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Conserved domains on  [gi|495619429|ref|WP_008344008|]
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MULTISPECIES: stage V sporulation protein K [Bacillus]

Protein Classification

spore_V_K family protein( domain architecture ID 11495558)

spore_V_K family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
spore_V_K TIGR02881
stage V sporulation protein K; Members of this protein family are the stage V sporulation ...
 50-311 2.11e-170

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


:

Pssm-ID: 163057 [Multi-domain]  Cd Length: 261  Bit Score: 473.05  E-value: 2.11e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429   50 IEREMNSLVGMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALHMMFKGNPGTGKTTVARLVGKLFFEMNVLSKGHLIEA 129
Cdd:TIGR02881   1 VERELSRMVGLDEVKALIKEIYAWIQINEKRKEEGLKTSKQVLHMIFKGNPGTGKTTVARILGKLFKEMNVLSKGHLIEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  130 ERGDLVGEYIGHTAQKTRDLIKKSLGGILFIDEAYSLARGGEKDFGKEAIDTLVKHMEDKQHEFILILAGYSKEMDHFLS 209
Cdd:TIGR02881  81 ERADLVGEYIGHTAQKTREVIKKALGGVLFIDEAYSLARGGEKDFGKEAIDTLVKGMEDNRNEFVLILAGYSDEMDYFLS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  210 LNPGLQSRFPININFPDYTVDQLMDIAKRMMADREYVFTQEAEWKLRDYLMHIKStTSPAKFSNGRFVRNTIEKAIRTQA 289
Cdd:TIGR02881 161 LNPGLRSRFPISIDFPDYTVEELMEIAERMVKEREYKLTEEAKWKLREHLYKVDQ-LSSREFSNARYVRNIIEKAIRRQA 239

                         250       260
                  ....*....|....*....|..
gi 495619429  290 MRLLLVDHYDKKDLLTIKSHDL 311
Cdd:TIGR02881 240 VRLLDKSDYSKEDLMLLKKEDL 261
 
Name Accession Description Interval E-value
spore_V_K TIGR02881
stage V sporulation protein K; Members of this protein family are the stage V sporulation ...
 50-311 2.11e-170

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


Pssm-ID: 163057 [Multi-domain]  Cd Length: 261  Bit Score: 473.05  E-value: 2.11e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429   50 IEREMNSLVGMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALHMMFKGNPGTGKTTVARLVGKLFFEMNVLSKGHLIEA 129
Cdd:TIGR02881   1 VERELSRMVGLDEVKALIKEIYAWIQINEKRKEEGLKTSKQVLHMIFKGNPGTGKTTVARILGKLFKEMNVLSKGHLIEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  130 ERGDLVGEYIGHTAQKTRDLIKKSLGGILFIDEAYSLARGGEKDFGKEAIDTLVKHMEDKQHEFILILAGYSKEMDHFLS 209
Cdd:TIGR02881  81 ERADLVGEYIGHTAQKTREVIKKALGGVLFIDEAYSLARGGEKDFGKEAIDTLVKGMEDNRNEFVLILAGYSDEMDYFLS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  210 LNPGLQSRFPININFPDYTVDQLMDIAKRMMADREYVFTQEAEWKLRDYLMHIKStTSPAKFSNGRFVRNTIEKAIRTQA 289
Cdd:TIGR02881 161 LNPGLRSRFPISIDFPDYTVEELMEIAERMVKEREYKLTEEAKWKLREHLYKVDQ-LSSREFSNARYVRNIIEKAIRRQA 239

                         250       260
                  ....*....|....*....|..
gi 495619429  290 MRLLLVDHYDKKDLLTIKSHDL 311
Cdd:TIGR02881 240 VRLLDKSDYSKEDLMLLKKEDL 261
cbbX CHL00181
CbbX; Provisional
 45-311 7.43e-76

CbbX; Provisional


Pssm-ID: 177083 [Multi-domain]  Cd Length: 287  Bit Score: 234.23  E-value: 7.43e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  45 SILREIEREmnsLVGMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALHMMFKGNPGTGKTTVARLVGKLFFEMNVLSKG 124
Cdd:CHL00181  16 EVLDILDEE---LVGLAPVKTRIREIAALLLIDRLRKNLGLTSSNPGLHMSFTGSPGTGKTTVALKMADILYKLGYIKKG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 125 HLIEAERGDLVGEYIGHTAQKTRDLIKKSLGGILFIDEAYSLAR-GGEKDFGKEAIDTLVKHMEDKQHEFILILAGYSKE 203
Cdd:CHL00181  93 HLLTVTRDDLVGQYIGHTAPKTKEVLKKAMGGVLFIDEAYYLYKpDNERDYGSEAIEILLQVMENQRDDLVVIFAGYKDR 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 204 MDHFLSLNPGLQSRFPININFPDYTVDQLMDIAKRMMADREYVFTQEAEWKLRDYlmhIKSTTSPAKFSNGRFVRNTIEK 283
Cdd:CHL00181 173 MDKFYESNPGLSSRIANHVDFPDYTPEELLQIAKIMLEEQQYQLTPEAEKALLDY---IKKRMEQPLFANARSVRNALDR 249

                        250       260       270
                 ....*....|....*....|....*....|
gi 495619429 284 AIRTQAMRLLL--VDHYDKKDLLTIKSHDL 311
Cdd:CHL00181 250 ARMRQANRIFEsgGRVLTKADLVTIEAEDI 279
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 26-315 1.97e-64

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: 208.23  E-value: 1.97e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  26 DADSEAEYLEALQKNEAKHSILREIEREMNSLVGMDEMKRNIKEIYAWIFVN-QKRQEQGLKVGKqalHMMFKGNPGTGK 104
Cdd:COG0464  128 ALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRpELREEYGLPPPR---GLLLYGPPGTGK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 105 TTVARLVGKLffemnvlSKGHLIEAERGDLVGEYIGHTAQKTRDLIKKSLG---GILFIDEAYSLA--RGGEKD-FGKEA 178
Cdd:COG0464  205 TLLARALAGE-------LGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGlapCVLFIDEADALAgkRGEVGDgVGRRV 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 179 IDTLVKHMEDKQHEFILILAGYskemdHFLSLNPGLQSRFPININFPDYTVDQLMDIAKRMMADREyvFTQEAEWKlrdy 258
Cdd:COG0464  278 VNTLLTEMEELRSDVVVIAATN-----RPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRP--LDEDVDLE---- 346

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495619429 259 lmHIKSTTspaKFSNGRFVRNTIEKAIRtQAMRlLLVDHYDKKDLL-TIKSHDLQMKE 315
Cdd:COG0464  347 --ELAEAT---EGLSGADIRNVVRRAAL-QALR-LGREPVTTEDLLeALEREDIFLKR 397
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 94-225 9.04e-22

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: 88.80  E-value: 9.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429   94 MMFKGNPGTGKTTVARLVGKlffEMNVlskgHLIEAERGDLVGEYIGHTAQKTRDLI---KKSLGGILFIDEAYSLAR-- 168
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAK---ELGA----PFIEISGSELVSKYVGESEKRLRELFeaaKKLAPCVIFIDEIDALAGsr 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495619429  169 -GGEKDFGKEAIDTLVKHMED---KQHEFILILAGYSKEMdhflsLNPGLQSRFPININFP 225
Cdd:pfam00004  74 gSGGDSESRRVVNQLLTELDGftsSNSKVIVIAATNRPDK-----LDPALLGRFDRIIEFP 129
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 75-225 1.34e-14

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: 69.87  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  75 FVNQKRQEQGLKVGKQALHMMFKGNPGTGKTTVARLVGKLFFEMNV----LSKGHLIEaerGDLVGEYIGHTA-QKTRDL 149
Cdd:cd00009    3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGApflyLNASDLLE---GLVVAELFGHFLvRLLFEL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495619429 150 IKKSLGGILFIDEAYSLARGGEKDFgKEAIDTLVKHMEDKqHEFILILAGYSKEMDHFLslnPGLQSRFPININFP 225
Cdd:cd00009   80 AEKAKPGVLFIDEIDSLSRGAQNAL-LRVLETLNDLRIDR-ENVRVIGATNRPLLGDLD---RALYDRLDIRIVIP 150
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 93-198 3.63e-07

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.91  E-value: 3.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429    93 HMMFKGNPGTGKTTVARLVGKLFFEMN----VLSKGHLIEAERGDLVGEYI---------GHTAQKTRDLIKKSLGGILF 159
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGggviYIDGEDILEEVLDQLLLIIVggkkasgsgELRLRLALALARKLKPDVLI 83

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 495619429   160 IDEAYSLARGGEKDFGKEAIDTLVKHMEDKQHEFILILA 198
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
 
Name Accession Description Interval E-value
spore_V_K TIGR02881
stage V sporulation protein K; Members of this protein family are the stage V sporulation ...
 50-311 2.11e-170

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


Pssm-ID: 163057 [Multi-domain]  Cd Length: 261  Bit Score: 473.05  E-value: 2.11e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429   50 IEREMNSLVGMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALHMMFKGNPGTGKTTVARLVGKLFFEMNVLSKGHLIEA 129
Cdd:TIGR02881   1 VERELSRMVGLDEVKALIKEIYAWIQINEKRKEEGLKTSKQVLHMIFKGNPGTGKTTVARILGKLFKEMNVLSKGHLIEV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  130 ERGDLVGEYIGHTAQKTRDLIKKSLGGILFIDEAYSLARGGEKDFGKEAIDTLVKHMEDKQHEFILILAGYSKEMDHFLS 209
Cdd:TIGR02881  81 ERADLVGEYIGHTAQKTREVIKKALGGVLFIDEAYSLARGGEKDFGKEAIDTLVKGMEDNRNEFVLILAGYSDEMDYFLS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  210 LNPGLQSRFPININFPDYTVDQLMDIAKRMMADREYVFTQEAEWKLRDYLMHIKStTSPAKFSNGRFVRNTIEKAIRTQA 289
Cdd:TIGR02881 161 LNPGLRSRFPISIDFPDYTVEELMEIAERMVKEREYKLTEEAKWKLREHLYKVDQ-LSSREFSNARYVRNIIEKAIRRQA 239

                         250       260
                  ....*....|....*....|..
gi 495619429  290 MRLLLVDHYDKKDLLTIKSHDL 311
Cdd:TIGR02881 240 VRLLDKSDYSKEDLMLLKKEDL 261
cbbX_cfxQ TIGR02880
probable Rubsico expression protein CbbX; Proteins in this family are now designated CbbX. ...
 37-311 1.97e-83

probable Rubsico expression protein CbbX; Proteins in this family are now designated CbbX. Some previously were CfxQ (carbon fixation Q). Its gene is often found immmediately downstream of the Rubisco large and small chain genes, and it is suggested to be necessary for Rubisco expression. CbbX has been shown to be necessary for photoautotrophic growth. This protein belongs to the larger family of pfam00004, ATPase family Associated with various cellular Activities. Within that larger family, members of this family are most closely related to the stage V sporulation protein K, or SpoVK, in endospore-forming bacteria such as Bacillus subtilis.


Pssm-ID: 200217 [Multi-domain]  Cd Length: 284  Bit Score: 253.61  E-value: 1.97e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429   37 LQKNEAKHSI---LREIEREmnsLVGMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALHMMFKGNPGTGKTTVARLVGK 113
Cdd:TIGR02880   4 LRAEYEGSGItevLDQLDRE---LIGLKPVKTRIREIAALLLVERARQKLGLASAAPTLHMSFTGNPGTGKTTVALRMAQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  114 LFFEMNVLSKGHLIEAERGDLVGEYIGHTAQKTRDLIKKSLGGILFIDEAYSLAR-GGEKDFGKEAIDTLVKHMEDKQHE 192
Cdd:TIGR02880  81 ILHRLGYVRKGHLVSVTRDDLVGQYIGHTAPKTKEVLKRAMGGVLFIDEAYYLYRpDNERDYGQEAIEILLQVMENNRDD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  193 FILILAGYSKEMDHFLSLNPGLQSRFPININFPDYTVDQLMDIAKRMMADREYVFTQEAEWKLRDYlmhIKSTTSPAKFS 272
Cdd:TIGR02880 161 LVVILAGYKDRMDSFFESNPGFSSRVAHHIDFPDYSDEELLEIAGLMLDEQQYRFTAEAETAFADY---IALRRTQPHFA 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 495619429  273 NGRFVRNTIEKAIRTQAMRLL--LVDHYDKKDLLTIKSHDL 311
Cdd:TIGR02880 238 NARSIRNALDRARLRQANRLFtaSDGVLDKSDLSTIAPEDI 278
T7SS_EccA TIGR03922
type VII secretion AAA-ATPase EccA; This model represents the AAA family ATPase, EccA, of the ...
 26-312 1.42e-81

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: 257.08  E-value: 1.42e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429   26 DADSE--AEYLEALQKNEAKHSILREIEREMNSLVGMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALHMMFKGNPGTG 103
Cdd:TIGR03922 245 DPSSApsRAEFVDPAAAERKAKLLAEAEAELAEQIGLERVKRQVAALKSSTAMALARAERGLPVAQTSNHMLFAGPPGTG 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  104 KTTVARLVGKLFFEMNVLSKGHLIEAERGDLVGEYIGHTAQKTRDLIKKSLGGILFIDEAYSL--ARGGEKD-FGKEAID 180
Cdd:TIGR03922 325 KTTIARVVAKIYCGLGVLRKPLVREVSRADLIGQYIGESEAKTNEIIDSALGGVLFLDEAYTLveTGYGQKDpFGLEAID 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  181 TLVKHMEDKQHEFILILAGYSKEMDHFLSLNPGLQSRFPININFPDYTVDQLMDIAKRMMADREYVFTQEAEWKLRDYLM 260
Cdd:TIGR03922 405 TLLARMENDRDRLVVIGAGYRKDLDKFLEVNEGLRSRFTRVIEFPSYSPDELVEIARRMATERDSVLDDAAADALLEAAT 484

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495619429  261 HIKSTTSPAK----------FSNGRFVRNTIEKAIRTQAMRLLLVDHYDK---KDLLTIKSHDLQ 312
Cdd:TIGR03922 485 TLAQDTTPDAngdlrrgldiAGNGRFVRNVVERAEEERDFRLDHSDRLDAvtvDDLMEITADDVA 549
cbbX CHL00181
CbbX; Provisional
 45-311 7.43e-76

CbbX; Provisional


Pssm-ID: 177083 [Multi-domain]  Cd Length: 287  Bit Score: 234.23  E-value: 7.43e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  45 SILREIEREmnsLVGMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALHMMFKGNPGTGKTTVARLVGKLFFEMNVLSKG 124
Cdd:CHL00181  16 EVLDILDEE---LVGLAPVKTRIREIAALLLIDRLRKNLGLTSSNPGLHMSFTGSPGTGKTTVALKMADILYKLGYIKKG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 125 HLIEAERGDLVGEYIGHTAQKTRDLIKKSLGGILFIDEAYSLAR-GGEKDFGKEAIDTLVKHMEDKQHEFILILAGYSKE 203
Cdd:CHL00181  93 HLLTVTRDDLVGQYIGHTAPKTKEVLKKAMGGVLFIDEAYYLYKpDNERDYGSEAIEILLQVMENQRDDLVVIFAGYKDR 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 204 MDHFLSLNPGLQSRFPININFPDYTVDQLMDIAKRMMADREYVFTQEAEWKLRDYlmhIKSTTSPAKFSNGRFVRNTIEK 283
Cdd:CHL00181 173 MDKFYESNPGLSSRIANHVDFPDYTPEELLQIAKIMLEEQQYQLTPEAEKALLDY---IKKRMEQPLFANARSVRNALDR 249

                        250       260       270
                 ....*....|....*....|....*....|
gi 495619429 284 AIRTQAMRLLL--VDHYDKKDLLTIKSHDL 311
Cdd:CHL00181 250 ARMRQANRIFEsgGRVLTKADLVTIEAEDI 279
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 26-315 1.97e-64

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: 208.23  E-value: 1.97e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  26 DADSEAEYLEALQKNEAKHSILREIEREMNSLVGMDEMKRNIKEIYAWIFVN-QKRQEQGLKVGKqalHMMFKGNPGTGK 104
Cdd:COG0464  128 ALALAAPLVTYEDIGGLEEELLELREAILDDLGGLEEVKEELRELVALPLKRpELREEYGLPPPR---GLLLYGPPGTGK 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 105 TTVARLVGKLffemnvlSKGHLIEAERGDLVGEYIGHTAQKTRDLIKKSLG---GILFIDEAYSLA--RGGEKD-FGKEA 178
Cdd:COG0464  205 TLLARALAGE-------LGLPLIEVDLSDLVSKYVGETEKNLREVFDKARGlapCVLFIDEADALAgkRGEVGDgVGRRV 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 179 IDTLVKHMEDKQHEFILILAGYskemdHFLSLNPGLQSRFPININFPDYTVDQLMDIAKRMMADREyvFTQEAEWKlrdy 258
Cdd:COG0464  278 VNTLLTEMEELRSDVVVIAATN-----RPDLLDPALLRRFDEIIFFPLPDAEERLEIFRIHLRKRP--LDEDVDLE---- 346

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495619429 259 lmHIKSTTspaKFSNGRFVRNTIEKAIRtQAMRlLLVDHYDKKDLL-TIKSHDLQMKE 315
Cdd:COG0464  347 --ELAEAT---EGLSGADIRNVVRRAAL-QALR-LGREPVTTEDLLeALEREDIFLKR 397
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
54-289 1.37e-24

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 99.57  E-value: 1.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  54 MNSLVGMDEMKRNIKEIYAWIFVNQKRQEQGLKVgkqALHMMFKGNPGTGKTTVARlvgKLFFEMNVlskgHLIEAERGD 133
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRKFGLWP---PRKILFYGPPGTGKTMLAE---ALAGELKL----PLLTVRLDS 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 134 LVGEYIGHTAQKTRDLIK--KSLGGILFIDEAYSLA--RGGEKDFG--KEAIDTLVKHMEDKQHEFILILAGYSKEMdhf 207
Cdd:COG1223   71 LIGSYLGETARNLRKLFDfaRRAPCVIFFDEFDAIAkdRGDQNDVGevKRVVNALLQELDGLPSGSVVIAATNHPEL--- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 208 lsLNPGLQSRFPININFPDYTVDQLMDIAKRMMadREYVFTQEAEWKLrdylmhIKSTTSPAKFSN-GRFVRNTIEKAIR 286
Cdd:COG1223  148 --LDSALWRRFDEVIEFPLPDKEERKEILELNL--KKFPLPFELDLKK------LAKKLEGLSGADiEKVLKTALKKAIL 217


                 ...
gi 495619429 287 TQA 289
Cdd:COG1223  218 EDR 220
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 94-225 9.04e-22

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: 88.80  E-value: 9.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429   94 MMFKGNPGTGKTTVARLVGKlffEMNVlskgHLIEAERGDLVGEYIGHTAQKTRDLI---KKSLGGILFIDEAYSLAR-- 168
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAK---ELGA----PFIEISGSELVSKYVGESEKRLRELFeaaKKLAPCVIFIDEIDALAGsr 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495619429  169 -GGEKDFGKEAIDTLVKHMED---KQHEFILILAGYSKEMdhflsLNPGLQSRFPININFP 225
Cdd:pfam00004  74 gSGGDSESRRVVNQLLTELDGftsSNSKVIVIAATNRPDK-----LDPALLGRFDRIIEFP 129
AAA_lid_6 pfam17866
AAA lid domain; This entry represents the alpha helical AAA+ lid domain that is found to the ...
 250-311 2.76e-15

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


Pssm-ID: 465539 [Multi-domain]  Cd Length: 60  Bit Score: 69.13  E-value: 2.76e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495619429  250 EAEWKLRDYLMHIKSTTSpakFSNGRFVRNTIEKAIRTQAMRLLLVDHYDKKDLLTIKSHDL 311
Cdd:pfam17866   2 EAEEKLRELLERARRDPN---FGNARFVRNLLERAIRRQALRLAAEEELTREDLMTLTAEDF 60
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 75-225 1.34e-14

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: 69.87  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  75 FVNQKRQEQGLKVGKQALHMMFKGNPGTGKTTVARLVGKLFFEMNV----LSKGHLIEaerGDLVGEYIGHTA-QKTRDL 149
Cdd:cd00009    3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGApflyLNASDLLE---GLVVAELFGHFLvRLLFEL 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495619429 150 IKKSLGGILFIDEAYSLARGGEKDFgKEAIDTLVKHMEDKqHEFILILAGYSKEMDHFLslnPGLQSRFPININFP 225
Cdd:cd00009   80 AEKAKPGVLFIDEIDSLSRGAQNAL-LRVLETLNDLRIDR-ENVRVIGATNRPLLGDLD---RALYDRLDIRIVIP 150
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 64-224 2.47e-08

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: 52.29  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  64 KRNIKEIYAWIFVNQKRQEQGLKVGKQALhmmFKGNPGTGKTTVARLVGKlffemnvLSKGHLIEAERGDLVGEYIGHTA 143
Cdd:cd19481    2 KASLREAVEAPRRGSRLRRYGLGLPKGIL---LYGPPGTGKTLLAKALAG-------ELGLPLIVVKLSSLLSKYVGESE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 144 QKTRDLI---KKSLGGILFIDEAYSLAR----GGEKDFGKEAIDTLVKHMEDKQHE--FILILAGYSKEMdhflsLNPGL 214
Cdd:cd19481   72 KNLRKIFeraRRLAPCILFIDEIDAIGRkrdsSGESGELRRVLNQLLTELDGVNSRskVLVIAATNRPDL-----LDPAL 146

                        170
                 ....*....|..
gi 495619429 215 QS--RFPININF 224
Cdd:cd19481  147 LRpgRFDEVIEF 158
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
58-306 8.19e-08

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 52.83  E-value: 8.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  58 VGMDEMKRNIKeiyawIFVN--QKRQEqglkvgkqAL-HMMFKGNPGTGKTTVARLVGKlffEMNV---LSKGHLIEaER 131
Cdd:PRK00080  28 IGQEKVKENLK-----IFIEaaKKRGE--------ALdHVLLYGPPGLGKTTLANIIAN---EMGVnirITSGPALE-KP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 132 GDLVGeyightaqktrdlIKKSL--GGILFIDEAYSLARGGEkdfgkeaiDTLVKHMEDkqheF---ILILAGYSK---E 203
Cdd:PRK00080  91 GDLAA-------------ILTNLeeGDVLFIDEIHRLSPVVE--------EILYPAMED----FrldIMIGKGPAArsiR 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 204 MD--HF-----------LSlNPgLQSRFPININFPDYTVDQLMDIAKRmMADreyvftqeaewklrdyLMHIKSTTSP-- 268
Cdd:PRK00080 146 LDlpPFtligattraglLT-SP-LRDRFGIVQRLEFYTVEELEKIVKR-SAR----------------ILGVEIDEEGal 206

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495619429 269 --AKFSNG---------RFVR--------NTIEKAIRTQAMRLLLVDHY-----DKKDLLTI 306
Cdd:PRK00080 207 eiARRSRGtprianrllRRVRdfaqvkgdGVITKEIADKALDMLGVDELgldemDRKYLRTI 268
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 57-175 1.28e-07

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 52.32  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  57 LVGMDEMKRNIKEIyawIFVNQKRQEQGLKVGKQALH-MMFKGNPGTGKTTVARLV-GKL---FFEMnVLSkghlieaer 131
Cdd:COG1222   80 IGGLDEQIEEIREA---VELPLKNPELFRKYGIEPPKgVLLYGPPGTGKTLLAKAVaGELgapFIRV-RGS--------- 146

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495619429 132 gDLVGEYIGHTAQKTRDL---IKKSLGGILFIDEAYSLA--RGGEKDFG 175
Cdd:COG1222  147 -ELVSKYIGEGARNVREVfelAREKAPSIIFIDEIDAIAarRTDDGTSG 194
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 93-198 3.63e-07

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 48.91  E-value: 3.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429    93 HMMFKGNPGTGKTTVARLVGKLFFEMN----VLSKGHLIEAERGDLVGEYI---------GHTAQKTRDLIKKSLGGILF 159
Cdd:smart00382   4 VILIVGPPGSGKTTLARALARELGPPGggviYIDGEDILEEVLDQLLLIIVggkkasgsgELRLRLALALARKLKPDVLI 83

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 495619429   160 IDEAYSLARGGEKDFGKEAIDTLVKHMEDKQHEFILILA 198
Cdd:smart00382  84 LDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
39-226 6.31e-07

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 50.80  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  39 KNEAKHSILREIEREMNSLVGMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALHMmfkGNPGTGKTTVARLVGKlffem 118
Cdd:PRK10733 136 KSKARMLTEDQIKTTFADVAGCDEAKEEVAELVEYLREPSRFQKLGGKIPKGVLMV---GPPGTGKTLLAKAIAG----- 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 119 nvLSKGHLIEAERGDLVGEYIGHTAQKTRDLI---KKSLGGILFIDEAYSLAR------GGEKDFGKEAIDTLVKHMED- 188
Cdd:PRK10733 208 --EAKVPFFTISGSDFVEMFVGVGASRVRDMFeqaKKAAPCIIFIDEIDAVGRqrgaglGGGHDEREQTLNQMLVEMDGf 285

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495619429 189 KQHEFILILAGYSKE--MDHFLsLNPGLQSRfPININFPD 226
Cdd:PRK10733 286 EGNEGIIVIAATNRPdvLDPAL-LRPGRFDR-QVVVGLPD 323
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 58-168 1.93e-06

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: 47.23  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  58 VGMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALhmmFKGNPGTGKTTVARLV----GKLFFEMNvlskghlieaeRGD 133
Cdd:cd19501    7 AGCEEAKEELKEVVEFLKNPEKFTKLGAKIPKGVL---LVGPPGTGKTLLAKAVageaGVPFFSIS-----------GSD 72

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495619429 134 LVGEYIGHTAQKTRDLI---KKSLGGILFIDEAYSLAR 168
Cdd:cd19501   73 FVEMFVGVGASRVRDLFeqaKKNAPCIVFIDEIDAVGR 110
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 58-168 3.20e-06

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


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 46.34  E-value: 3.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429   58 VGMDEMKRNIKeiyawIFVN--QKRQEqglkvgkqAL-HMMFKGNPGTGKTTVARLVGKlffEMNV---LSKGHLIEaER 131
Cdd:pfam05496  10 IGQEKVKENLK-----IFIEaaKQRGE--------ALdHVLLYGPPGLGKTTLANIIAN---EMGVnirITSGPAIE-RP 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 495619429  132 GDLVGeyightaqktrdlIKKSL--GGILFIDEAYSLAR 168
Cdd:pfam05496  73 GDLAA-------------ILTNLepGDVLFIDEIHRLNR 98
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 88-288 3.66e-06

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 48.16  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  88 GKQALHMMFKGNPGTGKTTVARLV----GKLFFEMN-VLSKGHLIEAergdlvgeyIGHTAQKTRDLIKKSlggILFIDE 162
Cdd:PRK13342  33 AGRLSSMILWGPPGTGKTTLARIIagatDAPFEALSaVTSGVKDLRE---------VIEEARQRRSAGRRT---ILFIDE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 163 aysLARggekdFGKEAIDTLVKHMEDkqHEFILILAgySKEMDHFlSLNPGLQSR------FPIninfpdyTVDQLMDIA 236
Cdd:PRK13342 101 ---IHR-----FNKAQQDALLPHVED--GTITLIGA--TTENPSF-EVNPALLSRaqvfelKPL-------SEEDIEQLL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495619429 237 KRMMADRE---YVFTQEAewklRDYLmhiksttspAKFSNG--RFVRNTIEKAIRTQ 288
Cdd:PRK13342 161 KRALEDKErglVELDDEA----LDAL---------ARLANGdaRRALNLLELAALGV 204
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 64-175 6.93e-05

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: 42.66  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  64 KRNIKEIYAWifvNQKRQEQGLKVGKQALH-MMFKGNPGTGKTTVARLVGKLfFEMNVLS-KGhlieaerGDLVGEYIGH 141
Cdd:cd19511    2 KRELKEAVEW---PLKHPDAFKRLGIRPPKgVLLYGPPGCGKTLLAKALASE-AGLNFISvKG-------PELFSKYVGE 70

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495619429 142 TAQKTRDLIKK---SLGGILFIDEAYSLA--RGGEKDFG 175
Cdd:cd19511   71 SERAVREIFQKarqAAPCIIFFDEIDSLAprRGQSDSSG 109
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 32-186 7.75e-05

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: 44.13  E-value: 7.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429   32 EYLEALQKNEAkhSILREIEREM-----NSLVGMDEMKRNIKEIYAWIFVNQKRQEQ-GLKVGKQALhmMFkGNPGTGKT 105
Cdd:TIGR01243 427 DFMEALKMVEP--SAIREVLVEVpnvrwSDIGGLEEVKQELREAVEWPLKHPEIFEKmGIRPPKGVL--LF-GPPGTGKT 501

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  106 TVARLVGKlffemnvLSKGHLIEAERGDLVGEYIGHTAQKTRDLIKK---SLGGILFIDEAYSLARGGEKDFGKEAIDTL 182
Cdd:TIGR01243 502 LLAKAVAT-------ESGANFIAVRGPEILSKWVGESEKAIREIFRKarqAAPAIIFFDEIDAIAPARGARFDTSVTDRI 574


                  ....
gi 495619429  183 VKHM 186
Cdd:TIGR01243 575 VNQL 578
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 59-167 2.30e-04

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: 41.12  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  59 GMDEMKRNIKEIYAWIFVNQKRQEQ-GLKVGKQALhmmFKGNPGTGKTTVARLVGKlffEMNVlskgHLIEAERGDLVGE 137
Cdd:cd19503    4 GLDEQIASLKELIELPLKYPELFRAlGLKPPRGVL---LHGPPGTGKTLLARAVAN---EAGA----NFLSISGPSIVSK 73

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495619429 138 YIGHTAQKTRDLI---KKSLGGILFIDEAYSLA 167
Cdd:cd19503   74 YLGESEKNLREIFeeaRSHAPSIIFIDEIDALA 106
RecA-like_HslU cd19498
ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease ...
 48-222 2.43e-04

ATP-dependent protease ATPase subunit HslU; HslU is a component of the ATP-dependent protease HslVU. In HslVU, HslU ATPase serves to unfold and translocate protein substrate, and the HslV protease degrades the unfolded proteins. This RecA-like_HslU 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: 410906 [Multi-domain]  Cd Length: 183  Bit Score: 41.21  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  48 REIEREMNS-LVGMDEMKRNIkeiyAWIFVNQKRQEQGLKVGKQAL---HMMFKGNPGTGKTTVARLVGKL----FFEmn 119
Cdd:cd19498    3 REIVSELDKyIIGQDEAKRAV----AIALRNRWRRMQLPEELRDEVtpkNILMIGPTGVGKTEIARRLAKLagapFIK-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429 120 vlskghlIEAERGDLVGeYIGHTAQK-TRDLIKkslgGILFIDEAYSLARGGE---KDFGKEAI--DTL---------VK 184
Cdd:cd19498   77 -------VEATKFTEVG-YVGRDVESiIRDLVE----GIVFIDEIDKIAKRGGssgPDVSREGVqrDLLpivegstvsTK 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 495619429 185 HMEDKQHEFILILAG---YSKEMDhflsLNPGLQSRFPINI 222
Cdd:cd19498  145 YGPVKTDHILFIAAGafhVAKPSD----LIPELQGRFPIRV 181
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 58-168 2.81e-04

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


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 41.99  E-value: 2.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  58 VGMDEMKRNIKeiyawIFVN--QKRQEqglkvgkqAL-HMMFKGNPGTGKTTVARLVGKlffEMNV---LSKGHLIEAEr 131
Cdd:COG2255   31 IGQEKVKENLK-----IFIEaaKKRGE--------ALdHVLLYGPPGLGKTTLAHIIAN---EMGVnirITSGPAIEKP- 93

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 495619429 132 GDLVGeyightaqktrdlIKKSL--GGILFIDEAYSLAR 168
Cdd:COG2255   94 GDLAA-------------ILTNLeeGDVLFIDEIHRLSR 119
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 94-186 4.73e-04

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: 40.19  E-value: 4.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  94 MMFKGNPGTGKTTVARLVGKLfFEMNVLS-KGhlieaerGDLVGEYIGHTAQKTRDLIKKSLGG---ILFIDEAYSLA-- 167
Cdd:cd19527   29 ILLYGPPGTGKTLLAKAIATE-CSLNFLSvKG-------PELINMYIGESEANVREVFQKARDAkpcVIFFDELDSLAps 100

                         90
                 ....*....|....*....
gi 495619429 168 RGGEKDFGKeAIDTLVKHM 186
Cdd:cd19527  101 RGNSGDSGG-VMDRVVSQL 118
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 94-195 7.14e-04

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: 39.42  E-value: 7.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  94 MMFKGNPGTGKTTVARLVGKlffemnvLSKGHLIEAERGDLVGEYIGHTAQKTRDLIKKSLGG---ILFIDEAYSLA--R 168
Cdd:cd19528   30 VLFYGPPGCGKTLLAKAIAN-------ECQANFISVKGPELLTMWFGESEANVRDIFDKARAAapcVLFFDELDSIAkaR 102

                         90       100       110
                 ....*....|....*....|....*....|....
gi 495619429 169 GGEKDFGKEAIDTLVKH-------MEDKQHEFIL 195
Cdd:cd19528  103 GGNIGDAGGAADRVINQiltemdgMNTKKNVFII 136
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 93-198 9.97e-04

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: 39.05  E-value: 9.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  93 HMMFKGNPGTGKTTVAR-LVGKLFFEMNVLSKGHLIEAERGdlvgeyiGHTA-QKTRDLIKKSLGG-ILFIDEAYSLARG 169
Cdd:cd19512   24 NILFYGPPGTGKTLFAKkLALHSGMDYAIMTGGDVAPMGRE-------GVTAiHKVFDWANTSRRGlLLFVDEADAFLRK 96

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495619429 170 GEKDFGKE----AIDTLVKHMEDKQHEFILILA 198
Cdd:cd19512   97 RSTEKISEdlraALNAFLYRTGEQSNKFMLVLA 129
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 64-175 2.62e-03

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: 37.86  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  64 KRNIKEIYAW-IFVNQKRQEQGLKVGKQALhmmFKGNPGTGKTTVARLVGKlffemnvLSKGHLIEAERGDLVGEYIGHT 142
Cdd:cd19529    2 KQELKEAVEWpLLKPEVFKRLGIRPPKGIL---LYGPPGTGKTLLAKAVAT-------ESNANFISVKGPELLSKWVGES 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 495619429 143 AQKTRDLIKK---SLGGILFIDEAYSLA--RGGEKDFG 175
Cdd:cd19529   72 EKAIREIFRKarqVAPCVIFFDEIDSIAprRGTTGDSG 109
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 59-176 3.18e-03

first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r1-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 37.80  E-value: 3.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  59 GMDEMKRNIKEIYAWIFVN-QKRQEQGLKVGKQALhmmFKGNPGTGKTTVARLV----GKLFFEMN---VLSKghlieae 130
Cdd:cd19519    4 GCRKQLAQIREMVELPLRHpELFKAIGIKPPRGIL---LYGPPGTGKTLIARAVanetGAFFFLINgpeIMSK------- 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495619429 131 rgdlvgeYIGHTAQKTRDLIK---KSLGGILFIDEAYSLARGGEKDFGK 176
Cdd:cd19519   74 -------LAGESESNLRKAFEeaeKNAPAIIFIDEIDAIAPKREKTHGE 115
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 98-169 3.34e-03

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: 37.41  E-value: 3.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495619429  98 GNPGTGKTTVARLVGKLFfEMNVLS-KGhlieaerGDLVGEYIGHTAQKTRDLIKKSLGG---ILFIDEAYSLA--RG 169
Cdd:cd19526   34 GPPGCGKTLLASAIASEC-GLNFISvKG-------PELLNKYIGASEQNVRDLFSRAQSAkpcILFFDEFDSIApkRG 103
ftsH CHL00176
cell division protein; Validated
 59-168 3.68e-03

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 38.88  E-value: 3.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495619429  59 GMDEMKRNIKEIYAWIFVNQKRQEQGLKVGKQALhmmFKGNPGTGKTTVARLVGklfFEMNVlskgHLIEAERGDLVGEY 138
Cdd:CHL00176 187 GIEEAKEEFEEVVSFLKKPERFTAVGAKIPKGVL---LVGPPGTGKTLLAKAIA---GEAEV----PFFSISGSEFVEMF 256

                         90       100       110
                 ....*....|....*....|....*....|...
gi 495619429 139 IGHTAQKTRDLIKKSLGG---ILFIDEAYSLAR 168
Cdd:CHL00176 257 VGVGAARVRDLFKKAKENspcIVFIDEIDAVGR 289
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
98-161 7.94e-03

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 36.72  E-value: 7.94e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495619429  98 GNPGTGKTTVARLVGKL----FFEMN--VLSKGHLIE--AERGDLVGEYightaQKTRDLIKKSLGGILFID 161
Cdd:COG1936    7 GTPGTGKTTVAKLLAERlgleVIHLNdlVKEEGLYTEvdEERDSLVVDE-----DALAEELEELKEGDVIIE 73
 
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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