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Conserved domains on  [gi|544186102|ref|NP_001269606.1|]
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peroxisome biogenesis factor 1 isoform 2 [Homo sapiens]

Protein Classification

PEX-2N and AAA domain-containing protein (domain architecture ID 11182382)

protein containing domains PEX-2N, PEX-1N, and AAA

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
820-949 6.06e-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: 278434  Cd Length: 130  Bit Score: 171.62  E-value: 6.06e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   820 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGV 899
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFVEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 544186102   900 TDRVVNQLLTQLDGVEGLQG-VYVLAATSRPDLIDPALLRpgRLDKCVYCP 949
Cdd:pfam00004   81 SRRVVNQLLTELDGFTSSLSkVIVIAATNRPDKLDPALLR--RFDRIIEFP 129
PEX-2N pfam09263
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a Cdc48 domain 2-like ...
19-98 5.32e-41

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: 286362  Cd Length: 81  Bit Score: 147.08  E-value: 5.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102    19 VAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSH-QPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLKPC 97
Cdd:pfam09263    1 VVFNNAKNCFLHLPSKLASQLRLQENQALELSWGHsQPVFLSWTENRSSSSQGENVVEINRQLGEKLGLKDGEQVFLRPC 80

                   .
gi 544186102    98 S 98
Cdd:pfam09263   81 T 81
PEX-1N pfam09262
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi ...
104-179 2.25e-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: 286361  Cd Length: 77  Bit Score: 119.52  E-value: 2.25e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544186102   104 QQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAAS-YGRLETDTKLLIQP 179
Cdd:pfam09262    1 TSVEVEPLTSDDWEILELHAEFLEDNLLSQVRVVSPGQILPVWVSGTTVAKFRVVSIEPSSSpFARLSPDTEVIVAP 77
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
581-642 6.52e-05

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  Cd Length: 151  Bit Score: 43.29  E-value: 6.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544186102  581 RQLMSLVAGLRNGALLLTGGKGSGKSTLAKAICKEAFDKlDAHVERVDCKALRALNDMIKEF 642
Cdd:cd00009     8 EALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRP-GAPFLYLNASDLLEGLVVAELF 68
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
595-1008 1.23e-98

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: 332.64  E-value: 1.23e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   595 LLLTGGKGSGKSTLAKAICKEA----------------------------------------FDKLDA----------HV 624
Cdd:TIGR01243  215 VLLYGPPGTGKTLLAKAVANEAgayfisingpeimskyygeseerlreifkeaeenapsiifIDEIDAiapkreevtgEV 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   625 ERVDCKALRALNDMIKEfisMGSLVALIATSQSQqSLHPLLVSAQGvhiFQCVQHIQPPNQEQRCEILCNVIKNKLDCDi 704
Cdd:TIGR01243  295 EKRVVAQLLTLMDGLKG---RGRVIVIGATNRPD-ALDPALRRPGR---FDREIVIRVPDKRARKEILKVHTRNMPLAE- 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   705 nkftDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSR-----------QSI--STREKLVLTTLDFQKALRGFLPASLRS 771
Cdd:TIGR01243  367 ----DVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfiregkinfeaEEIpaEVLKELKVTMKDFMEALKMVEPSAIRE 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   772 VNLHKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGP 851
Cdd:TIGR01243  443 VLVEVP-NVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   852 ELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHD-NTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPD 930
Cdd:TIGR01243  522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPD 601
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544186102   931 LIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHGMLLS 1008
Cdd:TIGR01243  602 ILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGS 679
 
Name Accession Description Interval E-value
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
820-949 6.06e-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: 278434  Cd Length: 130  Bit Score: 171.62  E-value: 6.06e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   820 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGV 899
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFVEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 544186102   900 TDRVVNQLLTQLDGVEGLQG-VYVLAATSRPDLIDPALLRpgRLDKCVYCP 949
Cdd:pfam00004   81 SRRVVNQLLTELDGFTSSLSkVIVIAATNRPDKLDPALLR--RFDRIIEFP 129
PEX-2N pfam09263
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a Cdc48 domain 2-like ...
19-98 5.32e-41

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: 286362  Cd Length: 81  Bit Score: 147.08  E-value: 5.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102    19 VAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSH-QPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLKPC 97
Cdd:pfam09263    1 VVFNNAKNCFLHLPSKLASQLRLQENQALELSWGHsQPVFLSWTENRSSSSQGENVVEINRQLGEKLGLKDGEQVFLRPC 80

                   .
gi 544186102    98 S 98
Cdd:pfam09263   81 T 81
PEX-1N pfam09262
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi ...
104-179 2.25e-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: 286361  Cd Length: 77  Bit Score: 119.52  E-value: 2.25e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544186102   104 QQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAAS-YGRLETDTKLLIQP 179
Cdd:pfam09262    1 TSVEVEPLTSDDWEILELHAEFLEDNLLSQVRVVSPGQILPVWVSGTTVAKFRVVSIEPSSSpFARLSPDTEVIVAP 77
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
812-950 1.82e-24

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  Cd Length: 151  Bit Score: 101.84  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  812 LPIRQRTGILLYGPPGTGKTLLAGVIARESRM---NFISVKGPELLSKYIGASEQ---AVRDIFIRAQAAKPCILFFDEF 885
Cdd:cd00009    14 LELPPPKNLLLYGPPGTGKTTLARAIANELFRpgaPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEI 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544186102  886 ESIAPRrghdntgVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPP 950
Cdd:cd00009    94 DSLSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
581-642 6.52e-05

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  Cd Length: 151  Bit Score: 43.29  E-value: 6.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544186102  581 RQLMSLVAGLRNGALLLTGGKGSGKSTLAKAICKEAFDKlDAHVERVDCKALRALNDMIKEF 642
Cdd:cd00009     8 EALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRP-GAPFLYLNASDLLEGLVVAELF 68
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
595-633 1.07e-04

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: 278434  Cd Length: 130  Bit Score: 42.20  E-value: 1.07e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 544186102   595 LLLTGGKGSGKSTLAKAICKEafdkLDAHVERVDCKALR 633
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKE----LGAPFVEISGSELV 35
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
595-1008 1.23e-98

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: 332.64  E-value: 1.23e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   595 LLLTGGKGSGKSTLAKAICKEA----------------------------------------FDKLDA----------HV 624
Cdd:TIGR01243  215 VLLYGPPGTGKTLLAKAVANEAgayfisingpeimskyygeseerlreifkeaeenapsiifIDEIDAiapkreevtgEV 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   625 ERVDCKALRALNDMIKEfisMGSLVALIATSQSQqSLHPLLVSAQGvhiFQCVQHIQPPNQEQRCEILCNVIKNKLDCDi 704
Cdd:TIGR01243  295 EKRVVAQLLTLMDGLKG---RGRVIVIGATNRPD-ALDPALRRPGR---FDREIVIRVPDKRARKEILKVHTRNMPLAE- 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   705 nkftDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSR-----------QSI--STREKLVLTTLDFQKALRGFLPASLRS 771
Cdd:TIGR01243  367 ----DVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfiregkinfeaEEIpaEVLKELKVTMKDFMEALKMVEPSAIRE 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   772 VNLHKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGP 851
Cdd:TIGR01243  443 VLVEVP-NVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   852 ELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHD-NTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPD 930
Cdd:TIGR01243  522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPD 601
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544186102   931 LIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHGMLLS 1008
Cdd:TIGR01243  602 ILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGS 679
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
595-1006 7.30e-92

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


Pssm-ID: 223540 [Multi-domain]  Cd Length: 494  Bit Score: 305.98  E-value: 7.30e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  595 LLLTGGKGSGKSTLAKAICKEA-------FDKLDAHVERVDCKALRALNDMIKEF----ISMGSLVALIATSQSQQSLHP 663
Cdd:COG0464    21 VLLHGPPGTGKTLLARALANEGaeflsinGPEILSKYVGESELRLRELFEEAEKLapsiIFIDEIDALAPKRSSDQGEVE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  664 LLVSAQGVHIFQCVQH------------------------------IQPPNQEQRCEILCNVIKNKLDCDinkftDLDLQ 713
Cdd:COG0464   101 RRVVAQLLALMDGLKRgqvivigatnrpdgldpakrrpgrfdreieVNLPDEAGRLEILQIHTRLMFLGP-----PGTGK 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  714 HVAKETGGFVARDFTVLVDRAIHSRLSRQSISTREKLVLTTLDFQKALRGFLPAslRSVNLHKPrDLGWDKIGGLHEVRQ 793
Cdd:COG0464   176 TLAARTVGKSGADLGALAKEAALRELRRAIDLVGEYIGVTEDDFEEALKKVLPS--RGVLFEDE-DVTLDDIGGLEEAKE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  794 ILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQ 873
Cdd:COG0464   253 ELKEAIETPLKRPELFRKLGLRPPKGVLLYGPPGTGKTLLAKAVALESRSRFISVKGSELLSKWVGESEKNIRELFEKAR 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  874 AAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQ 953
Cdd:COG0464   333 KLAPSIIFIDEIDSLASGRGPSEDGSGRRVVGQLLTELDGIEKAEGVLVIAATNRPDDLDPALLRPGRFDRLIYVPLPDL 412
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 544186102  954 VSRLEILNV-LSDS-LPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHGML 1006
Cdd:COG0464   413 EERLEIFKIhLRDKkPPLAEDVDLEELAEITEGYSGADIAALVREAALEALREAR 467
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
775-993 7.71e-67

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 231.64  E-value: 7.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  775 HKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELL 854
Cdd:PRK03992  124 ESP-NVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELV 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  855 SKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGvTDRVVN----QLLTQLDGVEGLQGVYVLAATSRPD 930
Cdd:PRK03992  203 QKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTS-GDREVQrtlmQLLAEMDGFDPRGNVKIIAATNRID 281
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544186102  931 LIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKAL 993
Cdd:PRK03992  282 ILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAI 344
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
820-952 6.83e-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: 6.83e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102    820 ILLYGPPGTGKTLLAGVIARESRMNFISVK-----------------GPELLSKYIGASEQAVRDIFIRAQAAKPCILFF 882
Cdd:smart00382    5 ILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDVLIL 84
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102    883 DEFESIaprrgHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPgRLDKCVYCPPPD 952
Cdd:smart00382   85 DEITSL-----LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
RuvB_N pfam05496
Holliday junction DNA helicase ruvB N-terminus; The RuvB protein makes up part of the RuvABC ...
820-853 8.87e-06

Holliday junction DNA helicase ruvB N-terminus; 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: 283214 [Multi-domain]  Cd Length: 234  Bit Score: 47.10  E-value: 8.87e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 544186102   820 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPEL 853
Cdd:pfam05496   53 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGPAI 86
 
Name Accession Description Interval E-value
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
820-949 6.06e-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: 278434  Cd Length: 130  Bit Score: 171.62  E-value: 6.06e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   820 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGV 899
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKELGAPFVEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDSE 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 544186102   900 TDRVVNQLLTQLDGVEGLQG-VYVLAATSRPDLIDPALLRpgRLDKCVYCP 949
Cdd:pfam00004   81 SRRVVNQLLTELDGFTSSLSkVIVIAATNRPDKLDPALLR--RFDRIIEFP 129
PEX-2N pfam09263
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a Cdc48 domain 2-like ...
19-98 5.32e-41

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: 286362  Cd Length: 81  Bit Score: 147.08  E-value: 5.32e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102    19 VAFTNARDCFLHLPRRLVAQLHLLQNQAIEVVWSH-QPAFLSWVEGRHFSDQGENVAEINRQVGQKLGLSNGGQVFLKPC 97
Cdd:pfam09263    1 VVFNNAKNCFLHLPSKLASQLRLQENQALELSWGHsQPVFLSWTENRSSSSQGENVVEINRQLGEKLGLKDGEQVFLRPC 80

                   .
gi 544186102    98 S 98
Cdd:pfam09263   81 T 81
PEX-1N pfam09262
Peroxisome biogenesis factor 1, N-terminal; Members of this family adopt a double psi ...
104-179 2.25e-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: 286361  Cd Length: 77  Bit Score: 119.52  E-value: 2.25e-31
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544186102   104 QQVEVEPLSADDWEILELHAVSLEQHLLDQIRIVFPKAIFPVWVDQQTYIFIQIVALIPAAS-YGRLETDTKLLIQP 179
Cdd:pfam09262    1 TSVEVEPLTSDDWEILELHAEFLEDNLLSQVRVVSPGQILPVWVSGTTVAKFRVVSIEPSSSpFARLSPDTEVIVAP 77
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
812-950 1.82e-24

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  Cd Length: 151  Bit Score: 101.84  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  812 LPIRQRTGILLYGPPGTGKTLLAGVIARESRM---NFISVKGPELLSKYIGASEQ---AVRDIFIRAQAAKPCILFFDEF 885
Cdd:cd00009    14 LELPPPKNLLLYGPPGTGKTTLARAIANELFRpgaPFLYLNASDLLEGLVVAELFghfLVRLLFELAEKAKPGVLFIDEI 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544186102  886 ESIAPRrghdntgVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPP 950
Cdd:cd00009    94 DSLSRG-------AQNALLRVLETLNDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRIVIPL 151
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
819-938 4.92e-05

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


Pssm-ID: 285029  Cd Length: 135  Bit Score: 43.43  E-value: 4.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   819 GILLYGPPGTGKTLLAGVIARE-SRMNFISVKGPELLSKY-------IGASEQAVRDIFIRAQAAKPCILFFDEFEsiap 890
Cdd:pfam07728    1 GVLLVGPPGTGKSTLARRLAAAlSNRPVFYVQLTRDTTEEdlkgrrnIGNGTTEWVDGPLVRAAREGEIAVLDEIN---- 76
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   891 rRGHDNtgVTDRVVNQL----LTQLDGVE----GLQGVYVLAATSRPDL----IDPALLR 938
Cdd:pfam07728   77 -RANPE--VLNSLLSLLderrLLLPEGGElvqaAPDDFRLIATMNPLDRglneLSPALRS 133
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
581-642 6.52e-05

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  Cd Length: 151  Bit Score: 43.29  E-value: 6.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544186102  581 RQLMSLVAGLRNGALLLTGGKGSGKSTLAKAICKEAFDKlDAHVERVDCKALRALNDMIKEF 642
Cdd:cd00009     8 EALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRP-GAPFLYLNASDLLEGLVVAELF 68
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
595-633 1.07e-04

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: 278434  Cd Length: 130  Bit Score: 42.20  E-value: 1.07e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 544186102   595 LLLTGGKGSGKSTLAKAICKEafdkLDAHVERVDCKALR 633
Cdd:pfam00004    1 LLLYGPPGTGKTTLAKAVAKE----LGAPFVEISGSELV 35
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
574-696 6.39e-04

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


Pssm-ID: 289934  Cd Length: 167  Bit Score: 40.60  E-value: 6.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   574 LLGR-PLSRQLMSLVAGLRNG---ALLLTGGKGSGKSTLAKAICKEAFDKlDAHVERVDCKALRALNDMIKEFISMGSLV 649
Cdd:pfam13191    2 LVGReAELERLLDALERVRSGrpgSVLLTGPSGTGKTSLLRELARRLARD-GGLFLRGKCDECIPYAPLLQALTRRGLLR 80
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 544186102   650 ALIATSQSQQslhPLLVSAQGVHIFQCVQHIQPPNQEQRCEILCNVI 696
Cdd:pfam13191   81 QLLTEEESAL---LEPWRARLLEALGPLPPLPPDEANRLLDALLRLL 124
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
820-890 6.91e-04

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


Pssm-ID: 285025  Cd Length: 165  Bit Score: 40.26  E-value: 6.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   820 ILLYGPPGTGKTLLAGVIARESRM---NFISVKGPELL-----SKYIGASEQAVRD----IFIRAQAAKP-CILFFDEFE 886
Cdd:pfam07724    4 FLFLGPTGVGKTELAKALAELLFGderALIRIDMSEYMeehsvSRLIGAPPGYVGYeeggQLTEAVRRKPySIVLIDEIE 83

                   ....
gi 544186102   887 SIAP 890
Cdd:pfam07724   84 KAHP 87
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the ...
807-885 5.96e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteristic of the AAA superfamily.


Pssm-ID: 289934  Cd Length: 167  Bit Score: 37.90  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   807 ELFANLPIRQRTGILLYGPPGTGKTLLAGVIAR---ESRMNFISVKGPELLSkYIGASEQAVRDIFIRAQAAKPCILFFD 883
Cdd:pfam13191   14 DALERVRSGRPGSVLLTGPSGTGKTSLLRELARrlaRDGGLFLRGKCDECIP-YAPLLQALTRRGLLRQLLTEEESALLE 92

                   ..
gi 544186102   884 EF 885
Cdd:pfam13191   93 PW 94
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
820-840 7.38e-03

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


Pssm-ID: 279280  Cd Length: 105  Bit Score: 36.44  E-value: 7.38e-03
                           10        20
                   ....*....|....*....|.
gi 544186102   820 ILLYGPPGTGKTLLAGVIARE 840
Cdd:pfam00910    1 IWLYGPPGCGKSTLAKYLARA 21
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
814-848 9.33e-03

IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is found associated with IS21 family insertion sequences. The function of this protein is unknown, but it may perform a transposase function.


Pssm-ID: 279959  Cd Length: 176  Bit Score: 37.30  E-value: 9.33e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 544186102   814 IRQRTGILLYGPPGTGKTLLAGVIARESRMNFISV 848
Cdd:pfam01695   43 IERHENIVLLGPPGTGKTHLACALGQAACRAGYSV 77
AAA_22 pfam13401
AAA domain;
593-644 9.57e-03

AAA domain;


Pssm-ID: 290137  Cd Length: 130  Bit Score: 36.55  E-value: 9.57e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 544186102   593 GALLLTGGKGSGKSTLAKAIcKEAFDKLDAHVERVDCKALRALNDMIKEFIS 644
Cdd:pfam13401    6 GILVLTGESGTGKTTLLRRL-LEQLDEADDSVVFVDLPSGTSPKDLLRALLR 56
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
595-1008 1.23e-98

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: 332.64  E-value: 1.23e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   595 LLLTGGKGSGKSTLAKAICKEA----------------------------------------FDKLDA----------HV 624
Cdd:TIGR01243  215 VLLYGPPGTGKTLLAKAVANEAgayfisingpeimskyygeseerlreifkeaeenapsiifIDEIDAiapkreevtgEV 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   625 ERVDCKALRALNDMIKEfisMGSLVALIATSQSQqSLHPLLVSAQGvhiFQCVQHIQPPNQEQRCEILCNVIKNKLDCDi 704
Cdd:TIGR01243  295 EKRVVAQLLTLMDGLKG---RGRVIVIGATNRPD-ALDPALRRPGR---FDREIVIRVPDKRARKEILKVHTRNMPLAE- 366
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   705 nkftDLDLQHVAKETGGFVARDFTVLVDRAIHSRLSR-----------QSI--STREKLVLTTLDFQKALRGFLPASLRS 771
Cdd:TIGR01243  367 ----DVDLDKLAEVTHGFVGADLAALAKEAAMAALRRfiregkinfeaEEIpaEVLKELKVTMKDFMEALKMVEPSAIRE 442
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   772 VNLHKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGP 851
Cdd:TIGR01243  443 VLVEVP-NVRWSDIGGLEEVKQELREAVEWPLKHPEIFEKMGIRPPKGVLLFGPPGTGKTLLAKAVATESGANFIAVRGP 521
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   852 ELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHD-NTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPD 930
Cdd:TIGR01243  522 EILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARfDTSVTDRIVNQLLTEMDGIQELSNVVVIAATNRPD 601
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 544186102   931 LIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHGMLLS 1008
Cdd:TIGR01243  602 ILDPALLRPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRESIGS 679
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
595-1006 7.30e-92

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


Pssm-ID: 223540 [Multi-domain]  Cd Length: 494  Bit Score: 305.98  E-value: 7.30e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  595 LLLTGGKGSGKSTLAKAICKEA-------FDKLDAHVERVDCKALRALNDMIKEF----ISMGSLVALIATSQSQQSLHP 663
Cdd:COG0464    21 VLLHGPPGTGKTLLARALANEGaeflsinGPEILSKYVGESELRLRELFEEAEKLapsiIFIDEIDALAPKRSSDQGEVE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  664 LLVSAQGVHIFQCVQH------------------------------IQPPNQEQRCEILCNVIKNKLDCDinkftDLDLQ 713
Cdd:COG0464   101 RRVVAQLLALMDGLKRgqvivigatnrpdgldpakrrpgrfdreieVNLPDEAGRLEILQIHTRLMFLGP-----PGTGK 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  714 HVAKETGGFVARDFTVLVDRAIHSRLSRQSISTREKLVLTTLDFQKALRGFLPAslRSVNLHKPrDLGWDKIGGLHEVRQ 793
Cdd:COG0464   176 TLAARTVGKSGADLGALAKEAALRELRRAIDLVGEYIGVTEDDFEEALKKVLPS--RGVLFEDE-DVTLDDIGGLEEAKE 252
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  794 ILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQ 873
Cdd:COG0464   253 ELKEAIETPLKRPELFRKLGLRPPKGVLLYGPPGTGKTLLAKAVALESRSRFISVKGSELLSKWVGESEKNIRELFEKAR 332
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  874 AAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQ 953
Cdd:COG0464   333 KLAPSIIFIDEIDSLASGRGPSEDGSGRRVVGQLLTELDGIEKAEGVLVIAATNRPDDLDPALLRPGRFDRLIYVPLPDL 412
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 544186102  954 VSRLEILNV-LSDS-LPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHGML 1006
Cdd:COG0464   413 EERLEIFKIhLRDKkPPLAEDVDLEELAEITEGYSGADIAALVREAALEALREAR 467
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
776-1002 3.76e-72

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


Pssm-ID: 224143 [Multi-domain]  Cd Length: 406  Bit Score: 247.18  E-value: 3.76e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  776 KPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLS 855
Cdd:COG1222   144 EKPDVTYEDIGGLDEQIQEIREVVELPLKNPELFEELGIDPPKGVLLYGPPGTGKTLLAKAVANQTDATFIRVVGSELVQ 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  856 KYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGvTDRVVN----QLLTQLDGVEGLQGVYVLAATSRPDL 931
Cdd:COG1222   224 KYIGEGARLVRELFELAREKAPSIIFIDEIDAIGAKRFDSGTS-GDREVQrtmlELLNQLDGFDPRGNVKVIMATNRPDI 302
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544186102  932 IDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEAL 1002
Cdd:COG1222   303 LDPALLRPGRFDRKIEFPLPDEEGRAEILKIHTRKMNLADDVDLELLARLTEGFSGADLKAICTEAGMFAI 373
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
765-1006 1.46e-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: 1.46e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   765 LPASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMN 844
Cdd:TIGR01243  160 REKPVREEIERKVPKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHLGIEPPKGVLLYGPPGTGKTLLAKAVANEAGAY 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   845 FISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLA 924
Cdd:TIGR01243  240 FISINGPEIMSKYYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMDGLKGRGRVIVIG 319
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   925 ATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHG 1004
Cdd:TIGR01243  320 ATNRPDALDPALRRPGRFDREIVIRVPDKRARKEILKVHTRNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRR 399

                   ..
gi 544186102  1005 ML 1006
Cdd:TIGR01243  400 FI 401
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
775-993 7.71e-67

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 231.64  E-value: 7.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  775 HKPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELL 854
Cdd:PRK03992  124 ESP-NVTYEDIGGLEEQIREVREAVELPLKKPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELV 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  855 SKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGvTDRVVN----QLLTQLDGVEGLQGVYVLAATSRPD 930
Cdd:PRK03992  203 QKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTS-GDREVQrtlmQLLAEMDGFDPRGNVKIIAATNRID 281
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544186102  931 LIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKAL 993
Cdd:PRK03992  282 ILDPAILRPGRFDRIIEVPLPDEEGRLEILKIHTRKMNLADDVDLEELAELTEGASGADLKAI 344
26Sp45 TIGR01242
26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an ...
776-1002 5.28e-64

26S proteasome subunit P45 family; Many proteins may score above the trusted cutoff because an internal


Pssm-ID: 130309 [Multi-domain]  Cd Length: 364  Bit Score: 222.75  E-value: 5.28e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   776 KPrDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLS 855
Cdd:TIGR01242  116 RP-NVSYEDIGGLEEQIREIREAVELPLKHPELFEEVGIEPPKGVLLYGPPGTGKTLLAKAVAHETNATFIRVVGSELVR 194
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   856 KYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGvTDRVVN----QLLTQLDGVEGLQGVYVLAATSRPDL 931
Cdd:TIGR01242  195 KYIGEGARLVREIFELAKEKAPSIIFIDEIDAIAAKRTDSGTS-GDREVQrtlmQLLAELDGFDPRGNVKVIAATNRPDI 273
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544186102   932 IDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEAL 1002
Cdd:TIGR01242  274 LDPALLRPGRFDRIIEVPLPDFEGRLEILKIHTRKMKLAEDVDLEAIAKMTEGASGADLKAICTEAGMFAI 344
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
783-1001 2.38e-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: 2.38e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   783 DKIGGLHEVRQILMDTIQLpAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASE 862
Cdd:TIGR01241   55 KDVAGIDEAKEELMEIVDF-LKNPSKFTKLGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   863 QAVRDIFIRAQAAKPCILFFDEFESIAPRRG------HDntgVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPAL 936
Cdd:TIGR01241  134 SRVRDLFEQAKKNAPCIIFIDEIDAVGRQRGaglgggND---EREQTLNQLLVEMDGFGTNTGVIVIAATNRPDVLDPAL 210
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544186102   937 LRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEA 1001
Cdd:TIGR01241  211 LRPGRFDRQVVVDLPDIKGREEILKVHAKNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLA 275
pup_AAA TIGR03689
proteasome ATPase; In the Actinobacteria, as shown for Mycobacterium tuberculosis, some ...
779-972 1.33e-50

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: 1.33e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   779 DLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIA----------RESRMNFISV 848
Cdd:TIGR03689  178 DVTYADIGGLGSQIEQIRDAVELPFLHPELYREYGLKPPKGVLLYGPPGCGKTLIAKAVAnslaarigaeGGGKSYFLNI 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   849 KGPELLSKYIGASEQAVRDIFIRAQAA----KPCILFFDEFESIAPRRGhdnTGVTD----RVVNQLLTQLDGVEGLQGV 920
Cdd:TIGR03689  258 KGPELLNKYVGETERQIRLIFQRAREKasegRPVIVFFDEMDSLFRTRG---SGVSSdvetTVVPQLLAEIDGVESLDNV 334
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 544186102   921 YVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEIL-NVLSDSLPLADD 972
Cdd:TIGR03689  335 IVIGASNREDMIDPAILRPGRLDVKIRIERPDAEAAADIFaKYLTDDLPLPED 387
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
767-1002 1.04e-49

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 182.66  E-value: 1.04e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  767 ASLRSVNLHKPRDLGWDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFI 846
Cdd:PTZ00454  129 SSIQLLQMSEKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQIGIDPPRGVLLYGPPGTGKTMLAKAVAHHTTATFI 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  847 SVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGV---TDRVVNQLLTQLDGVEGLQGVYVL 923
Cdd:PTZ00454  209 RVVGSEFVQKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGAdreVQRILLELLNQMDGFDQTTNVKVI 288
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544186102  924 AATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEAL 1002
Cdd:PTZ00454  289 MATNRADTLDPALLRPGRLDRKIEFPLPDRRQKRLIFQTITSKMNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAV 367
ftsH CHL00176
cell division protein; Validated
783-999 1.28e-48

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 184.10  E-value: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  783 DKIGGLHEVRQILMDTIQLpAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASE 862
Cdd:CHL00176  183 RDIAGIEEAKEEFEEVVSF-LKKPERFTAVGAKIPKGVLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEMFVGVGA 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  863 QAVRDIFIRAQAAKPCILFFDEFESIAPRRGhdnTGV------TDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPAL 936
Cdd:CHL00176  262 ARVRDLFKKAKENSPCIVFIDEIDAVGRQRG---AGIgggndeREQTLNQLLTEMDGFKGNKGVIVIAATNRVDILDAAL 338
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 544186102  937 LRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQL 999
Cdd:CHL00176  339 LRPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVSLELIARRTPGFSGADLANLLNEAAI 401
hflB PRK10733
ATP-dependent metalloprotease; Reviewed
795-1004 7.75e-48

ATP-dependent metalloprotease; Reviewed


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 181.77  E-value: 7.75e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  795 LMDTIQLPAKYPELFANLPirqrTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQA 874
Cdd:PRK10733  167 LVEYLREPSRFQKLGGKIP----KGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGVGASRVRDMFEQAKK 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  875 AKPCILFFDEFESIAPRRG------HDNTgvtDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYC 948
Cdd:PRK10733  243 AAPCIIFIDEIDAVGRQRGaglgggHDER---EQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVV 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 544186102  949 PPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHG 1004
Cdd:PRK10733  320 GLPDVRGREQILKVHMRRVPLAPDIDAAIIARGTPGFSGADLANLVNEAALFAARG 375
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
782-1002 1.48e-46

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 174.57  E-value: 1.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  782 WDKIGGLHEVRQILMDTIQLPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGAS 861
Cdd:PTZ00361  182 YADIGGLEQQIQEIKEAVELPLTHPELYDDIGIKPPKGVILYGPPGTGKTLLAKAVANETSATFLRVVGSELIQKYLGDG 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  862 EQAVRDIFIRAQAAKPCILFFDEFESIAPRRGHDNTGVT---DRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLR 938
Cdd:PTZ00361  262 PKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEkeiQRTMLELLNQLDGFDSRGDVKVIMATNRIESLDPALIR 341
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544186102  939 PGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEAL 1002
Cdd:PTZ00361  342 PGRIDRKIEFPNPDEKTKRRIFEIHTSKMTLAEDVDLEEFIMAKDELSGADIKAICTEAGLLAL 405
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
801-1004 6.70e-44

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


Pssm-ID: 223540 [Multi-domain]  Cd Length: 494  Bit Score: 167.69  E-value: 6.70e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  801 LPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMnFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCIL 880
Cdd:COG0464     2 LPLKEPELFKKLGIEPPKGVLLHGPPGTGKTLLARALANEGAE-FLSINGPEILSKYVGESELRLRELFEEAEKLAPSII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  881 FFDEFESIAPRRGHDNTGVTDRVVNQLLTQLDGVEGLQgVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEIL 960
Cdd:COG0464    81 FIDEIDALAPKRSSDQGEVERRVVAQLLALMDGLKRGQ-VIVIGATNRPDGLDPAKRRPGRFDREIEVNLPDEAGRLEIL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 544186102  961 NVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEALHG 1004
Cdd:COG0464   160 QIHTRLMFLGPPGTGKTLAARTVGKSGADLGALAKEAALRELRR 203
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
783-1001 7.92e-44

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


Pssm-ID: 223541 [Multi-domain]  Cd Length: 596  Bit Score: 169.04  E-value: 7.92e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  783 DKIGGLHEVRQILMDTIQlPAKYPELFANLPIRQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASE 862
Cdd:COG0465   150 ADVAGVDEAKEELSELVD-FLKNPKKYQALGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGA 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  863 QAVRDIFIRAQAAKPCILFFDEFESIAPRR------GHDNTgvtDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPAL 936
Cdd:COG0465   229 SRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglggGNDER---EQTLNQLLVEMDGFGGNEGVIVIAATNRPDVLDPAL 305
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 544186102  937 LRPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGADLKALLYNAQLEA 1001
Cdd:COG0465   306 LRPGRFDRQILVELPDIKGREQILKVHAKNKPLAEDVDLKKIARGTPGFSGADLANLLNEAALLA 370
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
778-1000 1.10e-37

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


Pssm-ID: 224144 [Multi-domain]  Cd Length: 368  Bit Score: 146.50  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  778 RDLGWDKIGGLHEVRQ---ILMDTIqlpaKYPELFANLPIRQrtgILLYGPPGTGKTLLAGVIARESRMNFISVKGPELL 854
Cdd:COG1223   116 SDITLDDVIGQEEAKRkcrLIMEYL----ENPERFGDWAPKN---VLFYGPPGTGKTMMAKALANEAKVPLLLVKATELI 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  855 SKYIGASEQAVRDIFIRAQAAKPCILFFDEFESIA-PRRGHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLID 933
Cdd:COG1223   189 GEHVGDGARRIHELYERARKAAPCIVFIDELDAIAlDRRYQELRGDVSEIVNALLTELDGIKENEGVVTIAATNRPELLD 268
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544186102  934 PALlrPGRLDKCVYCPPPDQVSRLEILNVLSDSLPLADDVDLQHVASVTDSFTGAD-----LKALLYNAQLE 1000
Cdd:COG1223   269 PAI--RSRFEEEIEFKLPNDEERLEILEYYAKKFPLPVDADLRYLAAKTKGMSGRDikekvLKTALHRAIAE 338
ycf46 CHL00195
Ycf46; Provisional
819-1003 9.77e-15

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 76.98  E-value: 9.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  819 GILLYGPPGTGKTLLAGVIARESRMNFISVKGPELLSKYIGASEQAVRDIFIRAQAAKPCILFFDEFE-SIAPRRGHDNT 897
Cdd:CHL00195  261 GLLLVGIQGTGKSLTAKAIANDWQLPLLRLDVGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDkAFSNSESKGDS 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  898 GVTDRVVNQLLTQLDgvEGLQGVYVLAATSRPDLIDPALLRPGRLDKCVYCPPPDQVSRLEILNV-LSDSLPLA-DDVDL 975
Cdd:CHL00195  341 GTTNRVLATFITWLS--EKKSPVFVVATANNIDLLPLEILRKGRFDEIFFLDLPSLEEREKIFKIhLQKFRPKSwKKYDI 418
                         170       180
                  ....*....|....*....|....*...
gi 544186102  976 QHVASVTDSFTGADlkalLYNAQLEALH 1003
Cdd:CHL00195  419 KKLSKLSNKFSGAE----IEQSIIEAMY 442
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
820-952 6.83e-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: 6.83e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102    820 ILLYGPPGTGKTLLAGVIARESRMNFISVK-----------------GPELLSKYIGASEQAVRDIFIRAQAAKPCILFF 882
Cdd:smart00382    5 ILIVGPPGSGKTTLARALARELGPPGGGVIyidgedileevldqlllIIVGGKKASGSGELRLRLALALARKLKPDVLIL 84
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102    883 DEFESIaprrgHDNTGVTDRVVNQLLTQLDGVEGLQGVYVLAATSRPDLIDPALLRPgRLDKCVYCPPPD 952
Cdd:smart00382   85 DEITSL-----LDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
820-884 2.12e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 53.16  E-value: 2.12e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 544186102  820 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPEllskyigASEQAVRDIFIRAQAA----KPCILFFDE 884
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 ...
812-912 9.53e-07

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: 9.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   812 LPIRQRTG-ILLYGPPGTGKTLLA----------GVIAREsrmNFISVKGPELLSKYIGASEQAVRDIFIRAQAAkpcIL 880
Cdd:TIGR03922  306 LPVAQTSNhMLFAGPPGTGKTTIArvvakiycglGVLRKP---LVREVSRADLIGQYIGESEAKTNEIIDSALGG---VL 379
                           90       100       110
                   ....*....|....*....|....*....|..
gi 544186102   881 FFDEFESIAPRRGHDNTGVTDRVVNQLLTQLD 912
Cdd:TIGR03922  380 FLDEAYTLVETGYGQKDPFGLEAIDTLLARME 411
ruvB PRK00080
Holliday junction DNA helicase RuvB; Reviewed
820-853 1.65e-06

Holliday junction DNA helicase RuvB; Reviewed


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 50.13  E-value: 1.65e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 544186102  820 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPEL 853
Cdd:PRK00080   54 VLLYGPPGLGKTTLANIIANEMGVNIRITSGPAL 87
spore_V_K TIGR02881
stage V sporulation protein K; Members of this protein family are the stage V sporulation ...
787-893 4.28e-06

stage V sporulation protein K; Members of this protein family are the stage V sporulation protein K (SpoVK), a close homolog of the Rubisco expression protein CbbX (TIGR02880) and a members of the ATPase family associated with various cellular activities (pfam00004). Members are strictly limited to bacterial endospore-forming species, but are not universal in this group and are missing from the Clostridium group. [Cellular processes, Sporulation and germination]


Pssm-ID: 163057 [Multi-domain]  Cd Length: 261  Bit Score: 48.56  E-value: 4.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   787 GLHEVRQILMdtiqlpakypELFANLPIRQRTG------------ILLYGPPGTGKTLLAGVIARESR-MN------FIS 847
Cdd:TIGR02881   10 GLDEVKALIK----------EIYAWIQINEKRKeeglktskqvlhMIFKGNPGTGKTTVARILGKLFKeMNvlskghLIE 79
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 544186102   848 VKGPELLSKYIGASEQAVRDIFIRAQAAkpcILFFDEFESIAprRG 893
Cdd:TIGR02881   80 VERADLVGEYIGHTAQKTREVIKKALGG---VLFIDEAYSLA--RG 120
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
822-884 5.57e-06

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


Pssm-ID: 225165 [Multi-domain]  Cd Length: 436  Bit Score: 48.77  E-value: 5.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 544186102  822 LYGPPGTGKTLLAGVIARESRMNFISVKGpellskyIGASEQAVRDIFIRAQ----AAKPCILFFDE 884
Cdd:COG2256    53 LWGPPGTGKTTLARLIAGTTNAAFEALSA-------VTSGVKDLREIIEEARknrlLGRRTILFLDE 112
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit [Replication, ...
820-853 6.05e-06

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


Pssm-ID: 225164 [Multi-domain]  Cd Length: 332  Bit Score: 48.32  E-value: 6.05e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 544186102  820 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPEL 853
Cdd:COG2255    55 VLLFGPPGLGKTTLAHIIANELGVNLKITSGPAL 88
RuvB_N pfam05496
Holliday junction DNA helicase ruvB N-terminus; The RuvB protein makes up part of the RuvABC ...
820-853 8.87e-06

Holliday junction DNA helicase ruvB N-terminus; 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: 283214 [Multi-domain]  Cd Length: 234  Bit Score: 47.10  E-value: 8.87e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 544186102   820 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPEL 853
Cdd:pfam05496   53 VLLYGPPGLGKTTLAHIIANEMGVNIRITSGPAI 86
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
819-866 2.34e-05

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


Pssm-ID: 224145 [Multi-domain]  Cd Length: 450  Bit Score: 46.96  E-value: 2.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 544186102  819 GILLYGPPGTGKTLLAGVIARE--SRMNFISVKGPELLSKYIGASE---QAVR 866
Cdd:COG1224    67 GILIVGPPGTGKTALAMGIARElgEDVPFVAISGSEIYSLEVKKTEaltQALR 119
PRK13341 PRK13341
recombination factor protein RarA/unknown domain fusion protein; Reviewed
821-884 3.29e-05

recombination factor protein RarA/unknown domain fusion protein; Reviewed


Pssm-ID: 237354 [Multi-domain]  Cd Length: 725  Bit Score: 46.59  E-value: 3.29e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 544186102  821 LLYGPPGTGKTLLAGVIARESRMNFIS-------VKgpELLSKYIGASEQavrdifiRAQAAKPCILFFDE 884
Cdd:PRK13341   56 ILYGPPGVGKTTLARIIANHTRAHFSSlnavlagVK--DLRAEVDRAKER-------LERHGKRTILFIDE 117
TIP49 pfam06068
TIP49 C-terminus; This family consists of the C-terminal region of several eukaryotic and ...
819-866 4.79e-05

TIP49 C-terminus; 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: 283678 [Multi-domain]  Cd Length: 395  Bit Score: 45.76  E-value: 4.79e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 544186102   819 GILLYGPPGTGKTLLAGVIARE--SRMNFISVKGPELLSKYIGASE---QAVR 866
Cdd:pfam06068   52 AVLLAGPPGTGKTALAIAISKElgEDTPFCPISGSEVYSLEMKKTEaltQAFR 104
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
820-890 2.10e-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: 2.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 544186102   820 ILLYGPPGTGKTLLAGVIARESRMNFISVKGPELlskyigaseQAVRDIF-IRAQAAKPCILFFDEFESIAP 890
Cdd:TIGR00635   33 LLLYGPPGLGKTTLAHIIANEMGVNLKITSGPAL---------EKPGDLAaILTNLEEGDVLFIDEIHRLSP 95
PRK08116 PRK08116
hypothetical protein; Validated
815-872 2.36e-04

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 43.09  E-value: 2.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 544186102  815 RQRTGILLYGPPGTGKTLLAGVIARESRMNFISVKG---PELLSK---YIGASEQAVRDIFIRA 872
Cdd:PRK08116  112 KENVGLLLWGSVGTGKTYLAACIANELIEKGVPVIFvnfPQLLNRiksTYKSSGKEDENEIIRS 175
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
816-885 5.23e-04

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


Pssm-ID: 224401 [Multi-domain]  Cd Length: 254  Bit Score: 42.01  E-value: 5.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102  816 QRTGILLYGPPGTGKTLLAGVIARES-----RMNFISVkgPELLSKYI-----GASEQAVRDIFIRAQaakpcILFFDEF 885
Cdd:COG1484   104 RGENLVLLGPPGVGKTHLAIAIGNELlkagiSVLFITA--PDLLSKLKaafdeGRLEEKLLRELKKVD-----LLIIDDI 176
PRK04195 PRK04195
replication factor C large subunit; Provisional
820-845 6.66e-04

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 42.22  E-value: 6.66e-04
                          10        20
                  ....*....|....*....|....*.
gi 544186102  820 ILLYGPPGTGKTLLAGVIAREsrMNF 845
Cdd:PRK04195   42 LLLYGPPGVGKTSLAHALAND--YGW 65
clpX TIGR00382
endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent ...
816-916 9.42e-04

endopeptidase Clp ATP-binding regulatory subunit (clpX); A member of the ATP-dependent proteases, ClpX has ATP-dependent chaperone activity and is required for specific ATP-dependent proteolytic activities expressed by ClpPX. The gene is also found to be involved in stress tolerance in Bacillus subtilis and is essential for the efficient acquisition of genes specifying type IA and IB restriction. [Protein fate, Protein folding and stabilization, Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273047 [Multi-domain]  Cd Length: 413  Bit Score: 41.68  E-value: 9.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 544186102   816 QRTGILLYGPPGTGKTLLAGVIARESRMNFISVKGPELL-SKYIGaseQAVRDIFIR--------AQAAKPCILFFDEFE 886
Cdd:TIGR00382  115 SKSNILLIGPTGSGKTLLAQTLARILNVPFAIADATTLTeAGYVG---EDVENILLKllqaadydVEKAQKGIIYIDEID 191
                           90       100       110
                   ....*....|....*....|....*....|....
gi 544186102   887 SIAprRGHDNTGVTDRV----VNQLLTQLdgVEG 916
Cdd:TIGR00382  192 KIS--RKSENPSITRDVsgegVQQALLKI--IEG 221
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
591-647 1.74e-03

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: 38.89  E-value: 1.74e-03
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 544186102    591 RNGALLLTGGKGSGKSTLAKAICKEaFDKLDAHVERVDCKALRALNDMIKEFISMGS 647
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARE-LGPPGGGVIYIDGEDILEEVLDQLLLIIVGG 56
MoxR COG0714
MoxR-like ATPase [General function prediction only];
820-885 6.18e-03

MoxR-like ATPase [General function prediction only];


Pssm-ID: 223786 [Multi-domain]  Cd Length: 329  Bit Score: 38.96  E-value: 6.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 544186102  820 ILLYGPPGTGKTLLAGVIARESRMNFISVKG-PELL-SKYIGASEQAVRDIFIRAQAAKP--------CILFFDEF 885
Cdd:COG0714    46 VLLEGPPGVGKTLLARALARALGLPFVRIQCtPDLLpSDLLGTYAYAALLLEPGEFRFVPgplfaavrVILLLDEI 121
rfc PRK00440
replication factor C small subunit; Reviewed
820-846 6.60e-03

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 38.70  E-value: 6.60e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 544186102  820 ILLYGPPGTGKTLLAGVIARES-----RMNFI 846
Cdd:PRK00440   41 LLFAGPPGTGKTTAALALARELygedwRENFL 72
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.15
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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