRFD 164
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 18-183 1.24e-13

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 69.80  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  18 RRPLNSVVLQQGLADRI--VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSL 94
Cdd:PTZ00361  176 KAPLESYADIGGLEQQIqeIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQ 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  95 SDD-----RLNHLLSVAPQQ--SLVLLEDVDAAFLSR---DLAVENPVKYqglgrlTFSGLLNALDGVASTEARIVFMTT 164
Cdd:PTZ00361  256 KYLgdgpkLVRELFRVAEENapSIVFIDEIDAIGTKRydaTSGGEKEIQR------TMLELLNQLDGFDSRGDVKVIMAT 329

                         170
                  ....*....|....*....
gi 1736318468 165 NHVDRLDPALIRPGRVDLK 183
Cdd:PTZ00361  330 NRIESLDPALIRPGRIDRK 348
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 29-183 1.12e-12

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: 64.28  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  29 GLADRI--VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELE----HSICLLSLTDSSLSDDRLNH 101
Cdd:cd19502     7 GLDEQIreIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDatfiRVVGSELVQKYIGEGARLVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 102 -LLSVAPQQ--SLVLLEDVDAAFLSR---DLAVENPVKYqglgrlTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALI 175
Cdd:cd19502    87 eLFEMAREKapSIIFIDEIDAIGAKRfdsGTGGDREVQR------TMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160


                  ....*...
gi 1736318468 176 RPGRVDLK 183
Cdd:cd19502   161 RPGRFDRK 168
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 36-186 2.69e-12

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: 63.07  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  36 RDVQEFIDNPKWYTDR----GIPYRRGYLLYGPPGCGKSSFITALAGElehsicllsltdsslsdDRLN-------HLLS 104
Cdd:cd19511     3 RELKEAVEWPLKHPDAfkrlGIRPPKGVLLYGPPGCGKTLLAKALASE-----------------AGLNfisvkgpELFS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 105 -------------------VAPqqSLVLLEDVDAAFLSRDLAVENPVKYQGLgrltfSGLLNALDGVASTEARIVFMTTN 165
Cdd:cd19511    66 kyvgeseravreifqkarqAAP--CIIFFDEIDSLAPRRGQSDSSGVTDRVV-----SQLLTELDGIESLKGVVVIAATN 138

                         170       180
                  ....*....|....*....|.
gi 1736318468 166 HVDRLDPALIRPGRVDLKEYV 186
Cdd:cd19511   139 RPDMIDPALLRPGRLDKLIYV 159
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 38-186 5.64e-12

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: 62.14  E-value: 5.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  38 VQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSL-----SDDRLNHLLSVAPQQS-- 110
Cdd:cd19528     9 VQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTmwfgeSEANVRDIFDKARAAApc 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736318468 111 LVLLEDVDAAFLSRDLAVENPvkyQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 186
Cdd:cd19528    89 VLFFDELDSIAKARGGNIGDA---GGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 29-183 6.21e-12

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: 64.73  E-value: 6.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  29 GLADRI--VRDVQE--FIdNPKWYTDRGIPYRRGYLLYGPPGCGKssfiTALAGELEHSICLLSLTDSSLSDDRLN---- 100
Cdd:TIGR03689 186 GLGSQIeqIRDAVElpFL-HPELYREYGLKPPKGVLLYGPPGCGK----TLIAKAVANSLAARIGAEGGGKSYFLNikgp 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 101 HLLS-----------VAPQQS----------LVLLEDVDAAFLSRDLAV----ENPVKYQglgrltfsgLLNALDGVAST 155
Cdd:TIGR03689 261 ELLNkyvgeterqirLIFQRArekasegrpvIVFFDEMDSLFRTRGSGVssdvETTVVPQ---------LLAEIDGVESL 331

                         170       180
                  ....*....|....*....|....*...
gi 1736318468 156 EARIVFMTTNHVDRLDPALIRPGRVDLK 183
Cdd:TIGR03689 332 DNVIVIGASNREDMIDPAILRPGRLDVK 359
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 45-186 2.64e-11

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: 60.20  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  45 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGElehsicllslTDSSLSDDRLNHLLS-------------------V 105
Cdd:cd19529    16 PEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATE----------SNANFISVKGPELLSkwvgesekaireifrkarqV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 106 APqqSLVLLEDVDAAFLSRDLAVENPVKYQGLGRltfsgLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEY 185
Cdd:cd19529    86 AP--CVIFFDEIDSIAPRRGTTGDSGVTERVVNQ-----LLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158


                  .
gi 1736318468 186 V 186
Cdd:cd19529   159 I 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
35-187 8.50e-11

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 61.59  E-value: 8.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  35 VRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGE-----LEHSICLLSLTDSSLSDDRLNHLLSVAPQQ 109
Cdd:PRK10733  164 VAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEakvpfFTISGSDFVEMFVGVGASRVRDMFEQAKKA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 110 S--LVLLEDVDAAFLSRDlavenpvkyQGLG------RLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 181
Cdd:PRK10733  244 ApcIIFIDEIDAVGRQRG---------AGLGgghderEQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFD 314


                  ....*.
gi 1736318468 182 LKEYVG 187
Cdd:PRK10733  315 RQVVVG 320
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 35-181 4.49e-10

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: 59.54  E-value: 4.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  35 VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLL-----SLTDSSLSDDRLNHLLSVAPQ 108
Cdd:TIGR01243 190 IREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISIngpeiMSKYYGESEERLREIFKEAEE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1736318468 109 Q--SLVLLEDVDAAFLSRDLAVENpvkyqgLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 181
Cdd:TIGR01243 270 NapSIIFIDEIDAIAPKREEVTGE------VEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFD 338
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 42-186 8.20e-10

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: 55.96  E-value: 8.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  42 IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALA--------------------GELEHSIcllsltdsslsddRLNH 101
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVAnesganfisvkgpellnkyvGESERAV-------------RQVF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 102 LLSVAPQQSLVLLEDVDAAFLSRDLAVEnpvkyQGLGRLTfSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 181
Cdd:cd19530    83 QRARASAPCVIFFDEVDALVPKRGDGGS-----WASERVV-NQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLD 156


                  ....*
gi 1736318468 182 LKEYV 186
Cdd:cd19530   157 KTLYV 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 45-181 9.50e-10

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: 55.90  E-value: 9.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  45 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSslsddrLNHLLSVAPQQSLVLLEDVDAA---- 120
Cdd:cd19526    16 PKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPEL------LNKYIGASEQNVRDLFSRAQSAkpci 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1736318468 121 --FLSRD-LAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 181
Cdd:cd19526    90 lfFDEFDsIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLD 153
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 45-183 1.15e-09

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 57.85  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  45 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSslsddrLNHLLSVAPQQ-------------SL 111
Cdd:PTZ00454  168 PELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEF------VQKYLGEGPRMvrdvfrlarenapSI 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1736318468 112 VLLEDVDAAFLSR-------DLAVEnpvkyqglgRLTFSgLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLK 183
Cdd:PTZ00454  242 IFIDEVDSIATKRfdaqtgaDREVQ---------RILLE-LLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRK 310
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 45-186 1.53e-09

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: 57.99  E-value: 1.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  45 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSL-----SDDRLNHLLSVAPQQS--LVLLEDV 117
Cdd:TIGR01243 476 PEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSkwvgeSEKAIREIFRKARQAApaIIFFDEI 555

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736318468 118 DAAFLSR----DLAVENPVKYQglgrltfsgLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 186
Cdd:TIGR01243 556 DAIAPARgarfDTSVTDRIVNQ---------LLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILV 619
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 35-181 1.64e-09

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: 55.52  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  35 VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLS-----LTDSSLSDDRLNHLLSVAPQ 108
Cdd:cd19519    12 IREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINgpeimSKLAGESESNLRKAFEEAEK 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736318468 109 Q--SLVLLEDVDAAFLSRDlavenpvKYQG-LGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 181
Cdd:cd19519    92 NapAIIFIDEIDAIAPKRE-------KTHGeVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
21-201 9.97e-09

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 54.12  E-value: 9.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  21 LNSVVLQQGLADRIVRDVQEF--IDNPKWYtdrGIPYRRGYLLYGPPGCGKSSFITALAGEL------------------ 80
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELrrRENLRKF---GLWPPRKILFYGPPGTGKTMLAEALAGELklplltvrldsligsylg 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  81 EHSicllsltdsslsdDRLNHLLSVAPQQSLVLLED-VDAAFLSRDLavENPVKYqgLGRLTfSGLLNALDGVASteaRI 159
Cdd:COG1223    78 ETA-------------RNLRKLFDFARRAPCVIFFDeFDAIAKDRGD--QNDVGE--VKRVV-NALLQELDGLPS---GS 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1736318468 160 VFM-TTNHVDRLDPALIRpgRVDLKEYVGYCSHWQLTQMFQRF 201
Cdd:COG1223   137 VVIaATNHPELLDSALWR--RFDEVIEFPLPDKEERKEILELN 177
ftsH CHL00176
cell division protein; Validated
 41-181 2.17e-08

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 54.29  E-value: 2.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  41 FIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELE---HSI--CLLSLTDSSLSDDRLNHLLSVAPQQS--LVL 113
Cdd:CHL00176  201 FLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEvpfFSIsgSEFVEMFVGVGAARVRDLFKKAKENSpcIVF 280

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 114 LEDVDAAFLSRDLAVE--NPVKYQglgrlTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 181
Cdd:CHL00176  281 IDEIDAVGRQRGAGIGggNDEREQ-----TLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFD 345
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 45-181 9.85e-08

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: 50.59  E-value: 9.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  45 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEH------------SICLLSLTDSSLSDDRLNHLLSVAPQQSLV 112
Cdd:cd19517    23 PEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvsffmrkgADCLSKWVGEAERQLRLLFEEAYRMQPSII 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1736318468 113 LLEDVDAaflsrdLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 181
Cdd:cd19517   103 FFDEIDG------LAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRRPGRFD 165
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 32-186 9.90e-08

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: 50.20  E-value: 9.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  32 DRIVRDVQEFIDNPKWYTDrGIPYRRGYLLYGPPGCGKSSFITALAGELEHS---------ICLLSLTDSSLSDDRLNHL 102
Cdd:cd19527     3 KEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNflsvkgpelINMYIGESEANVREVFQKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 103 LSVAPqqSLVLLEDVDAAFLSRDlaveNPVKYQGLGRLTFSGLLNALDGVASTEARI-VFMTTNHVDRLDPALIRPGRVD 181
Cdd:cd19527    82 RDAKP--CVIFFDELDSLAPSRG----NSGDSGGVMDRVVSQLLAELDGMSSSGQDVfVIGATNRPDLLDPALLRPGRFD 155


                  ....*
gi 1736318468 182 LKEYV 186
Cdd:cd19527   156 KLLYL 160
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 32-188 2.61e-07

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: 48.68  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  32 DRIVRDVQEFIDNPKWytdrgipyrRGYLLYGPPGCGKSSFITALAGELEHSIcllsltdssLSDDRLNHLLSVapqQSL 111
Cdd:cd00009     4 EEAIEALREALELPPP---------KNLLLYGPPGTGKTTLARAIANELFRPG---------APFLYLNASDLL---EGL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 112 VLLEDVDAAFLSRDLAVENPVKY--------QGLGRLTFSGLLNAL----DGVASTEARIVFMTTNHVDRLDPALIRPGR 179
Cdd:cd00009    63 VVAELFGHFLVRLLFELAEKAKPgvlfideiDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDR 142


                  ....*....
gi 1736318468 180 VDLKEYVGY 188
Cdd:cd00009   143 LDIRIVIPL 151
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
35-181 3.36e-07

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 50.81  E-value: 3.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  35 VRDVQEFIDNPKWYTDRG--IPyrRGYLLYGPPGCGKssfiT----ALAGElehsicllsltdsslsddrlnhllsvApq 108
Cdd:COG0465   154 LQEIVDFLKDPEKFTRLGakIP--KGVLLVGPPGTGK----TllakAVAGE--------------------------A-- 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468 109 qslvlledvDAAFLS------------------RDL------------------AVenpvkyqglGRLTFSGL------- 145
Cdd:COG0465   200 ---------GVPFFSisgsdfvemfvgvgasrvRDLfeqakknapciifideidAV---------GRQRGAGLggghder 261

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1736318468 146 ---LNAL----DGVASTEARIVFMTTNHVDRLDPALIRPGRVD 181
Cdd:COG0465   262 eqtLNQLlvemDGFEGNEGVIVIAATNRPDVLDPALLRPGRFD 304
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 52-183 7.47e-07

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: 47.87  E-value: 7.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  52 GIPYRRGYLLYGPPGCGKS---------------------SFITALAGELEHSIcllslTDSSLSDDRLNHLLSVAPQQS 110
Cdd:cd19504    31 GCKHVKGILLYGPPGTGKTlmarqigkmlnarepkivngpEILNKYVGESEANI-----RKLFADAEEEQRRLGANSGLH 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1736318468 111 LVLLEDVDAAFLSRDLAVENpvkyQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLK 183
Cdd:cd19504   106 IIIFDEIDAICKQRGSMAGS----TGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQ 174
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 56-187 1.10e-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: 46.98  E-value: 1.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468   56 RRGYLLYGPPGCGKSSFITALAGEL------------EHSICLLSLTDSSLSDDRLNHLLSVA------------PQQSL 111
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppgggviyidgEDILEEVLDQLLLIIVGGKKASGSGElrlrlalalarkLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1736318468  112 VLLEDVDAAflsrdlavenpVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPgRVDLKEYVG 187
Cdd:smart00382  82 LILDEITSL-----------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLL 145
PRK04195 PRK04195
replication factor C large subunit; Provisional
 19-80 1.06e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 46.07  E-value: 1.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1736318468  19 RP--LNSVVLQqglaDRIVRDVQEFIDNpkWytDRGIPyRRGYLLYGPPGCGKSSFITALAGEL 80
Cdd:PRK04195    9 RPktLSDVVGN----EKAKEQLREWIES--W--LKGKP-KKALLLYGPPGVGKTSLAHALANDY 63
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 52-181 1.26e-05

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: 44.28  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  52 GIPYRRGYLLYGPPGCGKSSFITALAGE-----LEHSICLLSLTDSSLSDDRLNHLLSVAPQQS--LVLLEDVDAAFLSR 124
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVwqlplLRLDMGRLFGGLVGESESRLRQMIQTAEAIApcVLWIDEIEKGFSNA 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1736318468 125 DLAVEnpvkyQGLGRLTFSGLLNALdgvaSTEARIVFM--TTNHVDRLDPALIRPGRVD 181
Cdd:cd19507   107 DSKGD-----SGTSSRVLGTFLTWL----QEKKKPVFVvaTANNVQSLPPELLRKGRFD 156
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 29-181 1.28e-05

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 45.59  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  29 GLADRIvRDVQEFID----NPKWYTDRGIPYRRGYLLYGPPGCGK------------SSFITALAGEL------EHSicl 86
Cdd:PRK03992  135 GLEEQI-REVREAVElplkKPELFEEVGIEPPKGVLLYGPPGTGKtllakavahetnATFIRVVGSELvqkfigEGA--- 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  87 lsltdsslsddRLNH-LLSVAPQQ--SLVLLEDVDAAFLSR-------DLAVEnpvkyqglgRlTFSGLLNALDGVAST- 155
Cdd:PRK03992  211 -----------RLVReLFELAREKapSIIFIDEIDAIAAKRtdsgtsgDREVQ---------R-TLMQLLAEMDGFDPRg 269

                         170       180
                  ....*....|....*....|....*.
gi 1736318468 156 EARIVfMTTNHVDRLDPALIRPGRVD 181
Cdd:PRK03992  270 NVKII-AATNRIDILDPAILRPGRFD 294
BCS1_N smart01024
This domain is found at the N terminal of the mitochondrial ATPase BCS1. It encodes the import ...
 1-24 1.35e-05

This domain is found at the N terminal of the mitochondrial ATPase BCS1. It encodes the import and intramitochondrial sorting for the protein;


Pssm-ID: 214980  Cd Length: 170  Bit Score: 44.14  E-value: 1.35e-05
                           10        20
                   ....*....|....*....|....
gi 1736318468    1 MYTAVGSEWRPFgYPRRRRPLNSV 24
Cdd:smart01024 148 IYTADGPEWRRF-APRRKRPLSSV 170
cell_div_CdvC NF041006
cell division protein CdvC;
57-81 2.10e-04

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 42.03  E-value: 2.10e-04
                          10        20
                  ....*....|....*....|....*
gi 1736318468  57 RGYLLYGPPGCGKSSFITALAGELE 81
Cdd:NF041006  135 RGILLYGPPGCGKTMLAAAVANEID 159
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 45-81 1.30e-03

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: 38.69  E-value: 1.30e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1736318468  45 PKWYTDRGIPYRrGYLLYGPPGCGKSSFITALAGELE 81
Cdd:cd19521    30 PHLFTGNRKPWS-GILLYGPPGTGKSYLAKAVATEAN 65
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 57-79 1.47e-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: 38.17  E-value: 1.47e-03
                          10        20
                  ....*....|....*....|...
gi 1736318468  57 RGYLLYGPPGCGKSSFITALAGE 79
Cdd:cd19520    36 KGVLLYGPPGCGKTMLAKATAKE 58
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 32-176 1.58e-03

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: 38.10  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  32 DRIVRDVQEFIDNPKWYTD-----RGIPyrRGYLLYGPPGCGKSSFITALAGEL-------EHSICLLSLTDSSLSDDRL 99
Cdd:cd19509     5 DDAKEALKEAVILPSLRPDlfpglRGPP--RGILLYGPPGTGKTLLARAVASESgstffsiSASSLVSKWVGESEKIVRA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1736318468 100 NHLLSVAPQQSLVLLEDVDaAFLSRDLAVEnpvkYQGLGRLTfSGLLNALDGV-ASTEARIVFM-TTNHVDRLDPALIR 176
Cdd:cd19509    83 LFALARELQPSIIFIDEID-SLLSERGSGE----HEASRRVK-TEFLVQMDGVlNKPEDRVLVLgATNRPWELDEAFLR 155
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 60-80 5.56e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 35.66  E-value: 5.56e-03
                          10        20
                  ....*....|....*....|.
gi 1736318468  60 LLYGPPGCGKSSFITALAGEL 80
Cdd:pfam00910   2 WLYGPPGCGKSTLAKYLARAL 22
Polyoma_lg_T_C pfam06431
Polyomavirus large T antigen C-terminus;
53-185 6.67e-03

Polyomavirus large T antigen C-terminus;


Pssm-ID: 283968  Cd Length: 417  Bit Score: 37.26  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1736318468  53 IPYRRGYLLYGPPGCGKSSFITALageLEhsICLLSLTDSSLSDDRLNHLLSVAPQQSLVLLEDVDA-AFLSRDLAvenp 131
Cdd:pfam06431 152 IPKKRYWLFKGPIDSGKTTLAAAL---LD--LCGGKALNVNLPLERLNFELGVAIDQFMVVFEDVKGtGAESRDLP---- 222

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1736318468 132 vkyQGLGRLTFSGLLNALDGVASteariVFMTTNHVDRlDPALIRPGRVDLKEY 185
Cdd:pfam06431 223 ---SGHGINNLDNLRDYLDGSVK-----VNLEKKHLNK-RTQIFPPGIVTMNEY 267
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH