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Conserved domains on  [gi|530360439|ref|XP_005244863|]
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ATPase family AAA domain-containing protein 3B isoform X1 [Homo sapiens]

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

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 ...
42-286 1.38e-117

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: 349.28  E-value: 1.38e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   42 APKDKWSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTLSE 121
Cdd:pfam12037  15 KPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  122 ETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR-----RATVEREMELRHKNEMLRVETEARAR 196
Cdd:pfam12037  95 ETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEAR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  197 AKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIE 276
Cdd:pfam12037 175 AKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYIE 254
                         250
                  ....*....|
gi 530360439  277 ARLGKPSLVR 286
Cdd:pfam12037 255 ARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
324-473 8.27e-105

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: 312.15  E-value: 8.27e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 324 LEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSR 403
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 404 RGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHF 473
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 ...
42-286 1.38e-117

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: 349.28  E-value: 1.38e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   42 APKDKWSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTLSE 121
Cdd:pfam12037  15 KPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  122 ETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR-----RATVEREMELRHKNEMLRVETEARAR 196
Cdd:pfam12037  95 ETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEAR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  197 AKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIE 276
Cdd:pfam12037 175 AKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYIE 254
                         250
                  ....*....|
gi 530360439  277 ARLGKPSLVR 286
Cdd:pfam12037 255 ARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
324-473 8.27e-105

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: 312.15  E-value: 8.27e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 324 LEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSR 403
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 404 RGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHF 473
Cdd:cd19512   81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
160-536 4.77e-32

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: 128.10  E-value: 4.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 160 EESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRA 239
Cdd:COG0464    2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 240 FVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQdVLEGVV 319
Cdd:COG0464   82 LAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA-ILDDLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 320 LSPSLEARVRDIAIATRNTKKNRGLY-----RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR-EGVTA-- 391
Cdd:COG0464  161 GLEEVKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEkn 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 392 MHKLFDWANTSRRGLLLFmDEADAFLRKRaTEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMV 471
Cdd:COG0464  239 LREVFDKARGLAPCVLFI-DEADALAGKR-GEVGDGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEII 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530360439 472 HFDLPQQEERERLVRLHFdncvlkpategKRRLKLAQFDYgrkcSEVARLTEGMSGREIAQLAVS 536
Cdd:COG0464  317 FFPLPDAEERLEIFRIHL-----------RKRPLDEDVDL----EELAEATEGLSGADIRNVVRR 366
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
315-570 8.00e-29

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 114.98  E-value: 8.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 315 LEGVVLSPSLEARVRDIAIATRNTKKNR--GLY--RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---E 387
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRkfGLWppRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSylgE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 388 GVTAMHKLFDWANtsRRGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRI 467
Cdd:COG1223   79 TARNLRKLFDFAR--RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALWRRF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 468 DVMVHFDLPQQEERERLVrlhfdncvlkpategKRRLKLAQFDYGRKCSEVARLTEGMSGREIAQLAVSWQATAYASEDG 547
Cdd:COG1223  157 DEVIEFPLPDKEERKEIL---------------ELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDRE 221
                        250       260
                 ....*....|....*....|...
gi 530360439 548 VLTEAMmdtrVQDAVQQHQQMMR 570
Cdd:COG1223  222 KVTKED----LEEALKQRKERKK 240
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
348-475 6.89e-24

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: 97.28  E-value: 6.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEEIS 426
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530360439  427 KDLRaTLNAFLYHM---GQHSNKFMLVLASNLPEQFDCAINSRIDVMVHFDL 475
Cdd:pfam00004  80 ESRR-VVNQLLTELdgfTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
346-577 6.27e-13

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: 71.86  E-value: 6.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  346 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEE 424
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  425 ISKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHfdncvlkpateg 500
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIH------------ 634
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  501 KRRLKLAQfdyGRKCSEVARLTEGMSG-------REIAQLAVSWQATAYASEDgvlTEAMMDTRVQDAVQQHQQMMRWLK 573
Cdd:TIGR01243 635 TRSMPLAE---DVDLEELAEMTEGYTGadieavcREAAMAALRESIGSPAKEK---LEVGEEEFLKDLKVEMRHFLEALK 708

                  ....
gi 530360439  574 RGRP 577
Cdd:TIGR01243 709 KVKP 712
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
348-533 2.22e-12

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 69.68  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAMHKLFDWANTSRRgLLLFMDEADAFLRKR-ATEEI 425
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDEIDAVGRQRgAGLGG 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 426 SKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHFdncvlkpateg 500
Cdd:PRK10733 267 GHDEReQTLNQMLVEMdGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILKVHM----------- 335
                        170       180       190
                 ....*....|....*....|....*....|...
gi 530360439 501 kRRLKLaqfDYGRKCSEVARLTEGMSGREIAQL 533
Cdd:PRK10733 336 -RRVPL---APDIDAAIIARGTPGFSGADLANL 364
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
346-460 3.10e-09

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: 55.84  E-value: 3.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   346 RHILLYGPPGTGKTLFAKKLALHSG------------------MDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGlL 407
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530360439   408 LFMDEADAFLRKrateEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFD 460
Cdd:smart00382  82 LILDEITSLLDA----EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
PTZ00121 PTZ00121
MAEBL; Provisional
57-227 2.37e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   57 RAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQ---LKSEQIRAQAEERRKtlSEETRQHQARAQYQ 133
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkMKAEEAKKAEEAKIK--AEELKKAEEEKKKV 1635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  134 DKLARQRYEDQLKQQQLLNEE---NLRKQEESVQKQEAMRRATVER--EMELRHKNEML-RVETEARARAKAERENADII 207
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEeenKIKAAEEAKKAEEDKKKAEEAKkaEEDEKKAAEALkKEAEEAKKAEELKKKEAEEK 1715
                         170       180
                  ....*....|....*....|..
gi 530360439  208 R--EQIRlKASEHRQTVLESIR 227
Cdd:PTZ00121 1716 KkaEELK-KAEEENKIKAEEAK 1736
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
55-229 9.30e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 9.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439    55 LERAAKAA----------RELEHSRYA---------KEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEER 115
Cdd:TIGR02168  205 LERQAEKAerykelkaelRELELALLVlrleelreeLEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   116 RKT------------LSEETRQHQARAQY--QDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELR 181
Cdd:TIGR02168  285 ELQkelyalaneisrLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360439   182 HKNEMLR---------VETEARARAKAERE----NADIIREQIRLKASEHRQTVLESIRTA 229
Cdd:TIGR02168  365 AELEELEsrleeleeqLETLRSKVAQLELQiaslNNEIERLEARLERLEDRRERLQQEIEE 425
 
Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
42-286 1.38e-117

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: 349.28  E-value: 1.38e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   42 APKDKWSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTLSE 121
Cdd:pfam12037  15 KPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  122 ETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR-----RATVEREMELRHKNEMLRVETEARAR 196
Cdd:pfam12037  95 ETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEAR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  197 AKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIE 276
Cdd:pfam12037 175 AKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYIE 254
                         250
                  ....*....|
gi 530360439  277 ARLGKPSLVR 286
Cdd:pfam12037 255 ARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
324-473 8.27e-105

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: 312.15  E-value: 8.27e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 324 LEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSR 403
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 404 RGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHF 473
Cdd:cd19512   81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
324-473 3.45e-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: 3.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 324 LEARVRDIAIATRNTKKNR----GLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDW 398
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRryglGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVgESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530360439 399 ANTSRRGLLLFmDEADAFLRKRATEEISKDLRATLNAFLYHM--GQHSNKFMLVLASNLPEQFDCAINS--RIDVMVHF 473
Cdd:cd19481   81 ARRLAPCILFI-DEIDAIGRKRDSSGESGELRRVLNQLLTELdgVNSRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
160-536 4.77e-32

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: 128.10  E-value: 4.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 160 EESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRA 239
Cdd:COG0464    2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 240 FVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQdVLEGVV 319
Cdd:COG0464   82 LAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA-ILDDLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 320 LSPSLEARVRDIAIATRNTKKNRGLY-----RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR-EGVTA-- 391
Cdd:COG0464  161 GLEEVKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEkn 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 392 MHKLFDWANTSRRGLLLFmDEADAFLRKRaTEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMV 471
Cdd:COG0464  239 LREVFDKARGLAPCVLFI-DEADALAGKR-GEVGDGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEII 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530360439 472 HFDLPQQEERERLVRLHFdncvlkpategKRRLKLAQFDYgrkcSEVARLTEGMSGREIAQLAVS 536
Cdd:COG0464  317 FFPLPDAEERLEIFRIHL-----------RKRPLDEDVDL----EELAEATEGLSGADIRNVVRR 366
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
315-570 8.00e-29

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 114.98  E-value: 8.00e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 315 LEGVVLSPSLEARVRDIAIATRNTKKNR--GLY--RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---E 387
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRkfGLWppRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSylgE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 388 GVTAMHKLFDWANtsRRGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRI 467
Cdd:COG1223   79 TARNLRKLFDFAR--RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALWRRF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 468 DVMVHFDLPQQEERERLVrlhfdncvlkpategKRRLKLAQFDYGRKCSEVARLTEGMSGREIAQLAVSWQATAYASEDG 547
Cdd:COG1223  157 DEVIEFPLPDKEERKEIL---------------ELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDRE 221
                        250       260
                 ....*....|....*....|...
gi 530360439 548 VLTEAMmdtrVQDAVQQHQQMMR 570
Cdd:COG1223  222 KVTKED----LEEALKQRKERKK 240
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
348-475 6.89e-24

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: 97.28  E-value: 6.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEEIS 426
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530360439  427 KDLRaTLNAFLYHM---GQHSNKFMLVLASNLPEQFDCAINSRIDVMVHFDL 475
Cdd:pfam00004  80 ESRR-VVNQLLTELdgfTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
340-565 7.79e-24

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 102.39  E-value: 7.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 340 KNRGLYRH--------ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRGLLLF 409
Cdd:COG1222   99 KNPELFRKygieppkgVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKyiG-EGARNVREVFELAREKAPSIIFI 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 410 mDEADAFLRKRATEEISKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLV 485
Cdd:COG1222  178 -DEIDAIAARRTDDGTSGEVQRTVNQLLAELdGFESRGDVLIIaATNRPDLLDPALlrPGRFDRVIEVPLPDEEAREEIL 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 486 RLHFdncvlkpategkRRLKLA-QFDYgrkcSEVARLTEGMSGREIAQLAVswQATAYASEDGVLTEAMMDtrVQDAVQQ 564
Cdd:COG1222  257 KIHL------------RDMPLAdDVDL----DKLAKLTEGFSGADLKAIVT--EAGMFAIREGRDTVTMED--LEKAIEK 316

                 .
gi 530360439 565 H 565
Cdd:COG1222  317 V 317
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
346-577 6.27e-13

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: 71.86  E-value: 6.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  346 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEE 424
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  425 ISKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHfdncvlkpateg 500
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIH------------ 634
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  501 KRRLKLAQfdyGRKCSEVARLTEGMSG-------REIAQLAVSWQATAYASEDgvlTEAMMDTRVQDAVQQHQQMMRWLK 573
Cdd:TIGR01243 635 TRSMPLAE---DVDLEELAEMTEGYTGadieavcREAAMAALRESIGSPAKEK---LEVGEEEFLKDLKVEMRHFLEALK 708

                  ....
gi 530360439  574 RGRP 577
Cdd:TIGR01243 709 KVKP 712
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
341-466 2.15e-12

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: 65.45  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 341 NRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVA--PMGrEGVTAMHKLFDWANtSRRGLLLFMDEADAFLR 418
Cdd:cd19509   28 LRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVskWVG-ESEKIVRALFALAR-ELQPSIIFIDEIDSLLS 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530360439 419 KRATEEISKDLRATlNAFLYHM----GQHSNKFMLVLASNLPEQFDCAINSR 466
Cdd:cd19509  106 ERGSGEHEASRRVK-TEFLVQMdgvlNKPEDRVLVLGATNRPWELDEAFLRR 156
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
348-533 2.22e-12

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 69.68  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAMHKLFDWANTSRRgLLLFMDEADAFLRKR-ATEEI 425
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDEIDAVGRQRgAGLGG 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 426 SKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHFdncvlkpateg 500
Cdd:PRK10733 267 GHDEReQTLNQMLVEMdGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILKVHM----------- 335
                        170       180       190
                 ....*....|....*....|....*....|...
gi 530360439 501 kRRLKLaqfDYGRKCSEVARLTEGMSGREIAQL 533
Cdd:PRK10733 336 -RRVPL---APDIDAAIIARGTPGFSGADLANL 364
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
346-463 2.88e-12

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: 65.33  E-value: 2.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTA--MHKLFDWANTSRRgLLLFMDEADAFLRKRATE 423
Cdd:cd19501   38 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGAsrVRDLFEQAKKNAP-CIVFIDEIDAVGRKRGAG 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530360439 424 EI-SKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI 463
Cdd:cd19501  116 LGgGHDEReQTLNQLLVEMdGFESNTGVIVIaATNRPDVLDPAL 159
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
329-475 1.03e-11

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: 62.93  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 329 RDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSG--------MDYAIMTGGDVapMGREGVTAMHKLFDWAN 400
Cdd:cd00009    3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFrpgapflyLNASDLLEGLV--VAELFGHFLVRLLFELA 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530360439 401 TSRRGLLLFMDEADAFlrkraTEEISKDLRATLNAFLYHMGQHSNkFMLVLASNLPE--QFDCAINSRIDVMVHFDL 475
Cdd:cd00009   81 EKAKPGVLFIDEIDSL-----SRGAQNALLRVLETLNDLRIDREN-VRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
ftsH CHL00176
cell division protein; Validated
348-534 1.03e-11

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 67.77  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTA--MHKLFDWANtSRRGLLLFMDEADAFLRKRATE-E 424
Cdd:CHL00176 219 VLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM-FVGVGAarVRDLFKKAK-ENSPCIVFIDEIDAVGRQRGAGiG 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 425 ISKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHFDNCVLKPATE 499
Cdd:CHL00176 297 GGNDEReQTLNQLLTEMdGFKGNKGVIVIaATNRVDILDAALlrPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVS 376
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 530360439 500 gkrrLKLaqfdygrkcseVARLTEGMSGREIAQLA 534
Cdd:CHL00176 377 ----LEL-----------IARRTPGFSGADLANLL 396
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
341-468 2.39e-11

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: 62.57  E-value: 2.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 341 NRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAMHKLFDWANTSRRGlLLFMDEADAFLR 418
Cdd:cd19521   36 NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSkwMG-ESEKLVKQLFAMARENKPS-IIFIDEVDSLCG 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530360439 419 KRATEEiSKDLRATLNAFLYHM---GQHSNKFMLVLASNLPEQFDCAINSRID 468
Cdd:cd19521  114 TRGEGE-SEASRRIKTELLVQMngvGNDSQGVLVLGATNIPWQLDSAIRRRFE 165
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
348-472 1.95e-10

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: 59.60  E-value: 1.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEEI 425
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKyvG-ESERAVREIFQKARQAAPC-IIFFDEIDSLAPRRGQSDS 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530360439 426 SKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVH 472
Cdd:cd19511  108 SGVTDRVVSQLLTELdGIESLKGVVVIaATNRPDMIDPALlrPGRLDKLIY 158
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
348-521 2.31e-10

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: 63.39  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR--AT 422
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI--MSKyygESEERLREIFKEAEENAPS-IIFIDEIDAIAPKReeVT 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  423 EEISKDLRATLNAFLYHMgQHSNKFMLVLASNLPEQFDCAIN--SRIDVMVHFDLPQQEERERLVRLHFDNcvlKPATEG 500
Cdd:TIGR01243 292 GEVEKRVVAQLLTLMDGL-KGRGRVIVIGATNRPDALDPALRrpGRFDREIVIRVPDKRARKEILKVHTRN---MPLAED 367
                         170       180
                  ....*....|....*....|.
gi 530360439  501 KRRLKLAQFDYGRKCSEVARL 521
Cdd:TIGR01243 368 VDLDKLAEVTHGFVGADLAAL 388
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
348-463 3.10e-10

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: 59.04  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATEEI 425
Cdd:cd19530   33 VLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKyvG-ESERAVRQVFQRARASAP-CVIFFDEVDALVPKRGDGGS 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 530360439 426 SKDLRaTLNAFLYHM--GQHSNKFMLVLASNLPEQFDCAI 463
Cdd:cd19530  111 WASER-VVNQLLTEMdgLEERSNVFVIAATNRPDIIDPAM 149
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
346-463 1.73e-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: 56.92  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRAT 422
Cdd:cd19503   35 RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSI--VSKylgESEKNLREIFEEARSHAPS-IIFIDEIDALAPKREE 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 530360439 423 --EEISKDLRATLNAFLYHMGQhSNKFMLVLASNLPEQFDCAI 463
Cdd:cd19503  112 dqREVERRVVAQLLTLMDGMSS-RGKVVVIAATNRPDAIDPAL 153
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
346-460 3.10e-09

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: 55.84  E-value: 3.10e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   346 RHILLYGPPGTGKTLFAKKLALHSG------------------MDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGlL 407
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 530360439   408 LFMDEADAFLRKrateEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFD 460
Cdd:smart00382  82 LILDEITSLLDA----EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLG 130
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
348-473 3.15e-09

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: 56.19  E-value: 3.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKLFDWANTsRRGLLLFMDEADAFLRKRATEEIS 426
Cdd:cd19502   40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSElVQKYIGEGARLVRELFEMARE-KAPSIIFIDEIDAIGAKRFDSGTG 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530360439 427 KD--LRATLNAFLYHMG--QHSNKFMLVLASNLPEQFDCAI--NSRIDVMVHF 473
Cdd:cd19502  119 GDreVQRTMLELLNQLDgfDPRGNIKVIMATNRPDILDPALlrPGRFDRKIEF 171
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
346-472 8.65e-09

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: 54.82  E-value: 8.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATe 423
Cdd:cd19528   28 KGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMwfG-ESEANVRDIFDKARAAAP-CVLFFDELDSIAKARGG- 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530360439 424 EISKDLRAT---LNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVH 472
Cdd:cd19528  105 NIGDAGGAAdrvINQILTEMdGMNTKKNVFIIgATNRPDIIDPAIlrPGRLDQLIY 160
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
346-463 2.13e-08

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: 53.98  E-value: 2.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR--AT 422
Cdd:cd19519   35 RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEImSKLAGESESNLRKAFEEAEKNAPA-IIFIDEIDAIAPKRekTH 113
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 530360439 423 EEISKDLRATLNAFLYHMGQHSNkFMLVLASNLPEQFDCAI 463
Cdd:cd19519  114 GEVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPAL 153
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
342-468 2.58e-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: 53.83  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 342 RGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR 420
Cdd:cd19522   30 RRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRgESEKLVRLLFEMARFYAPT-TIFIDEIDSICSRR 108
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 530360439 421 ATEEISKDLRATLNAFLYHM--------GQHSNKFMLVL-ASNLPEQFDCAINSRID 468
Cdd:cd19522  109 GTSEEHEASRRVKSELLVQMdgvggaseNDDPSKMVMVLaATNFPWDIDEALRRRLE 165
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
348-535 2.74e-08

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 55.99  E-value: 2.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTG--------GDVAPMGREgvtamhkLFDWANtSRRGLLLFMDEADAFLRK 419
Cdd:PRK03992 168 VLLYGPPGTGKTLLAKAVAHETNATFIRVVGselvqkfiGEGARLVRE-------LFELAR-EKAPSIIFIDEIDAIAAK 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 420 RATEEISKD--LRATLNAFLYHMGQHSNK--FMLVLASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHfdncv 493
Cdd:PRK03992 240 RTDSGTSGDreVQRTLMQLLAEMDGFDPRgnVKIIAATNRIDILDPAIlrPGRFDRIIEVPLPDEEGRLEILKIH----- 314
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 530360439 494 lkpategKRRLKLAQ-FDYgrkcSEVARLTEGMSGREIAQLAV 535
Cdd:PRK03992 315 -------TRKMNLADdVDL----EELAELTEGASGADLKAICT 346
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
346-463 1.30e-07

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: 51.34  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATE 423
Cdd:cd19529   28 KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSkwVG-ESEKAIREIFRKARQVAP-CVIFFDEIDSIAPRRGTT 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530360439 424 EISKDLRATLNAFLYHMG--QHSNKFMLVLASNLPEQFDCAI 463
Cdd:cd19529  106 GDSGVTERVVNQLLTELDglEEMNGVVVIAATNRPDIIDPAL 147
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
346-463 1.99e-07

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: 51.25  E-value: 1.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAMHKLFDWAnTSRRGLLLFMDEADAFLRKRatEE 424
Cdd:cd19518   35 RGVLLHGPPGCGKTMLANAIAGELKVPfLKISATEIVSGVSGESEEKIRELFDQA-ISNAPCIVFIDEIDAITPKR--ES 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530360439 425 ISKDL-RATLNAFLYHMGQHSN-----KFMLVL-ASNLPEQFDCAI 463
Cdd:cd19518  112 AQREMeRRIVSQLLTCMDELNNektagGPVLVIgATNRPDSLDPAL 157
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
348-467 2.15e-07

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: 50.89  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMtggDVAPMGREGVTAMHKLFDWANTSRRGL---LLFMDEADAFLRKRAT-- 422
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEAGARFINL---QVSSLTDKWYGESQKLVAAVFSLASKLqpsIIFIDEIDSFLRQRSStd 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 530360439 423 EEISKDLRATLNAFLYHMGQHSNKFMLVL-ASNLPEQFDCAINSRI 467
Cdd:cd19520  115 HEATAMMKAEFMSLWDGLSTDGNCRVIVMgATNRPQDLDEAILRRM 160
PTZ00121 PTZ00121
MAEBL; Provisional
57-227 2.37e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   57 RAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQ---LKSEQIRAQAEERRKtlSEETRQHQARAQYQ 133
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEekkMKAEEAKKAEEAKIK--AEELKKAEEEKKKV 1635
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  134 DKLARQRYEDQLKQQQLLNEE---NLRKQEESVQKQEAMRRATVER--EMELRHKNEML-RVETEARARAKAERENADII 207
Cdd:PTZ00121 1636 EQLKKKEAEEKKKAEELKKAEeenKIKAAEEAKKAEEDKKKAEEAKkaEEDEKKAAEALkKEAEEAKKAEELKKKEAEEK 1715
                         170       180
                  ....*....|....*....|..
gi 530360439  208 R--EQIRlKASEHRQTVLESIR 227
Cdd:PTZ00121 1716 KkaEELK-KAEEENKIKAEEAK 1736
PTZ00121 PTZ00121
MAEBL; Provisional
57-220 2.61e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.99  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   57 RAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVE-QLKSEQIRAQAEERRKTLSEETRQHQARAQYQDK 135
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  136 L----ARQRYEDQLKQQQLLNE-ENLRKQEESVQKQEAMRRATveremELRHKNEMLRVETEARARAKAERENADIIR-- 208
Cdd:PTZ00121 1431 KkadeAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKAD-----EAKKKAEEAKKADEAKKKAEEAKKKADEAKka 1505
                         170
                  ....*....|..
gi 530360439  209 EQIRLKASEHRQ 220
Cdd:PTZ00121 1506 AEAKKKADEAKK 1517
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
342-467 2.96e-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: 51.14  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 342 RGLYRHILLYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR 420
Cdd:cd19525   52 RGPPKGILLFGPPGTGKTLIGKCIASQSGATfFSISASSLTSKWVGEGEKMVRALFSVARCKQPA-VIFIDEIDSLLSQR 130
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530360439 421 --ATEEISKDLRATLNAFLYHMGQHSNKFMLVL-ASNLPEQFDCAINSRI 467
Cdd:cd19525  131 geGEHESSRRIKTEFLVQLDGATTSSEDRILVVgATNRPQEIDEAARRRL 180
PTZ00121 PTZ00121
MAEBL; Provisional
57-220 4.86e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.22  E-value: 4.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   57 RAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRktLSEETRQHQARAQYQDKL 136
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR--IEEVMKLYEEEKKMKAEE 1611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  137 ARQRYEDQLKQQQLLNEENLRK--------QEESVQKQEAMRRAtvEREMELRHKNEMLRVETEARA--RAKAERENADI 206
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKkveqlkkkEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKaeEAKKAEEDEKK 1689
                         170
                  ....*....|....
gi 530360439  207 IREQIRLKASEHRQ 220
Cdd:PTZ00121 1690 AAEALKKEAEEAKK 1703
PTZ00121 PTZ00121
MAEBL; Provisional
56-224 5.30e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 5.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRaQAEERRKT----LSEETRQ-HQARA 130
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-KADELKKAeelkKAEEKKKaEEAKK 1571
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  131 QYQDKLARQRYEDQLKQ---------QQLLNEENLRKQEESVQKQEAMRRA-TVEREMELRHKNEMLRVETEARARA--- 197
Cdd:PTZ00121 1572 AEEDKNMALRKAEEAKKaeearieevMKLYEEEKKMKAEEAKKAEEAKIKAeELKKAEEEKKKVEQLKKKEAEEKKKaee 1651
                         170       180
                  ....*....|....*....|....*...
gi 530360439  198 -KAERENADIIREQIRLKASEHRQTVLE 224
Cdd:PTZ00121 1652 lKKAEEENKIKAAEEAKKAEEDKKKAEE 1679
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
346-495 9.88e-07

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 51.30  E-value: 9.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR---- 420
Cdd:PTZ00454 180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEfVQKYLGEGPRMVRDVFRLARENAPS-IIFIDEVDSIATKRfdaq 258
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530360439 421 --ATEEISKDLRATLNAfLYHMGQHSNkFMLVLASNLPEQFDCAI--NSRIDVMVHFDLPQQEERerlvRLHFDNCVLK 495
Cdd:PTZ00454 259 tgADREVQRILLELLNQ-MDGFDQTTN-VKVIMATNRADTLDPALlrPGRLDRKIEFPLPDRRQK----RLIFQTITSK 331
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
56-220 1.04e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.86  E-value: 1.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  56 ERAAKAARELEhsRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTLsEETRQHQARAQYQDK 135
Cdd:COG1196  309 ERRRELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-EAELAEAEEELEELA 385
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 136 LARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKA 215
Cdd:COG1196  386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465

                 ....*
gi 530360439 216 SEHRQ 220
Cdd:COG1196  466 AELLE 470
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
63-229 1.08e-06

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: 51.66  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   63 RELEHSRYAKEALN--LAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKT---LSEETRQHQARAQYQDKLA 137
Cdd:pfam17380 378 RELERLQMERQQKNerVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRevrRLEEERAREMERVRLEEQE 457
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  138 RQRYEDQLKQQ---QLLNEENLRKQEESVQKQEAMRRATVEREMELR--------HKNEMLRVETEARARAKAERENADI 206
Cdd:pfam17380 458 RQQQVERLRQQeeeRKRKKLELEKEKRDRKRAEEQRRKILEKELEERkqamieeeRKRKLLEKEMEERQKAIYEEERRRE 537
                         170       180
                  ....*....|....*....|....
gi 530360439  207 IREQIRL-KASEHRQTVLESIRTA 229
Cdd:pfam17380 538 AEEERRKqQEMEERRRIQEQMRKA 561
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
346-467 1.23e-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: 48.69  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDY-----AIMTGGDVApmgrEGVTAMHKLFDWAnTSRRGLLLFMDEADAFLRKR 420
Cdd:cd19524   34 RGLLLFGPPGNGKTMLAKAVAAESNATFfnisaASLTSKYVG----EGEKLVRALFAVA-RELQPSIIFIDEVDSLLSER 108
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530360439 421 ATEEISKDLRATLNAFLYHMGQHSNKFMLVL---ASNLPEQFDCAINSRI 467
Cdd:cd19524  109 SEGEHEASRRLKTEFLIEFDGVQSNGDDRVLvmgATNRPQELDDAVLRRF 158
PTZ00121 PTZ00121
MAEBL; Provisional
57-220 1.79e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   57 RAAKAARELEHSRYAKEAlnlaqmqeqtlqleqqSKLKEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKL 136
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEA----------------RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMA 1263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  137 ARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREqirlKAS 216
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK----KAE 1339

                  ....
gi 530360439  217 EHRQ 220
Cdd:PTZ00121 1340 EAKK 1343
PTZ00121 PTZ00121
MAEBL; Provisional
56-219 2.32e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.91  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKE--YEAAVEQLKSEQIRAQAEERRKtlSEETRQHQARAQYQ 133
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEeaKKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKK 1498
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  134 DKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEA-----MRRATVEREMELRHKNEMLRVETEAR----ARAKAERENA 204
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAkkadeAKKAEEKKKADELKKAEELKKAEEKKkaeeAKKAEEDKNM 1578
                         170
                  ....*....|....*
gi 530360439  205 DIIREQIRLKASEHR 219
Cdd:PTZ00121 1579 ALRKAEEAKKAEEAR 1593
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
55-225 2.81e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  55 LERAAKAARELEHsryAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKsEQIRAQAEERRKTLSEETRQHQARAQYQD 134
Cdd:COG1196  255 LEELEAELAELEA---ELEELRLELEELELELEEAQAEEYELLAELARLE-QDIARLEERRRELEERLEELEEELAELEE 330
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 135 KLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLK 214
Cdd:COG1196  331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
                        170
                 ....*....|.
gi 530360439 215 ASEHRQTVLES 225
Cdd:COG1196  411 ALLERLERLEE 421
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
55-229 3.17e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  55 LERAAKAARELE--HSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQy 132
Cdd:COG1196  318 LEELEEELAELEeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA- 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 133 qdkLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIR 212
Cdd:COG1196  397 ---ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA 473
                        170
                 ....*....|....*..
gi 530360439 213 LKASEHRQTVLESIRTA 229
Cdd:COG1196  474 LLEAALAELLEELAEAA 490
PTZ00121 PTZ00121
MAEBL; Provisional
56-229 4.28e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAAR-ELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAA--VEQLKSEQIRAQAEERRKtlSEETRqhqaRAQY 132
Cdd:PTZ00121 1101 EEAKKTETgKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEArkAEDAKRVEIARKAEDARK--AEEAR----KAED 1174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  133 QDKL-ARQRYEDQLKQQQLLNEENLRKQE-----ESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADI 206
Cdd:PTZ00121 1175 AKKAeAARKAEEVRKAEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254
                         170       180       190
                  ....*....|....*....|....*....|....
gi 530360439  207 -----------IREQIRLKASEHRQTvlESIRTA 229
Cdd:PTZ00121 1255 rkfeearmahfARRQAAIKAEEARKA--DELKKA 1286
PTZ00121 PTZ00121
MAEBL; Provisional
56-224 5.53e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 5.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQS----KLKEYEAAVEQL-KSEQIRAQAEERRKTLSEETRQhqara 130
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeakKAEEAKIKAEELkKAEEEKKKVEQLKKKEAEEKKK----- 1648
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  131 qyQDKLARQRYEDQLKQQQLLN--EENLRKQEESVQKQEAMRRA--TVEREMELRHKNEMLRVETEARARA-----KAER 201
Cdd:PTZ00121 1649 --AEELKKAEEENKIKAAEEAKkaEEDKKKAEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEEKKKaeelkKAEE 1726
                         170       180
                  ....*....|....*....|...
gi 530360439  202 ENaDIIREQIRLKASEHRQTVLE 224
Cdd:PTZ00121 1727 EN-KIKAEEAKKEAEEDKKKAEE 1748
PTZ00121 PTZ00121
MAEBL; Provisional
56-222 7.26e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 7.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYE---AAVEQLKSEQIRaQAEERRKTLSEETRQHQARAQY 132
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakkAAEAKKKADEAK-KAEEAKKADEAKKAEEAKKADE 1538
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  133 QDKLARQRYEDQLKQ-QQLLNEENLRKQEESVQKQE----AMRRATVEREME-LRHKNEMLRVETEARARAKAER--ENA 204
Cdd:PTZ00121 1539 AKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEdknmALRKAEEAKKAEeARIEEVMKLYEEEKKMKAEEAKkaEEA 1618
                         170
                  ....*....|....*...
gi 530360439  205 DIIREQIRlKASEHRQTV 222
Cdd:PTZ00121 1619 KIKAEELK-KAEEEKKKV 1635
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
348-488 7.27e-06

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 48.61  E-value: 7.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR--ATEE 424
Cdd:PTZ00361 220 VILYGPPGTGKTLLAKAVANETSATFLRVVGSElIQKYLGDGPKLVRELFRVAEENAPS-IVFIDEIDAIGTKRydATSG 298
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530360439 425 ISKDLRATLNAFLYHMG--QHSNKFMLVLASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLH 488
Cdd:PTZ00361 299 GEKEIQRTMLELLNQLDgfDSRGDVKVIMATNRIESLDPALirPGRIDRKIEFPNPDEKTKRRIFEIH 366
PTZ00121 PTZ00121
MAEBL; Provisional
56-227 8.61e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 8.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAARELEHSRYAKEALNLAQmqeqTLQLEQQSKLKEYEAaveQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDK 135
Cdd:PTZ00121 1457 KKAEEAKKKAEEAKKADEAKKKAE----EAKKADEAKKKAEEA---KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  136 LARQRYEDQLKQ-QQLLNEENLRKQEEsVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLK 214
Cdd:PTZ00121 1530 AEEAKKADEAKKaEEKKKADELKKAEE-LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
                         170
                  ....*....|...
gi 530360439  215 ASEHRQTVLESIR 227
Cdd:PTZ00121 1609 AEEAKKAEEAKIK 1621
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
348-472 1.15e-05

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: 45.97  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAMHKLFDWANTSrRGLLLFMDEADAFLRKRATEEIS 426
Cdd:cd19527   29 ILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYiGESEANVREVFQKARDA-KPCVIFFDELDSLAPSRGNSGDS 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530360439 427 KDLR----ATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAI--NSRIDVMVH 472
Cdd:cd19527  108 GGVMdrvvSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALlrPGRFDKLLY 159
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
50-215 1.53e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.56  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  50 FDPTGLERAAKAARElehsryAKEALNLAQmqeqtLQLEQQSKLKEYEAAVEQLKSEQI-------RAQAEERRKTLSEE 122
Cdd:COG2268  186 LDALGRRKIAEIIRD------ARIAEAEAE-----RETEIAIAQANREAEEAELEQEREietariaEAEAELAKKKAEER 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 123 TRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERE 202
Cdd:COG2268  255 REAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRA 334
                        170
                 ....*....|...
gi 530360439 203 NADIIREQIRLKA 215
Cdd:COG2268  335 KGLAEAEGKRALA 347
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
346-466 1.72e-05

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: 45.26  E-value: 1.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTG-GDVAPMGREGVTAMHKLFDWANtSRRGLLLFMDEADAFLRKRATEE 424
Cdd:cd19523   34 RSILLFGPRGTGKTLLGRCLASQLGATFLRLRGsTLVAKWAGEGEKILQASFLAAR-CRQPSVLFISDLDALLSSQDDEA 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 530360439 425 -----ISKDLRATLNAFLyhmGQHSNKFMLVLASNLPEQFDCAINSR 466
Cdd:cd19523  113 spvgrLQVELLAQLDGVL---GSGEDGVLVVCTTSKPEEIDESLRRY 156
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
57-229 2.56e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 2.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  57 RAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSE--QIRAQAEERRKTLSEETRQhQARAQYQD 134
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLEleELELELEEAQAEEYELLAE-LARLEQDI 304
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 135 KLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELrhknEMLRVETEARARAKAERENADIIREQIRLK 214
Cdd:COG1196  305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE----EELEEAEAELAEAEEALLEAEAELAEAEEE 380
                        170
                 ....*....|....*
gi 530360439 215 ASEHRQTVLESIRTA 229
Cdd:COG1196  381 LEELAEELLEALRAA 395
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
346-463 3.49e-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: 44.42  E-value: 3.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDyaimtGGDVAPMGREGVTAMHKlfdWANTSRRGL-------------LLFMDE 412
Cdd:cd19517   35 RGVLFHGPPGTGKTLMARALAAECSKG-----GQKVSFFMRKGADCLSK---WVGEAERQLrllfeeayrmqpsIIFFDE 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530360439 413 AD--AFLRKRATEEISKDLRATLNAFLYHMgQHSNKFMLVLASNLPEQFDCAI 463
Cdd:cd19517  107 IDglAPVRSSKQEQIHASIVSTLLALMDGL-DNRGQVVVIGATNRPDALDPAL 158
PTZ00121 PTZ00121
MAEBL; Provisional
56-227 4.98e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTlSEETRQHQARAQYQDK 135
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA-AEALKKEAEEAKKAEE 1706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  136 LARQRYEDQLKQQQLLNEENLR--KQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAER-ENADIIREQIR 212
Cdd:PTZ00121 1707 LKKKEAEEKKKAEELKKAEEENkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRkEKEAVIEEELD 1786
                         170
                  ....*....|....*
gi 530360439  213 LKASEHRQTVLESIR 227
Cdd:PTZ00121 1787 EEDEKRRMEVDKKIK 1801
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
106-224 9.09e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 9.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 106 EQIRAQAE--ERRKTLSEETRQHQARAQ-YQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREmELRH 182
Cdd:COG1196  203 EPLERQAEkaERYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE-ELEL 281
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530360439 183 KNEMLRvETEARARAKAERENADIIREQIRLKASEHRQTVLE 224
Cdd:COG1196  282 ELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERLEELE 322
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
55-229 1.26e-04

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: 44.94  E-value: 1.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   55 LERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyQD 134
Cdd:pfam15709 348 LEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQ-QE 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  135 KLARQRYEDQLKQQQllneENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEaraRAKAEREnadiirEQIRLK 214
Cdd:pfam15709 427 EFRRKLQELQRKKQQ----EEAERAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQ---RQKQEAE------EKARLE 493
                         170
                  ....*....|....*
gi 530360439  215 ASEHRQTVLESIRTA 229
Cdd:pfam15709 494 AEERRQKEEEAARLA 508
PRK11637 PRK11637
AmiB activator; Provisional
101-209 1.56e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 44.30  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 101 EQLKSEQIRAQ----AEERRKTLSE--ETRQH--QARAQYQDKLARQR---YEDQLKQQQLLNEENLRKQ-----EESVQ 164
Cdd:PRK11637 150 ESQRGERILAYfgylNQARQETIAElkQTREElaAQKAELEEKQSQQKtllYEQQAQQQKLEQARNERKKtltglESSLQ 229
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 530360439 165 KQEAmrRATVEREMELRHKNEMLRVETEARARAKAERENADIIRE 209
Cdd:PRK11637 230 KDQQ--QLSELRANESRLRDSIARAEREAKARAEREAREAARVRD 272
PTZ00121 PTZ00121
MAEBL; Provisional
91-244 1.59e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   91 SKLKEYEAAVEQLKSEQIRAQAEERRKT----LSEETRQ-HQARAQYQDKLAR--QRYEDQLKQQQLLNEENLRKQEES- 162
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKAeearKAEDARKaEEARKAEDAKRVEiaRKAEDARKAEEARKAEDAKKAEAAr 1182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  163 ----VQKQEAMRRATVEREMELRHKNEMLRVETEARaRAKAERENADIIR-EQIRLKASEHRQTVLESIRTAGTLFGEGF 237
Cdd:PTZ00121 1183 kaeeVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261

                  ....*..
gi 530360439  238 RAFVTDR 244
Cdd:PTZ00121 1262 MAHFARR 1268
PTZ00121 PTZ00121
MAEBL; Provisional
55-220 1.66e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   55 LERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEA-AVEQLKSEQIRaQAEERRKtlSEETRQHQARAQYQ 133
Cdd:PTZ00121 1229 VKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIkAEEARKADELK-KAEEKKK--ADEAKKAEEKKKAD 1305
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  134 D---KLARQRYEDQLKQQQllnEENLRKQEESVQK-QEAMRRATVEREMELRHKNEMLRVETEARArAKAERENADIIRE 209
Cdd:PTZ00121 1306 EakkKAEEAKKADEAKKKA---EEAKKKADAAKKKaEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-AEKKKEEAKKKAD 1381
                         170
                  ....*....|.
gi 530360439  210 QIRLKASEHRQ 220
Cdd:PTZ00121 1382 AAKKKAEEKKK 1392
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
347-458 2.04e-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: 41.51  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  347 HILLYGPPGTGKTLFAKKLA------------LHSGMDYAIMTGG-DVAPMGREG-----VTAMhklfdwantsRRGLLL 408
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaalsnrpvfyvqLTRDTTEEDLFGRrNIDPGGASWvdgplVRAA----------REGEIA 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360439  409 FMDEADaflrkrateEISKDLRATLNAFLYH-----------MGQHSNKFMLVLASNLPEQ 458
Cdd:pfam07728  71 VLDEIN---------RANPDVLNSLLSLLDErrlllpdggelVKAAPDGFRLIATMNPLDR 122
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
348-471 2.22e-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: 42.03  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP----MGREGVtamHKLFDWANtSRRGLLLFMDEADAFLRKRATE 423
Cdd:cd19526   30 ILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNkyigASEQNV---RDLFSRAQ-SAKPCILFFDEFDSIAPKRGHD 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530360439 424 EISKDLRaTLNAFLYHM-GQHSNKFMLVLA-SNLPEQFDCAI--NSRIDVMV 471
Cdd:cd19526  106 STGVTDR-VVNQLLTQLdGVEGLDGVYVLAaTSRPDLIDPALlrPGRLDKLV 156
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
94-183 2.28e-04

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: 43.43  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   94 KEYEAAVEQLKSEQIRAQAEErrktLSEETRQHQARAQYQDKlarqRYEDQLKQ--------QQLLNEENLRKQEESVQK 165
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQEL----LREKQKEEEQMMEAQER----SYQEHVKQliekmeaeREQLLAEQERMLEHKLQE 273
                          90
                  ....*....|....*...
gi 530360439  166 QEAMRRATVEREMELRHK 183
Cdd:pfam02841 274 QEELLKEGFKTEAESLQK 291
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
93-222 2.89e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   93 LKEYEAAVEQLKS-----EQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEdQLKQQQLLNEENLRKQEESVQKQE 167
Cdd:COG4913   237 LERAHEALEDAREqiellEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLE 315
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530360439  168 AMRRATVEREMELRhkNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTV 222
Cdd:COG4913   316 ARLDALREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368
Zot COG4128
Zona occludens toxin, predicted ATPase [General function prediction only];
348-511 4.77e-04

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


Pssm-ID: 443304 [Multi-domain]  Cd Length: 276  Bit Score: 42.39  E-value: 4.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFA----KKLALHSG-------------------MDYAIMTGG---DVAPMGREGVTAMHKLFDWAnt 401
Cdd:COG4128    4 TLITGVPGSGKSYEAvwflIIPALKKGrrvitnipglkileriaehLGLAVPDTAeliNVDTDDPDGLEKMARWFHWA-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 402 sRRGLLLFMDEADAFLRKRATEEISKDLRatlNAFLYHmgQHSNkFMLVLASNLPEQFDCAINSRIDV-MVHFDLPQQEE 480
Cdd:COG4128   82 -PDGALIVIDEAQRVWPPRGKGSKPPDVV---QAFATH--RHHG-WDIVLITQNISLIHSFIRALIERhYRHRKLDGLGL 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 530360439 481 RERLVRLHFDNCVLKP-----ATEGKRRLKLAQFDY 511
Cdd:COG4128  155 RNRYEWPEHDGNPGKKtshdkATSKRYKYPKDVFGL 190
PTZ00121 PTZ00121
MAEBL; Provisional
56-220 5.36e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRKtlSEETRQHQAraqYQDK 135
Cdd:PTZ00121 1312 EEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK--EEAKKKADA---AKKK 1386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  136 LARQRYEDQLKQQQllneENLRKQEESVQKQEAMRRatveREMELRHKNEMLRVETEARARAKAEREnadiiREQIRLKA 215
Cdd:PTZ00121 1387 AEEKKKADEAKKKA----EEDKKKADELKKAAAAKK----KADEAKKKAEEKKKADEAKKKAEEAKK-----ADEAKKKA 1453

                  ....*
gi 530360439  216 SEHRQ 220
Cdd:PTZ00121 1454 EEAKK 1458
PTZ00121 PTZ00121
MAEBL; Provisional
57-209 5.59e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 5.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   57 RAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKlkeyeaAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKL 136
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE------AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEA 1735
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530360439  137 ARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREME------LRHKNEMLRVETEarARAKAERENADIIRE 209
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEavieeeLDEEDEKRRMEVD--KKIKDIFDNFANIIE 1812
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
95-215 5.62e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 42.34  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  95 EYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRY---EDQLK-QQQLLNE--------ENLRKQEES 162
Cdd:COG1566   80 DLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLdlaQRELErYQALYKKgavsqqelDEARAALDA 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530360439 163 VQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKA 215
Cdd:COG1566  160 AQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
92-200 5.74e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.49  E-value: 5.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  92 KLKEYEAavEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN---EENLRKQEESVQKQEA 168
Cdd:PRK09510 102 RLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAkkaAAEAKKKAEAEAAKKA 179
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 530360439 169 MRRATVEREMELRHKNEML---RVETEARARAKAE 200
Cdd:PRK09510 180 AAEAKKKAEAEAAAKAAAEakkKAEAEAKKKAAAE 214
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
62-225 5.99e-04

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: 42.80  E-value: 5.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   62 ARELEHSRyaKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKseqiRAQAEERRKTLSEETRQHQARAQYQDKLARQRY 141
Cdd:pfam17380 445 AREMERVR--LEEQERQQQVERLRQQEEERKRKKLELEKEKRD----RKRAEEQRRKILEKELEERKQAMIEEERKRKLL 518
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  142 EDQLKQQQ--LLNEENLRKQEESVQK----------QEAMRRATVEREM--ELRHKNEMLR--VETEARARAKAERENAD 205
Cdd:pfam17380 519 EKEMEERQkaIYEEERRREAEEERRKqqemeerrriQEQMRKATEERSRleAMEREREMMRqiVESEKARAEYEATTPIT 598
                         170       180
                  ....*....|....*....|
gi 530360439  206 IIREQIRLKASEHRQTVLES 225
Cdd:pfam17380 599 TIKPIYRPRISEYQPPDVES 618
PRK12704 PRK12704
phosphodiesterase; Provisional
91-227 6.51e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 6.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  91 SKLKEYEA-AVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN-EENLRKQEESVQKQEa 168
Cdd:PRK12704  31 AKIKEAEEeAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkEENLDRKLELLEKRE- 109
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 169 mrRATVEREMELRHKNEMLRvETEARARAKAERENADIirEQI-RLKASEHRQTVLESIR 227
Cdd:PRK12704 110 --EELEKKEKELEQKQQELE-KKEEELEELIEEQLQEL--ERIsGLTAEEAKEILLEKVE 164
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
346-422 7.02e-04

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: 40.94  E-value: 7.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 346 RHILLYGPPGTGKTLFAKKLA-LHSGMDYAIMTGGDVAP--MGrEGVTAMHKLFDWANTSRRGL-------LLFMDEADA 415
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGkMLNAREPKIVNGPEILNkyVG-ESEANIRKLFADAEEEQRRLgansglhIIIFDEIDA 114

                 ....*..
gi 530360439 416 FLRKRAT 422
Cdd:cd19504  115 ICKQRGS 121
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
348-366 7.19e-04

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 42.33  E-value: 7.19e-04
                         10
                 ....*....|....*....
gi 530360439 348 ILLYGPPGTGKTLFAKKLA 366
Cdd:COG0465  178 VLLVGPPGTGKTLLAKAVA 196
PTZ00121 PTZ00121
MAEBL; Provisional
56-212 8.56e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 8.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYE-----AAVEQLKSEQIRAQAEERRKtlSEETRQhQARA 130
Cdd:PTZ00121 1616 EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEenkikAAEEAKKAEEDKKKAEEAKK--AEEDEK-KAAE 1692
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  131 QYQDKLARQRYEDQLKQQQllnEENLRKQEEsVQKQEAMRRATVE----REMELRHKNEMLRVETEARARAKAERENADI 206
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKE---AEEKKKAEE-LKKAEEENKIKAEeakkEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768

                  ....*.
gi 530360439  207 IREQIR 212
Cdd:PTZ00121 1769 KAEEIR 1774
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
93-242 8.88e-04

Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 41.91  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   93 LKEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARaqyQDKLARQRYEDQLKQQQLLN-EENLRKQEESVQKQ--EAM 169
Cdd:pfam05262 203 LKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFA---QDNADKQRDEVRQKQQEAKNlPKPADTSSPKEDKQvaENQ 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  170 RRATVEREMELRHKNEMLRVETEARA----------RAKAERENADIIREqiRLKASEHRQTVLESIRTAGTLFGEGFRA 239
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEALKAKDHKAfdlkqeskasEKEAEDKELEAQKK--REPVAEDLQKTKPQVEAQPTSLNEDAID 357

                  ...
gi 530360439  240 FVT 242
Cdd:pfam05262 358 SSN 360
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
55-229 9.30e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 9.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439    55 LERAAKAA----------RELEHSRYA---------KEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEER 115
Cdd:TIGR02168  205 LERQAEKAerykelkaelRELELALLVlrleelreeLEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   116 RKT------------LSEETRQHQARAQY--QDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELR 181
Cdd:TIGR02168  285 ELQkelyalaneisrLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELE 364
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360439   182 HKNEMLR---------VETEARARAKAERE----NADIIREQIRLKASEHRQTVLESIRTA 229
Cdd:TIGR02168  365 AELEELEsrleeleeqLETLRSKVAQLELQiaslNNEIERLEARLERLEDRRERLQQEIEE 425
PRK10927 PRK10927
cell division protein FtsN;
101-201 9.34e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 41.59  E-value: 9.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 101 EQLKSEQ----IRAQAEERRK--TLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN------EENLRKQEESVQKQEA 168
Cdd:PRK10927 112 EQLTPEQrqllEQMQADMRQQptQLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAqqsrttEQSWQQQTRTSQAAPV 191
                         90       100       110
                 ....*....|....*....|....*....|....
gi 530360439 169 MRRATVEREMELRHK-NEMLRVETEARARAKAER 201
Cdd:PRK10927 192 QAQPRQSKPASTQQPyQDLLQTPAHTTAQSKPQQ 225
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
92-217 9.51e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 41.75  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   92 KLKEYEAAVEQLKS-EQIRAQAEERRKTLSEETRQH----------QARAQYQDKLARQRYEDQLKQQQllnEENLRKQE 160
Cdd:TIGR02794  93 ELEQRAAAEKAAKQaEQAAKQAEEKQKQAEEAKAKQaaeakakaeaEAERKAKEEAAKQAEEEAKAKAA---AEAKKKAE 169
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530360439  161 ESVQKQEAMRRATVERE-----MELRHKNEMLRVETEARARAKAERENADIIREQIRLKASE 217
Cdd:TIGR02794 170 EAKKKAEAEAKAKAEAEakakaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADE 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
56-220 9.71e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 9.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   56 ERAAKAARELEHSRYAKEALNLAQMQEqtlqleqqsKLKEYEAAVEQLKSEQirAQAEERRKTLSEETRQHQARaqyqdk 135
Cdd:COG4913   262 ERYAAARERLAELEYLRAALRLWFAQR---------RLELLEAELEELRAEL--ARLEAELERLEARLDALREE------ 324
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  136 laRQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEA-----RARAKAERENADIIREQ 210
Cdd:COG4913   325 --LDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEefaalRAEAAALLEALEEELEA 402
                         170
                  ....*....|
gi 530360439  211 IRLKASEHRQ 220
Cdd:COG4913   403 LEEALAEAEA 412
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
347-417 1.27e-03

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 41.61  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 347 HILLYGPPGTGKTLFAKKLALHSGMDY----AIMTggdvapmgreGVTAMHKLFDWANTSR---RGLLLFMDE------- 412
Cdd:PRK13342  38 SMILWGPPGTGKTTLARIIAGATDAPFealsAVTS----------GVKDLREVIEEARQRRsagRRTILFIDEihrfnka 107

                 ....*.
gi 530360439 413 -ADAFL 417
Cdd:PRK13342 108 qQDALL 113
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
348-417 1.51e-03

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 41.19  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 348 ILLYGPPGTGKTLFAKKLALHSGMDY----AIMTggdvapmgreGVTAMHKLFDWANTSR---RGLLLFMDE-------- 412
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFvalsAVTS----------GVKDIREVIEEARERRaygRRTILFVDEihrfnkaq 121

                 ....*
gi 530360439 413 ADAFL 417
Cdd:COG2256  122 QDALL 126
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
98-229 2.05e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 41.09  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   98 AAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKL------ARQRYEDQLKQQQLLNEENLRKQ---------EES 162
Cdd:COG3096   479 ELVCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLraqlaeLEQRLRQQQNAERLLEEFCQRIGqqldaaeelEEL 558
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  163 VQKQEAMR-------RATVEREMELRHKNEMLRVE-TEARARAKAERENADI---IREQI------RLKASEHRQTVLES 225
Cdd:COG3096   559 LAELEAQLeeleeqaAEAVEQRSELRQQLEQLRARiKELAARAPAWLAAQDAlerLREQSgealadSQEVTAAMQQLLER 638

                  ....
gi 530360439  226 IRTA 229
Cdd:COG3096   639 EREA 642
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
348-366 2.20e-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: 37.97  E-value: 2.20e-03
                          10
                  ....*....|....*....
gi 530360439  348 ILLYGPPGTGKTLFAKKLA 366
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLA 19
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
101-220 2.25e-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: 40.88  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  101 EQLKSEQIRAQAEE-------RRKTL-SEETRQHQARAQY-----QDKLA--RQRYEDQLKQQQLLNEENLRKQEESVQK 165
Cdd:pfam17380 294 EKMEQERLRQEKEEkareverRRKLEeAEKARQAEMDRQAaiyaeQERMAmeRERELERIRQEERKRELERIRQEEIAME 373
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530360439  166 QEAMRRatVER-EMELRHKNEMLRVETEARARAK-AERENADIIREQ------IRLKASEHRQ 220
Cdd:pfam17380 374 ISRMRE--LERlQMERQQKNERVRQELEAARKVKiLEEERQRKIQQQkvemeqIRAEQEEARQ 434
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
341-412 2.33e-03

Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain [Transcription, Signal transduction mechanisms];


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 40.86  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 341 NRGLyrHILLYGPPGTGKTLFAKKL---ALHSGM-------------DYA-----IM-----------TGgdvapmgreg 388
Cdd:COG1221  128 PKGL--HTLILGPTGVGKSFFAELMyeyAIEIGVlpedapfvvfncaDYAnnpqlLMsqlfgyvkgafTG---------- 195
                         90       100       110
                 ....*....|....*....|....*....|.
gi 530360439 389 vtamhklfdwANTSRRGLL-------LFMDE 412
Cdd:COG1221  196 ----------ADKDKEGLIekadggiLFLDE 216
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
55-344 2.36e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  55 LERAAKAARELEHSRYAKEALNLAQMQeqtlqleqqskLKEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQD 134
Cdd:COG4717  104 LEELEAELEELREELEKLEKLLQLLPL-----------YQELEALEAELAELPERLEELEERLEELRELEEELEELEAEL 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 135 KLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAmRRATVEREMELrhknemLRVETEARARAKAERENADIIREQIRLK 214
Cdd:COG4717  173 AELQEELEELLEQLSLATEEELQDLAEELEELQQ-RLAELEEELEE------AQEELEELEEELEQLENELEAAALEERL 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 215 ASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVL 294
Cdd:COG4717  246 KEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELL 325
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530360439 295 EALRHPIQVSR-RLLSRPQDVLEGVVLSPSLEARVRDIAIATRNTKKNRGL 344
Cdd:COG4717  326 AALGLPPDLSPeELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
151-366 2.41e-03

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 40.52  E-value: 2.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 151 LNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKAS----EHRQTVLESI 226
Cdd:COG1401   31 IRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEaavaIEELYELEAD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 227 RTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRR 306
Cdd:COG1401  111 SEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSE 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 307 LLSRPQDVLEGVvLSPSLEARVRDIAIATRnTKKNrglyrhILLYGPPGTGKTLFAKKLA 366
Cdd:COG1401  191 DLESEDDYLKDL-LREKFEETLEAFLAALK-TKKN------VILAGPPGTGKTYLARRLA 242
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
59-224 5.48e-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: 39.72  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439   59 AKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKEYEAAVEQLKSEQIRAQAEERRktlseETRQHQARAQYQDKLAR 138
Cdd:pfam17380 321 AEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMR-----ELERLQMERQQKNERVR 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  139 QRYEdQLKQQQLLNEENLRKQEESVQKQEAMRRATVE-REMELR---------------------HKNEMLRVETEARAR 196
Cdd:pfam17380 396 QELE-AARKVKILEEERQRKIQQQKVEMEQIRAEQEEaRQREVRrleeeraremervrleeqerqQQVERLRQQEEERKR 474
                         170       180
                  ....*....|....*....|....*...
gi 530360439  197 AKAERENadiiREQIRLKASEHRQTVLE 224
Cdd:pfam17380 475 KKLELEK----EKRDRKRAEEQRRKILE 498
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
347-365 5.53e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.67  E-value: 5.53e-03
                          10
                  ....*....|....*....
gi 530360439  347 HILLYGPPGTGKTLFAKKL 365
Cdd:pfam01078  24 NLLMIGPPGSGKTMLAKRL 42
44 PHA02544
clamp loader, small subunit; Provisional
347-493 5.59e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 39.20  E-value: 5.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439 347 HILLYGP-PGTGKTLFAKKLALHSGMDYAIMTGGDvapmGREGvTAMHKLFDWANT---SRRGLLLFMDEADaflrKRAT 422
Cdd:PHA02544  44 NMLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSD----CRID-FVRNRLTRFASTvslTGGGKVIIIDEFD----RLGL 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530360439 423 EEISKDLRATlnaflyhMGQHSNKFMLVLASNLPEQFDCAINSRIDVmVHFDLPQQEERERLVRLHFDNCV 493
Cdd:PHA02544 115 ADAQRHLRSF-------MEAYSKNCSFIITANNKNGIIEPLRSRCRV-IDFGVPTKEEQIEMMKQMIVRCK 177
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
346-373 5.72e-03

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 39.00  E-value: 5.72e-03
                         10        20
                 ....*....|....*....|....*...
gi 530360439 346 RHILLYGPPGTGKTLFAKKLALHSGMDY 373
Cdd:COG0714   32 GHLLLEGVPGVGKTTLAKALARALGLPF 59
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
101-220 5.98e-03

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 39.06  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360439  101 EQLKSEQIRAQAEERRKtlsEETRQHQARAQYQDKLARQRYEDQLKQQQllnEENLRKQEESVQKQEAMRRATVEREMEL 180
Cdd:TIGR02794  61 PAAKKEQERQKKLEQQA---EEAEKQRAAEQARQKELEQRAAAEKAAKQ---AEQAAKQAEEKQKQAEEAKAKQAAEAKA 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 530360439  181 RHKNEMLRvETEARARAKAERENADIIREQIRLKASEHRQ 220
Cdd:TIGR02794 135 KAEAEAER-KAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK 173
 
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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