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Conserved domains on  [gi|1701944567|ref|NP_001358378|]
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mitochondrial chaperone BCS1 isoform a [Homo sapiens]

Protein Classification

Graphical summary

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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 ...
 201-353 2.24e-91

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: 2.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 201 IVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVL 280
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLLNTAPKQSIIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1701944567 281 LEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 353
Cdd:cd19510    81 LEDIDAAFESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
BCS1_N smart01024
This domain is found at the N terminal of the mitochondrial ATPase BCS1. It encodes the import ...
 24-191 1.34e-83

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: 253.31  E-value: 1.34e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567   24 GVGTALALARKGVQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRH--STRTQHLSVETSYLQHESGRISTKFEFVPSP 101
Cdd:smart01024   2 LLGAAGAFLRRGISVAASLIRRRFLVTLEVPSKDESYAWLLEWLSQQpfRQRSRHLSVETSYTQHDNGKSSTSFSFVPGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567  102 GNHFIWYRGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFgY 181
Cdd:smart01024  82 GTHWFWYKGRWIWVTREREKTMADMRTGSPFETLTLTTLGRDRDVFKELLEEARELALKRTEGKTVIYTADGPEWRRF-A 160

                          170
                   ....*....|
gi 1701944567  182 PRRRRPLNSV 191
Cdd:smart01024 161 PRRKRPLSSV 170
 
Name Accession Description Interval E-value
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 201-353 2.24e-91

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: 2.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 201 IVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVL 280
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLLNTAPKQSIIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1701944567 281 LEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 353
Cdd:cd19510    81 LEDIDAAFESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
BCS1_N smart01024
This domain is found at the N terminal of the mitochondrial ATPase BCS1. It encodes the import ...
 24-191 1.34e-83

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: 253.31  E-value: 1.34e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567   24 GVGTALALARKGVQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRH--STRTQHLSVETSYLQHESGRISTKFEFVPSP 101
Cdd:smart01024   2 LLGAAGAFLRRGISVAASLIRRRFLVTLEVPSKDESYAWLLEWLSQQpfRQRSRHLSVETSYTQHDNGKSSTSFSFVPGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567  102 GNHFIWYRGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFgY 181
Cdd:smart01024  82 GTHWFWYKGRWIWVTREREKTMADMRTGSPFETLTLTTLGRDRDVFKELLEEARELALKRTEGKTVIYTADGPEWRRF-A 160

                          170
                   ....*....|
gi 1701944567  182 PRRRRPLNSV 191
Cdd:smart01024 161 PRRKRPLSSV 170
BCS1_N pfam08740
BCS1 N terminal; This domain is found at the N terminal of the mitochondrial ATPase BSC1. It ...
 25-191 3.64e-56

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.


Pssm-ID: 462583  Cd Length: 178  Bit Score: 182.83  E-value: 3.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567  25 VGTALALARKGVQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRH--STRTQHLSVETSYLQH------ESGRISTKFE 96
Cdd:pfam08740   1 LGALLAALRRGLRSLWSLLRRRFLSTVEIRSDDESYDWVLAWLSQQpfWRRSRSLSAETRTNSRsdddddDDGSKKKPLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567  97 FVPSPGNHFIWYRGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAV---- 172
Cdd:pfam08740  81 YTPGFGTHYFWYKGRWFAVSRERESSSSDLATGSPRETLTLSCLGRSPEPLKELLEEARELYLKKDEGKTVIYRAWrdgy 160

                         170
                  ....*....|....*....
gi 1701944567 173 GSEWRPFGYpRRRRPLNSV 191
Cdd:pfam08740 161 GGSWRRVGS-RPKRPLSTV 178
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 226-355 3.38e-19

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: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 226 YLLYGPPGCGKSSFITALAGEL-----EHSICLLSLTDSSLSDDRLNHLLSVAPQQ--SLVLLEDVDAAFLSRDlavenp 298
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELgapfiEISGSELVSKYVGESEKRLRELFEAAKKLapCVIFIDEIDALAGSRG------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1701944567 299 VKYQGLGRLTFSGLLNALDGVASTEAR-IVFMTTNHVDRLDPALIrpGRVDLKEYVGY 355
Cdd:pfam00004  75 SGGDSESRRVVNQLLTELDGFTSSNSKvIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 196-354 2.13e-16

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: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 196 GLaDRIVRDVQEFID----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSIcllsltdsslSDDRLNHLLS 271
Cdd:COG1222    82 GL-DEQIEEIREAVElplkNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPF----------IRVRGSELVS 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 272 -------------------VAPqqSLVLLEDVDAAFLSRDLAVENpvkyqGLGRLTFSGLLNALDGVASTEARIVFMTTN 332
Cdd:COG1222   151 kyigegarnvrevfelareKAP--SIIFIDEIDAIAARRTDDGTS-----GEVQRTVNQLLAELDGFESRGDVLIIAATN 223

                         170       180
                  ....*....|....*....|..
gi 1701944567 333 HVDRLDPALIRPGRVDLKEYVG 354
Cdd:COG1222   224 RPDLLDPALLRPGRFDRVIEVP 245
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 185-350 7.08e-13

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 69.80  E-value: 7.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 185 RRPLNSVVLQQGLADRI--VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSL 261
Cdd:PTZ00361  176 KAPLESYADIGGLEQQIqeIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQ 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 262 SDD-----RLNHLLSVAPQQ--SLVLLEDVDAAFLSR---DLAVENPVKYqglgrlTFSGLLNALDGVASTEARIVFMTT 331
Cdd:PTZ00361  256 KYLgdgpkLVRELFRVAEENapSIVFIDEIDAIGTKRydaTSGGEKEIQR------TMLELLNQLDGFDSRGDVKVIMAT 329

                         170
                  ....*....|....*....
gi 1701944567 332 NHVDRLDPALIRPGRVDLK 350
Cdd:PTZ00361  330 NRIESLDPALIRPGRIDRK 348
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 196-350 2.27e-11

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: 65.50  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 196 GLADRI--VRDVQE--FIdNPKWYTDRGIPYRRGYLLYGPPGCGKssfiTALAGELEHSICLLSLTDSSLSDDRLN---- 267
Cdd:TIGR03689 186 GLGSQIeqIRDAVElpFL-HPELYREYGLKPPKGVLLYGPPGCGK----TLIAKAVANSLAARIGAEGGGKSYFLNikgp 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 268 HLLS-----------VAPQQS----------LVLLEDVDAAFLSRDLAV----ENPVKYQglgrltfsgLLNALDGVAST 322
Cdd:TIGR03689 261 ELLNkyvgeterqirLIFQRArekasegrpvIVFFDEMDSLFRTRGSGVssdvETTVVPQ---------LLAEIDGVESL 331

                         170       180
                  ....*....|....*....|....*...
gi 1701944567 323 EARIVFMTTNHVDRLDPALIRPGRVDLK 350
Cdd:TIGR03689 332 DNVIVIGASNREDMIDPAILRPGRLDVK 359
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 223-354 4.29e-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: 46.21  E-value: 4.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567  223 RRGYLLYGPPGCGKSSFITALAGEL------------EHSICLLSLTDSSLSDDRLNHLLSVA------------PQQSL 278
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppgggviyidgEDILEEVLDQLLLIIVGGKKASGSGElrlrlalalarkLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944567  279 VLLEDVDAAflsrdlavenpVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPgRVDLKEYVG 354
Cdd:smart00382  82 LILDEITSL-----------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLL 145
cell_div_CdvC NF041006
cell division protein CdvC;
224-248 5.35e-04

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 42.03  E-value: 5.35e-04
                          10        20
                  ....*....|....*....|....*
gi 1701944567 224 RGYLLYGPPGCGKSSFITALAGELE 248
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 ...
 201-353 2.24e-91

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: 2.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 201 IVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSLSDDRLNHLLSVAPQQSLVL 280
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLLNTAPKQSIIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1701944567 281 LEDVDAAFLSRDLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 353
Cdd:cd19510    81 LEDIDAAFESREHNKKNPSAYGGLSRVTFSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDMKIYM 153
BCS1_N smart01024
This domain is found at the N terminal of the mitochondrial ATPase BCS1. It encodes the import ...
 24-191 1.34e-83

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: 253.31  E-value: 1.34e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567   24 GVGTALALARKGVQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRH--STRTQHLSVETSYLQHESGRISTKFEFVPSP 101
Cdd:smart01024   2 LLGAAGAFLRRGISVAASLIRRRFLVTLEVPSKDESYAWLLEWLSQQpfRQRSRHLSVETSYTQHDNGKSSTSFSFVPGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567  102 GNHFIWYRGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFgY 181
Cdd:smart01024  82 GTHWFWYKGRWIWVTREREKTMADMRTGSPFETLTLTTLGRDRDVFKELLEEARELALKRTEGKTVIYTADGPEWRRF-A 160

                          170
                   ....*....|
gi 1701944567  182 PRRRRPLNSV 191
Cdd:smart01024 161 PRRKRPLSSV 170
BCS1_N pfam08740
BCS1 N terminal; This domain is found at the N terminal of the mitochondrial ATPase BSC1. It ...
 25-191 3.64e-56

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.


Pssm-ID: 462583  Cd Length: 178  Bit Score: 182.83  E-value: 3.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567  25 VGTALALARKGVQLGLVAFRRHYMITLEVPARDRSYAWLLSWLTRH--STRTQHLSVETSYLQH------ESGRISTKFE 96
Cdd:pfam08740   1 LGALLAALRRGLRSLWSLLRRRFLSTVEIRSDDESYDWVLAWLSQQpfWRRSRSLSAETRTNSRsdddddDDGSKKKPLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567  97 FVPSPGNHFIWYRGKWIRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAV---- 172
Cdd:pfam08740  81 YTPGFGTHYFWYKGRWFAVSRERESSSSDLATGSPRETLTLSCLGRSPEPLKELLEEARELYLKKDEGKTVIYRAWrdgy 160

                         170
                  ....*....|....*....
gi 1701944567 173 GSEWRPFGYpRRRRPLNSV 191
Cdd:pfam08740 161 GGSWRRVGS-RPKRPLSTV 178
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 201-350 5.88e-33

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: 5.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 201 IVRDVQEFIDNPKWYTD---RGIPYRRGYLLYGPPGCGKSSFITALAGELEH-----SICLLSLTDSSLSDDRLNHLLSV 272
Cdd:cd19481     1 LKASLREAVEAPRRGSRlrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLplivvKLSSLLSKYVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 273 APQQ--SLVLLEDVDAAFLSRDLAVENPVkyqglGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLK 350
Cdd:cd19481    81 ARRLapCILFIDEIDAIGRKRDSSGESGE-----LRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 226-355 3.38e-19

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: 3.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 226 YLLYGPPGCGKSSFITALAGEL-----EHSICLLSLTDSSLSDDRLNHLLSVAPQQ--SLVLLEDVDAAFLSRDlavenp 298
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELgapfiEISGSELVSKYVGESEKRLRELFEAAKKLapCVIFIDEIDALAGSRG------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1701944567 299 VKYQGLGRLTFSGLLNALDGVASTEAR-IVFMTTNHVDRLDPALIrpGRVDLKEYVGY 355
Cdd:pfam00004  75 SGGDSESRRVVNQLLTELDGFTSSNSKvIVIAATNRPDKLDPALL--GRFDRIIEFPL 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 196-354 2.13e-16

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: 2.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 196 GLaDRIVRDVQEFID----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSIcllsltdsslSDDRLNHLLS 271
Cdd:COG1222    82 GL-DEQIEEIREAVElplkNPELFRKYGIEPPKGVLLYGPPGTGKTLLAKAVAGELGAPF----------IRVRGSELVS 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 272 -------------------VAPqqSLVLLEDVDAAFLSRDLAVENpvkyqGLGRLTFSGLLNALDGVASTEARIVFMTTN 332
Cdd:COG1222   151 kyigegarnvrevfelareKAP--SIIFIDEIDAIAARRTDDGTS-----GEVQRTVNQLLAELDGFESRGDVLIIAATN 223

                         170       180
                  ....*....|....*....|..
gi 1701944567 333 HVDRLDPALIRPGRVDLKEYVG 354
Cdd:COG1222   224 RPDLLDPALLRPGRFDRVIEVP 245
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 202-353 1.50e-14

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: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 202 VRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGE-----LEHSICLLSLTDSSLSDDRLNHLLSVAPQQ 276
Cdd:cd19501    16 LKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEagvpfFSISGSDFVEMFVGVGASRVRDLFEQAKKN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 277 S--LVLLEDVDAAFLSRDLAV--ENPVKYQglgrlTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEY 352
Cdd:cd19501    96 ApcIVFIDEIDAVGRKRGAGLggGHDEREQ-----TLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLRPGRFDRQVY 170


                  .
gi 1701944567 353 V 353
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 ...
 196-348 1.92e-14

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: 70.78  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 196 GLADRIVRdVQEFID----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELE--------HSIcllSLTDSSLSD 263
Cdd:cd19503     4 GLDEQIAS-LKELIElplkYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGanflsisgPSI---VSKYLGESE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 264 DRLNHLLSVAP--QQSLVLLEDVDAAFLSRDLAVEnpvkyqGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPAL 341
Cdd:cd19503    80 KNLREIFEEARshAPSIIFIDEIDALAPKREEDQR------EVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPAL 153


                  ....*..
gi 1701944567 342 IRPGRVD 348
Cdd:cd19503   154 RRPGRFD 160
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 113-396 2.14e-14

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: 74.18  E-value: 2.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 113 IRVERSREMQMIDLQTGTPWESVTFTALGTDRKVFFNILEEARELALQQEEGKTVMYTAVGSEWRPFGYPRRRRPLNSVV 192
Cdd:COG0464    81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLG 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 193 LQQGLADRIVRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELE-----------------HSiclls 255
Cdd:COG0464   161 GLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGlplievdlsdlvskyvgET----- 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 256 ltdsslsDDRLNHLLSVAPQQS--LVLLEDVDAAFLSRDLAVEnpvkyqGLGRLTFSGLLNALDGVasTEARIVFMTTNH 333
Cdd:COG0464   236 -------EKNLREVFDKARGLApcVLFIDEADALAGKRGEVGD------GVGRRVVNTLLTEMEEL--RSDVVVIAATNR 300

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1701944567 334 VDRLDPALIRpgRVDLKEYVGYCSHWQLTQMFQRFYPGQAPSLAENFAEhVLRATNQISPAQV 396
Cdd:COG0464   301 PDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLDEDVDLEE-LAEATEGLSGADI 360
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 196-348 3.84e-14

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: 70.13  E-value: 3.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 196 GLADRIVRDVQEF----IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGEL-----EHSICLLSLTDSSLSDDRL 266
Cdd:cd19518     3 GGMDSTLKELCELlihpILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELkvpflKISATEIVSGVSGESEEKI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 267 NHLLSVAPQQS--LVLLEDVDAAFLSRDLAVENpvkyqgLGRLTFSGLLNALDGV----ASTEARIVFMTTNHVDRLDPA 340
Cdd:cd19518    83 RELFDQAISNApcIVFIDEIDAITPKRESAQRE------MERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDSLDPA 156


                  ....*...
gi 1701944567 341 LIRPGRVD 348
Cdd:cd19518   157 LRRAGRFD 164
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 185-350 7.08e-13

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 69.80  E-value: 7.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 185 RRPLNSVVLQQGLADRI--VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSL 261
Cdd:PTZ00361  176 KAPLESYADIGGLEQQIqeIKEAVELpLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQ 255

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 262 SDD-----RLNHLLSVAPQQ--SLVLLEDVDAAFLSR---DLAVENPVKYqglgrlTFSGLLNALDGVASTEARIVFMTT 331
Cdd:PTZ00361  256 KYLgdgpkLVRELFRVAEENapSIVFIDEIDAIGTKRydaTSGGEKEIQR------TMLELLNQLDGFDSRGDVKVIMAT 329

                         170
                  ....*....|....*....
gi 1701944567 332 NHVDRLDPALIRPGRVDLK 350
Cdd:PTZ00361  330 NRIESLDPALIRPGRIDRK 348
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 196-350 3.55e-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: 3.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 196 GLADRI--VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELE----HSICLLSLTDSSLSDDRLNH 268
Cdd:cd19502     7 GLDEQIreIREVVELpLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDatfiRVVGSELVQKYIGEGARLVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 269 -LLSVAPQQ--SLVLLEDVDAAFLSR---DLAVENPVKYqglgrlTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALI 342
Cdd:cd19502    87 eLFEMAREKapSIIFIDEIDAIGAKRfdsGTGGDREVQR------TMLELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160


                  ....*...
gi 1701944567 343 RPGRVDLK 350
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 ...
 203-353 6.17e-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: 63.46  E-value: 6.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 203 RDVQEFIDNPKWYTDR----GIPYRRGYLLYGPPGCGKSSFITALAGElehsicllsltdsslsdDRLN-------HLLS 271
Cdd:cd19511     3 RELKEAVEWPLKHPDAfkrlGIRPPKGVLLYGPPGCGKTLLAKALASE-----------------AGLNfisvkgpELFS 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 272 -------------------VAPqqSLVLLEDVDAAFLSRDLAVENPVKYQGLgrltfSGLLNALDGVASTEARIVFMTTN 332
Cdd:cd19511    66 kyvgeseravreifqkarqAAP--CIIFFDEIDSLAPRRGQSDSSGVTDRVV-----SQLLTELDGIESLKGVVVIAATN 138

                         170       180
                  ....*....|....*....|.
gi 1701944567 333 HVDRLDPALIRPGRVDLKEYV 353
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 ...
 205-353 1.60e-11

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: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 205 VQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSL-----SDDRLNHLLSVAPQQS-- 277
Cdd:cd19528     9 VQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTmwfgeSEANVRDIFDKARAAApc 88

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944567 278 LVLLEDVDAAFLSRDLAVENPvkyQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 353
Cdd:cd19528    89 VLFFDELDSIAKARGGNIGDA---GGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIYI 161
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 196-350 2.27e-11

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: 65.50  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 196 GLADRI--VRDVQE--FIdNPKWYTDRGIPYRRGYLLYGPPGCGKssfiTALAGELEHSICLLSLTDSSLSDDRLN---- 267
Cdd:TIGR03689 186 GLGSQIeqIRDAVElpFL-HPELYREYGLKPPKGVLLYGPPGCGK----TLIAKAVANSLAARIGAEGGGKSYFLNikgp 260

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 268 HLLS-----------VAPQQS----------LVLLEDVDAAFLSRDLAV----ENPVKYQglgrltfsgLLNALDGVAST 322
Cdd:TIGR03689 261 ELLNkyvgeterqirLIFQRArekasegrpvIVFFDEMDSLFRTRGSGVssdvETTVVPQ---------LLAEIDGVESL 331

                         170       180
                  ....*....|....*....|....*...
gi 1701944567 323 EARIVFMTTNHVDRLDPALIRPGRVDLK 350
Cdd:TIGR03689 332 DNVIVIGASNREDMIDPAILRPGRLDVK 359
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 212-353 7.11e-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: 7.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 212 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGElehsicllslTDSSLSDDRLNHLLS-------------------V 272
Cdd:cd19529    16 PEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATE----------SNANFISVKGPELLSkwvgesekaireifrkarqV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 273 APqqSLVLLEDVDAAFLSRDLAVENPVKYQGLGRltfsgLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEY 352
Cdd:cd19529    86 AP--CVIFFDEIDSIAPRRGTTGDSGVTERVVNQ-----LLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158


                  .
gi 1701944567 353 V 353
Cdd:cd19529   159 I 159
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
202-354 4.11e-10

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 61.59  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 202 VRDVQEFIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGE-----LEHSICLLSLTDSSLSDDRLNHLLSVAPQQ 276
Cdd:PRK10733  164 VAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEakvpfFTISGSDFVEMFVGVGASRVRDMFEQAKKA 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 277 S--LVLLEDVDAAFLSRDlavenpvkyQGLG------RLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 348
Cdd:PRK10733  244 ApcIIFIDEIDAVGRQRG---------AGLGgghderEQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFD 314


                  ....*.
gi 1701944567 349 LKEYVG 354
Cdd:PRK10733  315 RQVVVG 320
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 209-353 9.84e-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: 57.11  E-value: 9.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 209 IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALA--------------------GELEHSIcllsltdsslsddRLNH 268
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVAnesganfisvkgpellnkyvGESERAV-------------RQVF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 269 LLSVAPQQSLVLLEDVDAAFLSRDLAVEnpvkyQGLGRLTfSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 348
Cdd:cd19530    83 QRARASAPCVIFFDEVDALVPKRGDGGS-----WASERVV-NQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLD 156


                  ....*
gi 1701944567 349 LKEYV 353
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 ...
 212-348 1.37e-09

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: 56.67  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 212 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSslsddrLNHLLSVAPQQSLVLLEDVDAA---- 287
Cdd:cd19526    16 PKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPEL------LNKYIGASEQNVRDLFSRAQSAkpci 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1701944567 288 --FLSRD-LAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 348
Cdd:cd19526    90 lfFDEFDsIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLD 153
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 202-348 1.94e-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: 59.54  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 202 VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLL-----SLTDSSLSDDRLNHLLSVAPQ 275
Cdd:TIGR01243 190 IREMVELpMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISIngpeiMSKYYGESEERLREIFKEAEE 269

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1701944567 276 Q--SLVLLEDVDAAFLSRDLAVENpvkyqgLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 348
Cdd:TIGR01243 270 NapSIIFIDEIDAIAPKREEVTGE------VEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFD 338
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 212-350 3.07e-09

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 58.24  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 212 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSslsddrLNHLLSVAPQQ-------------SL 278
Cdd:PTZ00454  168 PELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEF------VQKYLGEGPRMvrdvfrlarenapSI 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1701944567 279 VLLEDVDAAFLSR-------DLAVEnpvkyqglgRLTFSgLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLK 350
Cdd:PTZ00454  242 IFIDEVDSIATKRfdaqtgaDREVQ---------RILLE-LLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRK 310
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 202-348 3.50e-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: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 202 VRDVQEF-IDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLL-----SLTDSSLSDDRLNHLLSVAPQ 275
Cdd:cd19519    12 IREMVELpLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLIngpeiMSKLAGESESNLRKAFEEAEK 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944567 276 Q--SLVLLEDVDAAFLSRDlavenpvKYQG-LGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 348
Cdd:cd19519    92 NapAIIFIDEIDAIAPKRE-------KTHGeVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFD 160
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 212-353 6.63e-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: 6.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 212 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEHSICLLSLTDSSL-----SDDRLNHLLSVAPQQS--LVLLEDV 284
Cdd:TIGR01243 476 PEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEILSkwvgeSEKAIREIFRKARQAApaIIFFDEI 555

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1701944567 285 DAAFLSR----DLAVENPVKYQglgrltfsgLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLKEYV 353
Cdd:TIGR01243 556 DAIAPARgarfDTSVTDRIVNQ---------LLTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILV 619
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
188-350 2.87e-08

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 54.12  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 188 LNSVVLQQGLADRIVRDVQEF--IDNPKWYtdrGIPYRRGYLLYGPPGCGKSSFITALAGELE--------HSIcllSLT 257
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELrrRENLRKF---GLWPPRKILFYGPPGTGKTMLAEALAGELKlplltvrlDSL---IGS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 258 DSSLSDDRLNHLLSVAPQQSLVLLED-VDAAFLSRDLavENPVKYqgLGRLTfSGLLNALDGVASteaRIVFM-TTNHVD 335
Cdd:COG1223    75 YLGETARNLRKLFDFARRAPCVIFFDeFDAIAKDRGD--QNDVGE--VKRVV-NALLQELDGLPS---GSVVIaATNHPE 146

                         170
                  ....*....|....*
gi 1701944567 336 RLDPALIRpgRVDLK 350
Cdd:COG1223   147 LLDSALWR--RFDEV 159
ftsH CHL00176
cell division protein; Validated
 208-348 8.12e-08

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 54.29  E-value: 8.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 208 FIDNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELE---HSI--CLLSLTDSSLSDDRLNHLLSVAPQQS--LVL 280
Cdd:CHL00176  201 FLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEvpfFSIsgSEFVEMFVGVGAARVRDLFKKAKENSpcIVF 280

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 281 LEDVDAAFLSRDLAVE--NPVKYQglgrlTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 348
Cdd:CHL00176  281 IDEIDAVGRQRGAGIGggNDEREQ-----TLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFD 345
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 199-353 1.43e-07

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: 50.97  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 199 DRIVRDVQEFIDNPKWYTDrGIPYRRGYLLYGPPGCGKSSFITALAGELEHS---------ICLLSLTDSSLSDDRLNHL 269
Cdd:cd19527     3 KEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNflsvkgpelINMYIGESEANVREVFQKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 270 LSVAPqqSLVLLEDVDAAFLSRDlaveNPVKYQGLGRLTFSGLLNALDGVASTEARI-VFMTTNHVDRLDPALIRPGRVD 348
Cdd:cd19527    82 RDAKP--CVIFFDELDSLAPSRG----NSGDSGGVMDRVVSQLLAELDGMSSSGQDVfVIGATNRPDLLDPALLRPGRFD 155


                  ....*
gi 1701944567 349 LKEYV 353
Cdd:cd19527   156 KLLYL 160
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 212-348 1.80e-07

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: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 212 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELEH------------SICLLSLTDSSLSDDRLNHLLSVAPQQSLV 279
Cdd:cd19517    23 PEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSKggqkvsffmrkgADCLSKWVGEAERQLRLLFEEAYRMQPSII 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1701944567 280 LLEDVDAaflsrdLAVENPVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVD 348
Cdd:cd19517   103 FFDEIDG------LAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRRPGRFD 165
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 199-355 7.87e-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: 48.30  E-value: 7.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 199 DRIVRDVQEFIDNPKWytdrgipyrRGYLLYGPPGCGKSSFITALAGELEHSIcllsltdssLSDDRLNHLLSVapqQSL 278
Cdd:cd00009     4 EEAIEALREALELPPP---------KNLLLYGPPGTGKTTLARAIANELFRPG---------APFLYLNASDLL---EGL 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 279 VLLEDVDAAFLSRDLAVENPVKY--------QGLGRLTFSGLLNAL----DGVASTEARIVFMTTNHVDRLDPALIRPGR 346
Cdd:cd00009    63 VVAELFGHFLVRLLFELAEKAKPgvlfideiDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDR 142


                  ....*....
gi 1701944567 347 VDLKEYVGY 355
Cdd:cd00009   143 LDIRIVIPL 151
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 219-350 1.63e-06

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: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 219 GIPYRRGYLLYGPPGCGKS---------------------SFITALAGELEHSIcllslTDSSLSDDRLNHLLSVAPQQS 277
Cdd:cd19504    31 GCKHVKGILLYGPPGTGKTlmarqigkmlnarepkivngpEILNKYVGESEANI-----RKLFADAEEEQRRLGANSGLH 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1701944567 278 LVLLEDVDAAFLSRDLAVENpvkyQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPGRVDLK 350
Cdd:cd19504   106 IIIFDEIDAICKQRGSMAGS----TGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQ 174
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
202-348 1.96e-06

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 50.04  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 202 VRDVQEFIDNPKWYTDRG--IPyrRGYLLYGPPGCGKssfiT----ALAGElehsicllsltdsslsddrlnhllsvApq 275
Cdd:COG0465   154 LQEIVDFLKDPEKFTRLGakIP--KGVLLVGPPGTGK----TllakAVAGE--------------------------A-- 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 276 qslvlledvDAAFLS------------------RDL------------------AVenpvkyqglGRLTFSGL------- 312
Cdd:COG0465   200 ---------GVPFFSisgsdfvemfvgvgasrvRDLfeqakknapciifideidAV---------GRQRGAGLggghder 261

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1701944567 313 ---LNAL----DGVASTEARIVFMTTNHVDRLDPALIRPGRVD 348
Cdd:COG0465   262 eqtLNQLlvemDGFEGNEGVIVIAATNRPDVLDPALLRPGRFD 304
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 223-354 4.29e-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: 46.21  E-value: 4.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567  223 RRGYLLYGPPGCGKSSFITALAGEL------------EHSICLLSLTDSSLSDDRLNHLLSVA------------PQQSL 278
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELgppgggviyidgEDILEEVLDQLLLIIVGGKKASGSGElrlrlalalarkLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1701944567  279 VLLEDVDAAflsrdlavenpVKYQGLGRLTFSGLLNALDGVASTEARIVFMTTNHVDRLDPALIRPgRVDLKEYVG 354
Cdd:smart00382  82 LILDEITSL-----------LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLL 145
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 219-348 3.06e-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: 43.90  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 219 GIPYRRGYLLYGPPGCGKSSFITALAGE-----LEHSICLLSLTDSSLSDDRLNHLLSVAPQQS--LVLLEDVDAAFLSR 291
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVwqlplLRLDMGRLFGGLVGESESRLRQMIQTAEAIApcVLWIDEIEKGFSNA 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1701944567 292 DLAVEnpvkyQGLGRLTFSGLLNALdgvaSTEARIVFM--TTNHVDRLDPALIRPGRVD 348
Cdd:cd19507   107 DSKGD-----SGTSSRVLGTFLTWL----QEKKKPVFVvaTANNVQSLPPELLRKGRFD 156
PRK04195 PRK04195
replication factor C large subunit; Provisional
 186-247 3.10e-05

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 46.07  E-value: 3.10e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1701944567 186 RP--LNSVVLQqglaDRIVRDVQEFIDNpkWytDRGIPyRRGYLLYGPPGCGKSSFITALAGEL 247
Cdd:PRK04195    9 RPktLSDVVGN----EKAKEQLREWIES--W--LKGKP-KKALLLYGPPGVGKTSLAHALANDY 63
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 196-348 3.59e-05

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 45.59  E-value: 3.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 196 GLADRIvRDVQEFID----NPKWYTDRGIPYRRGYLLYGPPGCGK------------SSFITALAGEL------EHSicl 253
Cdd:PRK03992  135 GLEEQI-REVREAVElplkKPELFEEVGIEPPKGVLLYGPPGTGKtllakavahetnATFIRVVGSELvqkfigEGA--- 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 254 lsltdsslsddRLNH-LLSVAPQQ--SLVLLEDVDAAFLSR-------DLAVEnpvkyqglgRlTFSGLLNALDGVAST- 322
Cdd:PRK03992  211 -----------RLVReLFELAREKapSIIFIDEIDAIAAKRtdsgtsgDREVQ---------R-TLMQLLAEMDGFDPRg 269

                         170       180
                  ....*....|....*....|....*.
gi 1701944567 323 EARIVfMTTNHVDRLDPALIRPGRVD 348
Cdd:PRK03992  270 NVKII-AATNRIDILDPAILRPGRFD 294
cell_div_CdvC NF041006
cell division protein CdvC;
224-248 5.35e-04

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 42.03  E-value: 5.35e-04
                          10        20
                  ....*....|....*....|....*
gi 1701944567 224 RGYLLYGPPGCGKSSFITALAGELE 248
Cdd:NF041006  135 RGILLYGPPGCGKTMLAAAVANEID 159
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 212-248 2.90e-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: 38.30  E-value: 2.90e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1701944567 212 PKWYTDRGIPYRrGYLLYGPPGCGKSSFITALAGELE 248
Cdd:cd19521    30 PHLFTGNRKPWS-GILLYGPPGTGKSYLAKAVATEAN 65
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 224-246 3.09e-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: 3.09e-03
                          10        20
                  ....*....|....*....|...
gi 1701944567 224 RGYLLYGPPGCGKSSFITALAGE 246
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 ...
 199-343 4.12e-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: 37.72  E-value: 4.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1701944567 199 DRIVRDVQEFIDNPKWYTD-----RGIPyrRGYLLYGPPGCGKSSFITALAGEL-------EHSICLLSLTDSSLSDDRL 266
Cdd:cd19509     5 DDAKEALKEAVILPSLRPDlfpglRGPP--RGILLYGPPGTGKTLLARAVASESgstffsiSASSLVSKWVGESEKIVRA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1701944567 267 NHLLSVAPQQSLVLLEDVDaAFLSRDLAVEnpvkYQGLGRLTfSGLLNALDGV-ASTEARIVFM-TTNHVDRLDPALIR 343
Cdd:cd19509    83 LFALARELQPSIIFIDEID-SLLSERGSGE----HEASRRVK-TEFLVQMDGVlNKPEDRVLVLgATNRPWELDEAFLR 155
 
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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