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Conserved domains on  [gi|1126202629|ref|XP_019634723|]
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PREDICTED: LOW QUALITY PROTEIN: mitochondrial chaperone BCS1-like [Branchiostoma belcheri]

Protein Classification

mitochondrial chaperone BCS1( domain architecture ID 16123122)

mitochondrial chaperone BCS1, an AAA (ATPases Associated with diverse cellular Activities) protein of the mitochondria with a role in the biogenesis of the respiratory chain

CATH:  3.40.50.300
Gene Ontology:  GO:0016020|GO:0005524|GO:0016887
PubMed:  31988523|24361883|22575765|31988523
TCDB:  3.A.28

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 1.47e-104

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: 306.20  E-value: 1.47e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 201 ILQDVKEFISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSERGLSDDRLNHLLSVAPQQSIIL 280
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLLNTAPKQSIIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126202629 281 LEDIDAAFVSRELTPQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKEYI 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 2.08e-86

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: 260.24  E-value: 2.08e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629   24 GVGAGLAVLRKGSQFGMVAFRRHCMITLEIPSKDKSYHWLLQRITQN--AQRTQHLSVDTTFQQHDSGKISTRFDFVPSP 101
Cdd:smart01024   2 LLGAAGAFLRRGISVAASLIRRRFLVTLEVPSKDESYAWLLEWLSQQpfRQRSRHLSVETSYTQHDNGKSSTSFSFVPGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629  102 GTHFFWYKNNWIRIERTREKQMVDLHHGTPWETVQLTALGRNREMFFEILNEARELALQRTEGKTVMYTAMGPEWRQFgY 181
Cdd:smart01024  82 GTHWFWYKGRWIWVTREREKTMADMRTGSPFETLTLTTLGRDRDVFKELLEEARELALKRTEGKTVIYTADGPEWRRF-A 160

                          170
                   ....*....|
gi 1126202629  182 PRKRRPLSSV 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 1.47e-104

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: 306.20  E-value: 1.47e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 201 ILQDVKEFISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSERGLSDDRLNHLLSVAPQQSIIL 280
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLLNTAPKQSIIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126202629 281 LEDIDAAFVSRELTPQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKEYI 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 2.08e-86

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: 260.24  E-value: 2.08e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629   24 GVGAGLAVLRKGSQFGMVAFRRHCMITLEIPSKDKSYHWLLQRITQN--AQRTQHLSVDTTFQQHDSGKISTRFDFVPSP 101
Cdd:smart01024   2 LLGAAGAFLRRGISVAASLIRRRFLVTLEVPSKDESYAWLLEWLSQQpfRQRSRHLSVETSYTQHDNGKSSTSFSFVPGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629  102 GTHFFWYKNNWIRIERTREKQMVDLHHGTPWETVQLTALGRNREMFFEILNEARELALQRTEGKTVMYTAMGPEWRQFgY 181
Cdd:smart01024  82 GTHWFWYKGRWIWVTREREKTMADMRTGSPFETLTLTTLGRDRDVFKELLEEARELALKRTEGKTVIYTADGPEWRRF-A 160

                          170
                   ....*....|
gi 1126202629  182 PRKRRPLSSV 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 1.85e-58

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: 189.00  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629  25 VGAGLAVLRKGSQFGMVAFRRHCMITLEIPSKDKSYHWLLQRITQN--AQRTQHLSVDTTFQQH------DSGKISTRFD 96
Cdd:pfam08740   1 LGALLAALRRGLRSLWSLLRRRFLSTVEIRSDDESYDWVLAWLSQQpfWRRSRSLSAETRTNSRsdddddDDGSKKKPLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629  97 FVPSPGTHFFWYKNNWIRIERTREKQMVDLHHGTPWETVQLTALGRNREMFFEILNEARELALQRTEGKTVMYTAM---- 172
Cdd:pfam08740  81 YTPGFGTHYFWYKGRWFAVSRERESSSSDLATGSPRETLTLSCLGRSPEPLKELLEEARELYLKKDEGKTVIYRAWrdgy 160

                         170
                  ....*....|....*....
gi 1126202629 173 GPEWRQFGYpRKRRPLSSV 191
Cdd:pfam08740 161 GGSWRRVGS-RPKRPLSTV 178
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 226-354 1.57e-26

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: 103.06  E-value: 1.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 226 YLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSVAPQQ--SIILLEDIDAAFVSREltpqek 298
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSElvskyVGESEKRLRELFEAAKKLapCVIFIDEIDALAGSRG------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1126202629 299 AAYQGMGRLTFSGLLNALDGVASTEAR-IVFMTTNFIDRLDPALIrpGRVDMKEYIG 354
Cdd:pfam00004  75 SGGDSESRRVVNQLLTELDGFTSSNSKvIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 152-366 1.68e-23

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 100.08  E-value: 1.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 152 NEARELALQRTEGKTVMYTAMGPEWRQfgyPRKRRP---LSSVILHEGQADRILQDVKEFISNPKWYTDRGIPYRRGYLL 228
Cdd:COG1222    41 LLEEAPALLLNDANLTQKRLGTPRGTA---VPAESPdvtFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 229 YGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLL----SVAPqqSIILLEDIDAAFVSRELTPQEka 299
Cdd:COG1222   118 YGPPGTGKTLLAKAVAGELGAPFIRVRGSElvskyIGEGARNVREVFelarEKAP--SIIFIDEIDAIAARRTDDGTS-- 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126202629 300 ayqGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKEYIGHASEHQLREMFR 366
Cdd:COG1222   194 ---GEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILK 257
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 202-350 7.32e-17

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 82.13  E-value: 7.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 202 LQDVKEFI----SNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSV 272
Cdd:PTZ00361  192 IQEIKEAVelplTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSEliqkyLGDGPKLVRELFRV 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 273 APQQ--SIILLEDIDAAFVSRELTPQ--EKAAYQGMGRLtfsglLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVD 348
Cdd:PTZ00361  272 AEENapSIVFIDEIDAIGTKRYDATSggEKEIQRTMLEL-----LNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRID 346


                  ..
gi 1126202629 349 MK 350
Cdd:PTZ00361  347 RK 348
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 202-409 8.14e-15

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: 76.48  E-value: 8.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 202 LQDVKEFIS----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSV 272
Cdd:TIGR01243 187 KEKIREMVElpmkHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEimskyYGESEERLREIFKE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 273 APQQ--SIILLEDIDAafvsreLTPQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMK 350
Cdd:TIGR01243 267 AEENapSIIFIDEIDA------IAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFDRE 340

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 351 EYIGHASEHQLREMFRRFYPDQPQARSQEF-----------ASKVAAHGKDISIALVQGFFMLNKSDPDA 409
Cdd:TIGR01243 341 IVIRVPDKRARKEILKVHTRNMPLAEDVDLdklaevthgfvGADLAALAKEAAMAALRRFIREGKINFEA 410
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 223-354 1.03e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.14  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629  223 RRGYLLYGPPGCGKSSFITALAGELQ---YSICLMNLSERGLSDDRLNHLLSV---------------------APQQSI 278
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGppgGGVIYIDGEDILEEVLDQLLLIIVggkkasgsgelrlrlalalarKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126202629  279 ILLEDIDAAFVSRELtpqekaayqgmGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPgRVDMKEYIG 354
Cdd:smart00382  82 LILDEITSLLDAEQE-----------ALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLL 145
cell_div_CdvC NF041006
cell division protein CdvC;
202-247 1.93e-04

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 43.18  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1126202629 202 LQDVKEFISNPKWYTDR-------GIPyrRGYLLYGPPGCGKSSFITALAGEL 247
Cdd:NF041006  108 LEDVKEALKEAIVYPSKrpdlfplGWP--RGILLYGPPGCGKTMLAAAVANEI 158
 
Name Accession Description Interval E-value
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 201-353 1.47e-104

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: 306.20  E-value: 1.47e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 201 ILQDVKEFISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSERGLSDDRLNHLLSVAPQQSIIL 280
Cdd:cd19510     1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICDLNLSEVVLTDDRLNHLLNTAPKQSIIL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126202629 281 LEDIDAAFVSRELTPQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKEYI 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 2.08e-86

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: 260.24  E-value: 2.08e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629   24 GVGAGLAVLRKGSQFGMVAFRRHCMITLEIPSKDKSYHWLLQRITQN--AQRTQHLSVDTTFQQHDSGKISTRFDFVPSP 101
Cdd:smart01024   2 LLGAAGAFLRRGISVAASLIRRRFLVTLEVPSKDESYAWLLEWLSQQpfRQRSRHLSVETSYTQHDNGKSSTSFSFVPGP 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629  102 GTHFFWYKNNWIRIERTREKQMVDLHHGTPWETVQLTALGRNREMFFEILNEARELALQRTEGKTVMYTAMGPEWRQFgY 181
Cdd:smart01024  82 GTHWFWYKGRWIWVTREREKTMADMRTGSPFETLTLTTLGRDRDVFKELLEEARELALKRTEGKTVIYTADGPEWRRF-A 160

                          170
                   ....*....|
gi 1126202629  182 PRKRRPLSSV 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 1.85e-58

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: 189.00  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629  25 VGAGLAVLRKGSQFGMVAFRRHCMITLEIPSKDKSYHWLLQRITQN--AQRTQHLSVDTTFQQH------DSGKISTRFD 96
Cdd:pfam08740   1 LGALLAALRRGLRSLWSLLRRRFLSTVEIRSDDESYDWVLAWLSQQpfWRRSRSLSAETRTNSRsdddddDDGSKKKPLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629  97 FVPSPGTHFFWYKNNWIRIERTREKQMVDLHHGTPWETVQLTALGRNREMFFEILNEARELALQRTEGKTVMYTAM---- 172
Cdd:pfam08740  81 YTPGFGTHYFWYKGRWFAVSRERESSSSDLATGSPRETLTLSCLGRSPEPLKELLEEARELYLKKDEGKTVIYRAWrdgy 160

                         170
                  ....*....|....*....
gi 1126202629 173 GPEWRQFGYpRKRRPLSSV 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 ...
 201-353 2.86e-38

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: 135.49  E-value: 2.86e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 201 ILQDVKEFISNPKWYTD---RGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSV 272
Cdd:cd19481     1 LKASLREAVEAPRRGSRlrrYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSllskyVGESEKNLRKIFER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 273 APQQ--SIILLEDIDAAFVSRELTpqekaAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMK 350
Cdd:cd19481    81 ARRLapCILFIDEIDAIGRKRDSS-----GESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEV 155


                  ...
gi 1126202629 351 EYI 353
Cdd:cd19481   156 IEF 158
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 226-354 1.57e-26

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: 103.06  E-value: 1.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 226 YLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSVAPQQ--SIILLEDIDAAFVSREltpqek 298
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSElvskyVGESEKRLRELFEAAKKLapCVIFIDEIDALAGSRG------ 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1126202629 299 AAYQGMGRLTFSGLLNALDGVASTEAR-IVFMTTNFIDRLDPALIrpGRVDMKEYIG 354
Cdd:pfam00004  75 SGGDSESRRVVNQLLTELDGFTSSNSKvIVIAATNRPDKLDPALL--GRFDRIIEFP 129
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 152-366 1.68e-23

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 100.08  E-value: 1.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 152 NEARELALQRTEGKTVMYTAMGPEWRQfgyPRKRRP---LSSVILHEGQADRILQDVKEFISNPKWYTDRGIPYRRGYLL 228
Cdd:COG1222    41 LLEEAPALLLNDANLTQKRLGTPRGTA---VPAESPdvtFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 229 YGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLL----SVAPqqSIILLEDIDAAFVSRELTPQEka 299
Cdd:COG1222   118 YGPPGTGKTLLAKAVAGELGAPFIRVRGSElvskyIGEGARNVREVFelarEKAP--SIIFIDEIDAIAARRTDDGTS-- 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126202629 300 ayqGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKEYIGHASEHQLREMFR 366
Cdd:COG1222   194 ---GEVQRTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILK 257
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 194-348 1.03e-21

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: 91.31  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 194 HEGQADRILQDVKEF----ISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQysICLMNLSE-------RGLS 262
Cdd:cd19518     1 DIGGMDSTLKELCELlihpILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELK--VPFLKISAteivsgvSGES 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 263 DDRLNHLLSVAPQQS--IILLEDIDAafvsreLTPQEKAAYQGMGRLTFSGLLNALDGV----ASTEARIVFMTTNFIDR 336
Cdd:cd19518    79 EEKIRELFDQAISNApcIVFIDEIDA------ITPKRESAQREMERRIVSQLLTCMDELnnekTAGGPVLVIGATNRPDS 152

                         170
                  ....*....|..
gi 1126202629 337 LDPALIRPGRVD 348
Cdd:cd19518   153 LDPALRRAGRFD 164
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 1.24e-21

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: 90.81  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 196 GQADRILQDVKEFIS----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMN----LSER-GLSDDRL 266
Cdd:cd19503     3 GGLDEQIASLKELIElplkYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISgpsiVSKYlGESEKNL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 267 NHLLSVAP--QQSIILLEDIDAafvsreLTPQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRP 344
Cdd:cd19503    83 REIFEEARshAPSIIFIDEIDA------LAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRP 156


                  ....
gi 1126202629 345 GRVD 348
Cdd:cd19503   157 GRFD 160
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 184-375 9.82e-21

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: 93.44  E-value: 9.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 184 KRRPLSSVILHEGQADRILQDVKEFISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE----- 258
Cdd:COG0464   152 REAILDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDlvsky 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 259 RGLSDDRLNHLLSVAPQQS--IILLEDIDAAFVSREltpqekAAYQGMGRLTFSGLLNALDGVasTEARIVFMTTNFIDR 336
Cdd:COG0464   232 VGETEKNLREVFDKARGLApcVLFIDEADALAGKRG------EVGDGVGRRVVNTLLTEMEEL--RSDVVVIAATNRPDL 303

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1126202629 337 LDPALIRpgRVDMKEYIGHASEHQLREMFRRFYPDQPQA 375
Cdd:COG0464   304 LDPALLR--RFDEIIFFPLPDAEERLEIFRIHLRKRPLD 340
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 202-353 1.90e-19

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: 84.98  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 202 LQDVKEFISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSVAPQQ 276
Cdd:cd19501    16 LKEVVEFLKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDfvemfVGVGASRVRDLFEQAKKN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 277 S--IILLEDIDAafVSREltpqeKAAYQGMGRL----TFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMK 350
Cdd:cd19501    96 ApcIVFIDEIDA--VGRK-----RGAGLGGGHDereqTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLRPGRFDRQ 168


                  ...
gi 1126202629 351 EYI 353
Cdd:cd19501   169 VYV 171
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 202-350 7.32e-17

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 82.13  E-value: 7.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 202 LQDVKEFI----SNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSV 272
Cdd:PTZ00361  192 IQEIKEAVelplTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSEliqkyLGDGPKLVRELFRV 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 273 APQQ--SIILLEDIDAAFVSRELTPQ--EKAAYQGMGRLtfsglLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVD 348
Cdd:PTZ00361  272 AEENapSIVFIDEIDAIGTKRYDATSggEKEIQRTMLEL-----LNQLDGFDSRGDVKVIMATNRIESLDPALIRPGRID 346


                  ..
gi 1126202629 349 MK 350
Cdd:PTZ00361  347 RK 348
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 209-353 8.69e-17

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: 77.32  E-value: 8.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 209 ISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSIC------LMNL----SERGLSD--DRLNhllSVAPqq 276
Cdd:cd19511    13 LKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFIsvkgpeLFSKyvgeSERAVREifQKAR---QAAP-- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126202629 277 SIILLEDIDAAFVSREltpQEKAAyqGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKEYI 353
Cdd:cd19511    88 CIIFFDEIDSLAPRRG---QSDSS--GVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 202-354 4.03e-16

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: 75.55  E-value: 4.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 202 LQDVKEFIS----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSV 272
Cdd:cd19519     9 LAQIREMVElplrHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEimsklAGESESNLRKAFEE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 273 APQQ--SIILLEDIDAAFVSRELTPQEkaayqgMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMK 350
Cdd:cd19519    89 AEKNapAIIFIDEIDAIAPKREKTHGE------VERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDRE 162


                  ....
gi 1126202629 351 EYIG 354
Cdd:cd19519   163 IDIG 166
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 196-350 5.92e-16

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 75.07  E-value: 5.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 196 GQADRILQDVKEFIS----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSER-----GLSDDRL 266
Cdd:cd19502     6 GGLDEQIREIREVVElplkHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELvqkyiGEGARLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 267 NHLLSVAPQQ--SIILLEDIDAAFVSRelTPQEKAAYQGMGRlTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRP 344
Cdd:cd19502    86 RELFEMAREKapSIIFIDEIDAIGAKR--FDSGTGGDREVQR-TMLELLNQLDGFDPRGNIKVIMATNRPDILDPALLRP 162


                  ....*.
gi 1126202629 345 GRVDMK 350
Cdd:cd19502   163 GRFDRK 168
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 202-409 8.14e-15

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: 76.48  E-value: 8.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 202 LQDVKEFIS----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSV 272
Cdd:TIGR01243 187 KEKIREMVElpmkHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEimskyYGESEERLREIFKE 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 273 APQQ--SIILLEDIDAafvsreLTPQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMK 350
Cdd:TIGR01243 267 AEENapSIIFIDEIDA------IAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIGATNRPDALDPALRRPGRFDRE 340

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 351 EYIGHASEHQLREMFRRFYPDQPQARSQEF-----------ASKVAAHGKDISIALVQGFFMLNKSDPDA 409
Cdd:TIGR01243 341 IVIRVPDKRARKEILKVHTRNMPLAEDVDLdklaevthgfvGADLAALAKEAAMAALRRFIREGKINFEA 410
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 203-353 4.97e-14

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: 69.46  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 203 QDVKEFISNPKWYTDR----GIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSER-----GLSDDRLNHLLSVA 273
Cdd:cd19528     3 RELQELVQYPVEHPDKflkfGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELltmwfGESEANVRDIFDKA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 274 PQQS--IILLEDIDAAFVSRELTPQEKAayqGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKE 351
Cdd:cd19528    83 RAAApcVLFFDELDSIAKARGGNIGDAG---GAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLI 159


                  ..
gi 1126202629 352 YI 353
Cdd:cd19528   160 YI 161
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 209-353 5.95e-14

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: 69.05  E-value: 5.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 209 ISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSIC------LMNL----SERGLsddRLNHLLSVAPQQSI 278
Cdd:cd19530    16 IKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFIsvkgpeLLNKyvgeSERAV---RQVFQRARASAPCV 92

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126202629 279 ILLEDIDAafvsreLTPQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKEYI 353
Cdd:cd19530    93 IFFDEVDA------LVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLYV 161
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 201-348 1.50e-13

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: 67.84  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 201 ILQDVKEFISN-PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSIC------LMN----LSERGLSdDRLNHL 269
Cdd:cd19526     4 ALEETIEWPSKyPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFIsvkgpeLLNkyigASEQNVR-DLFSRA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126202629 270 LSVAPqqSIILLEDIDAafvsreLTPQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVD 348
Cdd:cd19526    83 QSAKP--CILFFDEFDS------IAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLD 153
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
197-367 2.87e-13

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 71.60  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 197 QADRILQDVKEFISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQ---YSICLMNLSER--GLSDDRLNHLLS 271
Cdd:PRK10733  159 EAKEEVAELVEYLREPSRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKvpfFTISGSDFVEMfvGVGASRVRDMFE 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 272 VAPQQS--IILLEDIDAafVSREltpqeKAAYQGMG----RLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPG 345
Cdd:PRK10733  239 QAKKAApcIIFIDEIDA--VGRQ-----RGAGLGGGhderEQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPG 311

                         170       180
                  ....*....|....*....|....*.
gi 1126202629 346 RVDMKEYIG----HASEHQLREMFRR 367
Cdd:PRK10733  312 RFDRQVVVGlpdvRGREQILKVHMRR 337
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 203-353 3.85e-13

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: 66.75  E-value: 3.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 203 QDVKEFIS----NPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSER-----GLSDDRLNHLLSVA 273
Cdd:cd19529     3 QELKEAVEwpllKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELlskwvGESEKAIREIFRKA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 274 PQQS--IILLEDIDAAFVSRELTPQekaayQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKE 351
Cdd:cd19529    83 RQVApcVIFFDEIDSIAPRRGTTGD-----SGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLI 157


                  ..
gi 1126202629 352 YI 353
Cdd:cd19529   158 YI 159
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 203-350 1.66e-12

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 68.64  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 203 QDVKEFI----SNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSVA 273
Cdd:PTZ00454  155 QEIREAVelplTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEfvqkyLGEGPRMVRDVFRLA 234

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1126202629 274 PQQ--SIILLEDIDAAFVSRelTPQEKAAYQGMGRLTFSgLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMK 350
Cdd:PTZ00454  235 RENapSIIFIDEVDSIATKR--FDAQTGADREVQRILLE-LLNQMDGFDQTTNVKVIMATNRADTLDPALLRPGRLDRK 310
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
188-417 4.43e-12

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 65.68  E-value: 4.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 188 LSSVILHEgQADRILQDVKEFISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLS 262
Cdd:COG1223     1 LDDVVGQE-EAKKKLKLIIKELRRRENLRKFGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSligsyLGET 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 263 DDRLNHLLSVAPQQ-SIILLEDIDAAFVSR---ELTPQekaayqgMGRLTfSGLLNALDGVASteaRIVFM-TTNFIDRL 337
Cdd:COG1223    80 ARNLRKLFDFARRApCVIFFDEFDAIAKDRgdqNDVGE-------VKRVV-NALLQELDGLPS---GSVVIaATNHPELL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 338 DPALIRpgRVDMKEYIGHASEHQLREMFRRF---YPDQPQARSQEFASK-VAAHGKDI--------SIALVQGFFMLNKS 405
Cdd:COG1223   149 DSALWR--RFDEVIEFPLPDKEERKEILELNlkkFPLPFELDLKKLAKKlEGLSGADIekvlktalKKAILEDREKVTKE 226

                         250
                  ....*....|..
gi 1126202629 406 DPDAVIENIDKM 417
Cdd:COG1223   227 DLEEALKQRKER 238
ftsH CHL00176
cell division protein; Validated
 202-348 6.52e-12

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 67.38  E-value: 6.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 202 LQDVKEFISNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQ---YSICLMNLSER--GLSDDRLNHLLSVAPQQ 276
Cdd:CHL00176  195 FEEVVSFLKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEvpfFSISGSEFVEMfvGVGAARVRDLFKKAKEN 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1126202629 277 S--IILLEDIDAafVSReltpqEKAAYQGMGR----LTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVD 348
Cdd:CHL00176  275 SpcIVFIDEIDA--VGR-----QRGAGIGGGNdereQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAALLRPGRFD 345
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 212-419 7.40e-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: 67.04  E-value: 7.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 212 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSIClmnlSERGLSDDRLN----HLLS-----------VAPQQ 276
Cdd:TIGR03689 205 PELYREYGLKPPKGVLLYGPPGCGKTLIAKAVANSLAARIG----AEGGGKSYFLNikgpELLNkyvgeterqirLIFQR 280

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 277 S----------IILLEDIDAAFVSR--------ELT--PQekaayqgmgrltfsgLLNALDGVASTEARIVFMTTNFIDR 336
Cdd:TIGR03689 281 ArekasegrpvIVFFDEMDSLFRTRgsgvssdvETTvvPQ---------------LLAEIDGVESLDNVIVIGASNREDM 345

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 337 LDPALIRPGRVDMKEYIGHASEHQLREMFRRFY-PDQPqarsqeFASKVAAHGKDisialvqgffmlNKSDPDAVIEN-I 414
Cdd:TIGR03689 346 IDPAILRPGRLDVKIRIERPDAEAAADIFAKYLtDDLP------LPEDLAAHDGD------------REATAAALIQRvV 407


                  ....*
gi 1126202629 415 DKMWT 419
Cdd:TIGR03689 408 DALYA 412
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 212-391 9.84e-12

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: 66.85  E-value: 9.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 212 PKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-----RGLSDDRLNHLLSVAPQQS--IILLEDI 284
Cdd:TIGR01243 476 PEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEilskwVGESEKAIREIFRKARQAApaIIFFDEI 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 285 DAAFVSRELTPQEKAAYQGMGRLtfsglLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMKEYIGHASEHQLREM 364
Cdd:TIGR01243 556 DAIAPARGARFDTSVTDRIVNQL-----LTEMDGIQELSNVVVIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEI 630

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1126202629 365 FRRFYPDQPQARS---QEFASKVAAH-GKDI 391
Cdd:TIGR01243 631 FKIHTRSMPLAEDvdlEELAEMTEGYtGADI 661
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 199-343 7.95e-11

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: 60.44  E-value: 7.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 199 DRILQDVKEFISNPKWYTD-----RGIPyrRGYLLYGPPGCGKSSFITALAGELQysICLMNLSERGL-------SDDRL 266
Cdd:cd19509     5 DDAKEALKEAVILPSLRPDlfpglRGPP--RGILLYGPPGTGKTLLARAVASESG--STFFSISASSLvskwvgeSEKIV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 267 NHLLSVAP--QQSIILLEDIDAAFVSRELTPQEKAAyqgmgRLTfSGLLNALDGV-ASTEARIVFM-TTNFIDRLDPALI 342
Cdd:cd19509    81 RALFALARelQPSIIFIDEIDSLLSERGSGEHEASR-----RVK-TEFLVQMDGVlNKPEDRVLVLgATNRPWELDEAFL 154


                  .
gi 1126202629 343 R 343
Cdd:cd19509   155 R 155
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 199-354 9.62e-11

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


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 59.85  E-value: 9.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 199 DRILQDVKEFISNPKWytdrgipyrRGYLLYGPPGCGKSSFITALAGEL---QYSICLMNLSE----------RGLSDDR 265
Cdd:cd00009     4 EEAIEALREALELPPP---------KNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDlleglvvaelFGHFLVR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 266 LNHLLSVAPQQSIILLEDIDAafvsreltpqekaayqgMGRLTFSGLLNAL----DGVASTEARIVFMTTNFIDRLDPAL 341
Cdd:cd00009    75 LLFELAEKAKPGVLFIDEIDS-----------------LSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDR 137

                         170
                  ....*....|...
gi 1126202629 342 IRPGRVDMKEYIG 354
Cdd:cd00009   138 ALYDRLDIRIVIP 150
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 196-348 1.55e-10

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: 59.45  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 196 GQADRILQDVKEFISNPKWYTDRGIPYR----RGYLLYGPPGCGKSSFITALAGELQY------------SICL---MNL 256
Cdd:cd19517     3 GGLSHYINQLKEMVFFPLLYPEVFAKFKitppRGVLFHGPPGTGKTLMARALAAECSKggqkvsffmrkgADCLskwVGE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 257 SERGLsddRLNHLLSVAPQQSIILLEDIDAafvsreLTPQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDR 336
Cdd:cd19517    83 AERQL---RLLFEEAYRMQPSIIFFDEIDG------LAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDA 153

                         170
                  ....*....|..
gi 1126202629 337 LDPALIRPGRVD 348
Cdd:cd19517   154 LDPALRRPGRFD 165
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 199-353 6.46e-10

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: 57.52  E-value: 6.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 199 DRILQDVKEFISNPKWYTDrGIPYRRGYLLYGPPGCGKSSFITALAGELQYSIC------LMNLSeRGLSDDRLNHLLSV 272
Cdd:cd19527     3 KEILDTIQLPLEHPELFSS-GLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLsvkgpeLINMY-IGESEANVREVFQK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 273 APQQS--IILLEDIDAafvsreLTPQEKAayQG-----MGRLTfSGLLNALDGVASTEARI-VFMTTNFIDRLDPALIRP 344
Cdd:cd19527    81 ARDAKpcVIFFDELDS------LAPSRGN--SGdsggvMDRVV-SQLLAELDGMSSSGQDVfVIGATNRPDLLDPALLRP 151


                  ....*....
gi 1126202629 345 GRVDMKEYI 353
Cdd:cd19527   152 GRFDKLLYL 160
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 219-350 2.85e-09

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: 55.96  E-value: 2.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 219 GIPYRRGYLLYGPPGCGKssfiTALAGELQYsicLMNLSER-------------GLSDDRLNHLLSVAPQQS-------- 277
Cdd:cd19504    31 GCKHVKGILLYGPPGTGK----TLMARQIGK---MLNAREPkivngpeilnkyvGESEANIRKLFADAEEEQrrlgansg 103

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126202629 278 --IILLEDIDAAFVSReltpQEKAAYQGMGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPGRVDMK 350
Cdd:cd19504   104 lhIIIFDEIDAICKQR----GSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLEVQ 174
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
202-348 9.18e-09

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 57.35  E-value: 9.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 202 LQDVKEFISNPKWYTDRG--IPyrRGYLLYGPPGCGKssfiT----ALAGELQ---YSIclmnlSerGlSD--------- 263
Cdd:COG0465   154 LQEIVDFLKDPEKFTRLGakIP--KGVLLVGPPGTGK----TllakAVAGEAGvpfFSI-----S--G-SDfvemfvgvg 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 264 -----D-----RLNhllsvAPqqSIILLEDIDAafvsreltpqekaayqgMGRLTFSGL----------LNAL----DGV 319
Cdd:COG0465   220 asrvrDlfeqaKKN-----AP--CIIFIDEIDA-----------------VGRQRGAGLggghdereqtLNQLlvemDGF 275

                         170       180
                  ....*....|....*....|....*....
gi 1126202629 320 ASTEARIVFMTTNFIDRLDPALIRPGRVD 348
Cdd:COG0465   276 EGNEGVIVIAATNRPDVLDPALLRPGRFD 304
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 219-348 1.03e-08

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


Pssm-ID: 410915 [Multi-domain]  Cd Length: 161  Bit Score: 54.30  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 219 GIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSER-----GLSDDRLNHLLSVAPQQS--IILLEDIDAAFvsr 291
Cdd:cd19507    27 GLPTPKGLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLfgglvGESESRLRQMIQTAEAIApcVLWIDEIEKGF--- 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1126202629 292 elTPQEKAAYQGMGRLTFSGLLNALdgvaSTEARIVFM--TTNFIDRLDPALIRPGRVD 348
Cdd:cd19507   104 --SNADSKGDSGTSSRVLGTFLTWL----QEKKKPVFVvaTANNVQSLPPELLRKGRFD 156
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 199-348 4.42e-08

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 54.84  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 199 DRILQDVKEFI----SNPKWYTDRGIPYRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLSE-------------RGL 261
Cdd:PRK03992  137 EEQIREVREAVelplKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSElvqkfigegarlvREL 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 262 SD---DRlnhllsvAPqqSIILLEDIDAAFVSR--ELTPQEkAAYQgmgRlTFSGLLNALDGVAST-EARIVfMTTNFID 335
Cdd:PRK03992  217 FElarEK-------AP--SIIFIDEIDAIAAKRtdSGTSGD-REVQ---R-TLMQLLAEMDGFDPRgNVKII-AATNRID 281

                         170
                  ....*....|...
gi 1126202629 336 RLDPALIRPGRVD 348
Cdd:PRK03992  282 ILDPAILRPGRFD 294
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 209-353 8.61e-08

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: 51.79  E-value: 8.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 209 ISNPKWYTDRGIPYRrGYLLYGPPGCGKSSFITALAGELQ---YSICLMNLSER--GLSDDRLNHLLSVAPQQ--SIILL 281
Cdd:cd19521    27 VKFPHLFTGNRKPWS-GILLYGPPGTGKSYLAKAVATEANstfFSVSSSDLVSKwmGESEKLVKQLFAMARENkpSIIFI 105

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1126202629 282 EDIDAAFVSRELTPQEKAayqgmgRLTFSGLLNALDGVASTEARI-VFMTTNFIDRLDPALIRpgRVDMKEYI 353
Cdd:cd19521   106 DEVDSLCGTRGEGESEAS------RRIKTELLVQMNGVGNDSQGVlVLGATNIPWQLDSAIRR--RFEKRIYI 170
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 224-343 1.18e-07

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: 51.27  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 224 RGYLLYGPPGCGKSSFITALAGELQY---SICLMNLSER--GLSDDRLNHLLSVAP--QQSIILLEDIDAAFVSRELTPQ 296
Cdd:cd19520    36 KGVLLYGPPGCGKTMLAKATAKEAGArfiNLQVSSLTDKwyGESQKLVAAVFSLASklQPSIIFIDEIDSFLRQRSSTDH 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1126202629 297 EKAAyqgMGRLTFSGLLNALDgvASTEARIVFM-TTNFIDRLDPALIR 343
Cdd:cd19520   116 EATA---MMKAEFMSLWDGLS--TDGNCRVIVMgATNRPQDLDEAILR 158
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 193-353 1.36e-07

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


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 51.14  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 193 LHEgqADRILqdvKEFISNPKWYTD--RGI--PYRrGYLLYGPPGCGKSSFITALAGELQYSicLMNLSE-------RGL 261
Cdd:cd19522     5 LEE--AKKLL---EEAVVLPMWMPEffKGIrrPWK-GVLMVGPPGTGKTLLAKAVATECGTT--FFNVSSstltskyRGE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 262 SDDRLNHLLSVAP--QQSIILLEDIDaAFVSRELTPQEKAAyqgmGRLTFSGLLNALDGVASTEAR-------IVFMTTN 332
Cdd:cd19522    77 SEKLVRLLFEMARfyAPTTIFIDEID-SICSRRGTSEEHEA----SRRVKSELLVQMDGVGGASENddpskmvMVLAATN 151

                         170       180
                  ....*....|....*....|.
gi 1126202629 333 FIDRLDPALIRpgRVDMKEYI 353
Cdd:cd19522   152 FPWDIDEALRR--RLEKRIYI 170
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 223-354 1.03e-06

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.14  E-value: 1.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629  223 RRGYLLYGPPGCGKSSFITALAGELQ---YSICLMNLSERGLSDDRLNHLLSV---------------------APQQSI 278
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGppgGGVIYIDGEDILEEVLDQLLLIIVggkkasgsgelrlrlalalarKLKPDV 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126202629  279 ILLEDIDAAFVSRELtpqekaayqgmGRLTFSGLLNALDGVASTEARIVFMTTNFIDRLDPALIRPgRVDMKEYIG 354
Cdd:smart00382  82 LILDEITSLLDAEQE-----------ALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLL 145
PRK04195 PRK04195
replication factor C large subunit; Provisional
 184-257 8.71e-06

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 47.61  E-value: 8.71e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1126202629 184 KRRP--LSSVILHEGqadrILQDVKEFISNpkWytDRGIPyRRGYLLYGPPGCGKSSFITALAGELQYSICLMNLS 257
Cdd:PRK04195    7 KYRPktLSDVVGNEK----AKEQLREWIES--W--LKGKP-KKALLLYGPPGVGKTSLAHALANDYGWEVIELNAS 73
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 218-353 9.30e-06

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 46.13  E-value: 9.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 218 RGIPyrRGYLLYGPPGCGKSSF---ITALAGELQYSICLMNLSER--GLSDDRLNHLLSVA--PQQSIILLEDIDAAFVS 290
Cdd:cd19525    52 RGPP--KGILLFGPPGTGKTLIgkcIASQSGATFFSISASSLTSKwvGEGEKMVRALFSVArcKQPAVIFIDEIDSLLSQ 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1126202629 291 RELTPQEKAayqgmgRLTFSGLLNALDGV--ASTEARIVFMTTNFIDRLDPALIRpgRVDMKEYI 353
Cdd:cd19525   130 RGEGEHESS------RRIKTEFLVQLDGAttSSEDRILVVGATNRPQEIDEAARR--RLVKRLYI 186
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 224-343 1.43e-05

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


Pssm-ID: 410932 [Multi-domain]  Cd Length: 164  Bit Score: 45.23  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 224 RGYLLYGPPGCGKSSFITALAGELQ---YSICLMNLSER--GLSDDRLNHLLSVAP--QQSIILLEDIDAAFVSRELTPQ 296
Cdd:cd19524    34 RGLLLFGPPGNGKTMLAKAVAAESNatfFNISAASLTSKyvGEGEKLVRALFAVARelQPSIIFIDEVDSLLSERSEGEH 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1126202629 297 EKAayqgmgRLTFSGLLNALDGVAST-EARIVFM-TTNFIDRLDPALIR 343
Cdd:cd19524   114 EAS------RRLKTEFLIEFDGVQSNgDDRVLVMgATNRPQELDDAVLR 156
ycf46 CHL00195
Ycf46; Provisional
 216-400 3.50e-05

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 45.78  E-value: 3.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 216 TDRGIPYRRGYLLYGPPGCGKSSFITALAGELQysICLMNL-------SERGLSDDRLNHLLSVAPQQS--IILLEDIDA 286
Cdd:CHL00195  252 SNYGLPTPRGLLLVGIQGTGKSLTAKAIANDWQ--LPLLRLdvgklfgGIVGESESRMRQMIRIAEALSpcILWIDEIDK 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 287 AFvsrelTPQEKAAYQGMGRLTFSGLLNALdgvaSTEARIVFM--TTNFIDRLDPALIRPGRVDMKEYIGHASEHQLREM 364
Cdd:CHL00195  330 AF-----SNSESKGDSGTTNRVLATFITWL----SEKKSPVFVvaTANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKI 400

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1126202629 365 F----RRFYPDQPQARSQEFASKVAAH--GKDISIALVQGFF 400
Cdd:CHL00195  401 FkihlQKFRPKSWKKYDIKKLSKLSNKfsGAEIEQSIIEAMY 442
cell_div_CdvC NF041006
cell division protein CdvC;
202-247 1.93e-04

cell division protein CdvC;


Pssm-ID: 468935 [Multi-domain]  Cd Length: 371  Bit Score: 43.18  E-value: 1.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1126202629 202 LQDVKEFISNPKWYTDR-------GIPyrRGYLLYGPPGCGKSSFITALAGEL 247
Cdd:NF041006  108 LEDVKEALKEAIVYPSKrpdlfplGWP--RGILLYGPPGCGKTMLAAAVANEI 158
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 219-348 2.52e-04

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


Pssm-ID: 410913 [Multi-domain]  Cd Length: 161  Bit Score: 41.21  E-value: 2.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1126202629 219 GIPYRRGYLLYGPPGCGKSSFITALAG------------ELQYS---------ICLMNLSERGLsdDRLNHLLSVAPQQS 277
Cdd:cd19505     8 GLSPSKGILLIGSIETGRSYLIKSLAAnsyvplirislnKLLYNkpdfgnddwIDGMLILKESL--HRLNLQFELAKAMS 85

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1126202629 278 --IILLEDIDAAFVSRELTPQEKAAYqgmgrlTFSGLLNAL----DGVASTEARIVFMTTNFIDRLDPALIRPGRVD 348
Cdd:cd19505    86 pcIIWIPNIHELNVNRSTQNLEEDPK------LLLGLLLNYlsrdFEKSSTRNILVIASTHIPQKVDPALIAPNRLD 156
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 227-253 5.54e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 36.04  E-value: 5.54e-03
                          10        20
                  ....*....|....*....|....*..
gi 1126202629 227 LLYGPPGCGKSSFITALAGELQYSICL 253
Cdd:pfam00910   2 WLYGPPGCGKSTLAKYLARALLKKLGL 28
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 227-249 7.85e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 38.14  E-value: 7.85e-03
                          10        20
                  ....*....|....*....|...
gi 1126202629 227 LLYGPPGCGKSSFITALAGELQY 249
Cdd:PRK13342   40 ILWGPPGTGKTTLARIIAGATDA 62
 
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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