NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767906275|ref|XP_011540546|]
View 

ATPase family AAA domain-containing protein 3B isoform X6 [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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
42-334 1.16e-115

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: 348.13  E-value: 1.16e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   42 APKDKWSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKmqlealnllhtlvwarslcragavqtq 121
Cdd:pfam12037  15 KPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIK--------------------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  122 erlsgsaspeqvpageccalqEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNE 201
Cdd:pfam12037  68 ---------------------EYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  202 ENLRKQEESVQKQEAMR-----RATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRT 276
Cdd:pfam12037 127 ELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINT 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767906275  277 AGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVR 334
Cdd:pfam12037 207 AGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYIEARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
372-521 2.23e-106

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


:

Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 319.47  E-value: 2.23e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 372 LEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSR 451
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 452 RGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHF 521
Cdd:cd19512   81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
 
Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
42-334 1.16e-115

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: 348.13  E-value: 1.16e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   42 APKDKWSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKmqlealnllhtlvwarslcragavqtq 121
Cdd:pfam12037  15 KPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIK--------------------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  122 erlsgsaspeqvpageccalqEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNE 201
Cdd:pfam12037  68 ---------------------EYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  202 ENLRKQEESVQKQEAMR-----RATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRT 276
Cdd:pfam12037 127 ELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINT 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767906275  277 AGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVR 334
Cdd:pfam12037 207 AGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYIEARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
372-521 2.23e-106

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 319.47  E-value: 2.23e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 372 LEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSR 451
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 452 RGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHF 521
Cdd:cd19512   81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
208-584 4.56e-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: 134.65  E-value: 4.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 208 EESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRA 287
Cdd:COG0464    2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 288 FVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQdVLEGVV 367
Cdd:COG0464   82 LAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA-ILDDLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 368 LSPSLEARVRDIAIATRNTKKNRGLY-----RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR-EGVTA-- 439
Cdd:COG0464  161 GLEEVKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEkn 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 440 MHKLFDWANTSRRGLLLFmDEADAFLRKRaTEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMV 519
Cdd:COG0464  239 LREVFDKARGLAPCVLFI-DEADALAGKR-GEVGDGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEII 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767906275 520 HFDLPQQEERERLVRLHFdncvlkpategKRRLKLAQFDYgrkcSEVARLTEGMSGREIAQLAVS 584
Cdd:COG0464  317 FFPLPDAEERLEIFRIHL-----------RKRPLDEDVDL----EELAEATEGLSGADIRNVVRR 366
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
363-618 3.15e-30

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 119.60  E-value: 3.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 363 LEGVVLSPSLEARVRDIAIATRNTKKNR--GLY--RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---E 435
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRkfGLWppRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSylgE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 436 GVTAMHKLFDWANtsRRGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRI 515
Cdd:COG1223   79 TARNLRKLFDFAR--RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALWRRF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 516 DVMVHFDLPQQEERERLVrlhfdncvlkpategKRRLKLAQFDYGRKCSEVARLTEGMSGREIAQLAVSWQATAYASKDG 595
Cdd:COG1223  157 DEVIEFPLPDKEERKEIL---------------ELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDRE 221
                        250       260
                 ....*....|....*....|...
gi 767906275 596 VLTEAMmdacVQDAVQQYRQKMR 618
Cdd:COG1223  222 KVTKED----LEEALKQRKERKK 240
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
396-523 3.22e-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: 98.43  E-value: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEEIS 474
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767906275  475 KDLRaTLNAFLYHM---GQHSNKFMLVLASNLPEQFDCAINSRIDVMVHFDL 523
Cdd:pfam00004  80 ESRR-VVNQLLTELdgfTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
394-581 2.96e-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: 73.02  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  394 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEE 472
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  473 ISKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHfdncvlkpateg 548
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIH------------ 634
                         170       180       190
                  ....*....|....*....|....*....|...
gi 767906275  549 KRRLKLAQfdyGRKCSEVARLTEGMSGREIAQL 581
Cdd:TIGR01243 635 TRSMPLAE---DVDLEELAEMTEGYTGADIEAV 664
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
396-581 8.10e-13

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 71.60  E-value: 8.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAMHKLFDWANTSRRgLLLFMDEADAFLRKR-ATEEI 473
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDEIDAVGRQRgAGLGG 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 474 SKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHFdncvlkpateg 548
Cdd:PRK10733 267 GHDEReQTLNQMLVEMdGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILKVHM----------- 335
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767906275 549 kRRLKLaqfDYGRKCSEVARLTEGMSGREIAQL 581
Cdd:PRK10733 336 -RRVPL---APDIDAAIIARGTPGFSGADLANL 364
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
394-524 6.43e-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: 58.15  E-value: 6.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   394 RHILLYGPPGTGKTLFAKKLALHSG------------------MDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGlL 455
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   456 LFMDEADAFLRKrateEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFD-CAINSRIDVMVHFDLP 524
Cdd:smart00382  82 LILDEITSLLDA----EQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGpALLRRRFDRRIVLLLI 147
PTZ00121 PTZ00121
MAEBL; Provisional
145-270 1.80e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  145 EAAVEQLKSEQIRaQAEERRKtlSEETRQHQaRAQYQDKLarQRYEDQLKQQQLLNEENLRKQEEsVQKQEAMRRATVER 224
Cdd:PTZ00121 1504 KAAEAKKKADEAK-KAEEAKK--ADEAKKAE-EAKKADEA--KKAEEKKKADELKKAEELKKAEE-KKKAEEAKKAEEDK 1576
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767906275  225 EMELRhKNEMLRVETEAR-----------ARAKAER----ENADIIREQIRlKASEHRQTV 270
Cdd:PTZ00121 1577 NMALR-KAEEAKKAEEARieevmklyeeeKKMKAEEakkaEEAKIKAEELK-KAEEEKKKV 1635
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
119-263 2.69e-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: 46.76  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  119 QTQERLSGSASPEQVPAGEccALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyqDKLARQRYEDQLKQQQL 198
Cdd:TIGR02794  54 RIQQQKKPAAKKEQERQKK--LEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK--QAEEKQKQAEEAKAKQA 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767906275  199 ------LNEENLRKQEESVQKQ---EAMRRATVEREMELRHKNEMLRVETEAR--ARAKAERENADIIREQIRLKA 263
Cdd:TIGR02794 130 aeakakAEAEAERKAKEEAAKQaeeEAKAKAAAEAKKKAEEAKKKAEAEAKAKaeAEAKAKAEEAKAKAEAAKAKA 205
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
142-223 3.67e-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: 38.33  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   142 QEYEAAVEQLKSEQIRAQAEerRKTLSEEtrqhqARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRAT 221
Cdd:smart00935  32 AELEKLEKELQKLKEKLQKD--AATLSEA-----AREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQKILDKINKAI 104

                   ..
gi 767906275   222 VE 223
Cdd:smart00935 105 KE 106
growth_prot_Scy NF041483
polarized growth protein Scy;
114-276 9.97e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.42  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  114 RAGAVQTQERLSGSASPEQVPAGECCA------LQEYEAAVEQLK------SEQIRAQAEERRKTLseetrqhqaRAQYQ 181
Cdd:NF041483  453 RAEAVAEGERIRGEARREAVQQIEEAArtaeelLTKAKADADELRstataeSERVRTEAIERATTL---------RRQAE 523
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  182 DKLARQRYE-DQLKQQQLLNEENLRKQEESVQKQeamRRATVEREMELRHK---NEMLRVETEARARAKAERENADIIR- 256
Cdd:NF041483  524 ETLERTRAEaERLRAEAEEQAEEVRAAAERAARE---LREETERAIAARQAeaaEELTRLHTEAEERLTAAEEALADARa 600
                         170       180
                  ....*....|....*....|....*.
gi 767906275  257 --EQIRLKASEH----RQTVLESIRT 276
Cdd:NF041483  601 eaERIRREAAEEterlRTEAAERIRT 626
 
Name Accession Description Interval E-value
ATAD3_N pfam12037
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ...
42-334 1.16e-115

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: 348.13  E-value: 1.16e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   42 APKDKWSNFDPTGLERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKmqlealnllhtlvwarslcragavqtq 121
Cdd:pfam12037  15 KPRTAYSGFDPEALERAAKAARELESSPHAKKALELMKKQEQTRQAELQAKIK--------------------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  122 erlsgsaspeqvpageccalqEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNE 201
Cdd:pfam12037  68 ---------------------EYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNE 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  202 ENLRKQEESVQKQEAMR-----RATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRT 276
Cdd:pfam12037 127 ELLRKQEESVAKQEAMRiqaqrRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLNLEQLREKANEERETVLESINT 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767906275  277 AGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVR 334
Cdd:pfam12037 207 AGSHIGGGLRALLTDWDKLVAAVGGLTALAAGVYTAKEGTGVAWRYIEARLGKPSLVR 264
RecA-like_ATAD3-like cd19512
ATPase domains of ATPase AAA-domain protein 3A (ATAD3A), -3B, and -3C, and similar ATPase ...
372-521 2.23e-106

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


Pssm-ID: 410920 [Multi-domain]  Cd Length: 150  Bit Score: 319.47  E-value: 2.23e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 372 LEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAMHKLFDWANTSR 451
Cdd:cd19512    1 LEARVRDIAIATRNTKKNKGLYRNILFYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGREGVTAIHKVFDWANTSR 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 452 RGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMVHF 521
Cdd:cd19512   81 RGLLLFVDEADAFLRKRSTEKISEDLRAALNAFLYRTGEQSNKFMLVLASNQPEQFDWAINDRIDEMVEF 150
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
208-584 4.56e-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: 134.65  E-value: 4.56e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 208 EESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRA 287
Cdd:COG0464    2 AELLALAVALALALLLLDDAALRLLLLLLLALAAALLLLLLLLLLLLLALLLVELLLLLLSGALAALLLLALLLLALLAL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 288 FVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQdVLEGVV 367
Cdd:COG0464   82 LAALLSALELLLLGELLLLLLLLLLLLLLLLDLERALLELLRESAEALALAAPLVTYEDIGGLEEELLELREA-ILDDLG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 368 LSPSLEARVRDIAIATRNTKKNRGLY-----RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR-EGVTA-- 439
Cdd:COG0464  161 GLEEVKEELRELVALPLKRPELREEYglpppRGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDL--VSKyVGETEkn 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 440 MHKLFDWANTSRRGLLLFmDEADAFLRKRaTEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRIDVMV 519
Cdd:COG0464  239 LREVFDKARGLAPCVLFI-DEADALAGKR-GEVGDGVGRRVVNTLLTEMEELRSDVVVIAATNRPDLLDPALLRRFDEII 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767906275 520 HFDLPQQEERERLVRLHFdncvlkpategKRRLKLAQFDYgrkcSEVARLTEGMSGREIAQLAVS 584
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 ...
372-521 1.12e-33

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 126.24  E-value: 1.12e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 372 LEARVRDIAIATRNTKKNR----GLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDW 446
Cdd:cd19481    1 LKASLREAVEAPRRGSRLRryglGLPKGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVgESEKNLRKIFER 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767906275 447 ANTSRRGLLLFmDEADAFLRKRATEEISKDLRATLNAFLYHM--GQHSNKFMLVLASNLPEQFDCAINS--RIDVMVHF 521
Cdd:cd19481   81 ARRLAPCILFI-DEIDAIGRKRDSSGESGELRRVLNQLLTELdgVNSRSKVLVIAATNRPDLLDPALLRpgRFDEVIEF 158
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
363-618 3.15e-30

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


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 119.60  E-value: 3.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 363 LEGVVLSPSLEARVRDIAIATRNTKKNR--GLY--RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---E 435
Cdd:COG1223    1 LDDVVGQEEAKKKLKLIIKELRRRENLRkfGLWppRKILFYGPPGTGKTMLAEALAGELKLPLLTVRLDSL--IGSylgE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 436 GVTAMHKLFDWANtsRRGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAINSRI 515
Cdd:COG1223   79 TARNLRKLFDFAR--RAPCVIFFDEFDAIAKDRGDQNDVGEVKRVVNALLQELDGLPSGSVVIAATNHPELLDSALWRRF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 516 DVMVHFDLPQQEERERLVrlhfdncvlkpategKRRLKLAQFDYGRKCSEVARLTEGMSGREIAQLAVSWQATAYASKDG 595
Cdd:COG1223  157 DEVIEFPLPDKEERKEIL---------------ELNLKKFPLPFELDLKKLAKKLEGLSGADIEKVLKTALKKAILEDRE 221
                        250       260
                 ....*....|....*....|...
gi 767906275 596 VLTEAMmdacVQDAVQQYRQKMR 618
Cdd:COG1223  222 KVTKED----LEEALKQRKERKK 240
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
388-618 3.12e-26

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


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 110.10  E-value: 3.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 388 KNRGLYRH--------ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRGLLLF 457
Cdd:COG1222   99 KNPELFRKygieppkgVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSKyiG-EGARNVREVFELAREKAPSIIFI 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 458 mDEADAFLRKRATEEISKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLV 533
Cdd:COG1222  178 -DEIDAIAARRTDDGTSGEVQRTVNQLLAELdGFESRGDVLIIaATNRPDLLDPALlrPGRFDRVIEVPLPDEEAREEIL 256
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 534 RLHFdncvlkpategkRRLKLA-QFDYgrkcSEVARLTEGMSGREIAQLAVswQATAYASKDGVLTEAMMDacVQDAVQQ 612
Cdd:COG1222  257 KIHL------------RDMPLAdDVDL----DKLAKLTEGFSGADLKAIVT--EAGMFAIREGRDTVTMED--LEKAIEK 316

                 ....*.
gi 767906275 613 YRQKMR 618
Cdd:COG1222  317 VKKKTE 322
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
396-523 3.22e-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: 98.43  E-value: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEEIS 474
Cdd:pfam00004   1 LLLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSKYVgESEKRLRELFEAAKKLAPC-VIFIDEIDALAGSRGSGGDS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767906275  475 KDLRaTLNAFLYHM---GQHSNKFMLVLASNLPEQFDCAINSRIDVMVHFDL 523
Cdd:pfam00004  80 ESRR-VVNQLLTELdgfTSSNSKVIVIAATNRPDKLDPALLGRFDRIIEFPL 130
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
394-581 2.96e-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: 73.02  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  394 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEE 472
Cdd:TIGR01243 488 KGVLLFGPPGTGKTLLAKAVATESGANFIAVRGPEIlSKWVGESEKAIREIFRKARQAAPA-IIFFDEIDAIAPARGARF 566
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  473 ISKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHfdncvlkpateg 548
Cdd:TIGR01243 567 DTSVTDRIVNQLLTEMdGIQELSNVVVIaATNRPDILDPALlrPGRFDRLILVPPPDEEARKEIFKIH------------ 634
                         170       180       190
                  ....*....|....*....|....*....|...
gi 767906275  549 KRRLKLAQfdyGRKCSEVARLTEGMSGREIAQL 581
Cdd:TIGR01243 635 TRSMPLAE---DVDLEELAEMTEGYTGADIEAV 664
hflB PRK10733
ATP-dependent zinc metalloprotease FtsH;
396-581 8.10e-13

ATP-dependent zinc metalloprotease FtsH;


Pssm-ID: 182683 [Multi-domain]  Cd Length: 644  Bit Score: 71.60  E-value: 8.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGRE-GVTAMHKLFDWANTSRRgLLLFMDEADAFLRKR-ATEEI 473
Cdd:PRK10733 188 VLMVGPPGTGKTLLAKAIAGEAKVPFFTISGSDFVEMFVGvGASRVRDMFEQAKKAAP-CIIFIDEIDAVGRQRgAGLGG 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 474 SKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHFdncvlkpateg 548
Cdd:PRK10733 267 GHDEReQTLNQMLVEMdGFEGNEGIIVIaATNRPDVLDPALlrPGRFDRQVVVGLPDVRGREQILKVHM----------- 335
                        170       180       190
                 ....*....|....*....|....*....|...
gi 767906275 549 kRRLKLaqfDYGRKCSEVARLTEGMSGREIAQL 581
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 ...
389-514 1.28e-12

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


Pssm-ID: 410917 [Multi-domain]  Cd Length: 163  Bit Score: 66.22  E-value: 1.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 389 NRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVA--PMGrEGVTAMHKLFDWANtSRRGLLLFMDEADAFLR 466
Cdd:cd19509   28 LRGPPRGILLYGPPGTGKTLLARAVASESGSTFFSISASSLVskWVG-ESEKIVRALFALAR-ELQPSIIFIDEIDSLLS 105
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767906275 467 KRATEEISKDLRATlNAFLYHM----GQHSNKFMLVLASNLPEQFDCAINSR 514
Cdd:cd19509  106 ERGSGEHEASRRVK-TEFLVQMdgvlNKPEDRVLVLGATNRPWELDEAFLRR 156
RecA-like_FtsH cd19501
ATP-dependent zinc metalloprotease FtsH; FtsH ATPase is a processive, ATP-dependent zinc ...
394-511 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 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTA--MHKLFDWANTSRRgLLLFMDEADAFLRKRATE 471
Cdd:cd19501   38 KGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEM-FVGVGAsrVRDLFEQAKKNAP-CIVFIDEIDAVGRKRGAG 115
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 767906275 472 EI-SKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI 511
Cdd:cd19501  116 LGgGHDEReQTLNQLLVEMdGFESNTGVIVIaATNRPDVLDPAL 159
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
377-523 1.60e-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: 65.63  E-value: 1.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 377 RDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYA---------IMTGGDVApmGREGVTAMHKLFDwA 447
Cdd:cd00009    3 QEEAIEALREALELPPPKNLLLYGPPGTGKTTLARAIANELFRPGApflylnasdLLEGLVVA--ELFGHFLVRLLFE-L 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767906275 448 NTSRRGLLLFMDEADAFlrkraTEEISKDLRATLNAFLYHMGQHSNkFMLVLASNLPE--QFDCAINSRIDVMVHFDL 523
Cdd:cd00009   80 AEKAKPGVLFIDEIDSL-----SRGAQNALLRVLETLNDLRIDREN-VRVIGATNRPLlgDLDRALYDRLDIRIVIPL 151
ftsH CHL00176
cell division protein; Validated
396-582 6.06e-12

cell division protein; Validated


Pssm-ID: 214386 [Multi-domain]  Cd Length: 638  Bit Score: 68.92  E-value: 6.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMgREGVTA--MHKLFDWANtSRRGLLLFMDEADAFLRKRATE-E 472
Cdd:CHL00176 219 VLLVGPPGTGKTLLAKAIAGEAEVPFFSISGSEFVEM-FVGVGAarVRDLFKKAK-ENSPCIVFIDEIDAVGRQRGAGiG 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 473 ISKDLR-ATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHFDNCVLKPATE 547
Cdd:CHL00176 297 GGNDEReQTLNQLLTEMdGFKGNKGVIVIaATNRVDILDAALlrPGRFDRQITVSLPDREGRLDILKVHARNKKLSPDVS 376
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767906275 548 gkrrLKLaqfdygrkcseVARLTEGMSGREIAQLA 582
Cdd:CHL00176 377 ----LEL-----------IARRTPGFSGADLANLL 396
RecA-like_VPS4 cd19521
ATPase domain of vacuolar protein sorting-associated protein 4; Vacuolar protein ...
389-516 1.46e-11

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


Pssm-ID: 410929 [Multi-domain]  Cd Length: 170  Bit Score: 63.34  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 389 NRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAMHKLFDWANTSRRGlLLFMDEADAFLR 466
Cdd:cd19521   36 NRKPWSGILLYGPPGTGKSYLAKAVATEANSTFFSVSSSDLVSkwMG-ESEKLVKQLFAMARENKPS-IIFIDEVDSLCG 113
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767906275 467 KRATEEiSKDLRATLNAFLYHM---GQHSNKFMLVLASNLPEQFDCAINSRID 516
Cdd:cd19521  114 TRGEGE-SEASRRIKTELLVQMngvGNDSQGVLVLGATNIPWQLDSAIRRRFE 165
CDC48 TIGR01243
AAA family ATPase, CDC48 subfamily; This subfamily of the AAA family ATPases includes two ...
396-569 4.72e-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: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR--AT 470
Cdd:TIGR01243 215 VLLYGPPGTGKTLLAKAVANEAGAYFISINGPEI--MSKyygESEERLREIFKEAEENAPS-IIFIDEIDAIAPKReeVT 291
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  471 EEISKDLRATLNAFLYHMgQHSNKFMLVLASNLPEQFDCAIN--SRIDVMVHFDLPQQEERERLVRLHFDNcvlKPATEG 548
Cdd:TIGR01243 292 GEVEKRVVAQLLTLMDGL-KGRGRVIVIGATNRPDALDPALRrpGRFDREIVIRVPDKRARKEILKVHTRN---MPLAED 367
                         170       180
                  ....*....|....*....|.
gi 767906275  549 KRRLKLAQFDYGRKCSEVARL 569
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 ...
396-520 2.02e-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: 2.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRATEEI 473
Cdd:cd19511   30 VLLYGPPGCGKTLLAKALASEAGLNFISVKGPELFSKyvG-ESERAVREIFQKARQAAPC-IIFFDEIDSLAPRRGQSDS 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767906275 474 SKDLRATLNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVH 520
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 ...
396-511 3.73e-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: 3.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATEEI 473
Cdd:cd19530   33 VLLYGPPGCGKTLLAKAVANESGANFISVKGPELLNKyvG-ESERAVRQVFQRARASAP-CVIFFDEVDALVPKRGDGGS 110
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 767906275 474 SKDLRaTLNAFLYHM--GQHSNKFMLVLASNLPEQFDCAI 511
Cdd:cd19530  111 WASER-VVNQLLTEMdgLEERSNVFVIAATNRPDIIDPAM 149
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
394-524 6.43e-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: 58.15  E-value: 6.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   394 RHILLYGPPGTGKTLFAKKLALHSG------------------MDYAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGlL 455
Cdd:smart00382   3 EVILIVGPPGSGKTTLARALARELGppgggviyidgedileevLDQLLLIIVGGKKASGSGELRLRLALALARKLKPD-V 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   456 LFMDEADAFLRKrateEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQFD-CAINSRIDVMVHFDLP 524
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 ...
394-511 1.22e-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: 57.69  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVapMGR---EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKRAT 470
Cdd:cd19503   35 RGVLLHGPPGTGKTLLARAVANEAGANFLSISGPSI--VSKylgESEKNLREIFEEARSHAPS-IIFIDEIDALAPKREE 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 767906275 471 --EEISKDLRATLNAFLYHMGQhSNKFMLVLASNLPEQFDCAI 511
Cdd:cd19503  112 dqREVERRVVAQLLTLMDGMSS-RGKVVVIAATNRPDAIDPAL 153
RecA-like_PAN_like cd19502
proteasome activating nucleotidase PAN and related proteasome subunits; This subfamily ...
396-521 1.45e-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: 57.73  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKLFDWANTsRRGLLLFMDEADAFLRKRATEEIS 474
Cdd:cd19502   40 VLLYGPPGTGKTLLAKAVANHTDATFIRVVGSElVQKYIGEGARLVRELFEMARE-KAPSIIFIDEIDAIGAKRFDSGTG 118
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767906275 475 KD--LRATLNAFLYHMG--QHSNKFMLVLASNLPEQFDCAI--NSRIDVMVHF 521
Cdd:cd19502  119 GDreVQRTMLELLNQLDgfDPRGNIKVIMATNRPDILDPALlrPGRFDRKIEF 171
PRK03992 PRK03992
proteasome-activating nucleotidase; Provisional
396-583 3.72e-09

proteasome-activating nucleotidase; Provisional


Pssm-ID: 179699 [Multi-domain]  Cd Length: 389  Bit Score: 59.08  E-value: 3.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTG--------GDVAPMGREgvtamhkLFDWANtSRRGLLLFMDEADAFLRK 467
Cdd:PRK03992 168 VLLYGPPGTGKTLLAKAVAHETNATFIRVVGselvqkfiGEGARLVRE-------LFELAR-EKAPSIIFIDEIDAIAAK 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 468 RATEEISKD--LRATLNAFLYHMGQHSNK--FMLVLASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLHfdncv 541
Cdd:PRK03992 240 RTDSGTSGDreVQRTLMQLLAEMDGFDPRgnVKIIAATNRIDILDPAIlrPGRFDRIIEVPLPDEEGRLEILKIH----- 314
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767906275 542 lkpategKRRLKLAQ-FDYgrkcSEVARLTEGMSGREIAQLAV 583
Cdd:PRK03992 315 -------TRKMNLADdVDL----EELAELTEGASGADLKAICT 346
RecA-like_CDC48_r2-like cd19528
second of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or ...
394-520 1.06e-08

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


Pssm-ID: 410936 [Multi-domain]  Cd Length: 161  Bit Score: 54.82  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPM--GrEGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATe 471
Cdd:cd19528   28 KGVLFYGPPGCGKTLLAKAIANECQANFISVKGPELLTMwfG-ESEANVRDIFDKARAAAP-CVLFFDELDSIAKARGG- 104
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767906275 472 EISKDLRAT---LNAFLYHM-GQHSNKFMLVL-ASNLPEQFDCAI--NSRIDVMVH 520
Cdd:cd19528  105 NIGDAGGAAdrvINQILTEMdGMNTKKNVFIIgATNRPDIIDPAIlrPGRLDQLIY 160
RecA-like_CDC48_r1-like cd19519
first of two ATPase domains of CDC48 and similar ATPase domains; CDC48 in yeast and p97 or VCP ...
394-511 1.06e-08

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


Pssm-ID: 410927 [Multi-domain]  Cd Length: 166  Bit Score: 55.13  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDV-APMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR--AT 470
Cdd:cd19519   35 RGILLYGPPGTGKTLIARAVANETGAFFFLINGPEImSKLAGESESNLRKAFEEAEKNAPA-IIFIDEIDAIAPKRekTH 113
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767906275 471 EEISKDLRATLNAFLYHMGQHSNkFMLVLASNLPEQFDCAI 511
Cdd:cd19519  114 GEVERRIVSQLLTLMDGLKQRAH-VIVMAATNRPNSIDPAL 153
RecA-like_KTNA1 cd19522
Katanin p60 ATPase-containing subunit A1; Katanin p60 ATPase-containing subunit A1 (KTNA1) is ...
390-516 1.80e-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: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 390 RGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMGR-EGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR 468
Cdd:cd19522   30 RRPWKGVLMVGPPGTGKTLLAKAVATECGTTFFNVSSSTLTSKYRgESEKLVRLLFEMARFYAPT-TIFIDEIDSICSRR 108
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 767906275 469 ATEEISKDLRATLNAFLYHM--------GQHSNKFMLVL-ASNLPEQFDCAINSRID 516
Cdd:cd19522  109 GTSEEHEASRRVKSELLVQMdgvggaseNDDPSKMVMVLaATNFPWDIDEALRRRLE 165
RecA-like_VCP_r2 cd19529
second of two ATPase domains of Valosin-containing protein-like ATPase (VAT) and similar ...
394-511 9.19e-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: 9.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP--MGrEGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATE 471
Cdd:cd19529   28 KGILLYGPPGTGKTLLAKAVATESNANFISVKGPELLSkwVG-ESEKAIREIFRKARQVAP-CVIFFDEIDSIAPRRGTT 105
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767906275 472 EISKDLRATLNAFLYHMG--QHSNKFMLVLASNLPEQFDCAI 511
Cdd:cd19529  106 GDSGVTERVVNQLLTELDglEEMNGVVVIAATNRPDIIDPAL 147
RecA-like_ATAD1 cd19520
ATPase domain of ATPase family AAA domain-containing protein 1 and similar ATPase domains; ...
396-515 1.77e-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: 51.27  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMtggDVAPMGREGVTAMHKLFDWANTSRRGL---LLFMDEADAFLRKRAT-- 470
Cdd:cd19520   38 VLLYGPPGCGKTMLAKATAKEAGARFINL---QVSSLTDKWYGESQKLVAAVFSLASKLqpsIIFIDEIDSFLRQRSStd 114
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767906275 471 EEISKDLRATLNAFLYHMGQHSNKFMLVL-ASNLPEQFDCAINSRI 515
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; ...
390-515 2.21e-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: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 390 RGLYRHILLYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR 468
Cdd:cd19525   52 RGPPKGILLFGPPGTGKTLIGKCIASQSGATfFSISASSLTSKWVGEGEKMVRALFSVARCKQPA-VIFIDEIDSLLSQR 130
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767906275 469 --ATEEISKDLRATLNAFLYHMGQHSNKFMLVL-ASNLPEQFDCAINSRI 515
Cdd:cd19525  131 geGEHESSRRIKTEFLVQLDGATTSSEDRILVVgATNRPQEIDEAARRRL 180
PTZ00454 PTZ00454
26S protease regulatory subunit 6B-like protein; Provisional
394-543 2.45e-07

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


Pssm-ID: 240423 [Multi-domain]  Cd Length: 398  Bit Score: 53.61  E-value: 2.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR---- 468
Cdd:PTZ00454 180 RGVLLYGPPGTGKTMLAKAVAHHTTATFIRVVGSEfVQKYLGEGPRMVRDVFRLARENAPS-IIFIDEVDSIATKRfdaq 258
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767906275 469 --ATEEISKDLRATLNAfLYHMGQHSNkFMLVLASNLPEQFDCAI--NSRIDVMVHFDLPQQEERerlvRLHFDNCVLK 543
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 ...
394-511 3.28e-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: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMD-YAIMTGGDVAPMGREGVTAMHKLFDWAnTSRRGLLLFMDEADAFLRKRatEE 472
Cdd:cd19518   35 RGVLLHGPPGCGKTMLANAIAGELKVPfLKISATEIVSGVSGESEEKIRELFDQA-ISNAPCIVFIDEIDAITPKR--ES 111
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767906275 473 ISKDL-RATLNAFLYHMGQHSN-----KFMLVL-ASNLPEQFDCAI 511
Cdd:cd19518  112 AQREMeRRIVSQLLTCMDELNNektagGPVLVIgATNRPDSLDPAL 157
RecA-like_spastin cd19524
ATPase domain of spastin; Spastin is an ATP-dependent microtubule-severing protein involved in ...
394-515 5.69e-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: 5.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDY-----AIMTGGDVApmgrEGVTAMHKLFDWAnTSRRGLLLFMDEADAFLRKR 468
Cdd:cd19524   34 RGLLLFGPPGNGKTMLAKAVAAESNATFfnisaASLTSKYVG----EGEKLVRALFAVA-RELQPSIIFIDEVDSLLSER 108
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 767906275 469 ATEEISKDLRATLNAFLYHMGQHSNKFMLVL---ASNLPEQFDCAINSRI 515
Cdd:cd19524  109 SEGEHEASRRLKTEFLIEFDGVQSNGDDRVLvmgATNRPQELDDAVLRRF 158
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
140-263 1.28e-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: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 140 ALQEYEAAVEQLKSEQI-------RAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQ 212
Cdd:COG2268  217 AQANREAEEAELEQEREietariaEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQE 296
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767906275 213 KQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKA 263
Cdd:COG2268  297 KEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALA 347
PTZ00121 PTZ00121
MAEBL; Provisional
145-270 1.80e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.68  E-value: 1.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  145 EAAVEQLKSEQIRaQAEERRKtlSEETRQHQaRAQYQDKLarQRYEDQLKQQQLLNEENLRKQEEsVQKQEAMRRATVER 224
Cdd:PTZ00121 1504 KAAEAKKKADEAK-KAEEAKK--ADEAKKAE-EAKKADEA--KKAEEKKKADELKKAEELKKAEE-KKKAEEAKKAEEDK 1576
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767906275  225 EMELRhKNEMLRVETEAR-----------ARAKAER----ENADIIREQIRlKASEHRQTV 270
Cdd:PTZ00121 1577 NMALR-KAEEAKKAEEARieevmklyeeeKKMKAEEakkaEEAKIKAEELK-KAEEEKKKV 1635
PTZ00121 PTZ00121
MAEBL; Provisional
131-268 2.10e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 2.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  131 EQVPAGECCALQEYEAAVEQLKSEQIRAQAEERRKTL--SEETRQ-HQARAQYQDKL-----------ARQRYEDQLKQQ 196
Cdd:PTZ00121 1544 EKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALrkAEEAKKaEEARIEEVMKLyeeekkmkaeeAKKAEEAKIKAE 1623
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  197 QLLNEENLRK--------QEESVQKQEAMRRAtvEREMELRHKNEMLRVETEARA--RAKAERENADIIREQIRLKASEH 266
Cdd:PTZ00121 1624 ELKKAEEEKKkveqlkkkEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKaeEAKKAEEDEKKAAEALKKEAEEA 1701

                  ..
gi 767906275  267 RQ 268
Cdd:PTZ00121 1702 KK 1703
PTZ00361 PTZ00361
26 proteosome regulatory subunit 4-like protein; Provisional
396-536 3.12e-06

26 proteosome regulatory subunit 4-like protein; Provisional


Pssm-ID: 185575 [Multi-domain]  Cd Length: 438  Bit Score: 50.15  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGD-VAPMGREGVTAMHKLFDWANTSRRGlLLFMDEADAFLRKR--ATEE 472
Cdd:PTZ00361 220 VILYGPPGTGKTLLAKAVANETSATFLRVVGSElIQKYLGDGPKLVRELFRVAEENAPS-IVFIDEIDAIGTKRydATSG 298
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767906275 473 ISKDLRATLNAFLYHMG--QHSNKFMLVLASNLPEQFDCAI--NSRIDVMVHFDLPQQEERERLVRLH 536
Cdd:PTZ00361 299 GEKEIQRTMLELLNQLDgfDSRGDVKVIMATNRIESLDPALirPGRIDRKIEFPNPDEKTKRRIFEIH 366
PTZ00121 PTZ00121
MAEBL; Provisional
56-275 3.47e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 50.52  E-value: 3.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   56 ERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQS-KLKMQLEALnllhtlVWARSLCRAGAVQTQERLSGSASPEQVP 134
Cdd:PTZ00121 1574 EDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeEAKKAEEAK------IKAEELKKAEEEKKKVEQLKKKEAEEKK 1647
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  135 AGECCALQEYE----AAVEQLKSEQIRAQAEERRKTLSEETRQHQA------RAQYQDKLARQRYEDQLKQQQLLNEENL 204
Cdd:PTZ00121 1648 KAEELKKAEEEnkikAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEAlkkeaeEAKKAEELKKKEAEEKKKAEELKKAEEE 1727
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767906275  205 R--KQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAER-ENADIIREQIRLKASEHRQTVLESIR 275
Cdd:PTZ00121 1728 NkiKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRkEKEAVIEEELDEEDEKRRMEVDKKIK 1801
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
141-272 3.86e-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: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 141 LQEYEAAVEQLKSEqiRAQAEeRRKTLSEETRQHQARAQ-YQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRR 219
Cdd:COG1196  195 LGELERQLEPLERQ--AEKAE-RYRELKEELKELEAELLlLKLRELEAELEELEAELEELEAELEELEAELAELEAELEE 271
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767906275 220 ATVEREmELRHKNEMLRvETEARARAKAERENADIIREQIRLKASEHRQTVLE 272
Cdd:COG1196  272 LRLELE-ELELELEEAQ-AEEYELLAELARLEQDIARLEERRRELEERLEELE 322
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
140-277 4.32e-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: 4.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 140 ALQEYEAAVEQLKSEQIRAQAEERRK-TLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR 218
Cdd:COG1196  352 ELEEAEAELAEAEEALLEAEAELAEAeEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 767906275 219 RATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTA 277
Cdd:COG1196  432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAA 490
PTZ00121 PTZ00121
MAEBL; Provisional
57-268 6.73e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 49.75  E-value: 6.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   57 RAAKAARELEHSRYAKEALNLAqmQEQTLQLEQQSKLKMQLEALNLLHTLVWARSLCRAGAVQTQE---RLSGSASPEQV 133
Cdd:PTZ00121 1134 RKAEDARKAEEARKAEDAKRVE--IARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEdarKAEAARKAEEE 1211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  134 PAGECCALQEYEAAVEQLK-SEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQ 212
Cdd:PTZ00121 1212 RKAEEARKAEDAKKAEAVKkAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKK 1291
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767906275  213 KQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREqirlKASEHRQ 268
Cdd:PTZ00121 1292 ADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKK----KAEEAKK 1343
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
140-277 9.39e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 9.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 140 ALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyqdKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRR 219
Cdd:COG1196  317 RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA---EAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767906275 220 ATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTA 277
Cdd:COG1196  394 AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
149-268 1.12e-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: 48.58  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  149 EQLKSEQIRAQAEE------RRKTLSEETRQHQARAQYQ-------DKLA--RQRYEDQLKQQQLLNEENLRKQEESVQK 213
Cdd:pfam17380 294 EKMEQERLRQEKEEkareveRRRKLEEAEKARQAEMDRQaaiyaeqERMAmeRERELERIRQEERKRELERIRQEEIAME 373
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767906275  214 QEAMRRatVER-EMELRHKNEMLRVETEARARAK-AERENADIIREQ------IRLKASEHRQ 268
Cdd:pfam17380 374 ISRMRE--LERlQMERQQKNERVRQELEAARKVKiLEEERQRKIQQQkvemeqIRAEQEEARQ 434
PTZ00121 PTZ00121
MAEBL; Provisional
57-268 1.13e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   57 RAAKAARELEHSRYAKEALNLAQmqeqtlqleqqSKLKMQLEALNLlhtlvwarslcRAGAVQTQERLSGSASPEQVPAG 136
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKK-----------EEAKKKADAAKK-----------KAEEKKKADEAKKKAEEDKKKAD 1408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  137 ECcalqeYEAAVEQLKSEQIRAQAEERRKtlSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEA 216
Cdd:PTZ00121 1409 EL-----KKAAAAKKKADEAKKKAEEKKK--ADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEE 1481
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767906275  217 MRRATveremELRHKNEMLRVETEARARAKAERENADIIR--EQIRlKASEHRQ 268
Cdd:PTZ00121 1482 AKKAD-----EAKKKAEEAKKKADEAKKAAEAKKKADEAKkaEEAK-KADEAKK 1529
PTZ00121 PTZ00121
MAEBL; Provisional
131-292 1.16e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  131 EQVPAGECCALQEYEAAVEQLKSEQIRAQAEERRKtlSEETRQ-HQARAQYQDKLAR--QRYEDQLKQQQLLNEENLRKQ 207
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARK--AEDARKaEEARKAEDAKRVEiaRKAEDARKAEEARKAEDAKKA 1178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  208 EES-----VQKQEAMRRATVEREMELRHKNEMLRVETEARaRAKAERENADIIR-EQIRLKASEHRQTVLESIRTAGTLF 281
Cdd:PTZ00121 1179 EAArkaeeVRKAEELRKAEDARKAEAARKAEEERKAEEAR-KAEDAKKAEAVKKaEEAKKDAEEAKKAEEERNNEEIRKF 1257
                         170
                  ....*....|.
gi 767906275  282 GEGFRAFVTDR 292
Cdd:PTZ00121 1258 EEARMAHFARR 1268
RecA-like_PEX6_r2 cd19527
second of two ATPase domains of Peroxisomal biogenesis factor 6 (PEX6); PEX6(also known as ...
396-520 1.35e-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: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG-REGVTAMHKLFDWANTSRRgLLLFMDEADAFLRKRATEEIS 474
Cdd:cd19527   29 ILLYGPPGTGKTLLAKAIATECSLNFLSVKGPELINMYiGESEANVREVFQKARDAKP-CVIFFDELDSLAPSRGNSGDS 107
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 767906275 475 KDLR----ATLNAFLYHMGQHSNKFMLVLASNLPEQFDCAI--NSRIDVMVH 520
Cdd:cd19527  108 GGVMdrvvSQLLAELDGMSSSGQDVFVIGATNRPDLLDPALlrPGRFDKLLY 159
PTZ00121 PTZ00121
MAEBL; Provisional
56-268 1.45e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   56 ERAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKMQlEALNLLHTLVWARSLCRAGAVQTQERlsgSASPEQVPA 135
Cdd:PTZ00121 1211 ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNN-EEIRKFEEARMAHFARRQAAIKAEEA---RKADELKKA 1286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  136 GECCALQEYEAAVEQLKSEQIRAQAEERRKT------------LSEETRQHQARAQYQDKLARQRYE---DQLKQQQLLN 200
Cdd:PTZ00121 1287 EEKKKADEAKKAEEKKKADEAKKKAEEAKKAdeakkkaeeakkKADAAKKKAEEAKKAAEAAKAEAEaaaDEAEAAEEKA 1366
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  201 EENLRKQEESVQKQEAMRRATVEREM--ELRHKNEMLRVETEARARAKAERENADiireQIRLKASEHRQ 268
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEEKKKadEAKKKAEEDKKKADELKKAAAAKKKAD----EAKKKAEEKKK 1432
PTZ00121 PTZ00121
MAEBL; Provisional
145-268 1.59e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  145 EAAVEQLKSEQIRAQAEERRKTlsEETRQHQARaqyQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAmRRATVER 224
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKT--ETGKAEEAR---KAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDA-KRVEIAR 1158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 767906275  225 EMELRHKNEMLRVETEARaRAKAERENADIIR-EQIRlKASEHRQ 268
Cdd:PTZ00121 1159 KAEDARKAEEARKAEDAK-KAEAARKAEEVRKaEELR-KAEDARK 1201
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
119-263 2.69e-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: 46.76  E-value: 2.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  119 QTQERLSGSASPEQVPAGEccALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyqDKLARQRYEDQLKQQQL 198
Cdd:TIGR02794  54 RIQQQKKPAAKKEQERQKK--LEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAK--QAEEKQKQAEEAKAKQA 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767906275  199 ------LNEENLRKQEESVQKQ---EAMRRATVEREMELRHKNEMLRVETEAR--ARAKAERENADIIREQIRLKA 263
Cdd:TIGR02794 130 aeakakAEAEAERKAKEEAAKQaeeEAKAKAAAEAKKKAEEAKKKAEAEAKAKaeAEAKAKAEEAKAKAEAAKAKA 205
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
142-303 2.78e-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: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  142 QEYEAAVEQLKS-EQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEdQLKQQQLLNEENLRKQEESVQKQEAMRRA 220
Cdd:COG4913   242 EALEDAREQIELlEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLE-LLEAELEELRAELARLEAELERLEARLDA 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  221 TVEREMELRhkNEMLRVETEARARAKAERENADIIREQIRLKasehRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATVA 300
Cdd:COG4913   321 LREELDELE--AQIRGNGGDRLEQLEREIERLERELEERERR----RARLEALLAALGLPLPASAEEFAALRAEAAALLE 394

                  ...
gi 767906275  301 GLT 303
Cdd:COG4913   395 ALE 397
RecA-like_Yta7-like cd19517
ATPase domain of Saccharomyces cerevisiae Yta7 and similar ATPase domains; Saccharomyces ...
394-511 3.19e-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: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDyaimtGGDVAPMGREGVTAMHKlfdWANTSRRGL-------------LLFMDE 460
Cdd:cd19517   35 RGVLFHGPPGTGKTLMARALAAECSKG-----GQKVSFFMRKGADCLSK---WVGEAERQLrllfeeayrmqpsIIFFDE 106
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767906275 461 AD--AFLRKRATEEISKDLRATLNAFLYHMgQHSNKFMLVLASNLPEQFDCAI 511
Cdd:cd19517  107 IDglAPVRSSKQEQIHASIVSTLLALMDGL-DNRGQVVVIGATNRPDALDPAL 158
PTZ00121 PTZ00121
MAEBL; Provisional
57-260 3.29e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   57 RAAKAARELEHSRYAKEALNLAqmqeqtlqlEQQSKLKMQLEALNLLHTLVWARSLCRAGAVQTQERLSGSASPEQVPAG 136
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMA---------LRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  137 E----CCALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNE-------ENLR 205
Cdd:PTZ00121 1629 EeekkKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEaeeakkaEELK 1708
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767906275  206 K-QEESVQKQEAMRRATVER----------EMELRHKNEMLRVETEARARAKAERENADIIREQIR 260
Cdd:PTZ00121 1709 KkEAEEKKKAEELKKAEEENkikaeeakkeAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
PRK11637 PRK11637
AmiB activator; Provisional
149-257 3.95e-05

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 46.61  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 149 EQLKSEQIRAQ----AEERRKTLSE--ETRQH--QARAQYQDKLARQR---YEDQLKQQQLLNEENLRKQ-----EESVQ 212
Cdd:PRK11637 150 ESQRGERILAYfgylNQARQETIAElkQTREElaAQKAELEEKQSQQKtllYEQQAQQQKLEQARNERKKtltglESSLQ 229
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 767906275 213 KQEAmrRATVEREMELRHKNEMLRVETEARARAKAERENADIIRE 257
Cdd:PRK11637 230 KDQQ--QLSELRANESRLRDSIARAEREAKARAEREAREAARVRD 272
RecA-like_fidgetin cd19523
ATPase domain of fidgetin; Fidgetin (FIGN) is a ATP-dependent microtubule severing protein. ...
394-514 4.07e-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: 4.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDYAIMTG-GDVAPMGREGVTAMHKLFDWANtSRRGLLLFMDEADAFLRKRATEE 472
Cdd:cd19523   34 RSILLFGPRGTGKTLLGRCLASQLGATFLRLRGsTLVAKWAGEGEKILQASFLAAR-CRQPSVLFISDLDALLSSQDDEA 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767906275 473 -----ISKDLRATLNAFLyhmGQHSNKFMLVLASNLPEQFDCAINSR 514
Cdd:cd19523  113 spvgrLQVELLAQLDGVL---GSGEDGVLVVCTTSKPEEIDESLRRY 156
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
142-231 4.78e-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: 45.74  E-value: 4.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  142 QEYEAAVEQLKSEQIRAQAEErrktLSEETRQHQARAQYQDKlarqRYEDQLKQ--------QQLLNEENLRKQEESVQK 213
Cdd:pfam02841 202 KEKAIEAERAKAEAAEAEQEL----LREKQKEEEQMMEAQER----SYQEHVKQliekmeaeREQLLAEQERMLEHKLQE 273
                          90
                  ....*....|....*...
gi 767906275  214 QEAMRRATVEREMELRHK 231
Cdd:pfam02841 274 QEELLKEGFKTEAESLQK 291
PTZ00121 PTZ00121
MAEBL; Provisional
57-268 5.39e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.67  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   57 RAAKAARELEHSRYAKEALNLAQMQEQTLQLEQQSKLKMQLEALnllhtlvwarslcRAGAVQTQERLSgsaSPEQVPAG 136
Cdd:PTZ00121 1200 RKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAK-------------KAEEERNNEEIR---KFEEARMA 1263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  137 ECCALQEYEAAVEQLKSEQIRaQAEERRKtlSEETRQHQARAQYQD---KLARQRYEDQLKQQQllnEENLRKQEESVQK 213
Cdd:PTZ00121 1264 HFARRQAAIKAEEARKADELK-KAEEKKK--ADEAKKAEEKKKADEakkKAEEAKKADEAKKKA---EEAKKKADAAKKK 1337
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767906275  214 -QEAMRRATVEREMELRHKNEMLRVETEARArAKAERENADIIREQIRLKASEHRQ 268
Cdd:PTZ00121 1338 aEEAKKAAEAAKAEAEAAADEAEAAEEKAEA-AEKKKEEAKKKADAAKKKAEEKKK 1392
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
141-272 6.46e-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: 6.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  141 LQEYEAAVEQLKSEQI-RAQAEERRKtlSEETRQHQARAQYQDKLARQRyeDQLKQQQLLNEENLRKQEESVqKQEAMRR 219
Cdd:pfam17380 365 IRQEEIAMEISRMRELeRLQMERQQK--NERVRQELEAARKVKILEEER--QRKIQQQKVEMEQIRAEQEEA-RQREVRR 439
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767906275  220 ATVER--EMELRHKNEM--------LRVETEARARAKAERENadiiREQIRLKASEHRQTVLE 272
Cdd:pfam17380 440 LEEERarEMERVRLEEQerqqqverLRQQEEERKRKKLELEK----EKRDRKRAEEQRRKILE 498
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
140-390 7.27e-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: 7.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 140 ALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRR 219
Cdd:COG1196  388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 220 ATVEREMELRHKNEMLRVETEARARAKAEREnadiIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATV 299
Cdd:COG1196  468 LLEEAALLEAALAELLEELAEAAARLLLLLE----AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAA 543
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 300 AGLTLLAVGVYSAKNATAVTGRFIEARLGK----PSLVRETSRITVLEALRHPIQVSRRLLSRPQDVLEGVVLSPSLEAR 375
Cdd:COG1196  544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRatflPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLL 623
                        250
                 ....*....|....*
gi 767906275 376 VRDIAIATRNTKKNR 390
Cdd:COG1196  624 GRTLVAARLEAALRR 638
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
143-263 8.67e-05

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 45.04  E-value: 8.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 143 EYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRY---EDQLK-QQQLLNE--------ENLRKQEES 210
Cdd:COG1566   80 DLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLdlaQRELErYQALYKKgavsqqelDEARAALDA 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767906275 211 VQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKA 263
Cdd:COG1566  160 AQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
AAA_5 pfam07728
AAA domain (dynein-related subfamily); This Pfam entry includes some of the AAA proteins not ...
395-506 1.12e-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: 42.66  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  395 HILLYGPPGTGKTLFAKKLA------------LHSGMDYAIMTGG-DVAPMGREG-----VTAMhklfdwantsRRGLLL 456
Cdd:pfam07728   1 GVLLVGPPGTGKTELAERLAaalsnrpvfyvqLTRDTTEEDLFGRrNIDPGGASWvdgplVRAA----------REGEIA 70
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767906275  457 FMDEADaflrkrateEISKDLRATLNAFLYH-----------MGQHSNKFMLVLASNLPEQ 506
Cdd:pfam07728  71 VLDEIN---------RANPDVLNSLLSLLDErrlllpdggelVKAAPDGFRLIATMNPLDR 122
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
154-268 1.21e-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: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  154 EQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQqllNEENLRKQEEsvqkqEAMRRATVEREMELRHKNE 233
Cdd:pfam05672  31 EQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRRE---EEERQRKAEE-----EAEEREQREQEEQERLQKQ 102
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 767906275  234 mlRVETEARARAKAERENADiiREQIRLKASEHRQ 268
Cdd:pfam05672 103 --KEEAEAKAREEAERQRQE--REKIMQQEEQERL 133
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
142-265 1.24e-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: 44.84  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  142 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQH----------QARAQYQDKLARQRYEDQLKQQQllnEENLRKQEESV 211
Cdd:TIGR02794  96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQaaeakakaeaEAERKAKEEAAKQAEEEAKAKAA---AEAKKKAEEAK 172
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767906275  212 QKQEAMRRATVERE-----MELRHKNEMLRVETEARARAKAERENADIIREQIRLKASE 265
Cdd:TIGR02794 173 KKAEAEAKAKAEAEakakaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADE 231
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
140-277 1.43e-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: 45.33  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  140 ALQEYEAA---VEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKL------ARQRYEDQLKQQQLLNEENLRKQ--- 207
Cdd:COG3096   470 ARRQFEKAyelVCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLraqlaeLEQRLRQQQNAERLLEEFCQRIGqql 549
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  208 ------EESVQKQEAMR-------RATVEREMELRHKNEMLRVE-TEARARAKAERENADI---IREQI--RLKAS---- 264
Cdd:COG3096   550 daaeelEELLAELEAQLeeleeqaAEAVEQRSELRQQLEQLRARiKELAARAPAWLAAQDAlerLREQSgeALADSqevt 629
                         170
                  ....*....|...
gi 767906275  265 EHRQTVLESIRTA 277
Cdd:COG3096   630 AAMQQLLEREREA 642
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
140-392 1.94e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 140 ALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAmRR 219
Cdd:COG4717  130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQ-RL 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 220 ATVEREMELrhknemLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKVTATV 299
Cdd:COG4717  209 AELEEELEE------AQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLV 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 300 AGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSR-RLLSRPQDVLEGVVLSPSLEARVRD 378
Cdd:COG4717  283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPeELLELLDRIEELQELLREAEELEEE 362
                        250
                 ....*....|....
gi 767906275 379 IAIATRNTKKNRGL 392
Cdd:COG4717  363 LQLEELEQEIAALL 376
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
142-273 2.12e-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: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  142 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQllnEENLRKQ---EESVQKQEAMR 218
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA---EEERRKQqemEERRRIQEQMR 559
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767906275  219 RATVEREM--ELRHKNEMLR--VETEaraRAKAERENA---DIIREQIRLKASEHRQTVLES 273
Cdd:pfam17380 560 KATEERSRleAMEREREMMRqiVESE---KARAEYEATtpiTTIKPIYRPRISEYQPPDVES 618
PTZ00121 PTZ00121
MAEBL; Provisional
149-277 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 767906275  149 EQLKSEQIRAQAEERRKtLSEETRQHQARAQYQDKLARQ--RYEDQLKQQQLLNEENLRKQEESvQKQEAMRRATVEREM 226
Cdd:PTZ00121 1149 EDAKRVEIARKAEDARK-AEEARKAEDAKKAEAARKAEEvrKAEELRKAEDARKAEAARKAEEE-RKAEEARKAEDAKKA 1226
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767906275  227 ELRHKNEMLRVETEARARAKAERENADI-----------IREQIRLKASEHRQTvlESIRTA 277
Cdd:PTZ00121 1227 EAVKKAEEAKKDAEEAKKAEEERNNEEIrkfeearmahfARRQAAIKAEEARKA--DELKKA 1286
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
141-277 2.15e-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: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 141 LQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRyeDQLKQQQllneENLRKQEESVQKQEAMRRA 220
Cdd:COG1196  222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL--EELRLEL----EELELELEEAQAEEYELLA 295
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 221 TVER-EMELRHKNEMLRVETEARARAKAERE--NADIIREQIRLKASEHRQTVLESIRTA 277
Cdd:COG1196  296 ELARlEQDIARLEERRRELEERLEELEEELAelEEELEELEEELEELEEELEEAEEELEE 355
Borrelia_P83 pfam05262
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
141-290 2.75e-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: 2.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  141 LQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARaqyQDKLARQRYEDQLKQQQLLN-EENLRKQEESVQKQ--EAM 217
Cdd:pfam05262 203 LKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFA---QDNADKQRDEVRQKQQEAKNlPKPADTSSPKEDKQvaENQ 279
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  218 RRATVEREMELRHKNEMLRVETEARA----------RAKAERENADIIREqiRLKASEHRQTVLESIRTAGTLFGEGFRA 287
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEALKAKDHKAfdlkqeskasEKEAEDKELEAQKK--REPVAEDLQKTKPQVEAQPTSLNEDAID 357

                  ...
gi 767906275  288 FVT 290
Cdd:pfam05262 358 SSN 360
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
140-277 3.02e-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: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   140 ALQEYEAAVEQLKSEQIRAQAEERRKT------------LSEETRQHQARAQY--QDKLARQRYEDQLKQQQLLNEENLR 205
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIEELQkelyalaneisrLEQQKQILRERLANleRQLEELEAQLEELESKLDELAEELA 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   206 KQEESVQKQEAMRRATVEREMELRHKNEMLR---------VETEARARAKAERE----NADIIREQIRLKASEHRQTVLE 272
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEELEsrleeleeqLETLRSKVAQLELQiaslNNEIERLEARLERLEDRRERLQ 420

                   ....*
gi 767906275   273 SIRTA 277
Cdd:TIGR02168  421 QEIEE 425
RecA-like_PEX1_r2 cd19526
second of two ATPase domains of Peroxisomal biogenesis factor 1 (PEX1); PEX1(also known as ...
396-468 4.06e-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: 41.65  E-value: 4.06e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAP----MGREGVtamHKLFDWANtSRRGLLLFMDEADAFLRKR 468
Cdd:cd19526   30 ILLYGPPGCGKTLLASAIASECGLNFISVKGPELLNkyigASEQNV---RDLFSRAQ-SAKPCILFFDEFDSIAPKR 102
PTZ00121 PTZ00121
MAEBL; Provisional
142-257 4.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 4.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  142 QEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRAT 221
Cdd:PTZ00121 1693 ALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767906275  222 VEREME------LRHKNEMLRVETEarARAKAERENADIIRE 257
Cdd:PTZ00121 1773 IRKEKEavieeeLDEEDEKRRMEVD--KKIKDIFDNFANIIE 1812
PRK12704 PRK12704
phosphodiesterase; Provisional
145-278 4.47e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 4.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 145 EAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN-EENLRKQEESVQKQEA------- 216
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkEENLDRKLELLEKREEelekkek 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 217 ----------MRRATVErEMELRHKNEMLRV----ETEARA------RAKAERENADIIR---EQIRLKAS-EHRQTVLE 272
Cdd:PRK12704 118 eleqkqqeleKKEEELE-ELIEEQLQELERIsgltAEEAKEillekvEEEARHEAAVLIKeieEEAKEEADkKAKEILAQ 196

                 ....*..
gi 767906275 273 SI-RTAG 278
Cdd:PRK12704 197 AIqRCAA 203
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
199-414 4.88e-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: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 199 LNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKAS----EHRQTVLESI 274
Cdd:COG1401   31 IRADDLRGAAELATRLAERLSEELLRADRAARATELVEELSAALEVVVLLLDLEKVELNEKLALSEaavaIEELYELEAD 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 275 RTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRR 354
Cdd:COG1401  111 SEIEAVGLLLELAERSDALEALERARLLLELADLEERAALETEVLEALEAELEELLAAPEDLSADALAAELSAAEELYSE 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 355 LLSRPQDVLEGVvLSPSLEARVRDIAIATRnTKKNrglyrhILLYGPPGTGKTLFAKKLA 414
Cdd:COG1401  191 DLESEDDYLKDL-LREKFEETLEAFLAALK-TKKN------VILAGPPGTGKTYLARRLA 242
RecA-like_NSF-SEC18_r1-like cd19504
first of two ATPase domains of NSF and SEC18, and similar ATPase domains; ...
394-470 5.04e-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: 41.71  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 394 RHILLYGPPGTGKTLFAKKLA-LHSGMDYAIMTGGDVAP--MGrEGVTAMHKLFDWANTSRRGL-------LLFMDEADA 463
Cdd:cd19504   36 KGILLYGPPGTGKTLMARQIGkMLNAREPKIVNGPEILNkyVG-ESEANIRKLFADAEEEQRRLgansglhIIIFDEIDA 114

                 ....*..
gi 767906275 464 FLRKRAT 470
Cdd:cd19504  115 ICKQRGS 121
ARGLU pfam15346
Arginine and glutamate-rich 1; ARGLU, arginine and glutamate-rich 1 protein family, is ...
143-250 5.34e-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: 40.80  E-value: 5.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  143 EYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLN---EENLRKQEESVQKQEAMRR 219
Cdd:pfam15346  27 ELEKRKDEIEAEVERRVEEARKIMEKQVLEELEREREAELEEERRKEEEERKKREELErilEENNRKIEEAQRKEAEERL 106
                          90       100       110
                  ....*....|....*....|....*....|.
gi 767906275  220 ATVERemELRHKNEMLRVETEARARAKAERE 250
Cdd:pfam15346 107 AMLEE--QRRMKEERQRREKEEEEREKREQQ 135
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
149-277 5.51e-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: 43.02  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  149 EQLKSEQIRAQAEER----------RKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQ-----LLNEENLRKQEESVQK 213
Cdd:pfam15709 367 QLERAEKMREELELEqqrrfeeirlRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQeefrrKLQELQRKKQQEEAER 446
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767906275  214 QEAMRRATVEREMEL----RHKNEMLRVETEARARAKAEREnadiirEQIRLKASEHRQTVLESIRTA 277
Cdd:pfam15709 447 AEAEKQRQKELEMQLaeeqKRLMEMAEEERLEYQRQKQEAE------EKARLEAEERRQKEEEAARLA 508
HflB COG0465
ATP-dependent Zn proteases [Posttranslational modification, protein turnover, chaperones];
396-414 5.58e-04

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


Pssm-ID: 440233 [Multi-domain]  Cd Length: 583  Bit Score: 43.10  E-value: 5.58e-04
                         10
                 ....*....|....*....
gi 767906275 396 ILLYGPPGTGKTLFAKKLA 414
Cdd:COG0465  178 VLLVGPPGTGKTLLAKAVA 196
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
149-268 5.89e-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: 42.53  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  149 EQLKSEQIRAQAEERRKtlsEETRQHQARAQYQDKLARQRYEDQLKQQQllnEENLRKQEESVQKQEAMRRATVEREMEL 228
Cdd:TIGR02794  61 PAAKKEQERQKKLEQQA---EEAEKQRAAEQARQKELEQRAAAEKAAKQ---AEQAAKQAEEKQKQAEEAKAKQAAEAKA 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767906275  229 RHKNEMLRvETEARARAKAERENADIIREQIRLKASEHRQ 268
Cdd:TIGR02794 135 KAEAEAER-KAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK 173
Zot COG4128
Zona occludens toxin, predicted ATPase [General function prediction only];
396-559 5.93e-04

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


Pssm-ID: 443304 [Multi-domain]  Cd Length: 276  Bit Score: 42.39  E-value: 5.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFA----KKLALHSG-------------------MDYAIMTGG---DVAPMGREGVTAMHKLFDWAnt 449
Cdd:COG4128    4 TLITGVPGSGKSYEAvwflIIPALKKGrrvitnipglkileriaehLGLAVPDTAeliNVDTDDPDGLEKMARWFHWA-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 450 sRRGLLLFMDEADAFLRKRATEEISKDLRatlNAFLYHmgQHSNkFMLVLASNLPEQFDCAINSRIDV-MVHFDLPQQEE 528
Cdd:COG4128   82 -PDGALIVIDEAQRVWPPRGKGSKPPDVV---QAFATH--RHHG-WDIVLITQNISLIHSFIRALIERhYRHRKLDGLGL 154
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767906275 529 RERLVRLHFDNCVLKP-----ATEGKRRLKLAQFDY 559
Cdd:COG4128  155 RNRYEWPEHDGNPGKKtshdkATSKRYKYPKDVFGL 190
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
140-273 6.45e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 6.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 140 ALQEYEAAVEQLKSE--QIRAQAEERRKTLSEETRQhQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAM 217
Cdd:COG1196  261 ELAELEAELEELRLEleELELELEEAQAEEYELLAE-LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL 339
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767906275 218 RRATVEREM---ELRHKNEMLRVETEARARA----KAEREnaDIIREQIRLKASEHRQTVLES 273
Cdd:COG1196  340 EELEEELEEaeeELEEAEAELAEAEEALLEAeaelAEAEE--ELEELAEELLEALRAAAELAA 400
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
140-265 7.10e-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: 42.21  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  140 ALQEYEAAVEQLK------SEQIRAQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEE---S 210
Cdd:pfam13868  56 ALEEEEEKEEERKeerkryRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEideF 135
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767906275  211 VQKQEAMRRATVEREMELRHKN-EMLRVETEARARAKAERENADIIREQIRLKASE 265
Cdd:pfam13868 136 NEEQAEWKELEKEEEREEDERIlEYLKEKAEREEEREAEREEIEEEKEREIARLRA 191
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
395-465 8.27e-04

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 42.38  E-value: 8.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 395 HILLYGPPGTGKTLFAKKLALHSGMDY----AIMTggdvapmgreGVTAMHKLFDWANTSR---RGLLLFMDE------- 460
Cdd:PRK13342  38 SMILWGPPGTGKTTLARIIAGATDAPFealsAVTS----------GVKDLREVIEEARQRRsagRRTILFIDEihrfnka 107

                 ....*.
gi 767906275 461 -ADAFL 465
Cdd:PRK13342 108 qQDALL 113
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
396-465 1.03e-03

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: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 396 ILLYGPPGTGKTLFAKKLALHSGMDY----AIMTggdvapmgreGVTAMHKLFDWANTSR---RGLLLFMDE-------- 460
Cdd:COG2256   52 MILWGPPGTGKTTLARLIANATDAEFvalsAVTS----------GVKDIREVIEEARERRaygRRTILFVDEihrfnkaq 121

                 ....*
gi 767906275 461 ADAFL 465
Cdd:COG2256  122 QDALL 126
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
139-276 1.39e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.95  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 139 CALQEYEAAVEQLKSEqiRAQAEERRKTLSEETrqhqARAQYQDKLARQRyedqlkqqqllneENLRKQEESVQKQEAMR 218
Cdd:PRK02224 468 ETIEEDRERVEELEAE--LEDLEEEVEEVEERL----ERAEDLVEAEDRI-------------ERLEERREDLEELIAER 528
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767906275 219 RATVEREME----LRHKNEMLRVETE-ARARAKAERENADIIREQI-----RLKASEHRQTVLESIRT 276
Cdd:PRK02224 529 RETIEEKREraeeLRERAAELEAEAEeKREAAAEAEEEAEEAREEVaelnsKLAELKERIESLERIRT 596
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
141-268 2.21e-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: 40.67  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  141 LQEYEAAV---EQLKSEQIRAQAEERRKTLSEETRQHQARAQYQD-KLARQRYEDQLKQQQLLNEENLRKQEESVQKQEA 216
Cdd:pfam13868  90 QEEYEEKLqerEQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEfNEEQAEWKELEKEEEREEDERILEYLKEKAEREE 169
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767906275  217 MRRATVER-EMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQ 268
Cdd:pfam13868 170 EREAEREEiEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQK 222
mukB PRK04863
chromosome partition protein MukB;
123-268 2.29e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.48  E-value: 2.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  123 RLSGSASPEQvpageccALQEYEAAVEQLKSEQIRAQaeerrktlseetRQHQARAQYQDklARQRYEDQLKQQQLLNEE 202
Cdd:PRK04863  484 KIAGEVSRSE-------AWDVARELLRRLREQRHLAE------------QLQQLRMRLSE--LEQRLRQQQRAERLLAEF 542
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767906275  203 NlRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQ 268
Cdd:PRK04863  543 C-KRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLA 607
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
143-258 2.32e-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: 2.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 143 EYEAAVEQLKSEQIRAQ--AEERRKTLSEETRQHQARAQYQdkLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMR-- 218
Cdd:COG2268  207 EAERETEIAIAQANREAeeAELEQEREIETARIAEAEAELA--KKKAEERREAETARAEAEAAYEIAEANAEREVQRQle 284
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767906275 219 RATVEREMELRHKNEMLRVETEA---RARAKAERE--------NADIIREQ 258
Cdd:COG2268  285 IAEREREIELQEKEAEREEAELEadvRKPAEAEKQaaeaeaeaEAEAIRAK 335
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
140-263 2.39e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 40.95  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 140 ALQEYEAAVEQLKSEQiraQAEERRK----TLSEETRQHQARAQyqDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQE 215
Cdd:PRK09510  60 VVEQYNRQQQQQKSAK---RAEEQRKkkeqQQAEELQQKQAAEQ--ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA 134
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767906275 216 AMRRATVEREMELRHKNEMLRVETEArARAKAERENADIIREQIRLKA 263
Cdd:PRK09510 135 EEAAAKAAAAAKAKAEAEAKRAAAAA-KKAAAEAKKKAEAEAAKKAAA 181
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
141-267 2.51e-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: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  141 LQEYEAAVEQLKSEQIR-AQAEERRKTLSEETRQHQARAQYQDKLARQRYEDQLKQQQLlnEENLRKQEESVQKQEAMRR 219
Cdd:pfam15709 338 LRAERAEMRRLEVERKRrEQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRL--EEERQRQEEEERKQRLQLQ 415
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767906275  220 ATVER----EMELRHKNEMLRVETEARARAKAERENADIIREQIRLkASEHR 267
Cdd:pfam15709 416 AAQERarqqQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEMQL-AEEQK 466
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
396-414 2.65e-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: 2.65e-03
                          10
                  ....*....|....*....
gi 767906275  396 ILLYGPPGTGKTLFAKKLA 414
Cdd:pfam00910   1 IWLYGPPGCGKSTLAKYLA 19
PspF COG1221
Transcriptional regulators containing an AAA-type ATPase domain and a DNA-binding domain ...
389-460 2.92e-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: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 389 NRGLyrHILLYGPPGTGKTLFAKKL---ALHSGM-------------DYA-----IM-----------TGgdvapmgreg 436
Cdd:COG1221  128 PKGL--HTLILGPTGVGKSFFAELMyeyAIEIGVlpedapfvvfncaDYAnnpqlLMsqlfgyvkgafTG---------- 195
                         90       100       110
                 ....*....|....*....|....*....|.
gi 767906275 437 vtamhklfdwANTSRRGLL-------LFMDE 460
Cdd:COG1221  196 ----------ADKDKEGLIekadggiLFLDE 216
OmpH smart00935
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
142-223 3.67e-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: 38.33  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   142 QEYEAAVEQLKSEQIRAQAEerRKTLSEEtrqhqARAQYQDKLARQRYEDQLKQQQLLNEENLRKQEESVQKQEAMRRAT 221
Cdd:smart00935  32 AELEKLEKELQKLKEKLQKD--AATLSEA-----AREKKEKELQKKVQEFQRKQQKLQQDLQKRQQEELQKILDKINKAI 104

                   ..
gi 767906275   222 VE 223
Cdd:smart00935 105 KE 106
RNase_Y_N pfam12072
RNase Y N-terminal region;
140-266 3.72e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 39.10  E-value: 3.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  140 ALQEYEA----AVEQLKSE--QIRAQAE----ERRKTLS---------EET--RQHQARAQYQDKLARQryEDQLKQQQl 198
Cdd:pfam12072  43 AKKEAETkkkeALLEAKEEihKLRAEAErelkERRNELQrqerrllqkEETldRKDESLEKKEESLEKK--EKELEAQQ- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  199 lneENLRKQEESVQKQEAMRRATVER-----------------EMELRHKNEMLRVETEARARAKAERENADIIREQIRL 261
Cdd:pfam12072 120 ---QQLEEKEEELEELIEEQRQELERisgltseeakeilldevEEELRHEAAVMIKEIEEEAKEEADKKAKEIIALAIQR 196

                  ....*
gi 767906275  262 KASEH 266
Cdd:pfam12072 197 CAADH 201
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
114-247 4.25e-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: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   114 RAGAVQTQERLS-GSASPEQVPAGECCALQEYEAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQYQDkLARQRYEDQ 192
Cdd:pfam12128  617 REKQAAAEEQLVqANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNS-LEAQLKQLD 695
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767906275   193 LKQQQLLNEENLRKQEESVQKQEAMRRATVEREMEL-RHKNEMLRVETEARARAKA 247
Cdd:pfam12128  696 KKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLaLLKAAIAARRSGAKAELKA 751
MoxR COG0714
MoxR-like ATPase [General function prediction only]; MoxR-like ATPase is part of the Pathway ...
394-421 4.32e-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: 39.77  E-value: 4.32e-03
                         10        20
                 ....*....|....*....|....*...
gi 767906275 394 RHILLYGPPGTGKTLFAKKLALHSGMDY 421
Cdd:COG0714   32 GHLLLEGVPGVGKTTLAKALARALGLPF 59
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
145-267 4.48e-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: 39.24  E-value: 4.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  145 EAAVEQLKSEQIRAQAEERRKTLSEETRQHQaraqyqDKLARQryEDQLKQQQLLNEENLRKQEEsVQKQEAMRRATVER 224
Cdd:pfam00261  61 EALEKLEEAEKAADESERGRKVLENRALKDE------EKMEIL--EAQLKEAKEIAEEADRKYEE-VARKLVVVEGDLER 131
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767906275  225 --------EMELRHKNEMLRVET------EARARAKAEREnaDIIREQIR-----LKASEHR 267
Cdd:pfam00261 132 aeeraelaESKIVELEEELKVVGnnlkslEASEEKASERE--DKYEEQIRfltekLKEAETR 191
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
138-250 4.61e-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: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  138 CCALQEYEAAVEQLKSEQIRAQaEERRKTLSEETRQHQAR---------AQYQDKLARQRYEDQLKQQQllneenlrkQE 208
Cdd:pfam15558  57 QQSQEQWQAEKEQRKARLGREE-RRRADRREKQVIEKESRwreqaedqeNQRQEKLERARQEAEQRKQC---------QE 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767906275  209 ESVQKQEAMRRATVEREMELRHKnemlRVETEARARAKAERE 250
Cdd:pfam15558 127 QRLKEKEEELQALREQNSLQLQE----RLEEACHKRQLKERE 164
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
149-272 5.87e-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: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  149 EQLKSEQ--IRAQAEERRKTLSEETRQHQA--RAQYQDKLARQ---RYEDQLKQQQLLNEENLRKQEEsvqKQEAMRRAT 221
Cdd:pfam15709 329 EQEKASRdrLRAERAEMRRLEVERKRREQEeqRRLQQEQLERAekmREELELEQQRRFEEIRLRKQRL---EEERQRQEE 405
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767906275  222 VEREMELRHK--NEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLE 272
Cdd:pfam15709 406 EERKQRLQLQaaQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELE 458
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
145-275 6.21e-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: 6.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  145 EAAVEQLKSEQIRAQAEERRKTLSEETRQHQARAQyQDKLARQRYEDQLKQQQLLNEENLRKQEEsvQKQEAMRRATVER 224
Cdd:pfam13868 209 KLYQEEQERKERQKEREEAEKKARQRQELQQAREE-QIELKERRLAEEAEREEEEFERMLRKQAE--DEEIEQEEAEKRR 285
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767906275  225 EMELRHKNEMLRVETEARARAKAERENADIIREQIRlKASEHRQTVLESIR 275
Cdd:pfam13868 286 MKRLEHRRELEKQIEEREEQRAAEREEELEEGERLR-EEEAERRERIEEER 335
NACHT COG5635
Predicted NTPase, NACHT family domain [Signal transduction mechanisms];
216-416 6.65e-03

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


Pssm-ID: 444362 [Multi-domain]  Cd Length: 935  Bit Score: 39.79  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 216 AMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLESIRTAGTLFGEGFRAFVTDRDKV 295
Cdd:COG5635    2 LLLLALILALLALVLLLDLLVTRLAIALAALLLLALVALGLALLALLDLLLADLGALLALVSRSALSAAALLARALSALL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 296 TATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSRRLLSRPQDVLEGVVLS-PSLEA 374
Cdd:COG5635   82 LVLLLLESLLLLLLLLLLLAEALLALLELAALLKAVLLSLSGGSDLVLLLSESDLLLALLILLLDADGLLVSLDdLYVPL 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767906275 375 RVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALH 416
Cdd:COG5635  162 NLLERIESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLALE 203
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
146-250 6.65e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 39.40  E-value: 6.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 146 AAVEQLKSEQiRAQAEERRKtlsEETRQHQArAQYQDKLARQRYEDQLKQQQlLNEENLRKQEESVQKQEAMRRATVERE 225
Cdd:PRK09510  59 AVVEQYNRQQ-QQQKSAKRA---EEQRKKKE-QQQAEELQQKQAAEQERLKQ-LEKERLAAQEQKKQAEEAAKQAALKQK 132
                         90       100
                 ....*....|....*....|....*
gi 767906275 226 MElrhknEMLRVETEARARAKAERE 250
Cdd:PRK09510 133 QA-----EEAAAKAAAAAKAKAEAE 152
44 PHA02544
clamp loader, small subunit; Provisional
395-541 6.94e-03

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 39.20  E-value: 6.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 395 HILLYGP-PGTGKTLFAKKLALHSGMDYAIMTGGDvapmGREGvTAMHKLFDWANT---SRRGLLLFMDEADaflrKRAT 470
Cdd:PHA02544  44 NMLLHSPsPGTGKTTVAKALCNEVGAEVLFVNGSD----CRID-FVRNRLTRFASTvslTGGGKVIIIDEFD----RLGL 114
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767906275 471 EEISKDLRATlnaflyhMGQHSNKFMLVLASNLPEQFDCAINSRIDVmVHFDLPQQEERERLVRLHFDNCV 541
Cdd:PHA02544 115 ADAQRHLRSF-------MEAYSKNCSFIITANNKNGIIEPLRSRCRV-IDFGVPTKEEQIEMMKQMIVRCK 177
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
140-287 7.81e-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: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   140 ALQEYEAAVEQLKS--EQIRAQAEERRKTLSEETRQ-HQARAQyqdklaRQRYEDQLKQQQLLNEENLRKQEESVQKQEA 216
Cdd:TIGR02168  359 ELEELEAELEELESrlEELEEQLETLRSKVAQLELQiASLNNE------IERLEARLERLEDRRERLQQEIEELLKKLEE 432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   217 MRRATVEREMELrhKNEMLRVETEARARAKAERENADIIREQIR---------LKASEHRQTVLESIRTAGTLFGEGFRA 287
Cdd:TIGR02168  433 AELKELQAELEE--LEEELEELQEELERLEEALEELREELEEAEqaldaaereLAQLQARLDSLERLQENLEGFSEGVKA 510
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
395-414 7.89e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 38.96  E-value: 7.89e-03
                         10        20
                 ....*....|....*....|
gi 767906275 395 HILLYGPPGTGKTLFAKKLA 414
Cdd:PRK00080  53 HVLLYGPPGLGKTTLANIIA 72
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
148-273 8.59e-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: 39.57  E-value: 8.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275   148 VEQLKSEQIRAQAEERRKTLSEE---TRQHQARAQYQDKLARQRyEDQLKQQQLLNEENLRKQEESVQKQEAMRRAtvER 224
Cdd:pfam02463  139 VQGGKIEIIAMMKPERRLEIEEEaagSRLKRKKKEALKKLIEET-ENLAELIIDLEELKLQELKLKEQAKKALEYY--QL 215
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 767906275   225 EMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLES 273
Cdd:pfam02463  216 KEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEE 264
Mg_chelatase pfam01078
Magnesium chelatase, subunit ChlI; Magnesium-chelatase is a three-component enzyme that ...
395-413 8.61e-03

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


Pssm-ID: 426032 [Multi-domain]  Cd Length: 207  Bit Score: 38.29  E-value: 8.61e-03
                          10
                  ....*....|....*....
gi 767906275  395 HILLYGPPGTGKTLFAKKL 413
Cdd:pfam01078  24 NLLMIGPPGSGKTMLAKRL 42
TolA COG3064
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
114-506 9.16e-03

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


Pssm-ID: 442298 [Multi-domain]  Cd Length: 485  Bit Score: 39.25  E-value: 9.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 114 RAGAVQTQERLSGSASPEQVPAgECCALQEYEAAVEQLKSEQIRAQAEERRKTLSEEtrQHQARAQYQDKLARQRYEdql 193
Cdd:COG3064    8 KAAEAAAQERLEQAEAEKRAAA-EAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE--AEQRAAELAAEAAKKLAE--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 194 KQQQLLNEENLRKQEESVQKQEAMRRATVEREMELRHKNEMLRVETEARARAKAERENADIIREQIRLKASEHRQTVLES 273
Cdd:COG3064   82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 274 IRTAGTLFGEGFRAFVTDRDKVTATVAGLTLLAVGVYSAKNATAVTGRFIEARLGKPSLVRETSRITVLEALRHPIQVSR 353
Cdd:COG3064  162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275 354 RLLSRPQDVLEGVVLSPSLEARVRDIAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTGGDVAPMG 433
Cdd:COG3064  242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767906275 434 REGVTAMHKLFDWANTSRRGLLLFMDEADAFLRKRATEEISKDLRATLNAFLYHMGQHSNKFMLVLASNLPEQ 506
Cdd:COG3064  322 AAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAA 394
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
379-473 9.23e-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: 38.82  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  379 IAIATRNTKKNRGLYRHILLYGPPGTGKTLFAKKLALHSGMDYAIMTG------GDVAPMgregVTAMHKlfdwantsrr 452
Cdd:TIGR00635  16 LQLFIEAAKMRQEALDHLLLYGPPGLGKTTLAHIIANEMGVNLKITSGpalekpGDLAAI----LTNLEE---------- 81
                          90       100
                  ....*....|....*....|.
gi 767906275  453 GLLLFMDEADAFlrKRATEEI 473
Cdd:TIGR00635  82 GDVLFIDEIHRL--SPAVEEL 100
growth_prot_Scy NF041483
polarized growth protein Scy;
114-276 9.97e-03

polarized growth protein Scy;


Pssm-ID: 469371 [Multi-domain]  Cd Length: 1293  Bit Score: 39.42  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  114 RAGAVQTQERLSGSASPEQVPAGECCA------LQEYEAAVEQLK------SEQIRAQAEERRKTLseetrqhqaRAQYQ 181
Cdd:NF041483  453 RAEAVAEGERIRGEARREAVQQIEEAArtaeelLTKAKADADELRstataeSERVRTEAIERATTL---------RRQAE 523
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767906275  182 DKLARQRYE-DQLKQQQLLNEENLRKQEESVQKQeamRRATVEREMELRHK---NEMLRVETEARARAKAERENADIIR- 256
Cdd:NF041483  524 ETLERTRAEaERLRAEAEEQAEEVRAAAERAARE---LREETERAIAARQAeaaEELTRLHTEAEERLTAAEEALADARa 600
                         170       180
                  ....*....|....*....|....*.
gi 767906275  257 --EQIRLKASEH----RQTVLESIRT 276
Cdd:NF041483  601 eaERIRREAAEEterlRTEAAERIRT 626
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH