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Conserved domains on  [gi|86561515|ref|NP_490816|]
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vesicle-fusing ATPase [Caenorhabditis elegans]

Protein Classification

vacuolar protein sorting-associated protein 4( domain architecture ID 15269737)

vacuolar protein sorting-associated protein 4 is an ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain.

CATH:  1.10.8.60
Gene Ontology:  GO:0005524|GO:0016887|GO:0007033|GO:0015031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 112-282 1.80e-126

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: 362.64  E-value: 1.80e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 112 KPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAgESTFFSISSSDLMSK 191
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEA-NSTFFSVSSSDLVSK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 192 WLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLNNDGILVLGATNIPWILDSA 271
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                       170
                ....*....|.
gi 86561515 272 IRRRFEKRIYI 282
Cdd:cd19521 160 IRRRFEKRIYI 170
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-79 1.52e-33

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


:

Pssm-ID: 239141  Cd Length: 75  Bit Score: 120.45  E-value: 1.52e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86561515   4 PALQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKYESQGdKQRNAIRDKVGQYLNRAEQIKTHLKDGKT 79
Cdd:cd02678   1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNP-KSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 365-425 1.62e-29

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


:

Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 109.12  E-value: 1.62e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86561515   365 LTPCSPGDPHAIAMNWLDVPGDKLANPPLSMQDISRSLASVKPTVNNTDLDRLEAFKNDFG 425
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPSDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 307-350 2.58e-08

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: 49.84  E-value: 2.58e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 86561515   307 DQDFKVLAERCEGYSGYDISILVKDALMQPVRRVQSATHFKHVS 350
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 112-282 1.80e-126

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: 362.64  E-value: 1.80e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 112 KPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAgESTFFSISSSDLMSK 191
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEA-NSTFFSVSSSDLVSK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 192 WLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLNNDGILVLGATNIPWILDSA 271
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                       170
                ....*....|.
gi 86561515 272 IRRRFEKRIYI 282
Cdd:cd19521 160 IRRRFEKRIYI 170
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 100-339 1.74e-84

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 261.48  E-value: 1.74e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 100 FQDKLSGAIVMEKPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFT--GnRKPWQGILLFGPPGTGKSYIAKAVATEAGe 177
Cdd:COG1222  60 LGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyG-IEPPKGVLLYGPPGTGKTLLAKAVAGELG- 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 178 STFFSISSSDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDN-ESESARRIKTEFMVQMQGVGlNNDGI 256
Cdd:COG1222 138 APFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDgTSGEVQRTVNQLLAELDGFE-SRGDV 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 257 LVLGATNIPWILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALM 334
Cdd:COG1222 217 LIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHL-RDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGM 295


                ....*
gi 86561515 335 QPVRR 339
Cdd:COG1222 296 FAIRE 300
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 108-426 5.81e-65

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: 221.32  E-value: 5.81e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   108 IVMEKPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFT--GNRKPwQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISS 185
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESG-ANFIAVRG 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   186 SDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESAR-RIKTEFMVQMQGVgLNNDGILVLGATNI 264
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTdRIVNQLLTEMDGI-QELSNVVVIAATNR 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   265 PWILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALMQPVRRVqs 342
Cdd:TIGR01243 600 PDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHT-RSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRES-- 676

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   343 athfkhVSGPSPKDPNVIAHDLLTPCSpgdphaiamnwldvpgdklanppLSMQDISRSLASVKPTVNNTDLDRLEAFKN 422
Cdd:TIGR01243 677 ------IGSPAKEKLEVGEEEFLKDLK-----------------------VEMRHFLEALKKVKPSVSKEDMLRYERLAK 727


                  ....
gi 86561515   423 DFGQ 426
Cdd:TIGR01243 728 ELKR 731
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 109-339 1.47e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 204.30  E-value: 1.47e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  109 VMEKPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFtgnRK----PWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSIS 184
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF---EEvgiePPKGVLLYGPPGTGKTLLAKAVAHETN-ATFIRVV 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  185 SSDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFM---VQMQGVGlNNDGILVLGA 261
Cdd:PRK03992 198 GSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMqllAEMDGFD-PRGNVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  262 TNIPWILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALMQPVRR 339
Cdd:PRK03992 277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHT-RKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 154-284 3.87e-55

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: 178.94  E-value: 3.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   154 ILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESE 233
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELG-APFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 86561515   234 SARRIKTEFMVQMQGVGLNNDGILVLGATNIPWILDSAIRRRFEKRIYIPL 284
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-79 1.52e-33

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 120.45  E-value: 1.52e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86561515   4 PALQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKYESQGdKQRNAIRDKVGQYLNRAEQIKTHLKDGKT 79
Cdd:cd02678   1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNP-KSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 365-425 1.62e-29

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 109.12  E-value: 1.62e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86561515   365 LTPCSPGDPHAIAMNWLDVPGDKLANPPLSMQDISRSLASVKPTVNNTDLDRLEAFKNDFG 425
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPSDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 6-71 4.93e-24

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 94.53  E-value: 4.93e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86561515     6 LQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKyESQGDKQRNAIRDKVGQYLNRAEQIK 71
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALK-ETKNEERRELLRAKIAEYLERAEELK 65
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 150-286 8.26e-21

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: 88.20  E-value: 8.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515    150 PWQGILLFGPPGTGKSYIAKAVATEAGEST--FFSISSSDLMS--------------KWLGESEKLVKNLFALAREHKPS 213
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86561515    214 IIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGvglnndGILVLGATNIPWILDSA-IRRRFEKRIYIPLPD 286
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK------NLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
4-76 5.35e-20

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 83.51  E-value: 5.35e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86561515      4 PALQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKYESqGDKQRNAIRDKVGQYLNRAEQIKTHLKD 76
Cdd:smart00745   3 DYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVES-DSKRREALKAKAAEYLDRAEEIKKSLLE 74
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 307-350 2.58e-08

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: 49.84  E-value: 2.58e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 86561515   307 DQDFKVLAERCEGYSGYDISILVKDALMQPVRRVQSATHFKHVS 350
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 152-220 1.55e-06

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 49.01  E-value: 1.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86561515  152 QGILLFGPPGTGKSYIAKAV---ATEAGESTFFsISSSDLMSKW-LGESE-KLVKNLFALARehkPSIIFIDEI 220
Cdd:NF038214  91 ENVLLLGPPGTGKTHLAIALgyaACRQGYRVRF-TTAADLVEQLaQARADgRLGRLLRRLAR---YDLLIIDEL 160
 
Name Accession Description Interval E-value
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 112-282 1.80e-126

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: 362.64  E-value: 1.80e-126
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 112 KPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAgESTFFSISSSDLMSK 191
Cdd:cd19521   1 KPNVKWEDVAGLEGAKEALKEAVILPVKFPHLFTGNRKPWSGILLYGPPGTGKSYLAKAVATEA-NSTFFSVSSSDLVSK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 192 WLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLNNDGILVLGATNIPWILDSA 271
Cdd:cd19521  80 WMGESEKLVKQLFAMARENKPSIIFIDEVDSLCGTRGEGESEASRRIKTELLVQMNGVGNDSQGVLVLGATNIPWQLDSA 159

                       170
                ....*....|.
gi 86561515 272 IRRRFEKRIYI 282
Cdd:cd19521 160 IRRRFEKRIYI 170
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 120-282 6.57e-94

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: 279.62  E-value: 6.57e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 120 IAGLEGAKEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESEKL 199
Cdd:cd19509   1 IAGLDDAKEALKEAVILPSLRPDLFPGLRGPPRGILLYGPPGTGKTLLARAVASESG-STFFSISASSLVSKWVGESEKI 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 200 VKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLN-NDGILVLGATNIPWILDSAIRRRFEK 278
Cdd:cd19509  80 VRALFALARELQPSIIFIDEIDSLLSERGSGEHEASRRVKTEFLVQMDGVLNKpEDRVLVLGATNRPWELDEAFLRRFEK 159


                ....
gi 86561515 279 RIYI 282
Cdd:cd19509 160 RIYI 163
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 100-339 1.74e-84

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 261.48  E-value: 1.74e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 100 FQDKLSGAIVMEKPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFT--GnRKPWQGILLFGPPGTGKSYIAKAVATEAGe 177
Cdd:COG1222  60 LGTPRGTAVPAESPDVTFDDIGGLDEQIEEIREAVELPLKNPELFRkyG-IEPPKGVLLYGPPGTGKTLLAKAVAGELG- 137

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 178 STFFSISSSDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDN-ESESARRIKTEFMVQMQGVGlNNDGI 256
Cdd:COG1222 138 APFIRVRGSELVSKYIGEGARNVREVFELAREKAPSIIFIDEIDAIAARRTDDgTSGEVQRTVNQLLAELDGFE-SRGDV 216

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 257 LVLGATNIPWILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALM 334
Cdd:COG1222 217 LIIAATNRPDLLDPALLRpgRFDRVIEVPLPDEEAREEILKIHL-RDMPLADDVDLDKLAKLTEGFSGADLKAIVTEAGM 295


                ....*
gi 86561515 335 QPVRR 339
Cdd:COG1222 296 FAIRE 300
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 108-282 2.16e-76

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: 235.65  E-value: 2.16e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 108 IVMEKPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSD 187
Cdd:cd19525  12 IMDHGPPINWADIAGLEFAKKTIKEIVVWPMLRPDIFTGLRGPPKGILLFGPPGTGKTLIGKCIASQSG-ATFFSISASS 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 188 LMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLN-NDGILVLGATNIPW 266
Cdd:cd19525  91 LTSKWVGEGEKMVRALFSVARCKQPAVIFIDEIDSLLSQRGEGEHESSRRIKTEFLVQLDGATTSsEDRILVVGATNRPQ 170

                       170
                ....*....|....*.
gi 86561515 267 ILDSAIRRRFEKRIYI 282
Cdd:cd19525 171 EIDEAARRRLVKRLYI 186
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 119-282 3.71e-75

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: 232.18  E-value: 3.71e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 119 DIAGLEGAKEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESEK 198
Cdd:cd19522   1 DIADLEEAKKLLEEAVVLPMWMPEFFKGIRRPWKGVLMVGPPGTGKTLLAKAVATECG-TTFFNVSSSTLTSKYRGESEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 199 LVKNLFALAREHKPSIIFIDEIDSLCSAR-SDNESESARRIKTEFMVQMQGVG--LNNDG----ILVLGATNIPWILDSA 271
Cdd:cd19522  80 LVRLLFEMARFYAPTTIFIDEIDSICSRRgTSEEHEASRRVKSELLVQMDGVGgaSENDDpskmVMVLAATNFPWDIDEA 159

                       170
                ....*....|.
gi 86561515 272 IRRRFEKRIYI 282
Cdd:cd19522 160 LRRRLEKRIYI 170
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 119-282 2.71e-70

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: 219.34  E-value: 2.71e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 119 DIAGLEGAKEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAgESTFFSISSSDLMSKWLGESEK 198
Cdd:cd19524   1 DIAGQDLAKQALQEMVILPSLRPELFTGLRAPARGLLLFGPPGNGKTMLAKAVAAES-NATFFNISAASLTSKYVGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 199 LVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLN-NDGILVLGATNIPWILDSAIRRRFE 277
Cdd:cd19524  80 LVRALFAVARELQPSIIFIDEVDSLLSERSEGEHEASRRLKTEFLIEFDGVQSNgDDRVLVMGATNRPQELDDAVLRRFT 159


                ....*
gi 86561515 278 KRIYI 282
Cdd:cd19524 160 KRVYV 164
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 117-342 1.45e-68

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: 222.86  E-value: 1.45e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 117 WTDIAGLEGAKEALKEAVILPIKFPQLFTGNRKPWQ-GILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGE 195
Cdd:COG0464 156 LDDLGGLEEVKEELRELVALPLKRPELREEYGLPPPrGLLLYGPPGTGKTLLARALAGELG-LPLIEVDLSDLVSKYVGE 234

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 196 SEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVglnNDGILVLGATNIPWILDSAIRRR 275
Cdd:COG0464 235 TEKNLREVFDKARGLAPCVLFIDEADALAGKRGEVGDGVGRRVVNTLLTEMEEL---RSDVVVIAATNRPDLLDPALLRR 311

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86561515 276 FEKRIYIPLPDIHARKEMFRIdVGKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALMQPVRRVQS 342
Cdd:COG0464 312 FDEIIFFPLPDAEERLEIFRI-HLRKRPLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGRE 377
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 108-426 5.81e-65

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: 221.32  E-value: 5.81e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   108 IVMEKPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFT--GNRKPwQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISS 185
Cdd:TIGR01243 443 VLVEVPNVRWSDIGGLEEVKQELREAVEWPLKHPEIFEkmGIRPP-KGVLLFGPPGTGKTLLAKAVATESG-ANFIAVRG 520

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   186 SDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESAR-RIKTEFMVQMQGVgLNNDGILVLGATNI 264
Cdd:TIGR01243 521 PEILSKWVGESEKAIREIFRKARQAAPAIIFFDEIDAIAPARGARFDTSVTdRIVNQLLTEMDGI-QELSNVVVIAATNR 599

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   265 PWILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALMQPVRRVqs 342
Cdd:TIGR01243 600 PDILDPALLRpgRFDRLILVPPPDEEARKEIFKIHT-RSMPLAEDVDLEELAEMTEGYTGADIEAVCREAAMAALRES-- 676

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   343 athfkhVSGPSPKDPNVIAHDLLTPCSpgdphaiamnwldvpgdklanppLSMQDISRSLASVKPTVNNTDLDRLEAFKN 422
Cdd:TIGR01243 677 ------IGSPAKEKLEVGEEEFLKDLK-----------------------VEMRHFLEALKKVKPSVSKEDMLRYERLAK 727


                  ....
gi 86561515   423 DFGQ 426
Cdd:TIGR01243 728 ELKR 731
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 109-339 1.47e-61

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 204.30  E-value: 1.47e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  109 VMEKPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFtgnRK----PWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSIS 184
Cdd:PRK03992 122 VIESPNVTYEDIGGLEEQIREVREAVELPLKKPELF---EEvgiePPKGVLLYGPPGTGKTLLAKAVAHETN-ATFIRVV 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  185 SSDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFM---VQMQGVGlNNDGILVLGA 261
Cdd:PRK03992 198 GSELVQKFIGEGARLVRELFELAREKAPSIIFIDEIDAIAAKRTDSGTSGDREVQRTLMqllAEMDGFD-PRGNVKIIAA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  262 TNIPWILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALMQPVRR 339
Cdd:PRK03992 277 TNRIDILDPAILRpgRFDRIIEVPLPDEEGRLEILKIHT-RKMNLADDVDLEELAELTEGASGADLKAICTEAGMFAIRD 355
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 119-282 5.05e-59

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: 190.33  E-value: 5.05e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 119 DIAGLEGAKEALKEAVILPIKFPQLFTGNR--KPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGES 196
Cdd:cd19520   1 DIGGLDEVITELKELVILPLQRPELFDNSRllQPPKGVLLYGPPGCGKTMLAKATAKEAG-ARFINLQVSSLTDKWYGES 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 197 EKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLN-NDGILVLGATNIPWILDSAIRRR 275
Cdd:cd19520  80 QKLVAAVFSLASKLQPSIIFIDEIDSFLRQRSSTDHEATAMMKAEFMSLWDGLSTDgNCRVIVMGATNRPQDLDEAILRR 159


                ....*..
gi 86561515 276 FEKRIYI 282
Cdd:cd19520 160 MPKRFHI 166
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 154-284 3.87e-55

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: 178.94  E-value: 3.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   154 ILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESE 233
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELG-APFIEISGSELVSKYVGESEKRLRELFEAAKKLAPCVIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 86561515   234 SARRIKTEFMVQMQGVGLNNDGILVLGATNIPWILDSAIRRRFEKRIYIPL 284
Cdd:pfam00004  80 ESRRVVNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 113-340 5.21e-54

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: 191.66  E-value: 5.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   113 PNVKWTDIAGLEGAKEALKEAVILPIKFPQLFTG-NRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSK 191
Cdd:TIGR01243 173 PKVTYEDIGGLKEAKEKIREMVELPMKHPELFEHlGIEPPKGVLLYGPPGTGKTLLAKAVANEAG-AYFISINGPEIMSK 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   192 WLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQgvGLNNDG-ILVLGATNIPWILDS 270
Cdd:TIGR01243 252 YYGESEERLREIFKEAEENAPSIIFIDEIDAIAPKREEVTGEVEKRVVAQLLTLMD--GLKGRGrVIVIGATNRPDALDP 329

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 86561515   271 AIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALMQPVRRV 340
Cdd:TIGR01243 330 ALRRpgRFDREIVIRVPDKRARKEILKVHT-RNMPLAEDVDLDKLAEVTHGFVGADLAALAKEAAMAALRRF 400
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 119-282 1.48e-53

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: 175.94  E-value: 1.48e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 119 DIAGLEGAKEALKEAVILPIKFPQLFTG-NRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESE 197
Cdd:cd19503   1 DIGGLDEQIASLKELIELPLKYPELFRAlGLKPPRGVLLHGPPGTGKTLLARAVANEAG-ANFLSISGPSIVSKYLGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 198 KLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGlNNDGILVLGATNIPWILDSAIRR--R 275
Cdd:cd19503  80 KNLREIFEEARSHAPSIIFIDEIDALAPKREEDQREVERRVVAQLLTLMDGMS-SRGKVVVIAATNRPDAIDPALRRpgR 158


                ....*..
gi 86561515 276 FEKRIYI 282
Cdd:cd19503 159 FDREVEI 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 126-282 2.05e-53

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: 175.55  E-value: 2.05e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 126 AKEALKEAVILPIKFPQLFT--GNRKPwQGILLFGPPGTGKSYIAKAVATEAGEStFFSISSSDLMSKWLGESEKLVKNL 203
Cdd:cd19511   1 VKRELKEAVEWPLKHPDAFKrlGIRPP-KGVLLYGPPGCGKTLLAKALASEAGLN-FISVKGPELFSKYVGESERAVREI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 204 FALAREHKPSIIFIDEIDSLCSARSDNESES-ARRIKTEFMVQMQGVGLnNDGILVLGATNIPWILDSAIRR--RFEKRI 280
Cdd:cd19511  79 FQKARQAAPCIIFFDEIDSLAPRRGQSDSSGvTDRVVSQLLTELDGIES-LKGVVVIAATNRPDMIDPALLRpgRLDKLI 157


                ..
gi 86561515 281 YI 282
Cdd:cd19511 158 YV 159
FtsH_fam TIGR01241
ATP-dependent metalloprotease FtsH; HflB(FtsH) is a pleiotropic protein required for correct ...
 111-349 3.43e-51

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: 179.79  E-value: 3.43e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   111 EKPNVKWTDIAGLEGAKEALKEAVILpIKFPQLFT--GNRKPwQGILLFGPPGTGKSYIAKAVATEAGEStFFSISSSDL 188
Cdd:TIGR01241  48 EKPKVTFKDVAGIDEAKEELMEIVDF-LKNPSKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVP-FFSISGSDF 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   189 MSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSAR------SDNESEsarRIKTEFMVQMQGVGlNNDGILVLGAT 262
Cdd:TIGR01241 125 VEMFVGVGASRVRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglggGNDERE---QTLNQLLVEMDGFG-TNTGVIVIAAT 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   263 NIPWILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALMQPVRRV 340
Cdd:TIGR01241 201 NRPDVLDPALLRpgRFDRQVVVDLPDIKGREEILKVHA-KNKKLAPDVDLKAVARRTPGFSGADLANLLNEAALLAARKN 279


                  ....*....
gi 86561515   341 QSATHFKHV 349
Cdd:TIGR01241 280 KTEITMNDI 288
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 126-282 9.88e-49

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: 163.22  E-value: 9.88e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 126 AKEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESEKLVKNLFA 205
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELG-LPLIVVKLSSLLSKYVGESEKNLRKIFE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 206 LAREHKPSIIFIDEIDSLCSARSDN-ESESARRIKTEFMVQMQGVGlNNDGILVLGATNIPWILDSAIRR--RFEKRIYI 282
Cdd:cd19481  80 RARRLAPCILFIDEIDAIGRKRDSSgESGELRRVLNQLLTELDGVN-SRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 119-282 4.03e-46

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: 156.58  E-value: 4.03e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 119 DIAGLEGAKEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESEK 198
Cdd:cd19523   1 DIAGLGALKAAIKEEVLWPLLRPDAFSGLLRLPRSILLFGPRGTGKTLLGRCLASQLG-ATFLRLRGSTLVAKWAGEGEK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 199 LVKNLFALAREHKPSIIFIDEIDSLCSARSDNESeSARRIKTEFMVQMQGV-GLNNDGILVLGATNIPWILDSAIRRRFE 277
Cdd:cd19523  80 ILQASFLAARCRQPSVLFISDLDALLSSQDDEAS-PVGRLQVELLAQLDGVlGSGEDGVLVVCTTSKPEEIDESLRRYFS 158


                ....*
gi 86561515 278 KRIYI 282
Cdd:cd19523 159 KRLLV 163
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 111-339 1.00e-45

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 162.63  E-value: 1.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  111 EKPNVKWTDIAGLEGAKEALKEAVILPIKFPQLFTG-NRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLM 189
Cdd:PTZ00454 138 EKPDVTYSDIGGLDIQKQEIREAVELPLTCPELYEQiGIDPPRGVLLYGPPGTGKTMLAKAVAHHTT-ATFIRVVGSEFV 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  190 SKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESAR---RIKTEFMVQMQGVGLNNDgILVLGATNIPW 266
Cdd:PTZ00454 217 QKYLGEGPRMVRDVFRLARENAPSIIFIDEVDSIATKRFDAQTGADRevqRILLELLNQMDGFDQTTN-VKVIMATNRAD 295

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86561515  267 ILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVGKnYNTLTDQDFKVLAERCEGYSGYDISILVKDALMQPVRR 339
Cdd:PTZ00454 296 TLDPALLRpgRLDRKIEFPLPDRRQKRLIFQTITSK-MNLSEEVDLEDFVSRPEKISAADIAAICQEAGMQAVRK 369
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 115-282 7.00e-45

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: 153.54  E-value: 7.00e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 115 VKWTDIAGLEGAKEALKEAVILpIKFPQLFT--GNRKPwQGILLFGPPGTGKSYIAKAVATEAGEStFFSISSSDLMSKW 192
Cdd:cd19501   1 VTFKDVAGCEEAKEELKEVVEF-LKNPEKFTklGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVP-FFSISGSDFVEMF 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 193 LGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESA-RRIKT--EFMVQMQGVGlNNDGILVLGATNIPWILD 269
Cdd:cd19501  78 VGVGASRVRDLFEQAKKNAPCIVFIDEIDAVGRKRGAGLGGGHdEREQTlnQLLVEMDGFE-SNTGVIVIAATNRPDVLD 156

                       170
                ....*....|....*
gi 86561515 270 SAIRR--RFEKRIYI 282
Cdd:cd19501 157 PALLRpgRFDRQVYV 171
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 126-282 1.10e-44

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: 152.65  E-value: 1.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 126 AKEALKEAVILPIKFPQLFT-GNRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESEKLVKNLF 204
Cdd:cd19529   1 VKQELKEAVEWPLLKPEVFKrLGIRPPKGILLYGPPGTGKTLLAKAVATESN-ANFISVKGPELLSKWVGESEKAIREIF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 205 ALAREHKPSIIFIDEIDSLCSAR-SDNESESARRIKTEFMVQMQGVGLNNDgILVLGATNIPWILDSAIRR--RFEKRIY 281
Cdd:cd19529  80 RKARQVAPCVIFFDEIDSIAPRRgTTGDSGVTERVVNQLLTELDGLEEMNG-VVVIAATNRPDIIDPALLRagRFDRLIY 158


                .
gi 86561515 282 I 282
Cdd:cd19529 159 I 159
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 117-280 2.31e-44

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: 152.49  E-value: 2.31e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 117 WTDIAGLEGAKEALKEAVILPIKFPQLFTG-NRKPWQGILLFGPPGTGKSYIAKAVATEAgESTFFSISSSDLMSKWLGE 195
Cdd:cd19502   2 YEDIGGLDEQIREIREVVELPLKHPELFEElGIEPPKGVLLYGPPGTGKTLLAKAVANHT-DATFIRVVGSELVQKYIGE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 196 SEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESAR---RIKTEFMVQMQGVGLNNDgILVLGATNIPWILDSAI 272
Cdd:cd19502  81 GARLVRELFEMAREKAPSIIFIDEIDAIGAKRFDSGTGGDRevqRTMLELLNQLDGFDPRGN-IKVIMATNRPDILDPAL 159

                       170
                ....*....|
gi 86561515 273 RR--RFEKRI 280
Cdd:cd19502 160 LRpgRFDRKI 169
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 119-283 2.36e-44

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: 152.21  E-value: 2.36e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 119 DIAGLEGAKEALKEAVILPIKFPQLFTG-NRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESE 197
Cdd:cd19519   1 DIGGCRKQLAQIREMVELPLRHPELFKAiGIKPPRGILLYGPPGTGKTLIARAVANETG-AFFFLINGPEIMSKLAGESE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 198 KLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLNNDgILVLGATNIPWILDSAIRR--R 275
Cdd:cd19519  80 SNLRKAFEEAEKNAPAIIFIDEIDAIAPKREKTHGEVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPALRRfgR 158


                ....*...
gi 86561515 276 FEKRIYIP 283
Cdd:cd19519 159 FDREIDIG 166
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
117-333 4.33e-44

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 154.27  E-value: 4.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 117 WTDIAGLEGAKEALKEAVI------LPIKFpqlftgNRKPWQGILLFGPPGTGKSYIAKAVATEAGEStFFSISSSDLMS 190
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKelrrreNLRKF------GLWPPRKILFYGPPGTGKTMLAEALAGELKLP-LLTVRLDSLIG 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 191 KWLGESEKLVKNLFALAREHkPSIIFIDEIDSLCSARSD-NESESARRIKTEFMVQMQGVglnNDGILVLGATNIPWILD 269
Cdd:COG1223  74 SYLGETARNLRKLFDFARRA-PCVIFFDEFDAIAKDRGDqNDVGEVKRVVNALLQELDGL---PSGSVVIAATNHPELLD 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86561515 270 SAIRRRFEKRIYIPLPDIHARKEMFRIDVGKNYNTLtDQDFKVLAERCEGYSGYDISILVKDAL 333
Cdd:COG1223 150 SALWRRFDEVIEFPLPDKEERKEILELNLKKFPLPF-ELDLKKLAKKLEGLSGADIEKVLKTAL 212
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
111-329 2.00e-40

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 151.73  E-value: 2.00e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 111 EKPNVKWTDIAGLEGAKEALKEAV-ILpiKFPQLFT--GNRKPwQGILLFGPPGTGKSYIAKAVATEAGEStFFSISSSD 187
Cdd:COG0465 135 DKPKVTFDDVAGVDEAKEELQEIVdFL--KDPEKFTrlGAKIP-KGVLLVGPPGTGKTLLAKAVAGEAGVP-FFSISGSD 210

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 188 LM--------SKwlgeseklVKNLFALAREHKPSIIFIDEIDSLCSAR------SDNESESarrikT--EFMVQMQGVGl 251
Cdd:COG0465 211 FVemfvgvgaSR--------VRDLFEQAKKNAPCIIFIDEIDAVGRQRgaglggGHDEREQ-----TlnQLLVEMDGFE- 276

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 252 NNDGILVLGATNIPWILDSAIRR--RFEKRIYIPLPDIHARKEMFRI---------DVgknyntltdqDFKVLAERCEGY 320
Cdd:COG0465 277 GNEGVIVIAATNRPDVLDPALLRpgRFDRQVVVDLPDVKGREAILKVharkkplapDV----------DLEVIARRTPGF 346


                ....*....
gi 86561515 321 SGYDISILV 329
Cdd:COG0465 347 SGADLANLV 355
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 102-332 5.12e-39

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 145.68  E-value: 5.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  102 DKLSGAIVMEK-PNVKWTDIAGLEGAKEALKEAVILPIKFPQLFTG-NRKPWQGILLFGPPGTGKSYIAKAVATEAgEST 179
Cdd:PTZ00361 166 DPLVSVMKVDKaPLESYADIGGLEQQIQEIKEAVELPLTHPELYDDiGIKPPKGVILYGPPGTGKTLLAKAVANET-SAT 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  180 FFSISSSDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKT---EFMVQMQGVGLNNDgI 256
Cdd:PTZ00361 245 FLRVVGSELIQKYLGDGPKLVRELFRVAEENAPSIVFIDEIDAIGTKRYDATSGGEKEIQRtmlELLNQLDGFDSRGD-V 323

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86561515  257 LVLGATNIPWILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVGKnYNTLTDQDFKVLAERCEGYSGYDISILVKDA 332
Cdd:PTZ00361 324 KVIMATNRIESLDPALIRpgRIDRKIEFPNPDEKTKRRIFEIHTSK-MTLAEDVDLEEFIMAKDELSGADIKAICTEA 400
ftsH CHL00176
cell division protein; Validated
 119-339 1.82e-38

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 147.12  E-value: 1.82e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  119 DIAGLEGAKEALKEAVILpIKFPQLFT--GNRKPwQGILLFGPPGTGKSYIAKAVATEAgESTFFSISSSDLMSKWLGES 196
Cdd:CHL00176 184 DIAGIEEAKEEFEEVVSF-LKKPERFTavGAKIP-KGVLLVGPPGTGKTLLAKAIAGEA-EVPFFSISGSEFVEMFVGVG 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  197 EKLVKNLFALAREHKPSIIFIDEIDSLCSARSDN------ESEsarRIKTEFMVQMQGVGLNNdGILVLGATNIPWILDS 270
Cdd:CHL00176 261 AARVRDLFKKAKENSPCIVFIDEIDAVGRQRGAGigggndERE---QTLNQLLTEMDGFKGNK-GVIVIAATNRVDILDA 336

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86561515  271 AIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALMQPVRR 339
Cdd:CHL00176 337 ALLRpgRFDRQITVSLPDREGRLDILKVHA-RNKKLSPDVSLELIARRTPGFSGADLANLLNEAAILTARR 406
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 123-282 2.00e-38

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: 136.46  E-value: 2.00e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 123 LEGAKEALKEAVILPIKFPQLFT--GNRKPwQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESEKLV 200
Cdd:cd19530   1 LDHVREELTMSILRPIKRPDIYKalGIDLP-TGVLLYGPPGCGKTLLAKAVANESG-ANFISVKGPELLNKYVGESERAV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 201 KNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGlNNDGILVLGATNIPWILDSAIRR--RFEK 278
Cdd:cd19530  79 RQVFQRARASAPCVIFFDEVDALVPKRGDGGSWASERVVNQLLTEMDGLE-ERSNVFVIAATNRPDIIDPAMLRpgRLDK 157


                ....
gi 86561515 279 RIYI 282
Cdd:cd19530 158 TLYV 161
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 127-282 3.33e-38

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: 135.72  E-value: 3.33e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 127 KEALKEAVILPIKFPQLFTG-NRKPWQGILLFGPPGTGKSYIAKAVATEAgESTFFSISSSDLMSKWLGESEKLVKNLFA 205
Cdd:cd19528   2 KRELQELVQYPVEHPDKFLKfGMTPSKGVLFYGPPGCGKTLLAKAIANEC-QANFISVKGPELLTMWFGESEANVRDIFD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 206 LAREHKPSIIFIDEIDSLCSARSDNESES---ARRIKTEFMVQMQGVGLNNDgILVLGATNIPWILDSAIRR--RFEKRI 280
Cdd:cd19528  81 KARAAAPCVLFFDELDSIAKARGGNIGDAggaADRVINQILTEMDGMNTKKN-VFIIGATNRPDIIDPAILRpgRLDQLI 159


                ..
gi 86561515 281 YI 282
Cdd:cd19528 160 YI 161
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 119-281 6.11e-37

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: 132.63  E-value: 6.11e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 119 DIAGLEGAKEALKEAVILPIKFPQLFTG-NRKPWQGILLFGPPGTGKSYIAKAVATEAGES----TFFSISSSDLMSKWL 193
Cdd:cd19517   1 DIGGLSHYINQLKEMVFFPLLYPEVFAKfKITPPRGVLFHGPPGTGKTLMARALAAECSKGgqkvSFFMRKGADCLSKWV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 194 GESEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQgvGLNNDG-ILVLGATNIPWILDSAI 272
Cdd:cd19517  81 GEAERQLRLLFEEAYRMQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMD--GLDNRGqVVVIGATNRPDALDPAL 158

                       170
                ....*....|.
gi 86561515 273 RR--RFEKRIY 281
Cdd:cd19517 159 RRpgRFDREFY 169
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 126-281 1.40e-36

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: 131.40  E-value: 1.40e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 126 AKEALKEAVILPIKFPQLFTGNRKPWQ-GILLFGPPGTGKSYIAKAVATEAGEStFFSISSSDLMSKWLGESEKLVKNLF 204
Cdd:cd19526   1 VKKALEETIEWPSKYPKIFASSPLRLRsGILLYGPPGCGKTLLASAIASECGLN-FISVKGPELLNKYIGASEQNVRDLF 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 205 ALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGV-GLnnDGILVLGATNIPWILDSAIRR--RFEKRIY 281
Cdd:cd19526  80 SRAQSAKPCILFFDEFDSIAPKRGHDSTGVTDRVVNQLLTQLDGVeGL--DGVYVLAATSRPDLIDPALLRpgRLDKLVY 157
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
105-347 3.84e-36

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 140.55  E-value: 3.84e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  105 SGAIVMEKPNVKWT--DIAGLEGAKEALKEAVIL---PIKFPQLftGNRKPwQGILLFGPPGTGKSYIAKAVATEAgEST 179
Cdd:PRK10733 137 SKARMLTEDQIKTTfaDVAGCDEAKEEVAELVEYlrePSRFQKL--GGKIP-KGVLMVGPPGTGKTLLAKAIAGEA-KVP 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  180 FFSISSSDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSLCSARS---DNESESARRIKTEFMVQMQGVGlNNDGI 256
Cdd:PRK10733 213 FFTISGSDFVEMFVGVGASRVRDMFEQAKKAAPCIIFIDEIDAVGRQRGaglGGGHDEREQTLNQMLVEMDGFE-GNEGI 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  257 LVLGATNIPWILDSAIRR--RFEKRIYIPLPDIHARKEMFRIDVgKNYNTLTDQDFKVLAERCEGYSGYDISILVKDALM 334
Cdd:PRK10733 292 IVIAATNRPDVLDPALLRpgRFDRQVVVGLPDVRGREQILKVHM-RRVPLAPDIDAAIIARGTPGFSGADLANLVNEAAL 370

                        250
                 ....*....|....*.
gi 86561515  335 QPVR---RVQSATHFK 347
Cdd:PRK10733 371 FAARgnkRVVSMVEFE 386
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 127-282 5.45e-36

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: 129.94  E-value: 5.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 127 KEALKEAVILPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAgESTFFSISSSDLMSKWLGESEKLVKNLFAL 206
Cdd:cd19527   2 KKEILDTIQLPLEHPELFSSGLRKRSGILLYGPPGTGKTLLAKAIATEC-SLNFLSVKGPELINMYIGESEANVREVFQK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 207 AREHKPSIIFIDEIDSLCSARSdNESESA---RRIKTEFMVQMQGVGLNNDGILVLGATNIPWILDSAIRR--RFEKRIY 281
Cdd:cd19527  81 ARDAKPCVIFFDELDSLAPSRG-NSGDSGgvmDRVVSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALLRpgRFDKLLY 159


                .
gi 86561515 282 I 282
Cdd:cd19527 160 L 160
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 119-280 9.41e-36

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: 129.45  E-value: 9.41e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 119 DIAGLEGAKEALKEAVILPIKFPQLF--TGnRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGES 196
Cdd:cd19518   1 DIGGMDSTLKELCELLIHPILPPEYFqhLG-VEPPRGVLLHGPPGCGKTMLANAIAGELK-VPFLKISATEIVSGVSGES 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 197 EKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLNND---GILVLGATNIPWILDSAIR 273
Cdd:cd19518  79 EEKIRELFDQAISNAPCIVFIDEIDAITPKRESAQREMERRIVSQLLTCMDELNNEKTaggPVLVIGATNRPDSLDPALR 158


                ....*....
gi 86561515 274 R--RFEKRI 280
Cdd:cd19518 159 RagRFDREI 167
MIT_VPS4 cd02678
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-79 1.52e-33

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.


Pssm-ID: 239141  Cd Length: 75  Bit Score: 120.45  E-value: 1.52e-33
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86561515   4 PALQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKYESQGdKQRNAIRDKVGQYLNRAEQIKTHLKDGKT 79
Cdd:cd02678   1 DFLQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHALKYEKNP-KSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
Vps4_C pfam09336
Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase ...
 365-425 1.62e-29

Vps4 C terminal oligomerization domain; This domain is found at the C terminal of ATPase proteins involved in vacuolar sorting. It forms an alpha helix structure and is required for oligomerization.


Pssm-ID: 462762 [Multi-domain]  Cd Length: 61  Bit Score: 109.12  E-value: 1.62e-29
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86561515   365 LTPCSPGDPHAIAMNWLDVPGDKLANPPLSMQDISRSLASVKPTVNNTDLDRLEAFKNDFG 425
Cdd:pfam09336   1 LTPCSPGDPGAIEMTWMDIPSDKLLEPPVTMKDFLKALKSSRPTVSKEDLEKYEEFTKEFG 61
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 121-284 1.38e-28

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: 109.54  E-value: 1.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 121 AGLEGAKEALKEAVILPikfpqlftgnrkPWQGILLFGPPGTGKSYIAKAVATEAGES--TFFSISSSDLMSKWLGESEK 198
Cdd:cd00009   1 VGQEEAIEALREALELP------------PPKNLLLYGPPGTGKTTLARAIANELFRPgaPFLYLNASDLLEGLVVAELF 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 199 ---LVKNLFALAREHKPSIIFIDEIDSLcsarsdneSESARRIKTEFMVQMQGVGLNNDGILVLGATNIPW--ILDSAIR 273
Cdd:cd00009  69 ghfLVRLLFELAEKAKPGVLFIDEIDSL--------SRGAQNALLRVLETLNDLRIDRENVRVIGATNRPLlgDLDRALY 140

                       170
                ....*....|.
gi 86561515 274 RRFEKRIYIPL 284
Cdd:cd00009 141 DRLDIRIVIPL 151
MIT pfam04212
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ...
 6-71 4.93e-24

MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.


Pssm-ID: 461228  Cd Length: 66  Bit Score: 94.53  E-value: 4.93e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 86561515     6 LQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKyESQGDKQRNAIRDKVGQYLNRAEQIK 71
Cdd:pfam04212   1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALK-ETKNEERRELLRAKIAEYLERAEELK 65
MIT cd02656
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ...
 4-78 1.93e-21

MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.


Pssm-ID: 239121  Cd Length: 75  Bit Score: 87.75  E-value: 1.93e-21
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 86561515   4 PALQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKYESQgDKQRNAIRDKVGQYLNRAEQIKTHLKDGK 78
Cdd:cd02656   1 ELLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKE-PKLRKLLRKKVKEYLDRAEFLKELLKKQK 74
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 150-286 8.26e-21

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: 88.20  E-value: 8.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515    150 PWQGILLFGPPGTGKSYIAKAVATEAGEST--FFSISSSDLMS--------------KWLGESEKLVKNLFALAREHKPS 213
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGggVIYIDGEDILEevldqllliivggkKASGSGELRLRLALALARKLKPD 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86561515    214 IIFIDEIDSLCSARSDNESESARRIKTEFMVQMQGvglnndGILVLGATNIPWILDSA-IRRRFEKRIYIPLPD 286
Cdd:smart00382  81 VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEK------NLTVILTTNDEKDLGPAlLRRRFDRRIVLLLIL 148
MIT smart00745
Microtubule Interacting and Trafficking molecule domain;
4-76 5.35e-20

Microtubule Interacting and Trafficking molecule domain;


Pssm-ID: 197854  Cd Length: 77  Bit Score: 83.51  E-value: 5.35e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86561515      4 PALQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKYESqGDKQRNAIRDKVGQYLNRAEQIKTHLKD 76
Cdd:smart00745   3 DYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVES-DSKRREALKAKAAEYLDRAEEIKKSLLE 74
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 152-282 3.59e-19

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: 84.46  E-value: 3.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 152 QGILLFGPPGTGKSYIAKAVATEAGESTFFSISSSDLMSKWLGESEKLVKNLFALAREHKPS--------IIFIDEIDSL 223
Cdd:cd19504  36 KGILLYGPPGTGKTLMARQIGKMLNAREPKIVNGPEILNKYVGESEANIRKLFADAEEEQRRlgansglhIIIFDEIDAI 115

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86561515 224 CSARSDNESESA--RRIKTEFMVQMQGV-GLNNdgILVLGATNIPWILDSAIRR--RFEKRIYI 282
Cdd:cd19504 116 CKQRGSMAGSTGvhDTVVNQLLSKIDGVeQLNN--ILVIGMTNRKDLIDEALLRpgRLEVQMEI 177
MIT_2 cd02684
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 4-74 4.34e-19

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with an n-terminal serine/threonine kinase domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239147  Cd Length: 75  Bit Score: 81.02  E-value: 4.34e-19
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86561515   4 PALQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKYESQGDKqRNAIRDKVGQYLNRAEQIKTHL 74
Cdd:cd02684   1 ESLEKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQR-KEALRQKVLQYVSRAEELKALI 70
RecA-like_Ycf46-like cd19507
ATPase domain of Ycf46 and similar ATPase domains; Ycf46 may play a role in the regulation of ...
 119-247 4.08e-14

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: 69.70  E-value: 4.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 119 DIAGLEGAKEALKEAVilPIKFPQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGESEK 198
Cdd:cd19507   1 DVGGLDNLKDWLKKRK--AAFSKQASAYGLPTPKGLLLVGIQGTGKSLTAKAIAGVWQ-LPLLRLDMGRLFGGLVGESES 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 86561515 199 LVKNLFALAREHKPSIIFIDEIDS-LCSARSDNESESARRIKTEFMVQMQ 247
Cdd:cd19507  78 RLRQMIQTAEAIAPCVLWIDEIEKgFSNADSKGDSGTSSRVLGTFLTWLQ 127
RecA-like_Pch2-like cd19508
ATPase domain of Pachytene checkpoint 2 (Pch2) and similar ATPase domains; Pch2 (known as ...
 124-282 2.42e-13

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: 68.63  E-value: 2.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 124 EGAKEALKEAVILPIKF------PQLFTGNRKpwqgILLFGPPGTGKSYIAKAVATEAG--------ESTFFSISSSDLM 189
Cdd:cd19508  23 SNLKSRLLDYVTTTLLFsdknvnTNLITWNRL----VLLHGPPGTGKTSLCKALAQKLSirlssryrYGQLIEINSHSLF 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 190 SKWLGESEKLVKNLFALARE---HKPSIIF--IDEIDSLCSAR----SDNESESARRIKTEFMVQMQGVGlNNDGILVLG 260
Cdd:cd19508  99 SKWFSESGKLVTKMFQKIQElidDKDALVFvlIDEVESLAAARsassSGTEPSDAIRVVNAVLTQIDRIK-RYHNNVILL 177

                       170       180
                ....*....|....*....|..
gi 86561515 261 ATNIPWILDSAIRRRFEKRIYI 282
Cdd:cd19508 178 TSNLLEKIDVAFVDRADIKQYI 199
ycf46 CHL00195
Ycf46; Provisional
 113-326 2.66e-11

Ycf46; Provisional


Pssm-ID: 177094 [Multi-domain]  Cd Length: 489  Bit Score: 65.04  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  113 PNVKWTDIAGLEGAKEALK--------EAVILPIKFPQlftgnrkpwqGILLFGPPGTGKSYIAKAVATEAGeSTFFSIS 184
Cdd:CHL00195 223 VNEKISDIGGLDNLKDWLKkrstsfskQASNYGLPTPR----------GLLLVGIQGTGKSLTAKAIANDWQ-LPLLRLD 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  185 SSDLMSKWLGESEKLVKNLFALAREHKPSIIFIDEIDSlCSARSDNESES--ARRIKTEFMVQMQGvglNNDGILVLG-A 261
Cdd:CHL00195 292 VGKLFGGIVGESESRMRQMIRIAEALSPCILWIDEIDK-AFSNSESKGDSgtTNRVLATFITWLSE---KKSPVFVVAtA 367

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86561515  262 TNIPWILDSAIRR-RFEKRIYIPLPDIHARKEMFRIDVGK-NYNTLTDQDFKVLAERCEGYSGYDIS 326
Cdd:CHL00195 368 NNIDLLPLEILRKgRFDEIFFLDLPSLEEREKIFKIHLQKfRPKSWKKYDIKKLSKLSNKFSGAEIE 434
MIT_1 cd02683
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 8-75 9.74e-11

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with unknown function, co-occuring with an as yet undescribed domain. The molecular function of the MIT domain is unclear.


Pssm-ID: 239146  Cd Length: 77  Bit Score: 57.43  E-value: 9.74e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 86561515   8 KAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKYESQGDKQRNaIRDKVGQYLNRAEQIKTHLK 75
Cdd:cd02683   5 AAKEVLKRAVELDQEGRFQEALVCYQEGIDLLMQVLKGTKDEAKKKN-LRQKISEYMDRAEAIKKRLD 71
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 147-280 1.85e-10

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: 59.08  E-value: 1.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 147 NRKPWQGILLFGPPGTGKSYIAKAVATEAGEStfFSISSSDLMSKWLGESEKLVKNLFALA-REHKPSIIFIDEIDSLCS 225
Cdd:cd19512  18 NKGLYRNILFYGPPGTGKTLFAKKLALHSGMD--YAIMTGGDVAPMGREGVTAIHKVFDWAnTSRRGLLLFVDEADAFLR 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 86561515 226 ARSDNE-SESARRIKTEFMVQMQgvGLNNDGILVLgATNIPWILDSAIRRRFEKRI 280
Cdd:cd19512  96 KRSTEKiSEDLRAALNAFLYRTG--EQSNKFMLVL-ASNQPEQFDWAINDRIDEMV 148
RecA-like_Ycf2 cd19505
ATPase domain of plant YCF2; Ycf2 is a chloroplast ATPase which has an essential function; ...
 150-272 2.96e-10

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: 58.54  E-value: 2.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 150 PWQGILLFGPPGTGKSYIAKAVATEA--------------GESTFFSISSSDLMSKWlGESEKLVKNLFALAREHKPSII 215
Cdd:cd19505  11 PSKGILLIGSIETGRSYLIKSLAANSyvplirislnkllyNKPDFGNDDWIDGMLIL-KESLHRLNLQFELAKAMSPCII 89

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 216 FIDEIDSLCSARSDNESESARRIKTEFMVQMQGVGLNND---GILVLGATNIPWILDSAI 272
Cdd:cd19505  90 WIPNIHELNVNRSTQNLEEDPKLLLGLLLNYLSRDFEKSstrNILVIASTHIPQKVDPAL 149
RecA-like_BCS1 cd19510
Mitochondrial chaperone BCS1; Mitochondrial chaperone BCS1 is necessary for the assembly of ...
 130-282 7.77e-09

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: 54.28  E-value: 7.77e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 130 LKEAVILPIKFPQLFTGNRKPW-QGILLFGPPGTGKSYIAKAVATEAGESTF-FSISSSDLmskwlgeSEKLVKNLfaLA 207
Cdd:cd19510   1 IIDDLKDFIKNEDWYNDRGIPYrRGYLLYGPPGTGKSSFIAALAGELDYDICdLNLSEVVL-------TDDRLNHL--LN 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 208 REHKPSIIFIDEIDSLCSARSDNESEsarRIKTEFMVQMQGVGLNN--DGI------LVLGATNIPWILDSAIRR--RFE 277
Cdd:cd19510  72 TAPKQSIILLEDIDAAFESREHNKKN---PSAYGGLSRVTFSGLLNalDGVasseerIVFMTTNHIERLDPALIRpgRVD 148


                ....*
gi 86561515 278 KRIYI 282
Cdd:cd19510 149 MKIYM 153
AAA_lid_3 pfam17862
AAA+ lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 307-350 2.58e-08

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: 49.84  E-value: 2.58e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 86561515   307 DQDFKVLAERCEGYSGYDISILVKDALMQPVRRVQSATHFKHVS 350
Cdd:pfam17862   1 DVDLEELAERTEGFSGADLEALCREAALAALRRGLEAVTQEDLE 44
RecA-like_IQCA1 cd19506
ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein ...
 154-282 7.72e-08

ATPase domain of IQ and AAA domain-containing protein 1 (IQCA1); IQCA1 (also known as dynein regulatory complex subunit 11, DRC11 and IQCA) is an ATPase subunit of the nexin-dynein regulatory complex (N-DRC). The 9 + 2 axoneme of most motile cilia and flagella consists of nine outer doublet microtubules arranged in a ring surrounding a central pair of two singlet microtubules. The N-DRC complex maintains alignment between outer doublet microtubules and limits microtubule sliding in motile axonemes. 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: 410914 [Multi-domain]  Cd Length: 160  Bit Score: 51.76  E-value: 7.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 154 ILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDLMSKWLGES--EKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNE 231
Cdd:cd19506  29 LLLAGPSGVGKKMLVHAICTETG-ANLFNLSPSNIAGKYPGKNglQMMLHLVLKVARQLQPSVIWIGDAEKTFYKKVPKT 107

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 86561515 232 SE--SARRIKTEFMVQMQGVGlNNDGILVLGATNIPWILD-SAIRRRFEKRIYI 282
Cdd:cd19506 108 EKqlDPKRLKKDLPKILKSLK-PEDRVLIVGTTSRPFEADlKSFCKVYNKIILI 160
MIT_SNX15 cd02677
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT ...
 6-75 2.28e-07

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This MIT domain sub-family is found in sorting nexin 15 and related proteins. The molecular function of the MIT domain is unclear.


Pssm-ID: 239140  Cd Length: 75  Bit Score: 48.11  E-value: 2.28e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86561515   6 LQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAIKYESqGDKQRNAIRDKVGQYLNRAEQI-KTHLK 75
Cdd:cd02677   3 LEQAAELIRLALEKEEEGDYEAAFEFYRAGVDLLLKGVQGDS-SPERREAVKRKIAEYLKRAEEIlRLHLS 72
TIP49 COG1224
DNA helicase TIP49, TBP-interacting protein [Transcription];
153-199 6.35e-07

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


Pssm-ID: 440837 [Multi-domain]  Cd Length: 452  Bit Score: 51.51  E-value: 6.35e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 86561515 153 GILLFGPPGTGKSYIAKAVATEAGEST-FFSISSSDLMSKWLGESEKL 199
Cdd:COG1224  66 GILIVGPPGTGKTALAVAIARELGEDTpFVAISGSEIYSAELKKTEFL 113
IS21_help_AAA NF038214
IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was ...
 152-220 1.55e-06

IS21-like element helper ATPase IstB; This protein family model resembles PF01695, but was built to hit full-length AAA+ ATPases of IS21 family IS (insertion sequence) elements.


Pssm-ID: 439516  Cd Length: 232  Bit Score: 49.01  E-value: 1.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86561515  152 QGILLFGPPGTGKSYIAKAV---ATEAGESTFFsISSSDLMSKW-LGESE-KLVKNLFALARehkPSIIFIDEI 220
Cdd:NF038214  91 ENVLLLGPPGTGKTHLAIALgyaACRQGYRVRF-TTAADLVEQLaQARADgRLGRLLRRLAR---YDLLIIDEL 160
TIP49 pfam06068
TIP49 P-loop domain; This family consists of the C-terminal region of several eukaryotic and ...
 122-203 2.89e-06

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: 48.84  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   122 GLEGAKEALKEA-VILpikfpQLFTGNRKPWQGILLFGPPGTGKSYIAKAVATEAGEST-FFSISSSDLMSKWLGESEKL 199
Cdd:pfam06068  25 GLVGQEKAREAAgVIV-----EMIKEGKIAGRAVLIAGPPGTGKTALAIAISKELGEDTpFTSISGSEVYSLEMKKTEAL 99


                  ....
gi 86561515   200 VKNL 203
Cdd:pfam06068 100 TQAF 103
MIT_calpain7_2 cd02680
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ...
 6-75 3.92e-06

MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.


Pssm-ID: 239143  Cd Length: 75  Bit Score: 44.60  E-value: 3.92e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   6 LQKAIELVTKATEEDTAGRYDQALRLYDQAIEYFLHAiKYESQGDKQRNAIRDKVGQYLNRAEQIKTHLK 75
Cdd:cd02680   3 LERAHFLVTQAFDEDEKGNAEEAIELYTEAVELCINT-SNETMDQALQTKLKQLARQALDRAEALKESMS 71
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 154-283 7.31e-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: 48.30  E-value: 7.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   154 ILLFGPPGTGKSYIAKAVATE-AG-----ESTFFSISSSDLMSKWLGESEKLVKNLF--ALARehkpsIIFIDEIDSLCS 225
Cdd:TIGR03922 315 MLFAGPPGTGKTTIARVVAKIyCGlgvlrKPLVREVSRADLIGQYIGESEAKTNEIIdsALGG-----VLFLDEAYTLVE 389

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86561515   226 ARSDNESESARRIKTEFMVQMQGvglNNDGILVLGA---TNIPWILDS--AIRRRFEKRIYIP 283
Cdd:TIGR03922 390 TGYGQKDPFGLEAIDTLLARMEN---DRDRLVVIGAgyrKDLDKFLEVneGLRSRFTRVIEFP 449
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 153-276 1.32e-05

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 44.59  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   153 GILLFGPPGTGKSYIAKAVATEAGESTFFSI------SSSDLMSKWLGESEKLVKNLFALAREHKPS-IIFIDEID---- 221
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAAALSNRPVFYVqltrdtTEEDLFGRRNIDPGGASWVDGPLVRAAREGeIAVLDEINranp 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86561515   222 ----SLCSARSDNEsesarriktefMVQMQGVGL---NNDGILVLGATNIP-----WiLDSAIRRRF 276
Cdd:pfam07728  81 dvlnSLLSLLDERR-----------LLLPDGGELvkaAPDGFRLIATMNPLdrglnE-LSPALRSRF 135
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 154-220 1.81e-05

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 46.62  E-value: 1.81e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 86561515  154 ILLFGPPGTGKSYIAKAVATEAGeSTFFSISSSDlmskwlgESEKLVKNLFALAREH----KPSIIFIDEI 220
Cdd:PRK13342  39 MILWGPPGTGKTTLARIIAGATD-APFEALSAVT-------SGVKDLREVIEEARQRrsagRRTILFIDEI 101
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 154-220 2.08e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 46.59  E-value: 2.08e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86561515 154 ILLFGPPGTGKSYIAKAVATEAGeSTFFSIS--SSdlmskwlGESEklVKNLFALAREH----KPSIIFIDEI 220
Cdd:COG2256  52 MILWGPPGTGKTTLARLIANATD-AEFVALSavTS-------GVKD--IREVIEEARERraygRRTILFVDEI 114
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
152-220 3.11e-05

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


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 45.16  E-value: 3.11e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86561515 152 QGILLFGPPGTGKSYIAKAVATEA---GESTFFsISSSDLMSKWL-----GESEKLVKNLfalareHKPSIIFIDEI 220
Cdd:COG1484 100 ENLILLGPPGTGKTHLAIALGHEAcraGYRVRF-TTAPDLVNELKearadGRLERLLKRL------AKVDLLILDEL 169
RecA-like_superfamily cd01120
RecA-like_NTPases; RecA-like NTPases. This superfamily includes the NTP binding domain of F1 ...
 154-243 3.88e-05

RecA-like_NTPases; RecA-like NTPases. This superfamily 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: 410865 [Multi-domain]  Cd Length: 119  Bit Score: 42.88  E-value: 3.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 154 ILLFGPPGTGKSYIAKAVATEAGESTFFSISSSDLmskwlgesEKLVKNLFALAREHKPSIIFIDEIDSLCSARSDNESE 233
Cdd:cd01120   1 ILITGPPGSGKTTLLLQFAEQALLSDEPVIFISFL--------DTILEAIEDLIEEKKLDIIIIDSLSSLARASQGDRSS 72

                        90
                ....*....|
gi 86561515 234 SARRIKTEFM 243
Cdd:cd01120  73 ELLEDLAKLL 82
AAA_2 pfam07724
AAA domain (Cdc48 subfamily); This Pfam entry includes some of the AAA proteins not detected ...
 154-221 6.69e-05

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: 43.34  E-value: 6.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   154 ILLFGPPGTGKSYIAKAVATE--AGESTFFSISSSDLM-----SKWLGESEKLVK-----NLFALAREHKPSIIFIDEID 221
Cdd:pfam07724   6 FLFLGPTGVGKTELAKALAELlfGDERALIRIDMSEYMeehsvSRLIGAPPGYVGyeeggQLTEAVRRKPYSIVLIDEIE 85
IstB_IS21 pfam01695
IstB-like ATP binding protein; This protein contains an ATP/GTP binding P-loop motif. It is ...
 152-220 7.65e-05

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: 426385 [Multi-domain]  Cd Length: 238  Bit Score: 43.97  E-value: 7.65e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 86561515   152 QGILLFGPPGTGKSYIAKAVATEA---GESTFFsISSSDLMSKWLGESE--KLVKNLFALARehkPSIIFIDEI 220
Cdd:pfam01695  93 QNVVLLGPPGVGKTHLAIALGVEAcraGYSVRF-TSAADLVNQLKRAHGdgKLTRKLQQLLK---PDVLILDEW 162
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
 154-296 2.85e-04

MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 42.46  E-value: 2.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 154 ILLFGPPGTGKSYIAKAVATEAGeSTFFSIS-SSDLM-SKWLGES--------EKLVKN-LFAlarehkpSIIFIDEIDs 222
Cdd:COG0714  34 LLLEGVPGVGKTTLAKALARALG-LPFIRIQfTPDLLpSDILGTYiydqqtgeFEFRPGpLFA-------NVLLADEIN- 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 223 lcsaRSDNESESA----------------RRIKTEFMVqmqgvglnndgIlvlgATNIP------WILDSAIRRRFEKRI 280
Cdd:COG0714 105 ----RAPPKTQSAlleameerqvtipggtYKLPEPFLV-----------I----ATQNPieqegtYPLPEAQLDRFLLKL 165

                       170
                ....*....|....*.
gi 86561515 281 YIPLPDihaRKEMFRI 296
Cdd:COG0714 166 YIGYPD---AEEEREI 178
clpA PRK11034
ATP-dependent Clp protease ATP-binding subunit; Provisional
 155-278 5.13e-04

ATP-dependent Clp protease ATP-binding subunit; Provisional


Pssm-ID: 236828 [Multi-domain]  Cd Length: 758  Bit Score: 42.52  E-value: 5.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  155 LLFGPPGTGKSYIAKAVATE---------AGESTFFSISSSDLM--SKWLGESEKLVKNLFALAREHKPSIIFIDEIDSL 223
Cdd:PRK11034 211 LLVGESGVGKTAIAEGLAWRivqgdvpevMADCTIYSLDIGSLLagTKYRGDFEKRFKALLKQLEQDTNSILFIDEIHTI 290

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 86561515  224 --CSARSDNESESARRIKTEfmvqmqgvgLNNDGILVLGAT------NIpWILDSAIRRRFEK 278
Cdd:PRK11034 291 igAGAASGGQVDAANLIKPL---------LSSGKIRVIGSTtyqefsNI-FEKDRALARRFQK 343
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 154-220 1.55e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.52  E-value: 1.55e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 154 ILLFGPPGTGKSYIAKAVA---TEAGESTFFSI------SSSDLMskwLGESEKLVKNLFAL-----------AREH--K 211
Cdd:COG1401 224 VILAGPPGTGKTYLARRLAealGGEDNGRIEFVqfhpswSYEDFL---LGYRPSLDEGKYEPtpgiflrfclkAEKNpdK 300


                ....*....
gi 86561515 212 PSIIFIDEI 220
Cdd:COG1401 301 PYVLIIDEI 309
clpC CHL00095
Clp protease ATP binding subunit
 147-296 1.71e-03

Clp protease ATP binding subunit


Pssm-ID: 214361 [Multi-domain]  Cd Length: 821  Bit Score: 40.81  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  147 NRKPWQGILLFGPPGTGKSYIAKAVA--TEAGESTFFSISSSDLM---------SKWLGESEKLVKNLFALAREHKPSII 215
Cdd:CHL00095 196 GRRTKNNPILIGEPGVGKTAIAEGLAqrIVNRDVPDILEDKLVITldiglllagTKYRGEFEERLKRIFDEIQENNNIIL 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  216 FIDEIDSLCSARSDNESESARRIKTEFMVQ--MQgvglnndgilVLGATNIPWI-----LDSAIRRRFEKrIYIPLPDIh 288
Cdd:CHL00095 276 VIDEVHTLIGAGAAEGAIDAANILKPALARgeLQ----------CIGATTLDEYrkhieKDPALERRFQP-VYVGEPSV- 343


                 ....*...
gi 86561515  289 arKEMFRI 296
Cdd:CHL00095 344 --EETIEI 349
COG1373 COG1373
Predicted ATPase, AAA+ superfamily [General function prediction only];
154-220 2.07e-03

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


Pssm-ID: 440984 [Multi-domain]  Cd Length: 405  Bit Score: 40.31  E-value: 2.07e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 86561515 154 ILLFGPPGTGKSYIAKAVATEAGESTFFSISSSDLMSKWLGESEKLVKNLFALAREHKPsiIFIDEI 220
Cdd:COG1373  23 VVITGPRQVGKTTLLKQLAKELENILYINLDDPRLRALAEEDPDDLLEALKELYPGKTY--LFLDEI 87
PRK08181 PRK08181
transposase; Validated
 154-191 2.79e-03

transposase; Validated


Pssm-ID: 136670 [Multi-domain]  Cd Length: 269  Bit Score: 39.53  E-value: 2.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 86561515  154 ILLFGPPGTGKSYIAKAVA---TEAGESTFFSiSSSDLMSK 191
Cdd:PRK08181 109 LLLFGPPGGGKSHLAAAIGlalIENGWRVLFT-RTTDLVQK 148
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 154-232 4.45e-03

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain 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: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 38.74  E-value: 4.45e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 154 ILLFGPPGTGKSYIAKAVA---------------TEAGestffsisssdlmskWLGES-----EKLVKNL-FALAREHKp 212
Cdd:cd19497  53 ILLIGPTGSGKTLLAQTLAkildvpfaiadattlTEAG---------------YVGEDvenilLKLLQAAdYDVERAQR- 116

                        90       100
                ....*....|....*....|
gi 86561515 213 SIIFIDEIDSLcSARSDNES 232
Cdd:cd19497 117 GIVYIDEIDKI-ARKSENPS 135
PRK08116 PRK08116
hypothetical protein; Validated
 153-174 5.56e-03

hypothetical protein; Validated


Pssm-ID: 236153 [Multi-domain]  Cd Length: 268  Bit Score: 38.46  E-value: 5.56e-03
                         10        20
                 ....*....|....*....|..
gi 86561515  153 GILLFGPPGTGKSYIAKAVATE 174
Cdd:PRK08116 116 GLLLWGSVGTGKTYLAACIANE 137
PRK09183 PRK09183
transposase/IS protein; Provisional
 154-189 6.52e-03

transposase/IS protein; Provisional


Pssm-ID: 181681  Cd Length: 259  Bit Score: 38.15  E-value: 6.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 86561515  154 ILLFGPPGTGKSYIAKAV---ATEAGESTFFsISSSDLM 189
Cdd:PRK09183 105 IVLLGPSGVGKTHLAIALgyeAVRAGIKVRF-TTAADLL 142
44 PHA02544
clamp loader, small subunit; Provisional
 132-226 7.08e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 38.43  E-value: 7.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515  132 EAVILPIKFPQLFTG----NRKPwqGILLFGP-PGTGKSYIAKAVATEAGESTFFSISSSDLMSkwlgesekLVKNL--- 203
Cdd:PHA02544  21 DECILPAADKETFKSivkkGRIP--NMLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSDCRID--------FVRNRltr 90

                         90       100
                 ....*....|....*....|....*
gi 86561515  204 FA--LAREHKPSIIFIDEIDSLCSA 226
Cdd:PHA02544  91 FAstVSLTGGGKVIIIDEFDRLGLA 115
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 154-222 7.94e-03

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 36.84  E-value: 7.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515 154 ILLFGPPGTGKSYIAKAVATE----AGESTFFSISSSDLMSKWL------------GESEKLvknlfALARE--HKPSII 215
Cdd:cd00267  28 VALVGPNGSGKSTLLRAIAGLlkptSGEILIDGKDIAKLPLEELrrrigyvpqlsgGQRQRV-----ALARAllLNPDLL 102


                ....*..
gi 86561515 216 FIDEIDS 222
Cdd:cd00267 103 LLDEPTS 109
COG0645 COG0645
Predicted kinase, contains AAA domain [General function prediction only];
154-176 7.98e-03

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


Pssm-ID: 440410 [Multi-domain]  Cd Length: 164  Bit Score: 36.81  E-value: 7.98e-03
                        10        20
                ....*....|....*....|...
gi 86561515 154 ILLFGPPGTGKSYIAKAVATEAG 176
Cdd:COG0645   2 ILVCGLPGSGKSTLARALAERLG 24
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 119-173 8.29e-03

Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that catalyzes the insertion of Mg2+ into protoporphyrin IX. This is the first unique step in the synthesis of (bacterio)chlorophyll. Due to this, it is thought that Mg-chelatase has an important role in channelling inter- mediates into the (bacterio)chlorophyll branch in response to conditions suitable for photosynthetic growth. ChlI and BchD have molecular weight between 38-42 kDa.


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 37.51  E-value: 8.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 86561515   119 DIAGLEGAKEALKEAVIlpikfpqlftGNrkpwQGILLFGPPGTGKSYIAKAVAT 173
Cdd:pfam01078   4 DVKGQEQAKRALEIAAA----------GG----HNLLMIGPPGSGKTMLAKRLPG 44
AAA_18 pfam13238
AAA domain;
154-239 9.34e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 36.25  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 86561515   154 ILLFGPPGTGKSYIAKAVATEAGESTFFS--ISSSDLMSKWLGES-----------EKLVKNLFALAREHKPSIIFIDEI 220
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRLGFGDNVRdlALENGLVLGDDPETreskrldedklDRLLDLLEENAALEEGGNLIIDGH 80

                          90
                  ....*....|....*....
gi 86561515   221 dslcsaRSDNESESARRIK 239
Cdd:pfam13238  81 ------LAELEPERAKDLV 93
 
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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