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Conserved domains on  [gi|1919013998|ref|XP_036603613|]
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ATPase family AAA domain-containing protein 3A [Trichosurus vulpecula]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 43-287 7.49e-122

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: 360.45  E-value: 7.49e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  43 TPKDKWSNFDPTGLERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTLNE 122
Cdd:pfam12037  15 KPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 123 ETRQHQARAQYQDKLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIR-----RATVEREMELRHKNEMLRIEAETRAR 197
Cdd:pfam12037  95 ETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEAR 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 198 ARAERENADIIREQIRLKAAEHRQTILESLKTAGTLFGEGFRAFVTDWDKVTATVAGLTLLAVGVYTAKNATAVAGRYIE 277
Cdd:pfam12037 175 AKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYIE 254

                         250
                  ....*....|
gi 1919013998 278 ARLGKPSLVR 287
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 ...
 325-474 2.52e-108

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


:

Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 321.40  E-value: 2.52e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 325 LEERVRDIAIATRNTKKNKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWANTSR 404
Cdd:cd19512     1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 405 RGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVNF 474
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 ...
 43-287 7.49e-122

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: 360.45  E-value: 7.49e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  43 TPKDKWSNFDPTGLERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTLNE 122
Cdd:pfam12037  15 KPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 123 ETRQHQARAQYQDKLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIR-----RATVEREMELRHKNEMLRIEAETRAR 197
Cdd:pfam12037  95 ETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEAR 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 198 ARAERENADIIREQIRLKAAEHRQTILESLKTAGTLFGEGFRAFVTDWDKVTATVAGLTLLAVGVYTAKNATAVAGRYIE 277
Cdd:pfam12037 175 AKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYIE 254

                         250
                  ....*....|
gi 1919013998 278 ARLGKPSLVR 287
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 ...
 325-474 2.52e-108

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 321.40  E-value: 2.52e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 325 LEERVRDIAIATRNTKKNKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWANTSR 404
Cdd:cd19512     1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 405 RGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVNF 474
Cdd:cd19512    81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 168-561 3.77e-29

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: 119.63  E-value: 3.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 168 EAIRRATVEREMELRHKNEMLRIEAETRARARAERENADIIREQIRLKAAEHRQTILESLKTAGTLFGEGFRAFVTDWDK 247
Cdd:COG0464     5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 248 VTATVAGLTLLAVGVYTAKNATAVAGRYIEARLGKPSLVRETSRITVLEALKHPITVGRRLASKPQ---DALEGVVLSPK 324
Cdd:COG0464    85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLElreAILDDLGGLEE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 325 LEERVRDIAIATRNTKKNKSLY-----RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGR-EGVTA--MHKV 396
Cdd:COG0464   165 VKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEknLREV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 397 FDWANTSRRGLLLFvDEADAFLRKRATEKiSEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVNFDL 476
Cdd:COG0464   243 FDKARGLAPCVLFI-DEADALAGKRGEVG-DGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEIIFFPL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 477 PQLPERERLVRMYFDKYilkpategkqrlklaQFDYGKKCSEIARLTEGMSGREISQLAIAWQALAYASEDGVLTEAMID 556
Cdd:COG0464   321 PDAEERLEIFRIHLRKR---------------PLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLL 385


                  ....*
gi 1919013998 557 TRVKD 561
Cdd:COG0464   386 EALER 390
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
316-570 3.09e-27

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 110.36  E-value: 3.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 316 LEGVVLSPKLEERVRDIAIATRNTKK----NKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGR---E 388
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENlrkfGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSylgE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 389 GVTAMHKVFDWANtsRRGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRI 468
Cdd:COG1223    79 TARNLRKLFDFAR--RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALWRRF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 469 DEMVNFDLPQLPERERLVRMYFDKYILKPATEGKqrlklaqfdygkkcsEIARLTEGMSGREISQLAIAWQALAYASEDG 548
Cdd:COG1223   157 DEVIEFPLPDKEERKEILELNLKKFPLPFELDLK---------------KLAKKLEGLSGADIEKVLKTALKKAILEDRE 221

                         250       260
                  ....*....|....*....|..
gi 1919013998 549 VLTEAMIDtrvkDAIQQHQQKM 570
Cdd:COG1223   222 KVTKEDLE----EALKQRKERK 239
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 349-476 2.04e-23

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 95.74  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 349 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGR-EGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRATEKIS 427
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1919013998 428 EDLR--ATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVNFDL 476
Cdd:pfam00004  80 ESRRvvNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
336-583 1.75e-12

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 70.06  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 336 TRNTKKNKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGRE-GVTAMHKVFDWANTSRRgLLLFVDEA 414
Cdd:PRK10733  175 SRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDEI 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 415 DAFLRKR-ATEKISEDLR-ATLNAFL-HRTGQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVNFDLPQLPERERLVRM 488
Cdd:PRK10733  254 DAVGRQRgAGLGGGHDEReQTLNQMLvEMDGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILKV 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 489 YFDKYILKPATEGkqrlklaqfdygkkcSEIARLTEGMSGREISQLAIawQALAYASEDGVLTEAMID-TRVKDAIQQHQ 567
Cdd:PRK10733  334 HMRRVPLAPDIDA---------------AIIARGTPGFSGADLANLVN--EAALFAARGNKRVVSMVEfEKAKDKIMMGA 396

                         250
                  ....*....|....*.
gi 1919013998 568 QKMEWLKAEGMEGSKS 583
Cdd:PRK10733  397 ERRSMVMTEAQKESTA 412
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 347-534 4.40e-09

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 59.54  E-value: 4.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDV-APMGREGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRATEK 425
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 426 ISEDLRATLNAFLHRT-GQHSNKFMLVL-ASNQPEQFDwaindridemvnfdlPQLPERERlvrmyFDKYILKPATEGKQ 503
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILD---------------PALLRPGR-----FDRLILVPPPDEEA 626

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1919013998 504 RLKLAQFDYGK-------KCSEIARLTEGMSGREISQL 534
Cdd:TIGR01243 627 RKEIFKIHTRSmplaedvDLEELAEMTEGYTGADIEAV 664
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 347-477 2.32e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 53.53  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  347 RNILMYGPPGTGKTLFAKKLA------------------MHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWANTSRRGlL 408
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALArelgppgggviyidgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  409 LFVDEADAFLRKRAtekiSEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWA-INDRIDEMVNFDLP 477
Cdd:smart00382  82 LILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147
PTZ00121 PTZ00121
MAEBL; Provisional
 56-230 3.98e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 3.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   56 LERAAKAARELEHSRHAKEAlslaqmqeqtlqleqqSKVKEYEAAVEQLKNEQVRiQAEERRKTlnEETRQHQARAQYQD 135
Cdd:PTZ00121  1156 IARKAEDARKAEEARKAEDA----------------KKAEAARKAEEVRKAEELR-KAEDARKA--EAARKAEEERKAEE 1216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  136 KlarQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRIEAETRA---RARAERENADIIREQI 212
Cdd:PTZ00121  1217 A---RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAeeaRKADELKKAEEKKKAD 1293

                          170
                   ....*....|....*...
gi 1919013998  213 RLKAAEHRQTILESLKTA 230
Cdd:PTZ00121  1294 EAKKAEEKKKADEAKKKA 1311
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-226 9.57e-03

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: 39.27  E-value: 9.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   92 SKVKEYEAAVEQLK-------NEQVRIQAE-----ERRKTLNEETRQHQARAQY--QDKLARQRYDDQLRQQQLLNEENL 157
Cdd:TIGR02168  260 AELQELEEKLEELRlevseleEEIEELQKElyalaNEISRLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEEL 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  158 RKQEESVQKQEAIRRATVEREMELRHKNEML-------RIEAETRARARAERE------NADIIREQIRLKAAEHRQTIL 224
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELesrleelEEQLETLRSKVAQLElqiaslNNEIERLEARLERLEDRRERL 419


                   ..
gi 1919013998  225 ES 226
Cdd:TIGR02168  420 QQ 421
 
Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
 43-287 7.49e-122

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: 360.45  E-value: 7.49e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  43 TPKDKWSNFDPTGLERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTLNE 122
Cdd:pfam12037  15 KPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 123 ETRQHQARAQYQDKLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIR-----RATVEREMELRHKNEMLRIEAETRAR 197
Cdd:pfam12037  95 ETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEAR 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 198 ARAERENADIIREQIRLKAAEHRQTILESLKTAGTLFGEGFRAFVTDWDKVTATVAGLTLLAVGVYTAKNATAVAGRYIE 277
Cdd:pfam12037 175 AKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYIE 254

                         250
                  ....*....|
gi 1919013998 278 ARLGKPSLVR 287
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 ...
 325-474 2.52e-108

ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase domains; ATPase AAA-domain protein 3 (ATAD3) is a ubiquitously expressed mitochondrial protein involved in mitochondrial dynamics, DNA-nucleoid structural organization, cholesterol transport and steroidogenesis. The ATAD3 gene family in human comprises three paralog genes: ATAD3A, ATAD3B and ATAD3C. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 321.40  E-value: 2.52e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 325 LEERVRDIAIATRNTKKNKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWANTSR 404
Cdd:cd19512     1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 405 RGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVNF 474
Cdd:cd19512    81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 324-474 1.49e-35

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: 130.87  E-value: 1.49e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 324 KLEERVRDIAIATRNTKKNKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGR-EGVTAMHKVFDWANT 402
Cdd:cd19481     4 SLREAVEAPRRGSRLRRYGLGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVgESEKNLRKIFERARR 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1919013998 403 SRRGLLLFvDEADAFLRKRATEKISEDLRATLNAFLHRT--GQHSNKFMLVLASNQPEQFDWAIND--RIDEMVNF 474
Cdd:cd19481    84 LAPCILFI-DEIDAIGRKRDSSGESGELRRVLNQLLTELdgVNSRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 168-561 3.77e-29

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: 119.63  E-value: 3.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 168 EAIRRATVEREMELRHKNEMLRIEAETRARARAERENADIIREQIRLKAAEHRQTILESLKTAGTLFGEGFRAFVTDWDK 247
Cdd:COG0464     5 LALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLALLAA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 248 VTATVAGLTLLAVGVYTAKNATAVAGRYIEARLGKPSLVRETSRITVLEALKHPITVGRRLASKPQ---DALEGVVLSPK 324
Cdd:COG0464    85 LLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLElreAILDDLGGLEE 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 325 LEERVRDIAIATRNTKKNKSLY-----RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGR-EGVTA--MHKV 396
Cdd:COG0464   165 VKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEknLREV 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 397 FDWANTSRRGLLLFvDEADAFLRKRATEKiSEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVNFDL 476
Cdd:COG0464   243 FDKARGLAPCVLFI-DEADALAGKRGEVG-DGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEIIFFPL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 477 PQLPERERLVRMYFDKYilkpategkqrlklaQFDYGKKCSEIARLTEGMSGREISQLAIAWQALAYASEDGVLTEAMID 556
Cdd:COG0464   321 PDAEERLEIFRIHLRKR---------------PLDEDVDLEELAEATEGLSGADIRNVVRRAALQALRLGREPVTTEDLL 385


                  ....*
gi 1919013998 557 TRVKD 561
Cdd:COG0464   386 EALER 390
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
316-570 3.09e-27

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 110.36  E-value: 3.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 316 LEGVVLSPKLEERVRDIAIATRNTKK----NKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGR---E 388
Cdd:COG1223     1 LDDVVGQEEAKKKLKLIIKELRRRENlrkfGLWPPRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSylgE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 389 GVTAMHKVFDWANtsRRGLLLFVDEADAFLRKRATEKISEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRI 468
Cdd:COG1223    79 TARNLRKLFDFAR--RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALWRRF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 469 DEMVNFDLPQLPERERLVRMYFDKYILKPATEGKqrlklaqfdygkkcsEIARLTEGMSGREISQLAIAWQALAYASEDG 548
Cdd:COG1223   157 DEVIEFPLPDKEERKEILELNLKKFPLPFELDLK---------------KLAKKLEGLSGADIEKVLKTALKKAILEDRE 221

                         250       260
                  ....*....|....*....|..
gi 1919013998 549 VLTEAMIDtrvkDAIQQHQQKM 570
Cdd:COG1223   222 KVTKEDLE----EALKQRKERK 239
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 349-476 2.04e-23

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 95.74  E-value: 2.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 349 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGR-EGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRATEKIS 427
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1919013998 428 EDLR--ATLNAFLHRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMVNFDL 476
Cdd:pfam00004  80 ESRRvvNQLLTELDGFTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 349-571 2.11e-20

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 92.38  E-value: 2.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 349 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPM--GrEGVTAMHKVFDWANTSRRGLLLFvDEADAFLRKRATEKI 426
Cdd:COG1222   115 VLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKyiG-EGARNVREVFELAREKAPSIIFI-DEIDAIAARRTDDGT 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 427 SEDLRATLNAFLHRT-GQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVNFDLPQLPERERLVRMYFDKYILKpategk 502
Cdd:COG1222   193 SGEVQRTVNQLLAELdGFESRGDVLIIaATNRPDLLDPALlrPGRFDRVIEVPLPDEEAREEILKIHLRDMPLA------ 266

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1919013998 503 qrlklAQFDYgkkcSEIARLTEGMSGREISqlAIAWQALAYASEDGVLTEAMIDtrVKDAIQQHQQKME 571
Cdd:COG1222   267 -----DDVDL----DKLAKLTEGFSGADLK--AIVTEAGMFAIREGRDTVTMED--LEKAIEKVKKKTE 322
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
336-583 1.75e-12

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 70.06  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 336 TRNTKKNKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGRE-GVTAMHKVFDWANTSRRgLLLFVDEA 414
Cdd:PRK10733  175 SRFQKLGGKIPKGVLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDEI 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 415 DAFLRKR-ATEKISEDLR-ATLNAFL-HRTGQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVNFDLPQLPERERLVRM 488
Cdd:PRK10733  254 DAVGRQRgAGLGGGHDEReQTLNQMLvEMDGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILKV 333

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 489 YFDKYILKPATEGkqrlklaqfdygkkcSEIARLTEGMSGREISQLAIawQALAYASEDGVLTEAMID-TRVKDAIQQHQ 567
Cdd:PRK10733  334 HMRRVPLAPDIDA---------------AIIARGTPGFSGADLANLVN--EAALFAARGNKRVVSMVEfEKAKDKIMMGA 396

                         250
                  ....*....|....*.
gi 1919013998 568 QKMEWLKAEGMEGSKS 583
Cdd:PRK10733  397 ERRSMVMTEAQKESTA 412
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
 347-464 1.24e-10

ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. It is anchored to the cytoplasmic membrane such that the amino- and carboxy-termini are exposed to the cytoplasm. It presents a membrane-bound hexameric structure that is able to unfold and degrade protein substrates. It is comprised of an N-terminal transmembrane region and the larger C-terminal cytoplasmic region, which consists of an ATPase domain and a protease domain. This RecA-Like FTsH subfamily represents the ATPase domain, and belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 60.32  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMgREGVTAmHKVFDWANTSRRG--LLLFVDEADAFLRKR-AT 423
Cdd:cd19501    38 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGA-SRVRDLFEQAKKNapCIVFIDEIDAVGRKRgAG 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1919013998 424 EKISEDLR-ATLNAFL-HRTGQHSNKFMLVL-ASNQPEQFDWAI 464
Cdd:cd19501   116 LGGGHDEReQTLNQLLvEMDGFESNTGVIVIaATNRPDVLDPAL 159
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 346-476 1.46e-09

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 56.77  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 346 YRNILMYGPPGTGKTLFAKKLAMHSG--------MDYAIMTGGDVapMGREGVTAMHKVFDWANTSRRGLLLFVDEADAF 417
Cdd:cd00009    19 PKNLLLYGPPGTGKTTLARAIANELFrpgapflyLNASDLLEGLV--VAELFGHFLVRLLFELAEKAKPGVLFIDEIDSL 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1919013998 418 lrkraTEKISEDLRATLNAFLHRTGQHSNkFMLVLASNQPE--QFDWAINDRIDEMVNFDL 476
Cdd:cd00009    97 -----SRGAQNALLRVLETLNDLRIDREN-VRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
 342-467 1.50e-09

ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This subfamily includes the ATPase domains of vacuolar protein sorting-associated protein 4 (VPS4), ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase), Katanin p60 ATPase-containing subunit A1 (KTNA1), Spastin, and Fidgetin-Like 1 (FIGL-1). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 56.98  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 342 NKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVA--PMGrEGVTAMHKVFDWANtSRRGLLLFVDEADAFLR 419
Cdd:cd19509    28 LRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVskWVG-ESEKIVRALFALAR-ELQPSIIFIDEIDSLLS 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1919013998 420 KRATEKiSEDLRATLNAFLHR----TGQHSNKFMLVLASNQPEQFDWAINDR 467
Cdd:cd19509   106 ERGSGE-HEASRRVKTEFLVQmdgvLNKPEDRVLVLGATNRPWELDEAFLRR 156
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 349-472 2.91e-09

second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL exists in two forms with N-terminal extensions of different lengths in mammalian cells. NVL has two alternatively spliced isoforms, a short form, NVL1, and a long form, NVL2. NVL2, the major species, is mainly present in the nucleolus, whereas NVL1 is nucleoplasmic. Each has an N-terminal domain, followed by two tandem ATPase domains; this subfamily includes the first of the two ATPase domains. NVL2 is involved in the biogenesis of the 60S ribosome subunit by associating specifically with ribosome protein L5 and modulating the function of DOB1. NVL2 is also required for telomerase assembly and the regulation of telomerase activity, and is involved in pre-rRNA processing. The role of NVL1 is unclear. This RecA-like_NVL_r1-like subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 56.34  E-value: 2.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 349 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPM--GrEGVTAMHKVFDWANTSRRGLLLFvDEADAFLRKRATEKI 426
Cdd:cd19530    33 VLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKyvG-ESERAVRQVFQRARASAPCVIFF-DEVDALVPKRGDGGS 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1919013998 427 SEDLRaTLNAFLHRT--GQHSNKFMLVLASNQPEQFDWAI--NDRIDEMV 472
Cdd:cd19530   111 WASER-VVNQLLTEMdgLEERSNVFVIAATNRPDIIDPAMlrPGRLDKTL 159
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
 347-472 3.13e-09

second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase domains; This subfamily includes the second of two ATPase domains of the molecular chaperone CDC48 in yeast and p97 or VCP in metazoans, Peroxisomal biogenesis factor 1 (PEX1) and -6 (PEX6), Valosin-containing protein-like ATPase (VAT), and nuclear VCP-like protein (NVL). This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 56.14  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPM--GrEGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRATE 424
Cdd:cd19511    28 KGVLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKyvG-ESERAVREIFQKARQAAPC-IIFFDEIDSLAPRRGQS 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1919013998 425 KISEDLRATLNAFLHRT-GQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 472
Cdd:cd19511   106 DSSGVTDRVVSQLLTELdGIESLKGVVVIaATNRPDMIDPALlrPGRLDKLI 157
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 347-534 4.40e-09

AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two members each from three archaeal species. It also includes yeast CDC48 (cell division control protein 48) and the human ortholog, transitional endoplasmic reticulum ATPase (valosin-containing protein). These proteins in eukaryotes are involved in the budding and transfer of membrane from the transitional endoplasmic reticulum to the Golgi apparatus.


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 59.54  E-value: 4.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDV-APMGREGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRATEK 425
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 426 ISEDLRATLNAFLHRT-GQHSNKFMLVL-ASNQPEQFDwaindridemvnfdlPQLPERERlvrmyFDKYILKPATEGKQ 503
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILD---------------PALLRPGR-----FDRLILVPPPDEEA 626

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1919013998 504 RLKLAQFDYGK-------KCSEIARLTEGMSGREISQL 534
Cdd:TIGR01243 627 RKEIFKIHTRSmplaedvDLEELAEMTEGYTGADIEAV 664
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
 347-468 7.00e-09

ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ATPase family AAA domain-containing protein 1 (ATAD1, also known as Thorase) is an ATPase that plays a critical role in regulating the surface expression of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors, thereby regulating synaptic plasticity, learning and memory. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 55.12  E-value: 7.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAP--MGrEGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKR--- 421
Cdd:cd19520    36 KGVLLYGPPGCGKTMLAKATAKEAGARFINLQVSSLTDkwYG-ESQKLVAAVFSLASKLQPS-IIFIDEIDSFLRQRsst 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1919013998 422 ---ATEKISEDLRATLNAFlhRTGQHSnKFMLVLASNQPEQFDWAINDRI 468
Cdd:cd19520   114 dheATAMMKAEFMSLWDGL--STDGNC-RVIVMGATNRPQDLDEAILRRM 160
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-299 1.65e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 1.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  56 LERAAKAARELE--HSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTLNEETRQHQARA-- 131
Cdd:COG1196   318 LEELEEELAELEeeLEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAae 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 132 --QYQDKLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRIEAETRARARAERENADIIR 209
Cdd:COG1196   398 laAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 210 EQIRLKAAEHRQTILESLKTAGTLFGEGFRAFVTDWDKVTATVAGLTLLAVGVYTAKNATAVAGRYIEARLGKPSLVRET 289
Cdd:COG1196   478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE 557

                         250
                  ....*....|
gi 1919013998 290 SRITVLEALK 299
Cdd:COG1196   558 VAAAAIEYLK 567
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
 342-472 1.77e-08

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 54.10  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 342 NKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAP--MGrEGVTAMHKVFDWANTSRRGlLLFVDEADAFLR 419
Cdd:cd19521    36 NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSkwMG-ESEKLVKQLFAMARENKPS-IIFIDEVDSLCG 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1919013998 420 KRAtEKISEDLRATLNAFL---HRTGQHSNKFMLVLASNQPEQFDWAINDRIDEMV 472
Cdd:cd19521   114 TRG-EGESEASRRIKTELLvqmNGVGNDSQGVLVLGATNIPWQLDSAIRRRFEKRI 168
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
 325-474 1.87e-08

proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily contains ATPase subunits of the eukaryotic 26S proteasome, and of the archaeal proteasome which carry out ATP-dependent degradation of substrates of the ubiquitin-proteasome pathway. The eukaryotic 26S proteasome consists of a proteolytic 20S core particle (CP), and a 19S regulatory particle (RP) which provides the ATP-dependence and the specificity for ubiquitinated proteins. In the archaea the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). This subfamily also includes various eukaryotic 26S subunits including, proteasome 26S subunit, ATPase 2 (PSMC2, also known as S7 and MSS1) which is a member of the 19S RP and has a chaperone like activity; and proteasome 20S subunit alpha 6 (PSMA6, also known as IOTA, p27K, and PROS27) which is a member of the 20S CP. This RecA-like_PAN subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 54.27  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 325 LEERVRDIAIATRNTKKNKSLYRNI--------LMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGD-VAPMGREGVTAMHK 395
Cdd:cd19502     8 LDEQIREIREVVELPLKHPELFEELgieppkgvLLYGPPGTGKTLLAKAVANHTDATFIRVVGSElVQKYIGEGARLVRE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 396 VFDWANTsRRGLLLFVDEADAFLRKRATEKISED---------LRATLNAFLHRtgqhsNKFMLVLASNQPEQFDWAI-- 464
Cdd:cd19502    88 LFEMARE-KAPSIIFIDEIDAIGAKRFDSGTGGDrevqrtmleLLNQLDGFDPR-----GNIKVIMATNRPDILDPALlr 161

                         170
                  ....*....|
gi 1919013998 465 NDRIDEMVNF 474
Cdd:cd19502   162 PGRFDRKIEF 171
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
 339-472 2.31e-08

second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP in metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the second of the two ATPase domains. CDC48's roles include in the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis, and in the formation of the nuclear envelope, and of the transitional endoplasmic reticulum (tER). This RecA-like_cdc48_r2-like subfamily belongs to the RecA-like family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 53.67  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 339 TKKNKSLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPM--GrEGVTAMHKVFDWANTSRRgLLLFVDEADA 416
Cdd:cd19528    20 LKFGMTPSKGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMwfG-ESEANVRDIFDKARAAAP-CVLFFDELDS 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1919013998 417 FLRKRATeKISEDLRAT---LNAFLHRT-GQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMV 472
Cdd:cd19528    98 IAKARGG-NIGDAGGAAdrvINQILTEMdGMNTKKNVFIIgATNRPDIIDPAIlrPGRLDQLI 159
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 347-477 2.32e-08

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 53.53  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  347 RNILMYGPPGTGKTLFAKKLA------------------MHSGMDYAIMTGGDVAPMGREGVTAMHKVFDWANTSRRGlL 408
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALArelgppgggviyidgediLEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  409 LFVDEADAFLRKRAtekiSEDLRATLNAFLHRTGQHSNKFMLVLASNQPEQFDWA-INDRIDEMVNFDLP 477
Cdd:smart00382  82 LILDEITSLLDAEQ----EALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
 346-472 3.87e-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: 53.06  E-value: 3.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 346 YRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMGR-EGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRATE 424
Cdd:cd19522    33 WKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRgESEKLVRLLFEMARFYAPT-TIFIDEIDSICSRRGTS 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1919013998 425 KISEDLRATLNAFLHR--------TGQHSNKFMLVL-ASNQPEQFDWAINDRIDEMV 472
Cdd:cd19522   112 EEHEASRRVKSELLVQmdgvggasENDDPSKMVMVLaATNFPWDIDEALRRRLEKRI 168
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
 347-464 4.56e-08

second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ATPase domains; The Valosin-containing protein-like ATPase of Thermoplasma acidophilum (VAT), is an archaeal homolog of the ubiquitous Cdc48/p97. It is a protein unfoldase that functions in concert with the 20S proteasome by unfolding proteasome substrates and passing them on for degradation. VAT forms a homohexamer, each monomer contains two tandem ATPase domains, referred to as D1 and D2, and an N-terminal domain. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410937 [Multi-domain]  Cd Length: 159  Bit Score: 52.88  E-value: 4.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAP--MGrEGVTAMHKVFDWANTSrRGLLLFVDEADAFLRKRA-- 422
Cdd:cd19529    28 KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSkwVG-ESEKAIREIFRKARQV-APCVIFFDEIDSIAPRRGtt 105

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1919013998 423 -----TEKISEDLRATLNAFlhrtgQHSNKFMLVLASNQPEQFDWAI 464
Cdd:cd19529   106 gdsgvTERVVNQLLTELDGL-----EEMNGVVVIAATNRPDIIDPAL 147
RecA-like_CDC48_NLV2_r1-like cd19503
first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and ...
 347-464 6.83e-08

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: 52.29  E-value: 6.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGR---EGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRAT 423
Cdd:cd19503    35 RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSI--VSKylgESEKNLREIFEEARSHAPS-IIFIDEIDALAPKREE 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1919013998 424 --EKISEDLRATLNAFLHRTGQhSNKFMLVLASNQPEQFDWAI 464
Cdd:cd19503   112 dqREVERRVVAQLLTLMDGMSS-RGKVVVIAATNRPDAIDPAL 153
ftsH CHL00176
cell division protein; Validated
 349-567 7.70e-08

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 55.44  E-value: 7.70e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 349 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMgREGVTA--MHKVFDWANtSRRGLLLFVDEADAFLRKRATE-K 425
Cdd:CHL00176  219 VLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM-FVGVGAarVRDLFKKAK-ENSPCIVFIDEIDAVGRQRGAGiG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 426 ISEDLR-ATLNAFL-HRTGQHSNKFMLVL-ASNQPEQFDWAI--NDRIDEMVNFDLPQLPERERLVRMYFDKYILKPATE 500
Cdd:CHL00176  297 GGNDEReQTLNQLLtEMDGFKGNKGVIVIaATNRVDILDAALlrPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVS 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 501 GKQrlklaqfdygkkcseIARLTEGMSGREISQLA--------------IAWQALAYASE---DGVLTEAMIDTRVKDAI 563
Cdd:CHL00176  377 LEL---------------IARRTPGFSGADLANLLneaailtarrkkatITMKEIDTAIDrviAGLEGTPLEDSKNKRLI 441


                  ....
gi 1919013998 564 QQHQ 567
Cdd:CHL00176  442 AYHE 445
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
 349-535 1.79e-07

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 53.68  E-value: 1.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 349 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTG--------GDVAPMGREgvtamhkVFDWANtSRRGLLLFVDEADAFLRK 420
Cdd:PRK03992  168 VLLYGPPGTGKTLLAKAVAHETNATFIRVVGselvqkfiGEGARLVRE-------LFELAR-EKAPSIIFIDEIDAIAAK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 421 RATEKISEDlratlnAFLHRTgqhsnkFMLVL----------------ASNQPEQFDWAI--NDRIDEMVNFDLPQLPER 482
Cdd:PRK03992  240 RTDSGTSGD------REVQRT------LMQLLaemdgfdprgnvkiiaATNRIDILDPAIlrPGRFDRIIEVPLPDEEGR 307

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1919013998 483 ERlvrmyfdkyILKPATegkQRLKLAQ-FDYgkkcSEIARLTEGMSGREISQLA 535
Cdd:PRK03992  308 LE---------ILKIHT---RKMNLADdVDL----EELAELTEGASGADLKAIC 345
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
 347-464 2.37e-07

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 50.90  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDV-APMGREGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKR--AT 423
Cdd:cd19519    35 RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEImSKLAGESESNLRKAFEEAEKNAPA-IIFIDEIDAIAPKRekTH 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1919013998 424 EKISEDLRATLNAFLhrTGQHSNKFMLVL-ASNQPEQFDWAI 464
Cdd:cd19519   114 GEVERRIVSQLLTLM--DGLKQRAHVIVMaATNRPNSIDPAL 153
PTZ00121 PTZ00121
MAEBL; Provisional
 56-230 3.98e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 53.61  E-value: 3.98e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   56 LERAAKAARELEHSRHAKEAlslaqmqeqtlqleqqSKVKEYEAAVEQLKNEQVRiQAEERRKTlnEETRQHQARAQYQD 135
Cdd:PTZ00121  1156 IARKAEDARKAEEARKAEDA----------------KKAEAARKAEEVRKAEELR-KAEDARKA--EAARKAEEERKAEE 1216

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  136 KlarQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRIEAETRA---RARAERENADIIREQI 212
Cdd:PTZ00121  1217 A---RKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAeeaRKADELKKAEEKKKAD 1293

                          170
                   ....*....|....*...
gi 1919013998  213 RLKAAEHRQTILESLKTA 230
Cdd:PTZ00121  1294 EAKKAEEKKKADEAKKKA 1311
PTZ00121 PTZ00121
MAEBL; Provisional
 57-228 6.64e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 6.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   57 ERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRiQAEERRKTLN----EETRQ-HQARA 131
Cdd:PTZ00121  1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKK-KADELKKAEElkkaEEKKKaEEAKK 1571

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  132 QYQDKLARQRYDDQLRQ---------QQLLNEENLRKQEESVQKQEA-IRRATVEREMELRHKNEML-RIEAETRARA-- 198
Cdd:PTZ00121  1572 AEEDKNMALRKAEEAKKaeearieevMKLYEEEKKMKAEEAKKAEEAkIKAEELKKAEEEKKKVEQLkKKEAEEKKKAee 1651

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1919013998  199 -RAERENADIIREQIRLKAAEHRQTILESLK 228
Cdd:PTZ00121  1652 lKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
 347-468 6.89e-07

ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; it may be involved in DNA double-strand break repair via homologous recombination. Caenorhabditis elegans FIGL-1 is a nuclear protein and controls the mitotic progression in the germ line and mouse FIGL-1 may be involved in the control of male meiosis. human FIGL-1 has been shown to be a centrosome protein involved in ciliogenesis perhaps as a microtubule-severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 49.99  E-value: 6.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMD-YAIMTGGDVAPMGREGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKRAtEK 425
Cdd:cd19525    56 KGILLFGPPGTGKTLIGKCIASQSGATfFSISASSLTSKWVGEGEKMVRALFSVARCKQPA-VIFIDEIDSLLSQRG-EG 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1919013998 426 ISEDLRATLNAFLHR----TGQHSNKFMLVLASNQPEQFDWAINDRI 468
Cdd:cd19525   134 EHESSRRIKTEFLVQldgaTTSSEDRILVVGATNRPQEIDEAARRRL 180
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
 347-522 7.08e-07

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: 52.22  E-value: 7.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVapMGR---EGVTAMHKVFDWANTSRRGlLLFVDEADAFLRKR-- 421
Cdd:TIGR01243 213 KGVLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI--MSKyygESEERLREIFKEAEENAPS-IIFIDEIDAIAPKRee 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 422 ATEKISEDLRATLNAFLHRTgQHSNKFMLVLASNQPEQFDWAIN--DRIDEMVNFDLPQLPERERLVRMYFDKyilKPAT 499
Cdd:TIGR01243 290 VTGEVEKRVVAQLLTLMDGL-KGRGRVIVIGATNRPDALDPALRrpGRFDREIVIRVPDKRARKEILKVHTRN---MPLA 365

                         170       180
                  ....*....|....*....|...
gi 1919013998 500 EGKQRLKLAQFDYGKKCSEIARL 522
Cdd:TIGR01243 366 EDVDLDKLAEVTHGFVGADLAAL 388
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
 349-472 1.07e-06

second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as Peroxin61)/PEX1 is a protein unfoldase; PEX6 and PEX1 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. This subfamily represents the second ATPase domain of PEX6. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 48.66  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 349 ILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAPMG-REGVTAMHKVFDWANTSRRGLLLFvDEADAFLRKRAT---- 423
Cdd:cd19527    29 ILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYiGESEANVREVFQKARDAKPCVIFF-DELDSLAPSRGNsgds 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1919013998 424 ----EKISEDLRATLNAfLHRTGQhsnKFMLVLASNQPEQFDWAI--NDRIDEMV 472
Cdd:cd19527   108 ggvmDRVVSQLLAELDG-MSSSGQ---DVFVIGATNRPDLLDPALlrPGRFDKLL 158
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 57-230 1.21e-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: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  57 ERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKnEQVRIQAEERRKTLNEETRQHQARAQYQDK 136
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE-QDIARLEERRRELEERLEELEEELAELEEE 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 137 LARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRIEAETRARARAERENADIIREQIRLKA 216
Cdd:COG1196   332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411

                         170
                  ....*....|....
gi 1919013998 217 AEHRQTILESLKTA 230
Cdd:COG1196   412 LLERLERLEEELEE 425
PTZ00121 PTZ00121
MAEBL; Provisional
 57-230 1.75e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   57 ERAAKAAR-ELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAA--VEQLKNEQVRIQAEERRKTlnEETRqhqaRAQY 133
Cdd:PTZ00121  1101 EEAKKTETgKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEArkAEDAKRVEIARKAEDARKA--EEAR----KAED 1174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  134 QDKLARQRYDDQLRQ-QQLLNEENLRKQE-----ESVQKQEAIRRATVEREMELRHKNEMLRIEAETRARARAERENADI 207
Cdd:PTZ00121  1175 AKKAEAARKAEEVRKaEELRKAEDARKAEaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1919013998  208 -----------IREQIRLKAAEHRQTilESLKTA 230
Cdd:PTZ00121  1255 rkfeearmahfARRQAAIKAEEARKA--DELKKA 1286
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
 347-486 2.05e-06

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 50.15  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGD-VAPMGREGVTAMHKVFDWANTSRRGlLLFVDEADAFLRK----- 420
Cdd:PTZ00454  180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEfVQKYLGEGPRMVRDVFRLARENAPS-IIFIDEVDSIATKrfdaq 258

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1919013998 421 ----RATEKISEDLRATLNAFlhrtgQHSNKFMLVLASNQPEQFDWAI--NDRIDEMVNFDLPQLPEReRLV 486
Cdd:PTZ00454  259 tgadREVQRILLELLNQMDGF-----DQTTNVKVIMATNRADTLDPALlrPGRLDRKIEFPLPDRRQK-RLI 324
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
 344-467 2.56e-06

ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 47.96  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 344 SLYRNILMYGPPGTGKTLFAKKLAMHSGMDYAIMTG-GDVAPMGREGVTAMHKVFDWANtSRRGLLLFVDEADAFLRKRA 422
Cdd:cd19523    31 RLPRSILLFGPRGTGKTLLGRCLASQLGATFLRLRGsTLVAKWAGEGEKILQASFLAAR-CRQPSVLFISDLDALLSSQD 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1919013998 423 TE-----KISEDLRATLNAFLhrtGQHSNKFMLVLASNQPEQFDWAINDR 467
Cdd:cd19523   110 DEaspvgRLQVELLAQLDGVL---GSGEDGVLVVCTTSKPEEIDESLRRY 156
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 59-225 2.61e-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: 50.51  E-value: 2.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  59 AAKAARELEHSRHAKEALSLAQMQEQTLQLEQqSKVKEYE--AAVEQLKNEQVRIQAEERRK-TLNEETRQHQARAQY-- 133
Cdd:pfam17380 343 AMERERELERIRQEERKRELERIRQEEIAMEI-SRMRELErlQMERQQKNERVRQELEAARKvKILEEERQRKIQQQKve 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 134 ------QDKLARQRYDDQLRQQQLLNEENLRKQEESVQKQ-EAIRRATVERemelrhKNEMLRIEAETRARARAERENAD 206
Cdd:pfam17380 422 meqiraEQEEARQREVRRLEEERAREMERVRLEEQERQQQvERLRQQEEER------KRKKLELEKEKRDRKRAEEQRRK 495

                         170
                  ....*....|....*....
gi 1919013998 207 IIREQIRlkaaEHRQTILE 225
Cdd:pfam17380 496 ILEKELE----ERKQAMIE 510
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-230 3.43e-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: 3.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  58 RAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQA--EERRKTLNEETRQhQARAQYQD 135
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELelEEAQAEEYELLAE-LARLEQDI 304

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 136 KLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVEREMELrhknEMLRIEAETRARARAERENADIIREQIRLK 215
Cdd:COG1196   305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE----EELEEAEAELAEAEEALLEAEAELAEAEEE 380

                         170
                  ....*....|....*
gi 1919013998 216 AAEHRQTILESLKTA 230
Cdd:COG1196   381 LEELAEELLEALRAA 395
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
 347-472 3.58e-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: 47.54  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDY-----AIMTGGDVApmgrEGVTAMHKVFDWAnTSRRGLLLFVDEADAFLRKR 421
Cdd:cd19524    34 RGLLLFGPPGNGKTMLAKAVAAESNATFfnisaASLTSKYVG----EGEKLVRALFAVA-RELQPSIIFIDEVDSLLSER 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1919013998 422 ATEKISEDLRATLNAFLHRTGQHSNKFMLVL---ASNQPEQFDWAINDRIDEMV 472
Cdd:cd19524   109 SEGEHEASRRLKTEFLIEFDGVQSNGDDRVLvmgATNRPQELDDAVLRRFTKRV 162
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-225 4.76e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  56 LERAAKAARELEHS-RHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTLNEETRQHQARAQYQ 134
Cdd:COG1196   255 LEELEAELAELEAElEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 135 DKLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRIEAETRARARAERENADIIREQIRL 214
Cdd:COG1196   335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414

                         170
                  ....*....|.
gi 1919013998 215 KAAEHRQTILE 225
Cdd:COG1196   415 RLERLEEELEE 425
PTZ00121 PTZ00121
MAEBL; Provisional
 57-231 6.98e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 6.98e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   57 ERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKvKEYEAAVEQLKNEQVRiQAEERRKTLNEETRQHQARAQYQDK 136
Cdd:PTZ00121  1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAEELK-KAEEEKKKVEQLKKKEAEEKKKAEE 1651

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  137 LARQRYDDQLRQQQLLNE--------ENLRKQEESVQKQEairRATVEREMELRHKNEMLRIEAETRARA---RAERENA 205
Cdd:PTZ00121  1652 LKKAEEENKIKAAEEAKKaeedkkkaEEAKKAEEDEKKAA---EALKKEAEEAKKAEELKKKEAEEKKKAeelKKAEEEN 1728

                          170       180
                   ....*....|....*....|....*.
gi 1919013998  206 DIIREQIRLKAAEHRQTILESLKTAG 231
Cdd:PTZ00121  1729 KIKAEEAKKEAEEDKKKAEEAKKDEE 1754
PTZ00121 PTZ00121
MAEBL; Provisional
 58-230 7.53e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 7.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   58 RAAKAARELEHSRHAKEAlslaqmqeqtlqleqqSKVKEYEAAVEQLKNEQVRIQAEERRKTlnEETRQHQARAQYQDkl 137
Cdd:PTZ00121  1200 RKAEAARKAEEERKAEEA----------------RKAEDAKKAEAVKKAEEAKKDAEEAKKA--EEERNNEEIRKFEE-- 1259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  138 arQRYDDQLRQQQLLNEENLRKQEEsVQKQEAIRRATVEREMELRHKNEMLRIEAETRARARAERENAdiirEQIRLKAA 217
Cdd:PTZ00121  1260 --ARMAHFARRQAAIKAEEARKADE-LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKA----EEAKKKAD 1332

                          170
                   ....*....|...
gi 1919013998  218 EHRQTILESLKTA 230
Cdd:PTZ00121  1333 AAKKKAEEAKKAA 1345
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
 347-464 1.37e-05

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: 45.86  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMD-YAIMTGGDVAPMGREGVTAMHKVFDWAnTSRRGLLLFVDEADAFLRKRatEK 425
Cdd:cd19518    35 RGVLLHGPPGCGKTMLANAIAGELKVPfLKISATEIVSGVSGESEEKIRELFDQA-ISNAPCIVFIDEIDAITPKR--ES 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1919013998 426 ISEDL-RATLNAFLHRTGQHSN-----KFMLVL-ASNQPEQFDWAI 464
Cdd:cd19518   112 AQREMeRRIVSQLLTCMDELNNektagGPVLVIgATNRPDSLDPAL 157
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
 347-474 1.55e-05

ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces cerevisiae Yta7 is a chromatin-associated AAA-ATPase involved in regulation of chromatin dynamics. Its human ortholog ANCCA/ATAD2 transcriptionally activates pathways of malignancy in a broad range of cancers. The RecA-like_Yta7 subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 45.58  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLAMHSGMDyaimtGGDVAPMGREGVTAMHKvfdWANTSRRGL-------------LLFVDE 413
Cdd:cd19517    35 RGVLFHGPPGTGKTLMARALAAECSKG-----GQKVSFFMRKGADCLSK---WVGEAERQLrllfeeayrmqpsIIFFDE 106

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1919013998 414 AD--AFLRKRATEKISEDLRATLNAF---LHRTGQhsnkFMLVLASNQPEQFDWAIN--DRIDEMVNF 474
Cdd:cd19517   107 IDglAPVRSSKQEQIHASIVSTLLALmdgLDNRGQ----VVVIGATNRPDALDPALRrpGRFDREFYF 170
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-225 2.13e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  56 LERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAE------ERRKTLNEETRQHQA 129
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEleeaeaELAEAEEALLEAEAE 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 130 RAQYQDKLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVEREME--LRHKNEMLRIEAETRARARAERENADI 207
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEelEEALAELEEEEEEEEEALEEAAEEEAE 453

                         170
                  ....*....|....*...
gi 1919013998 208 IREQIRLKAAEHRQTILE 225
Cdd:COG1196   454 LEEEEEALLELLAELLEE 471
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 63-225 2.48e-05

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: 47.43  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  63 ARELEHSRHAKEALSLAQmqeqTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTlNEETRQHQ-------ARAQYQD 135
Cdd:pfam17380 309 AREVERRRKLEEAEKARQ----AEMDRQAAIYAEQERMAMERERELERIRQEERKRE-LERIRQEEiameisrMRELERL 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 136 KLARQRYDDQLRQ--------------------QQLLNEENLRKQEESVqKQEAIRRATVER----------EMELRHKN 185
Cdd:pfam17380 384 QMERQQKNERVRQeleaarkvkileeerqrkiqQQKVEMEQIRAEQEEA-RQREVRRLEEERaremervrleEQERQQQV 462

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1919013998 186 EMLRIEAETRARARAERENadiiREQIRLKAAEHRQTILE 225
Cdd:pfam17380 463 ERLRQQEEERKRKKLELEK----EKRDRKRAEEQRRKILE 498
PTZ00121 PTZ00121
MAEBL; Provisional
 57-228 3.05e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   57 ERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEA--AVEQLKNEQVRIQAEERRKTLNEETRQHQARAQYQ 134
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  135 DKlarqRYDDQLRQQQllnEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRIEAETR----ARARAERENADIIRE 210
Cdd:PTZ00121  1481 EA----KKADEAKKKA---EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKkadeAKKAEEKKKADELKK 1553

                          170
                   ....*....|....*...
gi 1919013998  211 QIRLKAAEHRQTILESLK 228
Cdd:PTZ00121  1554 AEELKKAEEKKKAEEAKK 1571
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 56-230 3.56e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  56 LERAAKAARELEHSRHAKEALSLAQMQ-EQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAE-ERRKTLNEETRQHQARAQY 133
Cdd:COG1196   272 LRLELEELELELEEAQAEEYELLAELArLEQDIARLEERRRELEERLEELEEELAELEEElEELEEELEELEEELEEAEE 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 134 QDKLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVEREmELRHKNEMLRIEAETRARARAERENADIIREQIR 213
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEAL 430

                         170
                  ....*....|....*..
gi 1919013998 214 LKAAEHRQTILESLKTA 230
Cdd:COG1196   431 AELEEEEEEEEEALEEA 447
PRK10927 PRK10927
cell division protein FtsN;
102-202 4.00e-05

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 45.83  E-value: 4.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 102 EQLKNEQ----VRIQAEERRK--TLNEETRQHQARAQYQDKLARQRYDDQLRQQQLLN------EENLRKQEESVQKQEA 169
Cdd:PRK10927  112 EQLTPEQrqllEQMQADMRQQptQLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAqqsrttEQSWQQQTRTSQAAPV 191

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1919013998 170 IRRATVEREMELRHK-NEMLRIEAETRARARAER 202
Cdd:PRK10927  192 QAQPRQSKPASTQQPyQDLLQTPAHTTAQSKPQQ 225
PTZ00121 PTZ00121
MAEBL; Provisional
 57-228 4.39e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.39e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   57 ERAAKAARELEHSRHAKEALSLAQmqEQTLQLEQQSKVKEYEAAVE-QLKNEQVRIQAEERRKTLNEETRQHQARAQYQD 135
Cdd:PTZ00121  1444 KKADEAKKKAEEAKKAEEAKKKAE--EAKKADEAKKKAEEAKKADEaKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  136 KLARQ-------RYDDQLRQ-QQLLNEENLRKQEEsVQKQEAIRRATVEREMELRHKNEMLRIEAETRARARAERENADI 207
Cdd:PTZ00121  1522 KKADEakkaeeaKKADEAKKaEEKKKADELKKAEE-LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL 1600

                          170       180
                   ....*....|....*....|.
gi 1919013998  208 IREQIRLKAAEHRQTILESLK 228
Cdd:PTZ00121  1601 YEEEKKMKAEEAKKAEEAKIK 1621
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 341-418 5.72e-05

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 45.82  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 341 KNKSLYR--------NILMYGPPGTGKTLFAKKLAMHSGMDY----AIMTggdvapmgreGVTAMHKVFDWANTSR---R 405
Cdd:COG2256    36 PGKPLRRaieagrlsSMILWGPPGTGKTTLARLIANATDAEFvalsAVTS----------GVKDIREVIEEARERRaygR 105

                          90       100
                  ....*....|....*....|.
gi 1919013998 406 GLLLFVDE--------ADAFL 418
Cdd:COG2256   106 RTILFVDEihrfnkaqQDALL 126
PTZ00121 PTZ00121
MAEBL; Provisional
 58-221 5.77e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 5.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   58 RAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVE-QLKNEQVRIQAEERRKTLNEETRQHQARAQYQDK 136
Cdd:PTZ00121  1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEaKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEK 1430

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  137 L----ARQRYDDQLRQQQLLNE-ENLRKQEESVQKQEAIRRATveremELRHKNEMLRIEAETRARARAERENADIIR-- 209
Cdd:PTZ00121  1431 KkadeAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKAD-----EAKKKAEEAKKADEAKKKAEEAKKKADEAKka 1505

                          170
                   ....*....|..
gi 1919013998  210 EQIRLKAAEHRQ 221
Cdd:PTZ00121  1506 AEAKKKADEAKK 1517
PTZ00121 PTZ00121
MAEBL; Provisional
 60-228 7.52e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.90  E-value: 7.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   60 AKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAvEQLKN--EQVRIQAEERRKTLNEETRQ-HQARAQYQDK 136
Cdd:PTZ00121  1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKA-EELKKaeEENKIKAAEEAKKAEEDKKKaEEAKKAEEDE 1687

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  137 LARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVER----------EMELRHKNEMLRIEAETRARARAERENAD 206
Cdd:PTZ00121  1688 KKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENkikaeeakkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEE 1767

                          170       180
                   ....*....|....*....|..
gi 1919013998  207 IIREQIRlkaAEHRQTILESLK 228
Cdd:PTZ00121  1768 KKAEEIR---KEKEAVIEEELD 1786
PRK11637 PRK11637
AmiB activator; Provisional
 110-210 1.01e-04

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 45.07  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 110 RIQA------EERRKTLNE--ETRQH--QARAQYQDKLARQR---YDDQLRQQQLLNEENLRKQ-----EESVQKQEAir 171
Cdd:PRK11637  156 RILAyfgylnQARQETIAElkQTREElaAQKAELEEKQSQQKtllYEQQAQQQKLEQARNERKKtltglESSLQKDQQ-- 233

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1919013998 172 RATVEREMELRHKNEMLRIEAETRARARAERENADIIRE 210
Cdd:PRK11637  234 QLSELRANESRLRDSIARAEREAKARAEREAREAARVRD 272
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
 325-495 1.38e-04

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 44.76  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 325 LEERVRDIAIATRNTKKNKSLYRNI--------LMYGPPGTGKTLFAKKLAMHSGMDYAIMTG--------GDVAPMGRE 388
Cdd:PTZ00361  188 LEQQIQEIKEAVELPLTHPELYDDIgikppkgvILYGPPGTGKTLLAKAVANETSATFLRVVGseliqkylGDGPKLVRE 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 389 gvtaMHKVFDWANTSrrglLLFVDEADAFLRKR--ATEKISEDLRATLNAFLHRTG--QHSNKFMLVLASNQPEQFDWAI 464
Cdd:PTZ00361  268 ----LFRVAEENAPS----IVFIDEIDAIGTKRydATSGGEKEIQRTMLELLNQLDgfDSRGDVKVIMATNRIESLDPAL 339

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1919013998 465 --NDRIDEMVNFDLPQLPERERLVRMYFDKYIL 495
Cdd:PTZ00361  340 irPGRIDRKIEFPNPDEKTKRRIFEIHTSKMTL 372
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
51-217 2.18e-04

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 44.09  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  51 FDPTGLERAAKAARElehsRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTLNEETRQHQAR 130
Cdd:COG2268   186 LDALGRRKIAEIIRD----ARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETAR 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 131 AQYQDKLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRIEAETRARARAERENADIIRE 210
Cdd:COG2268   262 AEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAE 341


                  ....*..
gi 1919013998 211 QIRLKAA 217
Cdd:COG2268   342 GKRALAE 348
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 341-418 3.59e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 43.15  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 341 KNKSLYR--------NILMYGPPGTGKTLFAKKLAMHSGMDY----AIMTggdvapmgreGVTAMHKVFDWANTSR---R 405
Cdd:PRK13342   23 PGKPLRRmieagrlsSMILWGPPGTGKTTLARIIAGATDAPFealsAVTS----------GVKDLREVIEEARQRRsagR 92

                          90       100
                  ....*....|....*....|.
gi 1919013998 406 GLLLFVDE--------ADAFL 418
Cdd:PRK13342   93 RTILFIDEihrfnkaqQDALL 113
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
 348-421 3.62e-04

second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as Peroxin-1)/PEX6 is a protein unfoldase; PEX1 and PEX6 form a heterohexameric Type-2 AAA-ATPase complex and are essential for peroxisome biogenesis as they are required for the import of folded proteins into the peroxisomal matrix. PEX-1 is required for stability of PEX5. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410934 [Multi-domain]  Cd Length: 158  Bit Score: 41.26  E-value: 3.62e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1919013998 348 NILMYGPPGTGKTLFAKKLAMHSGMDYAIMTGGDVAP----MGREGVtamHKVFDWANtSRRGLLLFVDEADAFLRKR 421
Cdd:cd19526    29 GILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNkyigASEQNV---RDLFSRAQ-SAKPCILFFDEFDSIAPKR 102
PTZ00121 PTZ00121
MAEBL; Provisional
 57-228 3.63e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 3.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   57 ERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKN--EQVRIQAEERRKTlnEETRQHQARaqyq 134
Cdd:PTZ00121  1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKaaEALKKEAEEAKKA--EELKKKEAE---- 1713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  135 dklaRQRYDDQLRQQQllnEENLRKQEESVQKQEAIRRATVEREMELRHKNEMLRIEAETRARARAER-ENADIIREQIR 213
Cdd:PTZ00121  1714 ----EKKKAEELKKAE---EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRkEKEAVIEEELD 1786

                          170
                   ....*....|....*
gi 1919013998  214 LKAAEHRQTILESLK 228
Cdd:PTZ00121  1787 EEDEKRRMEVDKKIK 1801
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
56-345 4.99e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  56 LERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTLNEetRQHQARAQYQD 135
Cdd:COG4717    80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE--RLEELEERLEE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 136 KLARQRYDDQLRQQ--QLLNEENLRKQEESVQKQEAIRRATVEREM-ELRHKNEMLRIEAETRARARAERENADIIREQI 212
Cdd:COG4717   158 LRELEEELEELEAElaELQEELEELLEQLSLATEEELQDLAEELEElQQRLAELEEELEEAQEELEELEEELEQLENELE 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 213 RLKAAEHRQTILESLKTAGTL-----FGEGFRAFVTDWDKVTATVAGLTLLAVGVYTAKNATAVAGRYIEARLGKPSLVR 287
Cdd:COG4717   238 AAALEERLKEARLLLLIAAALlallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1919013998 288 ETSRITVLEALKHPITVGR-RLASKPQDALEGVVLSPKLEERVRDIAIATRNTKKNKSL 345
Cdd:COG4717   318 EEELEELLAALGLPPDLSPeELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 56-230 6.21e-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: 42.63  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  56 LERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTLNEETRQHQARAQyqd 135
Cdd:pfam15709 348 LEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQ--- 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 136 klaRQRYDDQLRQQQllneenLRKQEESVQKQEAIRRATVEREMEL--RHKNEMLRIEAETRARARAERENAdiirEQIR 213
Cdd:pfam15709 425 ---QEEFRRKLQELQ------RKKQQEEAERAEAEKQRQKELEMQLaeEQKRLMEMAEEERLEYQRQKQEAE----EKAR 491

                         170
                  ....*....|....*..
gi 1919013998 214 LKAAEHRQTILESLKTA 230
Cdd:pfam15709 492 LEAEERRQKEEEAARLA 508
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 97-367 8.12e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 42.06  E-value: 8.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  97 YEAAVEQLKNEQVRIQAEERRKTLNEETRQHQARAQYQDKLARQRYDDQLRQQQLLNEENLRKQEESVQKQEAIRRATVE 176
Cdd:COG1401     1 LLRPVLEFKFLIVGLRLKPLESEDAVRELGIRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 177 REMELRHKNEMLRIEAETRARARAERENADIIREQIRLKAAEHRQTILESLKTagtlfgEGFRAFVTDWDKVTATVAGLT 256
Cdd:COG1401    81 LDLEKVELNEKLALSEAAVAIEELYELEADSEIEAVGLLLELAERSDALEALE------RARLLLELADLEERAALETEV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 257 LLAVGVYTAKNATAVAGRYIEArlgKPSLVRETSRITVLEALKHPITVGRRLASKPQDALEGVVLSPKleervrdiaiat 336
Cdd:COG1401   155 LEALEAELEELLAAPEDLSADA---LAAELSAAEELYSEDLESEDDYLKDLLREKFEETLEAFLAALK------------ 219

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1919013998 337 rnTKKNkslyrnILMYGPPGTGKTLFAKKLA 367
Cdd:COG1401   220 --TKKN------VILAGPPGTGKTYLARRLA 242
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
 347-382 8.76e-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: 40.55  E-value: 8.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1919013998 347 RNILMYGPPGTGKTLFAKKLA-MHSGMDYAIMTGGDV 382
Cdd:cd19504    36 KGILLYGPPGTGKTLMARQIGkMLNAREPKIVNGPEI 72
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
 348-366 9.84e-04

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 40.60  E-value: 9.84e-04
                          10
                  ....*....|....*....
gi 1919013998 348 NILMYGPPGTGKTLFAKKL 366
Cdd:pfam01078  24 NLLMIGPPGSGKTMLAKRL 42
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
349-367 1.04e-03

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 41.95  E-value: 1.04e-03
                          10
                  ....*....|....*....
gi 1919013998 349 ILMYGPPGTGKTLFAKKLA 367
Cdd:COG0465   178 VLLVGPPGTGKTLLAKAVA 196
mukB PRK04863
chromosome partition protein MukB;
125-238 1.06e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.25  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  125 RQHQARAQYQDklARQRYDDQLRQQQLLNEENlRKQEESVQKQEAIRRATVEREMELRHKNEMLRIEAETRARARAEREN 204
Cdd:PRK04863   514 QLQQLRMRLSE--LEQRLRQQQRAERLLAEFC-KRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1919013998  205 ADIIREQIRLKAAEHR--QTILESLktaGTLFGEGF 238
Cdd:PRK04863   591 LQARIQRLAARAPAWLaaQDALARL---REQSGEEF 623
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
 348-415 1.28e-03

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: 39.20  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 348 NILMYGPPGTGKTLFAKKLA------------MHSGMDYAIMTGG-DVAPMGREG-----VTAMhkvfdwantsRRGLLL 409
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaalsnrpvfyvqLTRDTTEEDLFGRrNIDPGGASWvdgplVRAA----------REGEIA 70


                  ....*.
gi 1919013998 410 FVDEAD 415
Cdd:pfam07728  71 VLDEIN 76
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
57-223 1.35e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   57 ERAAKAARELEHSRHAKEALSLAQMQEqtlqleqqsKVKEYEAAVEQLKNEQVRIQAEERRKtlneETRQHQARAQYqDK 136
Cdd:COG4913    262 ERYAAARERLAELEYLRAALRLWFAQR---------RLELLEAELEELRAELARLEAELERL----EARLDALREEL-DE 327

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  137 LARQRYDDQLRQQQLLNEE--NLRKQEESVQKQEAIRRATVER-EMELRHKNEMLrieAETRARARAERENADIIREQIR 213
Cdd:COG4913    328 LEAQIRGNGGDRLEQLEREieRLERELEERERRRARLEALLAAlGLPLPASAEEF---AALRAEAAALLEALEEELEALE 404

                          170
                   ....*....|
gi 1919013998  214 LKAAEHRQTI 223
Cdd:COG4913    405 EALAEAEAAL 414
PRK12704 PRK12704
phosphodiesterase; Provisional
 92-228 1.61e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  92 SKVKEYEA-AVEQLKNEQVRIQAEERRKTLNEETRQHQARAQYQDKLARQRYDDQLRQQQLLN-EENLRKQEESVQKQEa 169
Cdd:PRK12704   31 AKIKEAEEeAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkEENLDRKLELLEKRE- 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998 170 irRATVEREMELRHKNEMLRIEAETRARARAERENadiIREQI-RLKAAEHRQTILESLK 228
Cdd:PRK12704  110 --EELEKKEKELEQKQQELEKKEEELEELIEEQLQ---ELERIsGLTAEEAKEILLEKVE 164
ClpX COG1219
ATP-dependent protease Clp, ATPase subunit ClpX [Posttranslational modification, protein ...
 343-367 2.12e-03

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


Pssm-ID: 440832 [Multi-domain]  Cd Length: 409  Bit Score: 40.80  E-value: 2.12e-03
                          10        20
                  ....*....|....*....|....*
gi 1919013998 343 KSlyrNILMYGPPGTGKTLFAKKLA 367
Cdd:COG1219   109 KS---NILLIGPTGSGKTLLAQTLA 130
YifB COG0606
Predicted Mg-chelatase, contains ChlI-like and ATPase domains, YifB family [Posttranslational ...
 348-366 2.55e-03

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


Pssm-ID: 440371 [Multi-domain]  Cd Length: 502  Bit Score: 40.79  E-value: 2.55e-03
                          10
                  ....*....|....*....
gi 1919013998 348 NILMYGPPGTGKTLFAKKL 366
Cdd:COG0606   213 NLLMIGPPGSGKTMLARRL 231
clpX PRK05342
ATP-dependent Clp protease ATP-binding subunit ClpX;
343-367 2.63e-03

ATP-dependent Clp protease ATP-binding subunit ClpX;


Pssm-ID: 235422 [Multi-domain]  Cd Length: 412  Bit Score: 40.53  E-value: 2.63e-03
                          10        20
                  ....*....|....*....|....*
gi 1919013998 343 KSlyrNILMYGPPGTGKTLFAKKLA 367
Cdd:PRK05342  108 KS---NILLIGPTGSGKTLLAQTLA 129
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 349-369 3.02e-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: 37.58  E-value: 3.02e-03
                          10        20
                  ....*....|....*....|.
gi 1919013998 349 ILMYGPPGTGKTLFAKKLAMH 369
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLARA 21
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 95-184 3.69e-03

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


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 39.58  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  95 KEYEAAVEQLKNEqvriQAEERRKTLNEETRQHQARAQYQDKlarqRYDDQLRQ--------QQLLNEENLRKQEESVQK 166
Cdd:pfam02841 202 KEKAIEAERAKAE----AAEAEQELLREKQKEEEQMMEAQER----SYQEHVKQliekmeaeREQLLAEQERMLEHKLQE 273

                          90
                  ....*....|....*...
gi 1919013998 167 QEAIRRATVEREMELRHK 184
Cdd:pfam02841 274 QEELLKEGFKTEAESLQK 291
PTZ00121 PTZ00121
MAEBL; Provisional
 57-221 3.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 3.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   57 ERAAKAARELEHSRHAKEALSLAQMQEQTLQLEQQSKVKEYEAAVEQLKNEQVRIQAEERRKTLNE-ETRQHQARAQYQD 135
Cdd:PTZ00121  1305 DEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKADAAK 1384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  136 KLARQ-RYDDQLRQQQllnEENLRKQEESVQKQEAIRRA-TVEREMELRHKNEMLRIEAETRARARAERENADIIR--EQ 211
Cdd:PTZ00121  1385 KKAEEkKKADEAKKKA---EEDKKKADELKKAAAAKKKAdEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKkaEE 1461

                          170
                   ....*....|
gi 1919013998  212 IRLKAAEHRQ 221
Cdd:PTZ00121  1462 AKKKAEEAKK 1471
RecA-like_ClpX cd19497
ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent ...
 348-367 8.49e-03

ATP-dependent Clp protease ATP-binding subunit ClpX; ClpX is a component of the ATP-dependent protease ClpXP. In ClpXP, ClpX ATPase serves to specifically recognize, unfold, and translocate protein substrates into the chamber of ClpP protease for degradation. This RecA-like_ClpX domain subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410905 [Multi-domain]  Cd Length: 251  Bit Score: 38.35  E-value: 8.49e-03
                          10        20
                  ....*....|....*....|
gi 1919013998 348 NILMYGPPGTGKTLFAKKLA 367
Cdd:cd19497    52 NILLIGPTGSGKTLLAQTLA 71
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 92-226 9.57e-03

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: 39.27  E-value: 9.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998   92 SKVKEYEAAVEQLK-------NEQVRIQAE-----ERRKTLNEETRQHQARAQY--QDKLARQRYDDQLRQQQLLNEENL 157
Cdd:TIGR02168  260 AELQELEEKLEELRlevseleEEIEELQKElyalaNEISRLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEEL 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1919013998  158 RKQEESVQKQEAIRRATVEREMELRHKNEML-------RIEAETRARARAERE------NADIIREQIRLKAAEHRQTIL 224
Cdd:TIGR02168  340 AELEEKLEELKEELESLEAELEELEAELEELesrleelEEQLETLRSKVAQLElqiaslNNEIERLEARLERLEDRRERL 419


                   ..
gi 1919013998  225 ES 226
Cdd:TIGR02168  420 QQ 421
 
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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