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Conserved domains on  [gi|4505725|ref|NP_000457|]
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peroxisomal ATPase PEX1 isoform 1 [Homo sapiens]

Protein Classification

PEX-2N and RecA-like_PEX1_r2 domain-containing protein( domain architecture ID 13760314)

protein containing domains PEX-2N, PEX-1N, and RecA-like_PEX1_r2

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CDC48 super family cl36852
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 595-1065 3.98e-107

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


The actual alignment was detected with superfamily member TIGR01243:

Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 355.37  E-value: 3.98e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     595 LLLTGGKGSGKSTLAKAICKEAfdklDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAglpavP 674
Cdd:TIGR01243  215 VLLYGPPGTGKTLLAKAVANEA----GAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIA-----P 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     675 EHEHSPDAVQSQRLAHALN--DMIKEfisMGSLVALIATSQSQqSLHPLLVSAQGvhiFQCVQHIQPPNQEQRCEILCNV 752
Cdd:TIGR01243  286 KREEVTGEVEKRVVAQLLTlmDGLKG---RGRVIVIGATNRPD-ALDPALRRPGR---FDREIVIRVPDKRARKEILKVH 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     753 IKNKLDCDinkftDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSR-----------QSI--STREKLVLTTLDFQKALR 819
Cdd:TIGR01243  359 TRNMPLAE-----DVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfiregkinfeaEEIpaEVLKELKVTMKDFMEALK 433

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     820 GFLPASLRSVNLHKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESR 899
Cdd:TIGR01243  434 MVEPSAIREVLVEVP-NVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESG 512

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     900 MNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHD-NTGVTDRVVNQLLTQLDGVEGLQGVY 978
Cdd:TIGR01243  513 ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVV 592

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     979 VLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEA 1058
Cdd:TIGR01243  593 VIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAA 672


                   ....*..
gi 4505725    1059 LHGMLLS 1065
Cdd:TIGR01243  673 LRESIGS 679
PEX-2N pfam09263
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a Cdc48 domain 2-like ...
 17-98 9.53e-45

Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a Cdc48 domain 2-like fold, with a beta-alpha-beta(3) arrangement. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substrate binding site, allowing for peroxisomal biogenesis, membrane fusion and protein translocation.


:

Pssm-ID: 462730  Cd Length: 83  Bit Score: 155.99  E-value: 9.53e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725      17 VTVAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSH-QPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLK 95
Cdd:pfam09263    1 VTVVFNNAKNCFLHLPSKLVSQLSLQENQALELSWGHgQPVFLSWTEGRHSSDQDENVVELNRQLGEKLGLKDGEQVFLR 80


                   ...
gi 4505725      96 PCS 98
Cdd:pfam09263   81 PCS 83
PEX-1N pfam09262
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi ...
 104-179 1.21e-31

Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi beta-barrel fold, similar in structure to the Cdc48 N-terminal domain. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substrate binding site, allowing for peroxisomal biogenesis, membrane fusion and protein translocation.


:

Pssm-ID: 462729  Cd Length: 77  Bit Score: 118.37  E-value: 1.21e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505725     104 QQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAAS-YGRLETDTKLLIQP 179
Cdd:pfam09262    1 TTVEVEPLTSDDWEILELHAEFLEDNLLSQVRVVSPGQILPVWVSGTTVARFRVTSIEPANSpFARLSPDTEVIVAP 77
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 595-1065 3.98e-107

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: 355.37  E-value: 3.98e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     595 LLLTGGKGSGKSTLAKAICKEAfdklDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAglpavP 674
Cdd:TIGR01243  215 VLLYGPPGTGKTLLAKAVANEA----GAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIA-----P 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     675 EHEHSPDAVQSQRLAHALN--DMIKEfisMGSLVALIATSQSQqSLHPLLVSAQGvhiFQCVQHIQPPNQEQRCEILCNV 752
Cdd:TIGR01243  286 KREEVTGEVEKRVVAQLLTlmDGLKG---RGRVIVIGATNRPD-ALDPALRRPGR---FDREIVIRVPDKRARKEILKVH 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     753 IKNKLDCDinkftDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSR-----------QSI--STREKLVLTTLDFQKALR 819
Cdd:TIGR01243  359 TRNMPLAE-----DVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfiregkinfeaEEIpaEVLKELKVTMKDFMEALK 433

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     820 GFLPASLRSVNLHKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESR 899
Cdd:TIGR01243  434 MVEPSAIREVLVEVP-NVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESG 512

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     900 MNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHD-NTGVTDRVVNQLLTQLDGVEGLQGVY 978
Cdd:TIGR01243  513 ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVV 592

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     979 VLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEA 1058
Cdd:TIGR01243  593 VIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAA 672


                   ....*..
gi 4505725    1059 LHGMLLS 1065
Cdd:TIGR01243  673 LRESIGS 679
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 848-1005 1.26e-104

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: 327.46  E-value: 1.26e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   848 VRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFI 927
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505725   928 RAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYC 1005
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVYC 158
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 800-1059 5.05e-93

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 302.31  E-value: 5.05e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   800 SISTREKLVLTTLDFQKALRGFLPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILL 879
Cdd:COG1222   38 ALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   880 YGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNT-GVTD 958
Cdd:COG1222  118 YGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTsGEVQ 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   959 RVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASV 1038
Cdd:COG1222  198 RTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKL 277

                        250       260
                 ....*....|....*....|.
gi 4505725  1039 TDSFTGADLKALLYNAQLEAL 1059
Cdd:COG1222  278 TEGFSGADLKAIVTEAGMFAI 298
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 832-1050 5.91e-67

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 231.64  E-value: 5.91e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    832 HKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELL 911
Cdd:PRK03992  124 ESP-NVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    912 SKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGvTDRVVN----QLLTQLDGVEGLQGVYVLAATSRPD 987
Cdd:PRK03992  203 QKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTS-GDREVQrtlmQLLAEMDGFDPRGNVKIIAATNRID 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505725    988 LIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKAL 1050
Cdd:PRK03992  282 ILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAI 344
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 877-1006 3.87e-49

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: 170.47  E-value: 3.87e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     877 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGV 956
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 4505725     957 TDRVVNQLLTQLDGVEGLQG-VYVLAATSRPDLIDPALLrpGRLDKCVYCP 1006
Cdd:pfam00004   81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
PEX-2N pfam09263
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a Cdc48 domain 2-like ...
 17-98 9.53e-45

Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a Cdc48 domain 2-like fold, with a beta-alpha-beta(3) arrangement. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substrate binding site, allowing for peroxisomal biogenesis, membrane fusion and protein translocation.


Pssm-ID: 462730  Cd Length: 83  Bit Score: 155.99  E-value: 9.53e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725      17 VTVAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSH-QPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLK 95
Cdd:pfam09263    1 VTVVFNNAKNCFLHLPSKLVSQLSLQENQALELSWGHgQPVFLSWTEGRHSSDQDENVVELNRQLGEKLGLKDGEQVFLR 80


                   ...
gi 4505725      96 PCS 98
Cdd:pfam09263   81 PCS 83
PEX-1N pfam09262
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi ...
 104-179 1.21e-31

Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi beta-barrel fold, similar in structure to the Cdc48 N-terminal domain. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substrate binding site, allowing for peroxisomal biogenesis, membrane fusion and protein translocation.


Pssm-ID: 462729  Cd Length: 77  Bit Score: 118.37  E-value: 1.21e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505725     104 QQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAAS-YGRLETDTKLLIQP 179
Cdd:pfam09262    1 TTVEVEPLTSDDWEILELHAEFLEDNLLSQVRVVSPGQILPVWVSGTTVARFRVTSIEPANSpFARLSPDTEVIVAP 77
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 877-1009 4.69e-14

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: 70.87  E-value: 4.69e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725      877 ILLYGPPGTGKTLLAGVIARESRMNFISVK-----------------GPELLSKYIGASEQAVRDIFIRAQAAKPCILFF 939
Cdd:smart00382    5 ILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDVLIL 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725      940 DEFESIaprrgHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPgRLDKCVYCPPPD 1009
Cdd:smart00382   85 DEITSL-----LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
 
Name Accession Description Interval E-value
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 595-1065 3.98e-107

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: 355.37  E-value: 3.98e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     595 LLLTGGKGSGKSTLAKAICKEAfdklDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAglpavP 674
Cdd:TIGR01243  215 VLLYGPPGTGKTLLAKAVANEA----GAYFISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIA-----P 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     675 EHEHSPDAVQSQRLAHALN--DMIKEfisMGSLVALIATSQSQqSLHPLLVSAQGvhiFQCVQHIQPPNQEQRCEILCNV 752
Cdd:TIGR01243  286 KREEVTGEVEKRVVAQLLTlmDGLKG---RGRVIVIGATNRPD-ALDPALRRPGR---FDREIVIRVPDKRARKEILKVH 358

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     753 IKNKLDCDinkftDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSR-----------QSI--STREKLVLTTLDFQKALR 819
Cdd:TIGR01243  359 TRNMPLAE-----DVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfiregkinfeaEEIpaEVLKELKVTMKDFMEALK 433

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     820 GFLPASLRSVNLHKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESR 899
Cdd:TIGR01243  434 MVEPSAIREVLVEVP-NVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESG 512

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     900 MNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHD-NTGVTDRVVNQLLTQLDGVEGLQGVY 978
Cdd:TIGR01243  513 ANFIAVRGPEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVV 592

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     979 VLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEA 1058
Cdd:TIGR01243  593 VIAATNRPDILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAA 672


                   ....*..
gi 4505725    1059 LHGMLLS 1065
Cdd:TIGR01243  673 LRESIGS 679
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 848-1005 1.26e-104

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: 327.46  E-value: 1.26e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   848 VRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFI 927
Cdd:cd19526    1 VKKALEETIEWPSKYPKIFASSPLRLRSGILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNKYIGASEQNVRDLFS 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505725   928 RAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYC 1005
Cdd:cd19526   81 RAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVEGLDGVYVLAATSRPDLIDPALLRPGRLDKLVYC 158
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 800-1059 5.05e-93

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 302.31  E-value: 5.05e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   800 SISTREKLVLTTLDFQKALRGFLPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILL 879
Cdd:COG1222   38 ALELLEEAPALLLNDANLTQKRLGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRKYGIEPPKGVLL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   880 YGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNT-GVTD 958
Cdd:COG1222  118 YGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDGTsGEVQ 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   959 RVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASV 1038
Cdd:COG1222  198 RTVNQLLAELDGFESRGDVLIIAATNRPDLLDPALLRPGRFDRVIEVPLPDEEAREEILKIHLRDMPLADDVDLDKLAKL 277

                        250       260
                 ....*....|....*....|.
gi 4505725  1039 TDSFTGADLKALLYNAQLEAL 1059
Cdd:COG1222  278 TEGFSGADLKAIVTEAGMFAI 298
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 848-1005 3.72e-83

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: 268.38  E-value: 3.72e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   848 VRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFI 927
Cdd:cd19511    1 VKRELKEAVEWPLKHPDAFKRLGIRPPKGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKYVGESERAVREIFQ 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505725   928 RAQAAKPCILFFDEFESIAPRRGHDN-TGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYC 1005
Cdd:cd19511   81 KARQAAPCIIFFDEIDSLAPRRGQSDsSGVTDRVVSQLLTELDGIESLKGVVVIAATNRPDMIDPALLRPGRLDKLIYV 159
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 781-1060 6.92e-81

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: 271.40  E-value: 6.92e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   781 ARDFTVLVDRAIHSRLSRQSISTREKLVLTTLDFQKALRGFLPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPA 860
Cdd:COG0464   98 LLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPL 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   861 KYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFD 940
Cdd:COG0464  178 KRPELREEYGLPPPRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGLAPCVLFID 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   941 EFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGlqGVYVLAATSRPDLIDPALLRpgRLDKCVYCPPPDQVSRLEILNVL 1020
Cdd:COG0464  258 EADALAGKRGEVGDGVGRRVVNTLLTEMEELRS--DVVVIAATNRPDLLDPALLR--RFDEIIFFPLPDAEERLEIFRIH 333

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 4505725  1021 SDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALH 1060
Cdd:COG0464  334 LRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALR 373
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 848-1004 4.93e-73

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: 239.70  E-value: 4.93e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   848 VRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFI 927
Cdd:cd19529    1 VKQELKEAVEWPLLKPEVFKRLGIRPPKGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSKWVGESEKAIREIFR 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505725   928 RAQAAKPCILFFDEFESIAPRRGHD-NTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVY 1004
Cdd:cd19529   81 KARQVAPCVIFFDEIDSIAPRRGTTgDSGVTERVVNQLLTELDGLEEMNGVVVIAATNRPDIIDPALLRAGRFDRLIY 158
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 845-1004 7.32e-71

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: 233.92  E-value: 7.32e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   845 LHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRD 924
Cdd:cd19530    1 LDHVREELTMSILRPIKRPDIYKALGIDLPTGVLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKYVGESERAVRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   925 IFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVY 1004
Cdd:cd19530   81 VFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLEERSNVFVIAATNRPDIIDPAMLRPGRLDKTLY 160
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 822-1063 2.81e-67

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: 242.51  E-value: 2.81e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     822 LPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMN 901
Cdd:TIGR01243  160 REKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAY 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     902 FISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLA 981
Cdd:TIGR01243  240 FISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIG 319

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     982 ATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHG 1061
Cdd:TIGR01243  320 ATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399


                   ..
gi 4505725    1062 ML 1063
Cdd:TIGR01243  400 FI 401
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 832-1050 5.91e-67

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 231.64  E-value: 5.91e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    832 HKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELL 911
Cdd:PRK03992  124 ESP-NVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    912 SKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGvTDRVVN----QLLTQLDGVEGLQGVYVLAATSRPD 987
Cdd:PRK03992  203 QKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTS-GDREVQrtlmQLLAEMDGFDPRGNVKIIAATNRID 281

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505725    988 LIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKAL 1050
Cdd:PRK03992  282 ILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAI 344
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 848-1004 1.24e-66

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: 221.62  E-value: 1.24e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   848 VRQILMDTIQLPAKYPELFAnLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFI 927
Cdd:cd19527    1 VKKEILDTIQLPLEHPELFS-SGLRKRSGILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYIGESEANVREVFQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   928 RAQAAKPCILFFDEFESIAPRRGH--DNTGVTDRVVNQLLTQLDGVE-GLQGVYVLAATSRPDLIDPALLRPGRLDKCVY 1004
Cdd:cd19527   80 KARDAKPCVIFFDELDSLAPSRGNsgDSGGVMDRVVSQLLAELDGMSsSGQDVFVIGATNRPDLLDPALLRPGRFDKLLY 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 841-1004 9.40e-66

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: 219.47  E-value: 9.40e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   841 KIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQ 920
Cdd:cd19503    1 DIGGLDEQIASLKELIELPLKYPELFRALGLKPPRGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSIVSKYLGESEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   921 AVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLD 1000
Cdd:cd19503   81 NLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMSSRGKVVVIAATNRPDAIDPALRRPGRFD 160


                 ....
gi 4505725  1001 KCVY 1004
Cdd:cd19503  161 REVE 164
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 848-1004 3.65e-65

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: 217.76  E-value: 3.65e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   848 VRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFI 927
Cdd:cd19528    1 VKRELQELVQYPVEHPDKFLKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMWFGESEANVRDIFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   928 RAQAAKPCILFFDEFESIAPRRG---HDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVY 1004
Cdd:cd19528   81 KARAAAPCVLFFDELDSIAKARGgniGDAGGAADRVINQILTEMDGMNTKKNVFIIGATNRPDIIDPAILRPGRLDQLIY 160
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 839-1001 1.40e-56

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: 193.32  E-value: 1.40e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   839 WDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGAS 918
Cdd:cd19502    2 YEDIGGLDEQIREIREVVELPLKHPELFEELGIEPPKGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSELVQKYIGEG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   919 EQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGvTDRVVN----QLLTQLDGVEGLQGVYVLAATSRPDLIDPALL 994
Cdd:cd19502   82 ARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTG-GDREVQrtmlELLNQLDGFDPRGNIKVIMATNRPDILDPALL 160


                 ....*..
gi 4505725   995 RPGRLDK 1001
Cdd:cd19502  161 RPGRFDR 167
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 842-1001 4.75e-55

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: 188.80  E-value: 4.75e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQA 921
Cdd:cd19519    2 IGGCRKQLAQIREMVELPLRHPELFKAIGIKPPRGILLYGPPGTGKTLIARAVANETGAFFFLINGPEIMSKLAGESESN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   922 VRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDK 1001
Cdd:cd19519   82 LRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAHVIVMAATNRPNSIDPALRRFGRFDR 161
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 840-1058 1.65e-53

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


Pssm-ID: 273520 [Multi-domain]  Cd Length: 495  Bit Score: 195.97  E-value: 1.65e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     840 DKIGGLHEVRQILMDTIQLpAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASE 919
Cdd:TIGR01241   55 KDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     920 QAVRDIFIRAQAAKPCILFFDEFESIAPRRG------HDntgVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPAL 993
Cdd:TIGR01241  134 SRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglgggND---EREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPAL 210

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505725     994 LRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEA 1058
Cdd:TIGR01241  211 LRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 848-1005 6.71e-53

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: 182.48  E-value: 6.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   848 VRQILMDTIQLPAKYPELFAnLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFI 927
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRR-YGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505725   928 RAQAAKPCILFFDEFESIAPRRG-HDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYC 1005
Cdd:cd19481   80 RARRLAPCILFIDEIDAIGRKRDsSGESGELRRVLNQLLTELDGVNSRSKVLVIAATNRPDLLDPALLRPGRFDEVIEF 158
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
 836-1029 9.91e-51

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: 187.99  E-value: 9.91e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     836 DLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIA----------RESRMNFISV 905
Cdd:TIGR03689  178 DVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAnslaarigaeGGGKSYFLNI 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     906 KGPELLSKYIGASEQAVRDIFIRAQAA----KPCILFFDEFESIAPRRGhdnTGVTD----RVVNQLLTQLDGVEGLQGV 977
Cdd:TIGR03689  258 KGPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRG---SGVSSdvetTVVPQLLAEIDGVESLDNV 334

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 4505725     978 YVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEIL-NVLSDSLPLADD 1029
Cdd:TIGR03689  335 IVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFaKYLTDDLPLPED 387
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 824-1059 5.91e-50

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 182.66  E-value: 5.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    824 ASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFI 903
Cdd:PTZ00454  129 SSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFI 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    904 SVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGV---TDRVVNQLLTQLDGVEGLQGVYVL 980
Cdd:PTZ00454  209 RVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGAdreVQRILLELLNQMDGFDQTTNVKVI 288

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505725    981 AATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEAL 1059
Cdd:PTZ00454  289 MATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAV 367
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 877-1006 3.87e-49

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: 170.47  E-value: 3.87e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     877 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGV 956
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 4505725     957 TDRVVNQLLTQLDGVEGLQG-VYVLAATSRPDLIDPALLrpGRLDKCVYCP 1006
Cdd:pfam00004   81 SRRVVNQLLTELDGFTSSNSkVIVIAATNRPDKLDPALL--GRFDRIIEFP 129
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
845-1051 1.50e-48

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 183.31  E-value: 1.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   845 LHEVRQILMDtiqlPAKYPELFANLPirqrTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKY--IGASEqaV 922
Cdd:COG0465  154 LQEIVDFLKD----PEKFTRLGAKIP----KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFvgVGASR--V 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   923 RDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTD---RVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRL 999
Cdd:COG0465  224 RDLFEQAKKNAPCIIFIDEIDAVGRQRGAGLGGGHDereQTLNQLLVEMDGFEGNEGVIVIAATNRPDVLDPALLRPGRF 303

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 4505725  1000 DKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALL 1051
Cdd:COG0465  304 DRQVVVDLPDVKGREAILKVHARKKPLAPDVDLEVIARRTPGFSGADLANLV 355
ftsH CHL00176
cell division protein; Validated
 840-1056 1.58e-48

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 184.48  E-value: 1.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    840 DKIGGLHEVRQILMDTIQLpAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASE 919
Cdd:CHL00176  183 RDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGA 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    920 QAVRDIFIRAQAAKPCILFFDEFESIAPRRGhdnTGV------TDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPAL 993
Cdd:CHL00176  262 ARVRDLFKKAKENSPCIVFIDEIDAVGRQRG---AGIgggndeREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAAL 338

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505725    994 LRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQL 1056
Cdd:CHL00176  339 LRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAI 401
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
852-1061 1.15e-47

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 181.77  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    852 LMDTIQLPAKYPELFANLPirqrTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQA 931
Cdd:PRK10733  167 LVEYLREPSRFQKLGGKIP----KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKK 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    932 AKPCILFFDEFESIAPRRG------HDNTgvtDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYC 1005
Cdd:PRK10733  243 AAPCIIFIDEIDAVGRQRGaglgggHDER---EQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVV 319

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 4505725   1006 PPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHG 1061
Cdd:PRK10733  320 GLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARG 375
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 842-1004 5.00e-47

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: 166.25  E-value: 5.00e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMDTIQLpAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQA 921
Cdd:cd19501    6 VAGCEEAKEELKEVVEF-LKNPEKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   922 VRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTD---RVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGR 998
Cdd:cd19501   85 VRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHDereQTLNQLLVEMDGFESNTGVIVIAATNRPDVLDPALLRPGR 164


                 ....*.
gi 4505725   999 LDKCVY 1004
Cdd:cd19501  165 FDRQVY 170
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 839-1059 9.63e-47

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 174.19  E-value: 9.63e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    839 WDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGAS 918
Cdd:PTZ00361  182 YADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    919 EQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVT---DRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLR 995
Cdd:PTZ00361  262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEkeiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505725    996 PGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEAL 1059
Cdd:PTZ00361  342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
874-1059 2.08e-45

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 164.29  E-value: 2.08e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   874 RTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAqAAKPCILFFDEFESIAPRRGHDN 953
Cdd:COG1223   35 PRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSLIGSYLGETARNLRKLFDFA-RRAPCVIFFDEFDAIAKDRGDQN 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   954 -TGVTDRVVNQLLTQLDGVEGlqGVYVLAATSRPDLIDPALLRpgRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDL 1032
Cdd:COG1223  114 dVGEVKRVVNALLQELDGLPS--GSVVIAATNHPELLDSALWR--RFDEVIEFPLPDKEERKEILELNLKKFPLPFELDL 189

                        170       180
                 ....*....|....*....|....*..
gi 4505725  1033 QHVASVTDSFTGADLKALLYNAQLEAL 1059
Cdd:COG1223  190 KKLAKKLEGLSGADIEKVLKTALKKAI 216
PEX-2N pfam09263
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a Cdc48 domain 2-like ...
 17-98 9.53e-45

Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a Cdc48 domain 2-like fold, with a beta-alpha-beta(3) arrangement. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substrate binding site, allowing for peroxisomal biogenesis, membrane fusion and protein translocation.


Pssm-ID: 462730  Cd Length: 83  Bit Score: 155.99  E-value: 9.53e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725      17 VTVAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSH-QPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLK 95
Cdd:pfam09263    1 VTVVFNNAKNCFLHLPSKLVSQLSLQENQALELSWGHgQPVFLSWTEGRHSSDQDENVVELNRQLGEKLGLKDGEQVFLR 80


                   ...
gi 4505725      96 PCS 98
Cdd:pfam09263   81 PCS 83
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 842-1004 5.87e-44

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: 157.13  E-value: 5.87e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMDTIQLPAKYPELFANLPIRQRtGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQA 921
Cdd:cd19509    1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPR-GILLYGPPGTGKTLLARAVASESGSTFFSISASSLVSKWVGESEKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   922 VRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEG--LQGVYVLAATSRPDLIDPALLRpgRL 999
Cdd:cd19509   80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNkpEDRVLVLGATNRPWELDEAFLR--RF 157


                 ....*
gi 4505725  1000 DKCVY 1004
Cdd:cd19509  158 EKRIY 162
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 863-1000 2.30e-41

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: 149.95  E-value: 2.30e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   863 PELFANLPIRQRTGILLYGPPGTGKTLLAGVI-----ARESRMnfisVKGPELLSKYIGASEQAVRDIFIRAQAA-KPC- 935
Cdd:cd19504   24 PEIVEQLGCKHVKGILLYGPPGTGKTLMARQIgkmlnAREPKI----VNGPEILNKYVGESEANIRKLFADAEEEqRRLg 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505725   936 ------ILFFDEFESIAPRRGH--DNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLD 1000
Cdd:cd19504  100 ansglhIIIFDEIDAICKQRGSmaGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRKDLIDEALLRPGRLE 172
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 842-1001 3.34e-41

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: 149.48  E-value: 3.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQA 921
Cdd:cd19518    2 IGGMDSTLKELCELLIHPILPPEYFQHLGVEPPRGVLLHGPPGCGKTMLANAIAGELKVPFLKISATEIVSGVSGESEEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   922 VRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGL----QGVYVLAATSRPDLIDPALLRPG 997
Cdd:cd19518   82 IRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEktagGPVLVIGATNRPDSLDPALRRAG 161


                 ....
gi 4505725   998 RLDK 1001
Cdd:cd19518  162 RFDR 165
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 842-1001 1.06e-39

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: 144.96  E-value: 1.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESR-----MNFISVKGPELLSKYIG 916
Cdd:cd19517    2 IGGLSHYINQLKEMVFFPLLYPEVFAKFKITPPRGVLFHGPPGTGKTLMARALAAECSkggqkVSFFMRKGADCLSKWVG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   917 ASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRP 996
Cdd:cd19517   82 EAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGLDNRGQVVVIGATNRPDALDPALRRP 161


                 ....*
gi 4505725   997 GRLDK 1001
Cdd:cd19517  162 GRFDR 166
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 842-999 3.95e-35

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: 131.78  E-value: 3.95e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMDTIQLPAKYPELFANLPIRQRT-GILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQ 920
Cdd:cd19520    2 IGGLDEVITELKELVILPLQRPELFDNSRLLQPPkGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDKWYGESQK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   921 AVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGV--EGLQGVYVLAATSRPDLIDPALLR--P 996
Cdd:cd19520   82 LVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLstDGNCRVIVMGATNRPQDLDEAILRrmP 161


                 ...
gi 4505725   997 GRL 999
Cdd:cd19520  162 KRF 164
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 833-1004 7.63e-35

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 131.14  E-value: 7.63e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   833 KPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRtGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLS 912
Cdd:cd19521    1 KP-NVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWS-GILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   913 KYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGV-EGLQGVYVLAATSRPDLIDP 991
Cdd:cd19521   79 KWMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVgNDSQGVLVLGATNIPWQLDS 158

                        170
                 ....*....|...
gi 4505725   992 ALLRpgRLDKCVY 1004
Cdd:cd19521  159 AIRR--RFEKRIY 169
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 842-1004 7.13e-33

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: 125.48  E-value: 7.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMDTIQLPAKYPELFANLPiRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQA 921
Cdd:cd19522    2 IADLEEAKKLLEEAVVLPMWMPEFFKGIR-RPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRGESEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   922 VRDIFIRAQAAKPCILFFDEFESIAPRRG-HDNTGVTDRVVNQLLTQLDGVEGLQG-------VYVLAATSRPDLIDPAL 993
Cdd:cd19522   81 VRLLFEMARFYAPTTIFIDEIDSICSRRGtSEEHEASRRVKSELLVQMDGVGGASEnddpskmVMVLAATNFPWDIDEAL 160

                        170
                 ....*....|.
gi 4505725   994 LRpgRLDKCVY 1004
Cdd:cd19522  161 RR--RLEKRIY 169
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 842-1004 9.01e-32

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: 122.27  E-value: 9.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMDTIQLPAKYPELFANLPIRQRtGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQA 921
Cdd:cd19524    2 IAGQDLAKQALQEMVILPSLRPELFTGLRAPAR-GLLLFGPPGNGKTMLAKAVAAESNATFFNISAASLTSKYVGEGEKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   922 VRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQG--VYVLAATSRPDLIDPALLRpgRL 999
Cdd:cd19524   81 VRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNGDdrVLVMGATNRPQELDDAVLR--RF 158


                 ....*
gi 4505725  1000 DKCVY 1004
Cdd:cd19524  159 TKRVY 163
PEX-1N pfam09262
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi ...
 104-179 1.21e-31

Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi beta-barrel fold, similar in structure to the Cdc48 N-terminal domain. It has been suggested that this domain may be involved in interactions with ubiquitin, ubiquitin-like protein modifiers, or ubiquitin-like domains, such as Ubx. Furthermore, the domain may possess a putative adaptor or substrate binding site, allowing for peroxisomal biogenesis, membrane fusion and protein translocation.


Pssm-ID: 462729  Cd Length: 77  Bit Score: 118.37  E-value: 1.21e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4505725     104 QQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAAS-YGRLETDTKLLIQP 179
Cdd:pfam09262    1 TTVEVEPLTSDDWEILELHAEFLEDNLLSQVRVVSPGQILPVWVSGTTVARFRVTSIEPANSpFARLSPDTEVIVAP 77
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 836-1004 4.88e-30

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: 118.17  E-value: 4.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   836 DLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRtGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYI 915
Cdd:cd19525   18 PINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPK-GILLFGPPGTGKTLIGKCIASQSGATFFSISASSLTSKWV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   916 GASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGL--QGVYVLAATSRPDLIDPAL 993
Cdd:cd19525   97 GEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSseDRILVVGATNRPQEIDEAA 176

                        170
                 ....*....|.
gi 4505725   994 LRpgRLDKCVY 1004
Cdd:cd19525  177 RR--RLVKRLY 185
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 869-1007 6.79e-25

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: 101.84  E-value: 6.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   869 LPIRQRTGILLYGPPGTGKTLLAGVIARESRM---NFISVKGPELLSKYIGASEQ---AVRDIFIRAQAAKPCILFFDEF 942
Cdd:cd00009   14 LELPPPKNLLLYGPPGTGKTTLARAIANELFRpgaPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEI 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505725   943 ESIAPRrghdntgVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPP 1007
Cdd:cd00009   94 DSLSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 842-995 1.94e-20

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 89.56  E-value: 1.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTgILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQA 921
Cdd:cd19523    2 IAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRS-ILLFGPRGTGKTLLGRCLASQLGATFLRLRGSTLVAKWAGEGEKI 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505725   922 VRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTdRVVNQLLTQLDGV--EGLQGVYVLAATSRPDLIDPALLR 995
Cdd:cd19523   81 LQASFLAARCRQPSVLFISDLDALLSSQDDEASPVG-RLQVELLAQLDGVlgSGEDGVLVVCTTSKPEEIDESLRR 155
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 595-731 7.84e-18

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: 81.10  E-value: 7.84e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     595 LLLTGGKGSGKSTLAKAICKEafdkLDAHVERVDCKALRGKRL----ENIQKTLEVAFSEAvwmqPSVVLLDDLDLIAGl 670
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKE----LGAPFIEISGSELVSKYVgeseKRLRELFEAAKKLA----PCVIFIDEIDALAG- 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505725     671 pavpeHEHSPDAVQSQRLAHALNDMIKEFISMGSLVALIATSQSQQSLHPLLVSAQGVHIF 731
Cdd:pfam00004   72 -----SRGSGGDSESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIE 127
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 842-1000 4.26e-17

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: 80.11  E-value: 4.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   842 IGGLHEVRQILMdtIQLPAKYPELFA-NLPIRQrtGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQ 920
Cdd:cd19507    2 VGGLDNLKDWLK--KRKAAFSKQASAyGLPTPK--GLLLVGIQGTGKSLTAKAIAGVWQLPLLRLDMGRLFGGLVGESES 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   921 AVRDIFIRAQAAKPCILFFDEFES-IAPRRGHDNTGVTDRVVNQLLTQLDgvEGLQGVYVLAATSRPDLIDPALLRPGRL 999
Cdd:cd19507   78 RLRQMIQTAEAIAPCVLWIDEIEKgFSNADSKGDSGTSSRVLGTFLTWLQ--EKKKPVFVVATANNVQSLPPELLRKGRF 155


                 .
gi 4505725  1000 D 1000
Cdd:cd19507  156 D 156
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 397-819 1.35e-15

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 80.34  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   397 AIKYTKNVEVLHLGKVWIPDDLRKRLNIEMHAVVRITPVEVTPKIPRSLKLQPRENLPKDISEEDIKTVFYSWLQQSTTT 476
Cdd:COG0464    1 LAELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   477 MLPLVISEEEFIKLETKDGLKEFSLSIVHSWEKEKDKNIFLLSPNLLQKTTIQVLLDPMVKEENSEEIDFILPFLkLSSL 556
Cdd:COG0464   81 LLAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAI-LDDL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   557 GGVNSLgVSSLEHITHSLLGRPLSRQLMSLVAGLRngaLLLTGGKGSGKSTLAKAICKEafdkLDAHVERVDCKALRGKR 636
Cdd:COG0464  160 GGLEEV-KEELRELVALPLKRPELREEYGLPPPRG---LLLYGPPGTGKTLLARALAGE----LGLPLIEVDLSDLVSKY 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   637 LENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAGlpavpehehSPDAVQSQRLAHALNDMIKEfisMGSL---VALIATSQ 713
Cdd:COG0464  232 VGETEKNLREVFDKARGLAPCVLFIDEADALAG---------KRGEVGDGVGRRVVNTLLTE---MEELrsdVVVIAATN 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   714 SQQSLHPLLVSAqgvhiFQCVQHIQPPNQEQRCEILCNVIKNKLDCDinkftDLDLQHVAKETGGFVARDFTVLVDRAIH 793
Cdd:COG0464  300 RPDLLDPALLRR-----FDEIIFFPLPDAEERLEIFRIHLRKRPLDE-----DVDLEELAEATEGLSGADIRNVVRRAAL 369

                        410       420
                 ....*....|....*....|....*...
gi 4505725   794 S--RLSRQSISTReklvlttlDFQKALR 819
Cdd:COG0464  370 QalRLGREPVTTE--------DLLEALE 389
ycf46 CHL00195
Ycf46; Provisional
 876-1060 2.65e-14

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 76.98  E-value: 2.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    876 GILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFE-SIAPRRGHDNT 954
Cdd:CHL00195  261 GLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDS 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725    955 GVTDRVVNQLLTQLDgvEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNV-LSDSLPLA-DDVDL 1032
Cdd:CHL00195  341 GTTNRVLATFITWLS--EKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIhLQKFRPKSwKKYDI 418

                         170       180
                  ....*....|....*....|....*...
gi 4505725   1033 QHVASVTDSFTGADlkalLYNAQLEALH 1060
Cdd:CHL00195  419 KKLSKLSNKFSGAE----IEQSIIEAMY 442
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 877-1009 4.69e-14

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: 70.87  E-value: 4.69e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725      877 ILLYGPPGTGKTLLAGVIARESRMNFISVK-----------------GPELLSKYIGASEQAVRDIFIRAQAAKPCILFF 939
Cdd:smart00382    5 ILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDVLIL 84

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725      940 DEFESIaprrgHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPgRLDKCVYCPPPD 1009
Cdd:smart00382   85 DEITSL-----LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 852-1004 5.03e-11

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: 62.37  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   852 LMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFI------SVKGPELLSKYIGASEQA---- 921
Cdd:cd19510    1 IIDDLKDFIKNEDWYNDRGIPYRRGYLLYGPPGTGKSSFIAALAGELDYDICdlnlseVVLTDDRLNHLLNTAPKQsiil 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   922 VRDIfiraqaakPCILFFDEFESIAPRRGHDNTGVTdrvVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDK 1001
Cdd:cd19510   81 LEDI--------DAAFESREHNKKNPSAYGGLSRVT---FSGLLNALDGVASSEERIVFMTTNHIERLDPALIRPGRVDM 149


                 ...
gi 4505725  1002 CVY 1004
Cdd:cd19510  150 KIY 152
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 877-993 1.05e-10

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


Pssm-ID: 410916 [Multi-domain]  Cd Length: 199  Bit Score: 62.46  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   877 ILLYGPPGTGKTLLAGVIARE--SRMNF-------ISVKGPELLSKYIGASEQAVRDIF--IRAQAAKPCILFF---DEF 942
Cdd:cd19508   55 VLLHGPPGTGKTSLCKALAQKlsIRLSSryrygqlIEINSHSLFSKWFSESGKLVTKMFqkIQELIDDKDALVFvliDEV 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4505725   943 ESIAPRRGHDNTGV--TD--RVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPAL 993
Cdd:cd19508  135 ESLAAARSASSSGTepSDaiRVVNAVLTQIDRIKRYHNNVILLTSNLLEKIDVAF 189
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 574-669 6.44e-09

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: 56.14  E-value: 6.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   574 LLGRPLSRQLMSLVAGLrngalLLTGGKGSGKSTLAKAICKEafdkLDAHVERVDCKALRGKRLENIQKTLEVAFSEAVW 653
Cdd:cd19481   13 RRGSRLRRYGLGLPKGI-----LLYGPPGTGKTLLAKALAGE----LGLPLIVVKLSSLLSKYVGESEKNLRKIFERARR 83

                         90
                 ....*....|....*.
gi 4505725   654 MQPSVVLLDDLDLIAG 669
Cdd:cd19481   84 LAPCILFIDEIDAIGR 99
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 595-712 3.31e-08

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: 54.22  E-value: 3.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   595 LLLTGGKGSGKSTLAKAICKEAfdklDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAglpavP 674
Cdd:cd19503   37 VLLHGPPGTGKTLLARAVANEA----GANFLSISGPSIVSKYLGESEKNLREIFEEARSHAPSIIFIDEIDALA-----P 107

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 4505725   675 EHEHSPDAVQSQRLAHALNDMiKEFISMGSLVALIATS 712
Cdd:cd19503  108 KREEDQREVERRVVAQLLTLM-DGMSSRGKVVVIAATN 144
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 581-668 1.01e-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: 52.53  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   581 RQLMSLVAGLRNGALLLTGGKGSGKSTLAKAICKEAFDKlDAHVERVDCKALRGK---RLENIQKTLEVAFSEAVWMQPS 657
Cdd:cd00009    8 EALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRP-GAPFLYLNASDLLEGlvvAELFGHFLVRLLFELAEKAKPG 86

                         90
                 ....*....|.
gi 4505725   658 VVLLDDLDLIA 668
Cdd:cd00009   87 VLFIDEIDSLS 97
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 877-941 1.28e-07

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 55.83  E-value: 1.28e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505725   877 ILLYGPPGTGKTLLAGVIARESRMNFISvkgpelLSkyigaseqAV-------RDIFIRAQAA----KPCILFFDE 941
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFVA------LS--------AVtsgvkdiREVIEEARERraygRRTILFVDE 113
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 591-741 1.69e-07

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: 51.99  E-value: 1.69e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725      591 RNGALLLTGGKGSGKSTLAKAICKEaFDKLDAHVERVDCKALRGKRLENIQ--------------KTLEVAFSEAVWMQP 656
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARE-LGPPGGGVIYIDGEDILEEVLDQLLliivggkkasgsgeLRLRLALALARKLKP 79

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725      657 SVVLLDDLDLIAglpavpehehspDAVQSQRLAHALNDMIKEFISMGSLVALIATSQSQQSLHPLLVsaqgVHIFQCVQH 736
Cdd:smart00382   80 DVLILDEITSLL------------DAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALL----RRRFDRRIV 143


                    ....*
gi 4505725      737 IQPPN 741
Cdd:smart00382  144 LLLIL 148
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 1029-1060 3.93e-07

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


Pssm-ID: 465537 [Multi-domain]  Cd Length: 45  Bit Score: 47.53  E-value: 3.93e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 4505725    1029 DVDLQHVASVTDSFTGADLKALLYNAQLEALH 1060
Cdd:pfam17862    1 DVDLEELAERTEGFSGADLEALCREAALAALR 32
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 877-941 6.29e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.16  E-value: 6.29e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505725    877 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPEllskyigASEQAVRDIFIRAQAA----KPCILFFDE 941
Cdd:PRK13342   39 MILWGPPGTGKTTLARIIAGATDAPFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILFIDE 100
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 869-969 2.84e-06

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


Pssm-ID: 188437 [Multi-domain]  Cd Length: 557  Bit Score: 51.77  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     869 LPIRQRTG-ILLYGPPGTGKTLLA----------GVIAREsrmNFISVKGPELLSKYIGASEQAVRDIFIRAQAAkpcIL 937
Cdd:TIGR03922  306 LPVAQTSNhMLFAGPPGTGKTTIArvvakiycglGVLRKP---LVREVSRADLIGQYIGESEAKTNEIIDSALGG---VL 379

                           90       100       110
                   ....*....|....*....|....*....|..
gi 4505725     938 FFDEFESIAPRRGHDNTGVTDRVVNQLLTQLD 969
Cdd:TIGR03922  380 FLDEAYTLVETGYGQKDPFGLEAIDTLLARME 411
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
877-910 4.79e-06

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 50.13  E-value: 4.79e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 4505725    877 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPEL 910
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 877-910 5.39e-06

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 47.88  E-value: 5.39e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 4505725     877 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPEL 910
Cdd:pfam05496   36 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAI 69
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 594-679 1.09e-05

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: 46.96  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   594 ALLLTGGKGSGKSTLAKAICKEafdkLDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAGLPAV 673
Cdd:cd19509   34 GILLYGPPGTGKTLLARAVASE----SGSTFFSISASSLVSKWVGESEKIVRALFALARELQPSIIFIDEIDSLLSERGS 109


                 ....*.
gi 4505725   674 PEHEHS 679
Cdd:cd19509  110 GEHEAS 115
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
876-923 1.69e-05

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 48.81  E-value: 1.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 4505725   876 GILLYGPPGTGKTLLAGVIARE--SRMNFISVKGPELLSKYIGASE---QAVR 923
Cdd:COG1224   66 GILIVGPPGTGKTALAVAIARElgEDTPFVAISGSEIYSAELKKTEflmQALR 118
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 877-1003 2.34e-05

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 45.60  E-value: 2.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   877 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSkyIGASE-QAVRDIFIRAQAA-KPCILFFDEFESIAPRRGHDNT 954
Cdd:cd19512   25 ILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGREGvTAIHKVFDWANTSrRGLLLFVDEADAFLRKRSTEKI 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 4505725   955 GVTDR-VVNQLLTQLdGVEGLQGVYVLaATSRPDLIDPALlrPGRLDKCV 1003
Cdd:cd19512  103 SEDLRaALNAFLYRT-GEQSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 148
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 586-679 3.40e-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: 45.61  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   586 LVAGLRNGA--LLLTGGKGSGKSTLAKAICKEAfdklDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDD 663
Cdd:cd19524   25 LFTGLRAPArgLLLFGPPGNGKTMLAKAVAAES----NATFFNISAASLTSKYVGEGEKLVRALFAVARELQPSIIFIDE 100

                         90
                 ....*....|....*.
gi 4505725   664 LDLIAGLPAVPEHEHS 679
Cdd:cd19524  101 VDSLLSERSEGEHEAS 116
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 877-908 3.47e-05

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 47.38  E-value: 3.47e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 4505725   877 ILLYGPPGTGKTLLAGVIARESRMNFISVKGP 908
Cdd:COG2255   57 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGP 88
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 876-1003 4.07e-05

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: 45.44  E-value: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   876 GILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSK-----------YIGASEQAVRDI---FIRAQAAKPCILFF-D 940
Cdd:cd19505   14 GILLIGSIETGRSYLIKSLAANSYVPLIRISLNKLLYNkpdfgnddwidGMLILKESLHRLnlqFELAKAMSPCIIWIpN 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4505725   941 EFESIAPRRGHDNTGVTDRVVNQLLTQL-DGVEG--LQGVYVLAATSRPDLIDPALLRPGRLDKCV 1003
Cdd:cd19505   94 IHELNVNRSTQNLEEDPKLLLGLLLNYLsRDFEKssTRNILVIASTHIPQKVDPALIAPNRLDTCI 159
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
871-906 7.07e-05

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 45.93  E-value: 7.07e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 4505725   871 IRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVK 906
Cdd:COG1484   96 IERGENLILLGPPGTGKTHLAIALGHEACRAGYRVR 131
PRK13341 PRK13341
AAA family ATPase;
878-941 1.06e-04

AAA family ATPase;


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.59  E-value: 1.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505725    878 LLYGPPGTGKTLLAGVIARESRMNFIS-------VKgpELLSKYIGASEQavrdifiRAQAAKPCILFFDE 941
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFSSlnavlagVK--DLRAEVDRAKER-------LERHGKRTILFIDE 117
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 876-923 1.75e-04

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


Pssm-ID: 399217 [Multi-domain]  Cd Length: 347  Bit Score: 45.38  E-value: 1.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 4505725     876 GILLYGPPGTGKTLLAGVIARE--SRMNFISVKGPELLSKYIGASE---QAVR 923
Cdd:pfam06068   52 AVLIAGPPGTGKTALAIAISKElgEDTPFTSISGSEVYSLEMKKTEaltQAFR 104
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 594-689 2.96e-04

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 42.95  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   594 ALLLTGGKGSGKSTLAKAICKEafdkLDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIagLPAV 673
Cdd:cd19523   35 SILLFGPRGTGKTLLGRCLASQ----LGATFLRLRGSTLVAKWAGEGEKILQASFLAARCRQPSVLFISDLDAL--LSSQ 108

                         90
                 ....*....|....*..
gi 4505725   674 PEhEHSP-DAVQSQRLA 689
Cdd:cd19523  109 DD-EASPvGRLQVELLA 124
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 595-677 4.04e-04

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: 42.41  E-value: 4.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   595 LLLTGGKGSGKSTLAKAICKEAfdklDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAGLPAVP 674
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEA----GARFINLQVSSLTDKWYGESQKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSST 113


                 ...
gi 4505725   675 EHE 677
Cdd:cd19520  114 DHE 116
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 877-947 6.22e-04

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 43.44  E-value: 6.22e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 4505725     877 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPELlskyigaseQAVRDIF-IRAQAAKPCILFFDEFESIAP 947
Cdd:TIGR00635   33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL---------EKPGDLAaILTNLEEGDVLFIDEIHRLSP 95
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 766-942 6.44e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 43.99  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   766 DLDLQHVAKETGGFVARDFTVLVDRAIHSRLSRQSISTREKLVLTTLDFQKALRGFLPASLRSVNLHKPRDLGWD---KI 842
Cdd:COG1401  110 DSEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAeelYS 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   843 GGLHEVRQILMDTIQlpAKYPELFANLPIRQRTG--ILLYGPPGTGKTLLAGVIAR------ESRMNFISV----KGPEL 910
Cdd:COG1401  190 EDLESEDDYLKDLLR--EKFEETLEAFLAALKTKknVILAGPPGTGKTYLARRLAEalggedNGRIEFVQFhpswSYEDF 267

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 4505725   911 LSKY---IGASEQAVRD-IFIRA--QAA----KPCILFFDEF 942
Cdd:COG1401  268 LLGYrpsLDEGKYEPTPgIFLRFclKAEknpdKPYVLIIDEI 309
PRK08116 PRK08116
hypothetical protein; Validated
 872-929 6.77e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 43.09  E-value: 6.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505725    872 RQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKG---PELLSK---YIGASEQAVRDIFIRA 929
Cdd:PRK08116  112 KENVGLLLWGSVGTGKTYLAACIANELIEKGVPVIFvnfPQLLNRiksTYKSSGKEDENEIIRS 175
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
595-646 9.78e-04

Predicted kinase, contains AAA domain [General function prediction only];


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 41.44  E-value: 9.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 4505725   595 LLLTGGK-GSGKSTLAKAICKEafdkLDAHVERVD--CKALRGKRLENIQKTLEV 646
Cdd:COG0645    1 LILVCGLpGSGKSTLARALAER----LGAVRLRSDvvRKRLFGAGLAPLERSPEA 51
PRK04195 PRK04195
replication factor C large subunit; Provisional
 877-902 1.98e-03

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 42.22  E-value: 1.98e-03
                          10        20
                  ....*....|....*....|....*.
gi 4505725    877 ILLYGPPGTGKTLLAGVIAREsrMNF 902
Cdd:PRK04195   42 LLLYGPPGVGKTSLAHALAND--YGW 65
APS_kinase pfam01583
Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3 ...
 595-651 2.21e-03

Adenylylsulphate kinase; Enzyme that catalyzes the phosphorylation of adenylylsulphate to 3'-phosphoadenylylsulfate. This domain contains an ATP binding P-loop motif.


Pssm-ID: 396247 [Multi-domain]  Cd Length: 154  Bit Score: 39.99  E-value: 2.21e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505725     595 LLLTGGKGSGKSTLAKAICKEAFDK------LDAHVERVD-CKAL---RGKRLENIQKTLEVA--FSEA 651
Cdd:pfam01583    5 IWLTGLSGAGKSTIANALERKLFEQgrsvyvLDGDNVRHGlNKDLgfsEEDRTENIRRIGEVAklFADA 73
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 877-947 3.31e-03

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


Pssm-ID: 400187 [Multi-domain]  Cd Length: 168  Bit Score: 39.87  E-value: 3.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725     877 ILLYGPPGTGKTLLAGVIARESRM---NFISVKGPELL-----SKYIGASEQAVRD----IFIRAQAAKP-CILFFDEFE 943
Cdd:pfam07724    6 FLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMeehsvSRLIGAPPGYVGYeeggQLTEAVRRKPySIVLIDEIE 85


                   ....
gi 4505725     944 SIAP 947
Cdd:pfam07724   86 KAHP 89
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
781-995 5.26e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 41.33  E-value: 5.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   781 ARDFTVLVDRAIHSRLSRQSISTREKLVLTTLDFQKALRGFLPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPA 860
Cdd:COG5635   73 LARALSALLLVLLLLESLLLLLLLLLLLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLV 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   861 KYPELFANLPIRQRTG--------------ILLYGPPGTGKTLLAGVIARESRMNFISVKGP-----------------E 909
Cdd:COG5635  153 SLDDLYVPLNLLERIEslkrlelleakkkrLLILGEPGSGKTTLLRYLALELAERYLDAEDPipilielrdlaeeasleD 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   910 LLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHdntgvtDRVVNQLLTQLDGVEGLQGVyvlaATSRPDLI 989
Cdd:COG5635  233 LLAEALEKRGGEPEDALERLLRNGRLLLLLDGLDEVPDEADR------DEVLNQLRRFLERYPKARVI----ITSRPEGY 302


                 ....*.
gi 4505725   990 DPALLR 995
Cdd:COG5635  303 DSSELE 308
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 595-722 6.90e-03

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: 38.96  E-value: 6.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505725   595 LLLTGGKGSGKSTLAKAICKEAfdklDAHVERVDCKALRGKRLENIQKTLEVAFSEAVWMQPSVVLLDDLDLIAglpavP 674
Cdd:cd19519   37 ILLYGPPGTGKTLIARAVANET----GAFFFLINGPEIMSKLAGESESNLRKAFEEAEKNAPAIIFIDEIDAIA-----P 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 4505725   675 EHEHSPDAVQSQRLAHALNDMikEFISMGSLVALIATSQSQQSLHPLL 722
Cdd:cd19519  108 KREKTHGEVERRIVSQLLTLM--DGLKQRAHVIVMAATNRPNSIDPAL 153
 
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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