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Conserved domains on  [gi|77917538|ref|NP_001030094|]
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ATPase family AAA domain-containing protein 3 [Rattus norvegicus]

Protein Classification

DUF3523 domain-containing ATPase family protein( domain architecture ID 15964341)

DUF3523 domain-containing ATPase family protein associated with various cellular activities (AAA), similar to ATPase AAA-domain protein 3 (ATAD3), a ubiquitously expressed mitochondrial protein

Gene Ontology:  GO:0005524|GO:0016887
PubMed:  15037234|18466635|28941010

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 27-285 2.63e-114

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


:

Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 341.19  E-value: 2.63e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    27 GAESGGDRGAGDRPSPKDKWSNFDPTGLERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQ 106
Cdd:pfam12037   1 GGPGSDKDPKKSNDKPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   107 IRVQAEERRKTLNEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAIR-----RATVEREMELRH 181
Cdd:pfam12037  81 QRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   182 KNEMLRVEAEARARAKADRENADIIREQIRLKAAEHRQTILESIRTAGTLFGEGFRAFVTDWDKVTATVAGLTLLAVGVY 261
Cdd:pfam12037 161 ETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVY 240

                         250       260
                  ....*....|....*....|....
gi 77917538   262 SAKNATSVAGRYIEARLGKPSLVR 285
Cdd:pfam12037 241 TAKEGTGVAWRYIEARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 323-472 9.43e-108

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: 319.86  E-value: 9.43e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 323 LEARVRDIAIATRNTKKNKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWASTSR 402
Cdd:cd19512   1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 403 RGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVCF 472
Cdd:cd19512  81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
 
Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 27-285 2.63e-114

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 341.19  E-value: 2.63e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    27 GAESGGDRGAGDRPSPKDKWSNFDPTGLERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQ 106
Cdd:pfam12037   1 GGPGSDKDPKKSNDKPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   107 IRVQAEERRKTLNEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAIR-----RATVEREMELRH 181
Cdd:pfam12037  81 QRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   182 KNEMLRVEAEARARAKADRENADIIREQIRLKAAEHRQTILESIRTAGTLFGEGFRAFVTDWDKVTATVAGLTLLAVGVY 261
Cdd:pfam12037 161 ETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVY 240

                         250       260
                  ....*....|....*....|....
gi 77917538   262 SAKNATSVAGRYIEARLGKPSLVR 285
Cdd:pfam12037 241 TAKEGTGVAWRYIEARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 323-472 9.43e-108

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: 319.86  E-value: 9.43e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 323 LEARVRDIAIATRNTKKNKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWASTSR 402
Cdd:cd19512   1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 403 RGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVCF 472
Cdd:cd19512  81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 166-555 1.25e-26

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: 112.31  E-value: 1.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 166 EAIRRATVEREMELRHKNEMLRVEAEARARAKADRENADIIREQIRLKAAEHRQTiLESIRTAGTLFGEGFRAFVTDWDK 245
Cdd:COG0464   5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLL-LLSGALAALLLLALLLLALLALLA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 246 VTATVAGLTLLAVGVYSAKNATSVAGRYIEARLGKPSLVRETSRISVLEALRHPIQVSRRLVSRPQDALEG----VILSP 321
Cdd:COG0464  84 ALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAilddLGGLE 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 322 SLEARVRDIAIATRNTKKNKSLY-----RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR-EGVTA--MHK 393
Cdd:COG0464 164 EVKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEknLRE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 394 VFDWASTSRRGLLLFvDEADAFLRKRATEKiSEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVCFA 473
Cdd:COG0464 242 VFDKARGLAPCVLFI-DEADALAGKRGEVG-DGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEIIFFP 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 474 LPQREERERLVRMYFDKYvlkpategkqrlkvaQFDYGKKCSEVAQLTAGMSGREIAQLAV-AWQAMAYSSEDGVLTEAM 552
Cdd:COG0464 320 LPDAEERLEIFRIHLRKR---------------PLDEDVDLEELAEATEGLSGADIRNVVRrAALQALRLGREPVTTEDL 384


                ...
gi 77917538 553 MDA 555
Cdd:COG0464 385 LEA 387
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
314-568 2.11e-25

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 105.35  E-value: 2.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 314 LEGVILSPSLEARVRDIAIATRNTKK----NKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---E 386
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENlrkfGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSylgE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 387 GVTAMHKVFDWAstSRRGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRI 466
Cdd:COG1223  79 TARNLRKLFDFA--RRAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALWRRF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 467 DEMVCFALPQREERERLVRMYFDKYVLKPATEGKqrlkvaqfdygkkcsEVAQLTAGMSGREIAQLAVAWQAMAYSSEDG 546
Cdd:COG1223 157 DEVIEFPLPDKEERKEILELNLKKFPLPFELDLK---------------KLAKKLEGLSGADIEKVLKTALKKAILEDRE 221

                       250       260
                ....*....|....*....|..
gi 77917538 547 VLTEAMmdarVQDAVQQHQQKM 568
Cdd:COG1223 222 KVTKED----LEEALKQRKERK 239
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 347-472 6.13e-23

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: 94.58  E-value: 6.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   347 VLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKRATEKIS 425
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 77917538   426 EDLR--ATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVCF 472
Cdd:pfam00004  80 ESRRvvNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEF 128
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
334-532 3.83e-12

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 69.29  E-value: 3.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  334 TRNTKKNKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTAmHKVFDWASTSRRG--LLLFVDE 411
Cdd:PRK10733 175 SRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGA-SRVRDMFEQAKKAapCIIFIDE 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  412 ADAFLRKR-ATEKISEDLR-ATLNAFL-HRTGQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVCFALPQREERERLVR 485
Cdd:PRK10733 253 IDAVGRQRgAGLGGGHDEReQTLNQMLvEMDGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILK 332

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 77917538  486 MYFDKYVLKPATEGkqrlkvaqfdygkkcSEVAQLTAGMSGREIAQL 532
Cdd:PRK10733 333 VHMRRVPLAPDIDA---------------AIIARGTPGFSGADLANL 364
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 345-532 5.61e-09

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: 59.15  E-value: 5.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKRATEK 423
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   424 ISEDLRATLNAFLHRT-GQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVCFALPQREERERLVRMYFDKYVLKPATEg 499
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVD- 645

                         170       180       190
                  ....*....|....*....|....*....|...
gi 77917538   500 kqrlkvaqfdygkkCSEVAQLTAGMSGREIAQL 532
Cdd:TIGR01243 646 --------------LEELAEMTEGYTGADIEAV 664
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 345-459 8.68e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 51.61  E-value: 8.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    345 RNVLMYGPPGTGKTLFAKKLALHSG------------------MDYAIMTGGDVAPMGREGVTAMHKVFDWASTSRRGlL 406
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 77917538    407 LFVDEADAFLRKRAtekiSEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFD 459
Cdd:smart00382  82 LILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
PTZ00121 PTZ00121
MAEBL; Provisional
 55-228 3.65e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    55 ERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRvQAEERRKTLN----EETRQ-HQARA 129
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-KADELKKAEElkkaEEKKKaEEAKK 1571

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   130 QYQDKLARQRYEDQLKQ---------QQLLNEENLRKQEESVQKQEA-IRRATVEREMELRHKNEMLRVEAEARARAKAD 199
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKaeearieevMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651

                         170       180
                  ....*....|....*....|....*....
gi 77917538   200 RENADiirEQIRLKAAEHRQTILESIRTA 228
Cdd:PTZ00121 1652 LKKAE---EENKIKAAEEAKKAEEDKKKA 1677
 
Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 27-285 2.63e-114

ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.


Pssm-ID: 463442 [Multi-domain]  Cd Length: 264  Bit Score: 341.19  E-value: 2.63e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    27 GAESGGDRGAGDRPSPKDKWSNFDPTGLERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQ 106
Cdd:pfam12037   1 GGPGSDKDPKKSNDKPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   107 IRVQAEERRKTLNEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAIR-----RATVEREMELRH 181
Cdd:pfam12037  81 QRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   182 KNEMLRVEAEARARAKADRENADIIREQIRLKAAEHRQTILESIRTAGTLFGEGFRAFVTDWDKVTATVAGLTLLAVGVY 261
Cdd:pfam12037 161 ETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVY 240

                         250       260
                  ....*....|....*....|....
gi 77917538   262 SAKNATSVAGRYIEARLGKPSLVR 285
Cdd:pfam12037 241 TAKEGTGVAWRYIEARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
 323-472 9.43e-108

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: 319.86  E-value: 9.43e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 323 LEARVRDIAIATRNTKKNKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWASTSR 402
Cdd:cd19512   1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 403 RGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVCF 472
Cdd:cd19512  81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 323-470 3.71e-33

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: 124.32  E-value: 3.71e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 323 LEARVRDIAIATRNTKKNKS----LYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKVFDW 397
Cdd:cd19481   1 LKASLREAVEAPRRGSRLRRyglgLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVgESEKNLRKIFER 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 77917538 398 ASTSRRGLLLFvDEADAFLRKRATEKISEDLRATLNAFLHRT--GQHSNKFMLVLASNQPEQFDWAIND--RIDEMV 470
Cdd:cd19481  81 ARRLAPCILFI-DEIDAIGRKRDSSGESGELRRVLNQLLTELdgVNSRSKVLVIAATNRPDLLDPALLRpgRFDEVI 156
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 166-555 1.25e-26

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: 112.31  E-value: 1.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 166 EAIRRATVEREMELRHKNEMLRVEAEARARAKADRENADIIREQIRLKAAEHRQTiLESIRTAGTLFGEGFRAFVTDWDK 245
Cdd:COG0464   5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLL-LLSGALAALLLLALLLLALLALLA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 246 VTATVAGLTLLAVGVYSAKNATSVAGRYIEARLGKPSLVRETSRISVLEALRHPIQVSRRLVSRPQDALEG----VILSP 321
Cdd:COG0464  84 ALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREAilddLGGLE 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 322 SLEARVRDIAIATRNTKKNKSLY-----RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR-EGVTA--MHK 393
Cdd:COG0464 164 EVKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEknLRE 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 394 VFDWASTSRRGLLLFvDEADAFLRKRATEKiSEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVCFA 473
Cdd:COG0464 242 VFDKARGLAPCVLFI-DEADALAGKRGEVG-DGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEIIFFP 319

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 474 LPQREERERLVRMYFDKYvlkpategkqrlkvaQFDYGKKCSEVAQLTAGMSGREIAQLAV-AWQAMAYSSEDGVLTEAM 552
Cdd:COG0464 320 LPDAEERLEIFRIHLRKR---------------PLDEDVDLEELAEATEGLSGADIRNVVRrAALQALRLGREPVTTEDL 384


                ...
gi 77917538 553 MDA 555
Cdd:COG0464 385 LEA 387
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
314-568 2.11e-25

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 105.35  E-value: 2.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 314 LEGVILSPSLEARVRDIAIATRNTKK----NKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---E 386
Cdd:COG1223   1 LDDVVGQEEAKKKLKLIIKELRRRENlrkfGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSylgE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 387 GVTAMHKVFDWAstSRRGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRI 466
Cdd:COG1223  79 TARNLRKLFDFA--RRAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALWRRF 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 467 DEMVCFALPQREERERLVRMYFDKYVLKPATEGKqrlkvaqfdygkkcsEVAQLTAGMSGREIAQLAVAWQAMAYSSEDG 546
Cdd:COG1223 157 DEVIEFPLPDKEERKEILELNLKKFPLPFELDLK---------------KLAKKLEGLSGADIEKVLKTALKKAILEDRE 221

                       250       260
                ....*....|....*....|..
gi 77917538 547 VLTEAMmdarVQDAVQQHQQKM 568
Cdd:COG1223 222 KVTKED----LEEALKQRKERK 239
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 347-472 6.13e-23

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: 94.58  E-value: 6.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   347 VLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKRATEKIS 425
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 77917538   426 EDLR--ATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVCF 472
Cdd:pfam00004  80 ESRRvvNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEF 128
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 347-533 7.87e-20

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 90.84  E-value: 7.87e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 347 VLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKVFDWASTSRRGLLLFvDEADAFLRKRATEKI 424
Cdd:COG1222 115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKyiG-EGARNVREVFELAREKAPSIIFI-DEIDAIAARRTDDGT 192

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 425 SEDLRATLNAFLHRT-GQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVCFALPQREERERLVRMYFdkyvlkpategk 500
Cdd:COG1222 193 SGEVQRTVNQLLAELdGFESRGDVLIIaATNRPDLLDPALlrPGRFDRVIEVPLPDEEAREEILKIHL------------ 260

                       170       180       190
                ....*....|....*....|....*....|....
gi 77917538 501 QRLKVA-QFDYgkkcSEVAQLTAGMSGREIAQLA 533
Cdd:COG1222 261 RDMPLAdDVDL----DKLAKLTEGFSGADLKAIV 290
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
334-532 3.83e-12

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 69.29  E-value: 3.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  334 TRNTKKNKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTAmHKVFDWASTSRRG--LLLFVDE 411
Cdd:PRK10733 175 SRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEM-FVGVGA-SRVRDMFEQAKKAapCIIFIDE 252

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  412 ADAFLRKR-ATEKISEDLR-ATLNAFL-HRTGQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVCFALPQREERERLVR 485
Cdd:PRK10733 253 IDAVGRQRgAGLGGGHDEReQTLNQMLvEMDGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILK 332

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 77917538  486 MYFDKYVLKPATEGkqrlkvaqfdygkkcSEVAQLTAGMSGREIAQL 532
Cdd:PRK10733 333 VHMRRVPLAPDIDA---------------AIIARGTPGFSGADLANL 364
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 345-462 1.82e-10

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: 59.94  E-value: 1.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTAmHKVFDWASTSRRG--LLLFVDEADAFLRKR-AT 421
Cdd:cd19501  38 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGA-SRVRDLFEQAKKNapCIVFIDEIDAVGRKRgAG 115

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 77917538 422 EKISEDLR-ATLNAFL-HRTGQHSNKFMLVL-ASNQPEQFDWAI 462
Cdd:cd19501 116 LGGGHDEReQTLNQLLvEMDGFESNTGVIVIaATNRPDVLDPAL 159
ftsH CHL00176
cell division protein; Validated
 347-533 1.46e-09

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 60.83  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  347 VLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTAMhKVFDWASTSRRG--LLLFVDEADAFLRKRATE-K 423
Cdd:CHL00176 219 VLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM-FVGVGAA-RVRDLFKKAKENspCIVFIDEIDAVGRQRGAGiG 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  424 ISEDLR-ATLNAFL-HRTGQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVCFALPQREERERLVRMYFDKYVLKPATE 498
Cdd:CHL00176 297 GGNDEReQTLNQLLtEMDGFKGNKGVIVIaATNRVDILDAALlrPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVS 376

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 77917538  499 GKQrlkvaqfdygkkcseVAQLTAGMSGREIAQLA 533
Cdd:CHL00176 377 LEL---------------IARRTPGFSGADLANLL 396
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 347-470 2.26e-09

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: 56.73  E-value: 2.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 347 VLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKVFDWASTSRRGLLLFvDEADAFLRKRATEKI 424
Cdd:cd19530  33 VLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKyvG-ESERAVRQVFQRARASAPCVIFF-DEVDALVPKRGDGGS 110

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 77917538 425 SEDLRaTLNAFLHRT--GQHSNKFMLVLASNQPEQFDWAI--NDRIDEMV 470
Cdd:cd19530 111 WASER-VVNQLLTEMdgLEERSNVFVIAATNRPDIIDPAMlrPGRLDKTL 159
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 345-472 2.47e-09

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: 56.53  E-value: 2.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKRAT 421
Cdd:cd19503  35 RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSI--VSKylgESEKNLREIFEEARSHAPS-IIFIDEIDALAPKREE 111

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 77917538 422 --EKISEDLRATLNAFLHRTGQhSNKFMLVLASNQPEQFDWAIN--DRIDEMVCF 472
Cdd:cd19503 112 dqREVERRVVAQLLTLMDGMSS-RGKVVVIAATNRPDAIDPALRrpGRFDREVEI 165
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 340-465 2.55e-09

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: 56.59  E-value: 2.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 340 NKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVA--PMGrEGVTAMHKVFDWAStSRRGLLLFVDEADAFLR 417
Cdd:cd19509  28 LRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVskWVG-ESEKIVRALFALAR-ELQPSIIFIDEIDSLLS 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 77917538 418 KRATEKiSEDLRATLNAFLHR----TGQHSNKFMLVLASNQPEQFDWAINDR 465
Cdd:cd19509 106 ERGSGE-HEASRRVKTEFLVQmdgvLNKPEDRVLVLGATNRPWELDEAFLRR 156
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 344-474 2.73e-09

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: 56.00  E-value: 2.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 344 YRNVLMYGPPGTGKTLFAKKLALHSG--------MDYAIMTGGDVapMGREGVTAMHKVFDWASTSRRGLLLFVDEADAF 415
Cdd:cd00009  19 PKNLLLYGPPGTGKTTLARAIANELFrpgapflyLNASDLLEGLV--VAELFGHFLVRLLFELAEKAKPGVLFIDEIDSL 96

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77917538 416 lrkraTEKISEDLRATLNAFLHRTGQHSNkFMLVLASNQPE--QFDWAINDRIDEMVCFAL 474
Cdd:cd00009  97 -----SRGAQNALLRVLETLNDLRIDREN-VRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 345-470 3.18e-09

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: 56.14  E-value: 3.18e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKRATE 422
Cdd:cd19511  28 KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKyvG-ESERAVREIFQKARQAAPC-IIFFDEIDSLAPRRGQS 105

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 77917538 423 KISEDLRATLNAFLHR-TGQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 470
Cdd:cd19511 106 DSSGVTDRVVSQLLTElDGIESLKGVVVIaATNRPDMIDPALlrPGRLDKLI 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 345-466 4.79e-09

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: 55.89  E-value: 4.79e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKR--- 419
Cdd:cd19520  36 KGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDkwYG-ESQKLVAAVFSLASKLQPS-IIFIDEIDSFLRQRsst 113

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 77917538 420 ---ATEKISEDLRATLNAFlhRTGQHSnKFMLVLASNQPEQFDWAINDRI 466
Cdd:cd19520 114 dheATAMMKAEFMSLWDGL--STDGNC-RVIVMGATNRPQDLDEAILRRM 160
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 345-532 5.61e-09

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: 59.15  E-value: 5.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKRATEK 423
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   424 ISEDLRATLNAFLHRT-GQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVCFALPQREERERLVRMYFDKYVLKPATEg 499
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIHTRSMPLAEDVD- 645

                         170       180       190
                  ....*....|....*....|....*....|...
gi 77917538   500 kqrlkvaqfdygkkCSEVAQLTAGMSGREIAQL 532
Cdd:TIGR01243 646 --------------LEELAEMTEGYTGADIEAV 664
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 345-533 1.06e-08

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: 57.99  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKR-- 419
Cdd:TIGR01243 213 KGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI--MSKyygESEERLREIFKEAEENAPS-IIFIDEIDAIAPKRee 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   420 ATEKISEDLRATLNAFLHRTgQHSNKFMLVLASNQPEQFDWAIN--DRIDEMVCFALPQREERerlvrmyfdKYVLKPAT 497
Cdd:TIGR01243 290 VTGEVEKRVVAQLLTLMDGL-KGRGRVIVIGATNRPDALDPALRrpGRFDREIVIRVPDKRAR---------KEILKVHT 359

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 77917538   498 EGKQRLKVAQFDYgkkcseVAQLTAGMSGREIAQLA 533
Cdd:TIGR01243 360 RNMPLAEDVDLDK------LAEVTHGFVGADLAALA 389
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 344-470 1.35e-08

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: 54.61  E-value: 1.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 344 YRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKVFD----WASTSrrgllLFVDEADAFLRK 418
Cdd:cd19522  33 WKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRgESEKLVRLLFEmarfYAPTT-----IFIDEIDSICSR 107

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 77917538 419 RATEKISEDLRATLNAFLHR--------TGQHSNKFMLVL-ASNQPEQFDWAINDRIDEMV 470
Cdd:cd19522 108 RGTSEEHEASRRVKSELLVQmdgvggasENDDPSKMVMVLaATNFPWDIDEALRRRLEKRI 168
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 337-470 2.01e-08

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: 53.67  E-value: 2.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 337 TKKNKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKVFDWASTSRRgLLLFVDEADA 414
Cdd:cd19528  20 LKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMwfG-ESEANVRDIFDKARAAAP-CVLFFDELDS 97

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77917538 415 FLRKRATeKISEDLRAT---LNAFLHRT-GQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 470
Cdd:cd19528  98 IAKARGG-NIGDAGGAAdrvINQILTEMdGMNTKKNVFIIgATNRPDIIDPAIlrPGRLDQLI 159
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 340-470 4.88e-08

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 52.94  E-value: 4.88e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 340 NKSLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAMHKVFDWASTSRRGlLLFVDEADAFLR 417
Cdd:cd19521  36 NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSkwMG-ESEKLVKQLFAMARENKPS-IIFIDEVDSLCG 113

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 77917538 418 KRAtEKISEDLRATLNAFL---HRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMV 470
Cdd:cd19521 114 TRG-EGESEASRRIKTELLvqmNGVGNDSQGVLVLGATNIPWQLDSAIRRRFEKRI 168
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 345-462 5.03e-08

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: 52.50  E-value: 5.03e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAMHKVFDWASTSRRgLLLFVDEADAFLRKRA-- 420
Cdd:cd19529  28 KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSkwVG-ESEKAIREIFRKARQVAP-CVIFFDEIDSIAPRRGtt 105

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 77917538 421 -----TEKISEDLRATLNAFlhrtgQHSNKFMLVLASNQPEQFDWAI 462
Cdd:cd19529 106 gdsgvTERVVNQLLTELDGL-----EEMNGVVVIAATNRPDIIDPAL 147
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 345-459 8.68e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 51.61  E-value: 8.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    345 RNVLMYGPPGTGKTLFAKKLALHSG------------------MDYAIMTGGDVAPMGREGVTAMHKVFDWASTSRRGlL 406
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 77917538    407 LFVDEADAFLRKRAtekiSEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFD 459
Cdd:smart00382  82 LILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 345-484 9.36e-08

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 54.38  E-value: 9.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKVFDWASTSRRGlLLFVDEADAFLRK----- 418
Cdd:PTZ00454 180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEfVQKYLGEGPRMVRDVFRLARENAPS-IIFIDEVDSIATKrfdaq 258

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77917538  419 ----RATEKISEDLRATLNAFlhrtgQHSNKFMLVLASNQPEQFDWAI--NDRIDEMVCFALPQREEReRLV 484
Cdd:PTZ00454 259 tgadREVQRILLELLNQMDGF-----DQTTNVKVIMATNRADTLDPALlrPGRLDRKIEFPLPDRRQK-RLI 324
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 345-472 9.73e-08

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: 51.95  E-value: 9.73e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKVFDWASTsRRGLLLFVDEADAFLRKRATEK 423
Cdd:cd19502  38 KGVLLYGPPGTGKTLLAKAVANHTDATFIRVVGSElVQKYIGEGARLVRELFEMARE-KAPSIIFIDEIDAIGAKRFDSG 116

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 424 ISED---------LRATLNAFLHRtgqhsNKFMLVLASNQPEQFDWAI--NDRIDEMVCF 472
Cdd:cd19502 117 TGGDrevqrtmleLLNQLDGFDPR-----GNIKVIMATNRPDILDPALlrPGRFDRKIEF 171
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 345-462 1.02e-07

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: 52.05  E-value: 1.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKR--AT 421
Cdd:cd19519  35 RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEImSKLAGESESNLRKAFEEAEKNAPA-IIFIDEIDAIAPKRekTH 113

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 77917538 422 EKISEDLRATLNAFLhrTGQHSNKFMLVL-ASNQPEQFDWAI 462
Cdd:cd19519 114 GEVERRIVSQLLTLM--DGLKQRAHVIVMaATNRPNSIDPAL 153
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 345-466 9.26e-07

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: 49.60  E-value: 9.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAMHKVFDWASTSRRGlLLFVDEADAFLRKRAtEK 423
Cdd:cd19525  56 KGILLFGPPGTGKTLIGKCIASQSGATfFSISASSLTSKWVGEGEKMVRALFSVARCKQPA-VIFIDEIDSLLSQRG-EG 133

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 77917538 424 ISEDLRATLNAFLHR----TGQHSNKFMLVLASNQPEQFDWAINDRI 466
Cdd:cd19525 134 EHESSRRIKTEFLVQldgaTTSSEDRILVVGATNRPQEIDEAARRRL 180
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 347-534 1.39e-06

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 50.99  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  347 VLMYGPPGTGKTLFAKKLALHSGMDYAIMTG--------GDVAPMGREgvtamhkVFDWAStSRRGLLLFVDEADAFLRK 418
Cdd:PRK03992 168 VLLYGPPGTGKTLLAKAVAHETNATFIRVVGselvqkfiGEGARLVRE-------LFELAR-EKAPSIIFIDEIDAIAAK 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  419 RATEKISEDlratlnAFLHRTgqhsnkFMLVL----------------ASNQPEQFDWAI--NDRIDEMVCFALPQREER 480
Cdd:PRK03992 240 RTDSGTSGD------REVQRT------LMQLLaemdgfdprgnvkiiaATNRIDILDPAIlrPGRFDRIIEVPLPDEEGR 307

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 77917538  481 ERLVRMYFDKYVLKPATegkqrlkvaqfDYgkkcSEVAQLTAGMSGREIAQLAV 534
Cdd:PRK03992 308 LEILKIHTRKMNLADDV-----------DL----EELAELTEGASGADLKAICT 346
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 347-470 2.07e-06

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: 47.89  E-value: 2.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 347 VLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAMHKVFDWASTSRRGLLLFvDEADAFLRKRAT---- 421
Cdd:cd19527  29 ILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYiGESEANVREVFQKARDAKPCVIFF-DELDSLAPSRGNsgds 107

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 77917538 422 ----EKISEDLRATLNAfLHRTGQhsnKFMLVLASNQPEQFDWAI--NDRIDEMV 470
Cdd:cd19527 108 ggvmDRVVSQLLAELDG-MSSSGQ---DVFVIGATNRPDLLDPALlrPGRFDKLL 158
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 342-465 3.42e-06

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: 47.57  E-value: 3.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 342 SLYRNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTG-GDVAPMGREGVTAMHKVFdWASTSRRGLLLFVDEADAFLRKRA 420
Cdd:cd19523  31 RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGsTLVAKWAGEGEKILQASF-LAARCRQPSVLFISDLDALLSSQD 109

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 77917538 421 TE-----KISEDLRATLNAFLhrtGQHSNKFMLVLASNQPEQFDWAINDR 465
Cdd:cd19523 110 DEaspvgRLQVELLAQLDGVL---GSGEDGVLVVCTTSKPEEIDESLRRY 156
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 345-470 5.36e-06

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: 46.77  E-value: 5.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMDY-----AIMTGGDVAPmGREGVTAMHKVfdwaSTSRRGLLLFVDEADAFLRKR 419
Cdd:cd19524  34 RGLLLFGPPGNGKTMLAKAVAAESNATFfnisaASLTSKYVGE-GEKLVRALFAV----ARELQPSIIFIDEVDSLLSER 108

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 77917538 420 ATEKISEDLRATLNAFLHRTGQHSNKFMLVL---ASNQPEQFDWAINDRIDEMV 470
Cdd:cd19524 109 SEGEHEASRRLKTEFLIEFDGVQSNGDDRVLvmgATNRPQELDDAVLRRFTKRV 162
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 345-471 7.64e-06

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: 46.63  E-value: 7.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAMHKVFDWAsTSRRGLLLFVDEADAFLRKRatEK 423
Cdd:cd19518  35 RGVLLHGPPGCGKTMLANAIAGELKVPfLKISATEIVSGVSGESEEKIRELFDQA-ISNAPCIVFIDEIDAITPKR--ES 111

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 77917538 424 ISEDL-RATLNAFLHRTGQHSN-----KFMLVL-ASNQPEQFDWAIN--DRIDEMVC 471
Cdd:cd19518 112 AQREMeRRIVSQLLTCMDELNNektagGPVLVIgATNRPDSLDPALRraGRFDREIC 168
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 345-462 1.58e-05

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: 45.58  E-value: 1.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLALHSGMDyaimtGGDVAPMGREGVTAMHKvfdWASTSRRGL-------------LLFVDE 411
Cdd:cd19517  35 RGVLFHGPPGTGKTLMARALAAECSKG-----GQKVSFFMRKGADCLSK---WVGEAERQLrllfeeayrmqpsIIFFDE 106

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 77917538 412 AD--AFLRKRATEKISEDLRATLNAF---LHRTGQhsnkFMLVLASNQPEQFDWAI 462
Cdd:cd19517 107 IDglAPVRSSKQEQIHASIVSTLLALmdgLDNRGQ----VVVIGATNRPDALDPAL 158
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 345-493 1.92e-05

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 47.46  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  345 RNVLMYGPPGTGKTLFAKKLALHSGMDYAIMTG--------GDVAPMGREgvtaMHKVFDWASTSrrglLLFVDEADAFL 416
Cdd:PTZ00361 218 KGVILYGPPGTGKTLLAKAVANETSATFLRVVGseliqkylGDGPKLVRE----LFRVAEENAPS----IVFIDEIDAIG 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  417 RKR--ATEKISEDLRATLNAFLHRTG--QHSNKFMLVLASNQPEQFDWAI--NDRIDEMVCFALPQREERERLVRMYFDK 490
Cdd:PTZ00361 290 TKRydATSGGEKEIQRTMLELLNQLDgfDSRGDVKVIMATNRIESLDPALirPGRIDRKIEFPNPDEKTKRRIFEIHTSK 369


                 ...
gi 77917538  491 YVL 493
Cdd:PTZ00361 370 MTL 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-337 2.04e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  55 ERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRVQAEERRKTLNEETRQHQARAQYQDK 134
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 135 LA--------RQRYEDQLKQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRVEAEARARAKADRENADII 206
Cdd:COG1196 389 LEalraaaelAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 207 REQIRLKAAEH------------RQTILESIRTAGTLFGEGFRAF---------------VTDWDKVTATVAGLTLLAVG 259
Cdd:COG1196 469 LEEAALLEAALaelleelaeaaaRLLLLLEAEADYEGFLEGVKAAlllaglrglagavavLIGVEAAYEAALEAALAAAL 548

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 260 VYSAKNATSVAGRYIE----ARLGK----PSLVRETSRISVLEALRHPIQVSRRLVSRPQDALEGVILSPSLEARVRDIA 331
Cdd:COG1196 549 QNIVVEDDEVAAAAIEylkaAKAGRatflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLV 628


                ....*.
gi 77917538 332 IATRNT 337
Cdd:COG1196 629 AARLEA 634
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-224 3.50e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  55 ERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKsEQIRVQAEERRKTLNEETRQHQARAQYQDK 134
Cdd:COG1196 253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-QDIARLEERRRELEERLEELEEELAELEEE 331

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 135 LARQRYEDQLKQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRVEAEARARAKADRENADIIREQIRLKA 214
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411

                       170
                ....*....|
gi 77917538 215 AEHRQTILES 224
Cdd:COG1196 412 LLERLERLEE 421
PTZ00121 PTZ00121
MAEBL; Provisional
 55-228 3.65e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.06  E-value: 3.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    55 ERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRvQAEERRKTLN----EETRQ-HQARA 129
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-KADELKKAEElkkaEEKKKaEEAKK 1571

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   130 QYQDKLARQRYEDQLKQ---------QQLLNEENLRKQEESVQKQEA-IRRATVEREMELRHKNEMLRVEAEARARAKAD 199
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKaeearieevMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEE 1651

                         170       180
                  ....*....|....*....|....*....
gi 77917538   200 RENADiirEQIRLKAAEHRQTILESIRTA 228
Cdd:PTZ00121 1652 LKKAE---EENKIKAAEEAKKAEEDKKKA 1677
PTZ00121 PTZ00121
MAEBL; Provisional
 56-219 4.55e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    56 RAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQ---LKSEQIRVQAEERRKTlnEETRQHQARAQYQ 132
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkMKAEEAKKAEEAKIKA--EELKKAEEEKKKV 1635

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   133 DKLARQRYEDQLKQQQLLNEENL---------RKQEESVQKQEAIRRATVE---------REMELRHKNEMLRVEAEARA 194
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEEEnkikaaeeaKKAEEDKKKAEEAKKAEEDekkaaealkKEAEEAKKAEELKKKEAEEK 1715

                         170       180
                  ....*....|....*....|....*....
gi 77917538   195 RAKADRENADIIR----EQIRLKAAEHRQ 219
Cdd:PTZ00121 1716 KKAEELKKAEEENkikaEEAKKEAEEDKK 1744
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 339-416 1.11e-04

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 45.05  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 339 KNKSLYR--------NVLMYGPPGTGKTLFAKKLALHSGMDY----AIMTggdvapmgreGVTAMHKVFDWASTSR---R 403
Cdd:COG2256  36 PGKPLRRaieagrlsSMILWGPPGTGKTTLARLIANATDAEFvalsAVTS----------GVKDIREVIEEARERRaygR 105

                        90       100
                ....*....|....*....|.
gi 77917538 404 GLLLFVDE--------ADAFL 416
Cdd:COG2256 106 RTILFVDEihrfnkaqQDALL 126
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 346-453 1.45e-04

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: 43.29  E-value: 1.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   346 NVLMYGPPGTGKTLFAKKL-----------ALHSGMDYAIM-TGGDVAPMGREGVTAMHKvfdwaSTSRRGLL------- 406
Cdd:pfam01078  24 NLLMIGPPGSGKTMLAKRLpgilpplteaeALEVTAIHSVAgLGGDGGLIRRRPFRAPHH-----SASAAALVgggsipr 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77917538   407 -----------LFVDEADAFLRkrateKISEDLRATLNAF---LHRTGQHSN---KFMLVLASN 453
Cdd:pfam01078  99 pgeislahngvLFLDELPEFKR-----RVLESLRQPLEDGeitISRARAKVTfpaRFQLVAAMN 157
PTZ00121 PTZ00121
MAEBL; Provisional
 55-219 1.68e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    55 ERAAKAARELEHSRHAKEALNLAQmqeqTLQLEQQSKLKEYEAaveQLKSEQIRVQAEERRKTLNEETRQHQARAQYQDK 134
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAE----EAKKADEAKKKAEEA---KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   135 LARQRYEDQLKQ-------QQLLNEENLRKQEEsVQKQEAIRRATVEREMELR-----HKNEMLRVEAEARARAKADREN 202
Cdd:PTZ00121 1530 AEEAKKADEAKKaeekkkaDELKKAEELKKAEE-KKKAEEAKKAEEDKNMALRkaeeaKKAEEARIEEVMKLYEEEKKMK 1608

                         170
                  ....*....|....*....
gi 77917538   203 ADIIR--EQIRLKAAEHRQ 219
Cdd:PTZ00121 1609 AEEAKkaEEAKIKAEELKK 1627
PTZ00121 PTZ00121
MAEBL; Provisional
 56-219 1.89e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    56 RAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVE-QLKSEQIRVQAEERRKTLNEETRQHQARAQYQDK 134
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   135 L----ARQRYEDQLKQQQLLNE-ENLRKQEESVQKQEAIRRATveremELRHKNEMLRVEAEARARAKADRENADIIR-- 207
Cdd:PTZ00121 1431 KkadeAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKAD-----EAKKKAEEAKKADEAKKKAEEAKKKADEAKka 1505

                         170
                  ....*....|..
gi 77917538   208 EQIRLKAAEHRQ 219
Cdd:PTZ00121 1506 AEAKKKADEAKK 1517
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 339-416 2.54e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 43.53  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  339 KNKSLYR--------NVLMYGPPGTGKTLFAKKLALHSGMDY----AIMTggdvapmgreGVTAMHKVFDWASTSR---R 403
Cdd:PRK13342  23 PGKPLRRmieagrlsSMILWGPPGTGKTTLARIIAGATDAPFealsAVTS----------GVKDLREVIEEARQRRsagR 92

                         90       100
                 ....*....|....*....|.
gi 77917538  404 GLLLFVDE--------ADAFL 416
Cdd:PRK13342  93 RTILFIDEihrfnkaqQDALL 113
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
347-365 3.38e-04

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 43.49  E-value: 3.38e-04
                        10
                ....*....|....*....
gi 77917538 347 VLMYGPPGTGKTLFAKKLA 365
Cdd:COG0465 178 VLLVGPPGTGKTLLAKAVA 196
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 346-419 4.30e-04

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: 41.26  E-value: 4.30e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 77917538 346 NVLMYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP----MGREGVtamHKVFDWAStSRRGLLLFVDEADAFLRKR 419
Cdd:cd19526  29 GILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNkyigASEQNV---RDLFSRAQ-SAKPCILFFDEFDSIAPKR 102
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 346-413 4.66e-04

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: 40.74  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   346 NVLMYGPPGTGKTLFAKKLA------------LHSGMDYAIMTGG-DVAPMGREG-----VTAMhkvfdwastsRRGLLL 407
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaalsnrpvfyvqLTRDTTEEDLFGRrNIDPGGASWvdgplVRAA----------REGEIA 70


                  ....*.
gi 77917538   408 FVDEAD 413
Cdd:pfam07728  71 VLDEIN 76
PTZ00121 PTZ00121
MAEBL; Provisional
 56-184 4.94e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 4.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    56 RAAKAARELEHSRHAKEAlnlaqmqeqtlqleqqSKLKEYEAAVEQLKSEQIRVQAEERRKT----LNEETRQ------- 124
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEA----------------RKAEDAKKAEAVKKAEEAKKDAEEAKKAeeerNNEEIRKfeearma 1263

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 77917538   125 HQARAQYQDKLARQRYEDQLKQ-QQLLNEENLRKQEESVQKQEAIRRATVEREM-ELRHKNE 184
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKaEEKKKADEAKKAEEKKKADEAKKKAEEAKKAdEAKKKAE 1325
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-228 5.27e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 5.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  56 RAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSE--QIRVQAEERRKTLNEETRQhQARAQYQD 133
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEleELELELEEAQAEEYELLAE-LARLEQDI 304

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 134 KLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAIRRATVEREMELrhknEMLRVEAEARARAKADRENADIIREQIRLK 213
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE----EELEEAEAELAEAEEALLEAEAELAEAEEE 380

                       170
                ....*....|....*
gi 77917538 214 AAEHRQTILESIRTA 228
Cdd:COG1196 381 LEELAEELLEALRAA 395
PRK10927 PRK10927
cell division protein FtsN;
100-177 5.37e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 42.36  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538  100 EQLKSEQ----IRVQAEERRK--TLNEETRQHQARAQYQDKLARQRYEDQLKQQQLLN------EENLRKQEESVQKQEA 167
Cdd:PRK10927 112 EQLTPEQrqllEQMQADMRQQptQLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAqqsrttEQSWQQQTRTSQAAPV 191

                         90
                 ....*....|
gi 77917538  168 IRRATVEREM 177
Cdd:PRK10927 192 QAQPRQSKPA 201
PTZ00121 PTZ00121
MAEBL; Provisional
 28-228 1.04e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    28 AESGGDRGagDRPSPKD-----KWSNFDPTGLERAAKAARE--------LEHSRHAKEALNLAQMQEQTLQLEQQSKLKE 94
Cdd:PTZ00121 1064 AHVGQDEG--LKPSYKDfdfdaKEDNRADEATEEAFGKAEEakktetgkAEEARKAEEAKKKAEDARKAEEARKAEDARK 1141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    95 YEAA--VEQLKSEQIRVQAEERRKTlnEETRqhqaRAQYQDKL-ARQRYEDQLKQQQLLNEENLRKQE-----ESVQKQE 166
Cdd:PTZ00121 1142 AEEArkAEDAKRVEIARKAEDARKA--EEAR----KAEDAKKAeAARKAEEVRKAEELRKAEDARKAEaarkaEEERKAE 1215

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 77917538   167 AIRRATVEREMELRHKNEMLR-----------VEAEARARAKADRENADIIREQIRLKAAEHRQTilESIRTA 228
Cdd:PTZ00121 1216 EARKAEDAKKAEAVKKAEEAKkdaeeakkaeeERNNEEIRKFEEARMAHFARRQAAIKAEEARKA--DELKKA 1286
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 93-182 1.40e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 41.12  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    93 KEYEAAVEQLKSEQIRVQAEErrktLNEETRQHQARAQYQDKlarqRYEDQLKQ--------QQLLNEENLRKQEESVQK 164
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQEL----LREKQKEEEQMMEAQER----SYQEHVKQliekmeaeREQLLAEQERMLEHKLQE 273

                          90
                  ....*....|....*...
gi 77917538   165 QEAIRRATVEREMELRHK 182
Cdd:pfam02841 274 QEELLKEGFKTEAESLQK 291
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 345-365 2.24e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.91  E-value: 2.24e-03
                        10        20
                ....*....|....*....|.
gi 77917538 345 RNVLMYGPPGTGKTLFAKKLA 365
Cdd:COG1401 222 KNVILAGPPGTGKTYLARRLA 242
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 61-187 3.67e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.49  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    61 ARELEHSRhaKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRvqaEERRKTLN---EETRQHQARAQYQDKLAR 137
Cdd:pfam17380 445 AREMERVR--LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEkelEERKQAMIEEERKRKLLE 519

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   138 QRYEDQLK-----QQQLLNEENLRKQ---EESVQKQEAIRRATVEREM--ELRHKNEMLR 187
Cdd:pfam17380 520 KEMEERQKaiyeeERRREAEEERRKQqemEERRRIQEQMRKATEERSRleAMEREREMMR 579
PTZ00121 PTZ00121
MAEBL; Provisional
 55-226 3.94e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    55 ERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEA---------AVEQLKSEQIRVQAEERRKTlnEETRQH 125
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkadeakkkAEEAKKAEEAKKKAEEAKKA--DEAKKK 1478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   126 QARAQYQDKLARQRYEDQLKQQQLLNE-------ENLRKQEESvQKQEAIRRATVEREMELRHKNEMLRveaeararaka 198
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKKAaeakkkaDEAKKAEEA-KKADEAKKAEEAKKADEAKKAEEKK----------- 1546

                         170       180
                  ....*....|....*....|....*...
gi 77917538   199 dreNADIIREQIRLKAAEHRQTILESIR 226
Cdd:PTZ00121 1547 ---KADELKKAEELKKAEEKKKAEEAKK 1571
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 346-364 4.18e-03

Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 40.02  E-value: 4.18e-03
                        10
                ....*....|....*....
gi 77917538 346 NVLMYGPPGTGKTLFAKKL 364
Cdd:COG0606 213 NLLMIGPPGSGKTMLARRL 231
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 54-228 4.97e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.55  E-value: 4.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    54 LERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRVQAEERRKTLNEETRQHQARAQyQD 133
Cdd:pfam15709 348 LEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQ-QE 426

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   134 KLARQRYEDQLKQQQllneENLRKQEESVQKQeairratveREMELRHKNEMLRVEAEARARAKADRENADIIREQIRLK 213
Cdd:pfam15709 427 EFRRKLQELQRKKQQ----EEAERAEAEKQRQ---------KELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLE 493

                         170
                  ....*....|....*
gi 77917538   214 AAEHRQTILESIRTA 228
Cdd:pfam15709 494 AEERRQKEEEAARLA 508
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 341-365 5.34e-03

ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 39.65  E-value: 5.34e-03
                        10        20
                ....*....|....*....|....*
gi 77917538 341 KSlyrNVLMYGPPGTGKTLFAKKLA 365
Cdd:COG1219 109 KS---NILLIGPTGSGKTLLAQTLA 130
PTZ00121 PTZ00121
MAEBL; Provisional
 56-185 6.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    56 RAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKlkeyeaAVEQLKSEQIRVQAEERRKTLNEETRQHQARAQYQDKL 135
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 77917538   136 ARQRYEDQLKQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEM 185
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEEL 1785
Zot COG4128
Zona occludens toxin, predicted ATPase [General function prediction only];
347-467 6.49e-03

Zona occludens toxin, predicted ATPase [General function prediction only];


Pssm-ID: 443304 [Multi-domain]  Cd Length: 276  Bit Score: 38.93  E-value: 6.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538 347 VLMYGPPGTGKTLFA----KKLALHSG-------------------MDYAIMTGGDVAPMGREGVTAMHKVFDWASTSRR 403
Cdd:COG4128   4 TLITGVPGSGKSYEAvwflIIPALKKGrrvitnipglkileriaehLGLAVPDTAELINVDTDDPDGLEKMARWFHWAPD 83

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 77917538 404 GLLLFVDEADAFLRKRATEKISEDLRATLNafLHRtgqHSNkFMLVLASNQPEQFDWAINDRID 467
Cdd:COG4128  84 GALIVIDEAQRVWPPRGKGSKPPDVVQAFA--THR---HHG-WDIVLITQNISLIHSFIRALIE 141
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 345-364 6.65e-03

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: 37.85  E-value: 6.65e-03
                        10        20
                ....*....|....*....|
gi 77917538 345 RNVLMYGPPGTGKTLFAKKL 364
Cdd:cd19504  36 KGILLYGPPGTGKTLMARQI 55
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 347-365 6.73e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 36.43  E-value: 6.73e-03
                          10
                  ....*....|....*....
gi 77917538   347 VLMYGPPGTGKTLFAKKLA 365
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLA 19
PTZ00121 PTZ00121
MAEBL; Provisional
 55-226 7.03e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538    55 ERAAKAARELEHSRHAKEALNLAQMQEQTLQLEQQSKLKEYEaavEQLKSEQIRVQAEERRKTlNEETRQHQARAQYQDK 134
Cdd:PTZ00121 1631 EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEE---DKKKAEEAKKAEEDEKKA-AEALKKEAEEAKKAEE 1706

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   135 LARQRYEDQLKQQQLLNEENLR--KQEESVQKQEAIRRATVEREMELRHKNEMLRVEAEARARAKADRENAD-IIREQIR 211
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEaVIEEELD 1786

                         170
                  ....*....|....*
gi 77917538   212 LKAAEHRQTILESIR 226
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIK 1801
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
341-365 8.73e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 38.60  E-value: 8.73e-03
                         10        20
                 ....*....|....*....|....*
gi 77917538  341 KSlyrNVLMYGPPGTGKTLFAKKLA 365
Cdd:PRK05342 108 KS---NILLIGPTGSGKTLLAQTLA 129
ATPase pfam06745
KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and ...
 344-430 9.16e-03

KaiC; This family is in the P-loop NTPase superfamily and is found in archaea, bacteria and eukaryotes. More than one copy is sometimes found in each protein. This family includes KaiC, which is one of the Kai proteins among which direct protein-protein association may be a critical process in the generation of circadian rhythms in cyanobacteria.


Pssm-ID: 429095 [Multi-domain]  Cd Length: 231  Bit Score: 38.00  E-value: 9.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 77917538   344 YRNVLMYGPPGTGKTLFAKKLALHSGMDY---AIMTGGDVAPMG-REGVTAMHkvFDWASTSRRGLLLFVDeADAFLRKR 419
Cdd:pfam06745  19 GRVVLITGGPGTGKTIFGLQFLYNGALKYgepGVFVTLEEPPEDlRENARSFG--WDLEKLEEEGKLAIID-ASTSGIGI 95

                          90
                  ....*....|.
gi 77917538   420 ATEKISEDLRA 430
Cdd:pfam06745  96 AEVEDRFDLEE 106
 
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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