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Conserved domains on  [gi|955080478|ref|NP_001304167|]
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ATPase family AAA domain-containing protein 3B isoform AAA-TOB3s precursor [Homo sapiens]

Protein Classification

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

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

Gene Ontology:  GO:0005524|GO:0016887

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
278-427 9.43e-108

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


:

Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 320.24  E-value: 9.43e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 278 LEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSR 357
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 358 RGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHF 427
Cdd:cd19512   81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
48-240 5.98e-102

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: 309.61  E-value: 5.98e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR--- 124
Cdd:pfam12037  67 KEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqa 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  125 --RATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVT 202
Cdd:pfam12037 147 qrRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLV 226
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 955080478  203 ATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVR 240
Cdd:pfam12037 227 AAVGGLTALAAGVYTAKEGTGVAWRYIEARLGKPSLVR 264
 
Name Accession Description Interval E-value
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
278-427 9.43e-108

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 320.24  E-value: 9.43e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 278 LEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSR 357
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 358 RGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHF 427
Cdd:cd19512   81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
48-240 5.98e-102

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: 309.61  E-value: 5.98e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR--- 124
Cdd:pfam12037  67 KEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqa 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  125 --RATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVT 202
Cdd:pfam12037 147 qrRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLV 226
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 955080478  203 ATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVR 240
Cdd:pfam12037 227 AAVGGLTALAAGVYTAKEGTGVAWRYIEARLGKPSLVR 264
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
114-490 3.86e-34

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: 133.88  E-value: 3.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 114 EESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRA 193
Cdd:COG0464    2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 194 FVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQdVLEGVV 273
Cdd:COG0464   82 LAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA-ILDDLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 274 LSPSLEARVRDIAIATRNTKKNRGLY-----RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR-EGVTA-- 345
Cdd:COG0464  161 GLEEVKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEkn 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 346 MHKLFDWANTSRRGLLLFmDEADAFLRKRaTEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMV 425
Cdd:COG0464  239 LREVFDKARGLAPCVLFI-DEADALAGKR-GEVGDGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEII 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 955080478 426 HFDLPQQEERERLVRLHFdncvlkpategKRRLKLAQFDYgrkcSEVARLTEGMSGREIAQLAVS 490
Cdd:COG0464  317 FFPLPDAEERLEIFRIHL-----------RKRPLDEDVDL----EELAEATEGLSGADIRNVVRR 366
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
302-429 3.17e-24

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 98.05  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEEIS 380
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 955080478  381 KDLRaTLNAFLYHM---GQHSNKFMLVLASNLPEQFDCAINSRIDVMVHFDL 429
Cdd:pfam00004  80 ESRR-VVNQLLTELdgfTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
300-487 2.18e-13

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 73.40  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  300 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEE 378
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  379 ISKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHfdncvlkpateg 454
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIH------------ 634
                         170       180       190
                  ....*....|....*....|....*....|...
gi 955080478  455 KRRLKLAQfdyGRKCSEVARLTEGMSGREIAQL 487
Cdd:TIGR01243 635 TRSMPLAE---DVDLEELAEMTEGYTGADIEAV 664
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
302-487 5.62e-13

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 71.99  E-value: 5.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAMHKLFDWANTSRRgLLLFMDEADAFLRKR-ATEEI 379
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDEIDAVGRQRgAGLGG 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 380 SKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHFdncvlkpateg 454
Cdd:PRK10733 267 GHDEReQTLNQMLVEMdGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILKVHM----------- 335
                        170       180       190
                 ....*....|....*....|....*....|...
gi 955080478 455 kRRLKLaqfDYGRKCSEVARLTEGMSGREIAQL 487
Cdd:PRK10733 336 -RRVPL---APDIDAAIIARGTPGFSGADLANL 364
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
300-430 9.15e-10

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: 57.38  E-value: 9.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   300 RHILLYGPPGTGKTLFAKKLALHSG------------------MDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGlL 361
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   362 LFMDEADAFLRKrateEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCA-INSRIDVMVHFDLP 430
Cdd:smart00382  82 LILDEITSLLDA----EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 147
PTZ00121 PTZ00121
MAEBL; Provisional
51-176 7.01e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 7.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   51 EAAVEQLKSEQIRaQAEERRKtlSEETRQHQaRAQYQDKLarQRYEDQLKQQQLLNEENLRKQEEsVQKQEAMRRATVER 130
Cdd:PTZ00121 1504 KAAEAKKKADEAK-KAEEAKK--ADEAKKAE-EAKKADEA--KKAEEKKKADELKKAEELKKAEE-KKKAEEAKKAEEDK 1576
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 955080478  131 EMELRhKNEMLRVETEAR-----------ARAKAER----ENADIIREQIRlKASEHRQTV 176
Cdd:PTZ00121 1577 NMALR-KAEEAKKAEEARieevmklyeeeKKMKAEEakkaEEAKIKAEELK-KAEEEKKKV 1635
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
46-169 1.03e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 51.41  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  46 ALQEYEAAVEQLKSEQI-------RAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQ 118
Cdd:COG2268  217 AQANREAEEAELEQEREietariaEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQE 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 955080478 119 KQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKA 169
Cdd:COG2268  297 KEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALA 347
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
25-169 9.18e-06

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.92  E-value: 9.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   25 QTQERLSGSASPEQVPAGEccALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyqDKLARQRYEDQLKQQQL 104
Cdd:TIGR02794  54 RIQQQKKPAAKKEQERQKK--LEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK--QAEEKQKQAEEAKAKQA 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 955080478  105 ------LNEENLRKQEESVQKQ---EAMRRATVEREMELRHKNEMLRVETEAR--ARAKAERENADIIREQIRLKA 169
Cdd:TIGR02794 130 aeakakAEAEAERKAKEEAAKQaeeEAKAKAAAEAKKKAEEAKKKAEAEAKAKaeAEAKAKAEEAKAKAEAAKAKA 205
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
48-129 2.45e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478    48 QEYEAAVEQLKSEQIRAQAEerRKTLSEEtrqhqARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRAT 127
Cdd:smart00935  32 AELEKLEKELQKLKEKLQKD--AATLSEA-----AREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQKILDKINKAI 104

                   ..
gi 955080478   128 VE 129
Cdd:smart00935 105 KE 106
growth_prot_Scy NF041483
polarized growth protein Scy;
20-182 7.53e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.42  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   20 RAGAVQTQERLSGSASPEQVPAGECCA------LQEYEAAVEQLK------SEQIRAQAEERRKTLseetrqhqaRAQYQ 87
Cdd:NF041483  453 RAEAVAEGERIRGEARREAVQQIEEAArtaeelLTKAKADADELRstataeSERVRTEAIERATTL---------RRQAE 523
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   88 DKLARQRYE-DQLKQQQLLNEENLRKQEESVQKQeamRRATVEREMELRHK---NEMLRVETEARARAKAERENADIIR- 162
Cdd:NF041483  524 ETLERTRAEaERLRAEAEEQAEEVRAAAERAARE---LREETERAIAARQAeaaEELTRLHTEAEERLTAAEEALADARa 600
                         170       180
                  ....*....|....*....|....*.
gi 955080478  163 --EQIRLKASEH----RQTVLESIRT 182
Cdd:NF041483  601 eaERIRREAAEEterlRTEAAERIRT 626
 
Name Accession Description Interval E-value
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
278-427 9.43e-108

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 320.24  E-value: 9.43e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 278 LEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSR 357
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 358 RGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHF 427
Cdd:cd19512   81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
48-240 5.98e-102

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: 309.61  E-value: 5.98e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR--- 124
Cdd:pfam12037  67 KEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELLRKQEESVAKQEAMRiqa 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  125 --RATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVT 202
Cdd:pfam12037 147 qrRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINTAGSHIGGGLRALLTDWDKLV 226
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 955080478  203 ATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVR 240
Cdd:pfam12037 227 AAVGGLTALAAGVYTAKEGTGVAWRYIEARLGKPSLVR 264
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
114-490 3.86e-34

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: 133.88  E-value: 3.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 114 EESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRA 193
Cdd:COG0464    2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 194 FVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQdVLEGVV 273
Cdd:COG0464   82 LAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA-ILDDLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 274 LSPSLEARVRDIAIATRNTKKNRGLY-----RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR-EGVTA-- 345
Cdd:COG0464  161 GLEEVKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEkn 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 346 MHKLFDWANTSRRGLLLFmDEADAFLRKRaTEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMV 425
Cdd:COG0464  239 LREVFDKARGLAPCVLFI-DEADALAGKR-GEVGDGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEII 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 955080478 426 HFDLPQQEERERLVRLHFdncvlkpategKRRLKLAQFDYgrkcSEVARLTEGMSGREIAQLAVS 490
Cdd:COG0464  317 FFPLPDAEERLEIFRIHL-----------RKRPLDEDVDL----EELAEATEGLSGADIRNVVRR 366
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
278-427 9.90e-34

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: 125.86  E-value: 9.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 278 LEARVRDIAIATRNTKKNR----GLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDW 352
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRryglGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVgESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 955080478 353 ANTSRRGLLLFmDEADAFLRKRATEEISKDLRATLNAFLYHM--GQHSNKFMLVLASNLPEQFDCAINS--RIDVMVHF 427
Cdd:cd19481   81 ARRLAPCILFI-DEIDAIGRKRDSSGESGELRRVLNQLLTELdgVNSRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
269-524 1.83e-30

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 119.60  E-value: 1.83e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 269 LEGVVLSPSLEARVRDIAIATRNTKKNR--GLY--RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---E 341
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRkfGLWppRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSylgE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 342 GVTAMHKLFDWANtsRRGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRI 421
Cdd:COG1223   79 TARNLRKLFDFAR--RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALWRRF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 422 DVMVHFDLPQQEERERLVrlhfdncvlkpategKRRLKLAQFDYGRKCSEVARLTEGMSGREIAQLAVSWQATAYASKDG 501
Cdd:COG1223  157 DEVIEFPLPDKEERKEIL---------------ELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDRE 221
                        250       260
                 ....*....|....*....|...
gi 955080478 502 VLTEAMmdacVQDAVQQYRQKMR 524
Cdd:COG1223  222 KVTKED----LEEALKQRKERKK 240
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
294-524 2.69e-26

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 109.71  E-value: 2.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 294 KNRGLYRH--------ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRGLLLF 363
Cdd:COG1222   99 KNPELFRKygieppkgVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKyiG-EGARNVREVFELAREKAPSIIFI 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 364 mDEADAFLRKRATEEISKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLV 439
Cdd:COG1222  178 -DEIDAIAARRTDDGTSGEVQRTVNQLLAELdGFESRGDVLIIaATNRPDLLDPALlrPGRFDRVIEVPLPDEEAREEIL 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 440 RLHFdncvlkpategkRRLKLA-QFDYgrkcSEVARLTEGMSGREIAQLAVswQATAYASKDGVLTEAMMDacVQDAVQQ 518
Cdd:COG1222  257 KIHL------------RDMPLAdDVDL----DKLAKLTEGFSGADLKAIVT--EAGMFAIREGRDTVTMED--LEKAIEK 316

                 ....*.
gi 955080478 519 YRQKMR 524
Cdd:COG1222  317 VKKKTE 322
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
302-429 3.17e-24

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


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 98.05  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEEIS 380
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 955080478  381 KDLRaTLNAFLYHM---GQHSNKFMLVLASNLPEQFDCAINSRIDVMVHFDL 429
Cdd:pfam00004  80 ESRR-VVNQLLTELdgfTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
300-487 2.18e-13

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


Pssm-ID: 273521 [Multi-domain]  Cd Length: 733  Bit Score: 73.40  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  300 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEE 378
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  379 ISKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHfdncvlkpateg 454
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIH------------ 634
                         170       180       190
                  ....*....|....*....|....*....|...
gi 955080478  455 KRRLKLAQfdyGRKCSEVARLTEGMSGREIAQL 487
Cdd:TIGR01243 635 TRSMPLAE---DVDLEELAEMTEGYTGADIEAV 664
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
302-487 5.62e-13

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 71.99  E-value: 5.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAMHKLFDWANTSRRgLLLFMDEADAFLRKR-ATEEI 379
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDEIDAVGRQRgAGLGG 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 380 SKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHFdncvlkpateg 454
Cdd:PRK10733 267 GHDEReQTLNQMLVEMdGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILKVHM----------- 335
                        170       180       190
                 ....*....|....*....|....*....|...
gi 955080478 455 kRRLKLaqfDYGRKCSEVARLTEGMSGREIAQL 487
Cdd:PRK10733 336 -RRVPL---APDIDAAIIARGTPGFSGADLANL 364
RecA-like_VPS4-like cd19509
ATPase domain of VPS4, ATAD1, K, KTNA1, Spastin, FIGL-1 and similar ATPase domains; This ...
295-420 9.92e-13

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: 66.22  E-value: 9.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 295 NRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVA--PMGrEGVTAMHKLFDWANtSRRGLLLFMDEADAFLR 372
Cdd:cd19509   28 LRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVskWVG-ESEKIVRALFALAR-ELQPSIIFIDEIDSLLS 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 955080478 373 KRATEEISKDLRATlNAFLYHM----GQHSNKFMLVLASNLPEQFDCAINSR 420
Cdd:cd19509  106 ERGSGEHEASRRVK-TEFLVQMdgvlNKPEDRVLVLGATNRPWELDEAFLRR 156
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
300-417 1.54e-12

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


Pssm-ID: 410909 [Multi-domain]  Cd Length: 171  Bit Score: 66.10  E-value: 1.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTA--MHKLFDWANTSRRgLLLFMDEADAFLRKRATE 377
Cdd:cd19501   38 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGAsrVRDLFEQAKKNAP-CIVFIDEIDAVGRKRGAG 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 955080478 378 EI-SKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI 417
Cdd:cd19501  116 LGgGHDEReQTLNQLLVEMdGFESNTGVIVIaATNRPDVLDPAL 159
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
283-429 1.67e-12

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: 65.25  E-value: 1.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 283 RDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYA---------IMTGGDVApmGREGVTAMHKLFDwA 353
Cdd:cd00009    3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGApflylnasdLLEGLVVA--ELFGHFLVRLLFE-L 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955080478 354 NTSRRGLLLFMDEADAFlrkraTEEISKDLRATLNAFLYHMGQHSNkFMLVLASNLPE--QFDCAINSRIDVMVHFDL 429
Cdd:cd00009   80 AEKAKPGVLFIDEIDSL-----SRGAQNALLRVLETLNDLRIDREN-VRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
ftsH CHL00176
cell division protein; Validated
302-488 4.70e-12

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 68.92  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTA--MHKLFDWANtSRRGLLLFMDEADAFLRKRATE-E 378
Cdd:CHL00176 219 VLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM-FVGVGAarVRDLFKKAK-ENSPCIVFIDEIDAVGRQRGAGiG 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 379 ISKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHFDNCVLKPATE 453
Cdd:CHL00176 297 GGNDEReQTLNQLLTEMdGFKGNKGVIVIaATNRVDILDAALlrPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVS 376
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 955080478 454 gkrrLKLaqfdygrkcseVARLTEGMSGREIAQLA 488
Cdd:CHL00176 377 ----LEL-----------IARRTPGFSGADLANLL 396
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
295-422 9.19e-12

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: 63.73  E-value: 9.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 295 NRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAMHKLFDWANTSRRGlLLFMDEADAFLR 372
Cdd:cd19521   36 NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSkwMG-ESEKLVKQLFAMARENKPS-IIFIDEVDSLCG 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 955080478 373 KRATEEiSKDLRATLNAFLYHM---GQHSNKFMLVLASNLPEQFDCAINSRID 422
Cdd:cd19521  114 TRGEGE-SEASRRIKTELLVQMngvGNDSQGVLVLGATNIPWQLDSAIRRRFE 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
302-475 3.72e-11

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: 66.08  E-value: 3.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR--AT 376
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI--MSKyygESEERLREIFKEAEENAPS-IIFIDEIDAIAPKReeVT 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  377 EEISKDLRATLNAFLYHMgQHSNKFMLVLASNLPEQFDCAIN--SRIDVMVHFDLPQQEERERLVRLHFDNcvlKPATEG 454
Cdd:TIGR01243 292 GEVEKRVVAQLLTLMDGL-KGRGRVIVIGATNRPDALDPALRrpGRFDREIVIRVPDKRARKEILKVHTRN---MPLAED 367
                         170       180
                  ....*....|....*....|.
gi 955080478  455 KRRLKLAQFDYGRKCSEVARL 475
Cdd:TIGR01243 368 VDLDKLAEVTHGFVGADLAAL 388
RecA-like_CDC48_r2-like cd19511
second of two ATPase domains of CDC48/p97, PEX1 and -6, VAT and NVL, and similar ATPase ...
302-426 1.78e-10

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


Pssm-ID: 410919 [Multi-domain]  Cd Length: 159  Bit Score: 59.60  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEEI 379
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKyvG-ESERAVREIFQKARQAAPC-IIFFDEIDSLAPRRGQSDS 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 955080478 380 SKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVH 426
Cdd:cd19511  108 SGVTDRVVSQLLTELdGIESLKGVVVIaATNRPDMIDPALlrPGRLDKLIY 158
RecA-like_NVL_r2-like cd19530
second of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
302-417 3.56e-10

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


Pssm-ID: 410938 [Multi-domain]  Cd Length: 161  Bit Score: 59.04  E-value: 3.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATEEI 379
Cdd:cd19530   33 VLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKyvG-ESERAVRQVFQRARASAP-CVIFFDEVDALVPKRGDGGS 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 955080478 380 SKDLRaTLNAFLYHM--GQHSNKFMLVLASNLPEQFDCAI 417
Cdd:cd19530  111 WASER-VVNQLLTEMdgLEERSNVFVIAATNRPDIIDPAM 149
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
300-430 9.15e-10

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: 57.38  E-value: 9.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   300 RHILLYGPPGTGKTLFAKKLALHSG------------------MDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGlL 361
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   362 LFMDEADAFLRKrateEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCA-INSRIDVMVHFDLP 430
Cdd:smart00382  82 LILDEITSLLDA----EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPAlLRRRFDRRIVLLLI 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 ...
300-417 1.20e-09

first of two ATPase domains of CDC48 and NLV2, and similar ATPase domains; CDC48 in yeast and p97 or VCP metazoans is an ATP-dependent molecular chaperone which plays an essential role in many cellular processes, by segregating polyubiquitinated proteins from complexes or membranes. Cdc48/p97 consists of an N-terminal domain and two ATPase domains; this subfamily represents the first of the two ATPase domains. This subfamily also includes the first of the two ATPase domains of NVL (nuclear VCP-like protein) 2, an isoform of NVL mainly present in the nucleolus, which is involved in ribosome biogenesis, in telomerase assembly and the regulation of telomerase activity, and in pre-rRNA processing. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410911 [Multi-domain]  Cd Length: 165  Bit Score: 57.30  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRAT 376
Cdd:cd19503   35 RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSI--VSKylgESEKNLREIFEEARSHAPS-IIFIDEIDALAPKREE 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 955080478 377 --EEISKDLRATLNAFLYHMGQhSNKFMLVLASNLPEQFDCAI 417
Cdd:cd19503  112 dqREVERRVVAQLLTLMDGMSS-RGKVVVIAATNRPDAIDPAL 153
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
302-427 1.47e-09

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


Pssm-ID: 410910 [Multi-domain]  Cd Length: 171  Bit Score: 57.35  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKLFDWANTsRRGLLLFMDEADAFLRKRATEEIS 380
Cdd:cd19502   40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSElVQKYIGEGARLVRELFEMARE-KAPSIIFIDEIDAIGAKRFDSGTG 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 955080478 381 KD--LRATLNAFLYHMG--QHSNKFMLVLASNLPEQFDCAI--NSRIDVMVHF 427
Cdd:cd19502  119 GDreVQRTMLELLNQLDgfDPRGNIKVIMATNRPDILDPALlrPGRFDRKIEF 171
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
302-489 3.36e-09

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 59.08  E-value: 3.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTG--------GDVAPMGREgvtamhkLFDWANtSRRGLLLFMDEADAFLRK 373
Cdd:PRK03992 168 VLLYGPPGTGKTLLAKAVAHETNATFIRVVGselvqkfiGEGARLVRE-------LFELAR-EKAPSIIFIDEIDAIAAK 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 374 RATEEISKD--LRATLNAFLYHMGQHSNK--FMLVLASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHfdncv 447
Cdd:PRK03992 240 RTDSGTSGDreVQRTLMQLLAEMDGFDPRgnVKIIAATNRIDILDPAIlrPGRFDRIIEVPLPDEEGRLEILKIH----- 314
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 955080478 448 lkpategKRRLKLAQ-FDYgrkcSEVARLTEGMSGREIAQLAV 489
Cdd:PRK03992 315 -------TRKMNLADdVDL----EELAELTEGASGADLKAICT 346
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
300-417 8.87e-09

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: 55.13  E-value: 8.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR--AT 376
Cdd:cd19519   35 RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEImSKLAGESESNLRKAFEEAEKNAPA-IIFIDEIDAIAPKRekTH 113
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 955080478 377 EEISKDLRATLNAFLYHMGQHSNkFMLVLASNLPEQFDCAI 417
Cdd:cd19519  114 GEVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPAL 153
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
300-426 8.93e-09

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 54.82  E-value: 8.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATe 377
Cdd:cd19528   28 KGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMwfG-ESEANVRDIFDKARAAAP-CVLFFDELDSIAKARGG- 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 955080478 378 EISKDLRAT---LNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVH 426
Cdd:cd19528  105 NIGDAGGAAdrvINQILTEMdGMNTKKNVFIIgATNRPDIIDPAIlrPGRLDQLIY 160
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
296-422 1.37e-08

Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is the catalytic subunit of the Katanin complex which is severs microtubules in an ATP-dependent manner, and is implicated in multiple aspects of microtubule dynamics. In addition to the p60 catalytic ATPase subunit, Katanin contains an accessory subunit (p80 or p80-like). The microtubule-severing activity of the ATPase is essential for female meiotic spindle assembly, and male gamete production; and the katanin complex severing microtubules is under tight regulation during the transition from the meiotic to mitotic stage to allow proper embryogenesis. This subfamily belongs to the RecA-like NTPase family which includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. The RecA-like NTPase family also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410930 [Multi-domain]  Cd Length: 170  Bit Score: 54.61  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 296 RGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR 374
Cdd:cd19522   30 RRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRgESEKLVRLLFEMARFYAPT-TIFIDEIDSICSRR 108
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 955080478 375 ATEEISKDLRATLNAFLYHM--------GQHSNKFMLVL-ASNLPEQFDCAINSRID 422
Cdd:cd19522  109 GTSEEHEASRRVKSELLVQMdgvggaseNDDPSKMVMVLaATNFPWDIDEALRRRLE 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
300-417 7.33e-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: 52.11  E-value: 7.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATE 377
Cdd:cd19529   28 KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSkwVG-ESEKAIREIFRKARQVAP-CVIFFDEIDSIAPRRGTT 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 955080478 378 EISKDLRATLNAFLYHMG--QHSNKFMLVLASNLPEQFDCAI 417
Cdd:cd19529  106 GDSGVTERVVNQLLTELDglEEMNGVVVIAATNRPDIIDPAL 147
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
55-183 1.01e-07

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: 55.13  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   55 EQLKSEQIRAQAEERRKT---LSEETRQHQARAQYQDKLARQRYEDQLKQQ---QLLNEENLRKQEESVQKQEAMRRATV 128
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQRevrRLEEERAREMERVRLEEQERQQQVERLRQQeeeRKRKKLELEKEKRDRKRAEEQRRKIL 497
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 955080478  129 EREMELR--------HKNEMLRVETEARARAKAERENADIIREQIRL-KASEHRQTVLESIRTA 183
Cdd:pfam17380 498 EKELEERkqamieeeRKRKLLEKEMEERQKAIYEEERRREAEEERRKqQEMEERRRIQEQMRKA 561
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
302-421 1.30e-07

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


Pssm-ID: 410928 [Multi-domain]  Cd Length: 166  Bit Score: 51.66  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMtggDVAPMGREGVTAMHKLFDWANTSRRGL---LLFMDEADAFLRKRAT-- 376
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEAGARFINL---QVSSLTDKWYGESQKLVAAVFSLASKLqpsIIFIDEIDSFLRQRSStd 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 955080478 377 EEISKDLRATLNAFLYHMGQHSNKFMLVL-ASNLPEQFDCAINSRI 421
Cdd:cd19520  115 HEATAMMKAEFMSLWDGLSTDGNCRVIVMgATNRPQDLDEAILRRM 160
RecA-like_Figl-1 cd19525
ATPase domain of Fidgetin-Like 1 (FIGL-1); FIGL-1 may participate in DNA repair in the nucleus; ...
296-421 1.87e-07

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


Pssm-ID: 410933 [Multi-domain]  Cd Length: 186  Bit Score: 51.53  E-value: 1.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 296 RGLYRHILLYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR 374
Cdd:cd19525   52 RGPPKGILLFGPPGTGKTLIGKCIASQSGATfFSISASSLTSKWVGEGEKMVRALFSVARCKQPA-VIFIDEIDSLLSQR 130
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 955080478 375 --ATEEISKDLRATLNAFLYHMGQHSNKFMLVL-ASNLPEQFDCAINSRI 421
Cdd:cd19525  131 geGEHESSRRIKTEFLVQLDGATTSSEDRILVVgATNRPQEIDEAARRRL 180
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
300-449 2.53e-07

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 53.23  E-value: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR---- 374
Cdd:PTZ00454 180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEfVQKYLGEGPRMVRDVFRLARENAPS-IIFIDEVDSIATKRfdaq 258
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 955080478 375 --ATEEISKDLRATLNAfLYHMGQHSNkFMLVLASNLPEQFDCAI--NSRIDVMVHFDLPQQEERerlvRLHFDNCVLK 449
Cdd:PTZ00454 259 tgADREVQRILLELLNQ-MDGFDQTTN-VKVIMATNRADTLDPALlrPGRLDRKIEFPLPDRRQK----RLIFQTITSK 331
RecA-like_NVL_r1-like cd19518
first of two ATPase domains of NVL (nuclear VCP-like protein) and similar ATPase domains; NVL ...
300-417 2.85e-07

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


Pssm-ID: 410926 [Multi-domain]  Cd Length: 169  Bit Score: 50.87  E-value: 2.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAMHKLFDWAnTSRRGLLLFMDEADAFLRKRatEE 378
Cdd:cd19518   35 RGVLLHGPPGCGKTMLANAIAGELKVPfLKISATEIVSGVSGESEEKIRELFDQA-ISNAPCIVFIDEIDAITPKR--ES 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 955080478 379 ISKDL-RATLNAFLYHMGQHSN-----KFMLVL-ASNLPEQFDCAI 417
Cdd:cd19518  112 AQREMeRRIVSQLLTCMDELNNektagGPVLVIgATNRPDSLDPAL 157
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
300-421 5.18e-07

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: 49.85  E-value: 5.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDY-----AIMTGGDVApmgrEGVTAMHKLFDWAnTSRRGLLLFMDEADAFLRKR 374
Cdd:cd19524   34 RGLLLFGPPGNGKTMLAKAVAAESNATFfnisaASLTSKYVG----EGEKLVRALFAVA-RELQPSIIFIDEVDSLLSER 108
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 955080478 375 ATEEISKDLRATLNAFLYHMGQHSNKFMLVL---ASNLPEQFDCAINSRI 421
Cdd:cd19524  109 SEGEHEASRRLKTEFLIEFDGVQSNGDDRVLvmgATNRPQELDDAVLRRF 158
PTZ00121 PTZ00121
MAEBL; Provisional
51-176 7.01e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 7.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   51 EAAVEQLKSEQIRaQAEERRKtlSEETRQHQaRAQYQDKLarQRYEDQLKQQQLLNEENLRKQEEsVQKQEAMRRATVER 130
Cdd:PTZ00121 1504 KAAEAKKKADEAK-KAEEAKK--ADEAKKAE-EAKKADEA--KKAEEKKKADELKKAEELKKAEE-KKKAEEAKKAEEDK 1576
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 955080478  131 EMELRhKNEMLRVETEAR-----------ARAKAER----ENADIIREQIRlKASEHRQTV 176
Cdd:PTZ00121 1577 NMALR-KAEEAKKAEEARieevmklyeeeKKMKAEEakkaEEAKIKAEELK-KAEEEKKKV 1635
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
46-169 1.03e-06

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 51.41  E-value: 1.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  46 ALQEYEAAVEQLKSEQI-------RAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQ 118
Cdd:COG2268  217 AQANREAEEAELEQEREietariaEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQE 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 955080478 119 KQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKA 169
Cdd:COG2268  297 KEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALA 347
PTZ00121 PTZ00121
MAEBL; Provisional
53-181 1.23e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   53 AVEQLKSEQIRAQAEERRKtlSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREM 132
Cdd:PTZ00121 1453 AEEAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKA 1530
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 955080478  133 ELRHKNEmlrveteaRARAKAERENADIIREQIRLKASEHRQTVLESIR 181
Cdd:PTZ00121 1531 EEAKKAD--------EAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK 1571
PTZ00121 PTZ00121
MAEBL; Provisional
37-178 1.35e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   37 EQVPAGECCALQEYEAAVEQLKSEQIRAQAEERR---KTLSEETRQHQAR-AQYQDKLARQRYEDQLK---QQQLLNEEN 109
Cdd:PTZ00121 1532 EAKKADEAKKAEEKKKADELKKAEELKKAEEKKKaeeAKKAEEDKNMALRkAEEAKKAEEARIEEVMKlyeEEKKMKAEE 1611
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 955080478  110 LRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENaDIIREQIRLKASEHRQTVLE 178
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEN-KIKAAEEAKKAEEDKKKAEE 1679
PTZ00121 PTZ00121
MAEBL; Provisional
55-181 1.39e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   55 EQLKSEQIRAQAEERRKtlSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEE---NLRKQEESVQKQEAMRRATVER- 130
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIK--AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEeenKIKAAEEAKKAEEDKKKAEEAKk 1682
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 955080478  131 -EMELRHKNEML-RVETEARARAKAERENADIIR--EQIRlKASEHRQTVLESIR 181
Cdd:PTZ00121 1683 aEEDEKKAAEALkKEAEEAKKAEELKKKEAEEKKkaEELK-KAEEENKIKAEEAK 1736
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
46-183 1.43e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  46 ALQEYEAAVEQLKSE--QIRAQAEERRKTLSEETRQhQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAM 123
Cdd:COG1196  261 ELAELEAELEELRLEleELELELEEAQAEEYELLAE-LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 124 RRATVEREMELrhknEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTA 183
Cdd:COG1196  340 EELEEELEEAE----EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAA 395
PTZ00121 PTZ00121
MAEBL; Provisional
46-178 1.58e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   46 ALQEYEAAVEQLKSEQIRAQaEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN--EENLRKQEESVQKQEAM 123
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKkaEEDKKKAEEAKKAEEDE 1687
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955080478  124 RRA--TVEREMELRHKNEMLRVETEARARA-----KAERENaDIIREQIRLKASEHRQTVLE 178
Cdd:PTZ00121 1688 KKAaeALKKEAEEAKKAEELKKKEAEEKKKaeelkKAEEEN-KIKAEEAKKEAEEDKKKAEE 1748
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
302-442 2.35e-06

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 50.15  E-value: 2.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR--ATEE 378
Cdd:PTZ00361 220 VILYGPPGTGKTLLAKAVANETSATFLRVVGSElIQKYLGDGPKLVRELFRVAEENAPS-IVFIDEIDAIGTKRydATSG 298
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955080478 379 ISKDLRATLNAFLYHMG--QHSNKFMLVLASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLH 442
Cdd:PTZ00361 299 GEKEIQRTMLELLNQLDgfDSRGDVKVIMATNRIESLDPALirPGRIDRKIEFPNPDEKTKRRIFEIH 366
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
47-183 2.45e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  47 LQEYEAAVEQLKSEQIRAQAEER-RKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRR 125
Cdd:COG1196  241 LEELEAELEELEAELEELEAELAeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 955080478 126 AtverEMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTA 183
Cdd:COG1196  321 L----EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
47-178 3.16e-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: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  47 LQEYEAAVEQLKSEqiRAQAEeRRKTLSEETRQHQARAQ-YQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRR 125
Cdd:COG1196  195 LGELERQLEPLERQ--AEKAE-RYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 955080478 126 ATVEREmELRHKNEMLRvETEARARAKAERENADIIREQIRLKASEHRQTVLE 178
Cdd:COG1196  272 LRLELE-ELELELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERLEELE 322
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
46-183 3.85e-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: 3.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  46 ALQEYEAAVEQLKSEQIRAQAEERRK-TLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR 124
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAeEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 955080478 125 RATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTA 183
Cdd:COG1196  432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
PTZ00121 PTZ00121
MAEBL; Provisional
58-181 3.92e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   58 KSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQ--RYEDQLKQQQLLNEENLRKQEEsVQKQEAMRRATVEREMELR 135
Cdd:PTZ00121 1491 KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADE-LKKAEELKKAEEKKKAEEA 1569
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 955080478  136 HKNE------MLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIR 181
Cdd:PTZ00121 1570 KKAEedknmaLRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621
PTZ00121 PTZ00121
MAEBL; Provisional
55-181 4.13e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.14  E-value: 4.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   55 EQLKSEQIRAQAEERRKTlSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLR--KQEESVQKQEAMRRATVEREM 132
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKA-AEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENkiKAEEAKKEAEEDKKKAEEAKK 1751
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 955080478  133 ELRHKNEMLRVETEARARAKAER-ENADIIREQIRLKASEHRQTVLESIR 181
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRkEKEAVIEEELDEEDEKRRMEVDKKIK 1801
PTZ00121 PTZ00121
MAEBL; Provisional
37-198 5.47e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 5.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   37 EQVPAGECCALQEYEAAVEQLK-SEQIRaQAEERRKtlSEETRQ-HQARAQYQDKLAR--QRYEDQLKQQQLLNEENLRK 112
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKkAEDAR-KAEEARK--AEDARKaEEARKAEDAKRVEiaRKAEDARKAEEARKAEDAKK 1177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  113 QEES-----VQKQEAMRRATVEREMELRHKNEMLRVETEARaRAKAERENADIIR-EQIRLKASEHRQTVLESIRTAGTL 186
Cdd:PTZ00121 1178 AEAArkaeeVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRK 1256
                         170
                  ....*....|..
gi 955080478  187 FGEGFRAFVTDR 198
Cdd:PTZ00121 1257 FEEARMAHFARR 1268
PTZ00121 PTZ00121
MAEBL; Provisional
55-183 5.61e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 5.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   55 EQLKSEQIRAQAEERRKtlSEETRqhqaRAQYQDKL-ARQRYEDQLKQQQLLNEENLRKQE-----ESVQKQEAMRRATV 128
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARK--AEEAR----KAEDAKKAeAARKAEEVRKAEELRKAEDARKAEaarkaEEERKAEEARKAED 1222
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 955080478  129 EREMELRHKNEMLRVETEARARAKAERENADI-----------IREQIRLKASEHRQTvlESIRTA 183
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIrkfeearmahfARRQAAIKAEEARKA--DELKKA 1286
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
46-179 5.96e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  46 ALQEYEAAVEQLKsEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRR 125
Cdd:COG1196  289 EEYELLAELARLE-QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 955080478 126 ATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLES 179
Cdd:COG1196  368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
PTZ00121 PTZ00121
MAEBL; Provisional
51-183 6.59e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.37  E-value: 6.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   51 EAAVEQLKSEQIRAQAEERRKTlsEETRQHQARaqyQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAmRRATVER 130
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKT--ETGKAEEAR---KAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDA-KRVEIAR 1158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 955080478  131 EMELRHKNEMLRVETEARaRAKAERENADIIR-EQIRlKASEHRQtvLESIRTA 183
Cdd:PTZ00121 1159 KAEDARKAEEARKAEDAK-KAEAARKAEEVRKaEELR-KAEDARK--AEAARKA 1208
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
46-183 8.46e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 8.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  46 ALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyqdKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRR 125
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 955080478 126 ATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTA 183
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
25-169 9.18e-06

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 47.92  E-value: 9.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   25 QTQERLSGSASPEQVPAGEccALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyqDKLARQRYEDQLKQQQL 104
Cdd:TIGR02794  54 RIQQQKKPAAKKEQERQKK--LEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK--QAEEKQKQAEEAKAKQA 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 955080478  105 ------LNEENLRKQEESVQKQ---EAMRRATVEREMELRHKNEMLRVETEAR--ARAKAERENADIIREQIRLKA 169
Cdd:TIGR02794 130 aeakakAEAEAERKAKEEAAKQaeeEAKAKAAAEAKKKAEEAKKKAEAEAKAKaeAEAKAKAEEAKAKAEAAKAKA 205
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
55-174 9.19e-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: 48.58  E-value: 9.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   55 EQLKSEQIRAQAEE------RRKTLSEETRQHQARAQYQ-------DKLA--RQRYEDQLKQQQLLNEENLRKQEESVQK 119
Cdd:pfam17380 294 EKMEQERLRQEKEEkareveRRRKLEEAEKARQAEMDRQaaiyaeqERMAmeRERELERIRQEERKRELERIRQEEIAME 373
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 955080478  120 QEAMRRatVER-EMELRHKNEMLRVETEARARAK-AERENADIIREQ------IRLKASEHRQ 174
Cdd:pfam17380 374 ISRMRE--LERlQMERQQKNERVRQELEAARKVKiLEEERQRKIQQQkvemeqIRAEQEEARQ 434
PTZ00121 PTZ00121
MAEBL; Provisional
51-174 9.43e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 9.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   51 EAAVEQLKSEQIRAQAEERRKtlSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATver 130
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD--- 1486
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 955080478  131 emELRHKNEMLRVETEARARAKAERENADIIR--EQIRlKASEHRQ 174
Cdd:PTZ00121 1487 --EAKKKAEEAKKKADEAKKAAEAKKKADEAKkaEEAK-KADEAKK 1529
PTZ00121 PTZ00121
MAEBL; Provisional
48-174 1.04e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRAT 127
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEE 1300
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 955080478  128 VEREMELRHKNEMLRVETEARARAKAERENADIIREqirlKASEHRQ 174
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK----KAEEAKK 1343
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
302-426 1.15e-05

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


Pssm-ID: 410935 [Multi-domain]  Cd Length: 160  Bit Score: 45.97  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAMHKLFDWANTSrRGLLLFMDEADAFLRKRATEEIS 380
Cdd:cd19527   29 ILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYiGESEANVREVFQKARDA-KPCVIFFDELDSLAPSRGNSGDS 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 955080478 381 KDLR----ATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAI--NSRIDVMVH 426
Cdd:cd19527  108 GGVMdrvvSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALlrPGRFDKLLY 159
PTZ00121 PTZ00121
MAEBL; Provisional
58-174 1.99e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.83  E-value: 1.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   58 KSEQIRAQAEERRKTLSEETRQHQARAQYQDKL----ARQRYEDQLKQQQLLNE-ENLRKQEESVQKQEAMRRATverem 132
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkadeAKKKAEEAKKADEAKKKaEEAKKAEEAKKKAEEAKKAD----- 1473
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 955080478  133 ELRHKNEMLRVETEARARAKAERENADIIR--EQIRLKASEHRQ 174
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKkaAEAKKKADEAKK 1517
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
48-209 2.45e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKS-EQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEdQLKQQQLLNEENLRKQEESVQKQEAMRRA 126
Cdd:COG4913   242 EALEDAREQIELlEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLEARLDA 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  127 TVEREMELRhkNEMLRVETEARARAKAERENADIIREQIRLKasehRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATVA 206
Cdd:COG4913   321 LREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERR----RARLEALLAALGLPLPASAEEFAALRAEAAALLE 394

                  ...
gi 955080478  207 GLT 209
Cdd:COG4913   395 ALE 397
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
300-417 2.90e-05

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


Pssm-ID: 410925 [Multi-domain]  Cd Length: 170  Bit Score: 44.81  E-value: 2.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDyaimtGGDVAPMGREGVTAMHKlfdWANTSRRGL-------------LLFMDE 366
Cdd:cd19517   35 RGVLFHGPPGTGKTLMARALAAECSKG-----GQKVSFFMRKGADCLSK---WVGEAERQLrllfeeayrmqpsIIFFDE 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 955080478 367 AD--AFLRKRATEEISKDLRATLNAFLYHMgQHSNKFMLVLASNLPEQFDCAI 417
Cdd:cd19517  107 IDglAPVRSSKQEQIHASIVSTLLALMDGL-DNRGQVVVIGATNRPDALDPAL 158
PTZ00121 PTZ00121
MAEBL; Provisional
34-166 3.21e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   34 ASPEQVPAGECCALQEYEAAVEQL---------KSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQL 104
Cdd:PTZ00121 1615 AEEAKIKAEELKKAEEEKKKVEQLkkkeaeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAL 1694
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  105 LNE-------ENLRK-QEESVQKQEAMRRATVER----------EMELRHKNEMLRVETEARARAKAERENADIIREQIR 166
Cdd:PTZ00121 1695 KKEaeeakkaEELKKkEAEEKKKAEELKKAEEENkikaeeakkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
48-137 3.28e-05

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: 46.13  E-value: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRAQAEErrktLSEETRQHQARAQYQDKlarqRYEDQLKQ--------QQLLNEENLRKQEESVQK 119
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQEL----LREKQKEEEQMMEAQER----SYQEHVKQliekmeaeREQLLAEQERMLEHKLQE 273
                          90
                  ....*....|....*...
gi 955080478  120 QEAMRRATVEREMELRHK 137
Cdd:pfam02841 274 QEELLKEGFKTEAESLQK 291
PRK11637 PRK11637
AmiB activator; Provisional
55-163 3.63e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 46.61  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  55 EQLKSEQIRAQ----AEERRKTLSE--ETRQH--QARAQYQDKLARQR---YEDQLKQQQLLNEENLRKQ-----EESVQ 118
Cdd:PRK11637 150 ESQRGERILAYfgylNQARQETIAElkQTREElaAQKAELEEKQSQQKtllYEQQAQQQKLEQARNERKKtltglESSLQ 229
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 955080478 119 KQEAmrRATVEREMELRHKNEMLRVETEARARAKAERENADIIRE 163
Cdd:PRK11637 230 KDQQ--QLSELRANESRLRDSIARAEREAKARAEREAREAARVRD 272
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
300-420 3.97e-05

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


Pssm-ID: 410931 [Multi-domain]  Cd Length: 163  Bit Score: 44.49  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTG-GDVAPMGREGVTAMHKLFDWANtSRRGLLLFMDEADAFLRKRATEE 378
Cdd:cd19523   34 RSILLFGPRGTGKTLLGRCLASQLGATFLRLRGsTLVAKWAGEGEKILQASFLAAR-CRQPSVLFISDLDALLSSQDDEA 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 955080478 379 -----ISKDLRATLNAFLyhmGQHSNKFMLVLASNLPEQFDCAINSR 420
Cdd:cd19523  113 spvgrLQVELLAQLDGVL---GSGEDGVLVVCTTSKPEEIDESLRRY 156
PTZ00121 PTZ00121
MAEBL; Provisional
48-183 4.29e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRaQAEERRKtlSEETRqhqaRAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEA-MRRA 126
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAK-KAEEKKK--ADELK----KAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEArIEEV 1597
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 955080478  127 TVEREMELRHKNEMLRVETEARARAKAEREnadiiREQIRLKASEHRQTVLESIRTA 183
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKK-----AEEEKKKVEQLKKKEAEEKKKA 1649
PTZ00121 PTZ00121
MAEBL; Provisional
15-174 4.63e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   15 ARSLCRAGAVQTQERLSGSASPEQVPAGECCALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQ- 93
Cdd:PTZ00121 1280 ADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEa 1359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   94 -RYEDQLKQQQLLNEENLRKQEESVQKQEAMRRA--TVEREMELRHKNEMLRVETEARARAKAERENADIIR--EQIRLK 168
Cdd:PTZ00121 1360 eAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAdeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKkaDEAKKK 1439

                  ....*.
gi 955080478  169 ASEHRQ 174
Cdd:PTZ00121 1440 AEEAKK 1445
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
48-171 4.68e-05

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 45.99  E-value: 4.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQH----------QARAQYQDKLARQRYEDQLKQQQllnEENLRKQEESV 117
Cdd:TIGR02794  96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQaaeakakaeaEAERKAKEEAAKQAEEEAKAKAA---AEAKKKAEEAK 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 955080478  118 QKQEAMRRATVERE-----MELRHKNEMLRVETEARARAKAERENADIIREQIRLKASE 171
Cdd:TIGR02794 173 KKAEAEAKAKAEAEakakaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADE 231
PTZ00121 PTZ00121
MAEBL; Provisional
46-173 4.96e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 4.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   46 ALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN-EENLRKQEESVQKQEAMR 124
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKaEEDEKKAAEALKKEAEEA 1701
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 955080478  125 RATVE---REMELRHKNEMLRVETEARaraKAERENADIIREQIRLKASEHR 173
Cdd:PTZ00121 1702 KKAEElkkKEAEEKKKAEELKKAEEEN---KIKAEEAKKEAEEDKKKAEEAK 1750
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
47-178 5.43e-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: 46.27  E-value: 5.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   47 LQEYEAAVEQLKSEQI-RAQAEERRKtlSEETRQHQARAQYQDKLARQRyeDQLKQQQLLNEENLRKQEESVqKQEAMRR 125
Cdd:pfam17380 365 IRQEEIAMEISRMRELeRLQMERQQK--NERVRQELEAARKVKILEEER--QRKIQQQKVEMEQIRAEQEEA-RQREVRR 439
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 955080478  126 ATVER--EMELRHKNEM--------LRVETEARARAKAERENadiiREQIRLKASEHRQTVLE 178
Cdd:pfam17380 440 LEEERarEMERVRLEEQerqqqverLRQQEEERKRKKLELEK----EKRDRKRAEEQRRKILE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
46-296 6.77e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 6.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  46 ALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRR 125
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 126 ATVEREMELRHKNEMLRVETEARARAKAEREnadiIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATV 205
Cdd:COG1196  468 LLEEAALLEAALAELLEELAEAAARLLLLLE----AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 206 AGLTLLAVGVYSAKNATAVTGRFIEARLGK----PSLVRETSRITVLEALRHPIQVSRRLLSRPQDVLEGVVLSPSLEAR 281
Cdd:COG1196  544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
                        250
                 ....*....|....*
gi 955080478 282 VRDIAIATRNTKKNR 296
Cdd:COG1196  624 GRTLVAARLEAALRR 638
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
49-169 8.62e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.04  E-value: 8.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  49 EYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRY---EDQLK-QQQLLNE--------ENLRKQEES 116
Cdd:COG1566   80 DLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLdlaQRELErYQALYKKgavsqqelDEARAALDA 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 955080478 117 VQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKA 169
Cdd:COG1566  160 AQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
60-174 1.04e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 42.72  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   60 EQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQqllNEENLRKQEEsvqkqEAMRRATVEREMELRHKNE 139
Cdd:pfam05672  31 EQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRRE---EEERQRKAEE-----EAEEREQREQEEQERLQKQ 102
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 955080478  140 mlRVETEARARAKAERENADiiREQIRLKASEHRQ 174
Cdd:pfam05672 103 --KEEAEAKAREEAERQRQE--REKIMQQEEQERL 133
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
301-412 1.17e-04

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


Pssm-ID: 400191 [Multi-domain]  Cd Length: 135  Bit Score: 42.28  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  301 HILLYGPPGTGKTLFAKKLA------------LHSGMDYAIMTGG-DVAPMGREG-----VTAMhklfdwantsRRGLLL 362
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaalsnrpvfyvqLTRDTTEEDLFGRrNIDPGGASWvdgplVRAA----------REGEIA 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 955080478  363 FMDEADaflrkrateEISKDLRATLNAFLYH-----------MGQHSNKFMLVLASNLPEQ 412
Cdd:pfam07728  71 VLDEIN---------RANPDVLNSLLSLLDErrlllpdggelVKAAPDGFRLIATMNPLDR 122
PTZ00121 PTZ00121
MAEBL; Provisional
48-174 1.50e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 45.13  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRaQAEERRKtlSEETRQHQARAQYQD---KLARQRYEDQLKQQQllnEENLRKQEESVQK-QEAM 123
Cdd:PTZ00121 1269 QAAIKAEEARKADELK-KAEEKKK--ADEAKKAEEKKKADEakkKAEEAKKADEAKKKA---EEAKKKADAAKKKaEEAK 1342
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 955080478  124 RRATVEREMELRHKNEMLRVETEARArAKAERENADIIREQIRLKASEHRQ 174
Cdd:PTZ00121 1343 KAAEAAKAEAEAAADEAEAAEEKAEA-AEKKKEEAKKKADAAKKKAEEKKK 1392
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
46-183 1.60e-04

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


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 44.94  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   46 ALQEYEAA---VEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKL------ARQRYEDQLKQQQLLNEENLRKQ--- 113
Cdd:COG3096   470 ARRQFEKAyelVCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLraqlaeLEQRLRQQQNAERLLEEFCQRIGqql 549
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  114 ------EESVQKQEAMR-------RATVEREMELRHKNEMLRVE-TEARARAKAERENADI---IREQI--RLKAS---- 170
Cdd:COG3096   550 daaeelEELLAELEAQLeeleeqaAEAVEQRSELRQQLEQLRARiKELAARAPAWLAAQDAlerLREQSgeALADSqevt 629
                         170
                  ....*....|...
gi 955080478  171 EHRQTVLESIRTA 183
Cdd:COG3096   630 AAMQQLLEREREA 642
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
48-178 1.60e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyQDKLARQRYEDQLKQQQLLNEENLRKQEESV--QKQEAMRR 125
Cdd:pfam17380 396 QELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR-QREVRRLEEERAREMERVRLEEQERQQQVERlrQQEEERKR 474
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 955080478  126 ATVEREMELRHKNE-------MLRVETEARARAKAERENAD-------------IIREQIRLKASEHRQTVLE 178
Cdd:pfam17380 475 KKLELEKEKRDRKRaeeqrrkILEKELEERKQAMIEEERKRkllekemeerqkaIYEEERRREAEEERRKQQE 547
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
48-179 1.70e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 44.73  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQllnEENLRKQ---EESVQKQEAMR 124
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA---EEERRKQqemEERRRIQEQMR 559
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955080478  125 RATVEREM--ELRHKNEMLR--VETEaraRAKAERENA---DIIREQIRLKASEHRQTVLES 179
Cdd:pfam17380 560 KATEERSRleAMEREREMMRqiVESE---KARAEYEATtpiTTIKPIYRPRISEYQPPDVES 618
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
47-196 1.84e-04

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


Pssm-ID: 114011 [Multi-domain]  Cd Length: 489  Bit Score: 44.22  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   47 LQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARaqyQDKLARQRYEDQLKQQQLLN-EENLRKQEESVQKQ--EAM 123
Cdd:pfam05262 203 LKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFA---QDNADKQRDEVRQKQQEAKNlPKPADTSSPKEDKQvaENQ 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  124 RRATVEREMELRHKNEMLRVETEARA----------RAKAERENADIIREqiRLKASEHRQTVLESIRTAGTLFGEGFRA 193
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEALKAKDHKAfdlkqeskasEKEAEDKELEAQKK--REPVAEDLQKTKPQVEAQPTSLNEDAID 357

                  ...
gi 955080478  194 FVT 196
Cdd:pfam05262 358 SSN 360
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
47-183 1.90e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  47 LQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRyeDQLKQQQllneENLRKQEESVQKQEAMRRA 126
Cdd:COG1196  222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL--EELRLEL----EELELELEEAQAEEYELLA 295
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 127 TVER-EMELRHKNEMLRVETEARARAKAERE--NADIIREQIRLKASEHRQTVLESIRTA 183
Cdd:COG1196  296 ELARlEQDIARLEERRRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEE 355
PTZ00121 PTZ00121
MAEBL; Provisional
48-163 2.13e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   48 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRAT 127
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 955080478  128 VEREME------LRHKNEMLRVETEarARAKAERENADIIRE 163
Cdd:PTZ00121 1773 IRKEKEavieeeLDEEDEKRRMEVD--KKIKDIFDNFANIIE 1812
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
55-174 2.40e-04

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 43.68  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   55 EQLKSEQIRAQAEERRKtlsEETRQHQARAQYQDKLARQRYEDQLKQQQllnEENLRKQEESVQKQEAMRRATVEREMEL 134
Cdd:TIGR02794  61 PAAKKEQERQKKLEQQA---EEAEKQRAAEQARQKELEQRAAAEKAAKQ---AEQAAKQAEEKQKQAEEAKAKQAAEAKA 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 955080478  135 RHKNEMLRvETEARARAKAERENADIIREQIRLKASEHRQ 174
Cdd:TIGR02794 135 KAEAEAER-KAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK 173
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
46-183 2.40e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478    46 ALQEYEAAVEQLKSEQIRAQAEERRKT------------LSEETRQHQARAQY--QDKLARQRYEDQLKQQQLLNEENLR 111
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEELQkelyalaneisrLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   112 KQEESVQKQEAMRRATVEREMELRHKNEMLR---------VETEARARAKAERE----NADIIREQIRLKASEHRQTVLE 178
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELEsrleeleeqLETLRSKVAQLELQiaslNNEIERLEARLERLEDRRERLQ 420

                   ....*
gi 955080478   179 SIRTA 183
Cdd:TIGR02168  421 QEIEE 425
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
49-156 3.47e-04

Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is required for the oestrogen-dependent expression of ESR1 target genes. It functions in cooperation with MED1. The family of proteins is found in eukaryotes.


Pssm-ID: 405931 [Multi-domain]  Cd Length: 151  Bit Score: 41.19  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   49 EYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN---EENLRKQEESVQKQEAMRR 125
Cdd:pfam15346  27 ELEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELEEERRKEEEERKKREELErilEENNRKIEEAQRKEAEERL 106
                          90       100       110
                  ....*....|....*....|....*....|.
gi 955080478  126 ATVERemELRHKNEMLRVETEARARAKAERE 156
Cdd:pfam15346 107 AMLEE--QRRMKEERQRREKEEEEREKREQQ 135
PRK10927 PRK10927
cell division protein FtsN;
55-155 3.61e-04

cell division protein FtsN;


Pssm-ID: 236797 [Multi-domain]  Cd Length: 319  Bit Score: 43.13  E-value: 3.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  55 EQLKSEQ----IRAQAEERRK--TLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN------EENLRKQEESVQKQEA 122
Cdd:PRK10927 112 EQLTPEQrqllEQMQADMRQQptQLVEVPWNEQTPEQRQQTLQRQRQAQQLAEQQRLAqqsrttEQSWQQQTRTSQAAPV 191
                         90       100       110
                 ....*....|....*....|....*....|....
gi 955080478 123 MRRATVEREMELRHK-NEMLRVETEARARAKAER 155
Cdd:PRK10927 192 QAQPRQSKPASTQQPyQDLLQTPAHTTAQSKPQQ 225
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
105-320 3.63e-04

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 43.22  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 105 LNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKAS----EHRQTVLESI 180
Cdd:COG1401   31 IRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEaavaIEELYELEAD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 181 RTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRR 260
Cdd:COG1401  111 SEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSE 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 261 LLSRPQDVLEGVvLSPSLEARVRDIAIATRnTKKNrglyrhILLYGPPGTGKTLFAKKLA 320
Cdd:COG1401  191 DLESEDDYLKDL-LREKFEETLEAFLAALK-TKKN------VILAGPPGTGKTYLARRLA 242
PRK12704 PRK12704
phosphodiesterase; Provisional
51-184 3.72e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 3.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  51 EAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN-EENLRKQEESVQKQEA------- 122
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkEENLDRKLELLEKREEelekkek 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 123 ----------MRRATVErEMELRHKNEMLRV----ETEARA------RAKAERENADIIR---EQIRLKAS-EHRQTVLE 178
Cdd:PRK12704 118 eleqkqqeleKKEEELE-ELIEEQLQELERIsgltAEEAKEillekvEEEARHEAAVLIKeieEEAKEEADkKAKEILAQ 196

                 ....*..
gi 955080478 179 SI-RTAG 184
Cdd:PRK12704 197 AIqRCAA 203
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
55-183 3.76e-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: 43.40  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   55 EQLKSEQIRAQAEER----------RKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQ-----LLNEENLRKQEESVQK 119
Cdd:pfam15709 367 QLERAEKMREELELEqqrrfeeirlRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQeefrrKLQELQRKKQQEEAER 446
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955080478  120 QEAMRRATVEREMEL----RHKNEMLRVETEARARAKAEREnadiirEQIRLKASEHRQTVLESIRTA 183
Cdd:pfam15709 447 AEAEKQRQKELEMQLaeeqKRLMEMAEEERLEYQRQKQEAE------EKARLEAEERRQKEEEAARLA 508
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
302-374 3.92e-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: 3.92e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP----MGREGVtamHKLFDWANtSRRGLLLFMDEADAFLRKR 374
Cdd:cd19526   30 ILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNkyigASEQNV---RDLFSRAQ-SAKPCILFFDEFDSIAPKR 102
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
300-376 4.45e-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: 41.32  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 300 RHILLYGPPGTGKTLFAKKLA-LHSGMDYAIMTGGDVAP--MGrEGVTAMHKLFDWANTSRRGL-------LLFMDEADA 369
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGkMLNAREPKIVNGPEILNkyVG-ESEANIRKLFADAEEEQRRLgansglhIIIFDEIDA 114

                 ....*..
gi 955080478 370 FLRKRAT 376
Cdd:cd19504  115 ICKQRGS 121
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
302-320 4.68e-04

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 43.10  E-value: 4.68e-04
                         10
                 ....*....|....*....
gi 955080478 302 ILLYGPPGTGKTLFAKKLA 320
Cdd:COG0465  178 VLLVGPPGTGKTLLAKAVA 196
Zot COG4128
Zona occludens toxin, predicted ATPase [General function prediction only];
302-465 4.94e-04

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


Pssm-ID: 443304 [Multi-domain]  Cd Length: 276  Bit Score: 42.39  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFA----KKLALHSG-------------------MDYAIMTGG---DVAPMGREGVTAMHKLFDWAnt 355
Cdd:COG4128    4 TLITGVPGSGKSYEAvwflIIPALKKGrrvitnipglkileriaehLGLAVPDTAeliNVDTDDPDGLEKMARWFHWA-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 356 sRRGLLLFMDEADAFLRKRATEEISKDLRatlNAFLYHmgQHSNkFMLVLASNLPEQFDCAINSRIDV-MVHFDLPQQEE 434
Cdd:COG4128   82 -PDGALIVIDEAQRVWPPRGKGSKPPDVV---QAFATH--RHHG-WDIVLITQNISLIHSFIRALIERhYRHRKLDGLGL 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 955080478 435 RERLVRLHFDNCVLKP-----ATEGKRRLKLAQFDY 465
Cdd:COG4128  155 RNRYEWPEHDGNPGKKtshdkATSKRYKYPKDVFGL 190
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
46-298 4.95e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  46 ALQEYEAAVEQLKSEQIRAQAEERRKT-------LSEETRQHQAR-AQYQDKLAR-----QRYEDQLKQQQLLNEENLRK 112
Cdd:COG4717   96 ELEELEEELEELEAELEELREELEKLEkllqllpLYQELEALEAElAELPERLEEleerlEELRELEEELEELEAELAEL 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 113 QEESVQKQEAMRRATVEREMELRHKNEMLRVE-TEARARAKAERENADIIREQI-RLKASEHRQTVLESIRTAGTLFG-- 188
Cdd:COG4717  176 QEELEELLEQLSLATEEELQDLAEELEELQQRlAELEEELEEAQEELEELEEELeQLENELEAAALEERLKEARLLLLia 255
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 189 ---EGFRAFVTDRDKVTATVAGLTLLAVGV------YSAKNATAVTGRFIEAR-LGKPSLVRETSRITVLEALRHPIQVS 258
Cdd:COG4717  256 aalLALLGLGGSLLSLILTIAGVLFLVLGLlallflLLAREKASLGKEAEELQaLPALEELEEEELEELLAALGLPPDLS 335
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 955080478 259 R-RLLSRPQDVLEGVVLSPSLEARVRDIAIATRNTKKNRGL 298
Cdd:COG4717  336 PeELLELLDRIEELQELLREAEELEEELQLEELEQEIAALL 376
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
46-171 5.44e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 42.60  E-value: 5.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   46 ALQEYEAAVEQLK------SEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEE---S 116
Cdd:pfam13868  56 ALEEEEEKEEERKeerkryRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEideF 135
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 955080478  117 VQKQEAMRRATVEREMELRHKN-EMLRVETEARARAKAERENADIIREQIRLKASE 171
Cdd:pfam13868 136 NEEQAEWKELEKEEEREEDERIlEYLKEKAEREEEREAEREEIEEEKEREIARLRA 191
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
301-371 6.66e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 42.38  E-value: 6.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 301 HILLYGPPGTGKTLFAKKLALHSGMDY----AIMTggdvapmgreGVTAMHKLFDWANTSR---RGLLLFMDE------- 366
Cdd:PRK13342  38 SMILWGPPGTGKTTLARIIAGATDAPFealsAVTS----------GVKDLREVIEEARQRRsagRRTILFIDEihrfnka 107

                 ....*.
gi 955080478 367 -ADAFL 371
Cdd:PRK13342 108 qQDALL 113
PTZ00121 PTZ00121
MAEBL; Provisional
46-174 7.62e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   46 ALQEYEAAVEQLKSEQIRAQAEERRKtlSEETRQHQAraqYQDKLARQRYEDQLKQQQllnEENLRKQEEsVQKQEAMRR 125
Cdd:PTZ00121 1348 AKAEAEAAADEAEAAEEKAEAAEKKK--EEAKKKADA---AKKKAEEKKKADEAKKKA---EEDKKKADE-LKKAAAAKK 1418
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 955080478  126 atveREMELRHKNEMLRVETEARARAKAEREnadiiREQIRLKASEHRQ 174
Cdd:PTZ00121 1419 ----KADEAKKKAEEKKKADEAKKKAEEAKK-----ADEAKKKAEEAKK 1458
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
302-371 8.38e-04

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


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 41.97  E-value: 8.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 302 ILLYGPPGTGKTLFAKKLALHSGMDY----AIMTggdvapmgreGVTAMHKLFDWANTSR---RGLLLFMDE-------- 366
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFvalsAVTS----------GVKDIREVIEEARERRaygRRTILFVDEihrfnkaq 121

                 ....*
gi 955080478 367 ADAFL 371
Cdd:COG2256  122 QDALL 126
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
47-154 8.58e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 42.10  E-value: 8.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  47 LQEYEAavEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQ-----QQLLNEENLRKQEESVQKQE 121
Cdd:PRK09510 103 LKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRaaaaaKKAAAEAKKKAEAEAAKKAA 180
                         90       100       110
                 ....*....|....*....|....*....|....
gi 955080478 122 AMRRATVEREMELRHKNEM-LRVETEARARAKAE 154
Cdd:PRK09510 181 AEAKKKAEAEAAAKAAAEAkKKAEAEAKKKAAAE 214
PTZ00121 PTZ00121
MAEBL; Provisional
49-174 1.09e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   49 EYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKlarQRYEDQLKQQQLLNE--ENLRKQEESVQKQEAMRRA 126
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED---KKKADELKKAAAAKKkaDEAKKKAEEKKKADEAKKK 1439
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 955080478  127 TVEREM--ELRHKNEMLRVETEARARAKAEREnadiiREQIRLKASEHRQ 174
Cdd:PTZ00121 1440 AEEAKKadEAKKKAEEAKKAEEAKKKAEEAKK-----ADEAKKKAEEAKK 1484
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
46-169 1.13e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 41.72  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  46 ALQEYEAAVEQLKSEQiraQAEERRK----TLSEETRQHQARAQyqDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQE 121
Cdd:PRK09510  60 VVEQYNRQQQQQKSAK---RAEEQRKkkeqQQAEELQQKQAAEQ--ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA 134
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 955080478 122 AMRRATVEREMELRHKNEMLRVETEArARAKAERENADIIREQIRLKA 169
Cdd:PRK09510 135 EEAAAKAAAAAKAKAEAEAKRAAAAA-KKAAAEAKKKAEAEAAKKAAA 181
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
45-182 1.34e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  45 CALQEYEAAVEQLKSEqiRAQAEERRKTLSEETrqhqARAQYQDKLARQRyedqlkqqqllneENLRKQEESVQKQEAMR 124
Cdd:PRK02224 468 ETIEEDRERVEELEAE--LEDLEEEVEEVEERL----ERAEDLVEAEDRI-------------ERLEERREDLEELIAER 528
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 955080478 125 RATVEREME----LRHKNEMLRVETE-ARARAKAERENADIIREQI-----RLKASEHRQTVLESIRT 182
Cdd:PRK02224 529 RETIEEKREraeeLRERAAELEAEAEeKREAAAEAEEEAEEAREEVaelnsKLAELKERIESLERIRT 596
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
47-174 1.53e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.06  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   47 LQEYEAAV---EQLKSEQIRAQAEERRKTLSEETRQHQARAQYQD-KLARQRYEDQLKQQQLLNEENLRKQEESVQKQEA 122
Cdd:pfam13868  90 QEEYEEKLqerEQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEfNEEQAEWKELEKEEEREEDERILEYLKEKAEREE 169
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 955080478  123 MRRATVER-EMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQ 174
Cdd:pfam13868 170 EREAEREEiEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQK 222
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
61-156 1.64e-03

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


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 40.98  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   61 QIRAQAEERRKTLSEETRQHQARaqyQDKLARQryEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEM 140
Cdd:TIGR02794  47 AVAQQANRIQQQKKPAAKKEQER---QKKLEQQ--AEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA 121
                          90       100
                  ....*....|....*....|
gi 955080478  141 L----RVETEARARAKAERE 156
Cdd:TIGR02794 122 EeakaKQAAEAKAKAEAEAE 141
PTZ00121 PTZ00121
MAEBL; Provisional
85-183 1.74e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   85 QYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEAR-----ARAKAERENAD 159
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARkaedaKRVEIARKAED 1162
                          90       100
                  ....*....|....*....|....
gi 955080478  160 IIREQIRLKASEHRQtvLESIRTA 183
Cdd:PTZ00121 1163 ARKAEEARKAEDAKK--AEAARKA 1184
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
47-173 1.79e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 41.09  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   47 LQEYEAAVEQLKSEQIR-AQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLlnEENLRKQEESVQKQEAMRR 125
Cdd:pfam15709 338 LRAERAEMRRLEVERKRrEQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRL--EEERQRQEEEERKQRLQLQ 415
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 955080478  126 ATVER----EMELRHKNEMLRVETEARARAKAERENADIIREQIRLkASEHR 173
Cdd:pfam15709 416 AAQERarqqQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQL-AEEQK 466
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
49-164 1.92e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 41.01  E-value: 1.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  49 EYEAAVEQLKSEQIRAQ--AEERRKTLSEETRQHQARAQYQdkLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR-- 124
Cdd:COG2268  207 EAERETEIAIAQANREAeeAELEQEREIETARIAEAEAELA--KKKAEERREAETARAEAEAAYEIAEANAEREVQRQle 284
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 955080478 125 RATVEREMELRHKNEMLRVETEA---RARAKAERE--------NADIIREQ 164
Cdd:COG2268  285 IAEREREIELQEKEAEREEAELEadvRKPAEAEKQaaeaeaeaEAEAIRAK 335
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
302-320 2.27e-03

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


Pssm-ID: 459992  Cd Length: 102  Bit Score: 37.97  E-value: 2.27e-03
                          10
                  ....*....|....*....
gi 955080478  302 ILLYGPPGTGKTLFAKKLA 320
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLA 19
mukB PRK04863
chromosome partition protein MukB;
29-174 2.32e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.10  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   29 RLSGSASPEQvpageccALQEYEAAVEQLKSEQIRAQaeerrktlseetRQHQARAQYQDklARQRYEDQLKQQQLLNEE 108
Cdd:PRK04863  484 KIAGEVSRSE-------AWDVARELLRRLREQRHLAE------------QLQQLRMRLSE--LEQRLRQQQRAERLLAEF 542
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 955080478  109 NlRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQ 174
Cdd:PRK04863  543 C-KRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLA 607
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
295-366 2.42e-03

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


Pssm-ID: 440834 [Multi-domain]  Cd Length: 835  Bit Score: 40.86  E-value: 2.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 295 NRGLyrHILLYGPPGTGKTLFAKKL---ALHSGM-------------DYA-----IM-----------TGgdvapmgreg 342
Cdd:COG1221  128 PKGL--HTLILGPTGVGKSFFAELMyeyAIEIGVlpedapfvvfncaDYAnnpqlLMsqlfgyvkgafTG---------- 195
                         90       100       110
                 ....*....|....*....|....*....|.
gi 955080478 343 vtamhklfdwANTSRRGLL-------LFMDE 366
Cdd:COG1221  196 ----------ADKDKEGLIekadggiLFLDE 216
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
48-129 2.45e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 214922 [Multi-domain]  Cd Length: 140  Bit Score: 38.72  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478    48 QEYEAAVEQLKSEQIRAQAEerRKTLSEEtrqhqARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRAT 127
Cdd:smart00935  32 AELEKLEKELQKLKEKLQKD--AATLSEA-----AREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQKILDKINKAI 104

                   ..
gi 955080478   128 VE 129
Cdd:smart00935 105 KE 106
RNase_Y_N pfam12072
RNase Y N-terminal region;
46-172 2.53e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.48  E-value: 2.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   46 ALQEYEA----AVEQLKSE--QIRAQAE----ERRKTLS---------EET--RQHQARAQYQDKLARQryEDQLKQQQl 104
Cdd:pfam12072  43 AKKEAETkkkeALLEAKEEihKLRAEAErelkERRNELQrqerrllqkEETldRKDESLEKKEESLEKK--EKELEAQQ- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  105 lneENLRKQEESVQKQEAMRRATVER-----------------EMELRHKNEMLRVETEARARAKAERENADIIREQIRL 167
Cdd:pfam12072 120 ---QQLEEKEEELEELIEEQRQELERisgltseeakeilldevEEELRHEAAVMIKEIEEEAKEEADKKAKEIIALAIQR 196

                  ....*
gi 955080478  168 KASEH 172
Cdd:pfam12072 197 CAADH 201
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
51-173 2.81e-03

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 39.63  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   51 EAAVEQLKSEQIRAQAEERRKTLSEETRQHQaraqyqDKLARQryEDQLKQQQLLNEENLRKQEEsVQKQEAMRRATVER 130
Cdd:pfam00261  61 EALEKLEEAEKAADESERGRKVLENRALKDE------EKMEIL--EAQLKEAKEIAEEADRKYEE-VARKLVVVEGDLER 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 955080478  131 --------EMELRHKNEMLRVET------EARARAKAEREnaDIIREQIR-----LKASEHR 173
Cdd:pfam00261 132 aeeraelaESKIVELEEELKVVGnnlkslEASEEKASERE--DKYEEQIRfltekLKEAETR 191
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
52-156 3.01e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.17  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  52 AAVEQLKSEQiRAQAEERRKtlsEETRQHQArAQYQDKLARQRYEDQLKQQQlLNEENLRKQEESVQKQEAMRRATVERE 131
Cdd:PRK09510  59 AVVEQYNRQQ-QQQKSAKRA---EEQRKKKE-QQQAEELQQKQAAEQERLKQ-LEKERLAAQEQKKQAEEAAKQAALKQK 132
                         90       100
                 ....*....|....*....|....*
gi 955080478 132 MElrhknEMLRVETEARARAKAERE 156
Cdd:PRK09510 133 QA-----EEAAAKAAAAAKAKAEAE 152
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
20-153 3.49e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.59  E-value: 3.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478    20 RAGAVQTQERLS-GSASPEQVPAGECCALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDkLARQRYEDQ 98
Cdd:pfam12128  617 REKQAAAEEQLVqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS-LEAQLKQLD 695
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 955080478    99 LKQQQLLNEENLRKQEESVQKQEAMRRATVEREMEL-RHKNEMLRVETEARARAKA 153
Cdd:pfam12128  696 KKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLaLLKAAIAARRSGAKAELKA 751
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
44-156 3.84e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 40.02  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   44 CCALQEYEAAVEQLKSEQIRAQaEERRKTLSEETRQHQAR---------AQYQDKLARQRYEDQLKQQQllneenlrkQE 114
Cdd:pfam15558  57 QQSQEQWQAEKEQRKARLGREE-RRRADRREKQVIEKESRwreqaedqeNQRQEKLERARQEAEQRKQC---------QE 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 955080478  115 ESVQKQEAMRRATVEREMELRHKnemlRVETEARARAKAERE 156
Cdd:pfam15558 127 QRLKEKEEELQALREQNSLQLQE----RLEEACHKRQLKERE 164
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
20-412 3.99e-03

Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 40.02  E-value: 3.99e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  20 RAGAVQTQERLSGSASPEQVPAgECCALQEYEAAVEQLKSEQIRAQAEERRKTLSEEtrQHQARAQYQDKLARQRYEdql 99
Cdd:COG3064    8 KAAEAAAQERLEQAEAEKRAAA-EAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE--AEQRAAELAAEAAKKLAE--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 100 KQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLES 179
Cdd:COG3064   82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 180 IRTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSR 259
Cdd:COG3064  162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 260 RLLSRPQDVLEGVVLSPSLEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG 339
Cdd:COG3064  242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 955080478 340 REGVTAMHKLFDWANTSRRGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQ 412
Cdd:COG3064  322 AAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAA 394
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
300-327 4.08e-03

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


Pssm-ID: 440478 [Multi-domain]  Cd Length: 292  Bit Score: 39.38  E-value: 4.08e-03
                         10        20
                 ....*....|....*....|....*...
gi 955080478 300 RHILLYGPPGTGKTLFAKKLALHSGMDY 327
Cdd:COG0714   32 GHLLLEGVPGVGKTTLAKALARALGLPF 59
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
55-178 4.14e-03

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


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 4.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   55 EQLKSEQ--IRAQAEERRKTLSEETRQHQA--RAQYQDKLARQ---RYEDQLKQQQLLNEENLRKQEEsvqKQEAMRRAT 127
Cdd:pfam15709 329 EQEKASRdrLRAERAEMRRLEVERKRREQEeqRRLQQEQLERAekmREELELEQQRRFEEIRLRKQRL---EEERQRQEE 405
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 955080478  128 VEREMELRHK--NEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLE 178
Cdd:pfam15709 406 EERKQRLQLQaaQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELE 458
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
51-181 4.66e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.52  E-value: 4.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   51 EAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyQDKLARQRYEDQLKQQQLLNEENLRKQEEsvQKQEAMRRATVER 130
Cdd:pfam13868 209 KLYQEEQERKERQKEREEAEKKARQRQELQQAREE-QIELKERRLAEEAEREEEEFERMLRKQAE--DEEIEQEEAEKRR 285
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 955080478  131 EMELRHKNEMLRVETEARARAKAERENADIIREQIRlKASEHRQTVLESIR 181
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAAEREEELEEGERLR-EEEAERRERIEEER 335
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
54-179 5.24e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 5.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478    54 VEQLKSEQIRAQAEERRKTLSEE---TRQHQARAQYQDKLARQRyEDQLKQQQLLNEENLRKQEESVQKQEAMRRAtvER 130
Cdd:pfam02463  139 VQGGKIEIIAMMKPERRLEIEEEaagSRLKRKKKEALKKLIEET-ENLAELIIDLEELKLQELKLKEQAKKALEYY--QL 215
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 955080478   131 EMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLES 179
Cdd:pfam02463  216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEE 264
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
122-322 5.57e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 39.79  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 122 AMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKV 201
Cdd:COG5635    2 LLLLALILALLALVLLLDLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 202 TATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQDVLEGVVLS-PSLEA 280
Cdd:COG5635   82 LVLLLLESLLLLLLLLLLLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDdLYVPL 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 955080478 281 RVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALH 322
Cdd:COG5635  162 NLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALE 203
44 PHA02544
clamp loader, small subunit; Provisional
301-447 5.79e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 39.20  E-value: 5.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 301 HILLYGP-PGTGKTLFAKKLALHSGMDYAIMTGGDvapmGREGvTAMHKLFDWANT---SRRGLLLFMDEADaflrKRAT 376
Cdd:PHA02544  44 NMLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSD----CRID-FVRNRLTRFASTvslTGGGKVIIIDEFD----RLGL 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 955080478 377 EEISKDLRATlnaflyhMGQHSNKFMLVLASNLPEQFDCAINSRIDVmVHFDLPQQEERERLVRLHFDNCV 447
Cdd:PHA02544 115 ADAQRHLRSF-------MEAYSKNCSFIITANNKNGIIEPLRSRCRV-IDFGVPTKEEQIEMMKQMIVRCK 177
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-174 6.26e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   46 ALQEYEAAVEQLKSEQirAQAEERRKTLSEETRQHQARaqyqdklaRQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRR 125
Cdd:COG4913   289 RLELLEAELEELRAEL--ARLEAELERLEARLDALREE--------LDELEAQIRGNGGDRLEQLEREIERLERELEERE 358
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 955080478  126 ATVEREMELRHKNEMLRVETEA-----RARAKAERENADIIREQIRLKASEHRQ 174
Cdd:COG4913   359 RRRARLEALLAALGLPLPASAEefaalRAEAAALLEALEEELEALEEALAEAEA 412
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
46-193 6.31e-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: 39.65  E-value: 6.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478    46 ALQEYEAAVEQLKS--EQIRAQAEERRKTLSEETRQ-HQARAQyqdklaRQRYEDQLKQQQLLNEENLRKQEESVQKQEA 122
Cdd:TIGR02168  359 ELEELEAELEELESrlEELEEQLETLRSKVAQLELQiASLNNE------IERLEARLERLEDRRERLQQEIEELLKKLEE 432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   123 MRRATVEREMELrhKNEMLRVETEARARAKAERENADIIREQIR---------LKASEHRQTVLESIRTAGTLFGEGFRA 193
Cdd:TIGR02168  433 AELKELQAELEE--LEEELEELQEELERLEEALEELREELEEAEqaldaaereLAQLQARLDSLERLQENLEGFSEGVKA 510
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
301-320 7.12e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 38.96  E-value: 7.12e-03
                         10        20
                 ....*....|....*....|
gi 955080478 301 HILLYGPPGTGKTLFAKKLA 320
Cdd:PRK00080  53 HVLLYGPPGLGKTTLANIIA 72
growth_prot_Scy NF041483
polarized growth protein Scy;
20-182 7.53e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.42  E-value: 7.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   20 RAGAVQTQERLSGSASPEQVPAGECCA------LQEYEAAVEQLK------SEQIRAQAEERRKTLseetrqhqaRAQYQ 87
Cdd:NF041483  453 RAEAVAEGERIRGEARREAVQQIEEAArtaeelLTKAKADADELRstataeSERVRTEAIERATTL---------RRQAE 523
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   88 DKLARQRYE-DQLKQQQLLNEENLRKQEESVQKQeamRRATVEREMELRHK---NEMLRVETEARARAKAERENADIIR- 162
Cdd:NF041483  524 ETLERTRAEaERLRAEAEEQAEEVRAAAERAARE---LREETERAIAARQAeaaEELTRLHTEAEERLTAAEEALADARa 600
                         170       180
                  ....*....|....*....|....*.
gi 955080478  163 --EQIRLKASEH----RQTVLESIRT 182
Cdd:NF041483  601 eaERIRREAAEEterlRTEAAERIRT 626
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
301-319 7.86e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 37.90  E-value: 7.86e-03
                          10
                  ....*....|....*....
gi 955080478  301 HILLYGPPGTGKTLFAKKL 319
Cdd:pfam01078  24 NLLMIGPPGSGKTMLAKRL 42
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
47-181 8.02e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 38.75  E-value: 8.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478   47 LQEYEAAVEQLKSEQIRAQAEERRKtlsEETRQHQARAQYQDKLARQRYEDQLKQQqLLNEENLRKQEEsVQKQEAMRRA 126
Cdd:pfam13868 157 ILEYLKEKAEREEEREAEREEIEEE---KEREIARLRAQQEKAQDEKAERDELRAK-LYQEEQERKERQ-KEREEAEKKA 231
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 955080478  127 TVEREM------ELRHKNEMLRVETE--------ARARAKAERENADIIREQIRLKASEHRQTVLESIR 181
Cdd:pfam13868 232 RQRQELqqareeQIELKERRLAEEAEreeeeferMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIE 300
PRK12704 PRK12704
phosphodiesterase; Provisional
47-172 8.75e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 8.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  47 LQEYEAAVEQLKSEQIRAQAEE---RRKTLSEETRQHQARAQYQDKLARQRyEDQL-KQQQLLN---------------- 106
Cdd:PRK12704  44 LEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNELQKLEKRLLQK-EENLdRKLELLEkreeelekkekeleqk 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478 107 EENLRKQEESVQKQEAMRRATVER-----------------EMELRHKNEMLRVETEARARAKAERENADIIREQIRLKA 169
Cdd:PRK12704 123 QQELEKKEEELEELIEEQLQELERisgltaeeakeillekvEEEARHEAAVLIKEIEEEAKEEADKKAKEILAQAIQRCA 202

                 ...
gi 955080478 170 SEH 172
Cdd:PRK12704 203 ADH 205
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
56-193 8.77e-03

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


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 38.70  E-value: 8.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  56 QLKSEQIRAQAEERRktlseETRQHQARAQYQ--------------DKLARQRYEDQLKQQQLLNEENLRK--QEESVQK 119
Cdd:COG2268  196 EIIRDARIAEAEAER-----ETEIAIAQANREaeeaeleqereietARIAEAEAELAKKKAEERREAETARaeAEAAYEI 270
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 955080478 120 QEAMRRATVEREMELRHKNEMLRVETEARARAKAE-----RENADIIREQIRLKASEHrqtvLESIRTAGTLFGEGFRA 193
Cdd:COG2268  271 AEANAEREVQRQLEIAEREREIELQEKEAEREEAEleadvRKPAEAEKQAAEAEAEAE----AEAIRAKGLAEAEGKRA 345
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
285-379 9.60e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 38.44  E-value: 9.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 955080478  285 IAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTG------GDVAPMgregVTAMHKlfdwantsrr 358
Cdd:TIGR00635  16 LQLFIEAAKMRQEALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAI----LTNLEE---------- 81
                          90       100
                  ....*....|....*....|.
gi 955080478  359 GLLLFMDEADAFlrKRATEEI 379
Cdd:TIGR00635  82 GDVLFIDEIHRL--SPAVEEL 100
 
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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